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Database: UniProt
Entry: M2QPU3_9PSEU
LinkDB: M2QPU3_9PSEU
Original site: M2QPU3_9PSEU 
ID   M2QPU3_9PSEU            Unreviewed;       359 AA.
AC   M2QPU3;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   ORFNames=C791_8129 {ECO:0000313|EMBL:EMD28696.1};
OS   Amycolatopsis azurea DSM 43854.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=1238180 {ECO:0000313|EMBL:EMD28696.1, ECO:0000313|Proteomes:UP000014137};
RN   [1] {ECO:0000313|EMBL:EMD28696.1, ECO:0000313|Proteomes:UP000014137}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43854 {ECO:0000313|EMBL:EMD28696.1,
RC   ECO:0000313|Proteomes:UP000014137};
RA   Khatri I., Kaur I., Subramanian S., Mayilraj S.;
RT   "Genome assembly of Amycolatopsis azurea DSM 43854.";
RL   Submitted (OCT-2012) 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}.
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:EMD28696.1}.
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DR   EMBL; ANMG01000009; EMD28696.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2QPU3; -.
DR   PATRIC; fig|1238180.3.peg.1524; -.
DR   Proteomes; UP000014137; Unassembled WGS sequence.
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.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EMD28696.1}.
FT   DOMAIN          107..196
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   359 AA;  40709 MW;  BD382A5F2E9A8C70 CRC64;
     MELPVMPPVK PMLAKAVHEL PRTPGLLYEP KWDGFRCVVF RDGDEVVLGS RNDRPLTRYF
     PELVELLKEA LPERCVVDGE IVLVTEGGLD FEALQLRLHP AASRVNKLAE ETPTSFVVFD
     LLALDDRDLT PEPFSERRKL LESVVDTKFA RVHLTPLSED PDVAQDWFTR FEGAGFDGVM
     AKPADAPYEQ DKRVMWKVKH QRTADCVVAG FRWHKDGVGV GSLLLGLYND EGVLHHVGVA
     SSFTAARRRE LVDELAPLRE NALEHHPWRE WAEAHEEAGG RMPGAGSRWA PKKDLSWEPV
     RIEWVAEVRY EHVEGTRFRH GGRLVRFRPD REPASCTYEQ LEEVPPAELA TLFTELGEA
//
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