ID   C1AUS5_RHOOB            Unreviewed;       347 AA.
AC   C1AUS5;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   Name=ligC {ECO:0000313|EMBL:BAH53415.1};
GN   OrderedLocusNames=ROP_51680 {ECO:0000313|EMBL:BAH53415.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH53415.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH53415.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH53415.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) 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   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|ARBA:ARBA00007572}.
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DR   EMBL; AP011115; BAH53415.1; -; Genomic_DNA.
DR   RefSeq; WP_015888921.1; NC_012522.1.
DR   AlphaFoldDB; C1AUS5; -.
DR   STRING; 632772.ROP_51680; -.
DR   KEGG; rop:ROP_51680; -.
DR   PATRIC; fig|632772.20.peg.5395; -.
DR   HOGENOM; CLU_008325_4_1_11; -.
DR   OrthoDB; 9770771at2; -.
DR   Proteomes; UP000002212; 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; 3.30.470.30; 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:BAH53415.1}.
FT   DOMAIN          11..206
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|Pfam:PF01068"
FT   DOMAIN          225..321
FT                   /note="DNA ligase ATP-dependent C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04679"
SQ   SEQUENCE   347 AA;  38304 MW;  66A589E3487652BE CRC64;
     MDLPVMPPLQ PMLAKAASSV PAQPESGLAW SYEPKWDGFR VLVFRDGDEV VLGSRGGKDL
     ARYFPELVRA VKDELPERCV VDGELVVPRN IDGRTRLDWE SLSERIHPAE SRVTMLAEKT
     PAQFVAFDLL ALGDRDLSRE DFSVRRAQLV DTIGGGPSCH VTAATESSAT ATEWFEAFEG
     AGLDGVVAKK LVGPYLPNKR EMVKVKHART ADCVVIGYRP HKSQPGIGSM LLGLYDGDQM
     AMVGGASAFT AARRIELLAE LDELRVGDDV VADGAPTRWQ SGNDRTWVPL RPERVVEVAY
     DQMEGARFRH AARFLRWRPD RTPDECTFQQ LEVPVRYDLA DVLAGGS
//