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Database: UniProt/TrEMBL
Entry: E6WT36_PSEUU
LinkDB: E6WT36_PSEUU
Original site: E6WT36_PSEUU 
ID   E6WT36_PSEUU            Unreviewed;       932 AA.
AC   E6WT36;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
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=Psesu_1418 {ECO:0000313|EMBL:ADV27265.1};
OS   Pseudoxanthomonas suwonensis (strain 11-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=743721 {ECO:0000313|EMBL:ADV27265.1, ECO:0000313|Proteomes:UP000008632};
RN   [1] {ECO:0000313|EMBL:ADV27265.1, ECO:0000313|Proteomes:UP000008632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11-1 {ECO:0000313|Proteomes:UP000008632};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Ovchinnikova G., Siebers A.K., Allgaier M., Thelen M.P.,
RA   Hugenholtz P., Gladden J., Woyke T.;
RT   "Complete sequence of Pseudoxanthomonas suwonensis 11-1.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002446; ADV27265.1; -; Genomic_DNA.
DR   RefSeq; WP_013535093.1; NC_014924.1.
DR   AlphaFoldDB; E6WT36; -.
DR   STRING; 743721.Psesu_1418; -.
DR   KEGG; psu:Psesu_1418; -.
DR   eggNOG; COG1793; Bacteria.
DR   eggNOG; COG3285; Bacteria.
DR   HOGENOM; CLU_008325_0_1_6; -.
DR   OrthoDB; 9802472at2; -.
DR   Proteomes; UP000008632; 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; 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   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:ADV27265.1};
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:UP000008632};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          316..408
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          172..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          553..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          610..648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        624..648
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   932 AA;  102485 MW;  111D22BB41D02997 CRC64;
     MSLVDYRRKR SFDRTREPEP GKPAPRGQRP IFVVQLHHAS RRHYDFRLQV GDALKSWAVP
     KGPSYDPSVK RMAVEVEDHP LDYAGFEGDI PKGEYGGGHV ARFDHGVWST AGDPEEQLAK
     GHLRFELFGD RLKGGWHLVR SGKPARQPQW LLFKDKDGWA GTLEADDLLA EVTPPPEADR
     KRAGSGKAKP RRLAAVPAPR ARRKDWKKRA LALDGSRAAD APDGPFQPQL ARLGQAAPEG
     EQWLHEIKWD GYRILATVEE GEVRLWSRNA LEWTDRVPEI RDAVKALGLR SAALDGELIA
     GSGTREDFNL LQATLSGERP GTLAYVLFDL LHVDGVDITE ASLLERKELL QAVLEKGPAH
     LAYSSHIPGD GRQAIALAAE RHFEGIISKR ADRPYRPGRG DDWRKTKQLA SDEFAIVGYT
     APQGSRTGFG SLLLARPDAK HGWRYVGRVG TGFSDEMLRE LAPRLAKDTS SKPTAHVDTM
     DTALRRATWV PPRMVVEVFY RGIGGQQLLR QASLKTLRPD KDIEDLYDSD RGPGVAEETV
     MAAKGKAATK KTAATKGGAG KTATAKTATK KAPAREAVAK GAPTKAAKKA VKAPAEKAAA
     KAAKTSASKI VGKTPGAKTG ASRAATPTKA SAGTSRKRAT TPQDWPRLSS PTKVLFPDIR
     ATKQEVWDYY AAVMDHLLPE IVGRPLSVIR CPSGTGRQCF FQKHLTAGLE RVASVKLKEE
     SGTNAEYLVV EDEGGLMELV QFNALEFHPW GSHADNPDHA DRVVFDLDPG PDVPFAEVKK
     AAVDIRRQLE ALELASFLRV TGGKGLHVVV PLAPGCDWEL TKRFAHGFAD ALARSEPDRF
     VATATKSLRN RRIFVDYLRN GRGATAVASY SLRARPGAPV AMPIAWNELA RLPRADVYTM
     RDVPERLRRR RKDPWEGIDG LRQNLARWAR DE
//
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