UniProt: B4LSZ6

Database: UniProt
Entry: B4LSZ6_DROVI

LinkDB:  B4LSZ6_DROVI 
Original site:  B4LSZ6_DROVI

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Ontology (11)   
   GO (11)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (28)   
   InterPro (14)   
   Pfam (5)   
   PROSITE (5)   
   SMART (4)   
Literature (1)   
   PubMed (1)   
All databases (45)   

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ID   B4LSZ6_DROVI            Unreviewed;      2471 AA.
AC   B4LSZ6;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE            EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN   Name=Dvir\GJ16824 {ECO:0000313|EMBL:EDW63827.1};
GN   ORFNames=Dvir_GJ16824 {ECO:0000313|EMBL:EDW63827.1};
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244 {ECO:0000313|EMBL:EDW63827.1, ECO:0000313|Proteomes:UP000008792};
RN   [1] {ECO:0000313|EMBL:EDW63827.1, ECO:0000313|Proteomes:UP000008792}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15010-1051.87 {ECO:0000313|Proteomes:UP000008792};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
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; CH940649; EDW63827.1; -; Genomic_DNA.
DR   RefSeq; XP_002051672.1; XM_002051636.2.
DR   SMR; B4LSZ6; -.
DR   STRING; 7244.B4LSZ6; -.
DR   EnsemblMetazoa; FBtr0232749; FBpp0231241; FBgn0204003.
DR   GeneID; 6627365; -.
DR   KEGG; dvi:6627365; -.
DR   eggNOG; KOG0891; Eukaryota.
DR   HOGENOM; CLU_000178_7_1_1; -.
DR   InParanoid; B4LSZ6; -.
DR   OMA; MRQHSAK; -.
DR   OrthoDB; 8448at2759; -.
DR   PhylomeDB; B4LSZ6; -.
DR   Proteomes; UP000008792; 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:0016043; P:cellular component organization; IEA:UniProt.
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; 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; 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:UP000008792};
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          1355..1907
FT                   /note="FAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51189"
FT   DOMAIN          2081..2402
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          2439..2471
FT                   /note="FATC"
FT                   /evidence="ECO:0000259|PROSITE:PS51190"
SQ   SEQUENCE   2471 AA;  281624 MW;  7BB586E7B1C95A1E CRC64;
     MSTSSIVQQF VNGLKSRNRN VQNKAAQDLF LYVKTELREM SQEELVQFFD DFDHHIFNMV
     NATDINEKKG GALAMKCLIS GDALITRKGI SPYLNRLRDL LLINDVSVME IAARSLVKLA
     NMPGSKGAES FDFDIKKAFE MLSGDRQEYR RHAAVFILRE LAIALPTYFY QQILTFFEHI
     FNAIFDPKPA IRESAGEALR AALIVTAQRE STKQSSEPQW YKICYEEASS SFSSDVLTGK
     EQKGMTRDDR IHGGLIVFNE LFRCANAHWE RRYTTLKMLF PKSQHNKFLE ATNSSSVGNQ
