P8_RDVO
ID P8_RDVO Reviewed; 420 AA.
AC P17379;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 02-JUN-2021, entry version 90.
DE RecName: Full=Outer capsid protein P8;
DE AltName: Full=Structural protein P8;
DE Contains:
DE RecName: Full=Outer capsid protein P8';
DE Contains:
DE RecName: Full=Small peptide 1;
DE Short=Sp1;
OS Rice dwarf virus (isolate O) (RDV).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Phytoreovirus.
OX NCBI_TaxID=142805;
OH NCBI_TaxID=114194; Alopecurus aequalis.
OH NCBI_TaxID=90397; Echinochloa crus-galli (Barnyard grass) (Panicum crus-galli).
OH NCBI_TaxID=94400; Nephotettix cincticeps (Green rice leafhopper) (Selenocephalus cincticeps).
OH NCBI_TaxID=4530; Oryza sativa (Rice).
OH NCBI_TaxID=147271; Paspalum.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2794978; DOI=10.1099/0022-1317-70-10-2759;
RA Omura T., Ishikawa K., Hirano H., Ugaki M., Minobe Y., Tsuchizaki T.,
RA Kato H.;
RT "The outer capsid protein of rice dwarf virus is encoded by genome segment
RT S8.";
RL J. Gen. Virol. 70:2759-2764(1989).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
RX PubMed=14527391; DOI=10.1016/j.str.2003.08.012;
RA Nakagawa A., Miyazaki N., Taka J., Naitow H., Ogawa A., Fujimoto Z.,
RA Mizuno H., Higashi T., Watanabe Y., Omura T., Cheng R.H., Tsukihara T.;
RT "The atomic structure of rice dwarf virus reveals the self-assembly
RT mechanism of component proteins.";
RL Structure 11:1227-1238(2003).
CC -!- FUNCTION: Capsid protein which self-assembles to form the outer
CC icosahedral capsid with a T=13 symmetry, about 70 nm in diameter and
CC consisting of 780 molecules capsid proteins.
CC -!- SUBUNIT: Homotrimer. Homomultimer. Interacts with host peroxisomal
CC glycolate oxidase (GOX). This interaction mediates its relocation to
CC virus factories peripheral to host peroxisomes (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Outer capsid protein P8]: Virion {ECO:0000305}.
CC Host cytoplasm {ECO:0000250}. Note=Found in the peripheral regions of
CC spherical cytoplasmic structures, called virus factories, that appear
CC early after infection and are the site of viral replication and
CC packaging. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phytoreovirus outer capsid protein P8
CC family. {ECO:0000305}.
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DR EMBL; D00536; BAA00424.1; -; Genomic_RNA.
DR PIR; JQ0105; MWXRRD.
DR PDB; 1UF2; X-ray; 3.50 A; C/D/E/F/G/H/I/J/P/Q/R/S/T=1-420.
DR PDBsum; 1UF2; -.
DR SMR; P17379; -.
DR EvolutionaryTrace; P17379; -.
DR GO; GO:0030430; C:host cell cytoplasm; ISS:UniProtKB.
DR GO; GO:0044161; C:host cell cytoplasmic vesicle; ISS:UniProtKB.
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 GO; GO:0019048; P:modulation by virus of host process; ISS:UniProtKB.
DR InterPro; IPR008980; Capsid_hemagglutn.
DR InterPro; IPR009807; Phytoreo_P8.
DR InterPro; IPR008935; Virus_capsid_a-hlx_vir.
DR Pfam; PF07124; Phytoreo_P8; 1.
DR SUPFAM; SSF48345; SSF48345; 1.
DR SUPFAM; SSF49818; SSF49818; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Host cytoplasm; Host-virus interaction;
KW Outer capsid protein; Virion.
FT CHAIN 1..420
FT /note="Outer capsid protein P8"
FT /id="PRO_0000040674"
FT CHAIN 1..361
FT /note="Outer capsid protein P8'"
FT /id="PRO_0000040675"
FT CHAIN 362..420
FT /note="Small peptide 1"
FT /id="PRO_0000040676"
FT HELIX 3..22
FT /evidence="ECO:0007829|PDB:1UF2"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:1UF2"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:1UF2"
FT HELIX 58..73
FT /evidence="ECO:0007829|PDB:1UF2"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:1UF2"
FT HELIX 78..82
FT /evidence="ECO:0007829|PDB:1UF2"
FT HELIX 84..88
FT /evidence="ECO:0007829|PDB:1UF2"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:1UF2"
FT HELIX 112..121
FT /evidence="ECO:0007829|PDB:1UF2"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1UF2"
FT HELIX 132..141
FT /evidence="ECO:0007829|PDB:1UF2"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:1UF2"
FT HELIX 169..173
FT /evidence="ECO:0007829|PDB:1UF2"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:1UF2"
FT STRAND 188..195
FT /evidence="ECO:0007829|PDB:1UF2"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:1UF2"
FT TURN 212..216
FT /evidence="ECO:0007829|PDB:1UF2"
FT STRAND 217..226
FT /evidence="ECO:0007829|PDB:1UF2"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:1UF2"
FT STRAND 256..265
FT /evidence="ECO:0007829|PDB:1UF2"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:1UF2"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:1UF2"
FT STRAND 285..298
FT /evidence="ECO:0007829|PDB:1UF2"
FT HELIX 304..307
FT /evidence="ECO:0007829|PDB:1UF2"
FT TURN 308..311
FT /evidence="ECO:0007829|PDB:1UF2"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:1UF2"
FT HELIX 324..336
FT /evidence="ECO:0007829|PDB:1UF2"
FT HELIX 340..358
FT /evidence="ECO:0007829|PDB:1UF2"
FT TURN 361..363
FT /evidence="ECO:0007829|PDB:1UF2"
FT HELIX 378..385
FT /evidence="ECO:0007829|PDB:1UF2"
FT HELIX 393..413
FT /evidence="ECO:0007829|PDB:1UF2"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:1UF2"
SQ SEQUENCE 420 AA; 46425 MW; 401CCFDE5145DB2C CRC64;
MSRQMWLDTS ALLEAISEYV VRCNGDTFSG LTTGDFNALS NMFTQLSVSS AGYVSDPRVP
LQTMSNMFVS FITSTDRCGY MLRKTWFNSD TKPTVSDDFI TTYIRPRLQV PMSDTVRQLN
NLSLQPSAKP KLYERQNAIM KGLDIPYSEP IEPCKLFRSV AGQTGNIPMM GILATPPAQQ
QPFFVAERRR ILFGIRSNAA IPAGAYQFVV PAWASVLSVT GAYVYFTNSF FGTIIAGVTA
TATAADAATT FTVPTDANNL PVQTDSRLSF SLGGGNINLE LGVAKTGFCV AIEGEFTILA
NRSQAYYTLN SITQTPTSID DFDVSDFLTT FLSQLRACGQ YEIFSDAMDQ LTNSLITNYM
DPPAIPAGLA FTSPWFRFSE RARTILALQN VDLNIRKLIV RHLWVITSLI AVFGRYYRPN