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Database: UniProt
Entry: A0A0R2FW85_9LACO
LinkDB: A0A0R2FW85_9LACO
Original site: A0A0R2FW85_9LACO 
ID   A0A0R2FW85_9LACO        Unreviewed;       304 AA.
AC   A0A0R2FW85;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   22-APR-2020, entry version 17.
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=IV38_GL000415 {ECO:0000313|EMBL:KRN29530.1}, IV40_GL000253
GN   {ECO:0000313|EMBL:KRN33940.1};
OS   Lactobacillus selangorensis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=81857 {ECO:0000313|EMBL:KRN29530.1, ECO:0000313|Proteomes:UP000051751};
RN   [1] {ECO:0000313|EMBL:KRN29530.1, ECO:0000313|Proteomes:UP000051645, ECO:0000313|Proteomes:UP000051751}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-66 {ECO:0000313|EMBL:KRN29530.1,
RC   ECO:0000313|Proteomes:UP000051751}, and DSM 13344
RC   {ECO:0000313|EMBL:KRN33940.1, ECO:0000313|Proteomes:UP000051645};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:KRN29530.1}.
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DR   EMBL; JQAT01000001; KRN29530.1; -; Genomic_DNA.
DR   EMBL; JQAZ01000001; KRN33940.1; -; Genomic_DNA.
DR   EnsemblBacteria; KRN29530; KRN29530; IV38_GL000415.
DR   EnsemblBacteria; KRN33940; KRN33940; IV40_GL000253.
DR   PATRIC; fig|81857.3.peg.420; -.
DR   Proteomes; UP000051645; Unassembled WGS sequence.
DR   Proteomes; UP000051751; 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:KRN29530.1};
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:UP000051645};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00152, ECO:0000256|SAAS:SAAS01083609}.
FT   DOMAIN          24..239
FT                   /note="AP_endonuc_2"
FT                   /evidence="ECO:0000259|Pfam:PF01261"
FT   METAL           71
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           112
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           147
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           147
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           181
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           184
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           216
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           229
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           231
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           261
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
SQ   SEQUENCE   304 AA;  33470 MW;  3A793EC981A39EAB CRC64;
     MNGMKIGSHV SMKGTKMLLG SAQEAAAENA NAFMIYTGAP QNTRRKPTEK FQIEPAHAYM
     QEHGIDTIVV HAPYIVNLGN TLKPDKFEFG VQFMRDEVAR ADAIGAQQMA FHPGAHVGAG
     ADAALQQIIK GLNEILTEDQ TVHIAIETMA GKGTEVGTSF EQLATIIDGV QDNDKLSVCF
     DTCHTSDAGY AIKDDFDGVL NEFDHLIGLD RLQLIHLNDS KNPQGSHKDR HENIGFGTIG
     FDTLNYVAHH PQLETVPKIL ETPYIDGSKK KRAYSPYKRE IAMLETETFD PEMKDEILAE
     NEAS
//
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