ID G3JI44_CORMM Unreviewed; 394 AA.
AC G3JI44;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN ORFNames=CCM_05154 {ECO:0000313|EMBL:EGX90997.1};
OS Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX90997.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX90997.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX90997.1,
RC ECO:0000313|Proteomes:UP000001610};
RX PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT valued traditional Chinese medicine.";
RL Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
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 -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-6 (PP-V)
CC subfamily. {ECO:0000256|ARBA:ARBA00038400}.
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DR EMBL; JH126402; EGX90997.1; -; Genomic_DNA.
DR RefSeq; XP_006670362.1; XM_006670299.1.
DR AlphaFoldDB; G3JI44; -.
DR STRING; 983644.G3JI44; -.
DR GeneID; 18167173; -.
DR KEGG; cmt:CCM_05154; -.
DR VEuPathDB; FungiDB:CCM_05154; -.
DR eggNOG; KOG0373; Eukaryota.
DR HOGENOM; CLU_004962_8_3_1; -.
DR InParanoid; G3JI44; -.
DR OMA; MEGFKYH; -.
DR OrthoDB; 19833at2759; -.
DR Proteomes; UP000001610; Unassembled WGS sequence.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd07415; MPP_PP2A_PP4_PP6; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR047129; PPA2-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR PANTHER; PTHR45619; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A-RELATED; 1.
DR PANTHER; PTHR45619:SF10; SERINE_THREONINE-PROTEIN PHOSPHATASE 6 CATALYTIC SUBUNIT; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF033096; PPPtase_5; 2.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004273};
KW Reference proteome {ECO:0000313|Proteomes:UP000001610}.
FT DOMAIN 196..201
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 110..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 394 AA; 43667 MW; B6E23115E59C3F86 CRC64;
MTSSVPRPGP ANLSSNAGLD EWLEEAKQCH YLPERAMKEL CEKVKEILME ESNIQPVCTP
VTVCGDIHGQ FYDLLELFRV AGGMPGESHV EAPKTATAVI TSQDIEPPEI TNPKLLRKLK
PSNDDATNDD AGDDAERATA TAAGSADINS PVTSSQSAET RFIFLGDFVD RGYFSLETFT
LLMCLKAKYP ERIVLVRGNH ESRQITQVYG FYEECQQKYG NASVWKACCH VFDFLVLAAI
VDGEVLCVHG GLSPEIRTID QIRVVARAQE IPHEGAFCDL VWSDPEDVET WAISPRGAGW
LFGDKVATEF NHVNGLKLIA RAHQLVNEGY KYHFVEKSVV TVWSAPNYCY RCGNVASIMT
VDQDLDPKFS IFSAVPDDQR HVPAGRRGPS DYFL
//
