ID A0A1V6YDD1_PENNA Unreviewed; 431 AA.
AC A0A1V6YDD1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 08-NOV-2023, entry version 23.
DE RecName: Full=Endonuclease III homolog {ECO:0000256|HAMAP-Rule:MF_03183};
DE EC=3.2.2.- {ECO:0000256|HAMAP-Rule:MF_03183};
DE EC=4.2.99.18 {ECO:0000256|HAMAP-Rule:MF_03183};
DE AltName: Full=Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|HAMAP-Rule:MF_03183};
DE Short=DNA glycosylase/AP lyase {ECO:0000256|HAMAP-Rule:MF_03183};
GN Name=NTH1 {ECO:0000256|HAMAP-Rule:MF_03183};
GN ORFNames=PENNAL_c0024G06987 {ECO:0000313|EMBL:OQE85274.1},
GN PNAL_LOCUS4753 {ECO:0000313|EMBL:CAG8103199.1};
OS Penicillium nalgiovense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60175 {ECO:0000313|EMBL:OQE85274.1, ECO:0000313|Proteomes:UP000191691};
RN [1] {ECO:0000313|EMBL:OQE85274.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 13039 {ECO:0000313|EMBL:OQE85274.1};
RA Nielsen J.C., Nielsen J.;
RT "Uncovering the secondary metabolism of Penicillium species provides
RT insights into the evolution of 6-MSA pathways.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000191691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 13039 {ECO:0000313|Proteomes:UP000191691};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
RN [3] {ECO:0000313|EMBL:CAG8103199.1}
RP NUCLEOTIDE SEQUENCE.
RA Branca A.L. A.;
RL Submitted (JUL-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Bifunctional DNA N-glycosylase with associated
CC apurinic/apyrimidinic (AP) lyase function that catalyzes the first step
CC in base excision repair (BER), the primary repair pathway for the
CC repair of oxidative DNA damage. The DNA N-glycosylase activity releases
CC the damaged DNA base from DNA by cleaving the N-glycosidic bond,
CC leaving an AP site. The AP lyase activity cleaves the phosphodiester
CC bond 3' to the AP site by a beta-elimination. Primarily recognizes and
CC repairs oxidative base damage of pyrimidines. {ECO:0000256|HAMAP-
CC Rule:MF_03183}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC 2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03183};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03183}.
CC Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03183}.
CC -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000256|HAMAP-
CC Rule:MF_03183}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03183}.
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:OQE85274.1}.
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DR EMBL; CAJVNV010000199; CAG8103199.1; -; Genomic_DNA.
DR EMBL; MOOB01000024; OQE85274.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6YDD1; -.
DR STRING; 60175.A0A1V6YDD1; -.
DR OMA; WGWHKTQ; -.
DR OrthoDB; 3377194at2759; -.
DR Proteomes; UP000191691; Unassembled WGS sequence.
DR Proteomes; UP001153461; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000703; F:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006285; P:base-excision repair, AP site formation; IEA:UniProtKB-UniRule.
DR CDD; cd00056; ENDO3c; 1.
DR Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1.
DR HAMAP; MF_03183; Endonuclease_III_Nth; 1.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR InterPro; IPR000445; HhH_motif.
DR InterPro; IPR030841; NTH1.
DR PANTHER; PTHR43286; ENDONUCLEASE III-LIKE PROTEIN 1; 1.
DR PANTHER; PTHR43286:SF1; ENDONUCLEASE III-LIKE PROTEIN 1; 1.
DR Pfam; PF00633; HHH; 1.
DR Pfam; PF00730; HhH-GPD; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SUPFAM; SSF48150; DNA-glycosylase; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_03183};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_03183};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|HAMAP-
KW Rule:MF_03183};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03183};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_03183};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03183};
KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03183};
KW Reference proteome {ECO:0000313|Proteomes:UP000191691}.
FT DOMAIN 207..382
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
FT REGION 50..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 316
FT /note="Nucleophile; for N-glycosylase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03183"
FT SITE 335
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03183"
SQ SEQUENCE 431 AA; 47790 MW; 29B3B95B6F5E9CA6 CRC64;
MRTSRTSKDT AKVLQALSAP IGRQTRNSNV SALNSFAHNA NAIPTIKTEL ESEDVSTTPS
LSAVKIDDES SLSELSEADT ADIEDLLEPP LKRQKRNASP INPRVLKKSP SSRTPRKVIV
KDEPDQKPTP APKQRRRLPA RETRHIDGSV KVEPPSNWEK MYKIVQEMRK TGPASSAPVD
TMGCSELFWR ASSPIDRRFQ TLIALMLSSQ TKDTVTAVAM QRLHTELGDG TAPAQDIKIK
QEDDDDDSKP VDSTLNLTNI LAVDPTRLNE LIRTVGFHNN KTKYIKATAL ILRDQNGGDI
PSTPEGLMAL PGVGPKMAYL CMSAAWRQHL GIGVDVHVHR ITNLWGWNKT KTPEETRKAL
QSWLPDNKWY EINNLLVGLG QTVCLPVKRR CGDCKLAGLR LCKSEIRGLE PTLKAKKSPE
VDEPKVKIEA L
//
