ID A0A2S8WAA0_9CAUL Unreviewed; 540 AA.
AC A0A2S8WAA0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN ORFNames=CQ026_02110 {ECO:0000313|EMBL:PQZ84085.1};
OS Brevundimonas sp. MYb31.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=1848616 {ECO:0000313|EMBL:PQZ84085.1, ECO:0000313|Proteomes:UP000238612};
RN [1] {ECO:0000313|EMBL:PQZ84085.1, ECO:0000313|Proteomes:UP000238612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MYb31 {ECO:0000313|EMBL:PQZ84085.1,
RC ECO:0000313|Proteomes:UP000238612};
RA Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA Kaleta C., Schulenburg H.;
RT "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL Submitted (SEP-2017) 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:PQZ84085.1}.
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DR EMBL; PCPM01000003; PQZ84085.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S8WAA0; -.
DR OrthoDB; 9767858at2; -.
DR Proteomes; UP000238612; Unassembled WGS sequence.
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:PQZ84085.1}.
FT DOMAIN 310..432
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 540 AA; 59874 MW; E2F74DBD529CD0CA CRC64;
MRAFAALLDR LSFTASRNAK LRLIRDHLAD APDPDRGWAL AALTGALSFT AAKPAVIRQV
VEGRVDPELF RLSYDYVGDL AETVALIWPA RHGANREPEL SEVIDALNAA KRGEVQGLLE
AWLDALDADG RWALLKLVTG GLRVGVSARL AWQAAADFGG VEVADIQEVW HAQTPPYADL
MAWLDGRTGR PSAMAHGRFR PVMLAQPIDE AVDLPRLDPG EYAAEWKWDG IRVQAVSEGG
VKRLYSRTGE DVSGAFPDVV AALAYEGVID GELLVLRDGR VAPFGDLQQR LNRKTADARL
MISHPAGVRA YDLLAADGED LRALPFAERR KRLEGFVGEI GSDRIDLSPL VPFRTWEDLA
ARRAEPPPGD SQSAEGLMLK RLDSLYEAGR PRGPWFKWKR DPHLIDAVLM YAQRGHGKRS
SFYSDYTFGV WTEDADGVHV LTPVGKAYFG FTDEELKQLD RFVRENTVER FGPVRSVTAT
REFGLVLEVA FEGLQRSKRH KSGVAMRFPR ISRIRWDKPA READELPTLE AMLDAPSPAP
//
