POLG_HRV14
ID POLG_HRV14 Reviewed; 2179 AA.
AC P03303; Q82083; Q82123; Q84736; Q84737; Q84738; Q84739; Q84740; Q84741;
AC Q84774; Q84775; Q84776; Q84777; Q84778; Q84779; Q89441; Q89649; Q89763;
AC Q89883;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 218.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=P1;
DE Contains:
DE RecName: Full=Capsid protein VP0;
DE AltName: Full=VP4-VP2;
DE Contains:
DE RecName: Full=Capsid protein VP4;
DE AltName: Full=P1A;
DE AltName: Full=Virion protein 4;
DE Contains:
DE RecName: Full=Capsid protein VP2;
DE AltName: Full=P1B;
DE AltName: Full=Virion protein 2;
DE Contains:
DE RecName: Full=Capsid protein VP3;
DE AltName: Full=P1C;
DE AltName: Full=Virion protein 3;
DE Contains:
DE RecName: Full=Capsid protein VP1;
DE AltName: Full=P1D;
DE AltName: Full=Virion protein 1;
DE Contains:
DE RecName: Full=P2;
DE Contains:
DE RecName: Full=Protease 2A;
DE Short=P2A;
DE EC=3.4.22.29 {ECO:0000250|UniProtKB:P03300};
DE AltName: Full=Picornain 2A;
DE AltName: Full=Protein 2A;
DE Contains:
DE RecName: Full=Protein 2B;
DE Short=P2B;
DE Contains:
DE RecName: Full=Protein 2C;
DE Short=P2C;
DE EC=3.6.1.15 {ECO:0000250|UniProtKB:P03300};
DE Contains:
DE RecName: Full=P3;
DE Contains:
DE RecName: Full=Protein 3AB;
DE Contains:
DE RecName: Full=Protein 3A;
DE Short=P3A;
DE Contains:
DE RecName: Full=Viral protein genome-linked;
DE Short=VPg;
DE AltName: Full=Protein 3B;
DE Short=P3B;
DE Contains:
DE RecName: Full=Protein 3CD;
DE EC=3.4.22.28;
DE Contains:
DE RecName: Full=Protease 3C {ECO:0000255|PROSITE-ProRule:PRU01222};
DE EC=3.4.22.28 {ECO:0000255|PROSITE-ProRule:PRU01222};
DE AltName: Full=Picornain 3C {ECO:0000255|PROSITE-ProRule:PRU01222};
DE Short=P3C {ECO:0000255|PROSITE-ProRule:PRU01222};
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase {ECO:0000255|PROSITE-ProRule:PRU00539};
DE Short=RdRp;
DE EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
DE AltName: Full=3D polymerase;
DE Short=3Dpol;
DE AltName: Full=Protein 3D;
DE Short=3D;
OS Human rhinovirus 14 (HRV-14).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Enterovirus.
OX NCBI_TaxID=12131;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6093056; DOI=10.1093/nar/12.20.7859;
RA Stanway G., Hughes P.J., Mountford R.C., Minor P.D., Almond J.W.;
RT "The complete nucleotide sequence of a common cold virus: human rhinovirus
RT 14.";
RL Nucleic Acids Res. 12:7859-7875(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND PROTEOLYTIC CLEAVAGE (CAPSID PROTEIN
RP VP0).
RX PubMed=8383233; DOI=10.1128/jvi.67.4.2110-2122.1993;
RA Lee W.M., Monroe S., Rueckert R.R.;
RT "Role of maturation cleavage in infectivity of picornaviruses: activation
RT of an infectosome.";
RL J. Virol. 67:2110-2122(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2983312; DOI=10.1073/pnas.82.3.732;
RA Callahan P.L., Mizutani S., Colonno R.J.;
RT "Molecular cloning and complete sequence determination of RNA genome of
RT human rhinovirus type 14.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:732-736(1985).
RN [4]
RP FUNCTION (PROTEIN 3A), AND INTERACTION WITH HOST GBF1 (PROTEIN 3A).
RX PubMed=17005635; DOI=10.1128/jvi.01225-06;
RA Wessels E., Duijsings D., Lanke K.H., van Dooren S.H., Jackson C.L.,
RA Melchers W.J., van Kuppeveld F.J.;
RT "Effects of picornavirus 3A Proteins on Protein Transport and GBF1-
RT dependent COP-I recruitment.";
RL J. Virol. 80:11852-11860(2006).
RN [5]
RP FUNCTION (PROTEASE 3C).
RX PubMed=18572216; DOI=10.1016/j.virol.2008.05.019;
RA de Breyne S., Bonderoff J.M., Chumakov K.M., Lloyd R.E., Hellen C.U.;
RT "Cleavage of eukaryotic initiation factor eIF5B by enterovirus 3C
RT proteases.";
RL Virology 378:118-122(2008).
RN [6]
RP REVIEW.
RX PubMed=20629045; DOI=10.1002/rmv.654;
RA Fuchs R., Blaas D.;
RT "Uncoating of human rhinoviruses.";
RL Rev. Med. Virol. 20:281-297(2010).
RN [7]
RP REVIEW.
RX PubMed=23227049; DOI=10.1155/2012/826301;
RA Fuchs R., Blaas D.;
RT "Productive entry pathways of human rhinoviruses.";
RL Adv. Virol. 2012:826301-826301(2012).
RN [8]
RP FUNCTION (PROTEIN 3A).
RX PubMed=30755512; DOI=10.1128/mbio.02742-18;
RA Lyoo H., van der Schaar H.M., Dorobantu C.M., Rabouw H.H.,
RA Strating J.R.P.M., van Kuppeveld F.J.M.;
RT "ACBD3 is an essential pan-enterovirus host factor that mediates the
RT interaction between viral 3A protein and cellular protein PI4KB.";
RL MBio 10:0-0(2019).
RN [9]
RP FUNCTION (PROTEIN 3C), AND MUTAGENESIS OF CYS-1683.
RX PubMed=33093214; DOI=10.1126/science.aay2002;
RA Robinson K.S., Teo D.E.T., Tan K.S., Toh G.A., Ong H.H., Lim C.K., Lay K.,
RA Au B.V., Lew T.S., Chu J.J.H., Chow V.T.K., Wang Y., Zhong F.L.,
RA Reversade B.;
RT "Enteroviral 3C protease activates the human NLRP1 inflammasome in airway
RT epithelia.";
RL Science 0:0-0(2020).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=2993920; DOI=10.1038/317145a0;
RA Rossman M.G., Arnold E., Erickson J.W., Frankenberger E.A., Griffith J.P.,
RA Hecht H.-J., Johnson J.E., Kamer G., Luo M., Mosser A.G., Rueckert R.R.,
RA Sherry B., Vriend G.;
RT "Structure of a human common cold virus and functional relationship to
RT other picornaviruses.";
RL Nature 317:145-153(1985).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=2856083; DOI=10.1107/s0108767387011875;
RA Arnold E., Rossman M.G.;
RT "The use of molecular-replacement phases for the refinement of the human
RT rhinovirus 14 structure.";
RL Acta Crystallogr. A 44:270-282(1988).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=2156077; DOI=10.1016/0022-2836(90)90076-x;
RA Arnold E., Rossman M.G.;
RT "Analysis of the structure of a common cold virus, human rhinovirus 14,
RT refined at a resolution of 3.0 A.";
RL J. Mol. Biol. 211:763-801(1990).
