ID V5U5Q7_PLUXY Unreviewed; 495 AA.
AC V5U5Q7;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
OS Plutella xylostella (Diamondback moth) (Plutella maculipennis).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Yponomeutoidea;
OC Plutellidae; Plutella.
OX NCBI_TaxID=51655 {ECO:0000313|EMBL:AHB72693.1};
RN [1] {ECO:0000313|EMBL:AHB72693.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24132154;
RA Chen X., Zhang Y.;
RT "Molecular cloning and characterization of the calcineurin subunit A from
RT Plutella xylostella.";
RL Int. J. Mol. Sci. 14:20692-20703(2013).
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 ECO:0000256|RuleBase:RU004273};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000256|ARBA:ARBA00001965};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B subfamily.
CC {ECO:0000256|ARBA:ARBA00009905}.
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DR EMBL; KF425265; AHB72693.1; -; mRNA.
DR RefSeq; NP_001296069.1; NM_001309140.1.
DR AlphaFoldDB; V5U5Q7; -.
DR GeneID; 105384905; -.
DR KEGG; pxy:105384905; -.
DR OrthoDB; 1488111at2759; -.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0097720; P:calcineurin-mediated signaling; IEA:InterPro.
DR CDD; cd07416; MPP_PP2B; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041751; MPP_PP2B.
DR InterPro; IPR043360; PP2B.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR PANTHER; PTHR45673; SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT 1-RELATED; 1.
DR PANTHER; PTHR45673:SF1; SERINE_THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT 1-RELATED; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 2: Evidence at transcript level;
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004273};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 145..150
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 461..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 495 AA; 55979 MW; 9713F5621887F0CC CRC64;
MSGSNDKVST TQRMIQSVAF PPSHKLTVSE VFDEKSGKPL PEVLKQHFTL EGRIEENAAL
RIIQDGATLL RSEKTMIEID SPVTVCGDVH GQFYDLMKLF EVGGSPSCTK YLFLGDHVDR
GYFSIECVLY LWALKLCFPK TLFLLRGNHE CRHLTEYFTF KQECKIKYSE KVYDACMDAF
DCLPLAALMN QQFLCVHGGL SPEINNLDDI RKLDRFKEPP AFGAMCDLLW SDPLEDFGNE
KNAEHFSHNS VRGCSYFYSY AACCDFLQRN NLLSIIRAHE AQDAGYRMYR KSQTTGFPSL
ITIFSAPNYL DVYNNKAAVL KYENNVMNIR QFNCSPHPYW LPNFMDVFTW SLPFVGEKVT
EMLVNVLNIC SDDELMTEGE EALEEANLRK EVIRNKIRAI GKMAHVFSVL REESESVLQL
KGLTPTGALP LGALSGGKTS LKNALQGFSP NHKITSFAEA KGLDAINERM PPRRDGQRTP
DPQEKKPHVN SNAHS
//
