HELI_PSHV1
ID HELI_PSHV1 Reviewed; 855 AA.
AC Q6UDG9;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 54.
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=UL5;
OS Psittacid herpesvirus 1 (isolate Amazon parrot/-/97-0001/1997) (PsHV-1)
OS (Pacheco's disease virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Iltovirus.
OX NCBI_TaxID=670426;
OH NCBI_TaxID=152276; Amazona oratrix (yellow-headed parrot).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16873243; DOI=10.1128/jvi.00134-06;
RA Thureen D.R., Keeler C.L. Jr.;
RT "Psittacid herpesvirus 1 and infectious laryngotracheitis virus:
RT Comparative genome sequence analysis of two avian alphaherpesviruses.";
RL J. Virol. 80:7863-7872(2006).
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; AY372243; AAQ73741.1; -; Genomic_DNA.
DR RefSeq; NP_944435.1; NC_005264.1.
DR PRIDE; Q6UDG9; -.
DR GeneID; 2656955; -.
DR KEGG; vg:2656955; -.
DR Proteomes; UP000006840; 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; -; 1.
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..855
FT /note="DNA replication helicase"
FT /id="PRO_0000406834"
FT BINDING 78..85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04030"
SQ SEQUENCE 855 AA; 95258 MW; B1A7E3BA523B5E25 CRC64;
MAEDRGTRLW QFPDHVYLNF TAMHGIQHVV DRISSLAEES VTPAERPPLS WFEAVARADS
PDEVPPRELP FRVYLITGNA GSGKSTCIQA LTEMLNCVTT GSTRVAALNV FTKLSSAYTS
PAIQTIFHDF GFKGSHVQAV LGKFKYPKQP DPKSLVDAQM SDLYYYWDVL KDIANKVVEG
GLPETMRVLL SLELKSGKPF TDAAPFLSAA TPALIRSNVV LIDEAGVLGK HILTAVVFSW
WLHNALWQTR RYAEGKVPVI VCIGSPTQTD AMESVFEHST LRHLVSNKTN ILSHLIRSSE
MAERMNLNRN WTIFINNKRC TEQDFGNVLK AFEFGLPMNE GHARFLDQFV VSESYIKDPS
KLPGWTRLFA SHDDVKVYMS RLHANLRARR SDKFKVFVLP IYTVVSLEAF DKYKELTGQT
SLTMEKWLTA NASRLGNYSQ SRDLDVTTPR FEYGTADGKK FALITTDASH VLNSQISVTK
RVKKLVFGFE GSFGDFAAVL SEDTFFKKHG EDHVEFAYRF IAALLFSGMI AFYDFLRTEG
LPQDKVDAAY SRLQAVTADL LAATHEQLGI AAAAGAQTGS GARRSRNADA FAFDDDASEE
VTDAELDDLF GAMTDNSMDA FYLNYEKLPA DAHGQEIFFH FDMLKRLFSE RYDALSGLFG
KTFTSAPFRT FVGQASFNGS NAFVSSFSGG ILSFTSQTDA YTLRGVTRAP VPCFVDELFR
GRDWAAAILR ETDMPRVVVS DSMGFVSVIN HNMSTFVDNV SGEELQMAAT VDHGISSNLA
MTITRSQGLG LDRVAICFAT SQLKLNTAYV AMSRVTSCRY LRMNVNPLRT HYEDTRRVSA
HILAALRCKD VKLVY