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Database: UniProt/TrEMBL
Entry: A0A0U3NLN3_9ACTN
LinkDB: A0A0U3NLN3_9ACTN
Original site: A0A0U3NLN3_9ACTN 
ID   A0A0U3NLN3_9ACTN        Unreviewed;       353 AA.
AC   A0A0U3NLN3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   ORFNames=AS200_09240 {ECO:0000313|EMBL:ALV32203.1};
OS   Streptomyces sp. CdTB01.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV32203.1, ECO:0000313|Proteomes:UP000068029};
RN   [1] {ECO:0000313|EMBL:ALV32203.1, ECO:0000313|Proteomes:UP000068029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CdTB01 {ECO:0000313|EMBL:ALV32203.1,
RC   ECO:0000313|Proteomes:UP000068029};
RA   Tian Y., Zhou G., Yang H., Lu X.;
RT   "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT   bacterium tolerant to cadmium.";
RL   Submitted (DEC-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}.
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DR   EMBL; CP013743; ALV32203.1; -; Genomic_DNA.
DR   RefSeq; WP_058921886.1; NZ_CP013743.1.
DR   AlphaFoldDB; A0A0U3NLN3; -.
DR   STRING; 1725411.AS200_09240; -.
DR   KEGG; scx:AS200_09240; -.
DR   OrthoDB; 9770771at2; -.
DR   Proteomes; UP000068029; 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:SF4; DNA LIGASE 1; 1.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 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:ALV32203.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000068029}.
FT   DOMAIN          105..227
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   353 AA;  39429 MW;  0D5D7428A086CB6D CRC64;
     MDLPVMPPVK PMLAKSVAKI PPGMQYEAKW DGFRAIVFRD GAEVELGSRT GKPLTRYFPE
     LVSALRERVP ERCVLDGEIV IARDGHLDFD ALTERIHPAD SRVRTLAERT PSSFVAFDLL
     ALADESLLDV PLTDRRALLE RALSGVTAPV HLAPATTDLE VAQGWFEQYE GAGLDGVIAK
     PLTVRYLQDE RAMFKIKHER TADVVVAGYR LHKSGPVVGS LLLGLYDDQG RLQHVGVSAA
     FPMKRRAELI EELEPLRMAD VAGHPWAAWS DEAAHETARL PGAPSRWSGK KDLSWVPLSP
     ERVAEVAYDH MENGARFRHT ARFRRWRPDR TPDSCTYAQL EEPVRYDLGE ILG
//
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