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VP7_BTV10
ID   VP7_BTV10               Reviewed;         349 AA.
AC   P69361; P07886;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   02-JUN-2021, entry version 76.
DE   RecName: Full=Core protein VP7;
GN   Name=Segment-7;
OS   Bluetongue virus 10 (isolate USA) (BTV 10).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Orbivirus.
OX   NCBI_TaxID=10900;
OH   NCBI_TaxID=9891; Antilocapra americana (Pronghorn).
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
OH   NCBI_TaxID=9925; Capra hircus (Goat).
OH   NCBI_TaxID=46212; Culicoides variipennis (Biting midge).
OH   NCBI_TaxID=9940; Ovis aries (Sheep).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2831505; DOI=10.1093/nar/16.4.1620;
RA   Yu Y., Fukusho A., Ritter D.G., Roy P.;
RT   "Complete nucleotide sequence of the group-reactive antigen VP7 gene of
RT   bluetongue virus.";
RL   Nucleic Acids Res. 16:1620-1620(1988).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX   PubMed=7816101; DOI=10.1038/373167a0;
RA   Grimes J., Basak A.K., Roy P., Stuart D.;
RT   "The crystal structure of bluetongue virus VP7.";
RL   Nature 373:167-170(1995).
CC   -!- FUNCTION: The VP7 protein is one of the five proteins (with VP1, VP3,
CC       VP4, and VP6) which form the inner capsid of the virus.
CC   -!- SUBUNIT: Homotrimer that assemble in a complex of 260 capsomers on an
CC       inner scaffold composed of VP3.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the orbivirus VP7 family. {ECO:0000305}.
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DR   EMBL; X06463; CAA29771.1; -; Genomic_RNA.
DR   PIR; A28537; P7XR10.
DR   RefSeq; YP_052967.1; NC_006022.1.
DR   PDB; 1BVP; X-ray; 2.60 A; 1/2/3/4/5/6=1-349.
DR   PDBsum; 1BVP; -.
DR   SMR; P69361; -.
DR   GeneID; 2943155; -.
DR   KEGG; vg:2943155; -.
DR   EvolutionaryTrace; P69361; -.
DR   Proteomes; UP000007662; Genome.
DR   GO; GO:0019031; C:viral envelope; IEA:InterPro.
DR   GO; GO:0039624; C:viral outer capsid; IEA:UniProtKB-KW.
DR   GO; GO:0046789; F:host cell surface receptor binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:InterPro.
DR   Gene3D; 1.10.170.10; -; 1.
DR   Gene3D; 1.10.250.10; -; 1.
DR   InterPro; IPR008980; Capsid_hemagglutn.
DR   InterPro; IPR001803; Orbi_VP7_capsid.
DR   InterPro; IPR023178; Orbi_VP7_capsid_C.
DR   InterPro; IPR023176; Orbi_VP7_capsid_N.
DR   InterPro; IPR008935; Virus_capsid_a-hlx_vir.
DR   Pfam; PF00897; Orbi_VP7; 1.
DR   PRINTS; PR00903; VP7CAPSID.
DR   SUPFAM; SSF48345; SSF48345; 1.
DR   SUPFAM; SSF49818; SSF49818; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Glycoprotein; Outer capsid protein;
KW   Reference proteome; Virion.
FT   CHAIN           1..349
FT                   /note="Core protein VP7"
FT                   /id="PRO_0000222732"
FT   CARBOHYD        287
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   HELIX           2..15
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   STRAND          20..22
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   HELIX           27..44
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   HELIX           55..73
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   HELIX           90..94
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   HELIX           103..116
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   TURN            128..131
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   STRAND          133..136
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   STRAND          148..155
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   STRAND          158..163
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   STRAND          168..170
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   HELIX           172..174
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   TURN            175..177
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   STRAND          182..195
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   STRAND          201..203
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   STRAND          209..212
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   STRAND          215..217
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   STRAND          223..225
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   STRAND          227..229
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   STRAND          231..234
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   STRAND          237..239
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   STRAND          241..254
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   HELIX           263..271
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   HELIX           276..286
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   STRAND          289..291
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   STRAND          293..295
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   HELIX           304..323
FT                   /evidence="ECO:0007829|PDB:1BVP"
FT   HELIX           341..346
FT                   /evidence="ECO:0007829|PDB:1BVP"
SQ   SEQUENCE   349 AA;  38548 MW;  F08EDD6DD2CE86D9 CRC64;
     MDTIAARALT VMRACATLQE ARIVLEANVM EILGIAINRY NGLTLRGVTM RPTSLAQRNE
     MFFMCLDMML SAAGINVGPI SPDYTQHMAT IGVLATPEIP FTTEAANEIA RVTGETSTWG
     PARQPYGFFL ETEETFQPGR WFMRAAQAVT AVVCGPDMIQ VSLNAGARGD VQQIFQGRND
     PMMIYLVWRR IENFAMAQGN SQQTQAGVTV SVGGVDMRAG RIIAWDGQAA LHVHNPTQQN
     AMVQIQVVFY ISMDKTLNQY PALTAEIFNV YSFRDHTWHG LRTAILNRTT LPNMLPPIFP
     PNDRDSILTL LLLSTLADVY TVLRPEFAIH GVNPMPGPLT RAIARAAYV
 
 
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