ID   B0RRY9_XANCB            Unreviewed;       849 AA.
AC   B0RRY9;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 79.
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=lig2 {ECO:0000313|EMBL:CAP51224.1};
GN   ORFNames=XCCB100_1871 {ECO:0000313|EMBL:CAP51224.1};
OS   Xanthomonas campestris pv. campestris (strain B100).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=509169 {ECO:0000313|EMBL:CAP51224.1, ECO:0000313|Proteomes:UP000001188};
RN   [1] {ECO:0000313|EMBL:CAP51224.1, ECO:0000313|Proteomes:UP000001188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B100 {ECO:0000313|EMBL:CAP51224.1,
RC   ECO:0000313|Proteomes:UP000001188};
RX   PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA   Vorholter F.J., Schneiker S., Goesmann A., Krause L., Bekel T., Kaiser O.,
RA   Linke B., Patschkowski T., Ruckert C., Schmid J., Sidhu V.K., Sieber V.,
RA   Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K., Puhler A.;
RT   "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT   the reconstruction of metabolic pathways involved in xanthan
RT   biosynthesis.";
RL   J. Biotechnol. 134:33-45(2008).
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; AM920689; CAP51224.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0RRY9; -.
DR   KEGG; xca:xcc-b100_1871; -.
DR   HOGENOM; CLU_008325_0_0_6; -.
DR   Proteomes; UP000001188; 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:CAP51224.1};
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          317..410
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          531..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   849 AA;  93976 MW;  CAA30DAEA7367B3B CRC64;
     MSLSEYRRKR SFDKTREPEP GKLLPQGQRA IFVVQLHHAS RRHYDFRLQV GDALKSWAVP
     KGPSYDPAVK RMAVEVEDHP VDYASFEGEI PKGEYGGGHV AQFDHGVWAT AGDPEAQLAK
     GHLRFELFGS KLKGGWHLVR SSKPARQPQW LLFKEDDAYA GTLEADDLLA DVAAAPAEDV
     RRAGAGKAQR KALTTVPVPR ARARNAWTNA ALKLTHARRG DIDDAAFAPQ LAKLGQAPPE
     GAQWVHEIKW DGYRILATVT DGQVRLWSRN ALEWTDKIPD IRDAIQALNL RSARLDGELI
     AGRGTKEDFN LLQATLSGER QVPLALAVFD LLHIDGVEIS EAPLRERKQL LQQILANAPA
     GHLAYSSHVE GDGLEAFRVA GEQHFEGIIS KRADRPYRGG RSDDWRKTKQ LASQEYAVVG
     YTAPKGSRTG FGSLLLATPD PQHGWLYVGR VGSGFSDTLM QEVTQHLHGG GKRPTAHIPT
     EDTDLRGATW FAPRFVVEVF YRGIGGQQLL RQASLKAVRL DKDIADLADS DMGDVSPAQA
     DVADTPARGR KRANKQAPAQ GEPTLSSPTK LIYPDIRATK GDVWDYYHAV MDHLLPEIVG
     RPLSIIRCPN GAEKPCFFQK HHTAGLERVS SVRLKEETGS NAYYLVVEDA PGLLELVQFN
     ALEFHPWGSH AARPDMADRV VFDLDPGPDV PFAEVKRAAT DIRKLLAQLE LESFLRVSGG
     KGLHVVVPLN PGCDWELTKR FAKGFADALA QSEPDRFVAT ATKRFRNKRI FVDYLRNGRG
     ATAVASYSLR GRPGAPVALP LPWSDLAKLH RANAFTLRDV PDKLRRRRKD PWADIAQIQQ
     NLARWADQG
//