RN [13]
RP STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF 70-856 IN COMPLEX WITH
RP ICAM1, FUNCTION (CAPSID PROTEIN VP1), AND INTERACTION WITH HOST ICAM1
RP (CAPSID PROTEIN VP1).
RX PubMed=10562537; DOI=10.1093/emboj/18.22.6249;
RA Kolatkar P.R., Bella J., Olson N.H., Bator C.M., Baker T.S., Rossmann M.G.;
RT "Structural studies of two rhinovirus serotypes complexed with fragments of
RT their cellular receptor.";
RL EMBO J. 18:6249-6259(1999).
RN [14]
RP FUNCTION (PROTEASE 2A).
RX PubMed=12163599; DOI=10.1128/jvi.76.17.8787-8796.2002;
RA Gustin K.E., Sarnow P.;
RT "Inhibition of nuclear import and alteration of nuclear pore complex
RT composition by rhinovirus.";
RL J. Virol. 76:8787-8796(2002).
RN [15] {ECO:0007744|PDB:5W3E, ECO:0007744|PDB:5W3L, ECO:0007744|PDB:5W3M, ECO:0007744|PDB:5W3O}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.26 ANGSTROMS) OF 2-856, AND FUNCTION
RP (CAPSID PROTEIN VP1).
RX PubMed=28696310; DOI=10.1073/pnas.1707369114;
RA Dong Y., Liu Y., Jiang W., Smith T.J., Xu Z., Rossmann M.G.;
RT "Antibody-induced uncoating of human rhinovirus B14.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:8017-8022(2017).
RN [16] {ECO:0007744|PDB:6HLT}
RP X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 1430-1485, INTERACTION WITH HOST
RP ACBD3 (PROTEIN 3A), AND FUNCTION (PROTEIN 3A).
RX PubMed=31381608; DOI=10.1371/journal.ppat.1007962;
RA Horova V., Lyoo H., Rozycki B., Chalupska D., Smola M., Humpolickova J.,
RA Strating J.R.P.M., van Kuppeveld F.J.M., Boura E., Klima M.;
RT "Convergent evolution in the mechanisms of ACBD3 recruitment to
RT picornavirus replication sites.";
RL PLoS Pathog. 15:E1007962-E1007962(2019).
CC -!- FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300
CC Angstroms in diameter, composed of 60 copies of each capsid protein and
CC enclosing the viral positive strand RNA genome (By similarity). Capsid
CC protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1
CC interacts with host ICAM1 to provide virion attachment to target host
CC cells (PubMed:10562537). This attachment induces virion internalization
CC (By similarity). Tyrosine kinases are probably involved in the entry
CC process. After binding to its receptor, the capsid undergoes
CC conformational changes (By similarity). Capsid protein VP1 N-terminus
CC (that contains an amphipathic alpha-helix) and capsid protein VP4 are
CC externalized (Probable). Together, they shape a pore in the host
CC membrane through which viral genome is translocated to host cell
CC cytoplasm (PubMed:28696310). After genome has been released, the
CC channel shrinks. {ECO:0000250|UniProtKB:P03300,
CC ECO:0000269|PubMed:10562537, ECO:0000269|PubMed:28696310,
CC ECO:0000305|PubMed:28696310}.
CC -!- FUNCTION: [Capsid protein VP2]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The
CC capsid is 300 Angstroms in diameter, composed of 60 copies of each
CC capsid protein and enclosing the viral positive strand RNA genome (By
CC similarity). {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The
CC capsid is 300 Angstroms in diameter, composed of 60 copies of each
CC capsid protein and enclosing the viral positive strand RNA genome (By
CC similarity). {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Capsid protein VP4]: Lies on the inner surface of the capsid
CC shell (By similarity). After binding to the host receptor, the capsid
CC undergoes conformational changes (By similarity). Capsid protein VP4 is
CC released, Capsid protein VP1 N-terminus is externalized, and together,
CC they shape a pore in the host membrane through which the viral genome
CC is translocated into the host cell cytoplasm (By similarity).
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Capsid protein VP0]: Component of immature procapsids, which
CC is cleaved into capsid proteins VP4 and VP2 after maturation (By
CC similarity). Allows the capsid to remain inactive before the maturation
CC step (By similarity). {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Protease 2A]: Cysteine protease that cleaves viral
CC polyprotein and specific host proteins (By similarity). It is
CC responsible for the autocatalytic cleavage between the P1 and P2
CC regions, which is the first cleavage occurring in the polyprotein (By
CC similarity). Cleaves also the host translation initiation factor
CC EIF4G1, in order to shut down the capped cellular mRNA translation (By
CC similarity). Inhibits the host nucleus-cytoplasm protein and RNA
CC trafficking by cleaving host members of the nuclear pores including
CC NUP62 and NUP153 (Probable). Counteracts stress granule formation
CC probably by antagonizing its assembly or promoting its dissassembly (By
CC similarity). {ECO:0000250|UniProtKB:P03300,
CC ECO:0000250|UniProtKB:P03301, ECO:0000305|PubMed:12163599}.
CC -!- FUNCTION: [Protein 2B]: Plays an essential role in the virus
CC replication cycle by acting as a viroporin. Creates a pore in the host
CC reticulum endoplasmic and as a consequence releases Ca2+ in the
CC cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium
CC may trigger membrane trafficking and transport of viral ER-associated
CC proteins to viroplasms, sites of viral genome replication.
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Protein 2C]: Induces and associates with structural
CC rearrangements of intracellular membranes. Displays RNA-binding,
CC nucleotide binding and NTPase activities. May play a role in virion
CC morphogenesis and viral RNA encapsidation by interacting with the
CC capsid protein VP3. {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Protein 3AB]: Localizes the viral replication complex to the
CC surface of membranous vesicles. Together with protein 3CD binds the
CC Cis-Active RNA Element (CRE) which is involved in RNA synthesis
CC initiation. Acts as a cofactor to stimulate the activity of 3D
CC polymerase, maybe through a nucleid acid chaperone activity.
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Protein 3A]: Localizes the viral replication complex to the
CC surface of membranous vesicles (By similarity). It inhibits host cell
CC endoplasmic reticulum-to-Golgi apparatus transport and causes the
CC disassembly of the Golgi complex, possibly through GBF1 interaction
CC (PubMed:17005635). This would result in depletion of MHC, trail
CC receptors and IFN receptors at the host cell surface (PubMed:17005635).
