POLG_AIVA8
ID POLG_AIVA8 Reviewed; 2432 AA.
AC O91464; Q91QP4;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Leader protein;
DE Short=L;
DE Contains:
DE RecName: Full=Capsid protein VP0;
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=Protein 2A;
DE Short=P2A;
DE Contains:
DE RecName: Full=Protein 2B;
DE Short=P2B;
DE Contains:
DE RecName: Full=Protein 2C;
DE Short=P2C;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:P03300};
DE Contains:
DE RecName: Full=Protein 3A;
DE Short=P3A;
DE Contains:
DE RecName: Full=VPg;
DE Short=P3B;
DE AltName: Full=Protein 3B;
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;
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 Aichi virus (strain Human/A846/88/1989) (AiV) (Aichi virus (strain
OS A846/88)).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Kobuvirus.
OX NCBI_TaxID=650132;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9733894; DOI=10.1128/jvi.72.10.8408-8412.1998;
RA Yamashita T., Sakae K., Tsuzuki H., Suzuki Y., Ishikawa N., Takeda N.,
RA Miyamura T., Yamazaki S.;
RT "Complete nucleotide sequence and genetic organization of Aichi virus, a
RT distinct member of the Picornaviridae associated with acute gastroenteritis
RT in humans.";
RL J. Virol. 72:8408-8412(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11483747; DOI=10.1128/jvi.75.17.8021-8030.2001;
RA Sasaki J., Kusuhara Y., Maeno Y., Kobayashi N., Yamashita T., Sakae K.,
RA Takeda N., Taniguchi K.;
RT "Construction of an infectious cDNA clone of Aichi virus (a new member of
RT the family Picornaviridae) and mutational analysis of a stem-loop structure
RT at the 5' end of the genome.";
RL J. Virol. 75:8021-8030(2001).
RN [3]
RP PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN), FUNCTION (LEADER PROTEIN), AND
RP MUTAGENESIS OF GLN-168.
RX PubMed=14512530; DOI=10.1128/jvi.77.20.10799-10807.2003;
RA Sasaki J., Nagashima S., Taniguchi K.;
RT "Aichi virus leader protein is involved in viral RNA replication and
RT encapsidation.";
RL J. Virol. 77:10799-10807(2003).
RN [4]
RP FUNCTION (PROTEIN 2A).
RX PubMed=18653460; DOI=10.1128/jvi.01051-08;
RA Sasaki J., Taniguchi K.;
RT "Aichi virus 2A protein is involved in viral RNA replication.";
RL J. Virol. 82:9765-9769(2008).
RN [5]
RP SUBUNIT (PROTEIN 2A), SUBUNIT (PROTEIN 2B), SUBUNIT (PROTEIN 2C), SUBUNIT
RP (PROTEIN 3A), INTERACTION WITH PROTEIN 2C (PROTEIN 3A), INTERACTION WITH
RP PROTEIN 3A (PROTEIN 2C), INTERACTION WITH PROTEIN 3C (PROTEIN 2A),
RP INTERACTION WITH PROTEIN 2A (PROTEIN 3C), INTERACTION WITH PROTEIN 2B
RP (PROTEIN 2A), INTERACTION WITH PROTEIN 2A (PROTEIN 2B), INTERACTION WITH
RP PROTEIN 2C (PROTEIN 2A), INTERACTION WITH PROTEIN 2A (PROTEIN 2C),
RP INTERACTION WITH PROTEIN 2C (PROTEIN 3C), AND INTERACTION WITH PROTEIN 3C
RP (PROTEIN 2C).
RX PubMed=19879907; DOI=10.1016/j.virusres.2009.10.009;
RA Ishikawa K., Sasaki J., Taniguchi K.;
RT "Overall linkage map of the nonstructural proteins of Aichi virus.";
RL Virus Res. 147:77-84(2010).
RN [6]
RP PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN), AND MUTAGENESIS OF
RP 1043-HIS--ILE-1046; 1107-ASN-CYS-1106 AND 1964-GLN-GLN-1965.
RX PubMed=22226945; DOI=10.1016/j.virusres.2011.12.013;
RA Sasaki J., Ishikawa K., Taniguchi K.;
RT "3CD, but not 3C, cleaves the VP1/2A site efficiently during Aichi virus
RT polyprotein processing through interaction with 2A.";
RL Virus Res. 163:592-598(2012).
RN [7]
RP INTERACTION WITH HOST ACBD3 (PROTEIN 2B), INTERACTION WITH HOST ACBD3
RP (PROTEIN 2C), INTERACTION WITH HOST ACBD3 (PROTEIN 3A), IDENTIFICATION IN A
RP COMPLEX PROTEIN 3A/ACBD3/PI4KB (PROTEIN 3A), FUNCTION (PROTEIN 3A),
RP SUBCELLULAR LOCATION (PROTEIN 2B), SUBCELLULAR LOCATION (PROTEIN 2C), AND
RP SUBCELLULAR LOCATION (PROTEIN 3A).
