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VP35_MABVO
ID   VP35_MABVO              Reviewed;         329 AA.
AC   Q6UY68; O36425;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Polymerase cofactor VP35;
DE   AltName: Full=Marburg VP35;
DE            Short=mVP35;
GN   Name=VP35;
OS   Lake Victoria marburgvirus (strain Ozolin-75) (MARV) (Marburg virus (strain
OS   South Africa/Ozolin/1975)).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Filoviridae; Marburgvirus.
OX   NCBI_TaxID=482820;
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 Sanchez;
RX   PubMed=9448698; DOI=10.1006/viro.1997.8902;
RA   Sanchez A., Trappier S.G., Stroeher U., Nichol S.T., Bowen M.D.,
RA   Feldmann H.;
RT   "Variation in the glycoprotein and VP35 genes of Marburg virus strains.";
RL   Virology 240:138-146(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Bowen M.D., Thurman K., Minor E., Ibrahim M.S., Meyer R.F., Malfatti S.A.,
RA   Do L.H., Smith K.L., McCready P.M., Chain P.S.G.;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0007744|PDB:5XSQ}
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-28, AND INTERACTION WITH NP.
RX   PubMed=28659479; DOI=10.1128/jvi.00996-17;
RA   Zhu T., Song H., Peng R., Shi Y., Qi J., Gao G.F.;
RT   "Crystal Structure of the Marburg Virus Nucleoprotein Core Domain
RT   Chaperoned by a VP35 Peptide Reveals a Conserved Drug Target for
RT   Filovirus.";
RL   J. Virol. 91:0-0(2017).
RN   [4] {ECO:0007744|PDB:5F5O}
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-29, INTERACTION WITH NP, AND
RP   FUNCTION.
RX   PubMed=28566377; DOI=10.1128/jvi.00825-17;
RA   Liu B., Dong S., Li G., Wang W., Liu X., Wang Y., Yang C., Rao Z., Guo Y.;
RT   "Structural Insight into Nucleoprotein Conformation Change Chaperoned by
RT   VP35 Peptide in Marburg Virus.";
RL   J. Virol. 91:0-0(2017).
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, ECO:0000269|PubMed:28566377}.
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 (PubMed:28566377, PubMed:28659479). Disrupts innate immune
CC       signaling in infected host cell (By similarity).
CC       {ECO:0000250|UniProtKB:P35259, ECO:0000269|PubMed:28566377,
CC       ECO:0000269|PubMed:28659479}.
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; AF005730; AAC40455.1; -; Genomic_RNA.
DR   EMBL; AY358025; AAQ55256.1; -; Genomic_RNA.
DR   PDB; 5F5O; X-ray; 2.20 A; B/D/F=1-29.
DR   PDB; 5XSQ; X-ray; 2.60 A; B/D/F=1-28.
DR   PDBsum; 5F5O; -.
DR   PDBsum; 5XSQ; -.
DR   SMR; Q6UY68; -.
DR   PRIDE; Q6UY68; -.
DR   Proteomes; UP000000838; 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   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Host cytoplasm; Reference proteome;
KW   Transcription; Viral RNA replication; Virion.
FT   CHAIN           1..329
FT                   /note="Polymerase cofactor VP35"
FT                   /id="PRO_0000314996"
FT   DOMAIN          204..329
FT                   /note="VP35 IID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01071"
FT   COILED          70..120
FT                   /evidence="ECO:0000255"
FT   VARIANT         49
FT                   /note="P -> L (in strain: Isolate Sanchez)"
FT   VARIANT         72
FT                   /note="L -> H (in strain: Isolate Sanchez)"
FT   VARIANT         83..84
FT                   /note="IS -> TL (in strain: Isolate Sanchez)"
FT   TURN            4..6
FT                   /evidence="ECO:0007829|PDB:5F5O"
FT   HELIX           7..15
FT                   /evidence="ECO:0007829|PDB:5F5O"
FT   HELIX           22..25
FT                   /evidence="ECO:0007829|PDB:5F5O"
SQ   SEQUENCE   329 AA;  36131 MW;  3AE46FB8DDB09386 CRC64;
     MWDSSYMQQV SEGLMTGKVP IDQVFGANPL EKLYKRRKPK GTVGLQCSPC LMSKATSTDD
     IIWDQLIVKK TLADLLIPIN RQISDIQSTL SEVTTRVHEI ERQLHEITPV LKMGRTLEAI
     SKGMSEMLAK YDHLVISTGR TTAPAAAFDA YLNEHGVPPP QPAIFKDLGV AQQACSKGTM
     VKNATTDAAD KMSKVLELSE ETFSKPNLSA KDLALLLFTH LPGNNTPFHI LAQVLSKIAY
     KSGKSGAFLD AFHQILSEGE NAQAALTRLS RTFDAFLGVV PPVIRVKNFQ TVPRPCQKSL
     RAVPPNPTID KGWVCVYSSE QGETRALKI
 
 
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