D5_FOWPN
ID D5_FOWPN Reviewed; 791 AA.
AC P21969; Q9J5F1;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Primase D5;
DE EC=3.6.4.-;
GN OrderedLocusNames=FPV058; ORFNames=FPD5;
OS Fowlpox virus (strain NVSL) (FPV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Avipoxvirus.
OX NCBI_TaxID=928301;
OH NCBI_TaxID=7742; Vertebrata.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FP-1;
RX PubMed=2165135; DOI=10.1099/0022-1317-71-7-1517;
RA Tartaglia J., Winslow J., Goebel S.J., Johnson G.P., Taylor J.,
RA Paoletti E.;
RT "Nucleotide sequence analysis of a 10.5 kbp HindIII fragment of fowlpox
RT virus: relatedness to the central portion of the vaccinia virus HindIII D
RT region.";
RL J. Gen. Virol. 71:1517-1524(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10729156; DOI=10.1128/jvi.74.8.3815-3831.2000;
RA Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L.;
RT "The genome of fowlpox virus.";
RL J. Virol. 74:3815-3831(2000).
CC -!- FUNCTION: Primase which may have roles in initiation of DNA replication
CC or lagging-strand synthesis. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with A20. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the poxviridae D5 family. {ECO:0000305}.
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DR EMBL; X17202; CAA35068.1; -; Genomic_DNA.
DR EMBL; AF198100; AAF44402.1; -; Genomic_DNA.
DR PIR; E35216; E35216.
DR RefSeq; NP_039021.1; NC_002188.1.
DR PRIDE; P21969; -.
DR GeneID; 1486606; -.
DR KEGG; vg:1486606; -.
DR Proteomes; UP000008597; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004968; DNA_primase/NTPase_C.
DR InterPro; IPR014015; Helicase_SF3_DNA-vir.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014818; Phage/plasmid_primase_P4_C.
DR Pfam; PF08706; D5_N; 1.
DR Pfam; PF03288; Pox_D5; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51206; SF3_HELICASE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA replication; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..791
FT /note="Primase D5"
FT /id="PRO_0000099442"
FT DOMAIN 479..641
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT REGION 346..471
FT /note="Primase"
FT /evidence="ECO:0000250"
FT ACT_SITE 174
FT /evidence="ECO:0000255"
FT BINDING 505..512
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT CONFLICT 565
FT /note="C -> Y (in Ref. 1; CAA35068)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 791 AA; 92595 MW; 349147DB081A4FF1 CRC64;
MALSVIRNNH IIFVLKQIGV RTKHRENNNS KYVESFTCDE LERYIYSNPD CTLFETLKDE
EYYSNVRVFF DVDMDGRLDD KYQATHNFVN IITKFVADYA YNDCKMISNH RDKDKMITDM
KSNFSITEST DKEKTSFHLI FFNCYTTLDT LINMRKKLIV LTKESNNRLV KAIDTSVYRH
KPSLRIVGTK KDSINIHVHK KTKQNIHFKN YLFTYVDYNE EDCYYFVSEQ QHQSPDLLNW
KEEYIPFHDA IKKISKAIGN SIINLKDITA ENFTVTPLDI YYATPCNLCK KVSHKHPHHL
LISNDCIRIY KSGNPNSCKI KTISLEGNKL FSISQQIIDL NVINVSDRGE YLVWLKNVWR
MCEDDNNITK LILYMRDHLS SDCTDLLLCP RNRKVIEHNL KDMLIDTIET DTYPEKLQFL
NGVYDIKDSI FYQGNDAKKF VCTVSTGYKY EEGINVDDIT TELMSILDDI QPKTKENFEN
RELYEQILSS CLMGTTKQCI FFFYGETATG KSTTKKLLKS VMHNMFLETG QVILTEQMDK
GPNPFIANMH LKRVVFCSEL PDFSCNTSKK IRSDNIKKLT EPCVVGRSCY SNKINNRNHA
TIIIDTNYKP VFDKVDNAIM RRIALVNFKT HFTNTKKKVH NSKYDFIKPL NESLDSKIQS
NYFRYAFLKI LLGWFSKYHV PNLRILPTPD KIPDFKFRLK VESLIIPSNS THVKYVDKLM
KLGYITDDDG IPVLQLNIFQ QKLSLHFNVK LYGQDIDSFI MKNKKYMNLA DEYMSFIFIE
DLNTINEPRN T