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PAP_HHV2H
ID   PAP_HHV2H               Reviewed;         470 AA.
AC   P89463;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   02-JUN-2021, entry version 69.
DE   RecName: Full=DNA polymerase processivity factor;
DE   AltName: Full=DNA-binding protein UL42;
DE   AltName: Full=Polymerase accessory protein;
DE            Short=PAP;
GN   ORFNames=UL42;
OS   Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10315;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9499055; DOI=10.1128/jvi.72.3.2010-2021.1998;
RA   Dolan A., Jamieson F.E., Cunningham C., Barnett B.C., McGeoch D.J.;
RT   "The genome sequence of herpes simplex virus type 2.";
RL   J. Virol. 72:2010-2021(1998).
CC   -!- FUNCTION: Plays an essential role in viral DNA replication by acting as
CC       the polymerase accessory subunit. Associates with the viral polymerase
CC       to increase its processivity and forms high-affinity direct
CC       interactions with DNA. Facilitates the origin-binding protein loading
CC       onto DNA thus increasing its ability to assemble into a functional
CC       complex capable of unwinding duplex DNA (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the DNA polymerase catalytic subunit. Interacts
CC       with the origin-binding protein (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the herpesviridae DNA polymerase processivity
CC       factor family. {ECO:0000305}.
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DR   EMBL; Z86099; CAB06728.1; -; Genomic_DNA.
DR   RefSeq; YP_009137194.1; NC_001798.2.
DR   SMR; P89463; -.
DR   PRIDE; P89463; -.
DR   DNASU; 1487329; -.
DR   GeneID; 1487329; -.
DR   KEGG; vg:1487329; -.
DR   Proteomes; UP000001874; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   InterPro; IPR003202; Herpes_UL42.
DR   Pfam; PF02282; Herpes_UL42; 2.
PE   3: Inferred from homology;
KW   DNA replication; DNA-binding; Host nucleus; Reference proteome.
FT   CHAIN           1..470
FT                   /note="DNA polymerase processivity factor"
FT                   /id="PRO_0000385147"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          329..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          446..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           385..404
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        329..352
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..367
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..399
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   470 AA;  49884 MW;  73D2433B210669CB CRC64;
     MAHLPGGAAA APLSEDAIPS PRERTEDWPP CQIVLQGAEL NGILQAFAPL RTSLLDSLLV
     VGDRGILVHN AIFGEQVFLP LDHSQFSRYR WGGPTAAFLS LVDQKRSLLS VFRANQYPDL
     RRVELTVTGQ APFRTLVQRI WTTASDGEAV ELASETLMKR ELTSFAVLLP QGDPDVQLRL
     TKPQLTKVVN AVGDETAKPT TFELGPNGKF SVFNARTCVT FAAREEGASS STSAQVQILT
     SALKKAGQAA ANAKTVYGEN THRTFSVVVD DCSMRAVLRR LQVGGGTLKF FLTADVPSVC
     VTATGPNAVS AVFLLKPQRV CLNWLGRSPG SSTGSLASQD SRAGPTDSQD SSSEPDAGDR
     GAPEEEGLEG QARVPPAFPE PPGTKRRHPG AEVVPADDAT KRPKTGVPAA PTRAESPPLS
     ARYGPEAAEG GGDGGRYACY FRDLQTGDAS PSPLSAFRGP QRPPYGFGLP
 
 
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