ID   G2IP73_SPHSK            Unreviewed;       345 AA.
AC   G2IP73;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   ORFNames=SLG_10370 {ECO:0000313|EMBL:BAK65712.1};
OS   Sphingobium sp. (strain NBRC 103272 / SYK-6).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=627192 {ECO:0000313|EMBL:BAK65712.1, ECO:0000313|Proteomes:UP000001275};
RN   [1] {ECO:0000313|EMBL:BAK65712.1, ECO:0000313|Proteomes:UP000001275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 103272 / SYK-6 {ECO:0000313|Proteomes:UP000001275};
RX   PubMed=22207743; DOI=10.1128/JB.06254-11;
RA   Masai E., Kamimura N., Kasai D., Oguchi A., Ankai A., Fukui S.,
RA   Takahashi M., Yashiro I., Sasaki H., Harada T., Nakamura S., Katano Y.,
RA   Narita-Yamada S., Nakazawa H., Hara H., Katayama Y., Fukuda M.,
RA   Yamazaki S., Fujita N.;
RT   "Complete genome sequence of Sphingobium sp. strain SYK-6, a degrader of
RT   lignin-derived biaryls and monoaryls.";
RL   J. Bacteriol. 194:534-535(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   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|ARBA:ARBA00007572}.
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DR   EMBL; AP012222; BAK65712.1; -; Genomic_DNA.
DR   RefSeq; WP_014075363.1; NC_015976.1.
DR   AlphaFoldDB; G2IP73; -.
DR   STRING; 627192.SLG_10370; -.
DR   KEGG; ssy:SLG_10370; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_008325_4_1_5; -.
DR   Proteomes; UP000001275; Chromosome.
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; cd07905; Adenylation_DNA_ligase_LigC; 1.
DR   CDD; cd07970; OBF_DNA_ligase_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; IPR044119; Adenylation_LigC-like.
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; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR044117; OBF_LigC-like.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR45674:SF9; DNA LIGASE 3; 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.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:BAK65712.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001275}.
FT   DOMAIN          26..202
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|Pfam:PF01068"
FT   DOMAIN          219..318
FT                   /note="DNA ligase ATP-dependent C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04679"
SQ   SEQUENCE   345 AA;  38340 MW;  F14C862BF356D9B6 CRC64;
     MAGRLRAWFD DLLPMEARLV AELPSGDGWQ FEPKWDGFRV LILKDGPDVE LKSKSGKSLT
     RFFPELAAAI GALGDRALSL DGEIILPVSD MLSFDALQQR LHPAASRIAR LSRETPAEIM
     LFDVLHRGST RLADRPLEER RTALEAWHAT IRSPVLHLSP MTRDARQAKA WLDRTGGALD
     GIVAKRRDAP YRGGERAMAK IKQQRTADCV VGGFREADGA VVSLLLGLYG PDGKLNHVGF
     TSAIARDQRR ELRDRLLPLV APPGFTGKAP GGPSRWSGKR TSDWLPIKPS LVVEVRYDQV
     TGGRFRHGTR LLRWRPDKAP EQCTSDQLEQ PLSPAQLGSL IREWE
//