CC Plays an essential role in viral RNA replication by recruiting ACBD3
CC and PI4KB at the viral replication sites, thereby allowing the
CC formation of the rearranged membranous structures where viral
CC replication takes place (Probable). {ECO:0000250|UniProtKB:P03300,
CC ECO:0000269|PubMed:17005635, ECO:0000305|PubMed:30755512,
CC ECO:0000305|PubMed:31381608}.
CC -!- FUNCTION: [Viral protein genome-linked]: Acts as a primer for viral RNA
CC replication and remains covalently bound to viral genomic RNA. VPg is
CC uridylylated prior to priming replication into VPg-pUpU (By
CC similarity). The oriI viral genomic sequence may act as a template for
CC this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by
CC the RNA-dependent RNA polymerase to replicate the viral genome (By
CC similarity). Following genome release from the infecting virion in the
CC cytoplasm, the VPg-RNA linkage is probably removed by host TDP2 (By
CC similarity). During the late stage of the replication cycle, host TDP2
CC is excluded from sites of viral RNA synthesis and encapsidation,
CC allowing for the generation of progeny virions (By similarity).
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Protein 3CD]: Involved in the viral replication complex and
CC viral polypeptide maturation. It exhibits protease activity with a
CC specificity and catalytic efficiency that is different from protease
CC 3C. Protein 3CD lacks polymerase activity. Protein 3CD binds to the
CC 5'UTR of the viral genome. {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Protease 3C]: Major viral protease that mediates proteolytic
CC processing of the polyprotein (By similarity). Cleaves host EIF5B,
CC contributing to host translation shutoff (PubMed:18572216). Cleaves
CC also host PABPC1, contributing to host translation shutoff (By
CC similarity). Cleaves host NLRP1, triggers host N-glycine-mediated
CC degradation of the autoinhibitory NLRP1 N-terminal fragment
CC (PubMed:33093214). {ECO:0000250|UniProtKB:P03300,
CC ECO:0000269|PubMed:18572216, ECO:0000269|PubMed:33093214}.
CC -!- FUNCTION: [RNA-directed RNA polymerase]: Replicates the viral genomic
CC RNA on the surface of intracellular membranes. May form linear arrays
CC of subunits that propagate along a strong head-to-tail interaction
CC called interface-I. Covalently attaches UMP to a tyrosine of VPg, which
CC is used to prime RNA synthesis. The positive stranded RNA genome is
CC first replicated at virus induced membranous vesicles, creating a dsRNA
CC genomic replication form. This dsRNA is then used as template to
CC synthesize positive stranded RNA genomes. ss(+)RNA genomes are either
CC translated, replicated or encapsidated. {ECO:0000250|UniProtKB:P03300}.
CC -!- CATALYTIC ACTIVITY: [Protein 2C]:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC Evidence={ECO:0000250|UniProtKB:P03300};
CC -!- CATALYTIC ACTIVITY: [Protease 2A]:
CC Reaction=Selective cleavage of Tyr-|-Gly bond in the picornavirus
CC polyprotein.; EC=3.4.22.29; Evidence={ECO:0000250|UniProtKB:P03300};
CC -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY: [Protease 3C]:
CC Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus
CC polyprotein. In other picornavirus reactions Glu may be substituted
CC for Gln, and Ser or Thr for Gly.; EC=3.4.22.28;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01222};
CC -!- COFACTOR: [RNA-directed RNA polymerase]:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P03300};
CC Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal
CC center (By similarity). The magnesium ions are not prebound but only
CC present for catalysis (By similarity). Requires the presence of 3CDpro
CC or 3CPro (By similarity). {ECO:0000250|UniProtKB:P03300,
CC ECO:0000250|UniProtKB:P03313};
CC -!- ACTIVITY REGULATION: [RNA-directed RNA polymerase]: Replication or
CC transcription is subject to high level of random mutations by the
CC nucleotide analog ribavirin. {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [Capsid protein VP0]: Interacts with capsid protein VP1 and
CC capsid protein VP3 to form heterotrimeric protomers.
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [Capsid protein VP1]: Interacts with capsid protein VP0, and
CC capsid protein VP3 to form heterotrimeric protomers (By similarity).
CC Five protomers subsequently associate to form pentamers which serve as
CC building blocks for the capsid (By similarity). Interacts with capsid
CC protein VP2, capsid protein VP3 and capsid protein VP4 following
CC cleavage of capsid protein VP0 (By similarity). Interacts with host
CC ICAM1 (PubMed:10562537). {ECO:0000250|UniProtKB:P03300,
CC ECO:0000269|PubMed:10562537}.
CC -!- SUBUNIT: [Capsid protein VP2]: Interacts with capsid protein VP1 and
CC capsid protein VP3 in the mature capsid.
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [Capsid protein VP3]: Interacts with capsid protein VP0 and
CC capsid protein VP1 to form heterotrimeric protomers (By similarity).
CC Five protomers subsequently associate to form pentamers which serve as
CC building blocks for the capsid (By similarity). Interacts with capsid
CC protein VP4 in the mature capsid (By similarity). Interacts with
CC protein 2C; this interaction may be important for virion morphogenesis
CC (By similarity). {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [Capsid protein VP4]: Interacts with capsid protein VP1 and
CC capsid protein VP3. {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [Protease 2A]: Homodimer. {ECO:0000250|UniProtKB:P04936}.
CC -!- SUBUNIT: [Protein 2C]: Homohexamer; forms a hexameric ring structure
CC with 6-fold symmetry characteristic of AAA+ ATPases (By similarity).
CC Interacts (via N-terminus) with host RTN3 (via reticulon domain); this
CC interaction is important for viral replication (By similarity).
CC Interacts with capsid protein VP3; this interaction may be important
CC for virion morphogenesis (By similarity).
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [Protein 3AB]: Interacts with protein 3CD.
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [Protein 3A]: Homodimer (By similarity). Interacts with host
CC GBF1 (PubMed:17005635). Interacts (via GOLD domain) with host ACBD3
CC (via GOLD domain); this interaction allows the formation of a viral
CC protein 3A/ACBD3 heterotetramer with a 2:2 stoichiometry, which will
CC stimulate the recruitment of host PI4KB in order to synthesize PI4P at
CC the viral RNA replication sites (PubMed:31381608).
CC {ECO:0000250|UniProtKB:P03300, ECO:0000269|PubMed:17005635,
CC ECO:0000269|PubMed:31381608}.
