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Database: UniProt
Entry: A0A1J4KGP2_9EUKA
LinkDB: A0A1J4KGP2_9EUKA
Original site: A0A1J4KGP2_9EUKA 
ID   A0A1J4KGP2_9EUKA        Unreviewed;      2275 AA.
AC   A0A1J4KGP2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE            EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN   ORFNames=TRFO_20124 {ECO:0000313|EMBL:OHT10537.1};
OS   Tritrichomonas foetus.
OC   Eukaryota; Metamonada; Parabasalia; Tritrichomonadida; Tritrichomonadidae;
OC   Tritrichomonas.
OX   NCBI_TaxID=1144522 {ECO:0000313|EMBL:OHT10537.1, ECO:0000313|Proteomes:UP000179807};
RN   [1] {ECO:0000313|Proteomes:UP000179807}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K {ECO:0000313|Proteomes:UP000179807};
RA   Benchimol M., Almeida L.G., Vasconcelos A.T., Perreira-Neves A., Rosa I.A.,
RA   Tasca T., Bogo M.R., de Souza W.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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|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:OHT10537.1}.
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DR   EMBL; MLAK01000608; OHT10537.1; -; Genomic_DNA.
DR   VEuPathDB; TrichDB:TRFO_20124; -.
DR   OrthoDB; 8448at2759; -.
DR   Proteomes; UP000179807; 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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR   CDD; cd05169; PIKKc_TOR; 1.
DR   Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003152; FATC_dom.
DR   InterPro; IPR009076; FRB_dom.
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   PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR   PANTHER; PTHR11139:SF127; PHOSPHATIDYLINOSITOL 3-AND 4-KINASE FAMILY PROTEIN; 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; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-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:UP000179807};
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          1189..1733
FT                   /note="FAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51189"
FT   DOMAIN          1904..2232
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          2243..2275
FT                   /note="FATC"
FT                   /evidence="ECO:0000259|PROSITE:PS51190"
SQ   SEQUENCE   2275 AA;  259318 MW;  E31FD99589A17EAA CRC64;
     MNLKELPIPR TYPNLLKTYE AYYHGFYLDM VRMSNSNFLD YVDKYFDLLY FLAKFPGTEN
     SIRAAIGVVC LHQFGYHDFK KLTAVFDRLI PQVDLEYIKF TSWCVGKLVH HPDNYEMHYA
     SQLFSRVLDW TRMKGRRARP LAAAYMLESL SFNAGSIAVS FFPNFQIGIW SLVSFPSVLV
     IKGVAKAIAS YTRAIIRYGR NELTEYMTFL SKVCMKLLFF DDPVRVYAAL MLFEVLVNGF
     PNFFIPHLFE LLTDISDAAE GKALLVQGGA YVVISCLSQV GPSTFIDTMA DEHFAKTDEL
     LLEFPFEVTR SLTMMCQFIP EFIGTKLDKM KEFAIILIDE EPDCAFKLLA AIIEYFGSKV
     LPIPNEIMLK LIQLPISEDF KDFFVALMKC DTNLSNEVQQ ALNNKIIKEL KDGQKVIALN
     LVSKMPKELL FEHEKLLNAI WPLTVDKDIK TRSAVPTAIF NIGRCTELVT IQSISKRFCQ
     LAIYDQSVRA RCAILQALID NADESLASPD FRTFYEIFIN DDSSTVRELF YNLLVKLSRF
     NPMTIMALTR CAMLDTFFII RNIPSIRKRA KTIRGLPILI KAAGRSIKAY SGGLMDIILN
     ILGDYNSKAK FDNFLEEDAQ TCILIGVVDS LTLLAPMDPE IVSKHASIIV PILCDIVLTT
     DHRKLRLFIF ELFYVLLTAP ASTLDYRIQI PQILTTCSQF LMTTHSRKTK MEILKVLGAI
     GIVELHQRPP PKGTQTPPNM DNDLARQFFN PSRDADCSLD DSLLLSPSTS EQYFACYTAN
     ALIDILKDDQ LKEFYVETIR AVVEVLKHPK MFILTYFDMF VSRLLEILEC SSDKEINLYL
     PLFSNLILNS THNISPFLKR SLKLIHERFN DELSCVFIDL IIAFLTAVRD GFSPYASETI
     CLLVVILDDK KTVDGLLCKK VLKAFAILGV YSADLLYLVI PQISDAIICE QTLPTVRIAA
     LVTLTELAAQ VDLLPFLGPI ARSMEYCYIS FQTPKTIKAA FQLLYTILKS LGVAFLVNAQ
     PLLDFLKATN NETPELKELV YQVSQGKFGD GFHPLNVNKK PDPLPKIVEK PLSADSIISK
     AEDFERVGRN NERWLQSFIL CVISNSPSPS IKTCTTIATS YYPLAKKLFN CAFLSCWQKM
     NLESRSSLTH VFEQLLKVSD EEDSINRSLL NVIVFMDKIE QPIGIPVFDL VSASVRSGSV
     SYAIRLMMNL LDAQPDDVQV INKLIDVLVQ IGQWQNAIGV WRQSQMVSAT LSRTEVLSKL
     GMWDQVEPVY REQYNNNHSF KAFSGLIESL ASLARWKQLM DFHDDFEKLK VQQKQQLAPF
     FADAALHLSE WDKLHSALKY ASDDSWRCCV LSALSALHYK DFESVKRITN QTFSLLASRP
     MTFWADNHQI HRETMLECQE LIEVIEMNEW LTNPRKRDDI AEVWNQRLKT ATRDFDLWFA
     VLANRVRVAS VRDDALVQFF QMRSATLGKQ IHLDAFNILY PDFNLETASD AQKLCHAIAE
     WNVGHNQIAL SEVKKLTTQL QGNLLMRANV FYAQWLLETE GETFTNLKDA YTYLEATVKQ
     IDDSTILRYG QKTEVSKILS NTHQRNDKTN NLILPTQISE ELVMHVNQID MIRKWSDVNA
     ALINFDPENK VKYVVNAITA LSRCAKLTPA FPDGVQMLNL FFENADNEII FNETNDIIKN
     LPVKLLLQAS PQIEIQMSHG NMKVREFVNE LVFSLLEIHF HSLIYSLLVL KTSKNAARAK
     AATSILNKWN VKYPQICSEV NLIRSALLRA AVTWNEKIAN KVSDTYDHFQ RNNMSKVIST
     LKSILAMVSK PVCEMHDQFI KQHSRNLSML DQILKAYSPD NQSSVTQLTK WCKTMQDNLG
     EEIKRTRIIQ LSAISRELTE KDDFILAVPG TYKPNEPINH IKYFVGQFSV YMSKQQPKDV
     VIKGEDGIFY QYLLKGHEDL RLDERIMQFF RMVNSLLLKD SSLNSHPIQT VYVVPLSISH
     GLVQWATGTD TLRAIIEQYR RLHSRDPLEE YMLSDDFGNG AYDFLLPIQK VQILERIFHE
     IPDTDLANFF WLKAPSADVW MKQVQTYSIS IAITSIVGYI IGLGDRHPSN LLFDRNTGKV
     VHIDFGDCFE RASHRKYLPE VVPFRLTRMM VKALGAGGVE GEFKTSFVNM ANLLRANKQV
     LEMVLAIFVH EPLIDPDYAD DGASDNEKNY PMSPFTLKMS ALSEDTSPVN NSDDYHDTFT
     SSEEMRIRIR QKITGSCCIE GTTPLSAEEQ ATKLISEATD LYTLGKMYSG WCPFW
//
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