POLG_HRV2
ID POLG_HRV2 Reviewed; 2150 AA.
AC P04936;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 204.
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 2 (HRV-2).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Enterovirus; Rhinovirus A.
OX NCBI_TaxID=12130;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2987843; DOI=10.1093/nar/13.6.2111;
RA Skern T., Sommergruber W., Blaas D., Gruendler P., Fraundorfer F.,
RA Pieler C., Fogy I., Kuechler E.;
RT "Human rhinovirus 2: complete nucleotide sequence and proteolytic
RT processing signals in the capsid protein region.";
RL Nucleic Acids Res. 13:2111-2126(1985).
RN [2]
RP SEQUENCE REVISION.
RA Kuechler E.;
RL Submitted (FEB-1986) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBUNIT (PROTEASE 2A), AND ZINC-BINDING (PROTEASE 2A).
RX PubMed=8580843; DOI=10.1002/pro.5560041209;
RA Voss T., Meyer R., Sommergruber W.;
RT "Spectroscopic characterization of rhinoviral protease 2A: Zn is essential
RT for the structural integrity.";
RL Protein Sci. 4:2526-2531(1995).
RN [4]
RP FUNCTION (LEADER PROTEASE).
RX PubMed=11034318; DOI=10.1016/s0014-5793(00)01928-1;
RA Glaser W., Skern T.;
RT "Extremely efficient cleavage of eIF4G by picornaviral proteinases L and 2A
RT in vitro.";
RL FEBS Lett. 480:151-155(2000).
RN [5]
RP FUNCTION (CAPSID PROTEIN VP1), AND FUNCTION (CAPSID PROTEIN VP4).
RX PubMed=12191477; DOI=10.1016/s1097-2765(02)00603-2;
RA Hewat E.A., Neumann E., Blaas D.;
RT "The concerted conformational changes during human rhinovirus 2
RT uncoating.";
RL Mol. Cell 10:317-326(2002).
RN [6]
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 [7]
RP FUNCTION (PROTEASE 2A).
RX PubMed=20622012; DOI=10.1074/jbc.m110.143404;
RA Park N., Skern T., Gustin K.E.;
RT "Specific cleavage of the nuclear pore complex protein Nup62 by a viral
RT protease.";
RL J. Biol. Chem. 285:28796-28805(2010).
RN [8]
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 [9]
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 [10]
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 [11]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 225-239.
RX PubMed=1338980; DOI=10.1002/pro.5560010909;
RA Tormo J., Stadler E., Skern T., Auer H., Kanzler O., Betzel C., Blaas D.,
RA Fita I.;
RT "Three-dimensional structure of the Fab fragment of a neutralizing antibody
RT to human rhinovirus serotype 2.";
RL Protein Sci. 1:1154-1161(1992).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 851-992.
RX PubMed=10523291; DOI=10.1093/emboj/18.20.5463;
RA Petersen J.F., Cherney M.M., Liebig H.D., Skern T., Kuechler E.,
RA James M.N.;
RT "The structure of the 2A proteinase from a common cold virus: a proteinase
RT responsible for the shut-off of host-cell protein synthesis.";
RL EMBO J. 18:5463-5475(1999).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1508-1687.
RX PubMed=10500114; DOI=10.1073/pnas.96.20.11000;
RA Matthews D.A., Dragovich P.S., Webber S.E., Fuhrman S.A., Patick A.K.,
RA Zalman L.S., Hendrickson T.F., Love R.A., Prins T.J., Marakovits J.T.,
RA Zhou R., Tikhe J., Ford C.E., Meador J.W., Ferre R.A., Brown E.L.,
RA Binford S.L., Brothers M.A., DeLisle D.M., Worland S.T.;
RT "Structure-assisted design of mechanism-based irreversible inhibitors of
RT human rhinovirus 3C protease with potent antiviral activity against
RT multiple rhinovirus serotypes.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11000-11007(1999).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 71-856.
RX PubMed=10903863; DOI=10.1006/jmbi.2000.3943;
RA Verdaguer N., Blaas D., Fita I.;
RT "Structure of human rhinovirus serotype 2 (HRV2).";
RL J. Mol. Biol. 300:1179-1194(2000).