RX PubMed=22124328; DOI=10.1038/emboj.2011.429;
RA Sasaki J., Ishikawa K., Arita M., Taniguchi K.;
RT "ACBD3-mediated recruitment of PI4KB to picornavirus RNA replication
RT sites.";
RL EMBO J. 31:754-766(2012).
RN [8]
RP FUNCTION (PROTEIN 3A), MYRISTOYLATION AT GLY-1653, INTERACTION WITH HOST
RP ACBD3 (PROTEIN 3A), IDENTIFICATION IN A COMPLEX PROTEIN 3A/ACBD3/PI4KB
RP (PROTEIN 3A), MUTAGENESIS OF GLY-1653; ASN-1654; ARG-1655 AND ILE-1657, AND
RP INTERACTION WITH HOST PI4KB (PROTEIN 3A).
RX PubMed=22258260; DOI=10.1128/jvi.06778-11;
RA Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L., Derisi J.L.;
RT "The 3A protein from multiple picornaviruses utilizes the golgi adaptor
RT protein ACBD3 to recruit PI4KIIIbeta.";
RL J. Virol. 86:3605-3616(2012).
RN [9]
RP INTERACTION WITH HOST ACBD3 (PROTEIN 3A).
RX PubMed=23572552; DOI=10.1128/mbio.00098-13;
RA Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L., DeRisi J.L.;
RT "ACBD3 interaction with TBC1 domain 22 protein is differentially affected
RT by enteroviral and kobuviral 3A protein binding.";
RL MBio 4:E00098-E00098(2013).
RN [10]
RP IDENTIFICATION IN A COMPLEX PROTEIN 3A/ACBD3/PI4KB (PROTEIN 3A), FUNCTION
RP (PROTEIN 3A), SUBCELLULAR LOCATION (PROTEIN 2B), SUBCELLULAR LOCATION
RP (PROTEIN 2C), SUBCELLULAR LOCATION (PROTEIN 3A), AND MUTAGENESIS OF
RP ARG-1655 AND GLU-1663.
RX PubMed=24672044; DOI=10.1128/jvi.00208-14;
RA Ishikawa-Sasaki K., Sasaki J., Taniguchi K.;
RT "A complex comprising phosphatidylinositol 4-kinase IIIbeta, ACBD3, and
RT Aichi virus proteins enhances phosphatidylinositol 4-phosphate synthesis
RT and is critical for formation of the viral replication complex.";
RL J. Virol. 88:6586-6598(2014).
RN [11]
RP IDENTIFICATION IN A COMPLEX PROTEIN 3A/ACBD3/PI4KB (PROTEIN 3A), FUNCTION
RP (PROTEIN 3A), AND INTERACTION WITH HOST ACBD3.
RX PubMed=27989622; DOI=10.1016/j.str.2016.11.016;
RA McPhail J.A., Ottosen E.H., Jenkins M.L., Burke J.E.;
RT "The molecular basis of Aichi virus 3A protein activation of
RT phosphatidylinositol 4 kinase IIIbeta, PI4KB, through ACBD3.";
RL Structure 25:121-131(2017).
RN [12]
RP IDENTIFICATION IN A COMPLEX PROTEIN 3A/ACBD3/PI4KB (PROTEIN 3A),
RP SUBCELLULAR LOCATION (PROTEIN 3A), AND 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 [13] {ECO:0007744|PDB:5AOO}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 171-1016.
RX PubMed=26919522; DOI=10.1107/s2053230x16000923;
RA Sabin C., Plevka P.;
RT "The use of noncrystallographic symmetry averaging to solve structures from
RT data affected by perfect hemihedral twinning.";
RL Acta Crystallogr. F Struct. Biol. Commun. 72:188-197(2016).
RN [14] {ECO:0007744|PDB:5LVC}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS) OF 171-1016, FUNCTION
RP (CAPSID PROTEIN VP0), FUNCTION (CAPSID PROTEIN VP1), FUNCTION (CAPSID
RP PROTEIN VP3), SUBCELLULAR LOCATION (CAPSID PROTEIN VP0), SUBCELLULAR
RP LOCATION (CAPSID PROTEIN VP1), SUBCELLULAR LOCATION (CAPSID PROTEIN VP3),
RP INTERACTION WITH CAPSID PROTEIN VP1 (CAPSID PROTEIN VP0), INTERACTION WITH
RP CAPSID PROTEIN VP0 (CAPSID PROTEIN VP1), INTERACTION WITH CAPSID PROTEIN
RP VP3 (CAPSID PROTEIN VP0), INTERACTION WITH CAPSID PROTEIN VP0 (CAPSID
RP PROTEIN VP3), INTERACTION WITH CAPSID PROTEIN VP1 (CAPSID PROTEIN VP3), AND
RP INTERACTION WITH CAPSID PROTEIN VP3 (CAPSID PROTEIN VP1).
