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Database: UniProt
Entry: A0A101JDY7_9ACTN
LinkDB: A0A101JDY7_9ACTN
Original site: A0A101JDY7_9ACTN 
ID   A0A101JDY7_9ACTN        Unreviewed;       281 AA.
AC   A0A101JDY7;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   22-APR-2020, entry version 16.
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=ADL15_42485 {ECO:0000313|EMBL:KUL25068.1};
OS   Actinoplanes awajinensis subsp. mycoplanecinus.
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Actinoplanes.
OX   NCBI_TaxID=135947 {ECO:0000313|EMBL:KUL25068.1, ECO:0000313|Proteomes:UP000053244};
RN   [1] {ECO:0000313|EMBL:KUL25068.1, ECO:0000313|Proteomes:UP000053244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-16712 {ECO:0000313|EMBL:KUL25068.1,
RC   ECO:0000313|Proteomes:UP000053244};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) 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:KUL25068.1}.
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DR   EMBL; LLZH01000318; KUL25068.1; -; Genomic_DNA.
DR   RefSeq; WP_067704943.1; NZ_LLZH01000318.1.
DR   EnsemblBacteria; KUL25068; KUL25068; ADL15_42485.
DR   BioCyc; GCF_001509495:ADL15_RS42495-MONOMER; -.
DR   Proteomes; UP000053244; 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:KUL25068.1};
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:UP000053244};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00152, ECO:0000256|SAAS:SAAS01083609}.
FT   DOMAIN          71..237
FT                   /note="AP_endonuc_2"
FT                   /evidence="ECO:0000259|Pfam:PF01261"
FT   METAL           64
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           104
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           143
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00152"
FT   METAL           143
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   281 AA;  29279 MW;  23B37BD1DEBAE8A2 CRC64;
     MGSHTKTSGG LAKAALPYVD AAGSETLQVY VSNSRGWALP AGDPKQDVLF RDGIGEREMP
     AYIHASLLVN LGSPTELTVE RSIATLEHAL RRGKAIGATA VVYHAGSSVD EAHAEKAMHQ
     LHEQLLPLLE TAAAEGLPRL LVEPSAGGGR SLASKVQDLE AYLAAVDGHP WLGVCFDTCH
     AWAAGHDLAT PGGMTATLDA LVTAAGPGRL QLIHANDSKD DCGSTRDRHE TIGAGKIGSA
     PFAELFQHPA TAGVPIIVET PSVEHEGHAA DIALLKGLRK V
//
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