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Database: UniProt
Entry: A0A1I7WMM1_HETBA
LinkDB: A0A1I7WMM1_HETBA
Original site: A0A1I7WMM1_HETBA 
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
//
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