ID J3ETD0_9PSED Unreviewed; 848 AA.
AC J3ETD0;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
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 ORFNames=PMI21_02109 {ECO:0000313|EMBL:EJM18537.1};
OS Pseudomonas sp. GM18.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144324 {ECO:0000313|EMBL:EJM18537.1, ECO:0000313|Proteomes:UP000007280};
RN [1] {ECO:0000313|EMBL:EJM18537.1, ECO:0000313|Proteomes:UP000007280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM18 {ECO:0000313|EMBL:EJM18537.1,
RC ECO:0000313|Proteomes:UP000007280};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(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};
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:EJM18537.1}.
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DR EMBL; AKJT01000036; EJM18537.1; -; Genomic_DNA.
DR RefSeq; WP_007937011.1; NZ_AKJT01000036.1.
DR AlphaFoldDB; J3ETD0; -.
DR PATRIC; fig|1144324.3.peg.2057; -.
DR OrthoDB; 9802472at2; -.
DR Proteomes; UP000007280; 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; 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:EJM18537.1};
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 314..420
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 193..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 848 AA; 94007 MW; F87B4781816FFC9D CRC64;
MNKTLDDYNR IRDFVATPEP AAAKRSGKKT AKDHALQFCI QKHDASHLHY DFRLELDGAL
KSWAVPKGPS LDPKVKRLAI HVEDHPLDYA TFEGTIPEGH YGAGEVIVWD RGVWIPQDDP
AKAYAEGRLK FELQGEKLGG LWNLVRTHMP GKQEQWFLIK HQDGAARPES DYDVVAAEPD
SVLSDRTIVA RSKPGPVKKP AARARRERSS QLTGARKARL PELLKPELAT LVESAPDGEW
SYEIKFDGYR VMARIDHDEV KLFTRNGHDW THKLPEQAAA LAALGLESAW LDGEMVVADE
QGVPDFQALQ NAFDAGHSAS IVYYLFDLPY LNGVDLREVA VEARRVALAT VLKPNENPLL
RYSDTFNESP EALLDSACKM HMEGVIGKRL GSLYVSRRSS DWIKLKCKHR QEFIVVGFTD
PKGSRSAFGA LLLGLHDRDS GELRYAGKVG TGFSEASLKR LYGQLKPLLT KKPSVVNPPT
GVEAKAVHWL KPVLLAEVAF AEMTKDGSVR QAVFHGLRED KPAAGITEER PTTVKTSGTK
TKNTQAAPSQ VGLGRGKVRI THPERVIDAS SGTTKMQLAE YYASVAEWIL PQLKDRPVAL
VRAPDGIAGE LFFQKNAENL AIPGIITLDK ALTGQPMMVI NNAEALIGAV QMSTVELHTW
NATSVDLDKP DRFVLDLDPD PALPWRSMVE ATRLTLTVLD ELGLKAFLKT SGGKGIHLVV
PLTRKHGWDE VKDFSHAIVS HMAKLLPERF SAVSGPKNRV GRIFIDYLRN GLGATTICAY
AVRTREGLPV SVPIFREEVA ELKGANQWNL HTVHERLAEV GDEPWADLKK TRQTITAEMR
RRIGMKKQ
//
