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Database: UniProt/TrEMBL
Entry: B0T3L2_CAUSK
LinkDB: B0T3L2_CAUSK
Original site: B0T3L2_CAUSK 
ID   B0T3L2_CAUSK            Unreviewed;       918 AA.
AC   B0T3L2;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 78.
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=Caul_1769 {ECO:0000313|EMBL:ABZ70898.1};
OS   Caulobacter sp. (strain K31).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=366602 {ECO:0000313|EMBL:ABZ70898.1};
RN   [1] {ECO:0000313|EMBL:ABZ70898.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K31 {ECO:0000313|EMBL:ABZ70898.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Stephens C., Richardson P.;
RT   "Complete sequence of chromosome of Caulobacter sp. K31.";
RL   Submitted (JAN-2008) 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; CP000927; ABZ70898.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0T3L2; -.
DR   STRING; 366602.Caul_1769; -.
DR   KEGG; cak:Caul_1769; -.
DR   eggNOG; COG1793; Bacteria.
DR   eggNOG; COG3285; Bacteria.
DR   HOGENOM; CLU_008325_0_1_5; -.
DR   OMA; YMANLGC; -.
DR   OrthoDB; 9802472at2; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   CDD; cd07906; Adenylation_DNA_ligase_LigD_LigC; 1.
DR   CDD; cd07971; OBF_DNA_ligase_LigD; 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   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; BIFUNCTIONAL NON-HOMOLOGOUS END JOINING 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:ABZ70898.1};
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          387..478
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          224..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..241
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..289
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   918 AA;  99514 MW;  BBAF046B0C04F1DE CRC64;
     MAQGQLAEYR RKRDFQKTAE PSGDAAVASA PHARFVIQKH DATRLHYDFR LEVDGVLKSW
     AVTKGPSLDP ADKRLSVEVE DHPLDYGDFE GTIPKGQYGG GTVQLWDRGY WAPEPGFEDV
     AKALKKGELK FVLEGERLHG SWVLVRMNWD RNAKDGPKRQ VGGGRSNWLL IKHNDEAARP
     GEGAAVLEED ASIASGRTMS DIAAGKGKGP SAFILKTKGK GDAVWTSRTK AEREALQKEA
     QDTRAVEPTP SRLPGEGQDP DSSGESAGRH LGPGLRRGDG DKATKKAKAK TAVLPDFIEP
     QLCKSLDRPP SGPGWAHEIK FDGYRVQLRV EGGRATLRTR KGLDWTEKFA AIARAAADLP
     DSIIDGEVVA LDAAGQPDFA GLQAALSDGK TGDLIFFAFD LLAEGGEDLR ALPLHERKAR
     LKAMMGEDEP RLRFVDHFET AGDAVLLSAC KLELEGIISK RLDAPYRSGR SETWTKAKCR
     AGHDVVIGGY TTTGSAFRSL IAGVMRDGKL THVGRIGTGF GRDKVGKLLP RLKALETDTS
     PFEGKGAPRK ADDIHWVKPE LVAEIEYAGF TGDGSIRQAS FKGLREDIPA SEVQAEVPAK
     AETAELATPT PKAAPKSQTI ATAKTDSIVL GVTISKPDKP LWPDVDGAPG TKIDLARYMA
     AIGDWMLPHV KGRPASIIRV PDGIGGETFF QRHAMRGMSS LIDLVSVKGD KQPYIQFNRV
     EALIAAAQIA AVEIHPWNCQ PGDPEVAGRL VFDLDPAPGV TFEDVIAGAR EIRDRLEELG
     LVSFCKTTGG KGLHVVTPLS DKVEWAVAKT FAREVCARMA ADAPDKYLIT MSKKAREGRI
     FLDYLRNDRT STAVAPLSAR ARPGATVSMP LNWTQVKAGL DPTKYTIRTV PDLIAKSRAW
     EDYFDAAKPL KAAIKRLG
//
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