ID A0A0Q6VLZ5_9ACTN Unreviewed; 502 AA.
AC A0A0Q6VLZ5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=ASC61_00535 {ECO:0000313|EMBL:KQV73624.1};
OS Aeromicrobium sp. Root344.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=1736521 {ECO:0000313|EMBL:KQV73624.1, ECO:0000313|Proteomes:UP000051702};
RN [1] {ECO:0000313|EMBL:KQV73624.1, ECO:0000313|Proteomes:UP000051702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root344 {ECO:0000313|EMBL:KQV73624.1,
RC ECO:0000313|Proteomes:UP000051702};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV73624.1, ECO:0000313|Proteomes:UP000051702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root344 {ECO:0000313|EMBL:KQV73624.1,
RC ECO:0000313|Proteomes:UP000051702};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQV73624.1}.
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DR EMBL; LMDH01000001; KQV73624.1; -; Genomic_DNA.
DR RefSeq; WP_056207841.1; NZ_LMDH01000001.1.
DR AlphaFoldDB; A0A0Q6VLZ5; -.
DR STRING; 1736521.ASC61_00535; -.
DR OrthoDB; 3733803at2; -.
DR Proteomes; UP000051702; 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; IPR012308; DNA_ligase_ATP-dep_N.
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 Pfam; PF04675; DNA_ligase_A_N; 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; 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:UP000051702}.
FT DOMAIN 297..409
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 502 AA; 53375 MW; CCDAF016F2D3FA73 CRC64;
MLLADVVATS TAVAATRSRN AKATAIADLL GRVADEGADV IPVVTSYLSG VLRQRRTGLG
WRSLQDLPEP ADTATLDVAE VDAEFERIAA LAGAGSQVAR TEATRSLFAR ATADEQRWLR
GIVTGEVRQG ALDSLVQEGL AIAGGIPVAA VRRAAMMAGS TVDVAVAALI EGVGALALFT
LQVGRPVLPM LASTAPTVEA AMAKAGGGEV AIDTKLDGIR VQVHRQGDDV LVVTRSLDDV
TDRHPDLVAL ARTLPCRDIV LDGEVLALGP DGRPRPFQET ASRTTAAGKV VLTPAFFDVL
HLDGRDLVDA PTADRLAALE SVVPEAYRVR RIVTADPAEA EAFAAEVLAS GHEGVVVKSL
TATYAAGRRG ANWVKVKPVH TLDLVVLAVE RGSGRRSGWL SNIHLGARDG DTYVMLGKTF
KGMTDEILAW QTERFRELQN DDDGYVVTVR PEQVVEIAFD GVQRSTRYPG GVALRFARVI
RYRDDKPAAE ADTIETVRAF LS
//
