ID A0A409XNK3_PSICY Unreviewed; 769 AA.
AC A0A409XNK3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=CVT25_008745 {ECO:0000313|EMBL:PPQ92395.1};
OS Psilocybe cyanescens.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Psilocybe.
OX NCBI_TaxID=93625 {ECO:0000313|EMBL:PPQ92395.1, ECO:0000313|Proteomes:UP000283269};
RN [1] {ECO:0000313|EMBL:PPQ92395.1, ECO:0000313|Proteomes:UP000283269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2631 {ECO:0000313|EMBL:PPQ92395.1,
RC ECO:0000313|Proteomes:UP000283269};
RX PubMed=30283667; DOI=10.1002/evl3.42;
RA Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA Matheny P.B., Slot J.C.;
RT "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT diversity.";
RL Evol. Lett. 2:88-101(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001512};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001482};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SSU72 phosphatase family.
CC {ECO:0000256|ARBA:ARBA00008978}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000256|PROSITE-
CC ProRule:PRU00808}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC {ECO:0000256|ARBA:ARBA00025719}.
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:PPQ92395.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NHYD01001049; PPQ92395.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A409XNK3; -.
DR STRING; 93625.A0A409XNK3; -.
DR InParanoid; A0A409XNK3; -.
DR OrthoDB; 166567at2759; -.
DR Proteomes; UP000283269; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IEA:UniProtKB-UniRule.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd03750; proteasome_alpha_type_2; 1.
DR CDD; cd03016; PRX_1cys; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR045020; PRX_1cys.
DR InterPro; IPR006811; RNA_pol_II_suA.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR20383; RNA POLYMERASE II SUBUNIT A C-TERMINAL DOMAIN PHOSPHATASE; 1.
DR PANTHER; PTHR20383:SF9; RNA POLYMERASE II SUBUNIT A C-TERMINAL DOMAIN PHOSPHATASE SSU72; 1.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF04722; Ssu72; 1.
DR SMART; SM00948; Proteasome_A_N; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Antioxidant {ECO:0000256|ARBA:ARBA00022862};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|PROSITE-
KW ProRule:PRU00808}; Reference proteome {ECO:0000313|Proteomes:UP000283269}.
FT DOMAIN 294..461
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 769 AA; 84715 MW; 7094F610E77C92B4 CRC64;
MDPRRARDPR LARADPRLQQ SQAAQSTPVV PSVSYNAQYN TIPTHQWEEN VTANTSSSLE
ATFQTQATAP ISSDIPNSQT PTNANPPMSA SSSAAVYKPR PLFCVNRSME GHHVLAKAGY
RVISSGTGSA VRLPGPSIDK PNIYPFGTAY NAIYEELSSK DPRLYTANGL LPMLDRNRHI
KLAPERWQDS KTVADIVITC EERCFDAVCD DLLTRGGEFN KPVHVINMEI KDNHEEALIA
GKAMIDLAAA IEGADDIDES IDKILEVQQE KHPHSLLHAV LVTGSKALKE MPSLRLGNIA
PDFEAQTTEG PIKFHDWIGD SWAILFSHPG DFTPVCTTEL GEVARRSEDF KKRNVKVIGI
SANGLDEHEK WVKDINSYGA STGPTDVQFP IIADPDRKIS TLYDMLDEQD ATNRDAKGLP
FTIRTVFVID PKKTIRLTLA YPASTGRNFD EIIRVVDCET LFNWLITELL NLNDFIALQI
GDKHRVTTPV NWKKGDDVIV HPSVSNDEAK TLFPQFSQHL CRGCYSLTVF SPSGKLVQIE
HALAAVSQGT TSLGIKATNG IVIATEKKTS SILIDDSVIE KVATICPNIG IVYSGMGPDF
RILVTKARKS AQAYWKIYGE YPPTRVLTQE IATVMQQATQ SGGVRPYGVS LLVAGWDSHR
GPSLYQVDPS GSFWAWKASA IGKNMINAKT FLEKRYNDDI SLEDAIHTAL LTLKEGFEGQ
MTEKTIEIGV VTVPTPAELE EGKIGGETGR PKPTFRKLSE EEVRDYLAL
//