RX PubMed=27681122; DOI=10.1128/jvi.01601-16;
RA Sabin C., Fuzik T., Skubnik K., Palkova L., Lindberg A.M., Plevka P.;
RT "Structure of Aichi virus 1 and its empty particle: clues towards kobuvirus
RT genome release mechanism.";
RL J. Virol. 90:10800-10810(2016).
RN [15] {ECO:0007744|PDB:5GKA}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.70 ANGSTROMS) OF 174-762 AND 764-1016,
RP FUNCTION (CAPSID PROTEIN VP0), FUNCTION (CAPSID PROTEIN VP1), FUNCTION
RP (CAPSID PROTEIN VP3), SUBCELLULAR LOCATION (CAPSID PROTEIN VP0),
RP SUBCELLULAR LOCATION (CAPSID PROTEIN VP1), SUBCELLULAR LOCATION (CAPSID
RP PROTEIN VP3), INTERACTION WITH CAPSID PROTEIN VP1 (CAPSID PROTEIN VP0),
RP INTERACTION WITH CAPSID PROTEIN VP0 (CAPSID PROTEIN VP1), INTERACTION WITH
RP CAPSID PROTEIN VP3 (CAPSID PROTEIN VP0), INTERACTION WITH CAPSID PROTEIN
RP VP0 (CAPSID PROTEIN VP3), INTERACTION WITH CAPSID PROTEIN VP1 (CAPSID
RP PROTEIN VP3), AND INTERACTION WITH CAPSID PROTEIN VP3 (CAPSID PROTEIN VP1).
RX PubMed=27595320; DOI=10.1038/nmicrobiol.2016.150;
RA Zhu L., Wang X., Ren J., Kotecha A., Walter T.S., Yuan S., Yamashita T.,
RA Tuthill T.J., Fry E.E., Rao Z., Stuart D.I.;
RT "Structure of human Aichi virus and implications for receptor binding.";
RL Nat. Microbiol. 1:16150-16150(2016).
RN [16] {ECO:0007744|PDB:5LZ3}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 1653-1710, AND INTERACTION WITH
RP HOST ACBD3 (PROTEIN 3A).
RX PubMed=28065508; DOI=10.1016/j.str.2016.11.021;
RA Klima M., Chalupska D., Rozycki B., Humpolickova J., Rezabkova L.,
RA Silhan J., Baumlova A., Dubankova A., Boura E.;
RT "Kobuviral Non-structural 3A Proteins Act as Molecular Harnesses to Hijack
RT the Host ACBD3 Protein.";
RL Structure 25:219-230(2017).
CC -!- FUNCTION: [Leader protein]: Required for viral RNA replication and
CC viral RNA encapsidation (PubMed:14512530). Does not have any
CC proteolytic activity (PubMed:14512530). {ECO:0000269|PubMed:14512530}.
CC -!- FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP0 and VP3 (PubMed:27681122,
CC PubMed:27595320). Together they form an icosahedral capsid composed of
CC 60 copies of each VP0, VP1, and VP3 (PubMed:27681122, PubMed:27595320).
CC All the three latter proteins contain a beta-sheet structure called
CC beta-barrel jelly roll (PubMed:27595320). {ECO:0000269|PubMed:27595320,
CC ECO:0000269|PubMed:27681122}.
CC -!- FUNCTION: [Capsid protein VP0]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP1 and VP3 (PubMed:27681122,
CC PubMed:27595320). Together they form an icosahedral capsid composed of
CC 60 copies of each VP0, VP1, and VP3 (PubMed:27681122, PubMed:27595320).
CC All the three latter proteins contain a beta-sheet structure called
CC beta-barrel jelly roll (PubMed:27595320). {ECO:0000269|PubMed:27595320,
CC ECO:0000269|PubMed:27681122}.
CC -!- FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP0 and VP1 (PubMed:27681122,
CC PubMed:27595320). Together they form an icosahedral capsid composed of
CC 60 copies of each VP0, VP1, and VP3 (PubMed:27681122, PubMed:27595320).
CC All the three latter proteins contain a beta-sheet structure called
CC beta-barrel jelly roll (PubMed:27595320). {ECO:0000269|PubMed:27595320,
CC ECO:0000269|PubMed:27681122}.
CC -!- FUNCTION: [Protein 2A]: Required for viral RNA replication
CC (PubMed:18653460). Does not have any proteolytic activity
CC (PubMed:18653460). {ECO:0000269|PubMed:18653460}.
CC -!- FUNCTION: [Protein 2B]: Affects membrane integrity and causes an
CC increase in membrane permeability. {ECO:0000250}.
