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Database: UniProt/TrEMBL
Entry: L0EIU3_THECK
LinkDB: L0EIU3_THECK
Original site: L0EIU3_THECK 
ID   L0EIU3_THECK            Unreviewed;       317 AA.
AC   L0EIU3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   OrderedLocusNames=Theco_3019 {ECO:0000313|EMBL:AGA59080.1};
OS   Thermobacillus composti (strain DSM 18247 / JCM 13945 / KWC4).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Thermobacillus.
OX   NCBI_TaxID=717605 {ECO:0000313|EMBL:AGA59080.1, ECO:0000313|Proteomes:UP000010795};
RN   [1] {ECO:0000313|Proteomes:UP000010795}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18247 / JCM 13945 / KWC4
RC   {ECO:0000313|Proteomes:UP000010795};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Anderson I.,
RA   Woyke T.;
RT   "Complete sequence of chromosome of Thermobacillus composti KWC4.";
RL   Submitted (JAN-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};
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DR   EMBL; CP003255; AGA59080.1; -; Genomic_DNA.
DR   RefSeq; WP_015255818.1; NC_019897.1.
DR   AlphaFoldDB; L0EIU3; -.
DR   STRING; 717605.Theco_3019; -.
DR   KEGG; tco:Theco_3019; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_008325_4_0_9; -.
DR   OrthoDB; 9802472at2; -.
DR   Proteomes; UP000010795; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   CDD; cd07906; Adenylation_DNA_ligase_LigD_LigC; 1.
DR   CDD; cd07971; OBF_DNA_ligase_LigD; 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; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR029710; LIG4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR45997; DNA LIGASE 4; 1.
DR   PANTHER; PTHR45997:SF1; DNA LIGASE 4; 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   4: Predicted;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AGA59080.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010795}.
FT   DOMAIN          103..225
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   317 AA;  35106 MW;  FEA10C6A24362C07 CRC64;
     MEPIVPFEPI AADDIPAGPQ WAAQIKWDGV RMLVYFDGAA TKLVNRRLHE RTMQYPELAD
     ARRYCRARSA ILDGEIVAFD AARPSFHEVM RRDGIRNARA VPAAVREIPV TYMVFDILYL
     DGEWVTGRSL EERQRLLARA VEPDGRVRLV ENTDDGAKLF DVMRKHGMEG IVVKDLASTY
     AVGGKDGRWR KIKVRRDLTA AVGGVTCGGG RVNALLLGLY DGQGRLHYIG HAGSGRLTGR
     DWADITAAAE LLRTPDCPFA AKPPRSAGAV WIRPMLTAKV RYLEWTAGRT LRQPVIEVVS
     AGPGTDCTFD RLDEPTV
//
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