CC -!- FUNCTION: [Capsid protein VP1]: 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). Capsid protein VP1 mainly forms the vertices of the capsid
CC (By similarity). Capsid protein VP1 interacts with host cell receptor
CC to provide virion attachment to target host cells (By similarity). This
CC attachment induces virion internalization (By similarity). Tyrosine
CC kinases are probably involved in the entry process (By similarity).
CC After binding to its receptor, the capsid undergoes conformational
CC changes (By similarity). Capsid protein VP1 N-terminus (that contains
CC an amphipathic alpha-helix) and capsid protein VP4 are externalized (By
CC similarity). Together, they shape a pore in the host membrane through
CC which viral genome is translocated to host cell cytoplasm (By
CC similarity). {ECO:0000250|UniProtKB:P03300}.
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
CC (PubMed:11034318). Inhibits the host nucleus-cytoplasm protein and RNA
CC trafficking by cleaving host members of the nuclear pores
CC (PubMed:20622012). Counteracts stress granule formation probably by
CC antagonizing its assembly or promoting its dissassembly (By
CC similarity). {ECO:0000250|UniProtKB:P03300,
CC ECO:0000250|UniProtKB:P03301, ECO:0000269|PubMed:11034318,
CC ECO:0000269|PubMed:20622012}.
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. It inhibits host cell endoplasmic
CC reticulum-to-Golgi apparatus transport and causes the disassembly of
CC the Golgi complex, possibly through GBF1 interaction (PubMed:17005635).
CC This would result in depletion of MHC, trail receptors and IFN
CC receptors at the host cell surface (PubMed:17005635). Plays an
CC essential role in viral RNA replication by recruiting ACBD3 and PI4KB
CC at the viral replication sites, thereby allowing the formation of the
CC rearranged membranous structures where viral replication takes place
CC (Probable). {ECO:0000269|PubMed:17005635, ECO:0000305|PubMed:30755512}.
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: [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 -!- 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 (By similarity). Cleaves also
CC host PABPC1, contributing to host translation shutoff (By similarity).
CC Cleaves host NLRP1, triggers host N-glycine-mediated degradation of the
CC autoinhibitory NLRP1 N-terminal fragment (By similarity).
CC {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P03303}.
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).
CC {ECO:0000250|UniProtKB:P03300}.
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:0000269|PubMed:8580843}.
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 (By similarity).
CC {ECO:0000250|UniProtKB:P03300, ECO:0000269|PubMed:17005635}.
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
CC degenerate C4-type zinc-finger with only 3 cysteines (By similarity).
CC The C-terminus is involved in RNA-binding (By similarity). The extreme
CC C-terminus contains a region involved in oligomerization (By
CC similarity). {ECO:0000250|UniProtKB:B9VUU3,
CC 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:0000250|UniProtKB:P03300}.
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 -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure associated with cellular receptor;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1fpn";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure complexed with cellular receptor fragment;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1v9u";
CC ---------------------------------------------------------------------------
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DR EMBL; X02316; CAA26181.1; -; Genomic_RNA.
DR PIR; A03902; GNNYH2.
DR PDB; 1A3R; X-ray; 2.10 A; P=225-239.
DR PDB; 1CQQ; X-ray; 1.85 A; A=1508-1687.
DR PDB; 1FPN; X-ray; 2.60 A; 1=568-856, 2=70-330, 3=331-567, 4=2-69.
DR PDB; 1V9U; X-ray; 3.60 A; 1=568-856, 2=70-330, 3=331-567, 4=2-69.
DR PDB; 2HRV; X-ray; 1.95 A; A/B=851-992.
DR PDB; 2XYA; X-ray; 2.40 A; A=1508-1687.
DR PDB; 3DPR; X-ray; 3.50 A; A=568-856, B=70-330, C=331-567, D=2-69.
DR PDB; 3TN9; X-ray; 3.00 A; 1=568-856, 2=70-330, 3=331-567.
DR PDB; 3VDD; X-ray; 3.20 A; A=568-850, B=70-330, C=331-567, D=1-69.
