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H5_VACCW
ID   H5_VACCW                Reviewed;         203 AA.
AC   P07242; Q76ZS8;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   23-FEB-2022, entry version 80.
DE   RecName: Full=Late transcription elongation factor H5;
DE   AltName: Full=Viral late gene transcription factor 4;
DE            Short=VLTF-4;
GN   OrderedLocusNames=VACWR103; ORFNames=H5R;
OS   Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS   WR)).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10254;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3021979; DOI=10.1128/jvi.60.2.436-449.1986;
RA   Rosel J.L., Earl P.L., Weir J.P., Moss B.;
RT   "Conserved TAAATG sequence at the transcriptional and translational
RT   initiation sites of vaccinia virus late genes deduced by structural and
RT   functional analysis of the HindIII H genome fragment.";
RL   J. Virol. 60:436-449(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2462305;
RA   Gordon J., Kovala T., Dales S.;
RT   "Molecular characterization of a prominent antigen of the vaccinia virus
RT   envelope.";
RL   Virology 167:361-369(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA   Wohlhueter R.;
RT   "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT   redundancy and an error rate of 0.16/10kb.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=Dts57, IHDW, and WR;
RX   PubMed=20206959; DOI=10.1016/j.virol.2010.01.020;
RA   D'Costa S.M., Bainbridge T.W., Kato S.E., Prins C., Kelley K., Condit R.C.;
RT   "Vaccinia H5 is a multifunctional protein involved in viral DNA
RT   replication, postreplicative gene transcription, and virion
RT   morphogenesis.";
RL   Virology 401:49-60(2010).
RN   [5]
RP   IDENTIFICATION, AND SUBCELLULAR LOCATION.
RX   PubMed=8794318; DOI=10.1128/jvi.70.10.6796-6802.1996;
RA   Kovacs G.R., Moss B.;
RT   "The vaccinia virus H5R gene encodes late gene transcription factor 4:
RT   purification, cloning, and overexpression.";
RL   J. Virol. 70:6796-6802(1996).
RN   [6]
RP   INTERACTION WITH THE LATE TRANSCRIPTION ELONGATION FACTOR G2, AND POSSIBLE
RP   IDENTIFICATION IN A COMPLEX WITH A18 AND G2.
RX   PubMed=9636370; DOI=10.1006/viro.1998.9166;
RA   Black E.P., Moussatche N., Condit R.C.;
RT   "Characterization of the interactions among vaccinia virus transcription
RT   factors G2R, A18R, and H5R.";
RL   Virology 245:313-322(1998).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=10769065; DOI=10.1099/0022-1317-81-5-1231;
RA   Domi A., Beaud G.;
RT   "The punctate sites of accumulation of vaccinia virus early proteins are
RT   precursors of sites of viral DNA synthesis.";
RL   J. Gen. Virol. 81:1231-1235(2000).
RN   [8]
RP   PHOSPHORYLATION AT THR-84 AND THR-85.
RX   PubMed=11001589; DOI=10.1186/1471-2091-1-2;
RA   Brown N.G., Nick Morrice D., Beaud G., Hardie G., Leader D.P.;
RT   "Identification of sites phosphorylated by the vaccinia virus B1R kinase in
RT   viral protein H5R.";
RL   BMC Biochem. 1:2-2(2000).
RN   [9]
RP   INTERACTION WITH A20.
RX   PubMed=12490386; DOI=10.1006/viro.2002.1721;
RA   Ishii K., Moss B.;
RT   "Mapping interaction sites of the A20R protein component of the vaccinia
RT   virus DNA replication complex.";
RL   Virology 303:232-239(2002).
RN   [10]
RP   INTERACTION WITH VLTF-1 AND VLTF-3.
RX   PubMed=15518812; DOI=10.1016/j.virol.2004.08.017;
RA   Dellis S., Strickland K.C., McCrary W.J., Patel A., Stocum E., Wright C.F.;
RT   "Protein interactions among the vaccinia virus late transcription
RT   factors.";
RL   Virology 329:328-336(2004).
RN   [11]
RP   FUNCTION.
RX   PubMed=17376501; DOI=10.1016/j.virol.2007.02.016;
RA   Cresawn S.G., Condit R.C.;
RT   "A targeted approach to identification of vaccinia virus postreplicative
RT   transcription elongation factors: genetic evidence for a role of the H5R
RT   gene in vaccinia transcription.";
RL   Virology 363:333-341(2007).
RN   [12]
RP   FUNCTION, AND PHOSPHORYLATION.
RX   PubMed=18089571; DOI=10.1074/jbc.m709258200;
RA   D'Costa S.M., Bainbridge T.W., Condit R.C.;
RT   "Purification and properties of the vaccinia virus mRNA processing
RT   factor.";
RL   J. Biol. Chem. 283:5267-5275(2008).
