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Database: UniProt
Entry: A0A0V1CTW6_TRIBR
LinkDB: A0A0V1CTW6_TRIBR
Original site: A0A0V1CTW6_TRIBR 
ID   A0A0V1CTW6_TRIBR        Unreviewed;      2509 AA.
AC   A0A0V1CTW6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE            EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN   Name=Mtor {ECO:0000313|EMBL:KRY52731.1};
GN   ORFNames=T03_11326 {ECO:0000313|EMBL:KRY52731.1};
OS   Trichinella britovi (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY52731.1, ECO:0000313|Proteomes:UP000054653};
RN   [1] {ECO:0000313|EMBL:KRY52731.1, ECO:0000313|Proteomes:UP000054653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS120 {ECO:0000313|EMBL:KRY52731.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) 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:KRY52731.1}.
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DR   EMBL; JYDI01000099; KRY52731.1; -; Genomic_DNA.
DR   Proteomes; UP000054653; Unassembled WGS sequence.
DR   GO; GO:0031931; C:TORC1 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:0051247; P:positive regulation of protein metabolic process; IEA:UniProt.
DR   GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR   GO; GO:0042221; P:response to chemical; 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; 3.
DR   Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat 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:SF9; SERINE_THREONINE-PROTEIN KINASE MTOR; 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   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:UP000054653};
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          1417..1980
FT                   /note="FAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51189"
FT   DOMAIN          2131..2448
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          2477..2509
FT                   /note="FATC"
FT                   /evidence="ECO:0000259|PROSITE:PS51190"
SQ   SEQUENCE   2509 AA;  287583 MW;  846FB56F99353AE2 CRC64;
     MLLTTSTKKS KTRPIAHQIR PPPISAICFR TSVLCHRSSG SNVAATVAQI TENDAEYINS
     FFCIKMTAPA EYFLQRLCTK DEFARIQAAY DLYWYVKCEL TEVPQEVANA FREKFDFIIP
     ELLTSNISGE RSAAIYAIAC LAQGDASFSN VAPTNLRQTN PAGVASIRFH RYTHYLRNIL
     PSSDANLVQL AVRAGAHLAL RLSNLYTTEY VYFELKRATE WLQSASTDRT DNRLSAVIVM
     KELAYIAPTF FYQHTPHFFD CIFEALMDGK VQIRERAAEA IRAALVVTTQ RETKLEQKIH
     WHKQCYNEAN RFFEEARSSH ANVREDRVHG GLLVLNELLR NANSRWERII QELAESNISR
     SAILAHSQEL PKDFDFKERF TDLQEDVIAP LVSPSYFMNY ESRNCRLKIA EEFNEICSNV
