ID J2WL85_9SPHN Unreviewed; 531 AA.
AC J2WL85;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN ORFNames=PMI04_02059 {ECO:0000313|EMBL:EJK83455.1};
OS Sphingobium sp. AP49.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1144307 {ECO:0000313|EMBL:EJK83455.1};
RN [1] {ECO:0000313|EMBL:EJK83455.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP49 {ECO:0000313|EMBL:EJK83455.1};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(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};
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:EJK83455.1}.
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DR EMBL; AJVL01000053; EJK83455.1; -; Genomic_DNA.
DR RefSeq; WP_007709421.1; NZ_CP124576.1.
DR AlphaFoldDB; J2WL85; -.
DR STRING; 1144307.PMI04_02059; -.
DR PATRIC; fig|1144307.3.peg.1819; -.
DR eggNOG; COG1793; Bacteria.
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:EJK83455.1}.
FT DOMAIN 307..437
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 531 AA; 58778 MW; 431685101578778F CRC64;
MRQFSQLLDG LVYTRSRNGK LALIAAYMRE APDPDRGWAL AALTGNLDLK AVKASAIGEM
IRARTDPVLF EMSRDYVGDL AETVALLWPR AHDELAELDD GSLSLSAVID RLHTINRATA
PDALAQMMDH LDASGRFALL KLATGGLRVG ISARLAKTGF AQAFGLDVDD VEQVWHALAP
PYTALFDWAE GRSARPDPEG TPYFRPFMLA QPLEVDSVDL ADYAAEWKWD GIRIQIVGTG
PKHGGETRLY SRAGDDITGS FPEIAQAFTG HAVLDGELLV KGEFQGGEAA SFNALQQRLG
RKAVSAKMMA DYPAFVRLYD LLIEGDDDLR ALPWTDRRAR LEAYTAQLNP DQFDLSAVID
TPDFAALADI RAGARDAAIE GVMLKRRDSP YVAGRKAALW YKWKRDPLTA DCVMMYAQRG
HGKRSSFYSD YTFGCWTADG ELLPVGKAYS GFTDEELKWL DRFVRGNTVN RFGPVREVEK
TLVLEVAFDS IHDSKRHKSG LAMRFPRIAR IRKDKPAAEA DTVEGLKRLV S
//