UniProt: A0A4T2C395

Database: UniProt
Entry: A0A4T2C395_9MICO

LinkDB:  A0A4T2C395_9MICO 
Original site:  A0A4T2C395_9MICO

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (8)   
   Pfam (4)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (25)   

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ID   A0A4T2C395_9MICO        Unreviewed;       860 AA.
AC   A0A4T2C395;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   18-JUN-2025, 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=D4765_09115 {ECO:0000313|EMBL:TIH36896.1};
OS   Subtercola vilae.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Microbacteriaceae; Subtercola.
OX   NCBI_TaxID=2056433 {ECO:0000313|EMBL:TIH36896.1, ECO:0000313|Proteomes:UP000306192};
RN   [1] {ECO:0000313|EMBL:TIH36896.1, ECO:0000313|Proteomes:UP000306192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DB165 {ECO:0000313|EMBL:TIH36896.1,
RC   ECO:0000313|Proteomes:UP000306192};
RX   PubMed=31018526;
RA   Villalobos A.S., Wiese J., Imhoff J.F., Dorador C., Keller A.,
RA   Hentschel U.;
RT   "Systematic Affiliation and Genome Analysis of Subtercola vilae DB165(T)
RT   with Particular Emphasis on Cold Adaptation of an Isolate from a High-
RT   Altitude Cold Volcano Lake.";
RL   Microorganisms 7:0-E107(2019).
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   -!- SIMILARITY: In the C-terminal section; belongs to the ATP-dependent DNA
CC       ligase family. {ECO:0000256|ARBA:ARBA00049981}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the LigD polymerase
CC       family. {ECO:0000256|ARBA:ARBA00049990}.
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:TIH36896.1}.
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DR   EMBL; QYRT01000014; TIH36896.1; -; Genomic_DNA.
DR   RefSeq; WP_136641993.1; NZ_QYRT01000014.1.
DR   AlphaFoldDB; A0A4T2C395; -.
DR   OrthoDB; 9802472at2; -.
DR   Proteomes; UP000306192; 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; 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; 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   InterPro; IPR052171; NHEJ_LigD.
DR   NCBIfam; TIGR02777; LigD_PE_dom; 1.
DR   NCBIfam; TIGR02778; ligD_pol; 1.
DR   NCBIfam; TIGR02779; NHEJ_ligase_lig; 1.
DR   NCBIfam; NF007210; PRK09632.1; 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   3: Inferred from homology;
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:TIH36896.1};
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:UP000306192};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          636..758
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          306..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   860 AA;  92790 MW;  25DF161727C2CF8E CRC64;
     MAATKKSGAG ASAGAGDEVV VSVGGHRLKL THLEKVLYPE TGTTKADVLQ YYSAIADVML
     PHVRDRAATR KRWVNGVGTE AHPGQMFFQK NLDDGTPSWV KRRTIAHSDH DNEYPLVNDL
     ATLTWLAQIA ALEVHVPQWR FGRAGAALNP DRLVLDLDPG DGVGLPECAE VARFARTILQ
     GMGLEPFPVT SGSKGIHLYA ALDGSQSSEQ VSAVAHELAR VLEADHPELV VSDMKKSLRV
     GRVLVDWSQN SAAKTTVAPY SLRGRSRPTV AAPRTWRELA SASLAQLDYT EVLARVKRRG
     DPLAEGLGEQ LGEQRAASPA VDGSVPDAQQ PDRLHTYRSM RDASKTPEPV PDARPATTAG
     NSFVIQKHDA SRLHYDFRLE HDGVLVSWAI PKGPPTKSGQ NHLAVQTEDH PLEYGSFEGT
     IPKDEYGGGT VEIWDAGTYD LEKWRDGREI IATLHGTKAG GLGGDRKFAL IHTGSGKGAK
     AEQNWLIHLM QPQYSAASEK RHAHLPPQPD DEAPALNAAL AAADTPAKPI APMLATLGAA
     ADFADHSDAD DWAYEMKWDG IRAIATLDSR GVRLASRNGH DITAQYPDLA VPLAAALGSH
     EAVVDGEIVA FDPSGRPSFS RLQQRMNLQG EADVKRAVAA VTVHLVLFDI VHLDGRSLVR
     ETYDSRRALL ESTVTPDARS LVVVPAAFAG DFDAAFASSK QLGLEGVVAK KHDGSYGPGR
     RSHSWVKLKH HRTQEVVVGG WRPGSGRRAG GVGSLLLGIP GSDGQLQYVG RVGTGFSDAD
     VTRLAERFEG RGRASSPFVE VPRDVAADAH WLDPFRGPSH GPSFVGEVEF AEWTASQHLR
     QPVWRGWRAD KSPGDVVRES
//

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