ID   G2TMD9_HEYCO            Unreviewed;       613 AA.
AC   G2TMD9;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
DE   AltName: Full=NHEJ DNA polymerase {ECO:0000256|ARBA:ARBA00029943};
GN   ORFNames=Bcoa_3265 {ECO:0000313|EMBL:AEP02437.1};
OS   Heyndrickxia coagulans 36D1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX   NCBI_TaxID=345219 {ECO:0000313|EMBL:AEP02437.1, ECO:0000313|Proteomes:UP000009283};
RN   [1] {ECO:0000313|EMBL:AEP02437.1, ECO:0000313|Proteomes:UP000009283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=36D1 {ECO:0000313|EMBL:AEP02437.1,
RC   ECO:0000313|Proteomes:UP000009283};
RX   PubMed=22675583; DOI=10.4056/sigs.2365342;
RA   Rhee M.S., Moritz B.E., Xie G., Glavina Del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Chertkov O., Brettin T., Han C., Detter C.,
RA   Pitluck S., Land M.L., Patel M., Ou M., Harbrucker R., Ingram L.O.,
RA   Shanmugam K.T.;
RT   "Complete Genome Sequence of a thermotolerant sporogenic lactic acid
RT   bacterium, Bacillus coagulans strain 36D1.";
RL   Stand. Genomic Sci. 5:331-340(2011).
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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DR   EMBL; CP003056; AEP02437.1; -; Genomic_DNA.
DR   RefSeq; WP_014098446.1; NC_016023.1.
DR   AlphaFoldDB; G2TMD9; -.
DR   KEGG; bag:Bcoa_3265; -.
DR   eggNOG; COG1793; Bacteria.
DR   eggNOG; COG3285; Bacteria.
DR   HOGENOM; CLU_008325_0_2_9; -.
DR   OrthoDB; 9802472at2; -.
DR   Proteomes; UP000009283; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd07906; Adenylation_DNA_ligase_LigD_LigC; 1.
DR   CDD; cd04866; LigD_Pol_like_3; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 3.90.920.10; DNA primase, PRIM domain; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR014146; LigD_ligase_dom.
DR   InterPro; IPR033652; LigD_Pol-like_3.
DR   InterPro; IPR014145; LigD_pol_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014143; NHEJ_ligase_prk.
DR   NCBIfam; TIGR02778; ligD_pol; 1.
DR   NCBIfam; TIGR02779; NHEJ_ligase_lig; 1.
DR   NCBIfam; TIGR02776; NHEJ_ligase_prk; 1.
DR   PANTHER; PTHR42705; BIFUNCTIONAL NON-HOMOLOGOUS END JOINING PROTEIN LIGD; 1.
DR   PANTHER; PTHR42705:SF2; MULTIFUNCTIONAL NON-HOMOLOGOUS END JOINING DNA REPAIR PROTEIN LIGD; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF21686; LigD_Prim-Pol; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AEP02437.1};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009283};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          105..206
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   613 AA;  70594 MW;  544A3BA7BCBA351D CRC64;
     MKPMLPVLKW SLPDTGKWVY EIKYDGYRAI LDWTEDGMRL WSRNGKDLLP RFPEIRTFLQ
     TLEGRVKGQL PLRLDGELVL LENPYKAGFR ELQRRGRMKA EAAAEQAKMR PAHYLVFDLL
     MLGGEDMAGK PYLQRKKALE NLCETLALPL SPAPGETARV QQIPFTRDAS VLKETVKNFN
     SEGIVAKQTD SKWEAGKRVE TWIKVKNWKT AACFITAYDE KNGYFDVAVF KDGGIFPIGQ
     FLFSMNPDEK QILTEAVRKN AANNENGVYT IDPSICVEIF YLEWDGANLR EPHFHRFRFD
     LSPDACTFED FRLRNAAIPE EVEVTHPDKP LWKKRHVTKL DFLAYMREIS PFMLPFLSDR
     LLTVIRYPHG VFGEAFYQKN CPDYAPAFVD TAMHEDIRYI VCNDLKTLMW LANQLAVEYH
     IPFQTVNSRF VSEIVFDFDP PSRDAFQLAV EAALLLKQVT DALHLESFVK ISGNKGLQVY
     IPLPDRQFSW EDTRLFTEFM AAYFISKSPE HFTIERMKKK RGGKLYVDFV QHAEGKTIIA
     PYSMRGHEDA LVAAPLFWEE VNASLSPYDF TIETVLSRVN RYGCPFARFF ACKSGQPFAP
     VLAFLKQNKG RPI
//