ID W8QF60_9VIRU Unreviewed; 637 AA.
AC W8QF60;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 13-SEP-2023, entry version 34.
DE RecName: Full=DNA ligase (NAD(+)) {ECO:0000256|ARBA:ARBA00012722};
DE EC=6.5.1.2 {ECO:0000256|ARBA:ARBA00012722};
GN ORFNames=AMIV_120 {ECO:0000313|EMBL:AHL67609.1};
OS Anopheles minimus iridovirus.
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Pimascovirales; Iridoviridae; Betairidovirinae; Chloriridovirus.
OX NCBI_TaxID=1465751 {ECO:0000313|EMBL:AHL67609.1, ECO:0000313|Proteomes:UP000110868};
RN [1] {ECO:0000313|EMBL:AHL67609.1, ECO:0000313|Proteomes:UP000110868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMIV {ECO:0000313|EMBL:AHL67609.1};
RA Tong Y., Zhang J., Huang Y., Li S., Pei G., Zhang Z., Mi Z., An X.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00034005};
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DR EMBL; KF938901; AHL67609.1; -; Genomic_DNA.
DR RefSeq; YP_009021193.1; NC_023848.1.
DR GeneID; 18938281; -.
DR KEGG; vg:18938281; -.
DR OrthoDB; 2744at10239; -.
DR Proteomes; UP000110868; Genome.
DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR Gene3D; 1.10.287.610; Helix hairpin bin; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR001679; DNA_ligase.
DR InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
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; 1.
DR Pfam; PF03120; DNA_ligase_OB; 1.
DR Pfam; PF14520; HHH_5; 1.
DR PIRSF; PIRSF001604; LigA; 1.
DR SMART; SM00532; LIGANc; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF47794; Rad51 N-terminal domain-like; 1.
PE 4: Predicted;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AHL67609.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000110868}.
FT DOMAIN 8..410
FT /note="NAD-dependent DNA ligase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00532"
SQ SEQUENCE 637 AA; 70892 MW; 927B5C3DC2B2448B CRC64;
MKNKDPKNFI NKMDKLIQLK KRADQAYFNT DCPIMDDGEY DALVQTLKTE YNYVDQESVG
AHPTHNKAQL PVWMGSLTKH TTSKEIANFL NKLLMIERFS VQEKLDGISC LFVQDETGRT
KLYTRGNGST GSDISHLLAC GIQIPRIKEK VMVRGELVMS RKTFETKYSS QFSNPRNLVS
GLVCAKQQQR DNSLSDIKFI AYELISSTEI QMPVSEQLVR LGELGFEVVY HRSLKRKYIF
NECLMDYLTR RKRKSIYQID GLVIVCDDMK YVRNVADNPK YAFAFKNRAE NVAEAVVEKV
VWNLSKSGRY KPQICIVPVV LDSVTISRAT GHNAKFVVDN KIGRGAKLLI TRSGNVIPHV
LSVLEHSTEP LSLPANSQWV SVDLCHVGEG ETPDEVVIKQ MVHFCKKINA VNCKEKTISK
IYNAGFKTIE AIVSATAQDL QKIGSIGQTL AQKLVDSIQK GVRESTTKEL LAALNAFGDG
IGLRKIANLD LSDPRKETKG LSRQTVDAKI IPVLGAQLAR VNNLKTLAGC ASTAEQPALK
KTGADKIFVF TGFRDPSLEK QIATRLGKVN TSISKKTHTL VVDDKALSKP PSSKMLKAQS
LGINVITRKQ LCDLLDQTLA GLSCEFENEY ASSDEEC
//
