ID X6NQP0_RETFI Unreviewed; 2382 AA.
AC X6NQP0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN ORFNames=RFI_08520 {ECO:0000313|EMBL:ETO28610.1};
OS Reticulomyxa filosa.
OC Eukaryota; Sar; Rhizaria; Retaria; Foraminifera; Monothalamids;
OC Reticulomyxidae; Reticulomyxa.
OX NCBI_TaxID=46433 {ECO:0000313|EMBL:ETO28610.1, ECO:0000313|Proteomes:UP000023152};
RN [1] {ECO:0000313|EMBL:ETO28610.1, ECO:0000313|Proteomes:UP000023152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24332546;
RA Glockner G., Hulsmann N., Schleicher M., Noegel A.A., Eichinger L.,
RA Gallinger C., Pawlowski J., Sierra R., Euteneuer U., Pillet L.,
RA Moustafa A., Platzer M., Groth M., Szafranski K., Schliwa M.;
RT "The Genome of the Foraminiferan Reticulomyxa filosa.";
RL Curr. Biol. 0:0-0(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 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:ETO28610.1}.
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DR EMBL; ASPP01006570; ETO28610.1; -; Genomic_DNA.
DR EnsemblProtists; ETO28610; ETO28610; RFI_08520.
DR OMA; MRQHSAK; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000023152; 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: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:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR GO; GO:0050896; P:response to stimulus; 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:UP000023152};
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 1229..1817
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2002..2317
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2350..2382
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 160..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1018..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1357..1389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2382 AA; 267221 MW; D9AF9957EA339FF4 CRC64;
MSSFTSRLSI SGPKRSFSSS IETIQKASAE TIHGSLLTFG ELLRANKYMA DNFDTICEIV
IQFRQHKSKY IKAAVIELLP ELAKFNPERF TNRYLKQSVE HIVDVLNRSK DHRDNCYHAL
GAIALAVGAN ISKMLSLVLE LVKVGLNKYS KKAAQSSQFL TEEPEDGIGG SGGSGLGSSS
SSSSSSSGLG SSDEAVPNAT TTFHAALKCL SKLVCAVGVE LQEPIRPLID PMFSAGLSTT
LVETLRNICT QIPSLKREIH ALLALELWSI LCMSNKSLEE VIQYYSYMLD FERDRDRDPL
NLSNGNGNGN SNGNSNSNSH GHGHVGGYSG SSSSPRYAEQ KEHDNVSRFD RARTLTVALL
TGGSGGNNSS NSGGSGGGGG SKDSFVKKHS STSIGNDKRT NMNRETMNGL VLLALRALAD
FELSLHFVLP FLHEIVLCYL EYENVTVRKQ AAVTVGTMVL RIVSNINKIS TDVFSTQAAR
HLNNAISDVM DKLLSVGMTD QSWTIRSAIF GSLHTPLDHH LGQSSALRAL QLALNDEVFE
VRKQVLKVLG RLAQRNPAQV IPYLRKTLTQ LLTELQYSRD ITIQQESAEL LGILIDSCQF
LLKPFAPAIA RVMVAPLHQT MGDDILVETE ILRCIGKLSE IAHEDMVSYV DILLPRMEKF
LNDNWDIRRE AMRALGILGA VDPFTYKIKM NKKGSNYNTS AVAAIDNNSS GNLKSQSDIS
LLDSRSEDYY PTVVVHSLCK MLADNGLRVY HYDVLRAIVD VLKHVGKSRC GAFLAQVMPI
LLDIMKQSVA DVSHRQTLLE TLITIISVCE SHIRDYLDQV FEIVQAYWNV SNSTDVQLQS
LLLQLLTQIN FALGDELKVY LTDLIPLLLH VLHSDKSAER TSSLHVLQAL ETFGSSLEDL
LYLVIPPLMK IIEHTELNVS IRIRTIECIS KLCRCVNFSS FFSRAIHPLI RIIDDDNDQL
RGPAAQALCS LLVQMGPDYA IFIPNIDKIL KKHKAVSGEF TKLADRLIRN GNDPMLDSDV
YTDGIDDNGS GGGSNGGISN GGGGGGGGKG EEAMDTNDSL STGKDRNAGN LAADNGRNGD
GAEPSETGHN GNLGDDSNVK LSIQSEALHK VVKRWNADHT FSKEDWIEWL KSLQIELLKQ
SPALLLRLCV ALAQRHDPLA SELFNAAYLS CWTELEDWIQ DKLIQVQCRA FTEAQSKPGS
VPNEVLLTLL NLTEFMDRQG HGLPVGETNL GKVAEICHSY AKALYYKEKE FRFHFSNSVA
PLIEINNRLQ QTEAAEGLVE FAQHRQQMEV FARWFENLHR WEDALDAYEK KQMEKPMDVE
STVGRMRCHA ALGHWNQLHA LAIRNVSWDG AHKSDANEMK GLKHSSPRDG AAGGGGGGRT
GGDSSGYHNL TQTRQSEMAA LGAMSAWSLQ KWEDMTSFTQ QMSEDEMVAD TWFYRAILAV
HNKEYKSALE YIDRTREALD GEMTALVGES YNRAYDLCVR LQQLAEMEEI VYMQTHVEPQ
WKQRLKHVWA KRLNGCQKTV AVWQKVLSVR QMAISPREDV DTWLKFSSLC RKNGHLVLDM
QTLSAMLNET PEYCLRALST KQFPELYAKA QSTNSDIDSA KITFSLAKHC WSAGMHDQAK
DFLHYLITEL TKTSEPRELN IESAYSEMVA KCYVKLGVWA QESTHDLNDN VISQATQYFN
AATQHNTSSY WGWHDLAVMH YEAINRNNTT HVVAAVTSLF QSIALDHNTH YGTRLQDILR
LLQVWFNHGN DDRVSNVLRN GFNTVPVETW LAVIPQIIAR LPTASKEIAT LIEELLSKVG
KQHPQSLVYP LAVASKSAQQ KKGANSNEKA NENELLMTKI LNRMRGYSPF LVAEAFMVSD
ELIRAAILWD ERWYEALETA SRLYFGEKDP KAMLAQVDEM HEVMKQGATT LNEIAFEDTY
GRDLAEAREW CQRYRVTGNE SDLNQAWEYY AFVFRQISQH LPNLKHLELQ YVSPKLQKAQ
DLQLAVPGTY NAHKDTVSIS AFQQSLRVID SKQRPRRIVI LGSDGKEYAF LLKGHEDLRL
DERVMQLFGL VNTLLRNENE TRKRGLAIRA YSVIPLSPTS GVLEWMPNTD TLHSLIKEYR
ESHKMLNNIE NILMHQMAPD FAKLCLMPKV EVFEYVLRHT SGKDLQEMLW LKSASAEVWL
ERRTEYVRSL AVMSMVGYIL GLGDRHPSNL MMDKYSGKLI HIDFGDCFEV TMQRDKFPEK
FPFRLTRMLI NAMEVSGIEG NYRITCEAVM SLLRTNKESI QAVMEAFAYD PLINWRLLTT
DNDKQPQVKP KHKDIVPSES LVSTLPSTAQ ARPNSFVEQF EHDESINQKA VTVLKRLSQK
LRGRDFDDGK EYTVNEQVQR LILDATSHEN LCQAYLGWCP LW
//
