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Database: UniProt
Entry: A0A3N0DVX4_9ACTN
LinkDB: A0A3N0DVX4_9ACTN
Original site: A0A3N0DVX4_9ACTN 
ID   A0A3N0DVX4_9ACTN        Unreviewed;       500 AA.
AC   A0A3N0DVX4;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=EFL95_11395 {ECO:0000313|EMBL:RNL79573.1};
OS   Nocardioides marmorisolisilvae.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1542737 {ECO:0000313|EMBL:RNL79573.1, ECO:0000313|Proteomes:UP000277094};
RN   [1] {ECO:0000313|EMBL:RNL79573.1, ECO:0000313|Proteomes:UP000277094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIS18-7 {ECO:0000313|EMBL:RNL79573.1,
RC   ECO:0000313|Proteomes:UP000277094};
RA   Li F.;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC         diphosphate.; EC=6.5.1.1; Evidence={ECO:0000256|ARBA:ARBA00034003,
CC         ECO:0000256|RuleBase:RU000617};
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|RuleBase:RU004196}.
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:RNL79573.1}.
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DR   EMBL; RJSG01000002; RNL79573.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N0DVX4; -.
DR   OrthoDB; 3733803at2; -.
DR   Proteomes; UP000277094; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; 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; cd07901; Adenylation_DNA_ligase_Arch_LigB; 1.
DR   CDD; cd07972; OBF_DNA_ligase_Arch_LigB; 1.
DR   Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR000977; DNA_ligase_ATP-dep.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   NCBIfam; TIGR00574; dnl1; 1.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR45674:SF13; DNA LIGASE-RELATED; 1.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000617};
KW   DNA damage {ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|RuleBase:RU000617};
KW   DNA repair {ECO:0000256|RuleBase:RU000617};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000277094}.
FT   DOMAIN          291..405
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   500 AA;  53508 MW;  A38CA03F393D5B2C CRC64;
     MHLADLARVS TAVAATRSRL EKRALIADLL SAAPADEIDL VATYLSGTLR QRRTGVGWRG
     LADLPPPARV ASVGLLEIDA ALEQIAAFSG MGSSLARKRA VHDLFAALTD AEQDLLRALM
     TGGVRQGALD SVMLDAIAAA ADVPLAVVRR AAMFSAPTGP IAVAAMTGGV DALAAFDLVV
     GRPVRPMLAS SAPSVPEAVA ALGDAVVVDT KLDGIRIQVH KQGEEVLVFT RSLDEISERL
     PGVVTVVRAL PADGLILDGE ALLVAEDGRP RPFQETASET ASQGGTLARP YFFDLLAVGG
     EALIERPGHE RWSRLDEIVP TAFRTERIAT DDTATATRFF DEAVAGGQEG VIVKDPTAPY
     EAGRRGAAWV KVKPRHTLDL VVLGVEWGSG RRRGTLSNIH LGARDPETGD FVMLGKTFKG
     MTDEMLAWQT ERFTELKVSD DGWVVTVRPE QVVEIAFDGV QRSTRYPGGV ALRFARVLRY
     RDDKTPAEAD TLEAVRRFLA
//
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