     TWCCSSTKAS YNVQLQLALL CRLAAFDPQK FLAINFDDAV NYLWSCMTRE KLRPDCLVAI
     GLFFMALKEE MVPYLPKVFD FLNSCLPTKE SLNLKKRPVV VDTELFTCVT LIVRAVGSPL
     ESFLKPMIEP MVLTGLSPNL KLACYEITTK IPSLKKIIEQ GLLEQIYSVL LQQKMPNLLT
     LLQPIEPPTK PVVVTDPHIT SLALTILGTF PFQRFSLESF LRFIPEGYFA NECYEIRLEA
     VRCCCQILLP FVSTLTPEQS AAHNVSLLQM VNEVIKKFLD RRIRLMAFQC LTDSNAFCLH
     LAQDEVLKLI MMGLQDEDCS VREKIIHLLG KLTNVNPAYC VPALRRILMQ IIEEMSLSGL
     SRNEEQSARL FSCLVRCAPN FVKPYAKTAF EVLLPKLKDS DTNGDVVVSF LRALGDLVEL
     MPDKIEGYLD ALLPVLIQLA QDTVSAGKRK AILIEYFTNA SMWALSKVIE CTGFAVEPHK
     RYQDLLDLLL RTLKSEQSPD IRRETIRLIG FIGALDPYKQ KALHTAVDLA SNCTGLALSL
     PHIKDITDRR LEILQWFHWE RCSLEQFYPT FAIINLMSIL SDSTYNQQLL TAAVHSLVFI
     YYSLNDKGLT ALDQVFPTLV NIIRNSDPSM REFLFQQLGY LVSVVKHHVR PFLDDIFSLI
     RDFWTTKTQM RLTIILLVEQ LAAALGSQFK PYAASIIPSM LRIFLHDTSV GRSVTSKLLD
     AFKKTSFILE DHFHLLLPPI LSLAENVEVP IDVRRSAIET IDVFGETTSL SNFACRTVQT
     MVRVIDSEPE LRFAAMDLFC TLILHLGEDF LPFCRVIDPC LERNDVVHER YISLILKTME
     IGKINPTEEK FYKAMVRGRR CLLAKQQQVM QIEVRKVVCN VEQLRKIWLT NRCVSKEDWI
     AWLKRFSIQL LKESPVPALR SCYSVAVNHY QLASDLFNSA FASCWPELNE TYQDELIETL
     QLALSASECP EIIQAILNLA EFIDHTEKGP LPIDPKLLGE KALETRAFAK ALRCKEAEFY
     NEVTPEVLES LISINNMLQL RESSIGIVEI VRKRGIKVKD TERWYEKLND WDKALEAYEA
     KQNQFPDDME LTLGRMRCLE ALGNWSKVNE IVEKKWQSST VEYKEKMAHI ATCSAWGLGK
     WEAMQDYIAE ISQSTVEGCF YRAVLAVHHQ NFCEAQFRID QARDLLDNEL TAMLSESYSR
     AYDSIVMVQM LSELEETIDA KRNPEKRRIV PSVWWNRLQG CQRSVEDWQR ILQVRSLVLT
     PDEMRQMLLK FASLCRKSGK LAVSRRTILT LMDCDPDSCA PIKLPFERPE VCYAYCKQLN
     CEGRRDLALS QLQLLLEYGF KKPATLPAEL LSLKARCFLK LGQWSEQNLI NEDSPNVEVM
     QHYMYATELD SKAYKPWNAL ACANFNALLY YRQRAPIPLI QCQNDSGDSP LKPLNPNLLV
     PGTVPDDSVI TMYAVQAVKC FCRAVMLCHG NSLQDTLRQA FIQLLTLWFD YGHIPEVYDT
     LISRIKTVRV ETWLQVIPQL IARIDTPRHF VSHLIIEILM DIGKNHPQAL IYPLTVASKS
     SSSARRQAAD RVLKHMSDHS PNLVQQASMV SDELVRVAIL WHELWHEALE EASRLFFSDR
     NVKGMLDLLN PLHALIERGA TTMKEQSFNQ AYYRDLKEAQ ELCIKFRQRG NLRDVTQAWD
     LYYNVFRRIT KQLPLLSALD LQYVSPKLLK CKNLELAVPG TYDPSRPLVC IQSVQRRSDG
     QEYWFLLKGH EDTRQDERVM QLFGLVNTIL LQNPTTCRLN LTIQRYSVIP LSPNSGLIGW
     VPNCDTLHAL LRDYREKKKI LLNLEHRIMQ RVAPDYDHLP LMQKVEVFEF ALEHTPGDDL
     QKILWLKSPN SEVWFDRRTN YTRSLATMSM VGYILGLGDR HPSNLMLERM SGKIVHIDFG
     DCFEVAINRE KFPEKIPFRL TRMLINAMEV TGVEGNFRLT CEKVMSTLRA NRESIMAVLE
     AFVYDPLFSW KLIEREQFER KTKNVSLSDD DAISLLSGGP GFQPSEFVSR KALDIIQRIR
     DKLTGRDFSS ACPTTSKSLT VQAQVDLLIQ QALSHENLCQ CYIGWCPFW
//
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