ID A0A1I7WMM1_HETBA Unreviewed; 316 AA.
AC A0A1I7WMM1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 03-JUL-2019, entry version 10.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
OS Heterorhabditis bacteriophora (Entomopathogenic nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC Strongyloidea; Heterorhabditidae; Heterorhabditis.
OX NCBI_TaxID=37862 {ECO:0000313|Proteomes:UP000095283, ECO:0000313|WBParaSite:Hba_06403};
RN [1] {ECO:0000313|Proteomes:UP000095283, ECO:0000313|WBParaSite:Hba_06403}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23874975; DOI=10.1371/journal.pone.0069618;
RA Bai X., Adams B.J., Ciche T.A., Clifton S., Gaugler R., Kim K.S.,
RA Spieth J., Sternberg P.W., Wilson R.K., Grewal P.S.;
RT "A lover and a fighter: the genome sequence of an entomopathogenic
RT nematode Heterorhabditis bacteriophora.";
RL PLoS ONE 8:e69618-e69618(2013).
RN [2] {ECO:0000313|WBParaSite:Hba_06403}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000256|SAAS:SAAS01116782};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-
CC [protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-
CC COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977;
CC EC=3.1.3.16; Evidence={ECO:0000256|RuleBase:RU004273,
CC ECO:0000256|SAAS:SAAS01116780};
CC -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC {ECO:0000256|RuleBase:RU004273, ECO:0000256|SAAS:SAAS01017257}.
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DR WBParaSite; Hba_06403; Hba_06403; Hba_06403.
DR Proteomes; UP000095283; Whole Genome Shotgun Assembly.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR031675; STPPase_N.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW Complete proteome {ECO:0000313|Proteomes:UP000095283};
KW Hydrolase {ECO:0000256|RuleBase:RU004273,
KW ECO:0000256|SAAS:SAAS01017252};
KW Manganese {ECO:0000256|SAAS:SAAS01017251};
KW Metal-binding {ECO:0000256|SAAS:SAAS01017255};
KW Protein phosphatase {ECO:0000256|SAAS:SAAS01017274}.
FT DOMAIN 118 123 SER_THR_PHOSPHATASE.
FT {ECO:0000259|PROSITE:PS00125}.
SQ SEQUENCE 316 AA; 35358 MW; C5FBDFF90979B713 CRC64;
MAQLDVDNLM CRLLNVGVAG GRLTTSVSEQ ELQLCCQTAK AVFMNQPSLI ECEPPIVVCG
DIHGQYSDLL RIFDKNGFPP ETNYLFLGDY VDRGRQNIET ICLMFCYKIK YPESFFMLRG
NHECPAINRV YGWGKSIENE IMIIINLTAN YLVSSTTTLQ DTFNWMPLCG LIGGRILCMH
GGLSPQLTSL DDLRNIPRPQ DPANPSMGID LLWADPDQWV KGWQANTRGV SYVFGQDVVA
EMCSKLNIDL IARAHQVVQD GYEFFASKKM VTIFSAPHYC GQFDNYAATM KVNEDLLCNF
AMYKPTAKAA RIAAVG
//
