ID   A4T655_MYCGI            Unreviewed;       366 AA.
AC   A4T655;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   OrderedLocusNames=Mflv_1254 {ECO:0000313|EMBL:ABP43736.1};
OS   Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS   PYR-GCK)).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350054 {ECO:0000313|EMBL:ABP43736.1};
RN   [1] {ECO:0000313|EMBL:ABP43736.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP43736.1};
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., Mikhailova N., Miller C., Richardson P.;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABP43736.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP43736.1};
RX   PubMed=23469141;
RA   Badejo A.C., Badejo A.O., Shin K.H., Chai Y.G.;
RT   "A Gene Expression Study of the Activities of Aromatic Ring-Cleavage
RT   Dioxygenases in Mycobacterium gilvum PYR-GCK to Changes in Salinity and pH
RT   during Pyrene Degradation.";
RL   PLoS ONE 8:E58066-E58066(2013).
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; CP000656; ABP43736.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4T655; -.
DR   STRING; 350054.Mflv_1254; -.
DR   KEGG; mgi:Mflv_1254; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_008325_4_1_11; -.
DR   OrthoDB; 9770771at2; -.
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; 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; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ABP43736.1}.
FT   DOMAIN          108..251
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   366 AA;  40534 MW;  69534DA85536F2B0 CRC64;
     MAGMRLPVMP PLSPMLSKSV QQIPDGASYE PKWDGFRSIV FRDGDEIEFG SRNERPMTRY
     FPELVAAARS ELPPRCVVDG EIVIATAGGL DFEALQLRLH PAASRVTMLA EKTPASFIAF
     DLLALGDTDL TGRPFTERRA ALVDALAGAG PTFHVTPATR DIALATRWFD EFEGAGLDGV
     IAKPVDGVYL PDKRTMFKIK HRRTADCVVA GYRLHKSGDD AVGSLLLGLY DSDGALASVG
     VIGAFPMARR RALLAELQPL VTTFDEHPWN WAAHADPDVV RRHGGGSRWN AGKDLSFVPL
     RPERVVEVRY DHMEGRRFRH MAQFNRWRPD RTPRSCTFDQ LEQPVSFSLD DIGPGLTPRA
     GRPYRS
//