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Database: UniProt/TrEMBL
Entry: A0A0K1JJZ0_9MICO
LinkDB: A0A0K1JJZ0_9MICO
Original site: A0A0K1JJZ0_9MICO 
ID   A0A0K1JJZ0_9MICO        Unreviewed;       354 AA.
AC   A0A0K1JJZ0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   ORFNames=VV02_16195 {ECO:0000313|EMBL:AKU17044.1};
OS   Luteipulveratus mongoliensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC   Luteipulveratus.
OX   NCBI_TaxID=571913 {ECO:0000313|EMBL:AKU17044.1, ECO:0000313|Proteomes:UP000066480};
RN   [1] {ECO:0000313|EMBL:AKU17044.1, ECO:0000313|Proteomes:UP000066480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MN07-A0370 {ECO:0000313|EMBL:AKU17044.1,
RC   ECO:0000313|Proteomes:UP000066480};
RA   Juboi H., Basik A., Shamsul S.S., Arnold P., Schmitt E.K., Sanglier J.-J.,
RA   Yeo T.;
RT   "Luteipulveratus halotolerans sp. nov., a novel actinobacterium
RT   (Dermacoccaceae) from Sarawak, Malaysia.";
RL   Submitted (MAR-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; CP011112; AKU17044.1; -; Genomic_DNA.
DR   RefSeq; WP_052593084.1; NZ_CP011112.1.
DR   AlphaFoldDB; A0A0K1JJZ0; -.
DR   STRING; 571913.VV02_16195; -.
DR   KEGG; lmoi:VV02_16195; -.
DR   PATRIC; fig|571913.6.peg.3286; -.
DR   OrthoDB; 9770771at2; -.
DR   Proteomes; UP000066480; 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; 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:AKU17044.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000066480}.
FT   DOMAIN          124..256
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   354 AA;  38871 MW;  16A1DB78BF90EA1B CRC64;
     MELPFDLPIT PMLAKAVKGV PAADSVEGGL SYEPKWDGFR VLLLRDGDEV ELASRGSKPL
     TRYFPEVVAA AKEHLPERCA LDGEIVVRSG SPGAQRLDWE ALGQRIHPAA SRVEKLAGET
     PAEVIFFDAL AFGDESLLDQ PFATRRERLV KALSRLAADA PFHVTRVTDD PAKAEDWFTR
     FEGAGLDGVV AKPLEGTYEP GKRTMLKIKH SRTAEGVLLG YRIHKSGEGV GSLLLGMYDA
     DGNLRNVGGI SAFTMARRIE LIDELAELVV RDDDGGALTG ETDRSRFSGS KDVSFVRLRP
     EKVVEVKFDQ LEGSRFRHTV GFLRWRPDRE PGSCLLEQVE RAPSYDLDAV LGAD
//
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