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Database: UniProt
Entry: V4QJQ6_9CAUL
LinkDB: V4QJQ6_9CAUL
Original site: V4QJQ6_9CAUL 
ID   V4QJQ6_9CAUL            Unreviewed;       657 AA.
AC   V4QJQ6;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-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   ORFNames=AEYBE204_10425 {ECO:0000313|EMBL:ESQ79413.1};
OS   Asticcacaulis sp. YBE204.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=1282363 {ECO:0000313|EMBL:ESQ79413.1, ECO:0000313|Proteomes:UP000017808};
RN   [1] {ECO:0000313|EMBL:ESQ79413.1, ECO:0000313|Proteomes:UP000017808}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YBE204 {ECO:0000313|EMBL:ESQ79413.1,
RC   ECO:0000313|Proteomes:UP000017808};
RX   PubMed=24463524; DOI=10.1038/nature12900;
RA   Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT   "Sequential evolution of bacterial morphology by co-option of a
RT   developmental regulator.";
RL   Nature 506:489-493(2014).
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:ESQ79413.1}.
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DR   EMBL; AWGF01000005; ESQ79413.1; -; Genomic_DNA.
DR   RefSeq; WP_023462379.1; NZ_AWGF01000005.1.
DR   AlphaFoldDB; V4QJQ6; -.
DR   STRING; 1282363.AEYBE204_10425; -.
DR   PATRIC; fig|1282363.3.peg.2034; -.
DR   OrthoDB; 9802472at2; -.
DR   Proteomes; UP000017808; 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; 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; 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; 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};
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:UP000017808};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          110..244
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   657 AA;  73527 MW;  BDC9005DFB26ADD2 CRC64;
     MDDQGYRRKA RTTATLEFRE LELATLADAV PRGPDWVHEV KFDGYRTLTV IEAGKVTMYS
     RSGLDWTPKY RDIAKRLTAL KIDNAILDGE IVALNDQGAS SFSRLKAELS AGRSDELQYY
     VFDLLVLNGE DLTAFPLLDR KTRLEKLIQT ADFQNHVIYS EHFAENKNFL PHLCSLDMEG
     IISKRIDAPY RGGRGKTWLK VKCHKRQEFV IVGFTESTHA GRGFRSLLLG YYDGSTLKFA
     GKVGTGFNSD TLVDIRKKLN ALKVVPKPIS KLPPDVGHGT WVEPTLVCEV EFTEWTPEGR
     LRHPSFQGMR EDKPAKGLGR DKAVPVKAAI KAAEAEVKAE SVAPKPRHPS APLKSTDRVD
     VGGIGISHPA RVVFPGLGIT KLELAQFYER ITDRILPHIA NRPLSIVRAP DNVDGQQFFQ
     RHLPERGGLK HVEAVEVPVK DRTEAYMQIT DSQGLLALVQ WGGIEFHPWG SHSDRPTLPD
     RMIFDLDPDP EAPWENVIDG AAEVRDRMAE FGLQSFLKTT GGKGLHVVVP MTPKYGWPAI
     KAFTRAIAES MATDSPTRFI ANMSKAKRKG RIFIDYLRND LTSTAAAAFS VRARPGAGVS
     TPLFWKELTP MLIPGDYTMH TLQDRLKKQK TDPWADYFEI KQSLRPEILK ALKIAVE
//
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