ID A0A0V1CUB5_TRIBR Unreviewed; 2478 AA.
AC A0A0V1CUB5;
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:KRY52738.1};
GN ORFNames=T03_11326 {ECO:0000313|EMBL:KRY52738.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY52738.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY52738.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY52738.1};
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:KRY52738.1}.
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DR EMBL; JYDI01000099; KRY52738.1; -; 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..1949
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2100..2417
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2446..2478
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2478 AA; 284068 MW; 386A5FFA535A5894 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 TILLTLWFDY GHIPEVYDTL ISRIKTVRVE TWLQVIPQLI ARIDTPRHFV
SHLIIEILMD IGKNHPQALI YPLTVASKSS SSARRQAADR VLKHMSDHSP NLVQQASMVS
DELVRVAILW HELWHEALEE ASRLFFSDRN VKGMLDLLNP LHALIERGAT TMKEQSFNQA
YYRDLKEAQE LCIKFRQRGN LRDVTQAWDL YYNVFRRITK QLPLLSALDL QYVSPKLLKC
KNLELAVPGT YDPSRPLVCI QSVQRRSDGQ EYWFLLKGHE DTRQDERVMQ LFGLVNTILL
QNPTTCRLNL TIQRYSVIPL SPNSGLIGWV PNCDTLHALL RDYREKKKIL LNLEHRIMQR
VAPDYDHLPL MQKVEVFEFA LEHTPGDDLQ KILWLKSPNS EVWFDRRTNY TRSLATMSMV
GYILGLGDRH PSNLMLERMS GKIVHIDFGD CFEVAINREK FPEKIPFRLT RMLINAMEVT
GVEGNFRLTC EKVMSTLRAN RESIMAVLEA FVYDPLFSWK LIEREQFERK TKNVSLSDDD
AISLLSGGPG FQPSEFVSRK ALDIIQRIRD KLTGRDFSSA CPTTSKSLTV QAQVDLLIQQ
ALSHENLCQC YIGWCPFW
//
