ID K7FIV9_PELSI Unreviewed; 2521 AA.
AC K7FIV9;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 72.
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|Ensembl:ENSPSIP00000007969.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000007969.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000007969.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR EMBL; AGCU01113079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01113080; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01113081; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01113082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01113083; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01113084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01113085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01113086; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006127106.1; XM_006127044.2.
DR Ensembl; ENSPSIT00000008011.1; ENSPSIP00000007969.1; ENSPSIG00000006751.1.
DR GeneID; 102451030; -.
DR CTD; 2475; -.
DR GeneTree; ENSGT00930000151037; -.
DR HOGENOM; CLU_000178_7_1_1; -.
DR OMA; MRQHSAK; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000007267; 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; 4.
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; PS00915; PI3_4_KINASE_1; 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:UP000007267};
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 1368..1954
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2128..2441
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2489..2521
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 1798..1838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1808..1837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2521 AA; 286619 MW; A9A94F790F03E0F3 CRC64;
MSGTVSILQH FASGLKSRNE EIRAKAAKDL QHYVTMELRE MSQEESTRFY DQLNHHIFEL
VSSSDANERK GGILAIASLI GVEGGNATRI GRFANYLRNL LPSNDPVVME MASKAIGRLA
VAGDTFTAEY VEFEVKRALE WLGADRNEGR RHAAVLVLRE LAISVPTFFF QQVQPFFDNI
FVAVWDPKQA IREGAVSALR ACLILTTQRE PKEMQKPQWY RHTYEEAEKG FDETLAKEKG
MNRDDRIHGA LLILNELVRI SSMEGERLRE EMEEITQQQM VHDKYCKDLL GFGTKPRHIT
PFTSFQSVQP SQSNALVGLL GYSPHQGIMG FGASPVPAKS TLVESRCCRD LMEEKFDQVC
QWVLKCRTSK NSLIQMTILN LLPRLAAFRP SAFTADQYLP DTMNHVLSCV KKEKERTAAF
QALGLLSVAV RSEFQAYLPK VLEIIKAALP PKDFAHKRQK SMQVDATVFT CISMLARAMG
PCIQQDIKEL LEPMLAVGLS PALTAVLYDL SRQIPQLKKD IQDGLLKMLS LVLMHKPLRH
PGMPKGLAHQ LASPSLTNIP EASDVGSITL ALRTLGSFEF EGHSLTQFVR HCADHFLNSE
HKEIRMEAAR TCSRLLTPSI HLISGHAHVV SQTAVQVVAD VLSKLLVVGI TDPDPDIRYC
VLASLDERFD AHLAQAENLQ ALFVALNDQV FEIRELAICT VGRLSSMNPA FVMPFLRKML
IQILTELEHS GVGRIKEQSA RMLGHLVSNA PRLIRPYMEP ILKALIVKLK DPDPDPNPGV
INNVLATIGE LAQVSGLEMR KWVDELFIII MDMLQDSSLL AKRQVALWTL GQLVASTGYV
VEPYRKYPTL LDVLLNFLKT EQNQGTRREA IRVLGLLGAL DPYKHKVNIG MIDQSRDASA
VSLSESKSSQ DSSDYSTSEM LVNMGNLPLD EFYPAVSMVA LMRIFRDQSL SHHHTMVVQA
ITFIFKSLGL KCVQFLPQVM PTFLNVIRVC DGAIREFLFQ QLGMLVSFVR SHIRPYMDEI
VTLMRDFWVM NNSIQSTIIL LIEQIVVALG GEFKLYLPQL IPHMLRVFMH DSSPGRNVSV
KLLNAIQLFG ANLDDYLHLL LPPIVKLFDA QDVPVVARKA ALETVDRLTE SLDFTDYASR
IIHPIVRTLD LSPELRPTAM DTLSSLVFQL GKKYQIFIPM VNKVLVRHRI NHQRYDVLIC
RIVKGYTLAD EEEDPLIYQH RILRSNQGET LASGPVETGP MKKLHVSTIN LQKAWGAARR
VSKDDWLEWL RRLSLELLKD SSSPSLRSCW ALAQAYNPMA RDLFNAAFVS CWSELNEDQQ
DELIRSIELA LTSQDIAEVS QTLLNLAEFM EHSDKGPLPL RDDNGIVLLG ERAAKCRAYA
KALHYKELEF QKGPTPAILE SLISINNKLQ QPEAAAGVLE YAMKHFGELE IQATWYEKLH
EWEDALVAYD KKMDTNKDDP ELMLGRMRCL EALGEWGQLH QQCCEKWTLV IDETQAKMAR
MAAAAAWGLG QWDSMEEYTC MIPRDTHDGA FYRAVLALHQ DLFSLAQQCI DKARDLLDAE
LTAMAGESYS RAYGAMVSCQ MLSELEEVIQ YKLVPERREI IRQIWWERLQ GCQRIVEDWQ
RILMVRSLVV NPHEDMRTWL KYASLCGKSG RLALAHKTLV LLLGVDPSRQ LDHPLPTVHP
QVTYAYMKHM WKSARKIDAF QHMQHFVQTM QQQAQHAIAT EDQQHKQELH KLMARCFLKL
GEWQLNLQGI NESTIPKVLQ YYSASTEHDR NWYKAWHAWA VMNFEAVLHY KHQNQARDEK
KKLRHASGAS ITSANTEGSN SDSEAESTEN SPIPSPVQKK VTEDLSKTLL LYTVPAVQGF
FRSISLSRGN NLQDTLRVLT LWFDYGHWPD VNEALVEGVK AIQIDTWLQV IPQLIARIDT
PRPLVGRLIH QLLTDIGRYH PQALIYPLTV ASKSTTTARH NAANKILKNM CEHSNTLVQQ
AMMVSEELIR VAILWHEMWH EGLEEASRLY FGERNVKGMF EVLEPLHAMM ERGPQTLKET
SFNQAYGRDL MEAQEWCRKY MKSGNVKDLT QAWDLYYHVF RRISKQLPQL TSLELQYVSP
KLLMCRDLEL AVPGTYDPNQ PIIRIQSIAP SLQVITSKQR PRKLTLMGSN GHEFVFLLKG
HEDLRQDERV MQLFGLVNTL LANDPTSLRK NLSIQRYAVI PLSTNSGLIG WVPHCDTLHA
LIRDYREKKK ILLNIEHRIM LRMAPDYDHL TLMQKVEVFE HAVNNTAGDD LAKLLWLKSP
SSEVWFDRRT NYTRSLAVMS MVGYILGLGD RHPSNLMLDR LSGKILHIDF GDCFEVAMTR
EKFPEKIPFR LTRMLTNAME VTGLDGNYRI TCHTVMEVLR EHKDSVMAVL EAFVYDPLLN
WRLMDTNTKG NKRSRTRTDS YSASQSVEML DNVELGETAH KKTGTTVPES IHSFIGDGLV
KPEALNKKAI QIINRVRDKL TGRDFSHDET LDVPTQVELL IKQATSHENL CQCYIGWCPF
W
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