ID A0A0A2JM78_PENEN Unreviewed; 480 AA.
AC A0A0A2JM78;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Oxoglutarate/iron-dependent dioxygenase {ECO:0000313|EMBL:KGO54231.1};
GN ORFNames=PEX2_039350 {ECO:0000313|EMBL:KGO54231.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO54231.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO54231.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO54231.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO54231.1}.
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DR EMBL; JQFZ01000230; KGO54231.1; -; Genomic_DNA.
DR RefSeq; XP_016596704.1; XM_016741210.1.
DR AlphaFoldDB; A0A0A2JM78; -.
DR STRING; 27334.A0A0A2JM78; -.
DR GeneID; 27676629; -.
DR HOGENOM; CLU_026011_0_0_1; -.
DR OrthoDB; 325143at2759; -.
DR PhylomeDB; A0A0A2JM78; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; cd14279; CUE; 1.
DR Gene3D; 2.60.120.590; Alpha-ketoglutarate-dependent dioxygenase AlkB-like; 1.
DR InterPro; IPR027450; AlkB-like.
DR InterPro; IPR037151; AlkB-like_sf.
DR InterPro; IPR032854; ALKBH3.
DR InterPro; IPR003892; CUE.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR010666; Znf_GRF.
DR PANTHER; PTHR31212; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 3; 1.
DR PANTHER; PTHR31212:SF4; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 3; 1.
DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51140; CUE; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS51999; ZF_GRF; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000313|EMBL:KGO54231.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:KGO54231.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01343}.
FT DOMAIN 30..73
FT /note="CUE"
FT /evidence="ECO:0000259|PROSITE:PS51140"
FT DOMAIN 260..398
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT DOMAIN 409..454
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 480 AA; 54269 MW; B9A85467638E81E8 CRC64;
MDVFISRKRP RLSNSSEEAR DKSSDPCEDT TDTKLAILLS LFPTIKQDEL LDILISCEGS
VENVIGLLSA RDTAGGTPVG KKRAAITSTF GMQTSLSSHV FTTAEDGTMK PLHEIASKKK
LPPLQKGKTL HLYSPEDIAT YTPCTIIHNF LPAKEANELL LELLDESKHF SRYDFQLFNR
TVHSPHTYSV YVSTPEEHRQ HTSEYAYGGT YRSSVRQVTP QLRSVSRQVQ KTVNDEINKR
IRDVYPDGKK LQYQSPKEWR PNAAFVNCYD GPTESVGYHS DKLTYLGPHP VIGSLSLGVA
REFRVRRIVP RDDDDTAEED HDSNKTSPIP HSPRDQTAAT ARADAQGQIS IHLPHNSLLI
MHAEMQEAWK HSIAPAQTIS PHPISGNRRI NVTYRWYRDT LHPRYTPRCK CGEHTILRCA
QRKNGTRGRY MWMCYASYTP GKEGCSFFQW AEFDDDGDPV WEKKTIGDDA PTLTNFSASQ
//
