ID T1AZI6_9ZZZZ Unreviewed; 461 AA.
AC T1AZI6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA ligase (NAD(+)) {ECO:0000256|ARBA:ARBA00012722};
DE EC=6.5.1.2 {ECO:0000256|ARBA:ARBA00012722};
DE Flags: Fragment;
GN ORFNames=B1A_09363 {ECO:0000313|EMBL:EQD62972.1};
OS mine drainage metagenome.
OC unclassified sequences; metagenomes; ecological metagenomes.
OX NCBI_TaxID=410659 {ECO:0000313|EMBL:EQD62972.1};
RN [1] {ECO:0000313|EMBL:EQD62972.1}
RP NUCLEOTIDE SEQUENCE.
RA Mendez C., Richter M., Ferrer M., Sanchez J.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EQD62972.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24430486; DOI=10.1038/ismej.2013.242;
RA Mendez-Garcia C., Mesa V., Sprenger R.R., Richter M., Diez M.S., Solano J.,
RA Bargiela R., Golyshina O.V., Manteca A., Ramos J.L., Gallego J.R.,
RA Llorente I., Martins Dos Santos V.A., Jensen O.N., Pelaez A.I., Sanchez J.,
RA Ferrer M.;
RT "Microbial stratification in low pH oxic and suboxic macroscopic growths
RT along an acid mine drainage.";
RL ISME J. 8:1259-1274(2014).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EQD62972.1}.
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DR EMBL; AUZX01006667; EQD62972.1; -; Genomic_DNA.
DR AlphaFoldDB; T1AZI6; -.
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 Gene3D; 6.20.10.30; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_01588; DNA_ligase_A; 1.
DR InterPro; IPR041663; DisA/LigA_HHH.
DR InterPro; IPR001679; DNA_ligase.
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 PANTHER; PTHR23389; CHROMOSOME TRANSMISSION FIDELITY FACTOR 18; 1.
DR PANTHER; PTHR23389:SF9; DNA LIGASE; 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 SMART; SM00532; LIGANc; 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.
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:EQD62972.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..310
FT /note="NAD-dependent DNA ligase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00532"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EQD62972.1"
FT NON_TER 461
FT /evidence="ECO:0000313|EMBL:EQD62972.1"
SQ SEQUENCE 461 AA; 49649 MW; C33E0FFC02132C3D CRC64;
GSVGEDVTAN LRTLRAIPLR LRGAAPDVLE VRGEVIMPRA GFDAFNARAL AAGEKLLANP
RNGAAGSLRQ LDPRVTARRP LAFFAYGIGV IEPASLLPPT HSTTLQWLRT LGFPVAPEIA
TAQGFAGLIA YYRRIGTARD RLPYGIDGVV YKLDRYVDQQ ALGYVARAPR WAIAHKFPAE
EQMTVLEAID VQIGRTGAAT PVARLAPVQV AGVTVTNATL HNADQIERLD VRVGDTVIVR
RAGDVIPEVV RVVAERRPPR TRPWRMPTHC PVCGAQLLRE EGASAWRCSG GLSCAAQRRE
AILHFAARRA MDIDGLGERY IEDLIAFDYV HAPADLYRFT RDDLLAMKRK ADARDGTTPE
TVKQGKIATL WAENLLAAIA ASTRPTLARL LFALGIMHIG EETAKTLADA LGSLDRVRRA
PALALQCLPD IGHAVADSIA TFFAQPGNAA AVDALLAAGV A
//
