ID Q11MD8_CHESB Unreviewed; 536 AA.
AC Q11MD8;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN OrderedLocusNames=Meso_0032 {ECO:0000313|EMBL:ABG61437.1};
OS Chelativorans sp. (strain BNC1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Chelativorans.
OX NCBI_TaxID=266779 {ECO:0000313|EMBL:ABG61437.1};
RN [1] {ECO:0000313|EMBL:ABG61437.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BNC1 {ECO:0000313|EMBL:ABG61437.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of chromosome of Chelativorans sp. BNC1.";
RL Submitted (JUN-2006) 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};
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DR EMBL; CP000390; ABG61437.1; -; Genomic_DNA.
DR AlphaFoldDB; Q11MD8; -.
DR STRING; 266779.Meso_0032; -.
DR KEGG; mes:Meso_0032; -.
DR eggNOG; COG1793; Bacteria.
DR HOGENOM; CLU_005138_6_2_5; -.
DR OrthoDB; 9767858at2; -.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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 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; 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 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 DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ABG61437.1}.
FT DOMAIN 300..430
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 536 AA; 60371 MW; 1E6560D86F4A0E52 CRC64;
MERFAELLDR LVLTPSRNGK LRLLTDYFAT VPDPDRGYGL AALTGGIGFP AVKPAMLRML
VMERVDPVLF GYSYDYVGDL AETVSLIWPA GENEEAEAPS LSEVVERLAQ ASRSDAPAVV
ARLLDQLSPS GRFAAIKLAT GGLRVGVSAR LTKQALADFG QVDVQEIEEL WHGLWPPYTE
LFAWLEKRGP KPENAAKAPF RPVMLAHAIE EADFANLKPA DYAAEWKWDG IRVQAVAEDG
VRRLYSRTGD DISGAFPDLA EAMDFEAALD GELLVGDPRE RTGTFSDLQQ RLNRKSVSQK
MLRDYPVFMR CYDVLSLGGR DTRPLAYAER RELLKEFLTT LPPDRFDLSP AISFETWEDL
DDKRCNPPHP IIEGVMLKRR DSHYLPGRPK GPWFKWKRDP FTVDAVLMYA QRGHGKRSSF
YSDYTFGVWA GPEEEPMLVP VGKAYFGFTD EELKQIDKYV RDNTTERFGP VRAVRADRNH
GLVLEVAFEG LARSTRHKSG IAMRFPRISR LRWDKPSREA DRIETLEAMI PKGAGA
//
