GenomeNet

Database: UniProt
Entry: D6TPT1_9CHLR
LinkDB: D6TPT1_9CHLR
Original site: D6TPT1_9CHLR 
ID   D6TPT1_9CHLR            Unreviewed;       290 AA.
AC   D6TPT1;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   17-JUN-2020, entry version 50.
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=Krac_8850 {ECO:0000313|EMBL:EFH87516.1};
OS   Ktedonobacter racemifer DSM 44963.
OC   Bacteria; Chloroflexi; Ktedonobacteria; Ktedonobacterales;
OC   Ktedonobacteraceae; Ktedonobacter.
OX   NCBI_TaxID=485913 {ECO:0000313|EMBL:EFH87516.1, ECO:0000313|Proteomes:UP000004508};
RN   [1] {ECO:0000313|EMBL:EFH87516.1, ECO:0000313|Proteomes:UP000004508}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44963 {ECO:0000313|Proteomes:UP000004508};
RX   PubMed=22180814; DOI=10.4056/sigs.2114901;
RA   Chang Y.J., Land M., Hauser L., Chertkov O., Del Rio T.G., Nolan M.,
RA   Copeland A., Tice H., Cheng J.F., Lucas S., Han C., Goodwin L., Pitluck S.,
RA   Ivanova N., Ovchinikova G., Pati A., Chen A., Palaniappan K.,
RA   Mavromatis K., Liolios K., Brettin T., Fiebig A., Rohde M., Abt B.,
RA   Goker M., Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Non-contiguous finished genome sequence and contextual data of the
RT   filamentous soil bacterium Ktedonobacter racemifer type strain (SOSP1-
RT   21).";
RL   Stand. Genomic Sci. 5:97-111(2011).
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:EFH87516.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ADVG01000002; EFH87516.1; -; Genomic_DNA.
DR   RefSeq; WP_007912730.1; NZ_ADVG01000002.1.
DR   STRING; 485913.Krac_8850; -.
DR   EnsemblBacteria; EFH87516; EFH87516; Krac_8850.
DR   eggNOG; ENOG4105EFU; Bacteria.
DR   eggNOG; COG0648; LUCA.
DR   Proteomes; UP000004508; 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; PS00729; AP_NUCLEASE_F2_1; 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:EFH87516.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00152, ECO:0000256|SAAS:SAAS01083627,
KW   ECO:0000313|EMBL:EFH87516.1};
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:UP000004508};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00152, ECO:0000256|SAAS:SAAS01083609}.
FT   DOMAIN          18..237
FT                   /note="AP_endonuc_2"
FT                   /evidence="ECO:0000259|Pfam:PF01261"
FT   METAL           66
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           106
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           177
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           180
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           214
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           227
FT                   /note="Zinc 3"
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           259
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
SQ   SEQUENCE   290 AA;  31203 MW;  1679E3CC993C981D CRC64;
     MRIGRHMPTG SKPLKAIETA RQIGCQAIQV FASNPTGWKL PVLDEKSGQA FSTAARKQEL
     NPIVLHAPYL INLGTLDATI WEKSILLLTG TLQRGAQLGA SYVVFHTGSH RGAGVPTGLA
     RIAQGIERVM GQSPAEVMLL LENDVGAGNA LGHSFEHLAT VLAHLPQYSQ RLGVCLDTAH
     LWGAGHDIGT PQAAQQVLQH FDDTVGLARL KVLHLNDTAM ALGSHRDVHT RLGEGIIHPT
     GLRALLTDPR LSHVAVLMET PIETDEDGKE DWVHDAGQIA YAKSLCLPIE
//
DBGET integrated database retrieval system