UniProt: Q09E36

Database: UniProt
Entry: Q09E36_STIAD

LinkDB:  Q09E36_STIAD 
Original site:  Q09E36_STIAD

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (12)   
   InterPro (7)   
   Pfam (4)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (26)   

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ID   Q09E36_STIAD            Unreviewed;       836 AA.
AC   Q09E36;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 91.
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:EAU70093.1};
GN   OrderedLocusNames=STAUR_6997 {ECO:0000313|EMBL:ADO74753.1};
GN   ORFNames=STIAU_8411 {ECO:0000313|EMBL:EAU70093.1};
OS   Stigmatella aurantiaca (strain DW4/3-1).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Archangiaceae; Stigmatella.
OX   NCBI_TaxID=378806 {ECO:0000313|EMBL:EAU70093.1, ECO:0000313|Proteomes:UP000032702};
RN   [1] {ECO:0000313|EMBL:EAU70093.1, ECO:0000313|Proteomes:UP000032702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DW4/3-1 {ECO:0000313|EMBL:EAU70093.1,
RC   ECO:0000313|Proteomes:UP000032702};
RA   Nierman W.C.;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADO74753.1, ECO:0000313|Proteomes:UP000001351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO74753.1,
RC   ECO:0000313|Proteomes:UP000001351};
RX   PubMed=21037205; DOI=10.1093/molbev/msq292;
RA   Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA   Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA   Sogaard-Andersen L.;
RT   "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL   Mol. Biol. Evol. 28:1083-1097(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; CP002271; ADO74753.1; -; Genomic_DNA.
DR   EMBL; AAMD01000001; EAU70093.1; -; Genomic_DNA.
DR   RefSeq; WP_002609400.1; NZ_AAMD01000001.1.
DR   STRING; 378806.STAUR_6997; -.
DR   KEGG; sur:STAUR_6997; -.
DR   PATRIC; fig|378806.16.peg.9547; -.
DR   eggNOG; COG1793; Bacteria.
DR   eggNOG; COG3285; Bacteria.
DR   HOGENOM; CLU_008325_0_1_7; -.
DR   OrthoDB; 9802472at2; -.
DR   Proteomes; UP000001351; Chromosome.
DR   Proteomes; UP000032702; 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; cd04865; LigD_Pol_like_2; 1.
DR   CDD; cd07971; OBF_DNA_ligase_LigD; 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   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:EAU70093.1};
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          301..436
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          178..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          512..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   836 AA;  93061 MW;  FD4FE49892184E37 CRC64;
     MKTPRSLRTY RAKRDFQKTS EPAPEAKAPR RRGAPPLFVV HKHDATRLHY DLRLEIDGAL
     ASWALPKGPS FDPKTKRLAV ETEDHPLAYA GFEGRIPEGE YGGGDSLLWD RGTYETVPPG
     EAPEQRKKGH LTVQLHGEKL KGRWHLIRTK SRGKKAQWLC FKAMDGEADA DYDVTADRPE
     SVKSGRSATR GPVRKGALKS RPLPAEQLLE RVWPPMLAQL SVPTEADDAT HLYEVKYDGF
     RALAALSSGA LTLHSRNGHD LSGRFPQLAE ALRQLRVTEA VLDGEIIALD PQGRSRFQLL
     QKGSDAEQRF VAFDLLWLDG EDLRPRPLEA RRELLEQLLS GVKPPLQLSE RLDLPGDEAL
     AKARSQGWEG LIAKRRGAPY VGSRSRDWLK LKVQAAQETV ILGYLPIQNA RAREEIGALL
     VGVHGPDGYH DVGKVGTGFS SETRRELRAL LDRQRVRAPV AVDAKPRPGA VWVKPKYVAQ
     VHFTEWTHDG RLRHPVFQGL RTDKKPQEVV REQVSEPRKA AQKSKAAPKS GARRAPRAFS
     ARATRSQVQE EPAEAEGRAR LTHGDRVLYP QERLTKQDVF AYYREAAPLL LPVLANRPLA
     VQQWPAGIQA PGFFRHELSG MPAWLPTLRV KHEAKTLAHV NVQSLEALLW LANQSALTLH
     IWSSHAPKLA QPDWVVFDLD PGKGPWEDVI TVAQALREKL EALGLESLPK TSGKRGLHVL
     IPLAPGHTYA QTQRFAEKIA AELETELGSL ATTERTIQKR RGRLYLDVGQ NGRGKTVVAP
     YSLRAIPGAP FSAPLAWSEV TRKLDPLRFT LKTLSKRLDA VGDLFARALH GTQTLP
//

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