ID PRIM_HHV11 Reviewed; 1058 AA. AC P10236; B9VQI1; Q09I82; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 04-NOV-2026, entry version 102. 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 1 (strain 17) (HHV-1) (Human herpes simplex virus 1). OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes; OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus; OC Simplexvirus humanalpha1; Human herpesvirus 1. OX NCBI_TaxID=10299; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531; RA McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D., RA Perry L.J., Scott J.E., Taylor P.; RT "The complete DNA sequence of the long unique region in the genome of RT herpes simplex virus type 1."; RL J. Gen. Virol. 69:1531-1574(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2826807; DOI=10.1128/jvi.62.2.444-453.1988; RA McGeoch D.J., Dalrymple M.A., Dolan A., McNab D., Perry L.J., Taylor P., RA Challberg M.D.; RT "Structures of herpes simplex virus type 1 genes required for replication RT of virus DNA."; RL J. Virol. 62:444-453(1988). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nonneuroinvasive mutant HF10; RX PubMed=17218138; DOI=10.1016/j.micinf.2006.10.019; RA Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.; RT "Determination and analysis of the DNA sequence of highly attenuated herpes RT simplex virus type 1 mutant HF10, a potential oncolytic virus."; RL Microbes Infect. 9:142-149(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17 syn+; RA Cunningham C., Davison A.J.; RT "Herpes simplex virus type 1 bacterial artificial chromosome."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [5] RP INTERACTION WITH UL8 AND UL5. RX PubMed=2538835; DOI=10.1073/pnas.86.7.2186; RA Crute J.J., Tsurumi T., Zhu L.A., Weller S.K., Olivo P.D., Challberg M.D., RA Mocarski E.S., Lehman I.R.; RT "Herpes simplex virus 1 helicase-primase: a complex of three herpes-encoded RT gene products."; RL Proc. Natl. Acad. Sci. U.S.A. 86:2186-2189(1989). RN [6] RP FUNCTION, AND MUTAGENESIS OF ASP-628. RX PubMed=8189507; DOI=10.1128/jvi.68.6.3693-3701.1994; RA Klinedinst D.K., Challberg M.D.; RT "Helicase-primase complex of herpes simplex virus type 1: a mutation in the RT UL52 subunit abolishes primase activity."; RL J. Virol. 68:3693-3701(1994). RN [7] RP FUNCTION. RX PubMed=7775476; DOI=10.1074/jbc.270.23.14148; RA Dracheva S., Koonin E.V., Crute J.J.; RT "Identification of the primase active site of the herpes simplex virus type RT 1 helicase-primase."; RL J. Biol. Chem. 270:14148-14153(1995). RN [8] RP SUBCELLULAR LOCATION. RX PubMed=8811024; DOI=10.1099/0022-1317-77-9-2241; RA Marsden H.S., Cross A.M., Francis G.J., Patel A.H., MacEachran K., RA Murphy M., McVey G., Haydon D., Abbotts A., Stow N.D.; RT "The herpes simplex virus type 1 UL8 protein influences the intracellular RT localization of the UL52 but not the ICP8 or POL replication proteins in RT virus-infected cells."; RL J. Gen. Virol. 77:2241-2249(1996). 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, ECO:0000269|PubMed:7775476, CC ECO:0000269|PubMed:8189507}. 