ID A0A1V1V2A6_9CAUL Unreviewed; 854 AA.
AC A0A1V1V2A6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=SH203_02659 {ECO:0000313|EMBL:GAW42243.1};
OS Brevundimonas sp. SH203.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=345167 {ECO:0000313|EMBL:GAW42243.1, ECO:0000313|Proteomes:UP000195546};
RN [1] {ECO:0000313|EMBL:GAW42243.1, ECO:0000313|Proteomes:UP000195546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH203 {ECO:0000313|EMBL:GAW42243.1,
RC ECO:0000313|Proteomes:UP000195546};
RA Suzuki T., Kikuchi M., Habu N., Konno N.;
RT "Draft Genome Sequence of Brevundimonas sp. SH203, producing Cellouronate
RT (beta-1,4-linked polyglucuronate) lyase.";
RL Submitted (MAR-2017) 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};
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:GAW42243.1}.
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DR EMBL; BDMM01000006; GAW42243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V1V2A6; -.
DR OrthoDB; 9802472at2; -.
DR Proteomes; UP000195546; 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 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; 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:GAW42243.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000195546};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 317..412
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 197..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 854 AA; 91853 MW; FFFEC9FE772C454D CRC64;
MRGELKTYRA KRRFGETPEP KGAKGGRSKG GLRYLIQRHA ATRLHYDFRI EADGVLKSWA
VTKAPSRDTA VKRLAVEVED HPLDYGAFEG TIPDGNYGAG TVQMWDVGTW EPQEPDLEAA
WARGQIKMIL HGERLKGKWA LIRLKNDRGK PSKRNNWLLL KEKDDFAVAG EGDALAEIDA
SVTTGRSLAE IADGTKAWTA SRPTGRKGPA KPRPSKAAAK AKKPPAFAPI QLCKVADHPP
GGAGWAHEIK FDGYRLQIGV GGGRAVLRTR KGLDWSDRFP DLTAEAATWP DAVIDGELCA
LDDDHRPDFG ALQAAISDEK TGGLVYFAFD LLFEGAEDLR KLPLSHRKAR LQAYVDRIGK
GRGGRLRYVE HFASTGQAVL ESACRMDLEG VISKKLEAPY HAGRSSTWLK SKCRGRDEVV
IGGWSSEGGT RFRSLLVGVK GRGGLRYLGR VGTGYGEAVV KTLVPALKGA AADRSPFVGA
GVPKTAKDIH WVRPVLVAEV EHGGYTEAGS LRQAAFKGLR DDKAAAEVTE APQPPADMGD
AKKTTTTVRP AGKPGKVVVA GVTISSPDKV LWPGSGDRPA ITKADLARYY EAAAERLLAH
VADRPTSIIR APEGIGGETF FQRHAMAGSN PRLKLIDVKA RTPYVAAVDV GGLVAIAQSG
GLELHPWGCA PGRPETPEQI TFDLDPDAGL DFGDVIAAAR GVKTRLEALG LPAFVKTTGG
KGLHVVVPIK SDARSRVTWD QNKAFAKAVA DAMRAEAPDR FTTTLAKKAR GGKIFIDYLR
NGRMATAVAP WSPRARPGAG IAFPLSWGQV KAGLDPAAFN LWTYEALLKK PDPWADFRAS
AVSLKSALKK MGVP
//