CC -!- SUBUNIT: [Viral protein genome-linked]: Interacts with RNA-directed RNA
CC polymerase. {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [Protein 3CD]: Interacts with protein 3AB and with RNA-
CC directed RNA polymerase. {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [RNA-directed RNA polymerase]: Interacts with Viral protein
CC genome-linked and with protein 3CD. {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion
CC {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion
CC {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion
CC {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Note=Probably localizes to the surface of
CC intracellular membrane vesicles that are induced after virus infection
CC as the site for viral RNA replication. These vesicles are derived from
CC the endoplasmic reticulum.
CC -!- SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Note=Probably localizes to the surface of
CC intracellular membrane vesicles that are induced after virus infection
CC as the site for viral RNA replication. These vesicles are derived from
CC the endoplasmic reticulum.
CC -!- SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Note=Probably localizes to the surface of
CC intracellular membrane vesicles that are induced after virus infection
CC as the site for viral RNA replication. These vesicles are derived from
CC the endoplasmic reticulum.
CC -!- SUBCELLULAR LOCATION: [Protein 3AB]: Host cytoplasmic vesicle membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Note=Probably localizes to the surface of
CC intracellular membrane vesicles that are induced after virus infection
CC as the site for viral RNA replication. These vesicles are derived from
CC the endoplasmic reticulum.
CC -!- SUBCELLULAR LOCATION: [Viral protein genome-linked]: Virion
CC {ECO:0000250|UniProtKB:P03300}. Host cytoplasm
CC {ECO:0000250|UniProtKB:Q66478}.
CC -!- SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Protein 3CD]: Host nucleus
CC {ECO:0000250|UniProtKB:P03300}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P03300}. Host cytoplasmic vesicle membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Note=Probably localizes to the surface of
CC intracellular membrane vesicles that are induced after virus infection
CC as the site for viral RNA replication. These vesicles are derived from
CC the endoplasmic reticulum.
CC -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasmic
CC vesicle membrane {ECO:0000305}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes
CC to the surface of intracellular membrane vesicles that are induced
CC after virus infection as the site for viral RNA replication. These
CC vesicles are derived from the endoplasmic reticulum.
CC -!- DOMAIN: [Protein 2C]: The N-terminus has membrane-binding (By
CC similarity). The N-terminus also displays RNA-binding properties (By
CC similarity). The N-terminus is involved in oligomerization (By
CC similarity). The central part contains an ATPase domain and a C4-type
CC zinc-finger (By similarity). The C-terminus is involved in RNA-binding
CC (By similarity). The extreme C-terminus contains a region involved in
CC oligomerization (By similarity). {ECO:0000250|UniProtKB:P03300}.
CC -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the
CC viral proteases yield processing intermediates and the mature proteins.
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- PTM: [Capsid protein VP0]: Myristoylation is required for the formation
CC of pentamers during virus assembly. Further assembly of 12 pentamers
CC and a molecule of genomic RNA generates the provirion.
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- PTM: [Capsid protein VP0]: During virion maturation, immature virions
CC are rendered infectious following cleavage of VP0 into VP4 and VP2.
CC This maturation seems to be an autocatalytic event triggered by the
CC presence of RNA in the capsid and it is followed by a conformational
CC change infectious virion. {ECO:0000269|PubMed:8383233}.
CC -!- PTM: [Capsid protein VP4]: Myristoylation is required during RNA
CC encapsidation and formation of the mature virus particle.
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- PTM: [Viral protein genome-linked]: VPg is uridylylated by the
CC polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for
CC the genomic RNA replication. {ECO:0000250|UniProtKB:P03300}.
CC -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC {ECO:0000305}.
CC -!- CAUTION: The PDB data bank contains the 3D-structure coordinates of
CC proteins VP1, VP2, VP3 and VP4. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=4rhv";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=2r04";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=2r06";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=2r07";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=2rm2";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=2rmu";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=2rr1";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=2rs1";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=2rs3";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=2rs5";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=2hwb";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=2hwc";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1vrh";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1rmu";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1ruc";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1rud";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1rue";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1ruf";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1rug";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1ruh";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1rui";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1ruj";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1rvf";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1r08";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1r09";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1ncq";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1na1";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1k5m";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1d3i";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure complexed with antiviral compound SCH 38057;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1hri";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure complexed with antiviral compound SDZ 35-682;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1hrv";
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DR EMBL; X01087; CAA25565.1; -; Genomic_RNA.
DR EMBL; L05355; AAA45758.1; -; Genomic_RNA.
DR EMBL; K02121; AAA45756.1; -; Genomic_RNA.
DR PIR; A03901; GNNYH4.
DR RefSeq; NP_041009.1; NC_001490.1.
DR PDB; 1D3I; EM; 26.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 1HRI; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 1HRV; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 1K5M; X-ray; 2.70 A; A=568-856, B=70-331, C=332-567, D=2-69.
DR PDB; 1NA1; X-ray; 3.30 A; A=568-856, B=70-331, C=332-567, D=2-69.
DR PDB; 1NCQ; X-ray; 2.50 A; A=568-856, B=70-331, C=332-567, D=2-69.
DR PDB; 1R08; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 1R09; X-ray; 2.90 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 1RMU; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 1RUC; X-ray; 3.10 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 1RUD; X-ray; 2.90 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 1RUE; X-ray; 2.90 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 1RUF; X-ray; 2.90 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 1RUG; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 1RUH; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 1RUI; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 1RUJ; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 1RVF; X-ray; 4.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 1VRH; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 1XR5; X-ray; 2.80 A; A=1720-2179.
DR PDB; 2B0F; NMR; -; A=1538-1719.
DR PDB; 2HWB; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 2HWC; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 2IN2; NMR; -; A=1538-1719.
DR PDB; 2R04; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 2R06; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 2R07; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 2RM2; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 2RMU; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 2RR1; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 2RS1; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 2RS3; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 2RS5; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 4PDW; X-ray; 3.00 A; A=568-856, B=70-331, C=332-567.
DR PDB; 4RHV; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR PDB; 5W3E; EM; 2.53 A; A=568-856, B=332-567, C=70-331, D=2-69.
DR PDB; 5W3L; EM; 2.71 A; A=568-856, B=332-567, C=70-331, D=2-69.
DR PDB; 5W3M; EM; 2.26 A; A=568-856, B=332-567, C=70-331, D=2-69.
DR PDB; 5W3O; EM; 3.01 A; A=568-856, B=332-567, C=70-331.
DR PDB; 6HLT; X-ray; 2.81 A; B/D=1430-1485.
DR PDB; 6KYZ; X-ray; 1.84 A; A/D=1538-1719.
DR PDB; 6KZ0; X-ray; 2.40 A; A/D/G/J=1538-1719.
DR PDBsum; 1D3I; -.
DR PDBsum; 1HRI; -.
DR PDBsum; 1HRV; -.
DR PDBsum; 1K5M; -.
DR PDBsum; 1NA1; -.
DR PDBsum; 1NCQ; -.
DR PDBsum; 1R08; -.
DR PDBsum; 1R09; -.