CC   -!- FUNCTION: Involved in the co-transcriptional or post-transcriptional
CC       endoribonucleolytic cleavage that generates sequence-homogeneous 3'
CC       ends during late transcription. Involved in postreplicative
CC       transcription elongation on intermediate and late genes (Probable).
CC       Also involved in DNA replication and in multiple steps of virion
CC       morphogenesis. Required both for inclusion of virosoplasm into
CC       crescents as well as for maturation of immature virions (IV) into
CC       mature virions (MV). {ECO:0000269|PubMed:17376501,
CC       ECO:0000269|PubMed:18089571, ECO:0000269|PubMed:20206959, ECO:0000305}.
CC   -!- SUBUNIT: Interacts with the DNA polymerase processivity factor A20.
CC       Interacts with B1R kinase. Interacts with the late transcription
CC       factors VLTF-1 AND VLTF-3. Interacts with the late transcription
CC       elongation factor G2. Interacts with itself. Might be part of a
CC       transcription complex composed at least of G2, A18, and H5.
CC       {ECO:0000269|PubMed:12490386, ECO:0000269|PubMed:15518812,
CC       ECO:0000269|PubMed:9636370}.
CC   -!- INTERACTION:
CC       P07242; P68456: VACWR080; NbExp=4; IntAct=EBI-7272435, EBI-7273347;
CC       P07242; P68613: VLTF1; NbExp=4; IntAct=EBI-7272435, EBI-7273218;
CC       P07242; P68318: VLTF3; Xeno; NbExp=2; IntAct=EBI-7272435, EBI-7366338;
CC   -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm. Note=Early during viral
CC       infection, diffusely localizes within the cytoplasm. Following DNA
CC       replication, localizes specifically to virus factories.
CC   -!- INDUCTION: Constitutively expressed in abundance during viral
CC       replication.
CC   -!- PTM: Phosphorylated at multiple sites. Phosphorylation is necessary for
CC       cleavage activity. Phosphorylated by the viral B1R and F10 kinases
CC       (Probable). {ECO:0000305|PubMed:11001589, ECO:0000305|PubMed:18089571}.
CC   -!- SIMILARITY: Belongs to the chordopoxvirinae protein H5 family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to be p35/Ag35, a membrane protein
CC       involved in the biogenesis of the viral envelope encoded by H3L gene.
CC       {ECO:0000305|PubMed:2462305}.
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DR   EMBL; M13209; AAB59841.1; -; Genomic_DNA.
DR   EMBL; M23648; AAA47962.1; -; Genomic_DNA.
DR   EMBL; AY243312; AAO89382.1; -; Genomic_DNA.
DR   PIR; F24481; QQVZH6.
DR   RefSeq; YP_232985.1; NC_006998.1.
DR   SMR; P07242; -.
DR   DIP; DIP-2164N; -.
DR   IntAct; P07242; 9.
DR   MINT; P07242; -.
DR   iPTMnet; P07242; -.
DR   DNASU; 3707559; -.
DR   GeneID; 3707559; -.
DR   KEGG; vg:3707559; -.
DR   Proteomes; UP000000344; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IDA:UniProtKB.
DR   GO; GO:0019031; C:viral envelope; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0039693; P:viral DNA genome replication; IDA:UniProtKB.
DR   GO; GO:0019083; P:viral transcription; IDA:UniProtKB.
DR   InterPro; IPR004966; Pox_Ag35.
DR   Pfam; PF03286; Pox_Ag35; 1.
PE   1: Evidence at protein level;
KW   Elongation factor; Host cytoplasm; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome; Transcription; Transcription regulation; Virion.
FT   CHAIN           1..203
FT                   /note="Late transcription elongation factor H5"
FT                   /id="PRO_0000099204"
FT   REGION          25..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         84
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000305|PubMed:11001589"
FT   MOD_RES         85
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000305|PubMed:11001589"
FT   VARIANT         189
FT                   /note="G -> R (in strain: Dts57)"
SQ   SEQUENCE   203 AA;  22300 MW;  89B54D5DFD976B7D CRC64;
     MAWSITNKAD TSSFTKMAEI RAHLKNSAEN KDKNEDIFPE DVIIPSTKPK TKRATTPRKP
     AATKRSTKKE EVEEEVVIEE YHQTTEKNSP SPGVSDIVES VAAVELDDSD GDDEPMVQVE
     AGKVNHSARS DLSDLKVATD NIVKDLKKII TRISAVSTVL EDVQAAGISR QFTSMTKAIT
     TLSDLVTEGK SKVVRKKVKT CKK
 
 
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