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 3A]: Serves as membrane anchor via its hydrophobic
CC domain. Plays an essential role in viral RNA replication by recruiting
CC PI4KB at the viral replication sites, thereby allowing the formation of
CC the rearranged membranous structures where viral replication takes
CC place (PubMed:22124328, PubMed:24672044, PubMed:27989622,
CC PubMed:30755512, PubMed:22258260). Stimulates the enzymatic activity of
CC PI4KB, this activation is sensitized by ACBD3 (PubMed:24672044,
CC PubMed:27989622). {ECO:0000269|PubMed:22124328,
CC ECO:0000269|PubMed:22258260, ECO:0000269|PubMed:24672044,
CC ECO:0000269|PubMed:27989622, ECO:0000269|PubMed:30755512}.
CC -!- FUNCTION: [VPg]: Forms a primer, VPg-pU, which is utilized by the
CC polymerase for the initiation of RNA chains.
CC {ECO:0000250|UniProtKB:P03304}.
CC -!- FUNCTION: [Protease 3C]: Cysteine protease that generates mature viral
CC proteins from the precursor polyprotein (By similarity). In addition to
CC its proteolytic activity, it binds to viral RNA, and thus influences
CC viral genome replication. RNA and substrate cooperatively bind to the
CC protease (By similarity). {ECO:0000250|UniProtKB:P03304,
CC ECO:0000250|UniProtKB:P12296}.
CC -!- FUNCTION: [RNA-directed RNA polymerase]: Replicates the genomic and
CC antigenomic RNAs by recognizing replications specific signals (By
CC similarity). Performs VPg uridylylation (By similarity).
CC {ECO:0000250|UniProtKB:P12296}.
CC -!- CATALYTIC ACTIVITY:
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 -!- CATALYTIC ACTIVITY:
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:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000250|UniProtKB:P03300};
CC -!- SUBUNIT: [Capsid protein VP0]: Interacts with capsid protein VP1
CC (PubMed:27681122, PubMed:27595320). Interacts with capsid protein VP3
CC (PubMed:27681122, PubMed:27595320). {ECO:0000269|PubMed:27595320,
CC ECO:0000269|PubMed:27681122}.
CC -!- SUBUNIT: [Capsid protein VP1]: Interacts with capsid protein VP0
CC (PubMed:27681122, PubMed:27595320). Interacts with capsid protein VP3
CC (PubMed:27681122, PubMed:27595320). {ECO:0000269|PubMed:27595320,
CC ECO:0000269|PubMed:27681122}.
CC -!- SUBUNIT: [Capsid protein VP3]: Interacts with capsid protein VP0
CC (PubMed:27681122, PubMed:27595320). Interacts with capsid protein VP1
CC (PubMed:27681122, PubMed:27595320). {ECO:0000269|PubMed:27595320,
CC ECO:0000269|PubMed:27681122}.
CC -!- SUBUNIT: [Protein 2A]: Homodimer (PubMed:19879907). Interacts with
CC protein 2B (PubMed:19879907). Interacts with protein 2C
CC (PubMed:19879907). {ECO:0000269|PubMed:19879907}.
CC -!- SUBUNIT: [Protein 2B]: Homodimer (PubMed:19879907). Interacts with host
CC ABCD3 (PubMed:22124328). Interacts with protein 2A (PubMed:19879907).
CC Interacts with host ACBD3 (PubMed:22124328).
CC {ECO:0000269|PubMed:19879907, ECO:0000269|PubMed:22124328}.
CC -!- SUBUNIT: [Protein 2C]: Homodimer (PubMed:19879907). Interacts with host
CC ABCD3 (PubMed:22124328). Interacts with protein 2A (PubMed:19879907).
CC Interacts with protein 3A (PubMed:22124328). Interacts with protein 3C
CC (PubMed:19879907). Interacts with host ACBD3 (PubMed:22124328).
CC {ECO:0000269|PubMed:19879907, ECO:0000269|PubMed:22124328}.
CC -!- SUBUNIT: [Protein 3A]: Homodimer (PubMed:19879907). Interacts with host
CC ABCD3 (via GOLD domain) and PI4KB; these interactions allow the
CC formation of a viral protein/ACBD3/PI4KB complex in order to synthesize
CC PI4P at the viral RNA replication sites (PubMed:22124328,
CC PubMed:22258260, PubMed:24672044, PubMed:27989622, PubMed:30755512,
CC PubMed:28065508) (Probable). Interacts with protein 2C
CC (PubMed:19879907). Interacts with protein 3C (PubMed:19879907). Protein
CC 3C: Interacts with protein 2A (PubMed:19879907). Protein 3C: Interacts
CC with protein 2C (PubMed:19879907). {ECO:0000269|PubMed:19879907,
CC ECO:0000269|PubMed:22124328, ECO:0000269|PubMed:28065508,
CC ECO:0000305|PubMed:23572552, ECO:0000305|PubMed:28065508}.
