ID   Q31F09_HYDCU            Unreviewed;       266 AA.
AC   Q31F09;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   SubName: Full=ATP dependent DNA ligase, central {ECO:0000313|EMBL:ABB42264.1};
GN   OrderedLocusNames=Tcr_1672 {ECO:0000313|EMBL:ABB42264.1};
OS   Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira
OS   crunogena).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Hydrogenovibrio.
OX   NCBI_TaxID=317025 {ECO:0000313|EMBL:ABB42264.1};
RN   [1] {ECO:0000313|EMBL:ABB42264.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=XCL-2 {ECO:0000313|EMBL:ABB42264.1};
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   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Scott K.M., Sievert S., Kerfeld C.,
RA   Freyermuth S., Dobrinski K., Boller A., Fitzpatrick K., Thoma P., Moore J.,
RA   Richardson P.;
RT   "Complete sequence of Thiomicrospira crunogena XCL-2.";
RL   Submitted (JUL-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};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|ARBA:ARBA00001968};
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DR   EMBL; CP000109; ABB42264.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q31F09; -.
DR   STRING; 317025.Tcr_1672; -.
DR   KEGG; tcx:Tcr_1672; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_021047_0_0_6; -.
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:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd07896; Adenylation_kDNA_ligase_like; 1.
DR   CDD; cd08041; OBF_kDNA_ligase_like; 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; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR029319; DNA_ligase_OB.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR47810; DNA LIGASE; 1.
DR   PANTHER; PTHR47810:SF1; DNA LIGASE B; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF14743; DNA_ligase_OB_2; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
PE   4: Predicted;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000313|EMBL:ABB42264.1}.
FT   DOMAIN          28..182
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|Pfam:PF01068"
FT   DOMAIN          196..261
FT                   /note="DNA ligase OB-like"
FT                   /evidence="ECO:0000259|Pfam:PF14743"
SQ   SEQUENCE   266 AA;  30249 MW;  3934005C2F46331E CRC64;
     MATAYADAKK PKMLLLETYQ ENQSVLGWWM SEKLDGVRAK WNGKALISRG GHEIHAPDWF
     VADLPAFELD GELWTTRQDF ENVVSIVRQQ HPDSRWDAVS YQIFEVPNQL GNLMDRLAVL
     KNYLAKHQLT HVQIIPQTKI ISEAQLTSEF DRLTEIGAEG LVLRAPNQSY ETGRSRQALK
     MKAYEDDECQ VVGYKPGKGK ISGLVGALLC DWHGKMQLSI GSGLSLQERE HPPEIGQWIT
     FKYYGLTGSG KPRFPVFMRI RLDQDM
//