DR PDBsum; 1RMU; -.
DR PDBsum; 1RUC; -.
DR PDBsum; 1RUD; -.
DR PDBsum; 1RUE; -.
DR PDBsum; 1RUF; -.
DR PDBsum; 1RUG; -.
DR PDBsum; 1RUH; -.
DR PDBsum; 1RUI; -.
DR PDBsum; 1RUJ; -.
DR PDBsum; 1RVF; -.
DR PDBsum; 1VRH; -.
DR PDBsum; 1XR5; -.
DR PDBsum; 2B0F; -.
DR PDBsum; 2HWB; -.
DR PDBsum; 2HWC; -.
DR PDBsum; 2IN2; -.
DR PDBsum; 2R04; -.
DR PDBsum; 2R06; -.
DR PDBsum; 2R07; -.
DR PDBsum; 2RM2; -.
DR PDBsum; 2RMU; -.
DR PDBsum; 2RR1; -.
DR PDBsum; 2RS1; -.
DR PDBsum; 2RS3; -.
DR PDBsum; 2RS5; -.
DR PDBsum; 4PDW; -.
DR PDBsum; 4RHV; -.
DR PDBsum; 5W3E; -.
DR PDBsum; 5W3L; -.
DR PDBsum; 5W3M; -.
DR PDBsum; 5W3O; -.
DR PDBsum; 6HLT; -.
DR PDBsum; 6KYZ; -.
DR PDBsum; 6KZ0; -.
DR BMRB; P03303; -.
DR SMR; P03303; -.
DR IntAct; P03303; 2.
DR BindingDB; P03303; -.
DR ChEMBL; CHEMBL4295564; -.
DR DrugBank; DB08725; (S)-5-(7-(4-(4-Ethyl-4,5-dihydro-2-oxazolyl)phenoxy)heptyl)-3-methylisoxazole.
DR DrugBank; DB08543; 1-[2-HYDROXY-3-(4-CYCLOHEXYL-PHENOXY)-PROPYL]-4-(2-PYRIDYL)-PIPERAZINE.
DR DrugBank; DB08509; 1-[6-(2-CHLORO-4-METHYXYPHENOXY)-HEXYL]-IMIDAZOLE.
DR DrugBank; DB08540; 2-[4-(2H-1,4-BENZOTHIAZINE-3-YL)-PIPERAZINE-1-LY]-1,3-THIAZOLE-4-CARBOXYLIC ACID ETHYLESTER.
DR DrugBank; DB08017; 3-METHOXY-6-[4-(3-METHYLPHENYL)-1-PIPERAZINYL]PYRIDAZINE.
DR DrugBank; DB08727; 3-Methyl-5-(7-{4-[(4R)-4-methyl-4,5-dihydro-1,3-oxazol-2-yl]phenoxy}heptyl)-1,2-oxazole.
DR DrugBank; DB08728; 5-(3-(2,6-dichloro-4-(4,5-dihydro-2-oxazolyl)phenoxy)propyl)-3-methyl isoxazole.
DR DrugBank; DB08721; 5-(5-(2,6-dichloro-4-(4,5-dihydro-2-oxazolyl)phenoxy)pentyl)-3-(hydroxyethyl oxymethyleneoxymethyl) isoxazole.
DR DrugBank; DB08720; 5-(5-(4-(4,5-dihydro-2-oxazoly)phenoxy)pentyl)-3-methyl osoxazole.
DR DrugBank; DB08724; 5-(5-(4-(5-hydro-4-methyl-2-oxazolyl)phenoxy)pentyl)-3-methyl isoxazole.
DR DrugBank; DB08719; 5-(5-(6-CHLORO-4-(4,5-DIHYDRO-2-OXAZOLYL)PHENOXY)PENTYL)-3-METHYL ISOXAZOLE.
DR DrugBank; DB08726; 5-(7-(4-(4,5-dihydro-2-oxazolyl)phenoxy)heptyl)-3-methyl isoxazole.
DR DrugBank; DB08722; 5-(7-(6-chloro-4-(5-hydro-4-methyl-2-oxazolyl)phenoxy)heptyl)-3-methyl isoxazole.
DR DrugBank; DB05102; Rupintrivir.
DR DrugBank; DB03203; Sphingosine.
DR DrugBank; DB08723; WIN-54954.
DR MEROPS; C03.013; -.
DR MEROPS; C03.020; -.
DR MEROPS; N08.001; -.
DR PRIDE; P03303; -.
DR ABCD; P03303; 3 sequenced antibodies.
DR DNASU; 1461213; -.
DR GeneID; 1461213; -.
DR KEGG; vg:1461213; -.
DR EvolutionaryTrace; P03303; -.
DR Proteomes; UP000007679; Genome.
DR Proteomes; UP000118299; Genome.
DR GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0039618; C:T=pseudo3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0039520; P:induction by virus of host autophagy; ISS:UniProtKB.
DR GO; GO:0039664; P:lysis of host organelle involved in viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0044694; P:pore-mediated entry of viral genome into host cell; IEA:UniProtKB-KW.
DR GO; GO:0039690; P:positive stranded viral RNA replication; ISS:UniProtKB.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR GO; GO:0039522; P:suppression by virus of host mRNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0039611; P:suppression by virus of host translation initiation factor activity; ISS:UniProtKB.
DR GO; GO:0039540; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host RIG-I activity; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR CDD; cd00205; rhv_like; 3.
DR Gene3D; 2.40.10.10; -; 4.
DR Gene3D; 2.60.120.20; -; 3.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 4.10.80.10; -; 1.
DR Gene3D; 6.10.20.20; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014838; P3A.
DR InterPro; IPR036203; P3A_soluble_dom.
DR InterPro; IPR044067; PCV_3C_PRO.
DR InterPro; IPR000081; Peptidase_C3.
DR InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR003138; Pico_P1A.
DR InterPro; IPR036988; Pico_P1A_sf.
DR InterPro; IPR002527; Pico_P2B.
DR InterPro; IPR001676; Picornavirus_capsid.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR033703; Rhv-like.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR029053; Viral_coat.
DR Pfam; PF08727; P3A; 1.
DR Pfam; PF00548; Peptidase_C3; 1.
DR Pfam; PF02226; Pico_P1A; 1.
DR Pfam; PF00947; Pico_P2A; 1.
DR Pfam; PF01552; Pico_P2B; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00073; Rhv; 3.
DR Pfam; PF00910; RNA_helicase; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50494; SSF50494; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF89043; SSF89043; 1.
