ID W6UWH5_ECHGR Unreviewed; 3072 AA.
AC W6UWH5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Target of rapamycin {ECO:0000313|EMBL:EUB64971.1};
GN ORFNames=EGR_00240 {ECO:0000313|EMBL:EUB64971.1};
OS Echinococcus granulosus (Hydatid tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC Echinococcus granulosus group.
OX NCBI_TaxID=6210 {ECO:0000313|EMBL:EUB64971.1, ECO:0000313|Proteomes:UP000019149};
RN [1] {ECO:0000313|EMBL:EUB64971.1, ECO:0000313|Proteomes:UP000019149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24013640; DOI=10.1038/ng.2757;
RA Zheng H., Zhang W., Zhang L., Zhang Z., Li J., Lu G., Zhu Y., Wang Y.,
RA Huang Y., Liu J., Kang H., Chen J., Wang L., Chen A., Yu S., Gao Z.,
RA Jin L., Gu W., Wang Z., Zhao L., Shi B., Wen H., Lin R., Jones M.K.,
RA Brejova B., Vinar T., Zhao G., McManus D.P., Chen Z., Zhou Y., Wang S.;
RT "The genome of the hydatid tapeworm Echinococcus granulosus.";
RL Nat. Genet. 45:1168-1175(2013).
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 -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC {ECO:0000256|ARBA:ARBA00011031}.
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:EUB64971.1}.
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DR EMBL; APAU02000001; EUB64971.1; -; Genomic_DNA.
DR STRING; 6210.W6UWH5; -.
DR EnsemblMetazoa; XM_024489489.1; XP_024356167.1; GeneID_36335955.
DR OMA; MRQHSAK; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000019149; Unassembled WGS sequence.
DR GO; GO:0031931; C:TORC1 complex; IEA:UniProt.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
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: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; 2.
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; 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 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; PF08771; FRB_dom; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01346; DUF3385; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM01345; Rapamycin_bind; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
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; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000019149};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1739..2378
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2554..2867
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 2849..2893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2863..2888
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3072 AA; 339171 MW; EDF8891AC9F709AA CRC64;
MDGVLSRFLD GLKSSSDEIR LSTVAEIRRF VALELKEAAA SNYAEFIGDL CVEFEGMLSG
SDPNEKKGAI LAIGCLAEID FSAIAPYYSQ FINLLNLLST SSDLPLLVLA ARLLGEFGLL
LPNDFAEGQI KRACEYLKRG SLSTSQKQFY IVLRDLAAMA LRNTLAIAAE NEIGRRGQQM
SLDADANVDG FGDSAAHTSA NRAIPSSSSR QFLRGIGNTP IRKFSSSQQP AVPQANSYYC
PVNEPPMIWY HQCVGQPIFH VLVVNQTEGE LAVRSVNQTP WPVVISPSQQ MELSLVPGTH
LSALSSSVQV YGDEGVASEL LRQQQFRQQR AVPLVSEACQ RMLGANLDKI WELVLGCLNL
