ID A0A2T6FP16_9GAMM Unreviewed; 894 AA.
AC A0A2T6FP16;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=B0W54_06700 {ECO:0000313|EMBL:PUA30195.1};
OS Cellvibrio sp. 79.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1954207 {ECO:0000313|EMBL:PUA30195.1, ECO:0000313|Proteomes:UP000243979};
RN [1] {ECO:0000313|EMBL:PUA30195.1, ECO:0000313|Proteomes:UP000243979}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=79 {ECO:0000313|EMBL:PUA30195.1};
RA Zhang Y., Xu J., Wang N.;
RT "Cellvibrio sp. 79 recovered from metagenome.";
RL Submitted (FEB-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:PUA30195.1}.
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DR EMBL; MVDH01000001; PUA30195.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6FP16; -.
DR Proteomes; UP000243979; 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 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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
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:PUA30195.1};
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:UP000243979};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 40..145
FT /note="DNA ligase D 3'-phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF13298"
FT DOMAIN 249..425
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|Pfam:PF01068"
FT DOMAIN 444..541
FT /note="DNA ligase ATP-dependent C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04679"
FT DOMAIN 618..871
FT /note="DNA ligase D polymerase"
FT /evidence="ECO:0000259|Pfam:PF21686"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 842..869
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 894 AA; 99702 MW; D1521A32645F0F13 CRC64;
MTKPLREYHR KRNFDVTTEP RGDVQGKGKS PAHALQFVIQ KHDARRLHYD FRLELNGTLL
SWAIPKGPSL DPTDKRLAVH VEDHPLDYAS FEGHIPEGHY GGGDVIVWDR GIWEPVGDAT
AGYKSGKLKF VLIGEKLTGQ WTLVRTNLRG SGDKEQWLLI KERDDSARAS EEYDIVVELP
QSVVSGAVID PDKKKKNKIS VSTATPKAVT KKNATSKTSA AATKKPKTPV ARSAQKIKLP
DMLSPELATL VSEPPEGEWL YEIKFDGYRM LARIEDGKVK LITRNGNDWT ERLPLQANAI
ANLELHDSWL DGEIVVLNEK GVPDFQALQR AFEIGSSQHI LYYLFDAPFL NGVDMRAVPV
EERRAAVQKI IPNKAKNPLR FSAAFLADHR NIVESACALS LEGVIGKRAG SSYTSRRSPD
WIKLKCRLRQ EFVIVGFTKP RGSRSGFGAL LLGVYSRQNP ADLTYVGRVG TGFNETRLKQ
LHEKLKTLEI KKSPFAHDLS GALTRDVQWV KPTLVCEVEF AEWTGDNILR QAVFIALRTD
KPADEIIREQ AIKPGASNKD ETQKKSTATN KSRAGSSTSN STAAPAKSIN KIENSGANIA
GIKITNPDRI IDSESGSTKL ALAQFYDYVS PWLLPHLHDR PVSLLRAPEG VGGEQFFQKH
AEHMAIPHIH HLDQALDPGH ARLMQIDNTA ALVGCAQMST IELHTWGSTS DNIETPDRII
FDLDPDPSLP WRSVVEATRL TLAVLEELKL DAYLKTTGGK GLHIVVPLAR QLGWEYIKEF
SKSLSQFMAK QIPERFVAKM GPQNRIGKIF IDYLRNQRGA STVSAYSVRA RLGLPVSVPI
TLDELLTLKS SAQWNINNLQ ERLDKQKVDP WKGYKHRQKI TATMWKKLGV KAPL
//
