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Database: UniProt
Entry: A0A0M2HJX1_9MICO
LinkDB: A0A0M2HJX1_9MICO
Original site: A0A0M2HJX1_9MICO 
ID   A0A0M2HJX1_9MICO        Unreviewed;       348 AA.
AC   A0A0M2HJX1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   ORFNames=RS81_00312 {ECO:0000313|EMBL:KJL45130.1};
OS   Microbacterium ketosireducens.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=92835 {ECO:0000313|EMBL:KJL45130.1, ECO:0000313|Proteomes:UP000033956};
RN   [1] {ECO:0000313|EMBL:KJL45130.1, ECO:0000313|Proteomes:UP000033956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12510 {ECO:0000313|EMBL:KJL45130.1,
RC   ECO:0000313|Proteomes:UP000033956};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (FEB-2015) 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:KJL45130.1}.
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DR   EMBL; JYIZ01000026; KJL45130.1; -; Genomic_DNA.
DR   RefSeq; WP_045274325.1; NZ_JYIZ01000026.1.
DR   AlphaFoldDB; A0A0M2HJX1; -.
DR   STRING; 92835.RS81_00312; -.
DR   PATRIC; fig|92835.4.peg.324; -.
DR   OrthoDB; 9770771at2; -.
DR   Proteomes; UP000033956; 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:KJL45130.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033956}.
FT   DOMAIN          112..234
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   348 AA;  38521 MW;  80AD90BB5C90FFED CRC64;
     MPYEIPAPML AKAAAAVPDP AKTAGGLSFE PKWDGFRALV SWDGESVEIG SRGAKPLTRY
     FPELVEAFTR LLPEPCLIDG EIVVPTGEPG SQRLDWESLS QRIHPAASRV NMLAEKTPAM
     FIAFDLLARG DGDLQQEPFS ERRAQLVDLL GDVPHPVHVT RTTDDPDLAR RWLAEFEGAG
     LDGVVAKPLA QPYQPNKRAM IKIKHARTAD VVALGYRIHK SGEGVGSLLV GLHGDDGTLY
     PVGGVAAWSN ARRLELIDEL APFVVRDDDG EAVRGEGEKS RFQAGRADSS FVKLRPERVL
     EVRYDQLEGW RFRHTVQFER WRPDRDPSSC TYEQLETVSA YDLGDVLD
//
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