DR PDB; 4L3B; X-ray; 6.50 A; A=568-856, B=70-330, C=331-567.
DR PDB; 5FX5; X-ray; 1.70 A; A=1508-1687.
DR PDB; 5FX6; X-ray; 1.45 A; A=1508-1687.
DR PDB; 6FFN; X-ray; 1.75 A; A=1508-1687.
DR PDB; 6FFS; X-ray; 1.86 A; A=1508-1687.
DR PDB; 7ARA; X-ray; 2.24 A; A/B=851-992.
DR PDBsum; 1A3R; -.
DR PDBsum; 1CQQ; -.
DR PDBsum; 1FPN; -.
DR PDBsum; 1V9U; -.
DR PDBsum; 2HRV; -.
DR PDBsum; 2XYA; -.
DR PDBsum; 3DPR; -.
DR PDBsum; 3TN9; -.
DR PDBsum; 3VDD; -.
DR PDBsum; 4L3B; -.
DR PDBsum; 5FX5; -.
DR PDBsum; 5FX6; -.
DR PDBsum; 6FFN; -.
DR PDBsum; 6FFS; -.
DR PDBsum; 7ARA; -.
DR SMR; P04936; -.
DR DrugBank; DB02313; Ethyl (4R)-4-{[(2R,5S)-2-(4-fluorobenzyl)-6-methyl-5-{[(5-methyl-1,2-oxazol-3-yl)carbonyl]amino}-4-oxoheptanoyl]amino}-5-[(3S)-2-oxo-3-pyrrolidinyl]pentanoate.
DR DrugBank; DB03017; Lauric acid.
DR MEROPS; C03.007; -.
DR MEROPS; C03.021; -.
DR MEROPS; N08.001; -.
DR PRIDE; P04936; -.
DR ABCD; P04936; 1 sequenced antibody.
DR SABIO-RK; P04936; -.
DR EvolutionaryTrace; P04936; -.
DR Proteomes; UP000007682; 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; IDA:UniProtKB.
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; IDA: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; -; 2.
DR Gene3D; 2.60.120.20; -; 3.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 6.10.20.20; -; 1.
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; 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 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 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..2150
FT /note="Genome polyprotein"
FT /id="PRO_0000426506"
FT CHAIN 2..850
FT /note="P1"
FT /id="PRO_0000426507"
FT CHAIN 2..330
FT /note="Capsid protein VP0"
FT /id="PRO_0000426508"
FT CHAIN 2..69
FT /note="Capsid protein VP4"
FT /id="PRO_0000426509"
FT CHAIN 70..330
FT /note="Capsid protein VP2"
FT /id="PRO_0000426510"
FT CHAIN 331..561
FT /note="Capsid protein VP3"
FT /id="PRO_0000426511"
FT CHAIN 562..850
FT /note="Capsid protein VP1"
FT /id="PRO_0000426512"
FT CHAIN 851..1409
FT /note="P2"
FT /id="PRO_0000426513"
FT CHAIN 851..992
FT /note="Protease 2A"
FT /id="PRO_0000426514"
FT CHAIN 993..1087
FT /note="Protein 2B"
FT /id="PRO_0000040015"
FT CHAIN 1088..1409
FT /note="Protein 2C"
FT /id="PRO_0000040016"
FT CHAIN 1410..2150
FT /note="P3"
FT /id="PRO_0000426515"
FT CHAIN 1410..1507
FT /note="Protein 3AB"
FT /id="PRO_0000426516"
FT CHAIN 1410..1486
FT /note="Protein 3A"
FT /id="PRO_0000040017"
FT CHAIN 1487..1507
FT /note="Viral protein genome-linked"
FT /id="PRO_0000426517"
FT CHAIN 1508..2150
FT /note="Protein 3CD"
FT /id="PRO_0000426518"
FT CHAIN 1508..1690
FT /note="Protease 3C"
FT /id="PRO_0000426519"
FT CHAIN 1691..2150
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000426520"
FT TOPO_DOM 2..1463
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 1464..1479
FT /evidence="ECO:0000255"
FT TOPO_DOM 1480..2150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1181..1343
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1508..1686
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1918..2031
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ZN_FING 1350..1366
FT /note="C4-type; degenerate"
FT /evidence="ECO:0000250|UniProtKB:B9VUU3"
FT REGION 565..581
FT /note="Amphipathic alpha-helix"
FT /evidence="ECO:0000255"
FT REGION 592..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1221
FT /note="Oligomerization"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1088..1157
