UniProt: A0A143QFK0

Database: UniProt
Entry: A0A143QFK0_9NOCA

LinkDB:  A0A143QFK0_9NOCA 
Original site:  A0A143QFK0_9NOCA

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (14)   
   InterPro (8)   
   Pfam (4)   
   PROSITE (2)   
Literature (1)   
   PubMed (1)   
All databases (27)   

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ID   A0A143QFK0_9NOCA        Unreviewed;       765 AA.
AC   A0A143QFK0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
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=A3Q40_03914 {ECO:0000313|EMBL:AMY21262.1};
OS   Rhodococcus sp. PBTS 1.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1653478 {ECO:0000313|EMBL:AMY21262.1, ECO:0000313|Proteomes:UP000076180};
RN   [1] {ECO:0000313|EMBL:AMY21262.1, ECO:0000313|Proteomes:UP000076180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBTS 1 {ECO:0000313|EMBL:AMY21262.1,
RC   ECO:0000313|Proteomes:UP000076180};
RX   PubMed=27284129;
RA   Stamler R.A., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.J.;
RT   "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT   Draft Sequences for Rhodococcus Isolates PBTS 1 and PBTS 2.";
RL   Genome Announc. 4:0-0(2016).
RN   [2] {ECO:0000313|Proteomes:UP000076180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBTS 1 {ECO:0000313|Proteomes:UP000076180};
RA   Stamer R., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.;
RT   "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT   Draft Sequences for Rhodococcus spp. Isolates PBTS 1 and PBTS 2.";
RL   Submitted (APR-2016) 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; CP015219; AMY21262.1; -; Genomic_DNA.
DR   RefSeq; WP_068104640.1; NZ_CP015219.1.
DR   AlphaFoldDB; A0A143QFK0; -.
DR   STRING; 1653478.A3Q40_03914; -.
DR   KEGG; rhu:A3Q40_03914; -.
DR   PATRIC; fig|1653478.3.peg.3972; -.
DR   Proteomes; UP000076180; 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; cd04863; MtLigD_Pol_like; 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; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR014146; LigD_ligase_dom.
DR   InterPro; IPR014144; LigD_PE_domain.
DR   InterPro; IPR014145; LigD_pol_dom.
DR   InterPro; IPR033649; MtLigD_Pol-like.
DR   InterPro; IPR012340; NA-bd_OB-fold.
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; PS00333; DNA_LIGASE_A2; 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};
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:UP000076180};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          563..674
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          295..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..325
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   765 AA;  83955 MW;  AF9EE939C1A54B8D CRC64;
     MPPAGSTRRE IDGHTLAFTN PDKVLYPETG TTKAEVIDYY LAVADAMLPH LAGRPVTRKR
     WPNGVDHPAF FEKNLAASAP DWLDRRRIHH SDRVVVYPVF HGPADLAWLG QQAALEAHVP
     QWTFDRDEQG KATRIVFDLD PGDDVDLDTC ATVACAVRTM VTDIGLTAFP LTSGSKGIHL
     YVPLEKPVTS AGASTVAKRV ATLLEGTMPD LVTASMSKAL RPGKVFLDWS QNNGKKTTIA
     PYSLRGRSRP TVAAPRTWEE IEGGGLTQLA FTEVIDRLHR DGDLLADLDA AVPGGTADRL
     GPYRGKRTTS RTPEPVPTGT TPESRSAATT FVIQEHHARR LHYDFRLERD GVLVSWAVPK
     NLPTDTTSNH LAVHTEDHPL DYATFEGTIP AGEYGGGEVT VWDHGTYIEE KWRDDEVIVT
     LTGERVSGRY ALIRTGGDQW LVRRTKTTAS GVPQGDTALP TRVRPMLATA GELDALDADQ
     WSFEGKWDGV RVVATVDHGR TLLESRTGQD LTRRYAGITA LGADLADHVV VLDGEAVVYR
     ADGVTSFEAL QDAHPDDVQY ICFDILHLDG TDLTNKKFAD RRRILELLLT GIESATLSPL
     MAGTPAGALA ESERRGWEGI VAKRRDSVYE VGRRSTAWIK VKNWRTQEVV IGGWRAGKGG
     RAGSIGSLLL GVPEGDGLRY VGRVGTGFTE RARADLLDRL RPLARDDSPF DRPLPAVDRK
     DATWTEPALV GEVRFFEWTE GGSLRHPSWR GLRDDKSPAD VVREP
//

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