CC -!- INTERACTION:
CC O91464; Q9H3P7: ACBD3; Xeno; NbExp=13; IntAct=EBI-7587528, EBI-1791792;
CC PRO_0000448012; Q9H3P7: ACBD3; Xeno; NbExp=4; IntAct=EBI-22117245, EBI-1791792;
CC PRO_0000448014; Q9H3P7: ACBD3; Xeno; NbExp=5; IntAct=EBI-22117252, EBI-1791792;
CC PRO_0000448015; Q9H3P7: ACBD3; Xeno; NbExp=5; IntAct=EBI-22116975, EBI-1791792;
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion
CC {ECO:0000269|PubMed:27595320, ECO:0000269|PubMed:27681122}. Host
CC cytoplasm {ECO:0000250|UniProtKB:P12296}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion
CC {ECO:0000269|PubMed:27595320, ECO:0000269|PubMed:27681122}. Host
CC cytoplasm {ECO:0000250|UniProtKB:P12296}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion
CC {ECO:0000269|PubMed:27595320, ECO:0000269|PubMed:27681122}. Host
CC cytoplasm {ECO:0000250|UniProtKB:P12296}.
CC -!- SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:22124328, ECO:0000269|PubMed:24672044}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:P03304}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P03304}. Note=Probably localizes to the surface
CC of intracellular membrane vesicles that are induced after virus
CC infection as the site for viral RNA replication. These vesicles are
CC probably autophagosome-like vesicles. {ECO:0000250|UniProtKB:P03304}.
CC -!- SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:22124328, ECO:0000269|PubMed:24672044}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:P03304}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P03304}. Note=Probably localizes to the surface
CC of intracellular membrane vesicles that are induced after virus
CC infection as the site for viral RNA replication. These vesicles are
CC probably autophagosome-like vesicles. {ECO:0000250|UniProtKB:P03304}.
CC -!- SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:22124328, ECO:0000269|PubMed:24672044}; Single-pass
CC membrane protein {ECO:0000255}. Host Golgi apparatus membrane
CC {ECO:0000269|PubMed:30755512}; Single-pass membrane protein
CC {ECO:0000255}. Note=Probably localizes to intracellular membrane
CC vesicles that are induced after virus infection as the site for viral
CC RNA replication. {ECO:0000250|UniProtKB:P03304}.
CC -!- SUBCELLULAR LOCATION: [VPg]: Virion {ECO:0000250|UniProtKB:P03304}.
CC -!- SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm
CC {ECO:0000250|UniProtKB:P03304}.
CC -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasmic
CC vesicle membrane {ECO:0000250|UniProtKB:P03304}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:P03304}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P03304}. Note=Probably localizes to the surface
CC of intracellular membrane vesicles that are induced after virus
CC infection as the site for viral RNA replication. These vesicles are
CC probably autophagosome-like vesicles. {ECO:0000250|UniProtKB:P03304}.
CC -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages by the viral
CC protease in vivo yield a variety of precursors and mature proteins
CC (PubMed:22226945). The leader protein-VP0 junction is cleaved by 3C
CC proteinase (PubMed:14512530). The VP1/2A junction is cleaved by the
CC protein 3CD in association with protein 2A (PubMed:22226945).
CC {ECO:0000269|PubMed:14512530, ECO:0000269|PubMed:22226945}.
CC -!- PTM: [VPg]: Uridylylated by the polymerase and is covalently linked to
CC the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-
CC peptide primer for the polymerase. {ECO:0000250|UniProtKB:P12296}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31356.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB010145; BAA31356.1; ALT_FRAME; Genomic_RNA.
DR EMBL; AB040749; BAB62889.1; -; Genomic_RNA.
DR PDB; 5AOO; X-ray; 2.10 A; A=764-1016, B=171-540, C=541-763.
DR PDB; 5GKA; EM; 3.70 A; A=764-1016, B=174-540, C=541-762.
DR PDB; 5LVC; EM; 4.20 A; a=764-1016, b=171-540, c=541-763.
DR PDB; 5LZ3; X-ray; 3.00 A; B=1653-1710.
DR PDBsum; 5AOO; -.
DR PDBsum; 5GKA; -.
DR PDBsum; 5LVC; -.
DR PDBsum; 5LZ3; -.
DR SMR; O91464; -.
DR IntAct; O91464; 1.
DR MINT; O91464; -.
DR iPTMnet; O91464; -.
DR SABIO-RK; O91464; -.
DR Proteomes; UP000119554; Genome.
DR Proteomes; UP000137558; Genome.
DR GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0039618; C:T=pseudo3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0019028; C:viral capsid; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0039690; P:positive stranded viral RNA replication; IDA: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; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
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; -; 4.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR007053; LRAT_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
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; PF00548; Peptidase_C3; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00073; Rhv; 3.
DR Pfam; PF00910; RNA_helicase; 1.
