HELI_SHV21
ID HELI_SHV21 Reviewed; 781 AA.
AC Q01014;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=DNA replication helicase {ECO:0000255|HAMAP-Rule:MF_04030};
DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_04030};
GN Name=HELI {ECO:0000255|HAMAP-Rule:MF_04030}; OrderedLocusNames=44;
OS Saimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=10383;
OH NCBI_TaxID=9521; Saimiri sciureus (Common squirrel monkey).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=1321287; DOI=10.1128/jvi.66.8.5047-5058.1992;
RA Albrecht J.-C., Nicholas J., Biller D., Cameron K.R., Biesinger B.,
RA Newman C., Wittmann S., Craxton M.A., Coleman H., Fleckenstein B.,
RA Honess R.W.;
RT "Primary structure of the herpesvirus saimiri genome.";
RL J. Virol. 66:5047-5058(1992).
CC -!- FUNCTION: This protein may be a helicase and is required for
CC replication of viral DNA.
CC -!- FUNCTION: Component of the helicase/primase complex. Unwinds the DNA at
CC the replication forks and generates single-stranded DNA for both
CC leading and lagging strand synthesis. The primase synthesizes short RNA
CC primers on the lagging strand that the polymerase elongates using
CC dNTPs. Possesses helicase-like motifs and therefore may act as the
CC helicase subunit of the complex. {ECO:0000255|HAMAP-Rule:MF_04030}.
CC -!- SUBUNIT: Associates with the primase and the primase-associated factor
CC to form the helicase-primase complex. {ECO:0000255|HAMAP-
CC Rule:MF_04030}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04030}.
CC -!- SIMILARITY: Belongs to the herpesviridae helicase family.
CC {ECO:0000255|HAMAP-Rule:MF_04030}.
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DR EMBL; X64346; CAA45666.1; -; Genomic_DNA.
DR RefSeq; NP_040246.1; NC_001350.1.
DR PRIDE; Q01014; -.
DR GeneID; 1682486; -.
DR KEGG; vg:1682486; -.
DR Proteomes; UP000000587; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_04030; HSV_HELI; 1.
DR InterPro; IPR003840; DNA_helicase.
DR InterPro; IPR034711; HSV_HELI.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF02689; Herpes_Helicase; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 3: Inferred from homology;
KW ATP-binding; DNA replication; Helicase; Host nucleus; Hydrolase;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..781
FT /note="DNA replication helicase"
FT /id="PRO_0000115853"
FT BINDING 64..71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04030"
SQ SEQUENCE 781 AA; 88254 MW; 4099BD4A3AF94C68 CRC64;
MAELSPEFIL NMTSDAKVRI IVEKIRKLSN ITTRPPEMTL YNDQFDPEQC PGTLLPFTCY
VITGTAGAGK STSISALYQN LNCLITGATT VASQNLSRCL KTYCPTIFNA FGFKSKHINI
LPRSVPRRTL DTIEQIQNFE LCKYWPILTS IIQEFSKKKN LGQYSSISLA AFNMLAKMTT
TLWTTNVIVI DEAGTLSSHI LTAVVFCYWF YNSWLNTPLY RSGAVPCIVC VGSPTQTDAF
NSTYNHIQQK YNIMECDNIL SFIIGNKVVS EYISLTNNWA LFINNKRCTD PEFGHLLKTL
EYSLKISPKT MEYIDRFVVP KAQILNPLEF LGWTRLFLSH AEVKSYLSSL HTALVTGTNV
SGAKLFTCPI VCEVFTKAFN EYKSHVNLPS LTATEWLSKN LHRLSNYSQF IDQDMTAIHT
ETTDTSTKVT YLTKYVKNTY ISLNGKTKKC VCGYVGTYKN FKKILESESF IDSHANDQPE
FVYSFLCTIL YNSLYNFHNY GVTEKNESYL NDLANLKLPE NLTHLYTQTD LDIEREALML
EDDVFYHMVS PPPTASSASL PCLISWYTAL KDIFISRLKL ATTWFSNKFL DREFTSFTIN
MLVRDNIEFT STNGRLHGLL EYASTVESYK LQGYTFLPVN FGRSQTTVIS KDLQDKMPSI
VVQDSSGFIA CLEKNVNKML ETLDDGKSFH LCSAGDYGIS SKLAMTIVKA QGTSLDKVAI
CFSNHKKIKV SHIYVAISRA TNPNHIVMDC NPLKLLVNDT QSISSQHIIK ALNNPNTLLV
Y