ID V9WXQ7_9PSED Unreviewed; 830 AA.
AC V9WXQ7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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:AHD14574.1};
GN ORFNames=C163_12780 {ECO:0000313|EMBL:AHD14574.1};
OS Pseudomonas sp. FGI182.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1259844 {ECO:0000313|EMBL:AHD14574.1, ECO:0000313|Proteomes:UP000018783};
RN [1] {ECO:0000313|EMBL:AHD14574.1, ECO:0000313|Proteomes:UP000018783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGI182 {ECO:0000313|EMBL:AHD14574.1,
RC ECO:0000313|Proteomes:UP000018783};
RG DOE Joint Genome Institute;
RA Currie C., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) 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; CP007012; AHD14574.1; -; Genomic_DNA.
DR RefSeq; WP_025339089.1; NZ_CP007012.1.
DR AlphaFoldDB; V9WXQ7; -.
DR PATRIC; fig|1259844.3.peg.2500; -.
DR HOGENOM; CLU_008325_0_1_6; -.
DR Proteomes; UP000018783; 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:AHD14574.1};
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 305..411
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 830 AA; 92590 MW; AA7880F30F67E579 CRC64;
MAKPLQEYAR KRDFNATPEP SGKRSRGKRA HALQFCIQKH DASHLHYDFR LELDGTLKSW
AIPKGPSLDP KVRRLAVHVE DHPLDYADFE GHIPEGHYGA GDVIVWDRGI WEPEGDAREA
YAKGKLRFRL QGEKLTGVWN LFRTHLAGKK EQWMLVKSHD SQARSEADYS IVDAQPDSVL
SDRTLVPRKP AAKKAAAPRR KTASKGRKVP LPAQLQPQLA TLVDSPPSGD WRYEVKFDGY
RILARIDGDD VRLFTRNGHD WSGKMPRQVA ALRALGLDSA WLDGEVVVAG EDGAADFQAL
QNAFDTEHDE HITYYLFDLP FLGGQDLRHL PLQDRRNTLQ QLLEHNESDV LKYSADFDQP
VESLLDSACR LQLEGLIGKR VDSPYSGRRS PDWIKLKCKQ RQEFVIAGYT DPKGSRSGFG
ALLLALHDND SGELRYAGKV GTGFSATTLA SIHARLKPLE IARPALPNPP TGAEARGVHW
LKPQLLAEVA YAQMTRDGIV RHSVFHGLRD DKPATAIDLE RSMPAKTLPK RKQAKAPEAL
GELRLTHPER VVDATSGVTK REVAEYYAAV SQWILPQLEH RPVALVRAPD GLAGELFFQK
NAGQLHLPNV LSYDKAEAGQ AAMVVNRADT LLGAVQMNMI ELHTWNATDK DFDKPDRFVL
DLDPDPALPW KAMLEATQLA LTLLDELGLK VFLKTSGGKG MHLVVPLTRR ASWDEVKAFS
HGIVDYLARL FPDRLSAVSG PKNRIGRIFI DYLRNGKGAT TACAYTLRAR EGLPVSVPIW
REELPQLKGA NQWNIGNVLE RLGEVDDPWA EYGKTRQSIT VGMRKQLGLA
//
