ID PRIM_HCMVA Reviewed; 946 AA. AC P17149; Q7M6M2; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 2. DT 10-JUN-2026, entry version 93. DE RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_04011}; DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_04011}; GN Name=UL70; OS Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5). OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes; OC Herpesvirales; Orthoherpesviridae; Betaherpesvirinae; Cytomegalovirus; OC Cytomegalovirus humanbeta5; Human cytomegalovirus. OX NCBI_TaxID=10360; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=2161319; DOI=10.1007/978-3-642-74980-3_6; RA Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R., RA Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A., RA Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.; RT "Analysis of the protein-coding content of the sequence of human RT cytomegalovirus strain AD169."; RL Curr. Top. Microbiol. Immunol. 154:125-169(1990). RN [2] RP GENOME REANNOTATION. RX PubMed=12533697; DOI=10.1099/vir.0.18606-0; RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J., RA McGeoch D.J., Hayward G.S.; RT "The human cytomegalovirus genome revisited: comparison with the chimpanzee RT cytomegalovirus genome."; RL J. Gen. Virol. 84:17-28(2003). RN [3] RP ERRATUM OF PUBMED:12533697. RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J., RA McGeoch D.J., Hayward G.S.; RL J. Gen. Virol. 84:1053-1053(2003). RN [4] RP INTERACTION WITH UL102 AND UL105. RX PubMed=12076828; DOI=10.1016/s0168-1702(02)00054-0; RA McMahon T.P., Anders D.G.; RT "Interactions between human cytomegalovirus helicase-primase proteins."; RL Virus Res. 86:39-52(2002). 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 (By similarity). CC {ECO:0000255|HAMAP-Rule:MF_04011, ECO:0000269|PubMed:12076828}. 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}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA35386.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X17403; CAA35386.1; ALT_INIT; Genomic_DNA. DR EMBL; BK000394; DAA00166.1; -; Genomic_DNA. DR PIR; S09834; S09834. DR SMR; P17149; -. DR MINT; P17149; -. DR Proteomes; UP000008992; Segment. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IDA:UniProtKB. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR HAMAP; MF_04011; HSV_PRIM; 1. DR InterPro; IPR033685; HSV_PRIM. DR Pfam; PF03121; Herpes_UL52; 1. PE 1: Evidence at protein level; KW DNA replication; Host nucleus; Host-virus interaction; Metal-binding; KW Reference proteome; Transferase; Zinc; Zinc-finger. FT CHAIN 1..946 FT /note="DNA primase" FT /id="PRO_0000116115" FT ZN_FING 881..920 FT /note="CHC2-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011" FT REGION 596..626 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 617..626 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 517 FT /note="Essential for primase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011" FT SITE 519 FT /note="Essential for primase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011" SQ SEQUENCE 946 AA; 107826 MW; B64BFF01BF1D0A2D CRC64; MTLVLFATEY DSAHIVANVL SQTPTDHCVF PLLVKHQVSR RVYFCLQTQK CSDSRRVAPV FAVNNETLQL SRYLAARQPI PLSALIASLD EAETQPLYRH LFRTPVLSPE HGGEVREFKH LVYFHHAAVL RHLNQVFLCP TSPSWFISVF GHTEGQVLLT MAYYLFEGQY STISTVEEYV RSFCTRDLGT IIPTHASMGE FARLLLGSPF RQRVSAFVAY AVARNRRDYT ELEQVDTQIN AFRERARLPD TVCVHYVYLA YRTALARARL LEYRRVVAYD ADAAPEAQCT REPGFLGRRL STELLDVMQK YFSLDNFLHD YVETHLLRLD ESPHSATSPH GLGLAGYGGR IDGTHLAGFF GTSTQLARQL ERINTLSESV FSPLERSLSG LLRLCASLRT AQTYTTGTLT RYSQRRYLLP EPALAPLLER PLPVYRVHLP NDQHVFCAVA SETWHRSLFP RDLLRHVPDS RFSDEALTET VWLHDDDVAS TSPETQFYYT RHEVFNERLP VFNFVADFDL RLRDGVSGLA RHTVFELCRG LRRVWMTVWA SLFGYTHPDR HPVYFFKSAC PPNSVPVDAA GAPFDDDDYL DYRDERDTEE DEDGKEDKNN VPDNGVFQKT TSSVDTSPPY CRCKGKLGLR IITPFPACTV AVHPSVLRAV AQVLNHAVCL DAELHTLLDP ISHPESSLDT GIYHHGRSVR LPYMYKMDQD DGYFMHRRLL PLFIVPDAYR EHPLGFVRAQ LDLRNLLHHH PPHDLPALPL SPPPRVILSV RDKICPSTEA NFIETRSLNV TRYRRRGLTE VLAYHLYGGD GATAAAISDT DLQRLVVTRV WPPLLEHLTQ HYEPHVSEQF TAPHVLLFQP HGACCVAVKR RDGARTRDFR CLNYTHRNPQ ETVQVFIDLR TEHSYALWAS LWSRCFTKKC HSNAKNVHIS IKIRPPDAPV PPATAV //