KHTGVLHLVL KVIPRLVAFE RSTFLNRDIL REVINFLFDC VNRDREKGYA LVTLGLMTHS
VGDEFEKHGY LSQLISVLLN QLNSTKDVPA SKKRLGGLST AVLLTIGLIA KSLGSRACSS
LKPLLDPMIS RGLSQPMTVT CTLVAEYIPE LKRDVQDSLL KRINVILANS IGIGAASSIT
LGNGTVPCAL GSVPPGANTT GAHLAVAVPR ISSTRGRNSL AHTSSVRVRT SSIPLPGFPW
GEAFSKNSSS AEFDPSGDAL SESQLVASAE LVPSPMQKTL DAISDILGKL LIVGICDPDA
EVRKCVFSSL DSQFDNYLAQ SRHLNSLFVA LNDEVFAIRG LVMQCLGRLS DVNPACVQPT
LRSVLLKIIT DLADSGTTKN KEESAALVAI LAATAPHFIL PYGASLLHVI IPQIRNALPI
NLRMKLLIMR NERLQKAGNY HGDVPTDTNE ISLSTALLAS QSAAHSAAQA VQAVATATAR
GVGQQLARSV ASARPTLPTS SQTTAVCTRA VVAANQAAHS AAIAARVIST AIGRQGKCGS
AVYDEFPTSH GLGYPEYPRS GGCELDLLIG EPHETLPGTS QEFLAAAASL GGSEGPETSR
GFLVGTLDAI RPGEIGGFMS PNQLSIPGTL RAGRRILENT NAIWREPKGL VVALFSALAH
LSSVCPQAVV TLMDDLIPVL VYMLQDPTCH AKRSVAAWAF GVLVSNTGYV VRPYMKHPDL
MELLFALLRS VESKSIQIEI LRLLGLIGAV DPFKLKVSMG QYDYIQETDT AVSQYDVAES
RDVDITQSEL LVNLCWDNRE EFFAGYSLSA LINILREPGM RSNWDHVVRV IASVLESFNQ
RAIPCLHQVM MELFKCLQGL HETKLQEAIT HHMCSIVQII GPFAKEFASE IVDIITTYWN
FSASHIVQRN CIRLAGVIAK AIKTDFRPSM PRLVPCILRC LKQEMVDENV IALCDLISDL
GTLLDGHLHI LLPALTSLVA NLEDTPYEHL LRTSLEAKHA QSAQSITTVT TIAANAGSVP
VSQSAAVHAF SSSCSPESVE VMSATSPSYL DDSFVMGTPV DSLLVDSTGG VGSVGGGVAI
PSRSALRAAQ RAANSPSVPG SLQTRLAALR CITRVTEVLC VESLAANIVQ PLCRLLNALY
ERSLAVVEVK NKPSAPRLAL KALYPPCMDV IANLALQMGS AFKFIMPVVQ VTLNLINIPH
KRFDMAIEKV NSDGYRRPNL STDGQSISQD THANFTRKTD PDKLVKNYTL NSLNLQRAWQ
SSRLSSPEDW NLWLKTLSVS LLRESPSPAI RACARLTTIA PHVSRRLFNA AFMSCWKELR
DAEQDDLINT LENVLRLPSS ASQSREISQV ILNLEEFMAH ADKFSGKAPR VHLPLSLNLL
ADRAMKNRAF AKALRYKELE FLDEVEKRSS PNPSTLASLL AIYDKLQLTE ASNGVLLYAT
KNPRNKLTDE ELWYEKLHNW DRAIALCDRK LEDERIRDKT KPILCRLRCL HSLGQWSQLE
SMAWERWGHL SEGAREQVAP LATSAAITIG AWGRAAHYTQ AFAPADHEGG FYRALLALHE
GNYAAALDEV AKSRSILAAN LIPLTTEGYQ RTYPDLVDAQ LLSEVEEVIQ YKLVPERRAV
LHEAWHHRLL GCQSVVEDWG RIIQLRRLVL DPRENIKSCL RYAGLCRRSG RLSLSLQVLL
RMLPKDPSEV AWNEVVAAPD PAIVFSYTKL LWASGSREEA VTRLQVLRDS VIEPSLRAQA
TKLEEIGQEV AQQPFISSTS ITDIATRIDD LRCLMAKYLY IRSSPDVGGS RLPNSGLFSY
SPGVSQFKQL SISNEVQQNG TSDTAAQYGV VGLGGNAHFM DDKSVMMHKF VIKCYRTATE
HSPGNRSAWQ AWAMANYDLS TRLGIEQAQL DQKEIQIKQI ISSESSLDHT TLKQSLAGLG
QRRSILQRSI EQLAAPSDIL RLINLLFQFG HLPEIREIAR EGLGKIRLQN WLPVLQQLLA
RIDTPHEHVA NIIVDLLIAV GRQFPQALIY SLVLSFKSGG SDRRRYYATK ILYFMEEHSP
RLVYEAFLLN EELIRLSVSW MEMWFECLED ASRVYFGEKD TGKMFRLLYP LHQVMERGHE
TANEAAFLQE FGKELNNSRI YCERFENQGM RADLQQAWEG YYTLYRTLSK RVSNLSSLDL
TCAAPRLHAY GKDWMLAVPG TYKPHLPLVR LAGVKNCLMV MTSKQHPRKC TMLGSNGKTY
VFLLKGHEDT RQDERVMQFF GLINTLLMIN PETLRRNLTI QRFSIIPLST NTGLIGWVPN
SDTLHSLIRE YRDKTDITLN QEHREMLHLA PDFDRLNLSQ KTEVFEAGLR VSSGRDLANI
LWLKSHNSEV WFERRTTFIR SIAVMSMVGY ILGLGDRHPS NLMLCRETGK IVHIDFGDCF
EVAMMREKYP EKVPFRLTRM LITAMEVTGI DGVYRHTCET MMQLMRSNRD SLLAVLEAFI
HDPLLQWVLL ENKRPVLGPA AGGGVGVNNQ GVPPPPAPPL SANSTAPAQQ ALRGLPTQQQ
QQQTMDGEGE PHTKVPLGAG VGGGARYPQT RVSQQSQNIS AHSRNIPYVF TDPNYPSSLS
LRDCRHINPW RHHLCNGPWL GCYETAKAMR RQTESGAIVC ERVGMQNFIF SAKPPSESEY
HDEMQTGGMG NTRARDVLSR IRRKLDGNEN GAQTSVPLQV DDLIREATSV RLLVIYISVA
VLTRSEPRVE SV
//