DR PRINTS; PR00918; CALICVIRUSNS.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51934; LRAT; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Capsid protein; Covalent protein-RNA linkage;
KW 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 Golgi apparatus; Host membrane; Host mRNA suppression by virus;
KW Host-virus interaction; Hydrolase;
KW Inhibition of host mRNA nuclear export by virus; Ion channel;
KW Ion transport; Lipoprotein; Membrane; Myristate; Nucleotide-binding;
KW Nucleotidyltransferase; Phosphoprotein; Protease; Reference proteome;
KW RNA-binding; RNA-directed RNA polymerase;
KW T=pseudo3 icosahedral capsid protein; Thiol protease; Transferase;
KW Transmembrane; Transmembrane helix; Transport;
KW Viral attachment to host cell; Viral ion channel; Viral RNA replication;
KW Virion; Virus entry into host cell.
FT CHAIN 1..2432
FT /note="Genome polyprotein"
FT /id="PRO_0000448006"
FT CHAIN 1..170
FT /note="Leader protein"
FT /id="PRO_0000448007"
FT CHAIN 171..540
FT /note="Capsid protein VP0"
FT /id="PRO_0000448008"
FT CHAIN 541..763
FT /note="Capsid protein VP3"
FT /id="PRO_0000448009"
FT CHAIN 764..1016
FT /note="Capsid protein VP1"
FT /id="PRO_0000448010"
FT CHAIN 1017..1152
FT /note="Protein 2A"
FT /id="PRO_0000448011"
FT CHAIN 1153..1317
FT /note="Protein 2B"
FT /id="PRO_0000448012"
FT CHAIN 1175..2431
FT /note="Protein 3CD"
FT /id="PRO_0000448013"
FT CHAIN 1318..1652
FT /note="Protein 2C"
FT /id="PRO_0000448014"
FT CHAIN 1653..1747
FT /note="Protein 3A"
FT /id="PRO_0000448015"
FT CHAIN 1748..1774
FT /note="VPg"
FT /id="PRO_0000448016"
FT CHAIN 1775..1964
FT /note="Protease 3C"
FT /id="PRO_0000448017"
FT CHAIN 1965..2431
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000448018"
FT TRANSMEM 1712..1732
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1033..1121
FT /note="LRAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT DOMAIN 1422..1586
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1773..1954
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 2193..2308
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 201..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1746..1766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..336
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1816
FT /note="For protease 3C activity"
FT /evidence="ECO:0000250|UniProtKB:P03304,
FT ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1844
FT /note="For protease 3C activity"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT ACT_SITE 1917
FT /note="For protease 3C activity"
FT /evidence="ECO:0000250|UniProtKB:P03304,
FT ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 2199
FT /note="For RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P12296"
FT ACT_SITE 2294
FT /note="For RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P12296"
FT BINDING 1448..1455
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 170..171
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000269|PubMed:14512530"
FT SITE 540..541
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 763..764
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1016..1017
FT /note="Cleavage; by protein 3CD"
FT /evidence="ECO:0000269|PubMed:22226945"
FT SITE 1152..1153
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1317..1318
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1652..1653
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1747..1748
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1774..1775
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1964..1965
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000269|PubMed:22226945"
FT MOD_RES 109
FT /note="Phosphotyrosine; by host SYK"
FT /evidence="ECO:0000250|UniProtKB:Q66765"
FT MOD_RES 115
FT /note="Phosphoserine; by host CK2"
FT /evidence="ECO:0000250|UniProtKB:Q66765"
FT MOD_RES 1750
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT LIPID 171
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT LIPID 1653
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000269|PubMed:22258260"
FT MUTAGEN 168
FT /note="Q->P: Complete loss of proteolytic cleavage between
FT the leader protein and VP1 protein."
FT /evidence="ECO:0000269|PubMed:14512530"
FT MUTAGEN 1043..1046
FT /note="HWAI->AWAA: Complete loss of interaction between the
FT 3C-3D precursor and protein 2A."
FT /evidence="ECO:0000269|PubMed:22226945"
FT MUTAGEN 1105..1106
FT /note="NC->AA: No effect on the interaction between the 3C-
FT 3D precursor and protein 2A."
FT /evidence="ECO:0000269|PubMed:22226945"
FT MUTAGEN 1653
FT /note="G->A: Complete loss of myristoylation."
FT /evidence="ECO:0000269|PubMed:22258260"
FT MUTAGEN 1654
FT /note="N->A: Complete loss of myristoylation."
FT /evidence="ECO:0000269|PubMed:22258260"
FT MUTAGEN 1655
FT /note="R->A: Complete loss of myristoylation; loss of
FT interaction with host ACBD3. Loss of activation of host
FT PI4KB in vitro."
FT /evidence="ECO:0000269|PubMed:22258260,
FT ECO:0000269|PubMed:24672044"
FT MUTAGEN 1657
FT /note="I->A: Loss of interaction with host ACBD3 and
FT PI4KB."