DR PROSITE; PS51874; PCV_3C_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activation of host autophagy by virus; ATP-binding;
KW Autocatalytic cleavage; Capsid protein; Covalent protein-RNA linkage;
KW DNA replication; Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host translation shutoff by virus; Helicase; Host cytoplasm;
KW Host cytoplasmic vesicle; Host gene expression shutoff by virus;
KW Host membrane; Host mRNA suppression by virus; Host nucleus;
KW Host-virus interaction; Hydrolase;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host mRNA nuclear export by virus;
KW Inhibition of host RIG-I by virus; Inhibition of host RLR pathway by virus;
KW Ion channel; Ion transport; Lipoprotein; Magnesium; Membrane;
KW Metal-binding; Myristate; Nucleotide-binding; Nucleotidyltransferase;
KW Phosphoprotein; Pore-mediated penetration of viral genome into host cell;
KW Protease; Repeat; RNA-binding; RNA-directed RNA polymerase;
KW T=pseudo3 icosahedral capsid protein; Thiol protease; Transferase;
KW Transport; Viral attachment to host cell; Viral immunoevasion;
KW Viral ion channel; Viral penetration into host cytoplasm;
KW Viral penetration via lysis of host organellar membrane;
KW Viral RNA replication; Virion; Virus endocytosis by host;
KW Virus entry into host cell; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT CHAIN 2..2179
FT /note="Genome polyprotein"
FT /id="PRO_0000426536"
FT CHAIN 2..856
FT /note="P1"
FT /id="PRO_0000426537"
FT CHAIN 2..331
FT /note="Capsid protein VP0"
FT /id="PRO_0000426538"
FT CHAIN 2..69
FT /note="Capsid protein VP4"
FT /id="PRO_0000426539"
FT CHAIN 70..331
FT /note="Capsid protein VP2"
FT /id="PRO_0000426540"
FT CHAIN 332..561
FT /note="Capsid protein VP3"
FT /id="PRO_0000426541"
FT CHAIN 562..856
FT /note="Capsid protein VP1"
FT /id="PRO_0000426542"
FT CHAIN 857..1429
FT /note="P2"
FT /id="PRO_0000426543"
FT CHAIN 857..1002
FT /note="Protease 2A"
FT /id="PRO_0000040029"
FT CHAIN 1003..1099
FT /note="Protein 2B"
FT /id="PRO_0000040030"
FT CHAIN 1100..1429
FT /note="Protein 2C"
FT /id="PRO_0000426544"
FT CHAIN 1430..2179
FT /note="P3"
FT /id="PRO_0000426545"
FT CHAIN 1430..1537
FT /note="Protein 3AB"
FT /id="PRO_0000426546"
FT CHAIN 1430..1514
FT /note="Protein 3A"
FT /id="PRO_0000040032"
FT CHAIN 1515..1537
FT /note="Viral protein genome-linked"
FT /id="PRO_0000426547"
FT CHAIN 1538..2179
FT /note="Protein 3CD"
FT /id="PRO_0000426548"
FT CHAIN 1538..1719
FT /note="Protease 3C"
FT /id="PRO_0000426549"
FT CHAIN 1720..2179
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000426550"
FT TOPO_DOM 2..1491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 1492..1507
FT /evidence="ECO:0000255"
FT TOPO_DOM 1508..2179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1205..1361
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1538..1715
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1946..2060
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ZN_FING 1369..1386
FT /note="C4-type"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..584
FT /note="Amphipathic alpha-helix"
FT /evidence="ECO:0000255"
FT REGION 1101..1239
FT /note="Oligomerization"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1101..1173
FT /note="Membrane-binding"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1122..1126
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1413..1420
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1424..1429
FT /note="Oligomerization"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT ACT_SITE 876
FT /note="For protease 2A activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT ACT_SITE 894
FT /note="For protease 2A activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT ACT_SITE 965
FT /note="For protease 2A activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT ACT_SITE 1577
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1608
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1683
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT BINDING 911
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q9QF31"
FT BINDING 913
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q9QF31"
FT BINDING 971
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q9QF31"
FT BINDING 973
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q9QF31"
FT BINDING 1369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT BINDING 1372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT BINDING 1381
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT BINDING 1386
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT BINDING 1952
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT BINDING 1952
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT BINDING 2046
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT BINDING 2046
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT SITE 69..70
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000305|PubMed:8383233"
FT SITE 331..332
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 856..857
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1002..1003
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1099..1100
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1125
FT /note="Involved in the interaction with host RTN3"
FT /evidence="ECO:0000250|UniProtKB:Q66478"
FT SITE 1429..1430
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1514..1515
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1537..1538
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1719..1720
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT MOD_RES 1517
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT MUTAGEN 1683
FT /note="C->A: Inhibits protease 3C activity on host NLRP1."
FT /evidence="ECO:0000269|PubMed:33093214"
FT CONFLICT 368
