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Database: UniProt
Entry: A0A2S4UFB7_9BASI
LinkDB: A0A2S4UFB7_9BASI
Original site: A0A2S4UFB7_9BASI 
ID   A0A2S4UFB7_9BASI        Unreviewed;       597 AA.
AC   A0A2S4UFB7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=PSTT_15911 {ECO:0000313|EMBL:POV95977.1};
OS   Puccinia striiformis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=27350 {ECO:0000313|EMBL:POV95977.1, ECO:0000313|Proteomes:UP000239156};
RN   [1] {ECO:0000313|EMBL:POV95977.1, ECO:0000313|Proteomes:UP000239156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-210 {ECO:0000313|EMBL:POV95977.1,
RC   ECO:0000313|Proteomes:UP000239156};
RA   Xia C.;
RT   "Gene loss provides genomic basis for host adaptation in cereal stripe rust
RT   fungi.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU004273};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-5 (PP-T)
CC       subfamily. {ECO:0000256|ARBA:ARBA00008786}.
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:POV95977.1}.
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DR   EMBL; PKSL01000317; POV95977.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S4UFB7; -.
DR   VEuPathDB; FungiDB:PSHT_15265; -.
DR   VEuPathDB; FungiDB:PSTT_15911; -.
DR   Proteomes; UP000239156; Unassembled WGS sequence.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR013235; PPP_dom.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR45668:SF5; SERINE/THREONINE-PROTEIN PHOSPHATASE 5; 1.
DR   PANTHER; PTHR45668; SERINE/THREONINE-PROTEIN PHOSPHATASE 5-RELATED; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF08321; PPP5; 1.
DR   PIRSF; PIRSF033096; PPPtase_5; 2.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
DR   PROSITE; PS50005; TPR; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004273};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000239156};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT   REPEAT          162..195
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          374..379
FT                   /note="Serine/threonine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          67..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   597 AA;  66716 MW;  1C4760EB0B0399D1 CRC64;
     MASSSSSGDN QPSSPPPEDS RAPLGMLFDN QDSHENVELT SLSLEISFCF GNRIWSQVNA
     YDPSLDGTSV ASNPSNGVRP TDKSQLSQET IDEALRLKSE ANQRFTASQY QEALDLYTLS
     INTNPFDATV WCNRSAVRLK REEHGLAIMD TSKAIELDPK YVKAYFRRAT AQLSIMKPQL
     AIKDFKKCMA LDPSNAAARV QLDATTKLVR RLEFEKAIAS EDEEATSKRI RKLISEGACE
     LDNSYTGPML SKTEDGWKPS LEFIQGMLEW FKAGKTLPKR WVYEIILGCQ SVLLKEASMT
     EYTIPQNETC DVIGDTHGQF FDVLHLLSLT GLPPKHMLLV IFNGDFVDRG SWSTEVVLTV
     FALKWYMPHK VFLNRGNHET ADMNKVYGFE GETKKKYSEL CYKLFEEVFC ALPLCCLVTA
     SQQPESSEIS KVPAKPFFDA EGRKRFFIVH GGLFSKDEVS FDELKKIPRM VRKQPGNEGL
     MMECLWTDPQ DAPGRGPSKR GVGLGFGPDI TENWCRHSGV TAVIRSHEVR DNGYSIEHEG
     RCITVFSAPN YVDQVGNQGG FVRINEHGTL AFTSFKHQPH PNIKPMAYAG GFMGLGG
//
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