FT /evidence="ECO:0000269|PubMed:22258260"
FT MUTAGEN 1663
FT /note="E->A: Loss of activation of host PI4KB in vitro."
FT /evidence="ECO:0000269|PubMed:24672044"
FT MUTAGEN 1963..1964
FT /note="QQ->AA: Complete loss of cleavage at the 3C-3D
FT junction."
FT /evidence="ECO:0000269|PubMed:22226945"
FT CONFLICT 71
FT /note="R -> C (in Ref. 1; BAA31356)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="T -> N (in Ref. 1; BAA31356)"
FT /evidence="ECO:0000305"
FT CONFLICT 839
FT /note="N -> D (in Ref. 1; BAA31356)"
FT /evidence="ECO:0000305"
FT CONFLICT 1172
FT /note="E -> G (in Ref. 1; BAA31356)"
FT /evidence="ECO:0000305"
FT CONFLICT 1351
FT /note="R -> P (in Ref. 1; BAA31356)"
FT /evidence="ECO:0000305"
FT CONFLICT 1420
FT /note="I -> V (in Ref. 1; BAA31356)"
FT /evidence="ECO:0000305"
FT CONFLICT 2031
FT /note="E -> G (in Ref. 1; BAA31356)"
FT /evidence="ECO:0000305"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:5AOO"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:5AOO"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 345..353
FT /evidence="ECO:0007829|PDB:5AOO"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:5AOO"
FT HELIX 399..404
FT /evidence="ECO:0007829|PDB:5AOO"
FT HELIX 409..414
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 417..429
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 437..447
FT /evidence="ECO:0007829|PDB:5AOO"
FT HELIX 450..457
FT /evidence="ECO:0007829|PDB:5AOO"
FT HELIX 459..463
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 464..470
FT /evidence="ECO:0007829|PDB:5AOO"
FT TURN 471..473
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 475..481
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 486..491
FT /evidence="ECO:0007829|PDB:5AOO"
FT TURN 492..494
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 497..509
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 516..534
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 562..564
FT /evidence="ECO:0007829|PDB:5AOO"
FT HELIX 585..589
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 593..600
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 608..615
FT /evidence="ECO:0007829|PDB:5AOO"
FT TURN 616..620
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 621..624
FT /evidence="ECO:0007829|PDB:5AOO"
FT HELIX 625..632
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 633..638
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 640..646
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 653..662
FT /evidence="ECO:0007829|PDB:5AOO"
FT HELIX 671..674
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 677..694
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 699..704
FT /evidence="ECO:0007829|PDB:5AOO"
FT TURN 713..715
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 718..729
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 736..746
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 751..755
FT /evidence="ECO:0007829|PDB:5AOO"
FT HELIX 778..780
FT /evidence="ECO:0007829|PDB:5AOO"
FT HELIX 806..809
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 814..816
FT /evidence="ECO:0007829|PDB:5AOO"
FT TURN 819..822
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 826..829
FT /evidence="ECO:0007829|PDB:5AOO"
FT TURN 830..832
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 834..837
FT /evidence="ECO:0007829|PDB:5AOO"
FT HELIX 840..843
FT /evidence="ECO:0007829|PDB:5AOO"
FT HELIX 852..856
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 859..873
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 876..878
