PHOSP_VSIVS
ID PHOSP_VSIVS Reviewed; 265 AA.
AC Q8B0H8;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 29-SEP-2021, entry version 62.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
DE AltName: Full=NS;
DE AltName: Full=Protein M1;
GN Name=P;
OS Vesicular stomatitis Indiana virus (strain 85CLB South America) (VSIV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Vesiculovirus.
OX NCBI_TaxID=434490;
OH NCBI_TaxID=7158; Aedes.
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=58271; Culicoides.
OH NCBI_TaxID=9793; Equus asinus (Donkey) (Equus africanus asinus).
OH NCBI_TaxID=9796; Equus caballus (Horse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=252607; Lutzomyia.
OH NCBI_TaxID=7370; Musca domestica (House fly).
OH NCBI_TaxID=7190; Simuliidae (black flies).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12237430; DOI=10.1099/0022-1317-83-10-2475;
RA Rodriguez L.L., Pauszek S.J., Bunch T.A., Schumann K.R.;
RT "Full-length genome analysis of natural isolates of vesicular stomatitis
RT virus (Indiana 1 serotype) from North, Central and South America.";
RL J. Gen. Virol. 83:2475-2483(2002).
CC -!- FUNCTION: Essential component of the RNA polymerase transcription and
CC replication complex. Binds the viral ribonucleocapsid and positions the
CC L polymerase on the template. May act as a chaperone for newly
CC synthesized free N protein, so-called N(0). Plays a role in virion
CC assembly (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer when phosphorylated in domain I. This trimer is
CC stabilized by binding to the L protein. Binds N(0), and N in
CC ribonucleocapsid (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm {ECO:0000250}.
CC -!- DOMAIN: Sequences comparison studies have defined several domains.
CC Domain I binds the protein L, contains phosphorylation sites required
CC for trimerization and is involved in transcription. Hinge region is
CC highly variable and may act as a spacer between domain I and II. Domain
CC II is also phosphorylated, binds protein L, and plays a role in
CC replication. Domain III is basic and essential for binding the N-RNA
CC template (By similarity). {ECO:0000250}.
CC -!- PTM: Domain I is phosphorylated by host CK2. Domain II is
CC phosphorylated by other unknown kinases. Phosphorylation play an
CC important role in facilitating trimerization and possibly P-L complex
CC formation (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the vesiculovirus protein P family.
CC {ECO:0000305}.
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DR EMBL; AF473865; AAN16986.1; -; Genomic_RNA.
DR SMR; Q8B0H8; -.
DR Proteomes; UP000007625; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR Gene3D; 1.10.8.440; -; 1.
DR InterPro; IPR043036; Phosphoprotein_C_viral.
DR InterPro; IPR037263; Phosphoprotein_central.
DR SUPFAM; SSF160892; SSF160892; 1.
PE 3: Inferred from homology;
KW Chaperone; Host cytoplasm; Phosphoprotein; Viral RNA replication; Virion.
FT CHAIN 1..265
FT /note="Phosphoprotein"
FT /id="PRO_0000287352"
FT REGION 1..137
FT /note="Domain I"
FT /evidence="ECO:0000250"
FT REGION 42..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..210
FT /note="Hinge"
FT /evidence="ECO:0000250"
FT REGION 211..244
FT /note="Domain II"
FT /evidence="ECO:0000250"
FT REGION 245..265
FT /note="Domain III:"
FT /evidence="ECO:0000250"
FT MOD_RES 60
FT /note="Phosphoserine; by host CK2"
FT /evidence="ECO:0000250"
FT MOD_RES 62
FT /note="Phosphothreonine; by host CK2"
FT /evidence="ECO:0000250"
FT MOD_RES 64
FT /note="Phosphoserine; by host CK2"
FT /evidence="ECO:0000250"
FT MOD_RES 226
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 227
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
SQ SEQUENCE 265 AA; 29997 MW; CBD35DC6DF82EBAD CRC64;
MDNLTKVREY LKSYSRLDQA VGEIDEIEAQ RDEKSNYELF QEDGVEEHAK PSYFQAADDS
DTESEPEVED NQSLYVPDQE AEQVEGFIQG PLDDYADEEV DVVFTSDWKQ PELESDEHGK
TLRLTLPEGL SGEQKSQWLS TIKAVVQSAK YWNLAECTFE ASGEGVIMKE RQMTPDVYKV
TPVMNTHPSQ SEAVSDVWAL SKTSMTFQPK KAGLQPLTIS LDELFSSRGE FISVGGNGRM
SHKEAILLGL RYKKLYNQAR VKYSL