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Database: UniProt
Entry: A0A094ETG2_9PEZI
LinkDB: A0A094ETG2_9PEZI
Original site: A0A094ETG2_9PEZI 
ID   A0A094ETG2_9PEZI        Unreviewed;      1657 AA.
AC   A0A094ETG2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN   ORFNames=V500_10861 {ECO:0000313|EMBL:KFY82056.1};
OS   Pseudogymnoascus sp. VKM F-4518 (FW-2643).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420913 {ECO:0000313|EMBL:KFY82056.1, ECO:0000313|Proteomes:UP000029284};
RN   [1] {ECO:0000313|EMBL:KFY82056.1, ECO:0000313|Proteomes:UP000029284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4518 (FW-2643) {ECO:0000313|Proteomes:UP000029284};
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:KFY82056.1}.
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DR   EMBL; JPKC01003590; KFY82056.1; -; Genomic_DNA.
DR   STRING; 1420913.A0A094ETG2; -.
DR   HOGENOM; CLU_243535_0_0_1; -.
DR   Proteomes; UP000029284; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   CDD; cd00067; GAL4; 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; IPR032852; ALKBH2.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   InterPro; IPR001138; Zn2Cys6_DnaBD.
DR   PANTHER; PTHR31573; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 2; 1.
DR   PANTHER; PTHR31573:SF4; FE2OG DIOXYGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   4: Predicted;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029284}.
FT   DOMAIN          1434..1540
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   REGION          36..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          158..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          270..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          409..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          588..722
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          841..901
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          927..984
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..314
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..344
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..434
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..458
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        532..551
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        601..618
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..697
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        841..856
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        873..895
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        944..972
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1443
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT   BINDING         1452
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
SQ   SEQUENCE   1657 AA;  180687 MW;  77399BC041DF12AB CRC64;
     MAAKGCAYED GPPESSAEKE ISSIYANISA GNIIADSARR RKPPGGACTA ELVQKSGHKR
     PGRGQRLNEQ VVKGKNDPQA GIESTTAEPS RDTRSMGKKS SNFHSDMPMI EEVANSEKPA
     ISDEFEPVIV VERTPKRAKT KSRSSPAASA AKELFFHASE ADELERPEGP VITGGEAPVD
     DDNSAETPSL GFIQANVRPT QSSTLQPSKA SFCQSSAGNI TGGLKNASGT LGGQRQEGYR
     CVVVANGAAL TSTADSGLHR GLVTESFNEE LDQNQSATSI SQRSGPTSPS TGFYGQSSLN
     DSQHTSPLLD QTPRRKLRSS SHETIPQLRP SFHQPTNSLQ DKSSLLQPHE SSILLPSTPA
     LSSTLLGPSN NTSHFSDSKS IATFQVDTST ACQQDQQAHN QSITNVEGMA DASTRQSSAI
     ELDGESSSDL SDLDSSQEDF TDVEAGLNLN SPQPELADKQ EPSVSPVKSR PARQKKPTLK
     ALQKQKQQTP KKSRAQAPKE KNVLQKAAAR AKAVTKKAPA KPKLPKAATR ASGRKQKVEE
     EDEKDDFQPE KDLGFAISGS GVSLRDRSTL KAPVSYLDQV VATADLMQKP GAKTGLKMIV
     STKKTGETSA TRASAAPSNV RTPLPKKATP SAPCTPRQSK KPPPKSTKCA EPKLSPHDSG
     FSEVASTDDE QASSDFSPPS NSSSDSPQES SIISPSSPEE DAEEDIIEPS SPEVAPQRVR
     KKNGHFDVNV TVKDADARTD PPLGPELFEL AQKAKAKGQI AKRWNLDVAR RVDGIWMAPD
     KCDNCRDDRC VDCDRAFPCS SCIKKGKHCN VRTVMKRTAC NNNKQYDEAI TPLHLNAPIV
     SQNGDGTWNA TKQTPPTTRP KKRKRGDTSK DIANKSIAKS QGLRAVSTTR GKRLNNGPRR
     SGEVLQHLKA PHTFQNGDAT WNVTEQALPA SSVDKRKRKY ADPSKATGNS SAKRQHRLPA
     SGYSSSEETD LEDPANLGQA LVRSKKVPRA NRTYAPYHRS EQENLPAPYG EPPVWASKRQ
     QLCEALPYYR AYMSGGYLHD GLICGLLIDK EIRERDVFDE EVVITRCGGG RKLDEATNKM
     IQTTHQERSQ GNSLSPSKLP HYYNVLDWFH VTDVWVENVE GFKTWCVRME KIRLDEKSWW
     ASAGSTLPSP DRDLNAIKAA SQECLHCKNT SKVVFEQGWA CLKASCDKFF VFDSPVDDRK
     LFYTEAFLKE RTAYSGNAPG PLAPPLMAEA DMIIAGSHGT EAAFKQGIVC PLCKGCSRRT
     QWSKWSCETA GCGFTHSLPF RMTSVKDTMK DVGRNPPQQN YARDFGIKFE AKRIGAYDVF
     EYGIPGPKGN VVGVLQLFKS TDAINHRPDG PNDLFRLMQE SDFDLRRRPV RQPNSSGEIL
     TNHFATNWGA PYKFVVTQSS RGFSEAPAVC IKALKRLTWA GEQALTDIGE PFHPFNELLS
     IGYFEDCSIG FHDDGESTLG PTVATLSLGA SATMALRPKA KATMGNISRN AKGTKTPVLR
     VTLEHGDMVI MHGSGVQQYY EHEVVPNGTL RFALTCRYVR PDTLENDAER EDARIKGALP
     EGHEQYKYGG DENAIFTPEE IEKAKKAERL NALMRSLNDA AAIFRAGASQ GDDDERCQMR
     DLMGQFENEA LAPGVVGKPI CRKDCGEEVD VTMPNAP
//
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