VF205_IIV3
ID VF205_IIV3 Reviewed; 756 AA.
AC Q197A8;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Putative DNA ligase 052L;
DE EC=6.5.1.2;
GN ORFNames=IIV3-052L;
OS Invertebrate iridescent virus 3 (IIV-3) (Mosquito iridescent virus).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Pimascovirales; Iridoviridae; Betairidovirinae; Chloriridovirus.
OX NCBI_TaxID=345201;
OH NCBI_TaxID=7163; Aedes vexans (Inland floodwater mosquito) (Culex vexans).
OH NCBI_TaxID=42431; Culex territans.
OH NCBI_TaxID=332058; Culiseta annulata.
OH NCBI_TaxID=310513; Ochlerotatus sollicitans (eastern saltmarsh mosquito).
OH NCBI_TaxID=329105; Ochlerotatus taeniorhynchus (Black salt marsh mosquito) (Aedes taeniorhynchus).
OH NCBI_TaxID=7183; Psorophora ferox.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16912294; DOI=10.1128/jvi.00464-06;
RA Delhon G., Tulman E.R., Afonso C.L., Lu Z., Becnel J.J., Moser B.A.,
RA Kutish G.F., Rock D.L.;
RT "Genome of invertebrate iridescent virus type 3 (mosquito iridescent
RT virus).";
RL J. Virol. 80:8439-8449(2006).
CC -!- FUNCTION: Catalyzes the formation of phosphodiester linkages between
CC 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD
CC as a coenzyme and as the energy source for the reaction. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-
CC nicotinamide D-nucleotide.; EC=6.5.1.2;
CC -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family.
CC {ECO:0000305}.
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DR EMBL; DQ643392; ABF82082.1; -; Genomic_DNA.
DR RefSeq; YP_654624.1; NC_008187.1.
DR SMR; Q197A8; -.
DR PRIDE; Q197A8; -.
DR GeneID; 4156302; -.
DR KEGG; vg:4156302; -.
DR Proteomes; UP000001358; Genome.
DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR013839; DNAligase_adenylation.
DR InterPro; IPR013840; DNAligase_N.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004150; NAD_DNA_ligase_OB.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF01653; DNA_ligase_aden; 2.
DR Pfam; PF03120; DNA_ligase_OB; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00532; LIGANc; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 3: Inferred from homology;
KW DNA replication; Ligase; NAD; Reference proteome.
FT CHAIN 1..756
FT /note="Putative DNA ligase 052L"
FT /id="PRO_0000376961"
FT DOMAIN 648..742
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 610..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 103
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 756 AA; 85509 MW; E1FEA7C5C4EE89F5 CRC64;
MYDPQFEKYN QLLKLKEKAD KAYYNGVGDP IMSDEEYDNL VDYMDELNPD GGVKTKVGAS
PSRSKSVKLP MPMNSLDKIK TQHEFDNWMK NWKPKAMLLV KEKLDGVSCL AVFTLEQNKP
PKIELFTRGD GTTGTNITRL LNHGLKVGND YCFDDMVNED KWTTDWGCYL NAEAIDHWKK
LPVKKVYIRG ELIVTRKNFQ TWYSNRFMNA RNLVSGQVNK KSPDPKILQD IDFVPYDLVI
DLKRPTMTHE VEHLLFRMIG ATPVYTRFLF LSDTISTESM ADYLERRKEK SDYEIDGLVI
QVDDDTLFAP PDNRNPKDTV AFKIMGTTAR TTVTHVEWNL SKGSKYKPTI HITPVSLSGV
TISKVTGFHG KYISENKIGK GAVVLITRSG EVIPHIVSVI SPAAKQDVLL PSNGVWKGVD
IYYDGAEEPR EITVKKMVHF FTSLGCLGLK TMTVGRLYDA GYRTVEAIVG ADTKKLVLIN
GFRMVAQKLL PSMWVNVAKA TPHELMAALN AFGEGIGLRK IQNIDCSKPE ALEVIGMTKK
TVETRIWPIW NDVLARVNAL SRMAKSQLRK QETGSCEPEE DDDYNFGSYH PCHMPCQSSN
KIWECRSRSP SAAGSASPCR PTKRRDDWFD SSESSCATET CVVESPPKKR PPMQGYVFVF
TRFRDKDLER QITALGGKVL NNVNQNVTHV ITKEKGPYKK PYTGKLKFAL DNNLFVWSLV
HLKSIVADEQ EKLKRQRKCR ARSPSPCGTA CSTERD