ID A0A1W6DX16_9CAUD Unreviewed; 716 AA.
AC A0A1W6DX16;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA ligase (NAD(+)) {ECO:0000256|ARBA:ARBA00012722};
DE EC=6.5.1.2 {ECO:0000256|ARBA:ARBA00012722};
GN Name=ligA {ECO:0000313|EMBL:ARK07429.1};
GN ORFNames=LAV_00029 {ECO:0000313|EMBL:ARK07429.1};
OS Sphingobium phage Lacusarx.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Lacusarxvirus; Lacusarxvirus lacusarx.
OX NCBI_TaxID=1980139 {ECO:0000313|EMBL:ARK07429.1, ECO:0000313|Proteomes:UP000223906};
RN [1] {ECO:0000313|EMBL:ARK07429.1, ECO:0000313|Proteomes:UP000223906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Nielsen T.K., Carstens A.B., Kot W., Lametsch R., Neve H., Hansen L.H.;
RT "The first characterized phage against a member of the ecologically
RT important #sphingomonads reveals high dissimilarity against all other known
RT phages.";
RL Submitted (FEB-2017) 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};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; KY629563; ARK07429.1; -; Genomic_DNA.
DR OrthoDB; 10441at10239; -.
DR Proteomes; UP000223906; Genome.
DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd17748; BRCT_DNA_ligase_like; 1.
DR CDD; cd00114; LIGANc; 1.
DR Gene3D; 6.20.10.30; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
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 HAMAP; MF_01588; DNA_ligase_A; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR041663; DisA/LigA_HHH.
DR InterPro; IPR001679; DNA_ligase.
DR InterPro; IPR018239; DNA_ligase_AS.
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 InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR004149; Znf_DNAligase_C4.
DR NCBIfam; TIGR00575; dnlj; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF01653; DNA_ligase_aden; 1.
DR Pfam; PF03120; DNA_ligase_OB; 1.
DR Pfam; PF03119; DNA_ligase_ZBD; 1.
DR Pfam; PF12826; HHH_2; 1.
DR PIRSF; PIRSF001604; LigA; 1.
DR SMART; SM00292; BRCT; 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; SSF47781; RuvA domain 2-like; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS01055; DNA_LIGASE_N1; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ARK07429.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000223906};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 625..704
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
SQ SEQUENCE 716 AA; 78342 MW; A031102F47B797B5 CRC64;
MDADLLAAYT YNTMVRTDAD DDARNRHREL IHDLAAADVA YYEHDEPFMS DERYDDLKRE
LASIEADYPV LATPASPTQK VSGKASDRFA KVKHRQAMLS LDNSLTTEAL IKWVDNLQRG
DGSDDILAEL KMDGLSLSVT YENGKLVRAA TRGDGQIGED VTEQAKQITD LPNTIQFKGF
LEVRGECYMP RSVFAWLNED LDTKGKKKLV NCRNAAAGAL RQKDPAVTKA RRLKFMAFGV
TDESLPEYDS DIGILGILYV QGFSVVPHEL LARGKTGLHP RRIEALRASY DFDIDGIVFK
IDSRAARQAY GFTSRAPRWA TAYKFPAERK TTRLKEIVVQ TGRTGALTPV GVLEPIFVGG
VTVSSVTLHN EDEISRLHLV PGATVIVQRA GDVIPQVVGV DPNAPVVKGI YSFPTTCPSC
GGPTERPVGE AVRRCVSGFS CPAQVQGYLE HFVSRDAMNI DGLGPSQIED LIKYLGLSKA
SQIMELPDLY ISHFVPEAGR EFADAEVWFA MQSWEGYGKS SVAKLMSAIK KARSPELGRF
IYALGIRNVG ETTAKDIAKH LKTASAFFDC ITYENGFVDA GVGDIDGIGP VVMAALDGHF
SIEANYKEAF ALRRVLDIQD LKLASGPAIF EGEVICFTGS MTRWSRDQAI LIAEDLGAKT
TNSAAKKTTI LVAGANVGAK KIEAAEKFGC KVLDEAWFIA EVEKAMADGY KLDVMD
//
