ID Q11J79_CHESB Unreviewed; 845 AA.
AC Q11J79;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 24-JAN-2024, entry version 98.
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=Meso_1150 {ECO:0000313|EMBL:ABG62546.1};
OS Chelativorans sp. (strain BNC1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Chelativorans.
OX NCBI_TaxID=266779 {ECO:0000313|EMBL:ABG62546.1};
RN [1] {ECO:0000313|EMBL:ABG62546.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BNC1 {ECO:0000313|EMBL:ABG62546.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of chromosome of Chelativorans sp. BNC1.";
RL Submitted (JUN-2006) 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; CP000390; ABG62546.1; -; Genomic_DNA.
DR AlphaFoldDB; Q11J79; -.
DR STRING; 266779.Meso_1150; -.
DR KEGG; mes:Meso_1150; -.
DR eggNOG; COG1793; Bacteria.
DR eggNOG; COG3285; Bacteria.
DR HOGENOM; CLU_008325_0_0_5; -.
DR OMA; NWLLIKG; -.
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 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; 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:ABG62546.1};
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 334..469
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 845 AA; 93528 MW; F03B77FC10FAFC6A CRC64;
MALTTYRRKR NFSATPEPPG EEKASPRGDS FVIQKHAARR LHYDLRLEMD GVLKSWAVTR
GPSLVPGEKR LAVHVEDHPL DYGDFEGTIP KGEYGGGTVI VWDRGSWSPI GDAKKGYAKG
HLEFELHGEK LTGRWHLVRM AKKPREKKEN WLLIKGEDDA ARSEADPDIL EERPESVKTG
RVIEEVEGEA PGWSSKTGRI EQPAEAKPAR KKRATKAGSE KSAGEKISVP KRAKKAGYPG
FIEPALATLR STPPPGGRWL HEIKFDGYRL QAHIRDGKAR LLTRSGLDWT EKFGDAIVTA
LGSLPVRQAI MDGELIVEGA GGASDFSALQ AALSEGRVDR MALYLFDLLY LDGYDFRPVP
LAERKATLQK LLDGAPPVLR YSEHFEEDGE LVFRHACRLS LEGIVSKAGD AAYRSGRGKD
WIKSKCSMRQ EFVVAGYVPS TTSNRAIGSL VLGYYENERL IYAGRVGTGF SHALAQDLFK
RLDKMRIAKS PFAKKLTSEE ARGAKFVRPE LVAEVEFRTW TADNLIRHAS FRGLREDKSA
TDVTRETNQS KPAERAAPAI RLTHPDRIYW KDAGVTKQGL SDYYAEVWPR MGPFIVNRPL
ALVRCPDGVE GQCFFQKHAW RGQSHEIMKA VDPEDDEPII AIDGLPGLIG LVQGGTLEIH
PWGSQLEDLE RPDLINMDLD PGPDVTWQDV IDAAREVRER LAQAGLESFV KTSGGKGLHV
VAPLKPRADW PEVKAFAKGI ADAMASDTPE RFVATVTKAK RKGKILVDYL RNGRGATAVA
PYSTRARAGA AVSMPLFWEE LSPAITADYF TVANAPTRLA AIGKDPWEDF WRAAVPLGRK
ARRAA
//