FT /note="P -> L (in Ref. 3; AAA45756)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="I -> T (in Ref. 3; AAA45756)"
FT /evidence="ECO:0000305"
FT CONFLICT 722
FT /note="P -> H (in Ref. 3; AAA45756)"
FT /evidence="ECO:0000305"
FT CONFLICT 726..727
FT /note="NP -> KS (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 729..731
FT /note="EWD -> RVG (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 913
FT /note="C -> R (in Ref. 3; AAA45756)"
FT /evidence="ECO:0000305"
FT CONFLICT 942
FT /note="N -> S (in Ref. 3; AAA45756)"
FT /evidence="ECO:0000305"
FT CONFLICT 962
FT /note="P -> L (in Ref. 3; AAA45756)"
FT /evidence="ECO:0000305"
FT CONFLICT 982
FT /note="G -> E (in Ref. 3; AAA45756)"
FT /evidence="ECO:0000305"
FT CONFLICT 1193
FT /note="L -> F (in Ref. 3; AAA45756)"
FT /evidence="ECO:0000305"
FT CONFLICT 1193
FT /note="L -> H (in Ref. 2; AAA45758)"
FT /evidence="ECO:0000305"
FT CONFLICT 1220
FT /note="I -> T (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 1399
FT /note="I -> V (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 1446
FT /note="P -> S (in Ref. 3; AAA45756)"
FT /evidence="ECO:0000305"
FT CONFLICT 1739
FT /note="P -> A (in Ref. 3; AAA45756)"
FT /evidence="ECO:0000305"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1NCQ"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:5W3M"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:5W3O"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:5W3M"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:5W3M"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:5W3M"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:5W3M"
FT HELIX 159..167
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 168..180
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 188..197
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:5W3M"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:5W3M"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:5W3M"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:1K5M"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:5W3M"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:5W3M"
FT HELIX 247..252
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:5W3M"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 287..298
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 307..323
FT /evidence="ECO:0007829|PDB:5W3M"
FT TURN 339..342
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 368..373
FT /evidence="ECO:0007829|PDB:5W3E"
FT HELIX 374..377
FT /evidence="ECO:0007829|PDB:5W3M"
FT TURN 386..389
FT /evidence="ECO:0007829|PDB:1R09"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:5W3M"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 399..402
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 410..415
FT /evidence="ECO:0007829|PDB:5W3M"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:5W3M"
FT HELIX 427..432
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 435..440
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 442..448
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 455..463
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:5W3M"
FT HELIX 474..477
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 479..485
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 491..496
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 505..508
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 509..512
FT /evidence="ECO:0007829|PDB:1K5M"
FT STRAND 517..527
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 536..544
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 549..553
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 557..559
FT /evidence="ECO:0007829|PDB:5W3M"
FT HELIX 580..582
FT /evidence="ECO:0007829|PDB:1K5M"
FT STRAND 585..587
FT /evidence="ECO:0007829|PDB:5W3M"
FT HELIX 604..606
FT /evidence="ECO:0007829|PDB:5W3M"
FT HELIX 614..616
FT /evidence="ECO:0007829|PDB:5W3M"
FT HELIX 630..632
FT /evidence="ECO:0007829|PDB:5W3M"
FT HELIX 634..637
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 642..651
FT /evidence="ECO:0007829|PDB:5W3M"
FT TURN 660..664
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 665..670
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 673..676
FT /evidence="ECO:0007829|PDB:5W3M"
FT HELIX 677..683
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 686..702
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 714..719
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 722..724
FT /evidence="ECO:0007829|PDB:2RM2"
FT STRAND 729..731
FT /evidence="ECO:0007829|PDB:2HWB"
FT HELIX 733..736
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 738..740
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 742..746
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 749..755
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 760..766
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 772..774
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 776..778
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 780..782
FT /evidence="ECO:0007829|PDB:1RUE"
FT HELIX 784..786
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 790..795
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 804..822
FT /evidence="ECO:0007829|PDB:5W3M"
FT STRAND 832..834
FT /evidence="ECO:0007829|PDB:1NCQ"
FT HELIX 1446..1455
FT /evidence="ECO:0007829|PDB:6HLT"
FT HELIX 1459..1467
FT /evidence="ECO:0007829|PDB:6HLT"
FT STRAND 1470..1473
FT /evidence="ECO:0007829|PDB:6HLT"
FT STRAND 1479..1482
FT /evidence="ECO:0007829|PDB:6HLT"
FT HELIX 1542..1550
FT /evidence="ECO:0007829|PDB:6KYZ"
FT STRAND 1552..1557
FT /evidence="ECO:0007829|PDB:6KYZ"
FT STRAND 1560..1569
FT /evidence="ECO:0007829|PDB:6KYZ"
FT STRAND 1571..1575
FT /evidence="ECO:0007829|PDB:6KYZ"
FT HELIX 1576..1578
FT /evidence="ECO:0007829|PDB:6KYZ"
FT STRAND 1582..1586