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 ECO:0000269|PubMed:2538835}. CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04011, CC ECO:0000269|PubMed:8811024}. Note=Requires the presence of the primase CC associated factor to properly localize in the host cell nucleus. CC {ECO:0000255|HAMAP-Rule:MF_04011, ECO:0000269|PubMed:8811024}. CC -!- SIMILARITY: Belongs to the herpesviridae DNA primase family. CC {ECO:0000255|HAMAP-Rule:MF_04011}. 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; X14112; CAA32288.1; -; Genomic_DNA. DR EMBL; AH002360; AAA45826.1; -; Genomic_DNA. DR EMBL; DQ889502; ABI63513.1; -; Genomic_DNA. DR EMBL; FJ593289; ACM62276.1; -; Genomic_DNA. DR PIR; E29890; WMBE52. DR RefSeq; YP_009137128.1; NC_001806.2. DR PDB; 9NDA; EM; 2.90 A; A=2-1058. DR PDB; 9NDQ; EM; 3.00 A; A=2-1058. DR PDB; 9NDT; EM; 3.80 A; A=17-892. DR PDB; 9NDZ; EM; 3.00 A; A=1-1058. DR PDB; 9NE0; EM; 3.40 A; A=17-1040. DR PDB; 9NEB; EM; 2.80 A; A=1-1058. DR PDB; 9NEE; EM; 3.20 A; A=1-1058. DR PDB; 9NEL; EM; 3.20 A; A=1-1058. DR PDB; 9NN2; EM; 3.10 A; B=1-1058. DR PDB; 9NNP; EM; 3.20 A; B=1-1058. DR PDB; 9NQP; EM; 3.20 A; B=1-1058. DR PDB; 9UT1; EM; 3.14 A; B=1-1058. DR PDB; 9UT3; EM; 2.88 A; B=1-1058. DR PDB; 9UT4; EM; 2.91 A; B=1-1058. DR PDB; 9UT5; EM; 3.32 A; B=1-1058. DR PDB; 9UT6; EM; 3.12 A; B=1-1058. DR PDB; 9UT7; EM; 3.08 A; B=1-1058. DR PDB; 9VLQ; EM; 3.40 A; C=1-1058. DR EMDB; EMD-49269; -. DR EMDB; EMD-49276; -. DR EMDB; EMD-49277; -. DR EMDB; EMD-49290; -. DR EMDB; EMD-49291; -. DR EMDB; EMD-49304; -. DR EMDB; EMD-49306; -. DR EMDB; EMD-49326; -. DR EMDB; EMD-49563; -. DR EMDB; EMD-49585; -. DR EMDB; EMD-49669; -. DR EMDB; EMD-64478; -. DR EMDB; EMD-64479; -. DR EMDB; EMD-64480; -. DR EMDB; EMD-64481; -. DR EMDB; EMD-64482; -. DR EMDB; EMD-64483; -. DR EMDB; EMD-65163; -. DR SMR; P10236; -. DR BioGRID; 971449; 2. DR DIP; DIP-1092N; -. DR BindingDB; P10236; -. DR ChEMBL; CHEMBL4380; -. DR DNASU; 2703423; -. DR GeneID; 2703423; -. DR KEGG; vg:2703423; -. DR Proteomes; UP000009294; Segment. DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB. 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 3D-structure; DNA replication; Host nucleus; Metal-binding; KW Reference proteome; Transferase; Zinc; Zinc-finger. FT CHAIN 1..1058 FT /note="DNA primase" FT /id="PRO_0000116104" FT ZN_FING 988..1028 FT /note="CHC2-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011, FT ECO:0000305|PubMed:8189507" FT SITE 628 FT /note="Essential for primase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011" FT SITE 630 FT /note="Essential for primase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011" FT VARIANT 211 FT /note="V -> A (in strain: Nonneuroinvasive mutant HF10)" FT VARIANT 364 FT /note="S -> N (in strain: Nonneuroinvasive mutant HF10)" FT VARIANT 515 FT /note="P -> T (in strain: Nonneuroinvasive mutant HF10)" FT MUTAGEN 628 FT /note="D->Q: Complete loss of primase activity." FT /evidence="ECO:0000269|PubMed:8189507" FT STRAND 18..25 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 30..38 FT /evidence="ECO:0007829|PDB:9UT3" FT TURN 42..44 FT /evidence="ECO:0007829|PDB:9UT3" FT STRAND 48..57 FT /evidence="ECO:0007829|PDB:9UT3" FT STRAND 61..63 FT /evidence="ECO:0007829|PDB:9NN2" FT HELIX 67..77 FT /evidence="ECO:0007829|PDB:9UT3" FT STRAND 82..84 FT /evidence="ECO:0007829|PDB:9UT3" FT STRAND 89..96 FT /evidence="ECO:0007829|PDB:9UT3" FT STRAND 104..106 FT /evidence="ECO:0007829|PDB:9UT3" FT STRAND 109..118 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 121..133 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 139..145 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 148..152 FT /evidence="ECO:0007829|PDB:9UT3" FT STRAND 153..155 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 156..167 FT /evidence="ECO:0007829|PDB:9UT3" FT TURN 177..179 FT /evidence="ECO:0007829|PDB:9NN2" FT HELIX 185..194 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 199..220 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 222..225 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 228..235 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 239..245 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 246..252 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 253..256 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 259..262 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 265..274 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 279..282 FT /evidence="ECO:0007829|PDB:9VLQ" FT STRAND 284..286 FT /evidence="ECO:0007829|PDB:9UT5" FT HELIX 288..290 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 294..302 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 305..307 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 310..313 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 315..343 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 348..362 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 365..375 FT /evidence="ECO:0007829|PDB:9UT3" FT STRAND 377..381 FT /evidence="ECO:0007829|PDB:9NEE" FT HELIX 382..384 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 387..390 FT /evidence="ECO:0007829|PDB:9NEL" FT HELIX 392..396 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 397..401 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 402..407 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 410..417 FT /evidence="ECO:0007829|PDB:9NEB" FT STRAND 419..425 FT /evidence="ECO:0007829|PDB:9NEB" FT HELIX 428..437 FT /evidence="ECO:0007829|PDB:9NEB" FT HELIX 441..444 FT /evidence="ECO:0007829|PDB:9NEB" FT STRAND 452..456 FT /evidence="ECO:0007829|PDB:9NEB" FT HELIX 457..470 FT /evidence="ECO:0007829|PDB:9NEB" FT HELIX 472..474 FT /evidence="ECO:0007829|PDB:9UT4" FT HELIX 476..479 FT /evidence="ECO:0007829|PDB:9UT4" FT HELIX 506..509 FT /evidence="ECO:0007829|PDB:9NEB" FT STRAND 513..516 FT /evidence="ECO:0007829|PDB:9NNP" FT HELIX 521..524 FT /evidence="ECO:0007829|PDB:9NDA" FT STRAND 535..539 FT /evidence="ECO:0007829|PDB:9NEB" FT STRAND 541..543 FT /evidence="ECO:0007829|PDB:9NDA" FT STRAND 545..551 FT /evidence="ECO:0007829|PDB:9NEB" FT HELIX 555..559 FT /evidence="ECO:0007829|PDB:9NEB" FT HELIX 560..562 FT /evidence="ECO:0007829|PDB:9NEB" FT HELIX 566..570 FT /evidence="ECO:0007829|PDB:9NDA" FT HELIX 579..589 FT /evidence="ECO:0007829|PDB:9NEB" FT HELIX 604..610 FT /evidence="ECO:0007829|PDB:9NEB" FT STRAND 613..615 FT /evidence="ECO:0007829|PDB:9NEB" FT STRAND 620..622 FT /evidence="ECO:0007829|PDB:9UT7" FT STRAND 624..630 FT /evidence="ECO:0007829|PDB:9NEB" FT HELIX 639..660 FT /evidence="ECO:0007829|PDB:9NEB" FT TURN 668..670 FT /evidence="ECO:0007829|PDB:9NEB" FT STRAND 674..677 FT /evidence="ECO:0007829|PDB:9NEB" FT STRAND 757..759 FT /evidence="ECO:0007829|PDB:9VLQ" FT STRAND 761..767 FT /evidence="ECO:0007829|PDB:9NEB" FT STRAND 772..774 FT /evidence="ECO:0007829|PDB:9NEB" FT HELIX 777..792 FT /evidence="ECO:0007829|PDB:9NEB" FT HELIX 797..800 FT /evidence="ECO:0007829|PDB:9NDA" FT TURN 802..804 FT /evidence="ECO:0007829|PDB:9NDA" FT STRAND 805..808 FT /evidence="ECO:0007829|PDB:9UT7" FT HELIX 814..816 FT /evidence="ECO:0007829|PDB:9UT4" FT STRAND 821..823 FT /evidence="ECO:0007829|PDB:9NEB" FT STRAND 832..835 FT /evidence="ECO:0007829|PDB:9NN2" FT STRAND 841..843 FT /evidence="ECO:0007829|PDB:9NEB" FT HELIX 854..859 FT /evidence="ECO:0007829|PDB:9NEB" FT HELIX 863..865 FT /evidence="ECO:0007829|PDB:9NEB" FT STRAND 874..876 FT /evidence="ECO:0007829|PDB:9UT5" FT STRAND 881..888 FT /evidence="ECO:0007829|PDB:9NEB" FT HELIX 894..907 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 913..919 FT /evidence="ECO:0007829|PDB:9UT3" FT TURN 925..927 FT /evidence="ECO:0007829|PDB:9NN2" FT HELIX 929..948 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 950..955 FT /evidence="ECO:0007829|PDB:9UT3" FT STRAND 956..967 FT /evidence="ECO:0007829|PDB:9UT3" FT STRAND 970..977 FT /evidence="ECO:0007829|PDB:9UT3" FT STRAND 982..985 FT /evidence="ECO:0007829|PDB:9NN2" FT STRAND 989..991 FT /evidence="ECO:0007829|PDB:9UT3" FT STRAND 994..997 FT /evidence="ECO:0007829|PDB:9NN2" FT STRAND 1001..1009 FT /evidence="ECO:0007829|PDB:9UT3" FT HELIX 1011..1013 FT /evidence="ECO:0007829|PDB:9UT3" FT STRAND 1015..1023 FT /evidence="ECO:0007829|PDB:9UT3" FT STRAND 1025..1028 FT /evidence="ECO:0007829|PDB:9UT3" FT STRAND 1030..1032 FT /evidence="ECO:0007829|PDB:9NQP" FT STRAND 1034..1040 FT /evidence="ECO:0007829|PDB:9UT3" SQ SEQUENCE 1058 AA; 114424 MW; CB39341C31B768B4 CRC64; MGQEDGNRGE RRAAGTPVEV TALYATDGCV ITSSIALLTN SLLGAEPVYI FSYDAYTHDG RADGPTEQDR FEESRALYQA SGGLNGDSFR VTFCLLGTEV GGTHQARGRT RPMFVCRFER ADDVAALQDA LAHGTPLQPD HIAATLDAEA TFALHANMIL ALTVAINNAS PRTGRDAAAA QYDQGASLRS LVGRTSLGQR GLTTLYVHHE VRVLAAYRRA YYGSAQSPFW FLSKFGPDEK SLVLTTRYYL LQAQRLGGAG ATYDLQAIKD ICATYAIPHA PRPDTVSAAS LTSFAAITRF CCTSQYARGA AAAGFPLYVE RRIAADVRET SALEKFITHD RSCLRVSDRE FITYIYLAHF ECFSPPRLAT HLRAVTTHDP NPAASTEQPS PLGREAVEQF FCHVRAQLNI GEYVKHNVTP RETVLDGDTA KAYLRARTYA PGALTPAPAY CGAVDSATKM MGRLADAEKL LVPRGWPAFA PASPGEDTAG GTPPPQTCGI VKRLLRLAAT EQQGPTPPAI AALIRNAAVQ TPLPVYRISM VPTGQAFAAL AWDDWARITR DARLAEAVVS AEAAAHPDHG ALGRRLTDRI RAQGPVMPPG GLDAGGQMYV NRNEIFNGAL AITNIILDLD IALKEPVPFR RLHEALGHFR RGALAAVQLL FPAARVDPDA YPCYFFKSAC RPGPASVGSG SGLGNDDDGD WFPCYDDAGD EEWAEDPGAM DTSHDPPDDE VAYFDLCHEV GPTAEPRETD SPVCSCTDKI GLRVCMPVPA PYVVHGSLTM RGVARVIQQA VLLDRDFVEA IGSYVKNFLL IDTGVYAHGH SLRLPYFAKI APDGPACGRL LPVFVIPPAC KDVPAFVAAH ADPRRFHFHA PPTYLASPRE IRVLHSLGGD YVSFFERKAS RNALEHFGRR ETLTEVLGRY NVQPDAGGTV EGFASELLGR IVACIETHFP EHAGEYQAVS VRRAVSKDDW VLLQLVPVRG TLQQSLSCLR FKHGRASRAT ARTFVALSVG ANNRLCVSLC QQCFAAKCDS NRLHTLFTID AGTPCSPSVP CSTSQPSS //