ID A0A367LGX9_9HYPO Unreviewed; 961 AA.
AC A0A367LGX9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 22-FEB-2023, entry version 13.
DE RecName: Full=Prolyl 4-hydroxylase alpha subunit domain-containing protein {ECO:0000259|SMART:SM00702};
GN ORFNames=L249_8214 {ECO:0000313|EMBL:RCI13693.1};
OS Ophiocordyceps polyrhachis-furcata BCC 54312.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=1330021 {ECO:0000313|EMBL:RCI13693.1, ECO:0000313|Proteomes:UP000253664};
RN [1] {ECO:0000313|EMBL:RCI13693.1, ECO:0000313|Proteomes:UP000253664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 54312 {ECO:0000313|EMBL:RCI13693.1,
RC ECO:0000313|Proteomes:UP000253664};
RX PubMed=26511477; DOI=10.1186/s12864-015-2101-4;
RA Wichadakul D., Kobmoo N., Ingsriswang S., Tangphatsornruang S.,
RA Chantasingh D., Luangsa-ard J.J., Eurwilaichitr L.;
RT "Insights from the genome of Ophiocordyceps polyrhachis-furcata to
RT pathogenicity and host specificity in insect fungi.";
RL BMC Genomics 16:881-881(2015).
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:RCI13693.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LKCN02000005; RCI13693.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367LGX9; -.
DR STRING; 1330021.A0A367LGX9; -.
DR Proteomes; UP000253664; Unassembled WGS sequence.
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; 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.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000253664}.
FT DOMAIN 40..224
FT /note="Prolyl 4-hydroxylase alpha subunit"
FT /evidence="ECO:0000259|SMART:SM00702"
FT REGION 232..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..427
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..564
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..954
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 961 AA; 106548 MW; 3E5D7FE45BD045F5 CRC64;
MPKAKPSANR PAVEKAPEWP RFKPSLPVAD LTPQLHPATA KIALVPFFFP RSLCRDYVAF
FRTLPLQTTP ARPKRGEAAR VNDRFQVDDA VFARRLWEQT GLKEALTEDD KVKHLWVYRY
SKGQYFDCHY DDENNVELAT DPPTSARTTW TLLLYLTSAA EGCAGGETVF YPHDRKSWAE
AIVVPPETGL LLLHKHGDDC LLLCGHDATT THHVSLGNAP LTCRTLQADM SFHSAGGPQR
PYAPPPPRGH GDWQMPPQQH AGPRRPYDDG YGHYGGPDPR GRPAIRRPPL VNGPESYPGP
PREYHAYGEP GPDRSQFAIP GRSLTMPPQE AVQRQGPMPP RADTMPSHDP ASRGAVPPRP
ATATGSRPPP RRMYQHPSQG QPQEWHGRPY RQETSDDVFN SYFTPPPPRQ PNLPEAEEAP
PFQGRGPPPR IHDEEEEEEI LINRRGYTTP SPRPTFAYQP EHPGSYGRGG GGFDPMAPPP
TRGPSGHGNG QRFRGFEPRS GTAPPQMVSP DALPSHPTPV RPGLMANSMV SVSDRPPPVR
NYNGVPQAGP PQPMPPPPPQ HQQMPQQPVR AGHQVPVPVM GQPVTPAELE RLRVAIKHNA
NDQDSALLLA RKLVEAADVL TAKMPDAKQR ARTRDRYLVD AHKILKKLAN AQNQEAMFIM
ADGLGKGLFG HEPDNKEAFT LYHSAAKLGH AAAAYRTAVC CEIGQEEGGG TRKDPLKAMQ
WYRRAATLGD PPAMYKVGMI QLKGLLGQSK NPREAVGWLR RAAERANEEN PHALHELGLL
YESAQSNDVI IRDERYALSL FQDAADLGYK FSQFRLGCAS EYGLMGCPID PRQSIYWYSK
AAAQGEHQSE LALSGWYLTG SEGVLGQSDT EAYLWARKAA VAGLAKAEYA MGYFTEVGIG
VPANLEDAKR WYWRAAAQEF PKARERLEDL KRAGKHGRPR ERERISRSRI ERQQEGECSV
M
//
