ID E0VUA3_PEDHC Unreviewed; 307 AA.
AC E0VUA3;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN Name=8231236 {ECO:0000313|EnsemblMetazoa:PHUM448770-PA};
GN ORFNames=Phum_PHUM448770 {ECO:0000313|EMBL:EEB16959.1};
OS Pediculus humanus subsp. corporis (Body louse).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC Pediculus.
OX NCBI_TaxID=121224;
RN [1] {ECO:0000313|EMBL:EEB16959.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB16959.1};
RA Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA Amedeo P., Strausberg R.;
RT "Annotation of Pediculus humanus corporis strain USDA.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEB16959.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB16959.1};
RG The Human Body Louse Genome Consortium;
RA Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT "The genome of the human body louse.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:PHUM448770-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM448770-PA};
RG EnsemblMetazoa;
RL Submitted (FEB-2021) to UniProtKB.
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-4 (PP-X)
CC subfamily. {ECO:0000256|ARBA:ARBA00038328}.
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DR EMBL; AAZO01005475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS235784; EEB16959.1; -; Genomic_DNA.
DR RefSeq; XP_002429697.1; XM_002429652.1.
DR AlphaFoldDB; E0VUA3; -.
DR STRING; 121224.E0VUA3; -.
DR EnsemblMetazoa; PHUM448770-RA; PHUM448770-PA; PHUM448770.
DR GeneID; 8231236; -.
DR KEGG; phu:Phum_PHUM448770; -.
DR CTD; 8231236; -.
DR VEuPathDB; VectorBase:PHUM448770; -.
DR eggNOG; KOG0372; Eukaryota.
DR HOGENOM; CLU_004962_8_1_1; -.
DR InParanoid; E0VUA3; -.
DR OMA; QSTMPID; -.
DR OrthoDB; 19833at2759; -.
DR Proteomes; UP000009046; 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:SF8; SERINE_THREONINE-PROTEIN PHOSPHATASE 4 CATALYTIC SUBUNIT; 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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004273, ECO:0000313|EMBL:EEB16959.1};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000009046}.
FT DOMAIN 111..116
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
SQ SEQUENCE 307 AA; 35102 MW; FC41DA22BA04746B CRC64;
MSETSELDRQ IEQLKKCEII KESEVKALCA KAREILIEES NVQRVDSPVT VCGDIHGQFY
DLKELFKVGG DVPETNYLFM GDFVDRGFYS VETFLLLLAL KVRYPDRITL IRGNHESRQI
TQVYGFYDEC LRKYGSIAVW RYCTEIFDYL SLSAIIDGKI FCVHGGLSPS IHTLDQIRTI
DRKQEVPHDG PMCDLLWSDP EDTQGWGVSP RGAGFLFGSD VVAQFNTAND IDMICRAHQL
VMEGFKWHFN ETVLTVWSAP NYCYRCGNVA AILELNEHLQ RDFTIFEAAP QESRGIPLKK
PQADYFL
//
