GenomeNet

Database: UniProt
Entry: A0A061IUX9_TRYRA
LinkDB: A0A061IUX9_TRYRA
Original site: A0A061IUX9_TRYRA 
ID   A0A061IUX9_TRYRA        Unreviewed;      2434 AA.
AC   A0A061IUX9;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE            EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN   ORFNames=TRSC58_06676 {ECO:0000313|EMBL:ESL05666.1};
OS   Trypanosoma rangeli SC58.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Herpetosoma.
OX   NCBI_TaxID=429131 {ECO:0000313|EMBL:ESL05666.1, ECO:0000313|Proteomes:UP000031737};
RN   [1] {ECO:0000313|EMBL:ESL05666.1, ECO:0000313|Proteomes:UP000031737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC58 {ECO:0000313|EMBL:ESL05666.1,
RC   ECO:0000313|Proteomes:UP000031737};
RA   Stoco P.H., Wagner G., Gerber A., Zaha A., Thompson C., Bartholomeu D.C.,
RA   Luckemeyer D.D., Bahia D., Loreto E., Prestes E.B., Lima F.M.,
RA   Rodrigues-Luiz G., Vallejo G.A., Filho J.F., Monteiro K.M., Tyler K.M.,
RA   de Almeida L.G., Ortiz M.F., Siervo M.A., de Moraes M.H., Cunha O.L.,
RA   Mendonca-Neto R., Silva R., Teixeira S.M., Murta S.M., Sincero T.C.,
RA   Mendes T.A., Urmenyi T.P., Silva V.G., da Rocha W.D., Andersson B.,
RA   Romanha A.J., Steindel M., de Vasconcelos A.T., Grisard E.C.;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775,
CC         ECO:0000256|RuleBase:RU364109};
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC       {ECO:0000256|ARBA:ARBA00011031, ECO:0000256|RuleBase:RU364109}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ESL05666.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AUPL01006676; ESL05666.1; -; Genomic_DNA.
DR   EnsemblProtists; ESL05666; ESL05666; TRSC58_06676.
DR   VEuPathDB; TriTrypDB:TRSC58_06676; -.
DR   OrthoDB; 8448at2759; -.
DR   Proteomes; UP000031737; Unassembled WGS sequence.
DR   GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
DR   GO; GO:0010507; P:negative regulation of autophagy; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR   CDD; cd05169; PIKKc_TOR; 1.
DR   Gene3D; 1.20.120.150; FKBP12-rapamycin binding domain; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003152; FATC_dom.
DR   InterPro; IPR009076; FRB_dom.
DR   InterPro; IPR036738; FRB_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR024585; mTOR_dom.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR   InterPro; IPR018936; PI3/4_kinase_CS.
DR   InterPro; IPR003151; PIK-rel_kinase_FAT.
DR   InterPro; IPR014009; PIK_FAT.
DR   InterPro; IPR026683; TOR_cat.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR   PANTHER; PTHR11139:SF126; SERINE_THREONINE-PROTEIN KINASE TOR; 1.
DR   Pfam; PF11865; DUF3385; 1.
DR   Pfam; PF02259; FAT; 1.
DR   Pfam; PF02260; FATC; 1.
DR   Pfam; PF08771; FRB_dom; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   SMART; SM01346; DUF3385; 1.
DR   SMART; SM01343; FATC; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SMART; SM01345; Rapamycin_bind; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF47212; FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP); 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS51189; FAT; 1.
DR   PROSITE; PS51190; FATC; 1.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364109};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU364109};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU364109};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031737};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU364109};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364109}.
