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Database: UniProt
Entry: K1VT13_TRIAC
LinkDB: K1VT13_TRIAC
Original site: K1VT13_TRIAC 
ID   K1VT13_TRIAC            Unreviewed;       256 AA.
AC   K1VT13;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Phosphoadenosine phosphosulphate reductase domain-containing protein {ECO:0000259|Pfam:PF01507};
GN   ORFNames=A1Q2_05891 {ECO:0000313|EMBL:EKC99812.1};
OS   Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Trichosporon.
OX   NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKC99812.1, ECO:0000313|Proteomes:UP000006757};
RN   [1] {ECO:0000313|EMBL:EKC99812.1, ECO:0000313|Proteomes:UP000006757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 8904 {ECO:0000313|EMBL:EKC99812.1,
RC   ECO:0000313|Proteomes:UP000006757};
RX   PubMed=23193141; DOI=10.1128/EC.00264-12;
RA   Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT   "Genome sequence of the Trichosporon asahii environmental strain CBS
RT   8904.";
RL   Eukaryot. Cell 11:1586-1587(2012).
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:EKC99812.1}.
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DR   EMBL; AMBO01000361; EKC99812.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1VT13; -.
DR   STRING; 1220162.K1VT13; -.
DR   eggNOG; KOG0189; Eukaryota.
DR   HOGENOM; CLU_044089_0_1_1; -.
DR   InParanoid; K1VT13; -.
DR   OMA; PIARWTQ; -.
DR   OrthoDB; 1429290at2759; -.
DR   Proteomes; UP000006757; Unassembled WGS sequence.
DR   GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredoxin) activity; IEA:InterPro.
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   InterPro; IPR004511; PAPS/APS_Rdtase.
DR   InterPro; IPR002500; PAPS_reduct.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00434; cysH; 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:UP000006757}.
FT   DOMAIN          68..204
FT                   /note="Phosphoadenosine phosphosulphate reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01507"
FT   REGION          200..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   256 AA;  28385 MW;  A105D14E3D739582 CRC64;
     MTVDSDVLTP QYSPEQLEQI NKELDGKSPQ EVLAWAIDNI DGLYQTTAFG LTGLAAVDMI
     SKISQDREET HLVPLNVADT YIAPLHVYRP PGAETADEFA AKYGEKLWET DEASYDYLVK
     VEPAARAYKE LGVRAVITGR RRSQGADRSN LAAVEVDERG LIKVNPLITW SFKEVKDYVD
     REGVPYNSLL DQGYKSIGDW HSTAKPDPNA SDAGERSGRW QGKAKSECGL HTNYFEMKKK
     FEEKAAAQAA ANAPVQ
//
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