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Database: UniProt
Entry: A0A093X8P8_TALMA
LinkDB: A0A093X8P8_TALMA
Original site: A0A093X8P8_TALMA 
ID   A0A093X8P8_TALMA        Unreviewed;       281 AA.
AC   A0A093X8P8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Prolyl 4-hydroxylase alpha subunit domain-containing protein {ECO:0000259|SMART:SM00702};
GN   ORFNames=GQ26_0570390 {ECO:0000313|EMBL:KFX41593.1};
OS   Talaromyces marneffei PM1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX41593.1, ECO:0000313|Proteomes:UP000029285};
RN   [1] {ECO:0000313|EMBL:KFX41593.1, ECO:0000313|Proteomes:UP000029285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PM1 {ECO:0000313|EMBL:KFX41593.1,
RC   ECO:0000313|Proteomes:UP000029285};
RX   PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA   Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA   Lin X.;
RT   "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT   of Dimorphic Transition in Penicillium marneffei.";
RL   PLoS Genet. 10:e1004662-e1004662(2014).
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:KFX41593.1}.
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DR   EMBL; JPOX01000057; KFX41593.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093X8P8; -.
DR   eggNOG; ENOG502S6FN; Eukaryota.
DR   HOGENOM; CLU_041456_2_1_1; -.
DR   Proteomes; UP000029285; 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   InterPro; IPR045054; P4HA-like.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   PANTHER; PTHR10869:SF207; P4HA_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR   SMART; SM00702; P4Hc; 1.
PE   4: Predicted;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          38..274
FT                   /note="Prolyl 4-hydroxylase alpha subunit"
FT                   /evidence="ECO:0000259|SMART:SM00702"
SQ   SEQUENCE   281 AA;  31551 MW;  69F7C7C286B6345D CRC64;
     MPADVRPEFL PPQAPHNVTS TIIDFTATTP AIPEYKSCFA AVIDNFMTAA ECKELIALAE
     QSTPDGKWER AMINVGGGKQ VMATDYRNCG RIILDSTELA DRILGRLMPF FEGWDMVTLQ
     NKLGVTGLAG RRNNFHLTRL NERLRFLKYV GGEYFRPHCD GNYRTPDGSE ISYYTIQLYL
     SGEGEEGQDL EEFARRQKKE LNSKGIKTED KEGADEEKLL GGATSFMPSW ELADQAVRVW
     PKTGRVLVFQ QNNLWHGGDS VYGGTKYTVR AEVMYSKTPV A
//
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