ID B0RLL6_XANCB Unreviewed; 1001 AA.
AC B0RLL6;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-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 Name=dnl {ECO:0000313|EMBL:CAP49445.1};
GN ORFNames=XCCB100_0115 {ECO:0000313|EMBL:CAP49445.1};
OS Xanthomonas campestris pv. campestris (strain B100).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=509169 {ECO:0000313|EMBL:CAP49445.1, ECO:0000313|Proteomes:UP000001188};
RN [1] {ECO:0000313|EMBL:CAP49445.1, ECO:0000313|Proteomes:UP000001188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B100 {ECO:0000313|EMBL:CAP49445.1,
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; CAP49445.1; -; Genomic_DNA.
DR AlphaFoldDB; B0RLL6; -.
DR KEGG; xca:xcc-b100_0115; -.
DR HOGENOM; CLU_008325_0_2_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; 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:CAP49445.1};
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 345..454
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1001 AA; 106559 MW; 9797273463DD6B76 CRC64;
MSLRDYTRKR RFDQTPEPAE DAAATAHRQP IFVVQLHHAS SRHYDFRLEA DGVLKSWAVP
KGPSLRAGEK RLAVQVEDHP LAYAGFEGDI PQGQYGAGHV QVFDHGTWHC DGDALAALDA
GKLDFDLQGD KLRGGFAPVR TRLRGRQPQW LLIKRDDAHA ADLDADALVA DSDATAQAIE
TPSAAAAPAR RAKASRRRRT PAEALVTEKS ASASRPRASA ATQAHWRTRA LALPGARDAA
CPTGLRAQLT LLRAEAPDGA QWLHEIKWDG YRLLTDLVDG QAQLRSRNDQ AWTDSFAEVA
TAVQALPVRD ARLDGELVVL DAQGRSDFSA LQRAIDGTAR QPLRYLVFDL LGVAGVDLRA
TPLLERKQLL RALLGETPGT LAYSAHVIGR GPEVFAASAD KGWEGIVSRR ADAPYRGGRS
ADWVKTKHED SDEFVVVGYT DPKGARSGFG ALLLAQLDGT QLRYVGRVGT GFDSALLGEI
TAQLQALHSP QPTLELPAHI PGRPRDVHWV RPVLIAEVAF RGWAKQGLLR QAAFKRLRED
KPMSDLGGDR ATPGKSRGAR TRTAAAAAGK ASRAAATRTA AVSAGGSAAK PGKAGKSSTA
ADVSTPSRVA KQRVTPAASS AAKPGKPGKS SAAATGNASP RVAKRGAVSA ASASSAAKSG
KRSVSSESAA SGKPAAPAKA ASSKTARAPG MSSAKETSTA PAAPSTRKAK ALASAAPDGV
AITHPERVVF PAAGISKGDV AAYYRAVAPL VLPEIARRPL SLLRCPDGAA GMCFFQKHEG
RHLGAHIKAI PLKQKSGTED YLYIEDVAGL LELVQMNTLE LHPWGARVDD PEHPDRLVFD
LDPGDGVAWT QVVAAAREIR SKLRAAGLES AVRLSGGKGL HVVVPIVPQA SWDQARDFCE
AFAQALATQA PERYVATMSK AKRHGVIFVD WLRNGRGNTS VCSWSLRARE HATVAVPLRW
EELGKLSGPD AFPLDKAVQR AKRQRNDPWA EVLALKQVLP G
//
