ID G7W6F7_DESOD Unreviewed; 813 AA.
AC G7W6F7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
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=Desor_2615 {ECO:0000313|EMBL:AET68164.1};
OS Desulfosporosinus orientis (strain ATCC 19365 / DSM 765 / NCIMB 8382 / VKM
OS B-1628 / Singapore I) (Desulfotomaculum orientis).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=768706 {ECO:0000313|EMBL:AET68164.1, ECO:0000313|Proteomes:UP000006346};
RN [1] {ECO:0000313|Proteomes:UP000006346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19365 / DSM 765 / NCIMB 8382 / VKM B-1628
RC {ECO:0000313|Proteomes:UP000006346};
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., Pester M.,
RA Spring S., Ollivier B., Rattei T., Klenk H.-P., Wagner M., Loy A.,
RA Woyke T.;
RT "Complete sequence of Desulfosporosinus orientis DSM 765.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AET68164.1, ECO:0000313|Proteomes:UP000006346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19365 / DSM 765 / NCIMB 8382 / VKM B-1628
RC {ECO:0000313|Proteomes:UP000006346};
RX PubMed=23105050; DOI=10.1128/JB.01392-12;
RA Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J.,
RA Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L.,
RA Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., Land M.L.,
RA Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., Huntmann M., Wei C.L.,
RA Davenport K.W., Daligault H., Chain P.S., Chen A., Mavromatis K.,
RA Markowitz V., Szeto E., Mikhailova N., Pati A., Wagner M., Woyke T.,
RA Ollivier B., Klenk H.P., Spring S., Loy A.;
RT "Complete genome sequences of Desulfosporosinus orientis DSM765T,
RT Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei DSM13257T,
RT and Desulfosporosinus acidiphilus DSM22704T.";
RL J. Bacteriol. 194:6300-6301(2012).
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; CP003108; AET68164.1; -; Genomic_DNA.
DR RefSeq; WP_014184972.1; NC_016584.1.
DR AlphaFoldDB; G7W6F7; -.
DR STRING; 768706.Desor_2615; -.
DR KEGG; dor:Desor_2615; -.
DR PATRIC; fig|768706.3.peg.2629; -.
DR eggNOG; COG1793; Bacteria.
DR eggNOG; COG3285; Bacteria.
DR HOGENOM; CLU_008325_0_1_9; -.
DR OrthoDB; 9802472at2; -.
DR Proteomes; UP000006346; 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:AET68164.1};
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:UP000006346};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 293..418
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 501..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 813 AA; 92721 MW; 2F2F102E9508E20E CRC64;
MTVKLREYNE KRNFSRTLEP EGIPENPKEG LRFVVQHHIA RRDHYDLRLE WDGALLSWAV
PKGPSYNTRD KRLAVEVEDH PLEYRNFEGT IPKGEYGGGV VMLWDEGMWE PYVDVGEGLR
SGVLKFILKG RRLKGKWALV RLKRKAGETQ DNWLLLKEKD EYANPEDGIS EFTTSIRTGR
TMREIEEGED EKITQNPFSS TVVQLAKLVS TIPKGEDWLY ELKYDGYRIL AYIEGNSVRL
ITRNGHDFTQ RFQDVAYSLV DWAGGRAMIL DGEMTITDAA GKTDFQALQN YMKNPQAQNL
TYIIFDLLAL DGGDLRGQPL IDRKTTLAAL LEDAPQNLYY SRHIPGKGKE SFTAACEAGM
EGIVGKKAAS VYSGTRNGDW IKLKCEHRQE FVVGGYTLSN RKTRGISSLI LGVYSGGELV
YAGRVGTGLS EADMRELAEI FANLKRKVPP FRMAPRPKSN EQITWLEPEL VAEIKFAEWT
SDNLLRQASF KGLRRDKNPR DIKKEIEEEE TLSPSFPKEE ARPMKARDKS LIIEGIKISN
PDKVIFAEPE ITKRDVIRYY EKVAERMLPY VSHRVLSIVR CPKGISQTCF YKKHPGPGSR
GIVTIPVSSS DGETNDYFYI ENSKGLIYEA QMGTLEFHIW GSRVDELEKP DLMVFDLDPD
EGMDLSRVRQ GVRDMRDILA ELSLNSYLKT SGGKGYHVVV PLKPVVSWDV FYDFAKRVAQ
VMEQKWPDRY TSNVRKAKRT NKIFIDWIRN GRGATSIAPY SLRARKGAGV SMPIDWDELD
RVAPGGVDMA EALRRIGCHD PWQDFFRNHQ RLK
//
