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PRIM_HHV2H
ID   PRIM_HHV2H              Reviewed;        1066 AA.
AC   P89471;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   23-FEB-2022, entry version 70.
DE   RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_04011};
DE            EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_04011};
GN   ORFNames=UL52;
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: Essential component of the helicase/primase complex. Unwinds
CC       the DNA at the replication forks and generates single-stranded DNA for
CC       both leading and lagging strand synthesis. The primase initiates primer
CC       synthesis and thereby produces large amount of short RNA primers on the
CC       lagging strand that the polymerase elongates using dNTPs.
CC       {ECO:0000255|HAMAP-Rule:MF_04011}.
CC   -!- SUBUNIT: Associates with the helicase and the primase-associated factor
CC       to form the helicase-primase factor. {ECO:0000255|HAMAP-Rule:MF_04011}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04011}.
CC       Note=Requires the presence of the primase associated factor to properly
CC       localize in the host cell nucleus. {ECO:0000255|HAMAP-Rule:MF_04011}.
CC   -!- SIMILARITY: Belongs to the herpesviridae DNA primase family.
CC       {ECO:0000255|HAMAP-Rule:MF_04011}.
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DR   EMBL; Z86099; CAB06739.1; -; Genomic_DNA.
DR   ChEMBL; CHEMBL4630722; -.
DR   PRIDE; P89471; -.
DR   Proteomes; UP000001874; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04011; HSV_PRIM; 1.
DR   InterPro; IPR033685; HSV_PRIM.
PE   3: Inferred from homology;
KW   DNA replication; Host nucleus; Metal-binding; Reference proteome;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..1066
FT                   /note="DNA primase"
FT                   /id="PRO_0000385149"
FT   ZN_FING         995..1035
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
FT   REGION          694..727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            631
FT                   /note="Essential for primase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
FT   SITE            633
FT                   /note="Essential for primase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
SQ   SEQUENCE   1066 AA;  114654 MW;  A6BD223DED54C17F CRC64;
     MGTEDCDHEG RSVAAPVEVT ALYATDGCVI TSSLALLTNC LLGAEPLYIF SYDAYRSDAP
     NGPTGAPTEQ ERFEGSRALY RDAGGLNGDS FRVTFCLLGT EVGVTHHPKG RTRPMFVCRF
     ERADDVAVLQ DALGRGTPLL PAHVTATLDL EATFALHANI IMALTVAIVH NAPARIGSGS
     TAPLYEPGES MRSVVGRMSL GQRGLTTLFV HHEARVLGAY RRAYYGSAQS PFWFLSKFGP
     DEKSLVLAAR YYLLQAPRLG GAGATYDLQA VKDICATYAI PHDPRPDTLS AASLTSFAAI
     TRFCCTSQYS RGAAAAGFPL YVERRIAADV RETGALEKFI AHDRSCLRVS DREFITYIYL
     AHFECFSPPR LATHLRAVTT HDPSPAASTE QPSPLGREAV EQFFRHVRAQ LNIREYVKQN
     VTPRETALAG DAAAAYLRAR TYAPAALTPA PAYCGVADSS TKMMGRLAEA ERLLVPHGWP
     AFAPTTPGDD AGGGTAAPQT CGIVKRLLKL AATEQQGTTP PAIAALMQDA SVQTPLPVYR
     ITMSPTGQAF AAAARDDWAR VTRDARPPEA TVVADAAAAP EPGALGRRLT RRICARGPAL
     PPGGLAVGGQ MYVNRNEIFN AALAVTNIIL DLDIALKEPV PFPRLHEALG HFRRGALAAV
     QLLFPAARVD PDAYPCYFFK SACRPRAPPV CAGDGPSAGG DDGDGDWFPD AGGPGDEEWE
     EDTDPMDTTH GPLPDDEAAY LDLLHEQIPA ATPSEPDSVV CSCADKIGLR VCLPVPAPYV
     VHGSLTMRGV ARVIQQAVLL DRDFVEAVGS HVKNFLLIDT GVYAHGHSLR LPYFAKIGPD
     GSACGRLLPV FVIPPACEDV PAFVAAHADP RRFHFHAPPM FSAAPREIRV LHSLGGDYVS
     FFEKKASRNA LEHFGRRETL TEVLGRYDVR PDAGETVEGF ASELLGRIVA CIEAHFPEHA
     REYQAVSVRR AVIKDDWVLL QLIPGRGALN QSLSCLRFKH GRASRATART FLALSVGTNN
     RLCASLCQQC FATKCDNNRL HTLFTVDAGT PCSRSAPSST SRPSSS
 
 
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