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Database: UniProt/TrEMBL
Entry: A0A0X8CNJ7_9BRAD
LinkDB: A0A0X8CNJ7_9BRAD
Original site: A0A0X8CNJ7_9BRAD 
ID   A0A0X8CNJ7_9BRAD        Unreviewed;       553 AA.
AC   A0A0X8CNJ7;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   ORFNames=BCCGELA001_33925 {ECO:0000313|EMBL:AMA60718.1};
OS   Bradyrhizobium sp. CCGE-LA001.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1223566 {ECO:0000313|EMBL:AMA60718.1, ECO:0000313|Proteomes:UP000019052};
RN   [1] {ECO:0000313|EMBL:AMA60718.1, ECO:0000313|Proteomes:UP000019052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCGE-LA001 {ECO:0000313|EMBL:AMA60718.1,
RC   ECO:0000313|Proteomes:UP000019052};
RX   PubMed=24952318; DOI=10.1016/j.ympev.2014.06.006;
RA   Servin-Garciduenas L.E., Zayas-Del Moral A., Ormeno-Orrillo E., Rogel M.A.,
RA   Delgado-Salinas A., Sanchez F., Martinez-Romero E.;
RT   "Symbiont shift towards Rhizobium nodulation in a group of phylogenetically
RT   related Phaseolus species.";
RL   Mol. Phylogenet. Evol. 79:1-11(2014).
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};
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DR   EMBL; CP013949; AMA60718.1; -; Genomic_DNA.
DR   RefSeq; WP_060737293.1; NZ_CP013949.1.
DR   AlphaFoldDB; A0A0X8CNJ7; -.
DR   STRING; 1223566.BCCGELA001_33925; -.
DR   KEGG; brc:BCCGELA001_33925; -.
DR   Proteomes; UP000019052; Chromosome.
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:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd07897; Adenylation_DNA_ligase_Bac1; 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; IPR026333; ATP_dep_DNA_lig_pp_1105_fam.
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; TIGR04120; DNA_lig_bact; 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; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AMA60718.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          307..444
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   553 AA;  62269 MW;  B731515712397674 CRC64;
     MNRFAELLDR LAYEPGRNNK LRLITGYFRE VADPDRGYAL AALTGALSFK HAKPALIRDL
     IAARTDEVLF GLSYDYVGDL SETVALMWPK APLAAHNNPP PPSLTEVVTT LRTLGKTELP
     KQLERWLDEL DETGRWALLK LVTGALRIGI SARLAKTAAA ALGDKDPHEV ELIWPGLAPP
     YLDLFAWLEG RGDKPVNRDP APFRPVMLAH AIEDTDFASL DPADYIAEWK WDGIRVQAVA
     GRDERGHITA RLYSRTGEDI TGSFPDLVPS LRLPGAIDGE LLILREGRVQ SFNVLQQRLN
     RKVVSPKLIK EFPIHLRAYD LLGDDQNDLR ELPFAERRER LETFIAKLDD PRIDLSTTVP
     FASWEALTAA RADPASAGAG EDADAVEGVM LKRRDAPYLP GRPKGQWWKW KRDPHIIDAV
     LMYAQRGHGK RSSYYSDYTF GVWTGGDGGD ELVPVGKAYF GFTDEELLQI DRFVRRNTTE
     KFGPVRHVVH EPDKGLVLEV AFEGLQRSPR HKSGVAMRFP RISRLRWDKP PREADRLETL
     ERMLKAEPAE VEM
//
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