UniProt: A2SMK3

Database: UniProt
Entry: A2SMK3_METPP

LinkDB:  A2SMK3_METPP 
Original site:  A2SMK3_METPP

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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 (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (8)   
   Pfam (4)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (26)   

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ID   A2SMK3_METPP            Unreviewed;       864 AA.
AC   A2SMK3;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 95.
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=Mpe_B0011 {ECO:0000313|EMBL:ABM96792.1};
OS   Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OG   Plasmid RPME01 {ECO:0000313|EMBL:ABM96792.1,
OG   ECO:0000313|Proteomes:UP000000366}.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Methylibium.
OX   NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM96792.1, ECO:0000313|Proteomes:UP000000366};
RN   [1] {ECO:0000313|EMBL:ABM96792.1, ECO:0000313|Proteomes:UP000000366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1232 / LMG 22953 / PM1
RC   {ECO:0000313|Proteomes:UP000000366};
RC   PLASMID=RPME01 {ECO:0000313|EMBL:ABM96792.1,
RC   ECO:0000313|Proteomes:UP000000366};
RX   PubMed=17158667; DOI=10.1128/JB.01259-06;
RA   Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA   Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA   Hristova K.R.;
RT   "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT   proteobacterium Methylibium petroleiphilum PM1.";
RL   J. Bacteriol. 189:1931-1945(2007).
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; CP000556; ABM96792.1; -; Genomic_DNA.
DR   RefSeq; WP_011831409.1; NC_008826.1.
DR   AlphaFoldDB; A2SMK3; -.
DR   KEGG; mpt:Mpe_B0011; -.
DR   eggNOG; COG1793; Bacteria.
DR   eggNOG; COG3285; Bacteria.
DR   HOGENOM; CLU_008325_0_0_4; -.
DR   Proteomes; UP000000366; Plasmid RPME01.
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:ABM96792.1};
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   Plasmid {ECO:0000313|EMBL:ABM96792.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000366};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          328..434
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          199..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   864 AA;  94968 MW;  A6FC1BB4B2832984 CRC64;
     MGRTAPSTQA NADTPLSRYN AKRNFKVTSE PAGVPAKRSG KSKALCFVIQ KHWASRLHYD
     FRLELDGVML SWAVPKGPSY DPALKQMAIH VEDHPISYNT FEGTIPKGQY GAGTVIIWDR
     GTWEPEGDPR EGMAKGKLIF KLHGQKLAGL WELVRISKPG EVKQEQWLLL KKRGDAWARP
     TSEYDVISAL PDSVVEKPLG PVEEREQRAG GTAAGTPGPS GEADLQLAVQ APLPAKLAPQ
     LATLASAVPS GGSWIVETKF DGYRMLARVD GDDVRLFTRN GNDWTSKLKT VAAAVKDLGL
     DSAWLDGEIV VINQAGVPDF NRLQNAIDNS RSKDISFFVF DVPFLGGMDL RKVPVASRRQ
     VLNELFEQRQ SEVVRFSEAF DVPPAHMLEA ACKMGLEGVM VKRADAPYVS SRTDTWLKLK
     CQQRQEFIVV GFTDRAGAPT EVGGLLLGYH EDGKLRYAGS VGTGWNSATG RELRSTLAKL
     QVEKPALEAG AVKPGRWSKR PAGVERWVKP TMVVEVAFSE WTPDGHVRHP TFRGVRTDKP
     ATQITREKAE RPEGPVTETA AAVAGKPRTS VKVTNPDRVI DPSTGFKKVD LVRYYESIAD
     WMLPHLKDRP VSLVRAPEGI TGEQFFQKHP ETKMPGMTEL DPALWPGHSS LLAVGSAEAL
     VSAAQMNVVE FHTWNSTIKR INEPDRVIFD LDPGEGVSWA HLQEAAVLMH TLLTELGLEA
     WLKTSGGKGL HVVVPLAPKL DYDAVKGFSQ AAVQHMAKTI PQRFVAKSGG SNRVGRIFID
     YLRNGHGQTT ASAFSARVRP GMGVSMPVSW EQLRELKSGS QWSIATAREY LSFQKSDPWA
     AYWTSKQTLT KAMRLLGYAP KKAA
//

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