ID A0A0Q7T8Z0_9BACL Unreviewed; 319 AA.
AC A0A0Q7T8Z0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN ORFNames=ASD24_23445 {ECO:0000313|EMBL:KQY91687.1};
OS Paenibacillus sp. Root52.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736552 {ECO:0000313|EMBL:KQY91687.1, ECO:0000313|Proteomes:UP000051734};
RN [1] {ECO:0000313|Proteomes:UP000051734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root52 {ECO:0000313|Proteomes:UP000051734};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY91687.1, ECO:0000313|Proteomes:UP000051734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root52 {ECO:0000313|EMBL:KQY91687.1,
RC ECO:0000313|Proteomes:UP000051734};
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 -!- 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:KQY91687.1}.
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DR EMBL; LMFO01000005; KQY91687.1; -; Genomic_DNA.
DR RefSeq; WP_056694336.1; NZ_LMFO01000005.1.
DR AlphaFoldDB; A0A0Q7T8Z0; -.
DR STRING; 1736552.ASD24_23445; -.
DR OrthoDB; 9802472at2; -.
DR Proteomes; UP000051734; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR CDD; cd07906; Adenylation_DNA_ligase_LigD_LigC; 1.
DR CDD; cd07971; OBF_DNA_ligase_LigD; 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; IPR012309; DNA_ligase_ATP-dep_C.
DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR45674:SF15; DNA LIGASE (ATP); 1.
DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR Pfam; PF04679; DNA_ligase_A_C; 1.
DR Pfam; PF01068; DNA_ligase_A_M; 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 4: Predicted;
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KQY91687.1}.
FT DOMAIN 106..196
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 319 AA; 36367 MW; CC5E1A048BD869ED CRC64;
MFTPIIPFEP ISSLTLPTGS NWIAQIKWDG VRMLAYEDGQ ELRLINRRQH ERTAQYPELA
LSRNICSAPS YIVDGEIIAL DPDTGKPSFY HVLRRDRMSK PDAIAQAVQH IPITYMVFDI
LYYDGKWVTD QPLAQRQQLL HQVLTPSSHV QEVTNMSDPA ALLTVMRQHQ MEGIVIKDLA
STYGIRAKDA RWQKVKIMHD LYAMIGGVTF RSGIVNAIAV GVYDGSHFIY IGHVGTGRLN
SDTWRKLTAD IQPLIRQTNP FHNIPERSAE TTWIEPQIGV KVQYMELTHH RTLRHPSIQT
FAEVTQEDCP ASQLIQEEQ
//