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Database: UniProt
Entry: A0A094BM32_9PEZI
LinkDB: A0A094BM32_9PEZI
Original site: A0A094BM32_9PEZI 
ID   A0A094BM32_9PEZI        Unreviewed;       450 AA.
AC   A0A094BM32;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   13-SEP-2023, entry version 25.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFY11417.1};
GN   ORFNames=V492_04466 {ECO:0000313|EMBL:KFY11417.1};
OS   Pseudogymnoascus sp. VKM F-4246.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY11417.1, ECO:0000313|Proteomes:UP000029299};
RN   [1] {ECO:0000313|EMBL:KFY11417.1, ECO:0000313|Proteomes:UP000029299}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY11417.1,
RC   ECO:0000313|Proteomes:UP000029299};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KFY11417.1}.
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DR   EMBL; JPJU01001489; KFY11417.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094BM32; -.
DR   STRING; 1420902.A0A094BM32; -.
DR   HOGENOM; CLU_026011_0_0_1; -.
DR   Proteomes; UP000029299; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IEA:InterPro.
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; 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; PS51471; FE2OG_OXY; 1.
DR   PROSITE; PS51999; ZF_GRF; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029299};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU01343}.
FT   DOMAIN          216..343
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   DOMAIN          354..399
FT                   /note="GRF-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51999"
FT   REGION          402..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   450 AA;  50157 MW;  2D9872C3E0DA9399 CRC64;
     MTAQEESTDY KLSILISLHP DKDEGTLLET LLASDGSVER ALECLKLPLK KKPAISATSY
     QSSLSSITRT RKDGAAIKPL TKKGKTVHLY TPEDIEAHTP CSIIYNFLPA EEADALLQEL
     VDESPTYKTD TFQLFDRVVS SPHTFCLYVD SWGEAEKQKT QYVYDGKNVK DVRRTLPHMR
     DASHKVRETV NQEITRRIRS SPTGKKLHHQ SPHPWVPNTA FVNCYDGPRE SVGYHSDHLT
     YLGPRPVIGS LSLGVAREFR IRKIVAADDD AGDSDNSDAA RKRADAKADA QGQLSIHLPH
     NSLLVMHASM QEEWKHSIAP ARTVSPHPIS GNKRINITYR QYKASLHPRF TPKCGCGVST
     VLRVVQRQAG NRGKYMWMCY AGYVPGKEGC KFFEWAEFDE DGEPPWAEKA DCSDKQGSGD
     GEKRPGDNEE DHQVDGERGK EGALGPVDEG
//
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