FT /evidence="ECO:0007829|PDB:6KYZ"
FT STRAND 1589..1600
FT /evidence="ECO:0007829|PDB:6KYZ"
FT TURN 1602..1604
FT /evidence="ECO:0007829|PDB:2B0F"
FT STRAND 1606..1614
FT /evidence="ECO:0007829|PDB:6KYZ"
FT HELIX 1624..1626
FT /evidence="ECO:0007829|PDB:6KYZ"
FT STRAND 1635..1642
FT /evidence="ECO:0007829|PDB:6KYZ"
FT STRAND 1645..1663
FT /evidence="ECO:0007829|PDB:6KYZ"
FT STRAND 1666..1676
FT /evidence="ECO:0007829|PDB:6KYZ"
FT HELIX 1680..1682
FT /evidence="ECO:0007829|PDB:6KYZ"
FT STRAND 1686..1689
FT /evidence="ECO:0007829|PDB:6KYZ"
FT STRAND 1692..1700
FT /evidence="ECO:0007829|PDB:6KYZ"
FT STRAND 1702..1709
FT /evidence="ECO:0007829|PDB:6KYZ"
FT HELIX 1712..1714
FT /evidence="ECO:0007829|PDB:6KYZ"
FT STRAND 1721..1726
FT /evidence="ECO:0007829|PDB:1XR5"
FT HELIX 1728..1731
FT /evidence="ECO:0007829|PDB:1XR5"
FT HELIX 1748..1750
FT /evidence="ECO:0007829|PDB:1XR5"
FT HELIX 1773..1778
FT /evidence="ECO:0007829|PDB:1XR5"
FT HELIX 1791..1805
FT /evidence="ECO:0007829|PDB:1XR5"
FT HELIX 1816..1821
FT /evidence="ECO:0007829|PDB:1XR5"
FT STRAND 1824..1826
FT /evidence="ECO:0007829|PDB:1XR5"
FT HELIX 1839..1842
FT /evidence="ECO:0007829|PDB:1XR5"
FT HELIX 1846..1849
FT /evidence="ECO:0007829|PDB:1XR5"
FT TURN 1852..1855
FT /evidence="ECO:0007829|PDB:1XR5"
FT HELIX 1858..1867
FT /evidence="ECO:0007829|PDB:1XR5"
FT STRAND 1873..1877
FT /evidence="ECO:0007829|PDB:1XR5"
FT HELIX 1884..1888
FT /evidence="ECO:0007829|PDB:1XR5"
FT STRAND 1894..1897
FT /evidence="ECO:0007829|PDB:1XR5"
FT HELIX 1900..1906
FT /evidence="ECO:0007829|PDB:1XR5"
FT TURN 1907..1909
FT /evidence="ECO:0007829|PDB:1XR5"
FT HELIX 1911..1919
FT /evidence="ECO:0007829|PDB:1XR5"
FT TURN 1923..1926
FT /evidence="ECO:0007829|PDB:1XR5"
FT HELIX 1933..1936
FT /evidence="ECO:0007829|PDB:1XR5"
FT HELIX 1937..1939
FT /evidence="ECO:0007829|PDB:1XR5"
FT HELIX 1940..1943
FT /evidence="ECO:0007829|PDB:1XR5"
FT STRAND 1949..1955
FT /evidence="ECO:0007829|PDB:1XR5"
FT HELIX 1957..1959
FT /evidence="ECO:0007829|PDB:1XR5"
FT HELIX 1962..1975
FT /evidence="ECO:0007829|PDB:1XR5"
FT TURN 1978..1981
FT /evidence="ECO:0007829|PDB:1XR5"
FT HELIX 1982..1987
FT /evidence="ECO:0007829|PDB:1XR5"
FT STRAND 1988..1992
FT /evidence="ECO:0007829|PDB:1XR5"
FT STRAND 1994..2002
FT /evidence="ECO:0007829|PDB:1XR5"
FT STRAND 2008..2010
FT /evidence="ECO:0007829|PDB:1XR5"
FT HELIX 2011..2030
FT /evidence="ECO:0007829|PDB:1XR5"
FT HELIX 2036..2038
FT /evidence="ECO:0007829|PDB:1XR5"
FT STRAND 2040..2044
FT /evidence="ECO:0007829|PDB:1XR5"
FT STRAND 2047..2051
FT /evidence="ECO:0007829|PDB:1XR5"
FT HELIX 2058..2065
FT /evidence="ECO:0007829|PDB:1XR5"
FT TURN 2066..2069
FT /evidence="ECO:0007829|PDB:1XR5"
FT TURN 2086..2088
FT /evidence="ECO:0007829|PDB:1XR5"
FT STRAND 2094..2098
FT /evidence="ECO:0007829|PDB:1XR5"
FT STRAND 2100..2102
FT /evidence="ECO:0007829|PDB:1XR5"
FT STRAND 2105..2109
FT /evidence="ECO:0007829|PDB:1XR5"
FT HELIX 2112..2119
FT /evidence="ECO:0007829|PDB:1XR5"
FT STRAND 2121..2124
FT /evidence="ECO:0007829|PDB:1XR5"
FT TURN 2125..2127
FT /evidence="ECO:0007829|PDB:1XR5"
FT HELIX 2128..2139
FT /evidence="ECO:0007829|PDB:1XR5"
FT HELIX 2140..2142
FT /evidence="ECO:0007829|PDB:1XR5"
FT HELIX 2144..2154
FT /evidence="ECO:0007829|PDB:1XR5"
FT HELIX 2158..2162
FT /evidence="ECO:0007829|PDB:1XR5"
FT HELIX 2168..2177
FT /evidence="ECO:0007829|PDB:1XR5"
SQ SEQUENCE 2179 AA; 242991 MW; 827201A3032F0285 CRC64;
MGAQVSTQKS GSHENQNILT NGSNQTFTVI NYYKDAASTS SAGQSLSMDP SKFTEPVKDL
MLKGAPALNS PNVEACGYSD RVQQITLGNS TITTQEAANA VVCYAEWPEY LPDVDASDVN
KTSKPDTSVC RFYTLDSKTW TTGSKGWCWK LPDALKDMGV FGQNMFFHSL GRSGYTVHVQ
CNATKFHSGC LLVVVIPEHQ LASHEGGNVS VKYTFTHPGE RGIDLSSANE VGGPVKDVIY
NMNGTLLGNL LIFPHQFINL RTNNTATIVI PYINSVPIDS MTRHNNVSLM VIPIAPLTVP
TGATPSLPIT VTIAPMCTEF SGIRSKSIVP QGLPTTTLPG SGQFLTTDDR QSPSALPNYE
PTPRIHIPGK VHNLLEIIQV DTLIPMNNTH TKDEVNSYLI PLNANRQNEQ VFGTNLFIGD
GVFKTTLLGE IVQYYTHWSG SLRFSLMYTG PALSSAKLIL AYTPPGARGP QDRREAMLGT
HVVWDIGLQS TIVMTIPWTS GVQFRYTDPD TYTSAGFLSC WYQTSLILPP ETTGQVYLLS
FISACPDFKL RLMKDTQTIS QTVALTEGLG DELEEVIVEK TKQTVASISS GPKHTQKVPI
LTANETGATM PVLPSDSIET RTTYMHFNGS ETDVECFLGR AACVHVTEIQ NKDATGIDNH
REAKLFNDWK INLSSLVQLR KKLELFTYVR FDSEYTILAT ASQPDSANYS SNLVVQAMYV
PPGAPNPKEW DDYTWQSASN PSVFFKVGDT SRFSVPYVGL ASAYNCFYDG YSHDDAETQY
GITVLNHMGS MAFRIVNEHD EHKTLVKIRV YHRAKHVEAW IPRAPRALPY TSIGRTNYPK
NTEPVIKKRK GDIKSYGLGP RYGGIYTSNV KIMNYHLMTP EDHHNLIAPY PNRDLAIVST
GGHGAETIPH CNCTSGVYYS TYYRKYYPII CEKPTNIWIE GNPYYPSRFQ AGVMKGVGPA
EPGDCGGILR CIHGPIGLLT AGGSGYVCFA DIRQLECIAE EQGLSDYITG LGRAFGVGFT
DQISTKVTEL QEVAKDFLTT KVLSKVVKMV SALVIICRNH DDLVTVTATL ALLGCDGSPW
RFLKMYISKH FQVPYIERQA NDGWFRKFND ACNAAKGLEW IANKISKLIE WIKNKVLPQA
KEKLEFCSKL KQLDILERQI TTMHISNPTQ EKREQLFNNV LWLEQMSQKF APLYAVESKR
IRELKNKMVN YMQFKSKQRI EPVCVLIHGT PGSGKSLTTS IVGRAIAEHF NSAVYSLPPD
PKHFDGYQQQ EVVIMDDLNQ NPDGQDISMF CQMVSSVDFL PPMASLDNKG MLFTSNFVLA
STNSNTLSPP TILNPEALVR RFGFDLDICL HTTYTKNGKL NAGMSTKTCK DCHQPSNFKK
CCPLVCGKAI SLVDRTTNIR YSVDQLVTAI ISDFKSKMQI TDSLETLFQG PVYKDLEIDV
CNTPPPECIN DLLKSVDSEE IREYCKKKKW IIPEIPTNIE RAMNQASMII NTILMFVSTL
GIVYVIYKLF AQTQGPYSGN PPHNKLKAPT LRPVVVQGPN TEFALSLLRK NIMTITTSKG
EFTGLGIHDR VCVIPTHAQP GDDVLVNGQK IRVKDKYKLV DPENINLELT VLTLDRNEKF
RDIRGFISED LEGVDATLVV HSNNFTNTIL EVGPVTMAGL INLSSTPTNR MIRYDYATKT
GQCGGVLCAT GKIFGIHVGG NGRQGFSAQL KKQYFVEKQG QVIARHKVRE FNINPVNTPT
KSKLHPSVFY DVFPGDKEPA VLSDNDPRLE VKLTESLFSK YKGNVNTEPT ENMLVAVDHY
AGQLLSLDIP TSELTLKEAL YGVDGLEPID ITTSAGFPYV SLGIKKRDIL NKETQDTEKM
KFYLDKYGID LPLVTYIKDE LRSVDKVRLG KSRLIEASSL NDSVNMRMKL GNLYKAFHQN
PGVLTGSAVG CDPDVFWSVI PCLMDGHLMA FDYSNFDASL SPVWFVCLEK VLTKLGFAGS
SLIQSICNTH HIFRDEIYVV EGGMPSGCSG TSIFNSMINN IIIRTLILDA YKGIDLDKLK
ILAYGDDLIV SYPYELDPQV LATLGKNYGL TITPPDKSET FTKMTWENLT FLKRYFKPDQ
QFPFLVHPVM PMKDIHESIR WTKDPKNTQD HVRSLCMLAW HSGEKEYNEF IQKIRTTDIG
KCLILPEYSV LRRRWLDLF