FT /note="Membrane-binding"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1109..1113
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1393..1400
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1404..1409
FT /note="Oligomerization"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT ACT_SITE 868
FT /note="For protease 2A activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT ACT_SITE 885
FT /note="For protease 2A activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT ACT_SITE 956
FT /note="For protease 2A activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT ACT_SITE 1547
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1578
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1654
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT BINDING 902
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:8580843"
FT BINDING 904
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:8580843"
FT BINDING 962
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:8580843"
FT BINDING 964
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000305|PubMed:8580843"
FT BINDING 1350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B9VUU3"
FT BINDING 1361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B9VUU3"
FT BINDING 1366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B9VUU3"
FT BINDING 1924
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 1924
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 2017
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 2017
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:0000250|UniProtKB:P03300"
FT SITE 330..331
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 850..851
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 992..993
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1087..1088
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1112
FT /note="Involved in the interaction with host RTN3"
FT /evidence="ECO:0000250|UniProtKB:Q66478"
FT SITE 1409..1410
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1486..1487
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1507..1508
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1690..1691
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT MOD_RES 1489
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 STRAND 33..35
FT /evidence="ECO:0007829|PDB:1FPN"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1FPN"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:3VDD"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:1FPN"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:1FPN"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:3TN9"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:1FPN"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1FPN"
FT HELIX 159..167
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 168..180
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 187..197
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:1FPN"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:1FPN"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:1FPN"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:1A3R"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:1FPN"
FT TURN 244..247
FT /evidence="ECO:0007829|PDB:1FPN"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:1FPN"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:1FPN"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 290..305
