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Database: UniProt
Entry: R7ZEC5_LYSSH
LinkDB: R7ZEC5_LYSSH
Original site: R7ZEC5_LYSSH 
ID   R7ZEC5_LYSSH            Unreviewed;       614 AA.
AC   R7ZEC5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
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   Name=ligD {ECO:0000313|EMBL:EON72374.1};
GN   ORFNames=H131_12413 {ECO:0000313|EMBL:EON72374.1};
OS   Lysinibacillus sphaericus OT4b.31.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=1285586 {ECO:0000313|EMBL:EON72374.1, ECO:0000313|Proteomes:UP000013911};
RN   [1] {ECO:0000313|EMBL:EON72374.1, ECO:0000313|Proteomes:UP000013911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OT4b.31 {ECO:0000313|EMBL:EON72374.1,
RC   ECO:0000313|Proteomes:UP000013911};
RA   Pena-Montenegro T.D., Dussan J.;
RT   "Draft genome of the heavy metal tolerant bacterium Lysinibacillus
RT   sphaericus strain OT4b.31.";
RL   Submitted (APR-2013) 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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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:EON72374.1}.
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DR   EMBL; AQPX01000018; EON72374.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7ZEC5; -.
DR   PATRIC; fig|1285586.5.peg.2529; -.
DR   eggNOG; COG1793; Bacteria.
DR   eggNOG; COG3285; Bacteria.
DR   HOGENOM; CLU_008325_0_2_9; -.
DR   Proteomes; UP000013911; Unassembled WGS sequence.
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   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   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:EON72374.1};
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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          112..240
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   614 AA;  71988 MW;  4E439BE8A671B0F3 CRC64;
     MKVVVKMKPM LLTDVNEAPI GEEWLYETKY DGFRCILVWE EEEPILKSRN DNVLNHLFPE
     IIEFCMRIYD RIKPLLPLVL DGEVVYLTNH FKSNFSIVQK RGRMQNKDVI AEHAKHFPFH
     YVVFDLLKLK GEEQSNRYLK TRKQQLTKFF TAVKLPTTIN YQDGQLLQAI ENFEDSEMLL
     QTIRANNGEG IIAKKKTSKW VSNIRSTDWL KLKNWRYITV IVNKYDKGNG YFHGGVYQQG
     TFNEVVIFRH GMTDKERKTL VTFFQNNGTK RQETWELEPS ICVDIACIDF DGSKLREPRF
     HAFRLEINPE ACTWLQMQRQ LLPIPNNVQI THPDKPVWPE IGITKDGYLH YLQMISSYLL
     PFLYDRPLTL IRYPHGAPGE SFYQKSSPEK IPDFVTTARI ADTNFILCNN IETLLWLGNQ
     LALEFHIPFQ TIRTEKPTEI VFDLDPPSVD EFSLAMQGAR QLKEICDYFH LQSFVKTSGG
     KGLQLYIPLP EHAFSYEEVR IFTEFVCKFL CKQQPDFYTI ERLKKNRQKK LYLDYVQHAE
     GKTIISPYST RGNNKGLVAT PLNWDEVNEQ LRPEKFTIPT VLARMKDIGN PFRNFREIGE
     KQDFKSVLHH LRNS
//
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