ID   Q87ZG5_PSESM            Unreviewed;       851 AA.
AC   Q87ZG5;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 120.
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=PSPTO_3464 {ECO:0000313|EMBL:AAO56939.1};
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283 {ECO:0000313|EMBL:AAO56939.1, ECO:0000313|Proteomes:UP000002515};
RN   [1] {ECO:0000313|EMBL:AAO56939.1, ECO:0000313|Proteomes:UP000002515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000 {ECO:0000313|Proteomes:UP000002515};
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., Deboy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S., Brinkac L., Beanan M.J., Haft D.H., Nelson W.C., Davidsen T.,
RA   Zafar N., Zhou L., Liu J., Yuan Q., Khouri H., Fedorova N., Tran B.,
RA   Russell D., Berry K., Utterback T., Van Aken S.E., Feldblyum T.V.,
RA   D'Ascenzo M., Deng W.L., Ramos A.R., Alfano J.R., Cartinhour S.,
RA   Chatterjee A.K., Delaney T.P., Lazarowitz S.G., Martin G.B.,
RA   Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M., Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016853; AAO56939.1; -; Genomic_DNA.
DR   RefSeq; NP_793244.1; NC_004578.1.
DR   RefSeq; WP_011104572.1; NC_004578.1.
DR   AlphaFoldDB; Q87ZG5; -.
DR   STRING; 223283.PSPTO_3464; -.
DR   GeneID; 1185129; -.
DR   KEGG; pst:PSPTO_3464; -.
DR   PATRIC; fig|223283.9.peg.3545; -.
DR   eggNOG; COG1793; Bacteria.
DR   eggNOG; COG3285; Bacteria.
DR   HOGENOM; CLU_008325_0_1_6; -.
DR   OrthoDB; 9802472at2; -.
DR   PhylomeDB; Q87ZG5; -.
DR   Proteomes; UP000002515; 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:AAO56939.1};
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:UP000002515};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          314..451
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          188..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          528..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   851 AA;  94338 MW;  BFDDFED84CD4153C CRC64;
     MVKPASEYTR KRNFDVTSEP LESKRKGKAR SGALSFVIQK HDARNLHYDF RLELDGTLKS
     WAVPKGPSLD PKQKRLAVHV EDHPLDYAAF EGSIPKGQYG GGDVIVWDRG IWQPHGDPRK
     TYEDGKLKFT LIGEKLSGEW ALVRTRLKGS GSKEQWLLIK EKDDIARPAA EYDITEAQPQ
     SVISGAHVGA GRSAPAKPKA KAVEAKPARK PAPKKAKAVF PDTFAPQLAT LVDAPPAGDW
     LYEIKFDGYR MLTRIQNDEV RLFTRNGNDW TDQLPELTKA LKGLKLQDSW FDGEVVVLDE
     QGLPDFQGLQ NAFDEGHSKN IFYYLFDMPF LSGEDLREVP LEQRRDALKQ VLGSQRSRLL
     RYSDAFQAGH QDIVASAAAM GLEGVIGKRA GSAYVGKRNA DWIKLKCRLR QEFVIVGYTA
     PQGSRSAFGA LLLAVNDDAQ GLVYAGRVGT GFTEATLKHV HKQLKPLHRE ESPLAKKLTS
     AQARGVQWVE PTLVCEAEFA QWTREGIVRQ AAFFGLRGDK PAGDVVREDA QPAEAASVTP
     EPSRQPGKKT ARGKVDVAGT GISHPQRVID STTGTKKIEL AQFYESIADW ILPYLNKRPV
     ALLRCPEGID GEQFFQKHAE HLAIPHIRQL DRALDPGHAA LMEIDSVQAL VGAAQMGAIE
     LHTWGATRDR IETPDHFVLD LDPDPALPWR SMIEATQMVL AVLEELGLEA FLKTSGGKGM
     HIIVPLARQA EWDTVKAFAK AIAEFISRQL PERFTATMGP KNRVGKIFID YLRNSRGGST
     VTAYSVRARP GLPVSVPIAL HELTGLTSSA QWDITNLEQR LSQLKSDPWA GYSNRRKITQ
     KMWKQLGAKQ P
//