ID A0A1E3IEW8_9TREE Unreviewed; 673 AA.
AC A0A1E3IEW8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Nuclear protein {ECO:0000313|EMBL:ODN87058.1};
GN ORFNames=L203_03832 {ECO:0000313|EMBL:ODN87058.1};
OS Cryptococcus depauperatus CBS 7841.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus.
OX NCBI_TaxID=1295531 {ECO:0000313|EMBL:ODN87058.1, ECO:0000313|Proteomes:UP000094043};
RN [1] {ECO:0000313|EMBL:ODN87058.1, ECO:0000313|Proteomes:UP000094043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 7841 {ECO:0000313|EMBL:ODN87058.1,
RC ECO:0000313|Proteomes:UP000094043};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (JUN-2016) 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:ODN87058.1}.
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DR EMBL; AWGK01000015; ODN87058.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3IEW8; -.
DR STRING; 1295531.A0A1E3IEW8; -.
DR VEuPathDB; FungiDB:L203_03832; -.
DR OrthoDB; 100633at2759; -.
DR Proteomes; UP000094043; Unassembled WGS sequence.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR Gene3D; 3.60.130.20; Oxoglutarate/iron-dependent oxygenase, C-terminal degradation domain; 1.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR InterPro; IPR019601; Oxoglutarate/Fe-dep_Oase_C.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR043044; TPA1/Ofd1_C.
DR InterPro; IPR039558; TPA1/OFD1_N.
DR PANTHER; PTHR12117; HISTONE ACETYLTRANSFERASE COMPLEX; 1.
DR PANTHER; PTHR12117:SF0; PROLYL 3-HYDROXYLASE OGFOD1; 1.
DR Pfam; PF13661; 2OG-FeII_Oxy_4; 1.
DR Pfam; PF10637; Ofd1_CTDD; 1.
DR SMART; SM00702; P4Hc; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000094043};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 54..284
FT /note="Prolyl 4-hydroxylase alpha subunit"
FT /evidence="ECO:0000259|SMART:SM00702"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 673 AA; 73624 MW; 65A901DAD280280D CRC64;
MPAAARERSP SSAAGRSAKK HKNSPDQSAT ASINHPSVDQ VTAYREEYVN ASPFKHAVIS
GVLSDEMLEG VVQECKKFGI RGEEGSLPGW GWEQKETDIY KIQQTPDLSS LSPEHLPDVT
LEALPQLTRL KEALYSQEFR NLVRQVTGCG ALSGKKTDLS AALYTKGSHL LLHDDSISSR
LVSYILYLPY SSADAAKGDV ELVPSANGDF FKGWDPAWGG SLELFPVETG EEVGPPSVKR
HKKVSATWGQ IIIFEVQPGR SYHAVEEVVV DEGRRRFSVS GWFHRPVEDE EGYQVFDQEK
AKKDLSSLAQ ITAAPSISFL SYPTPPPPGL KPSDIAFLAN YLASSYLTST TLERLSGQFV
EASEIVLHNF LLPELAAKLK AETESADKKD YGSYKGLLTP QDLGEDDGWV IQGPSSKHRY
LSLTSLSTST PIIQSIHNVL FPSDAFRAWL SVVSSLAPVG HRNEARRFRK GLDYTLANGE
GKDGDARLDV SLGATWWADV PAGSDEEDTL AEHGGWEAYL AAPDEDEDPA VYQSSLAKKA
AKADRDHDAH HANGNKERKV ETSEHKANGN GTDGPSISTG NQELEFDPNQ FSPSDFDSDS
EANEEDDGPL LTQPVAFNKL LLVLRDPGVM KFVKYLGASA PGSRWDVQGE YEVGVLEEEE
EEEREEGSGE VRT
//