ID H0FYB9_RHIML Unreviewed; 348 AA.
AC H0FYB9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN ORFNames=SM0020_10975 {ECO:0000313|EMBL:EHK77973.1};
OS Sinorhizobium meliloti CCNWSX0020.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=1107881 {ECO:0000313|EMBL:EHK77973.1, ECO:0000313|Proteomes:UP000004038};
RN [1] {ECO:0000313|EMBL:EHK77973.1, ECO:0000313|Proteomes:UP000004038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCNWSX0020 {ECO:0000313|EMBL:EHK77973.1,
RC ECO:0000313|Proteomes:UP000004038};
RX PubMed=22328762; DOI=10.1128/JB.06682-11;
RA Li Z., Ma Z., Hao X., Wei G.;
RT "Draft Genome Sequence of Sinorhizobium meliloti CCNWSX0020, a Nitrogen-
RT Fixing Symbiont with Copper Tolerance Capability Isolated from Lead-Zinc
RT Mine Tailings.";
RL J. Bacteriol. 194:1267-1268(2012).
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; AGVV01000016; EHK77973.1; -; Genomic_DNA.
DR AlphaFoldDB; H0FYB9; -.
DR PATRIC; fig|1107881.3.peg.2219; -.
DR Proteomes; UP000004038; 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:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR CDD; cd07906; Adenylation_DNA_ligase_LigD_LigC; 1.
DR Gene3D; 3.30.1490.70; -; 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; IPR014146; LigD_ligase_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR NCBIfam; TIGR02779; NHEJ_ligase_lig; 1.
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; PS50160; DNA_LIGASE_A3; 1.
PE 4: Predicted;
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EHK77973.1}.
FT DOMAIN 135..226
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 348 AA; 38198 MW; 3C04F9658092AB30 CRC64;
MSRRAKPLLP DDQVLKSKPA RPRDPAQPNL PFDPMPTRVE PCLALLKTAP PKGADWAFEV
KWDGYRLALH IEPKGVRIIT RGGHDWTHRF PAIAAAAKNL GLGTAILDGE AVVLDEQSRS
DFGALLQRSL GGRGGKRSSA ASVFFPFDLL YFDGHDLKGA ELSVRRHLLE DFLDGAIGAI
QLSEEVHGDS TALLAHACSM GLEGIIVKHR DRPYRSGRAG DWLKIKCVQS ESFMIIGYEQ
STVACSGIGS LLLAGRKGHD WAYVGSVGTG FNTKNAEYLR ATLDKLKTKQ PAVPTQGQEP
DLCPADIDRG NRVSWMDRRR QLRHASYKGL REVQDNAAVF DVSERLVG
//
