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Database: UniProt
Entry: Q585I6_TRYB2
LinkDB: Q585I6_TRYB2
Original site: Q585I6_TRYB2 
ID   Q585I6_TRYB2            Unreviewed;       294 AA.
AC   Q585I6; D6XFV0;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   16-OCT-2019, entry version 107.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=Tb927.4.3640 {ECO:0000313|EMBL:AAX79219.1};
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:AAX79219.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GUTat10.1 {ECO:0000313|EMBL:AAX79219.1};
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 (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAX79219.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GUTat10.1 {ECO:0000313|EMBL:AAX79219.1};
RA   El-Sayed N.M., Khalak H., Adams M.D.;
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AAZ10955.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:AAZ10955.1};
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:AAZ10955.1, ECO:0000313|Proteomes:UP000008524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:AAZ10955.1,
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:AAX79219.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GUTat10.1 {ECO:0000313|EMBL:AAX79219.1};
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; AC023489; AAX79219.1; -; Genomic_DNA.
DR   EMBL; CP000067; AAZ10955.1; -; Genomic_DNA.
DR   RefSeq; XP_844514.1; XM_839421.1.
DR   STRING; 5691.AAZ10955; -.
DR   GeneDB; Tb927.4.3640:pep; -.
DR   GeneID; 3656897; -.
DR   KEGG; tbr:Tb927.4.3640; -.
DR   EuPathDB; TriTrypDB:Tb927.4.3640; -.
DR   HOGENOM; HOG000172697; -.
DR   KO; K01090; -.
DR   OMA; ECKRRSN; -.
DR   Proteomes; UP000008524; Chromosome 4.
DR   GO; GO:0005929; C:cilium; IDA:GeneDB.
DR   GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016787; F:hydrolase activity; ISM:GeneDB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISM:GeneDB.
DR   GO; GO:0044145; P:modulation of development of symbiont involved in interaction with host; IMP:GeneDB.
DR   GO; GO:0006470; P:protein dephosphorylation; ISM:GeneDB.
DR   GO; GO:0052106; P:quorum sensing involved in interaction with host; IMP:GeneDB.
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:AAX79219.1};
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      116    121       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
SQ   SEQUENCE   294 AA;  33578 MW;  96AFC75E3D2909F7 CRC64;
     MTLVQTLLER MLSAKGNTAQ RQILIREEDI RTILNAVRDV FMSQPVVLDI TPPVRICGDI
     HGQYYDLLRV FEKCGFPPYS NYLFLGDYVD RGRHSVETIT LLFCYKIVYP ENFFLLRGNH
     ECASINKMYG FFDDVKRRYN IKLFKAFTDV FNTMPVCCVV GEKIICMHGG LSPDMTSLAA
     VNEIERPLDV PDKGILCDLL WADPEEEVKG FLESDRGVSY LFGEDIVTDF LDMVDMDLVV
     RAHQVMERGY GFFANRQLVT IFSAPNYCGE FDNDAAVMNV DEKLQCSFAI IAAR
//
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