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Database: UniProt
Entry: A0A1J4K4V2_9EUKA
LinkDB: A0A1J4K4V2_9EUKA
Original site: A0A1J4K4V2_9EUKA 
ID   A0A1J4K4V2_9EUKA        Unreviewed;      2247 AA.
AC   A0A1J4K4V2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
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_06182 {ECO:0000313|EMBL:OHT04748.1};
OS   Tritrichomonas foetus.
OC   Eukaryota; Metamonada; Parabasalia; Tritrichomonadida; Tritrichomonadidae;
OC   Tritrichomonas.
OX   NCBI_TaxID=1144522 {ECO:0000313|EMBL:OHT04748.1, 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|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:OHT04748.1}.
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DR   EMBL; MLAK01000782; OHT04748.1; -; Genomic_DNA.
DR   VEuPathDB; TrichDB:TRFO_06182; -.
DR   OrthoDB; 8448at2759; -.
DR   Proteomes; UP000179807; Unassembled WGS sequence.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05169; PIKKc_TOR; 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; 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; PF00454; PI3_PI4_kinase; 1.
DR   SMART; SM01346; DUF3385; 1.
DR   SMART; SM01343; FATC; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
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   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU364109};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364109}.
FT   DOMAIN          1152..1648
FT                   /note="FAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51189"
FT   DOMAIN          1856..2179
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          2215..2247
FT                   /note="FATC"
FT                   /evidence="ECO:0000259|PROSITE:PS51190"
FT   REGION          2126..2170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2126..2144
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2247 AA;  258419 MW;  0B497397CBB2B4E9 CRC64;
     MKTRNVPITH LTYKELIENA RKTREIEYSR LSTLSYEKLS NVTSQSINSI SLPRPTSDPS
     QIFKISSLIY TLLKLRQDHY PKLISILNNL NTDRNEQVGI FVSYVYSKVL KHAQRGFLQQ
     KLDVCLLKLQ STSNVLQTAY FLFFLAQHSP NSILLCITQF INATTKVIMH KREDVRLVGY
     ETLKLYLQIL ERTGNSQYPT FPLYFFALKN LHNRQGAFLI FSSLLEYSPE SINDQAVLMD
     FFIKLLPECS EDLRSLVLRN LVLLAPLQLD DFKRKYFKFV VDSLWRENNL ENADSIVSSS
     LCDLIHLVPE LFESTKMNFI IIIRNLLNLA FKAPLDGGFL ILSAVVTYFP EVIQEHPIEI
     ANILIQTTIC KMFIEVVPKI FYDFNCVWDK FKFYLSNKII NDPHYIENED ILNFLATCPP
     LESQEVMKFL ITTLSHKNPN IRCIAPRALL AHIPYDNKKF IQEIVFRLIT ISLSDPEPKV
     REMILRSFSS KCYPFLTTDP ILTCMTSLVK DEKINVSNAA IEILGNLSKL NPFDSLPTLR
     SLILDALLML DSPRPLRIKE EMTRTFMTII EAAHEILPVY CPTLCLIALR QLSFTPLCEL
     TYFDQSYLHK INLNITKAIG SIADRDVSLI QPHIPQFTNF FIWLLQQHGP KQLKIAVVTT
     LYKIMSGTNA INEIDVAPMF SALTMIASKW NSRKLNVAVL KLIGLIGAVD QSIFSSDSTT
     KKDNTIKSTN PAYPMACACR TLISVLSDDF LVIYHSEAIR SLVNIFCFDE TATVSFFNEF
     MLLFLDQIRK QMTSEYIMLL TKLCSEAPRD WIMHYTNEIL ELIRELWKSP NSALTLDLIP
     TIAAVFADRF SSFLPECMTF VLDTLYANRT SQYEICHKVF ATIVTIKNIS KDYHFLLFPE
     IIEVATLPST LFEVRIDALI SLKVLVQQTY CIPFSAAILR CIISCIQIHD PKIQGPALMV
     LYSLMIKLGD LFSFYAEQIV LTLQEHNLLT AHFLELLQSK THTYEESPFI DTEDPFTVVP
     GQDSMKSKTE HVIVNEDDIK SALLFQDEET PWNWKEWYRS IIKTLLENCP SRALNSCAFL
     SDVLFTTAEN LFNTSFMSIW VNLSTDTQLY ITGPLTRALL SEALPGAIRT SLVNLFDFME
     RNEHPIQISR QVLCQASEKC SQFAKAFYFV LRWYEEDPHN IEAIETLIRL STSLGLKKTI
     IGISKQLSSS MDFVSNPQWS EQLGQWSNAL EVYEKMPPTA ASLEGILRCL KNLQRWDEII
     SKMDEFENLP TAAKHNMAAI VATALFHRQQ WSKLPPVLEY CTHESVRVLI ITALYQISQN
     KRDEALQTVA QGFQLLAQNA RGVFKHDKAA LYPLLVKAQQ LQEITEIAYH KQNLEVWEKR
     LSLCRQSYDV YHQIMSVHLT VFPVQETMKD SLKMIKLAMR TKDFQLFDAS LHFLFPDQQN
     WPIEVSFLYA KGTWERGLQR EALTEAKEIL RKYRTDDKNL KAKIFFCCGQ WIISMTPPNK
     VSNVIQNAIK FLEQSIMQGT HYYHAWHRWA WASSVIYNVD KSNLKSAFNA INGFLECVRL
     KNENLLSELL QMISLFFSAN LSDDMFNATA EHIAELSDPV LLKIIPQLFI QLSHDGTRSS
     AFASQITEKL LPDHFHVLLY PLILLSRNNN RAAISILETF QEENPSAVYQ SKIVSDGLLL
     CSSSTFEIYN DAIVKAVRYL QKQKIDKAQK KLFDCLQNQL RPGDAQQANE LKNELESIYN
     TMIYKLPQQN AFKFNYGIQP GIQNQTNYIN QMNKLNMTHQ HGKQNIRNNE KMVEMLVRQF
     IKALQSIYSK IHSHIVSNRT VSMHISAPSL AQLKNSILAV PGTYSIDEQV INIFQFDPTL
     DIFNSKMRPR LVAVYGSDGI AHRSLLKGRE DLRMDQRVMQ FFELINQHIF NDFTNEARSM
     KITTYSITPL STNAGLIQFV DGTDTLYSLI SEYRSSHSVP VFAEQDSMET FSIKNVDLLT
     PVQRLEALRF AANENKDTDL RELMWLNSPS SREWVTRSLQ FTQSCALMSI IGYVIGLGDR
     HPSNLMIHRT SGNIVHIDFG DCFEVGKKRI KFPENVPFRL TRLMKRSFGP TGIDGEFRLT
     CEETCKLVRS HKESIMAVLD IFLQEPLDNE DSDDDEDEAE ETETANENEN HNQTQNNSEN
     EENRENRESD IETQSIEMLE MEQFEEEEVH KKGSIEESLS RILQKIIGND FDPKNELTIQ
     EQVDSLIADA TNMYNLAYLY HGWTPLW
//
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