VP35_MABVA
ID VP35_MABVA Reviewed; 329 AA.
AC Q1PD52;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Polymerase cofactor VP35;
DE AltName: Full=Marburg VP35;
DE Short=mVP35;
GN Name=VP35;
OS Lake Victoria marburgvirus (strain Angola/2005) (MARV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Marburgvirus.
OX NCBI_TaxID=378830;
OH NCBI_TaxID=9534; Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9407; Rousettus aegyptiacus (Egyptian rousette) (Egyptian fruit bat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Ang0126, Isolate Ang0214, Isolate Ang0215, Isolate Ang0754,
RC Isolate Ang0998, Isolate Ang1379c, Isolate Ang1381, and Isolate Ang1386;
RX PubMed=16775337; DOI=10.1128/jvi.00069-06;
RA Towner J.S., Khristova M.L., Sealy T.K., Vincent M.J., Erickson B.R.,
RA Bawiec D.A., Hartman A.L., Comer J.A., Zaki S.R., Stroeher U.,
RA Gomes da Silva F., del Castillo F., Rollin P.E., Ksiazek T.G., Nichol S.T.;
RT "Marburgvirus genomics and association with a large hemorrhagic fever
RT outbreak in Angola.";
RL J. Virol. 80:6497-6516(2006).
CC -!- FUNCTION: Plays an essential role in viral RNA synthesis and also a
CC role in suppressing innate immune signaling.
CC {ECO:0000250|UniProtKB:P35259}.
CC -!- SUBUNIT: Homooligomer. Homomultimerization via the coiled coil domain
CC is a prerequisite for binding to L. Found in a trimeric complex in
CC which VP35 bridges L and the nucleoprotein (By similarity). Interacts
CC with NP (By similarity). Disrupts innate immune signaling in infected
CC host cell (By similarity). {ECO:0000250|UniProtKB:P35259,
CC ECO:0000250|UniProtKB:Q6UY68}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P35259}. Host
CC cytoplasm {ECO:0000250|UniProtKB:P35259}.
CC -!- SIMILARITY: Belongs to the filoviridae polymerase cofactor VP35 family.
CC {ECO:0000255|PROSITE-ProRule:PRU01071, ECO:0000305}.
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DR EMBL; DQ447653; ABE27013.1; -; Genomic_RNA.
DR EMBL; DQ447654; ABE27020.1; -; Genomic_RNA.
DR EMBL; DQ447655; ABE27027.1; -; Genomic_RNA.
DR EMBL; DQ447656; ABE27034.1; -; Genomic_RNA.
DR EMBL; DQ447657; ABE27041.1; -; Genomic_RNA.
DR EMBL; DQ447658; ABE27048.1; -; Genomic_RNA.
DR EMBL; DQ447659; ABE27055.1; -; Genomic_RNA.
DR EMBL; DQ447660; ABE27062.1; -; Genomic_RNA.
DR SMR; Q1PD52; -.
DR PRIDE; Q1PD52; -.
DR Proteomes; UP000008242; Genome.
DR Proteomes; UP000097432; Genome.
DR Proteomes; UP000102513; Genome.
DR Proteomes; UP000109618; Genome.
DR Proteomes; UP000115353; Genome.
DR Proteomes; UP000130744; Genome.
DR Proteomes; UP000168007; Genome.
DR Proteomes; UP000171838; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR Gene3D; 1.10.8.950; -; 1.
DR Gene3D; 2.10.10.70; -; 1.
DR InterPro; IPR002953; Filo_VP35.
DR InterPro; IPR031163; VP35_IID.
DR InterPro; IPR043061; VP35_IID_b-sht.
DR InterPro; IPR043060; VP35_IID_hlx.
DR Pfam; PF02097; Filo_VP35; 1.
DR PIRSF; PIRSF018326; VP35_FiloV; 1.
DR PRINTS; PR01240; FILOVP35.
DR PROSITE; PS51735; VP35_IID; 1.
PE 3: Inferred from homology;
KW Coiled coil; Host cytoplasm; Reference proteome; Transcription;
KW Viral RNA replication; Virion.
FT CHAIN 1..329
FT /note="Polymerase cofactor VP35"
FT /id="PRO_0000314995"
FT DOMAIN 204..329
FT /note="VP35 IID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01071"
FT COILED 70..120
FT /evidence="ECO:0000255"
SQ SEQUENCE 329 AA; 36145 MW; 69E142BA99BBE004 CRC64;
MWDSSYMQQV SEGLMTGKVP IDQVFGTNPL EKLYKRRKPK GTVGLQCSPC LMSKATSTDD
IIWDQLVVRK TLADLLIPIN RQISDIQSTL SEVTTRVHEI ERQLHEITPV LKMGRTLEAI
SKGMSEMLAK YDHLVISTGR TTAPAAAFDA YLNEHGVPPP QPAIFKDLGV AQQACSKGTT
VKNATTDAAD KMSKVLELSE ETFSKPNLSA KDLALLLFTH LPGNNTPFHI LAQVLSKIAY
KSGKSGAFLD AFHQILSEGE NAQAALTRLS RTFDAFLGVV PPVIRVKNFQ TVPRPCQKSL
RAVPPNPTID KGWVCVYSSE QGETRALKI