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 309..325
FT /evidence="ECO:0007829|PDB:1FPN"
FT TURN 338..341
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 367..372
FT /evidence="ECO:0007829|PDB:3DPR"
FT HELIX 374..377
FT /evidence="ECO:0007829|PDB:1FPN"
FT TURN 389..393
FT /evidence="ECO:0007829|PDB:1FPN"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 399..403
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 411..416
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 418..421
FT /evidence="ECO:0007829|PDB:3VDD"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:1FPN"
FT HELIX 428..433
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 436..441
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 443..449
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 456..464
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:1FPN"
FT HELIX 474..478
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 480..489
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 492..497
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 506..509
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 517..524
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 530..532
FT /evidence="ECO:0007829|PDB:3TN9"
FT STRAND 534..544
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 549..553
FT /evidence="ECO:0007829|PDB:1FPN"
FT TURN 572..579
FT /evidence="ECO:0007829|PDB:3VDD"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:3VDD"
FT STRAND 599..602
FT /evidence="ECO:0007829|PDB:3VDD"
FT HELIX 604..606
FT /evidence="ECO:0007829|PDB:1FPN"
FT HELIX 614..617
FT /evidence="ECO:0007829|PDB:1FPN"
FT HELIX 630..632
FT /evidence="ECO:0007829|PDB:1FPN"
FT HELIX 634..638
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 642..650
FT /evidence="ECO:0007829|PDB:1FPN"
FT TURN 654..658
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 661..665
FT /evidence="ECO:0007829|PDB:1FPN"
FT HELIX 672..678
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 681..698
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 707..713
FT /evidence="ECO:0007829|PDB:1FPN"
FT HELIX 726..729
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 731..733
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 735..739
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 746..749
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 754..760
FT /evidence="ECO:0007829|PDB:1FPN"
FT TURN 774..777
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 782..787
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 796..814
FT /evidence="ECO:0007829|PDB:1FPN"
FT STRAND 855..866
FT /evidence="ECO:0007829|PDB:2HRV"
FT HELIX 867..869
FT /evidence="ECO:0007829|PDB:2HRV"
FT HELIX 874..876
FT /evidence="ECO:0007829|PDB:2HRV"
FT STRAND 878..881
FT /evidence="ECO:0007829|PDB:2HRV"
FT HELIX 882..884
FT /evidence="ECO:0007829|PDB:2HRV"
FT STRAND 886..896
FT /evidence="ECO:0007829|PDB:2HRV"
FT STRAND 906..911
FT /evidence="ECO:0007829|PDB:2HRV"
FT TURN 912..915
FT /evidence="ECO:0007829|PDB:2HRV"
FT STRAND 916..921
FT /evidence="ECO:0007829|PDB:2HRV"
FT STRAND 923..930
FT /evidence="ECO:0007829|PDB:2HRV"
FT STRAND 934..936
FT /evidence="ECO:0007829|PDB:7ARA"
FT STRAND 938..948
FT /evidence="ECO:0007829|PDB:2HRV"
FT STRAND 959..962
FT /evidence="ECO:0007829|PDB:2HRV"
FT STRAND 965..973
FT /evidence="ECO:0007829|PDB:2HRV"
FT STRAND 975..982
FT /evidence="ECO:0007829|PDB:2HRV"
FT HELIX 983..986
FT /evidence="ECO:0007829|PDB:2HRV"