     LTTIVPRLKV PFVDKLGSTQ MHMEGEQHNA TGNKLTSQNV LESAYAHEIL KEHFITICDN
     VLEQRTSKSP YVQQALLQIL PRLAAFNREV FVAQYLKTCV AHLMSILRGK EKDRNVAYIT
     IGYIAVAVES DIEKHLKHIM GSIKQALPAK DLASKRKPPV DAAVFACITL LAHAVKSQIA
     DDVREILEQM FHTGLSPALT VCLRELAENV PQLKSAITDG LIGILFQVLM NKPATIPYAT
     MPPISIDASL LLQSADSPTI VLALRTLGTF NFEEQNMLDF VQRCADYFIV HEHQEIRLEA
     VQTCTRLLKL AVQSSDSMEN SKTLSDTVSH VIERLLSVAI TDMDYNVRIR ILRSLDETFD
     AKLAQPESLN ALFITLHDEI FEIRELAMVT IGRLSSMNPA YVMPKLRTTM IELLTDLKYS
     GMSRNKEQSA RMLDHLVIST PRLISSYMNP ILKALVPKLH EPESNPGVVL NVLRTIGDLA
     EVNGGSNEME LWADELLSIL LEMLGDAGSP DKRGVALWTL GQLISATGRV VSPYHKYPVL
     IDILINFLKT EQRRSIRRET IRVLGLLGAM DPYKHKMNKG LIDSQKDNVL IAYSDGKADE
     SQDISTAELL VNMGSHALDE YYPAVAIAAL MRILRDPTLS TRHTSVVQAV TFIFHTLGIK
     CVPYLAQVLP NLLDNVRTAD NNLREFLFQQ LAILVAFVKL HIISYMDDIF KLIKEFWTIN
     TPLHSTLINL IEQIAVALGC EFRDYLAQLI PQILRVLQHD NSKDRMVTRR LLQALQKFGS
     TLGYYLPLIV PPIVKFFDSP YVPQQVSLVA LETINSLAGQ LDFTDFSSRI IHPLVRVLET
     EPELREQAMT TLRSLVKQLG KKYLVFVPMV QRTINKHRIV DAEYEKLLDH IQSNSTLVDG
     CGIGVGIGGD FGQRQAKPKY NEPFVLDSNS SSKNLKVSTN ALRTAWQVTR RVSKDDWVEW
     LKRLSIGLLK ESPSHALRAC CVLAQDYDTL LRDLFNAAFI SCWTELSPEH RHELTQSLIQ
     ALQVTDMPEI TQTILNLAEF MEHCDRDPIP IETQLLGTHA MACRAYAKAL RYKEEEFVPR
     QEAHVFESLI HINNKLQQRE AAEGLLTTYR NTASEGSVHG RWYEKLHNWD QALHHYQLNL
     NADPNDLEAR LGHMRCLEAL GDWSQLSTRC KEEWPNFSTE AKSRASPLAA VAAWGLKDWD
     GMQEYVRCIP VDTQDGSFYR AVLAVHHDDF ETAQRLIDET RDLLDTELTS MAGESYERAY
     GAMVCVQMLA ELEEVIQYKL IPERREPLKA MWWKRLQGGQ RLVEDWRRII QVHSLVVKPH
     EYIHTWLKYA SLCRKSGSLY LSHKTLVMLL GTDPALAPDE PLPCNQPQVT YAYTKYLAAS
     SQPQLAYKQL RDFVNTYSTQ LSCLPSEALK QQDQRLMARC YLRLATWQDK LHENRPNPDA
     VQGALECFEK ATNYDPNWYK AWHLWAYMNF KVVQSQKQVL ENQRQQSPAS MGLGLDSEHL
     IIQQYAVPAV QGFFRSISLI RGNSLQDTLR LLTLWFDYGH HAEVYEALFS GMKMIEINTW
     LQVIPQLIAR IDTHRKLVGQ LIHQLLMDIG KNHPQALVYP LTVASKSASL ARKNAAFKIL
     DSMRKHSPTL VEQAVMCSEE LIRVAILWHE QWHEGLEEAS RLYFGDRNVK GMFEILEPLH
     AMLDRGPQTL KETSFSQAYG RELTEAYEWT QRYKTSAVLM DLDRAWDIYY HVFQKISRQL
     PQLTSLELPY VSPKLMTCKN LELAVPGSYN PGQELIRINH IKTNLQVITS KQRPRKLCIR
     GSNGKDYMYL LKGHEDLRQD ERVMQLFSLV NTLLLDDPDT FRRNLAIQRY AVIPLSTNSG
     LIGWVPHCDT LHTLIRDYRE KKKVPLNQEH RTMLNYAPDY DHLTLMQKVE VFEYALGQTQ
     GDDLAKLLWL KSPSSELWFE RRNNYTRSLA VMSMVGYILG LGDRHPSNLM LDRMSGKILH
     IDFGDCFEVA MTREKFPEKI PFRLTRMLIK AMEVTGIEGT YRRTCESVML VLRRNKDSLM
     AVLEAFVYDP LLNWRLLDVD KKANDTTATT AAGASGGSPS NSIEQESLLQ GNPLAKSKTY
     EAQQLHVGYT NVADVTNSKA SMVIQRVNRK LTGTDFQMTE MTEQQQVELL IQQATNNENL
     CQCYIGWCPF W
//

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