ID A0A2H3IYN3_9EURO Unreviewed; 898 AA.
AC A0A2H3IYN3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Oxoglutarate/iron-dependent dioxygenase {ECO:0000313|EMBL:PCH03137.1};
GN ORFNames=PENO1_033890 {ECO:0000313|EMBL:PCH03137.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH03137.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCH03137.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCH03137.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
CC -!- SIMILARITY: Belongs to the isochorismatase family.
CC {ECO:0000256|ARBA:ARBA00006336}.
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:PCH03137.1}.
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DR EMBL; NPFK01000072; PCH03137.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3IYN3; -.
DR STRING; 290292.A0A2H3IYN3; -.
DR OrthoDB; 1644896at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IEA:InterPro.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0035552; P:oxidative single-stranded DNA demethylation; IEA:InterPro.
DR CDD; cd00431; cysteine_hydrolases; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 2.60.120.590; Alpha-ketoglutarate-dependent dioxygenase AlkB-like; 1.
DR Gene3D; 3.40.50.850; Isochorismatase-like; 1.
DR InterPro; IPR027450; AlkB-like.
DR InterPro; IPR037151; AlkB-like_sf.
DR InterPro; IPR032854; ALKBH3.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR000868; Isochorismatase-like.
DR InterPro; IPR036380; Isochorismatase-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR PANTHER; PTHR31212; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 3; 1.
DR PANTHER; PTHR31212:SF5; ISOCHORISMATASE FAMILY PROTEIN FAMILY (AFU_ORTHOLOGUE AFUA_3G14500); 1.
DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF00857; Isochorismatase; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52499; Isochorismatase-like hydrolases; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000313|EMBL:PCH03137.1};
KW Oxidoreductase {ECO:0000313|EMBL:PCH03137.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218381}.
FT DOMAIN 528..644
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 253..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 898 AA; 99129 MW; 550F50348E3DDC79 CRC64;
MNPLALFSSF SNLPSIETRK ALLLLDFQND FVRPNGRLPV RKTLDFIDLI PGLVQSFRRT
GEIVWVRTQY EGSRPVVDDY GSEIIITSAG PLDTKNQKKG RHGRQENRSD VNDVVDPEAF
LSGPEPACLP QTAGVQFPAP ILAAIDHDHD IVIEKSDYSA LQSPGMVLSL RSRFVTELYI
CGSLSNVSVY ATALDAAQQG FAITLIEDCM GYRSFARHEE AVRRLADIVG ANGISVQELL
EEEDWEETHE IAHASTAHPA ASQPKPLTQS NMTPPPSGIE NVLDHLAVQN SPITKRSSIA
ESVATPSPNT TVYSTGIIEA DDNPYDDDDV PIVLPPSKYS RARGTREART SGTNQTRVRR
TKSGKSPSSS RRPGSSAAES VTLGRASTSP VLTTTSHKAP NDVSPGSSAL KSLPSPPIAE
ASYAKKKKKI ANDYLGPDDS IAEGDSRIVY NLDLPTDAFE KIQKEVNWQK MYHLSGQVPR
LVAVQGLIAR DKSFPIYRHP ADESPILELF TKTVDAVRIC AEQIVGHPLN HALIQLYRDG
QDNISEHSDK TLDIVRGSSI VNVSLGAQRV MTLRTKKSAP TDGEDGRHKQ QVPMPHGSMF
ILGPQSNTRW LHGIRPDKRP ESEKSHEEKA YNGERISLTF RNIGTFINPE RGTIWGQGAV
SKRADAARKV IHGDASEAER LIRAFGSENR ETEFDWDAVY GRGFDVVNFV EPAVAHLTLS
GDPIADMRVR LCLTENGMRY IAQPRKTRDI QQIVYTSPDR NTVITGDIQI LLYLASLDPN
SELARPGVDV VRGGNHLIQI TQLGTAWHEY LLSGSNAEFG LLSSWNERLR EADQHYIAGQ
ALTIDDIALW PILHQIEIQK GAISGSSRYP YLSTYYQRIE KRGCVRVVMN EIAHERGC
//
