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Database: UniProt
Entry: A0A1A2Z3B4_9MYCO
LinkDB: A0A1A2Z3B4_9MYCO
Original site: A0A1A2Z3B4_9MYCO 
ID   A0A1A2Z3B4_9MYCO        Unreviewed;       331 AA.
AC   A0A1A2Z3B4;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   ORFNames=A5707_03775 {ECO:0000313|EMBL:OBI43982.1};
OS   Mycobacterium kyorinense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=487514 {ECO:0000313|EMBL:OBI43982.1, ECO:0000313|Proteomes:UP000093592};
RN   [1] {ECO:0000313|Proteomes:UP000093592}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E861 {ECO:0000313|Proteomes:UP000093592};
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Sam S., Sreng N.,
RA   Him V., Kerleguer A., Cheng S.;
RL   Submitted (JUN-2016) 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:OBI43982.1}.
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DR   EMBL; LZKJ01000140; OBI43982.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A2Z3B4; -.
DR   Proteomes; UP000093592; 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.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:OBI43982.1}.
FT   DOMAIN          13..192
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|Pfam:PF01068"
FT   DOMAIN          210..307
FT                   /note="DNA ligase ATP-dependent C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04679"
SQ   SEQUENCE   331 AA;  37175 MW;  6CAA355478FA149B CRC64;
     MLAKAAGKLP DEPGVWSYEP KWDGFRALVF RDGDEVMLQS RNGKDLGRYF PELLEALRTE
     VSPRCVLDGE IVVPRDVDGR VRLDWDSLSQ RIHPAASRIN MLAEHTPAHF IGFDVLATGS
     APLLGEPFRI RRAALSELVD AKDWCHVTGT TEDPELGAHW LTTFEGAGLD GVVAKRLDGP
     YLPGKREMVK IKHARDADCV AMGYRVHKSG EGIGSILLGL YRDGRLHMVG GAASFTAKDR
     LKLLAELEPL RVGDDVVYDG EPSRWNAAAD KRWVPIRPDR VAEVAYDQME GDRFRHTVRF
     VRWRPDRDPQ SCTFDQLDVP LNYDLYDVLE S
//
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