FT HELIX 1509..1521
FT /evidence="ECO:0007829|PDB:5FX6"
FT STRAND 1522..1527
FT /evidence="ECO:0007829|PDB:5FX6"
FT STRAND 1530..1539
FT /evidence="ECO:0007829|PDB:5FX6"
FT STRAND 1541..1545
FT /evidence="ECO:0007829|PDB:5FX6"
FT HELIX 1546..1548
FT /evidence="ECO:0007829|PDB:5FX6"
FT STRAND 1552..1556
FT /evidence="ECO:0007829|PDB:5FX6"
FT STRAND 1559..1570
FT /evidence="ECO:0007829|PDB:5FX6"
FT STRAND 1576..1584
FT /evidence="ECO:0007829|PDB:5FX6"
FT HELIX 1594..1596
FT /evidence="ECO:0007829|PDB:5FX6"
FT STRAND 1604..1611
FT /evidence="ECO:0007829|PDB:5FX6"
FT STRAND 1615..1617
FT /evidence="ECO:0007829|PDB:5FX6"
FT STRAND 1619..1634
FT /evidence="ECO:0007829|PDB:5FX6"
FT STRAND 1637..1647
FT /evidence="ECO:0007829|PDB:5FX6"
FT HELIX 1651..1653
FT /evidence="ECO:0007829|PDB:6FFN"
FT STRAND 1657..1660
FT /evidence="ECO:0007829|PDB:5FX6"
FT STRAND 1663..1671
FT /evidence="ECO:0007829|PDB:5FX6"
FT STRAND 1676..1680
FT /evidence="ECO:0007829|PDB:5FX6"
FT HELIX 1683..1685
FT /evidence="ECO:0007829|PDB:5FX6"
SQ SEQUENCE 2150 AA; 241978 MW; 6E0DF9F4945D9D0C CRC64;
MGAQVSRQNV GTHSTQNSVS NGSSLNYFNI NYFKDAASNG ASKLEFTQDP SKFTDPVKDV
LEKGIPTLQS PTVEACGYSD RIIQITRGDS TITSQDVANA IVAYGVWPHY LSSKDASAID
KPSQPDTSSN RFYTLRSVTW SSSSKGWWWK LPDALKDMGI FGENMFYHYL GRSGYTIHVQ
CNASKFHQGT LIVALIPEHQ IASALHGNVN VGYNYTHPGE TGREVKAETR LNPDLQPTEE
YWLNFDGTLL GNITIFPHQF INLRSNNSAT IIAPYVNAVP MDSMRSHNNW SLVIIPICPL
ETSSAINTIP ITISISPMCA EFSGARAKRQ GLPVFITPGS GQFLTTDDFQ SPCALPWYHP
TKEISIPGEV KNLVEICQVD SLVPINNTDT YINSENMYSV VLQSSINAPD KIFSIRTDVA
SQPLATTLIG EISSYFTHWT GSLRFSFMFC GTANTTVKLL LAYTPPGIAE PTTRKDAMLG
THVIWDVGLQ STISMVVPWI SASHYRNTSP GRSTSGYITC WYQTRLVIPP QTPPTARLLC
FVSGCKDFCL RMARDTNLHL QSGAIAQNPV ENYIDEVLNE VLVVPNINSS NPTTSNSAPA
LDAAETGHTS SVQPEDVIET RYVQTSQTRD EMSLESFLGR SGCIHESKLE VTLANYNKEN
FTVWAINLQE MAQIRRKFEL FTYTRFDSEI TLVPCISALS QDIGHITMQY MYVPPGAPVP
NSRDDYAWQS GTNASVFWQH GQAYPRFSLP FLSVASAYYM FYDGYDEQDQ NYGTANTNNM
GSLCSRIVTE KHIHKVHIMT RIYHKAKHVK AWCPRPPRAL EYTRAHRTNF KIEDRSIQTA
IVTRPIITTA GPSDMYVHVG NLIYRNLHLF NSEMHESILV SYSSDLIIYR TNTVGDDYIP
SCDCTQATYY CKHKNRYFPI TVTSHDWYEI QESEYYPKHI QYNLLIGEGP CEPGDCGGKL
LCKHGVIGIV TAGGDNHVAF IDLRHFHCAE EQGVTDYIHM LGEAFGNGFV DSVKEHIHAI
NPVGNISKKI IKWMLRIISA MVIIIRNSSD PQTILATLTL IGCSGSPWRF LKEKFCKWTQ
LNYIHKESDS WLKKFTEACN AARGLEWIGN KISKFIEWMK SMLPQAQLKV KYLNELKKLN
LYEKQVESLR VADMKTQEKI KMEIDTLHDL SRKFLPLYAS EAKRIKTLYI KCDNIIKQKK
RCEPVAIVIH GPPGAGKSIT TNFLAKMITN DSDIYSLPPD PKYFDGYDQQ SVVIMDDIMQ
NPAGDDMTLF CQMVSSVTFI PPMADLPDKG KAFDSRFVLC STNHSLLTPP TITSLPAMNR
RFFLDLDIIV HDNFKDPQGK LNVAAAFRPC DVDNRIGNAR CCPFVCGKAV SFKDRNSCNK
YSLAQVYNIM IEEDRRRRQV VDVMTAIFQG PIDMKNPPPP AITDLLQSVR TPEVIKYCEG
NRWIIPAECK IEKELNLANT IITIIANVIG MARIIYVIYK LFCTLQGPYS GEPKPKTKIP
ERRVVTQGPE EEFGMSLIKH NSCVITTENG KFTGLGVYDR FVVVPTHADP GKEIQVDGIT
TKVIDSYDLY NKNGIKLEIT VLKLDRNEKF RDIRRYIPNN EDDYPNCNLA LLANQPEPTI
INVGDVVSYG NILLSGNQTA RMLKYSYPTK SGYCGGVLYK IGQVLGIHVG GNGRDGFSAM
LLRSYFTDVQ GQITLSKKTS ECNLPSIHTP CKTKLQPSVF YDVFPGSKEP AVLSEKDARL
QVDFNEALFS KYKGNTDCSI NDHIRIASSH YAAQLITLDI DPKPITLEDS VFGTDGLEAL
DLNTSAGFPY IAMGVKKRDL INNKTKDISK LKEAIDKYGV DLPMVTFLKD ELRKHEKVIK
GKTRVIEASS VNDTLLFRTT FGNLFSKFHL NPGIVTGSAV GCDPEVFWSK IPAMLDDKCI
MAFDYTNYDG SIHPIWFEAL KQVLVDLSFN PTLIDRLCKS KHIFKNTYYE VEGGVPSGCS
GTSIFNTMIN NIIIRTLVLD AYKNIDLDKL KIIAYGDDVI FSYIHELDME AIAIEGVKYG
LTITPADKSN TFVKLDYSNV TFLKRGFKQD EKYNFLIHPT FPEDEIFESI RWTKKPSQMH
EHVLSLCHLM WHNGRDAYKK FVEKIRSVSA GRALYIPPYD LLLHEWYEKF
