ID   I4A4U0_DESDJ            Unreviewed;       812 AA.
AC   I4A4U0;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
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   OrderedLocusNames=Desde_0514 {ECO:0000313|EMBL:AFL98974.1};
OS   Desulfitobacterium dehalogenans (strain ATCC 51507 / DSM 9161 / JW/IU-DC1).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=756499 {ECO:0000313|EMBL:AFL98974.1, ECO:0000313|Proteomes:UP000006053};
RN   [1] {ECO:0000313|Proteomes:UP000006053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51507 / DSM 9161 / JW/IU-DC1
RC   {ECO:0000313|Proteomes:UP000006053};
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., Kruse T.,
RA   de Vos W.M., Smidt H., Woyke T.;
RT   "Complete sequence of Desulfitobacterium dehalogenans ATCC 51507.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFL98974.1, ECO:0000313|Proteomes:UP000006053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51507 / DSM 9161 / JW/IU-DC1
RC   {ECO:0000313|Proteomes:UP000006053};
RX   PubMed=25512312; DOI=10.1128/JB.02370-14;
RA   Kruse T., van de Pas B.A., Atteia A., Krab K., Hagen W.R., Goodwin L.,
RA   Chain P., Boeren S., Maphosa F., Schraa G., de Vos W.M., van der Oost J.,
RA   Smidt H., Stams A.J.;
RT   "Genomic, proteomic, and biochemical analysis of the organohalide
RT   respiratory pathway in Desulfitobacterium dehalogenans.";
RL   J. Bacteriol. 197:893-904(2015).
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; CP003348; AFL98974.1; -; Genomic_DNA.
DR   RefSeq; WP_014792468.1; NC_018017.1.
DR   AlphaFoldDB; I4A4U0; -.
DR   STRING; 756499.Desde_0514; -.
DR   KEGG; ddh:Desde_0514; -.
DR   eggNOG; COG1793; Bacteria.
DR   eggNOG; COG3285; Bacteria.
DR   HOGENOM; CLU_008325_0_0_9; -.
DR   OrthoDB; 9802472at2; -.
DR   Proteomes; UP000006053; 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; cd07971; OBF_DNA_ligase_LigD; 1.
DR   CDD; cd04862; PaeLigD_Pol_like; 1.
DR   Gene3D; 3.30.1490.70; -; 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; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR014146; LigD_ligase_dom.
DR   InterPro; IPR014144; LigD_PE_domain.
DR   InterPro; IPR014145; LigD_pol_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014143; NHEJ_ligase_prk.
DR   InterPro; IPR033651; PaeLigD_Pol-like.
DR   NCBIfam; TIGR02777; LigD_PE_dom; 1.
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; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF13298; LigD_N; 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; 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:AFL98974.1};
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          293..415
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          494..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..513
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   812 AA;  91956 MW;  79ACFD22DD10E977 CRC64;
     MTAELNPYNQ KRNFAKTLEP EGIRVISQED LKFVVQHHLA RRDHYDLRLE WEGALLSWAV
     PKGPSYDTRD KRLAVQVEDH PLEYRNFEGT IPKGEYGGGV VMLWDEGSWE PYGDVDEGLR
     EGVLKFVLKG RRLKGKWALV RMKEKAGEKK DNWLLLKEKD EYAQTADGIA ELTTSIRTGR
     TMAEIEEGED EKFTQNPFSS IEVQLAKLVH SIPEGKDWLY ELKYDGYRIV AYIEGNSVRL
     ITRNGHDYTE RFRDVASSLL DWAEGRAMIL DGEMVVTDPE GKTDFQALQN YLKNPRAKNL
     TYILFDLLAL DGADLRGHSL IDRKETLAGL MEDAPPNLHY SRHVRGKGKE SYLAACEGGM
     EGIIGKKADS LYSGARNGDW IKLKCAKRQE FVIGGYTLSH KKTSGISSLL LGVYEGEELV
     YAGRAGTGLS EADMKELEEK FKSIKSRVAP FKAAPKPRSN EKITWLEPEL VAEIQFAEWT
     KEDRLRQASF KGLRGDKNPR EIQREKADEE IQPQPVQKGR SPMKTNSNSI IIEGIKISSP
     DKVIFAQPEI TKVDVIRYYE KVAERMLPYV SHRVLSIVRC PKGVAQTCFY KKHPGPGSQG
     IVTIPILTSD GGTEDYFYIE NISGLIAEAQ MGTLEFHIWG SRVDELEKPD LLVFDLDPDE
     GMDLGTVRQG VRDIKDILAE LSLNSYLKTS GGKGYHVVVP LKPAVSWEVF HDFARGVAQV
     MEQKWPDRYT SNVRKAKRTN KIFIDWIRNG RGATSIAPYS LRARKGAGVS MPILWEELDM
     VAPDGVDMAE ALRRIEGSDP WQDFFQNQQR LK
//