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Database: UniProt
Entry: A0A1R3UT42_9ACTN
LinkDB: A0A1R3UT42_9ACTN
Original site: A0A1R3UT42_9ACTN 
ID   A0A1R3UT42_9ACTN        Unreviewed;       287 AA.
AC   A0A1R3UT42;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   22-APR-2020, entry version 14.
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=BQ8420_24230 {ECO:0000313|EMBL:SIO89955.1};
OS   Nocardiopsis sp. JB363.
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Nocardiopsis; unclassified Nocardiopsis.
OX   NCBI_TaxID=1434837 {ECO:0000313|EMBL:SIO89955.1, ECO:0000313|Proteomes:UP000195722};
RN   [1] {ECO:0000313|EMBL:SIO89955.1, ECO:0000313|Proteomes:UP000195722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB363 {ECO:0000313|EMBL:SIO89955.1,
RC   ECO:0000313|Proteomes:UP000195722};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-2016) 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}.
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DR   EMBL; FRFF01000150; SIO89955.1; -; Genomic_DNA.
DR   Proteomes; UP000195722; 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; 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:SIO89955.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00152, ECO:0000256|SAAS:SAAS01083627,
KW   ECO:0000313|EMBL:SIO89955.1};
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:UP000195722};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00152, ECO:0000256|SAAS:SAAS01083609}.
FT   DOMAIN          28..243
FT                   /note="AP_endonuc_2"
FT                   /evidence="ECO:0000259|Pfam:PF01261"
FT   REGION          264..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   METAL           72
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           149
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           149
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           183
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           186
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           220
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           233
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           235
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           265
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
SQ   SEQUENCE   287 AA;  30794 MW;  4A2CB1E90EFDD4AB CRC64;
     MNNTEQRPQS PVGAHVPVAG GMATKGLAYA DKIGAETVQV FVSNPRGWAT NDGDPTQDAM
     MRERTDLPVF VHAPYLINPG TPNEETAAKS ITSMEHALRR SARIGALGAV MHTGSAVSGT
     REDGLARARE RLLPMLERLG EDVPPLLLEP MAGQGQVLCA TVDDLVPYFE ALDWHPNVGV
     CLDTAHLFAA GHDISTVEGM REALDRFGEV VGADRLKLIH CNDSKAPCGS NKDRHENIGK
     GHIGAEPFAE LFRHPVTAGV PITLETPGPE GPHSEDVTTL KKLREQA
//
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