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Database: UniProt
Entry: A0A1V8SA32_9PEZI
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Original site: A0A1V8SA32_9PEZI 
ID   A0A1V8SA32_9PEZI        Unreviewed;       301 AA.
AC   A0A1V8SA32;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Phosphoadenosine phosphosulfate reductase {ECO:0000313|EMBL:OQN95721.1};
GN   ORFNames=B0A48_18261 {ECO:0000313|EMBL:OQN95721.1};
OS   Rachicladosporium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX   NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQN95721.1, ECO:0000313|Proteomes:UP000192596};
RN   [1] {ECO:0000313|Proteomes:UP000192596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA   Coleine C., Masonjones S., Stajich J.E.;
RT   "Genomes of endolithic fungi from Antarctica.";
RL   Submitted (MAR-2017) 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:OQN95721.1}.
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DR   EMBL; NAJO01000080; OQN95721.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V8SA32; -.
DR   STRING; 1507870.A0A1V8SA32; -.
DR   InParanoid; A0A1V8SA32; -.
DR   OrthoDB; 1429290at2759; -.
DR   Proteomes; UP000192596; 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   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:UP000192596}.
FT   DOMAIN          64..242
FT                   /note="Phosphoadenosine phosphosulphate reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01507"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          237..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..258
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   301 AA;  34327 MW;  8F49FDE78ACD151E CRC64;
     MAFRQRSSSS DRDGAESGYA SGSSIASLPD VYFTRPHLKF VNAQLNRLEP QEVLKWCLTS
     FPQLYQTSAF GLTGLAIMDM VANIDFPINP DIECIFLDTL YHFPQTMDLV EKVKQRYPQL
     KLHIYKPEGC ETTADFEAKF GEKLWETDDE RYDFLAKVEP AQRAYRELDV KAVLTGRRKT
     QGGKRGDIDI VEVDDAGLIK LNPLANWSFK QVQTYIKEHD VPTNDLLDQG YRSVGDWHST
     QPVTDSEDER AGRWKGKGKT ECGIHNKRSR YAMFLQEQEE QRQRELSEAI SKGLNISAVG
     S
//
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