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NFI_THEPD
ID   NFI_THEPD               Reviewed;         232 AA.
AC   A1RY04;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Endonuclease V {ECO:0000255|HAMAP-Rule:MF_00801};
DE            EC=3.1.21.7 {ECO:0000255|HAMAP-Rule:MF_00801};
DE   AltName: Full=Deoxyinosine 3'endonuclease {ECO:0000255|HAMAP-Rule:MF_00801};
DE   AltName: Full=Deoxyribonuclease V {ECO:0000255|HAMAP-Rule:MF_00801};
DE            Short=DNase V {ECO:0000255|HAMAP-Rule:MF_00801};
GN   Name=nfi {ECO:0000255|HAMAP-Rule:MF_00801}; OrderedLocusNames=Tpen_0682;
OS   Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermofilales; Thermofilaceae;
OC   Thermofilum.
OX   NCBI_TaxID=368408;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2475 / Hrk 5;
RX   PubMed=18263724; DOI=10.1128/jb.01949-07;
RA   Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA   Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA   Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA   Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT   "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT   biosynthetic pathways without genome reduction.";
RL   J. Bacteriol. 190:2957-2965(2008).
CC   -!- FUNCTION: DNA repair enzyme involved in the repair of deaminated bases.
CC       Selectively cleaves double-stranded DNA at the second phosphodiester
CC       bond 3' to a deoxyinosine leaving behind the intact lesion on the
CC       nicked DNA. {ECO:0000255|HAMAP-Rule:MF_00801}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage at apurinic or apyrimidinic sites to
CC         products with a 5'-phosphate.; EC=3.1.21.7;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00801};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00801};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00801}.
CC   -!- SIMILARITY: Belongs to the endonuclease V family. {ECO:0000255|HAMAP-
CC       Rule:MF_00801}.
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DR   EMBL; CP000505; ABL78084.1; -; Genomic_DNA.
DR   RefSeq; WP_011752349.1; NC_008698.1.
DR   AlphaFoldDB; A1RY04; -.
DR   SMR; A1RY04; -.
DR   STRING; 368408.Tpen_0682; -.
DR   EnsemblBacteria; ABL78084; ABL78084; Tpen_0682.
DR   GeneID; 4601882; -.
DR   KEGG; tpe:Tpen_0682; -.
DR   eggNOG; arCOG00929; Archaea.
DR   HOGENOM; CLU_047631_1_1_2; -.
DR   OMA; RIHFRQA; -.
DR   OrthoDB; 80668at2157; -.
DR   Proteomes; UP000000641; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043737; F:deoxyribonuclease V activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   CDD; cd06559; Endonuclease_V; 1.
DR   HAMAP; MF_00801; Endonuclease_5; 1.
DR   InterPro; IPR007581; Endonuclease-V.
DR   PANTHER; PTHR28511; PTHR28511; 1.
DR   Pfam; PF04493; Endonuclease_5; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA damage; DNA repair; Endonuclease; Hydrolase; Magnesium;
KW   Metal-binding; Nuclease; Reference proteome.
FT   CHAIN           1..232
FT                   /note="Endonuclease V"
FT                   /id="PRO_1000047006"
FT   BINDING         43
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
FT   BINDING         109
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
FT   SITE            79
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
SQ   SEQUENCE   232 AA;  25905 MW;  9ECA368C803B57BF CRC64;
     MRVHRLPENF SLERARRAQL AIARMVLEED SLPESVRRAA GVDVAFKGDY AFAAAVVVEY
     PSFSVVDYSV TRTEVRFPYV PTLLAFREVW PAYTALKRLK SEPDVLLVDG NGRLHPFKAG
     FACHLGVLVD KPTIGVAKKL LVGEVGSWKS GVAPVLYRGE VLGMAVKTSE RSKPVFVSIG
     HKISLNTAVW IVRMFTKRGL RLPEPLRLAH LYATAYARGN MEEKDFYLDE PS
 
 
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