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Database: UniProt
Entry: A0A1J9QCV4_9EURO
LinkDB: A0A1J9QCV4_9EURO
Original site: A0A1J9QCV4_9EURO 
ID   A0A1J9QCV4_9EURO        Unreviewed;       300 AA.
AC   A0A1J9QCV4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Phosphoadenosine phosphosulfate reductase {ECO:0000313|EMBL:OJD18035.1};
GN   ORFNames=AJ78_01927 {ECO:0000313|EMBL:OJD18035.1};
OS   Emergomyces pasteurianus Ep9510.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX   NCBI_TaxID=1447872 {ECO:0000313|EMBL:OJD18035.1, ECO:0000313|Proteomes:UP000182235};
RN   [1] {ECO:0000313|EMBL:OJD18035.1, ECO:0000313|Proteomes:UP000182235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 9510 {ECO:0000313|EMBL:OJD18035.1,
RC   ECO:0000313|Proteomes:UP000182235};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C.A., Munoz J.F., Imamovic A., Priest M.E., Young S., Clay O.K.,
RA   McEwen J.G.;
RT   "Emmonsia species relationships and genome sequence.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate. {ECO:0000256|ARBA:ARBA00024327}.
CC   -!- SIMILARITY: Belongs to the PAPS reductase family. CysH subfamily.
CC       {ECO:0000256|ARBA:ARBA00009732}.
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:OJD18035.1}.
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DR   EMBL; LGRN01000048; OJD18035.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J9QCV4; -.
DR   STRING; 1447872.A0A1J9QCV4; -.
DR   VEuPathDB; FungiDB:AJ78_01927; -.
DR   OrthoDB; 1429290at2759; -.
DR   Proteomes; UP000182235; Unassembled WGS sequence.
DR   GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredoxin) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); IEA:InterPro.
DR   CDD; cd01713; PAPS_reductase; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00063; CysH; 1.
DR   InterPro; IPR004511; PAPS/APS_Rdtase.
DR   InterPro; IPR002500; PAPS_reduct.
DR   InterPro; IPR011800; PAPS_reductase_CysH.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00434; cysH; 1.
DR   NCBIfam; TIGR02057; PAPS_reductase; 1.
DR   PANTHER; PTHR46509; PHOSPHOADENOSINE PHOSPHOSULFATE REDUCTASE; 1.
DR   PANTHER; PTHR46509:SF1; PHOSPHOADENOSINE PHOSPHOSULFATE REDUCTASE; 1.
DR   Pfam; PF01507; PAPS_reduct; 1.
DR   PIRSF; PIRSF000857; PAPS_reductase; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182235}.
FT   DOMAIN          69..246
FT                   /note="Phosphoadenosine phosphosulphate reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01507"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   300 AA;  34186 MW;  41F846EFBC56769A CRC64;
     MPSKIASSYP SDSEHMETES GYVSGSTSEA SLPELVFTKP HLKFLNSQLQ FLEPQDILRW
     CITTLPGLYQ TTAFGLTGLV TLDMLSKLNI PRPRLVDLIF LDTLHHFQET HALIDRVRKH
     YPSTNIHIYN PEGVSTAEEF SQKYGPKLWE TSDQLYDWVA KVEPAQRAYR ELQVNAVLTG
     RRRSQGGKRG DLDIIEVDET GLIKINPLAN WSFAQVKNYI TEHNVPYNEL LDRGYKSIGD
     WHSTQPVKEN EDERSGRWKG QQKTECGIHN PLSKYAQFLR DQELKRQGEA LSQALKAGGD
//
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