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
//