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Database: UniProt
Entry: N9XNG7_9CLOT
LinkDB: N9XNG7_9CLOT
Original site: N9XNG7_9CLOT 
ID   N9XNG7_9CLOT            Unreviewed;       278 AA.
AC   N9XNG7;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   22-APR-2020, entry version 38.
DE   RecName: Full=Probable endonuclease 4 {ECO:0000256|HAMAP-Rule:MF_00152};
DE            EC=3.1.21.2 {ECO:0000256|HAMAP-Rule:MF_00152};
DE   AltName: Full=Endodeoxyribonuclease IV {ECO:0000256|HAMAP-Rule:MF_00152};
DE   AltName: Full=Endonuclease IV {ECO:0000256|HAMAP-Rule:MF_00152};
GN   Name=nfo {ECO:0000256|HAMAP-Rule:MF_00152};
GN   ORFNames=HMPREF1092_01956 {ECO:0000313|EMBL:ENZ01248.1};
OS   Clostridium thermobutyricum.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=29372 {ECO:0000313|EMBL:ENZ01248.1, ECO:0000313|Proteomes:UP000013097};
RN   [1] {ECO:0000313|EMBL:ENZ01248.1, ECO:0000313|Proteomes:UP000013097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=209318 {ECO:0000313|EMBL:ENZ01248.1,
RC   ECO:0000313|Proteomes:UP000013097};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Courvalin P., Lambert T.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Clostridium colicanis 209318.";
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endonuclease IV plays a role in DNA repair. It cleaves
CC       phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating
CC       a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_00152}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphooligonucleotide end-
CC         products.; EC=3.1.21.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00152};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00152};
CC       Note=Binds 3 Zn(2+) ions. {ECO:0000256|HAMAP-Rule:MF_00152};
CC   -!- SIMILARITY: Belongs to the AP endonuclease 2 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00152, ECO:0000256|SAAS:SAAS01083619}.
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:ENZ01248.1}.
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DR   EMBL; AGYT01000009; ENZ01248.1; -; Genomic_DNA.
DR   RefSeq; WP_002598450.1; NZ_KB850956.1.
DR   STRING; 999411.HMPREF1092_01956; -.
DR   EnsemblBacteria; ENZ01248; ENZ01248; HMPREF1092_01956.
DR   PATRIC; fig|999411.4.peg.1922; -.
DR   HOGENOM; CLU_025885_4_1_9; -.
DR   OrthoDB; 1088517at2; -.
DR   BioCyc; GCF_000371465-HMP:HMPREF1092_RS09505-MONOMER; -.
DR   Proteomes; UP000013097; Unassembled WGS sequence.
DR   GO; GO:0008833; F:deoxyribonuclease IV (phage-T4-induced) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   CDD; cd00019; AP2Ec; 1.
DR   HAMAP; MF_00152; Nfo; 1.
DR   InterPro; IPR001719; AP_endonuc_2.
DR   InterPro; IPR018246; AP_endonuc_F2_Zn_BS.
DR   InterPro; IPR036237; Xyl_isomerase-like_sf.
DR   InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR   PANTHER; PTHR21445; PTHR21445; 1.
DR   Pfam; PF01261; AP_endonuc_2; 1.
DR   SMART; SM00518; AP2Ec; 1.
DR   SUPFAM; SSF51658; SSF51658; 1.
DR   TIGRFAMs; TIGR00587; nfo; 1.
DR   PROSITE; PS00730; AP_NUCLEASE_F2_2; 1.
DR   PROSITE; PS00731; AP_NUCLEASE_F2_3; 1.
DR   PROSITE; PS51432; AP_NUCLEASE_F2_4; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00152,
KW   ECO:0000256|SAAS:SAAS01083620};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00152,
KW   ECO:0000256|SAAS:SAAS01083629};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_00152,
KW   ECO:0000256|SAAS:SAAS01083624, ECO:0000313|EMBL:ENZ01248.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00152, ECO:0000256|SAAS:SAAS01083627};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00152,
KW   ECO:0000256|SAAS:SAAS01083611};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00152, ECO:0000256|SAAS:SAAS01083625};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013097};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00152, ECO:0000256|SAAS:SAAS01083609}.
FT   DOMAIN          20..232
FT                   /note="AP_endonuc_2"
FT                   /evidence="ECO:0000259|Pfam:PF01261"
FT   METAL           67
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           107
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           142
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           142
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           176
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           179
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           211
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           224
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           226
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           256
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
SQ   SEQUENCE   278 AA;  31275 MW;  97353738F53AD15D CRC64;
     MLNIGCHLST TKGFEHMGKE ALSIGGNTFQ FFTRNPRGGK AKEINQKDID GLLKIMKENN
     FSQILAHAPY TLNACSGTES TRQFAIETMK DDLERMEYLP NNLYNFHPGS HVKQGVEVGI
     NYIVDMLNQV LKPEQTTTVL LETMAGKGTE VGRTFEEIAE IISKVELKDK MGVCLDTCHI
     HDGGYDIVND LDGVLEEFDR VIGLDRLKAI HLNDSKNPIN SHKDRHEKIG EGFLGEEAIK
     RIINHPKLKG IPFFLETPND IEGYAKEIEL LKSLYTLE
//
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