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Database: UniProt
Entry: Q584K2_TRYB2
LinkDB: Q584K2_TRYB2
Original site: Q584K2_TRYB2 
ID   Q584K2_TRYB2            Unreviewed;       346 AA.
AC   Q584K2; D6XER0;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   16-OCT-2019, entry version 110.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=Tb927.4.5030 {ECO:0000313|EMBL:AAX80549.1};
OS   Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC   Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=185431 {ECO:0000313|Proteomes:UP000008524};
RN   [1] {ECO:0000313|EMBL:AAX80549.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GUTat10.1 {ECO:0000313|EMBL:AAX80549.1};
RA   El-Sayed N.M., Khalak H., Adams M.D.;
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAX80549.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GUTat10.1 {ECO:0000313|EMBL:AAX80549.1};
RA   Ghedin E., Blandin G., Bartholomeu D., Caler E., Haas B., Hannick L.,
RA   Shallom J., Hou L., Djikeng A., Feldblyum T., Hostetler J.,
RA   Johnson J., Jones K., Koo H.L., Larkin C., Pai G., Peterson J.,
RA   Khalak H.G., Salzberg S., Simpson A.J., Tallon L., Van Aken S.,
RA   Wanless D., White O., Wortman J., Fraser C.M., El-Sayed N.M.A.;
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AAZ11093.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:AAZ11093.1};
RX   PubMed=16020724; DOI=10.1126/science.1112181;
RA   El-Sayed N.M., Myler P.J., Blandin G., Berriman M., Crabtree J.,
RA   Aggarwal G., Caler E., Renauld H., Worthey E.A., Hertz-Fowler C.,
RA   Ghedin E., Peacock C., Bartholomeu D.C., Haas B.J., Tran A.N.,
RA   Wortman J.R., Alsmark U.C., Angiuoli S., Anupama A., Badger J.,
RA   Bringaud F., Cadag E., Carlton J.M., Cerqueira G.C., Creasy T.,
RA   Delcher A.L., Djikeng A., Embley T.M., Hauser C., Ivens A.C.,
RA   Kummerfeld S.K., Pereira-Leal J.B., Nilsson D., Peterson J.,
RA   Salzberg S.L., Shallom J., Silva J.C., Sundaram J., Westenberger S.,
RA   White O., Melville S.E., Donelson J.E., Andersson B., Stuart K.D.,
RA   Hall N.;
RT   "Comparative genomics of trypanosomatid parasitic protozoa.";
RL   Science 309:404-409(2005).
RN   [4] {ECO:0000313|EMBL:AAZ11093.1, ECO:0000313|Proteomes:UP000008524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:AAZ11093.1,
RC   ECO:0000313|Proteomes:UP000008524};
RX   PubMed=16020726; DOI=10.1126/science.1112642;
RA   Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA   Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B.,
RA   Bohme U., Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L.,
RA   Wickstead B., Alsmark U.C.M., Arrowsmith C., Atkin R.J., Barron A.J.,
RA   Bringaud F., Brooks K., Carrington M., Cherevach I.,
RA   Chillingworth T.J., Churcher C., Clark L.N., Corton C.H., Cronin A.,
RA   Davies R.M., Doggett J., Djikeng A., Feldblyum T., Field M.C.,
RA   Fraser A., Goodhead I., Hance Z., Harper D., Harris B.R., Hauser H.,
RA   Hostetler J., Ivens A., Jagels K., Johnson D., Johnson J., Jones K.,
RA   Kerhornou A.X., Koo H., Larke N., Landfear S., Larkin C., Leech V.,
RA   Line A., Lord A., Macleod A., Mooney P.J., Moule S., Martin D.M.,
RA   Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA   Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E.,
RA   Rajandream M.A., Reitter C., Salzberg S.L., Sanders M., Schobel S.,
RA   Sharp S., Simmonds M., Simpson A.J., Tallon L., Turner C.M., Tait A.,
RA   Tivey A.R., Van Aken S., Walker D., Wanless D., Wang S., White B.,
RA   White O., Whitehead S., Woodward J., Wortman J., Adams M.D.,
RA   Embley T.M., Gull K., Ullu E., Barry J.D., Fairlamb A.H.,
RA   Opperdoes F., Barrell B.G., Donelson J.E., Hall N., Fraser C.M.,
RA   Melville S.E., El-Sayed N.M.A.;
RT   "The genome of the African trypanosome Trypanosoma brucei.";
RL   Science 309:416-422(2005).
RN   [5] {ECO:0000313|EMBL:AAX80549.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GUTat10.1 {ECO:0000313|EMBL:AAX80549.1};
RA   Haas B., Blandin G., El-Sayed N.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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   EMBL; AC079815; AAX80549.1; -; Genomic_DNA.
DR   EMBL; CP000067; AAZ11093.1; -; Genomic_DNA.
DR   RefSeq; XP_844652.1; XM_839559.1.
DR   STRING; 5691.AAZ11093; -.
DR   GeneDB; Tb927.4.5030:pep; -.
DR   GeneID; 3657039; -.
DR   KEGG; tbr:Tb927.4.5030; -.
DR   EuPathDB; TriTrypDB:Tb927.4.5030; -.
DR   HOGENOM; HOG000172697; -.
DR   KO; K01090; -.
DR   OMA; QYNGINS; -.
DR   Proteomes; UP000008524; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
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:UP000008524};
KW   Hydrolase {ECO:0000256|RuleBase:RU004273,
KW   ECO:0000256|SAAS:SAAS01017252, ECO:0000313|EMBL:AAX80549.1};
KW   Manganese {ECO:0000256|SAAS:SAAS01017251};
KW   Metal-binding {ECO:0000256|SAAS:SAAS01017255};
KW   Protein phosphatase {ECO:0000256|SAAS:SAAS01017274};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008524}.
FT   DOMAIN      159    164       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
FT   REGION       46     65       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   346 AA;  39346 MW;  890CCD82F785A0A0 CRC64;
     MNCDEIIKKL LLNPVHNTAA TRGPAGENCE SNQRTYTRIS RLAAFQSAQT QESTPKTNGT
     GRATTEGLTE AEVRWLVMES RALFMSQPML VEIAAPVRIC GDVHGQYTDL LRLFDLGGFP
     PDANYIFLGD YVDRGDQSLE TICLLLAYKL SFPETFFLLR GNHECSSINR IYGFFDECKR
     RYSVRLWKQF TDTFNCMPVA GLVEGRILCM HGGLSPELTD LDQIRRILRP TDVPDSGLIC
     DLLWSDPSTN MESNWSENDR GVSWTFSESV VKSFNKKFDL DLICRAHQVV DAGYEFFAAR
     QLVTVFSAPN YCDEFDNAGA FMCVDENFMC SFIRIEPTRT LLRYFF
//
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