FT   DOMAIN          1287..1859
FT                   /note="FAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51189"
FT   DOMAIN          2034..2354
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          2402..2434
FT                   /note="FATC"
FT                   /evidence="ECO:0000259|PROSITE:PS51190"
SQ   SEQUENCE   2434 AA;  273696 MW;  EBDB5B66A1AC762C CRC64;
     MFTIAGKDNL ASTIRRIADD PARRTAVVEE EIKRTKELQR KNLQEYESTV SSLLICLENF
     DVVRGDAPEI TCALTVLDIL LRLDLTTIQI SQCSSYARLC LCAVSDTSIA PAAARTFAET
     LVNSMTSDFA RMEIDETLSW IELPDDSMRA RRICGLLVLQ QVALRIPMLI LPKLGTLCEK
     LWSGLASSDG MIRDTSAQLF KVCGKLLSNR SPTLRIKTVD TLLSQLKSNL AAKSRESNLA
     GLLAFETVVM SSIGGSSQPR YEDLSIMLVP YIMSGGSSAN SELVQKLLFH CLVVLCRYNT
     TLFIINHLKD TVSFALKSIR NLFQHCTAFD MLSDIIPMVG KSAFTSFVKE TCEAVCFISE
     MSPTPCWESL KCFSVIFREC PPPDVESYID PCIENVFNWG LSSQLIECMR DIISLSSIKG
     RTKLEEALLD MISVTLCGLP FRQVAGTRIK TGNYPDSEPT ESQIVVALDA LIQFGFSDSE
     LMGDFLRDSV LPLIDSPSAC VRNAAVNTIV SLLIPPGIKG ELTMARRICV DMIVSRMLVV
     GLANPDPVIR ATILSSFTQS FYPYLSELQF LTQLFSALGD EDICCRIAAT GLLCRMVNHY
     PSHILPILRK EILHILYTLS SEDTGNKVLN GLLLLDAVAS NAPQFVVNLT DGIIKVLGRH
     LSALEVNSPI LQPLLRCCTS VARAVRFFGH NKPIFTLEVE RVCELLDLLP LDTEFAASRL
     WCLRFIGATL GPQIGGRSPY DVYPQLYRRL SGILKNSDDD LDLRLEALRC AGTIGVLDTR
     VFQSLGLGQN TQQTKLERNN SHTLSHAMCC RHVLRAIASL LDPDEKRVSV SKDSLLRVGI
     QTVLYIGECC PCSRAEMAVV IPAIVRAAGE LSPGRLLGIV LHELAQIVKC VGPTSLSNVA
     TLHTFCDVAW ERCPVYRFLI VRLASTIASL REKGDQKYLQ SDARVLPIKL DALNDADSSE
     YLRYAILEYV VKHTETLQFC AEIVVLDLLR ATQRNPIEFG VYAVTALRTV CTTLNVDELT
     GVIVRGLLAA LKMHSTILMQ NTEYTSFTNR IMSVFCVLIV QLQGEFIKYS SQVIRTLKTL
     RISNAEFTTL QGLLLKGFPC TLSASLLAEY HTQVVSLLKK CELMVTRGIS YLGEVWSARN
     NTEDAAVVFS DDERPLPLAE QRIINTLKTT PLTKEEWLRW IDQFSISVMQ ESPYRVFRCV
     SLPIGTNSTP LVERSPEFTQ DILRLAFRAL WNFGSASIRS SIVDFFRQTL QRPTWSSTVP
     DDFITAMLSL VEYMDVVGMT LPIAANDLSE CAWSRGMLAK ALYWREVAYR EDPASTIESL
     TILYSELHQP DSAVSLLGGA SESQKRYLLQ QSEILRLAGY TEALRLTQQE IDRDMMGSET
     SSESFVKPLQ YRSKNLRRFC GVTGRSYPDI SAFFRSEDTT SDLQMEQQVR QMMSLSEFGD
     YDKVLQQWGV IFNQYKGKKV DTEENILFYV SQYAADASIR LQSWGTLEDA LMWMPKDSVH
     YYISRAALSI HKGQYDEASL AVNEGRKLLL DELAGLLHES YIRAYESLVI AQELSELEEV
     VVAQRVKEAV STQHLCSISR LWSQRILMMS PTVPVWKQVL SVRGLLIPPS EDVTTQLRFV
     KLCRRANAKQ LERFTLLQLL GSRCPTYEQL MSHNANPRVV MQYIGFLSEN GELGPNGPYG
     LESDLLRKLI DTHSKVENAT LLSRAYVRLG TKAELREAIE CYKAATLYDP NWFHAWRMCA
     EANVELLNTN YSDAAYAAAI EGYIQSIKLG ISDSTMIQDV LKLLTLLSRP SDSEDGLRKL
     REQVLEVSSR AWYLVVPQLI ARLDSGSDGS CQLIADILTP VAFDYPISLL YPLNLSAMSD
     SERRKKLAHM ILEKLKAKFP VIVLQGRLVI HELLRISDLV YEKWYDQLDA AANAFFGRRH
     YHEMVENLLL LHEELHRAPE TIVEAEFTCK YSKSLQEAQE WLQSYKRTGS VADLHSAWHI
     YHCVYRQIDE HVRARNRLQL PFCSPKLFEA RNLSVGIPDA MPTDEGSVSC IASFNDTLVV
     IASKQRPKRL SVITTEGKKQ KYLLKGREDL RLDERVMQLF RLVNSLMMSD SRACKNSGFQ
     IKRYSVTPLK DTVGIIGWVS GCDTLHELVK KYRTYRGVPA ELELRMLNQI ITFDQPRAYD
     FLTVMSKVEV MEFLADHTTG HDIRKVMWIS AASCETWLEQ RQEFTTSLAT TSVVGYILGL
     GDRHPNNIMI QRTSGLMVHI DFGDCFEVAM TRDKFPEKVP FRLTRMLRNA LDVSGVDGAF
     RTRAEIAMCV LRDGSHSVLA ILEAFIQDPL ISWRLLNRPG EEPQSSAERH TFEQMRPRKL
     YSPAAFRGKP PRDSVSTEAV RTARHASVRE EVDMTHKGVT IFGRVRSKLK GEDFMQTALA
     SASMDPKAQV ARLIVEATDI TNVAQSWSGW YPFW
//
DBGET integrated database retrieval system