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 880..887
FT /evidence="ECO:0007829|PDB:5AOO"
FT HELIX 899..902
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 905..912
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 916..924
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 929..935
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 939..942
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 947..949
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 954..956
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 958..964
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 974..991
FT /evidence="ECO:0007829|PDB:5AOO"
FT STRAND 1655..1658
FT /evidence="ECO:0007829|PDB:5LZ3"
FT HELIX 1670..1678
FT /evidence="ECO:0007829|PDB:5LZ3"
SQ SEQUENCE 2432 AA; 265458 MW; E451BABAD3CD1460 CRC64;
MAATRVSRSV LAAVAHSAAH RTYHTVLDCY DRLYLNTNPH LSYPLPKNSS FPCPFCQYDE
QNEVLSPESL RGEGAEPCWK CSQDKPRRKY NTTPPEDWLY DSDVQSWFYP ETYYSDLQQK
FFDKLALLSL PGAYQAKTPE ERALAGALTQ LLNFPSTPPL TLPTTNLQRQ GNSVTNIYGN
GNNVTTDVGA NGWAPTVSTG LGDGPVSASA DSLPGRSGGA SSEKTHTVSG SSNKVGSRFS
KWWEPAAARA SESATDSAIE GIDAAGKAAS KAITRKLDRP AAPSSTANPQ PSLIALNPSA
TQSGNASILT GSTAPSLLAY PTATPVPLPN PDEPSQPGPS GDRTWLLDTV TWSQEFTRGW
NIAGSNGMQW TGLESLIFPV STDTNWTSTS SPTAYPLPFS FVRAYPDSSW AAMYNTHSMW
NCGWRVQVTV NGSQFHAGAL ILYMVPEATT HAIQTARDNA GFVFPYVILN LYESNTATIE
VPYISPTPNT SSGLHAPWTF YLQVLSPLNP PPSLPTSLSC SIYVTPVDSS FHGLRYLAPQ
HWKTRAVPGA GTFGSAVAGQ ELPLCGVRAY YPPNAYIPAQ VRDWLEFAHR PGLMATVPWT
MADEPAERLG IFPVSPSAIA GTGAPISYVI SLFSQWRGEL AAHLLFTGSA QHYGRLVVCY
TPAAPQPPST MQEAMRGTYT VWDVNAASTL EFTIPFISNS YWKTVDVNNP DALLSTTGYV
SIWVQNPLVG PHTAPASALV QAFISAGESF NVRLMQNPAL TSQTLTEDLD APQDTGNIEN
GAADNSPQPR TTFDYTGNPL PPDTKLENFF SFYRLLPMGG SGAPSLSFPA DEGTIIPLNP
INWLKGADVS GIAAMLSCFT YIAADLRITL RFSNPNDNPA TMLVAFAPPG ATIPLKPTRQ
MLSNFYMAEV PVSAATSTMV SFSIPYTSPL SAIPTSYFGW EDWSGTNFGQ LSSGSWGNLM
LIPSLSVDSA IPFDFQLSCW VAFGNFKAWV PRPPPPLPPL PTPAANAERT VAVIKQGAAS
ATPDVDPDDR VYIVRAQRPT YVHWAIRKVA PDGSAKQISL SRSGIQALVA LEPPEGEPYL
EILPSHWTLA ELQLGNKWEY SATNNCTHFV SSITGESLPN TGFSLALGIG ALTAIAASAA
VAVKALPGIR RQGLLTLSAD TETNQTLNKI TESVNQAAQV VSQFDLSGPA NSVSLAASDI
REAAHKVASS LNGFTDVIAD IKDSLFTRVS DAVESGVATF LTWLVKLFGY LLVLFGSPTP
MSISGLLVII CADLAPHARE FFTASGNVLS SLYYWIASKL GLSVTPQECE RATLEPQGLK
DFNDGALAMR NVEWIGETAW KWAHRLLDWI RGKAKTDPQA KLADVHDEIM LHYSDSILAL
GSEKLPIDHI TKSISRCREL VSIAQEAKSG PHSSFLNQAI KNYTLAISQH RKCQTGPRPE
PVVVYLYGPP GTGKSLLASL LAQTLSQRLA GTPDDVYSPS SASCEYFDGY TGQTVHFIDD
IGQDPEGRDW ANFPNLVSSA PFIVPMASLE EKGTHYTSKV IVVTSNFHEP NERAARSMGA
LRRRVHLRIN VTSNGVPFDP TNALNPIPGT QSKYFTAQTP LTLFQSNTVR LDRDSIWTPT
FTNMDELVDA IVTRLDRSTG VSNSLASLIR RQGNRVIDAE PREIPLEYAD DLLEAMAHHR
PVPCSLGLSQ AIANNTPIQQ ISETFWKYRK PIFTCTTFLA VLGFLCSVIP LARSLWKSKQ
DTPQEPQAAY SAISHQKPKP KSQKPVPTRH IQRQGISPAV PGISNNVVHV ESGNGLNKNV
MSGFYIFSRF LLVPTHLREP HHTTLTVGAD TYDWATLQTQ EFGEITIVHT PTSRQYKDMR
RFIGAHPHPT GLLVSQFKAA PLYVRISDNR ILDLDFPGVV VCKQAYGYRA ATFEGLCGSP
LVTDDPSGVK ILGLHVAGVA GTSGFSAPIH PILGQITQFA TTQQSLIVPT AEVRPGVNVN
RMSRLHPSPA YGAFPVKKQP APLKRNDKRL QEGVDLDTQL FLKHGKGDVT EPWPGLEAAA
DLYFSTFPTS LPVLTQEQAI HGTPNMEGLD MGQAAGYPWN TLGRSRRSLF DEVEPGVFVP
KPELQAEINQ TLEDPDYVYS TFLKDELRPT AKVEQGLTRI VEAAPIHAIV AGRMLLGGLI
DYMQGRPGEH GSAVGCNPDV HWTSFFYAFS EFSQVYDLDY KCFDATLPSA VFTLVADHLT
RITGDPRVGR YIHSIRHSHH IYGNRMYDMI GGNPSGCVAT SILNTIINNI CVLSALIQHP
DFSPSRFHIL AYGDDVIYAT EPPIHPSFLR EFYQKHTPLV VTPANKGQDF PPTSTIYEVT
FLKRWFVPDD VRPIYIHPVM DPDTYEQSVM WLRDGDFQDV VTSLCHLAFH SGPKTYAAWC
MKVREQCLKS GFAPNFLPYS YLQLRWLNLL AA
