ID A0A2C5YXS0_9HYPO Unreviewed; 1240 AA.
AC A0A2C5YXS0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 22-FEB-2023, entry version 16.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=CDD80_3126 {ECO:0000313|EMBL:PHH74365.1};
OS Ophiocordyceps camponoti-rufipedis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2004952 {ECO:0000313|EMBL:PHH74365.1, ECO:0000313|Proteomes:UP000226431};
RN [1] {ECO:0000313|EMBL:PHH74365.1, ECO:0000313|Proteomes:UP000226431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Map16 {ECO:0000313|EMBL:PHH74365.1,
RC ECO:0000313|Proteomes:UP000226431};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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:PHH74365.1}.
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DR EMBL; NJES01000279; PHH74365.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5YXS0; -.
DR STRING; 2004952.A0A2C5YXS0; -.
DR OrthoDB; 5474539at2759; -.
DR Proteomes; UP000226431; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR InterPro; IPR006597; Sel1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR46430:SF3; ACTIVATOR OF C KINASE PROTEIN 1; 1.
DR PANTHER; PTHR46430; PROTEIN SKT5-RELATED; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR Pfam; PF08238; Sel1; 7.
DR SMART; SM00702; P4Hc; 1.
DR SMART; SM00671; SEL1; 7.
DR SUPFAM; SSF81901; HCP-like; 2.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000226431}.
FT DOMAIN 127..255
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1209..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..466
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..637
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1240 AA; 136504 MW; DA31D1A2678D7B06 CRC64;
MPKAKTSSKR PPATSEPAQQ PPSWPRFKPA LPVADLAPQL HPATSKIALI PSFFPRSLCR
DFVAFLRTLP LQTTPGRPKR GEATRVNDRF QVDDGHFARR LWEETGLKEA LTLSDDVRDL
WGGEPVGLNA NIRVYRYTTG QFFDCHYDDD NDVDVSTDPP TPARTTWTLL LYLTSSTEGC
VGGETVFYTR DRKSPAEAIV VPPETGLLLL HKHGADCLLV GVGSVLCSVW LTRLQHEGRE
VTAGEKWVLR TDICVRRIDR PSVYFGLAES LADLAGSHPM SRPRDSGRSA GRRRSKLQVP
GPAGWILQRL APRTRALSQV GLVRATDSVC SARMYKYRGC GPTSTLLRQF SMWDPSTGDF
CPPATCPDLS QRAPLNHGPL PRLPRFAPLQ TPTLTNFPRL SSNLSCAIVP QQTINRHDDS
ILLDYAPLTR TSILTTPSPG HEDMSYHGVG GPQRPYPPPQ PAPPRGYGER QMPQQQHGGP
PRGQYDDGYG HYGPQVQRHR PGPEPVPHRW RSEPGRGAPG PQTAVPRGPS SDHGSVRRPQ
MPHGPDSYPG PPRDYHGHGG YDEQGPDRSQ FVPPGRSMTM PSQDAVRQGA MQQPPPPPHR
ADTMPYHDPA GRGGGVPPRP STATGSRPPP RRMLPPQPQG QPQEWHGRGY RQETSEEGFD
SYFAQPGPAE AEGRGPPPDP RRGAPHQMPR LHHAKSEANF REPQMAVFEM PAEVPMMPAV
PPIQAYQPEY AGGYGRGGGG GGGGFEPMGS RGPPPPGHAN GQHRFHGYDP RPGTAPPQQQ
QQMSSPDALP SHPTPVRPGH MANSMVSVND RPPPVRNYGG VPQNGPPQQQ QQQQLQQAPP
QQGRVAVRAG LQVPEPAMTG QLVTPSELEQ LRMAIKHNAN DHDSALMLAR KLVEAADVLI
ANIPDAKQRA RTRERYLMDA HKILKKLANA QNQEAMFIMA DGLGRGLFGH EPDNKEAFAL
YHSAAKLGHA AAAYRTAVCC EIGQEEGGGT RKDPLKAMQW YRRAATLGDP PAMYKVGMIL
LKGLLGQNKN PREAVGWLRR AAERANEENP HALHELGLLY ESAQSNDVII RDERYALSLF
QDAADLGYKF SQFRLGCAFE YGLMGCPIDP RQSIFWYSKA AAQAEHQSEL ALSGWYLTGS
DGVLGQSDTE AYLWARKAAV AGLAKAEYAM GYFTEVGIGV PANLEDAKRW YWRAAAQEFP
KARERLEDLK RAGKHGRPRE RERISRSRIE RQQEGECSVM
//
