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Database: UniProt
Entry: H2Y9G6_CIOSA
LinkDB: H2Y9G6_CIOSA
Original site: H2Y9G6_CIOSA 
ID   H2Y9G6_CIOSA            Unreviewed;      2344 AA.
AC   H2Y9G6;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE            EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
OS   Ciona savignyi (Pacific transparent sea squirt).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC   Cionidae; Ciona.
OX   NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000001964.1, ECO:0000313|Proteomes:UP000007875};
RN   [1] {ECO:0000313|Proteomes:UP000007875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., Ait-zahra M.,
RA   Allen N., Allen T., An P., Anderson M., Anderson S., Arachchi H.,
RA   Armbruster J., Bachantsang P., Baldwin J., Barry A., Bayul T.,
RA   Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., Borowsky M.,
RA   Boukhgalter B., Brunache A., Butler J., Calixte N., Calvo S., Camarata J.,
RA   Campo K., Chang J., Cheshatsang Y., Citroen M., Collymore A., Considine T.,
RA   Cook A., Cooke P., Corum B., Cuomo C., David R., Dawoe T., Degray S.,
RA   Dodge S., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A.,
RA   Elkins T., Engels R., Erickson J., Farina A., Faro S., Ferreira P.,
RA   Fischer H., Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G.,
RA   Gnerre S., Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K.,
RA   Hafez N., Hagopian D., Hagos B., Hall J., Hatcher B., Heller A.,
RA   Higgins H., Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E.,
RA   Iliev I., Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M.,
RA   Karlsson E., Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E.,
RA   Labutti K., Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T.,
RA   Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., Lui A.,
RA   Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., Manning J.,
RA   Marabella R., Maru K., Matthews C., Mauceli E., Mccarthy M., Mcdonough S.,
RA   Mcghee T., Meldrim J., Meneus L., Mesirov J., Mihalev A., Mihova T.,
RA   Mikkelsen T., Mlenga V., Moru K., Mozes J., Mulrain L., Munson G.,
RA   Naylor J., Newes C., Nguyen C., Nguyen N., Nguyen T., Nicol R., Nielsen C.,
RA   Nizzari M., Norbu C., Norbu N., O'donnell P., Okoawo O., O'leary S.,
RA   Omotosho B., O'neill K., Osman S., Parker S., Perrin D., Phunkhang P.,
RA   Piqani B., Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V.,
RA   Raymond C., Retta R., Richardson S., Rise C., Rodriguez J., Rogers J.,
RA   Rogov P., Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T.,
RA   Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C.,
RA   Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., Stetson K.,
RA   Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., Tenzing P.,
RA   Tesfaye S., Theodore J., Thoulutsang Y., Topham K., Towey S., Tsamla T.,
RA   Tsomo N., Vallee D., Vassiliev H., Venkataraman V., Vinson J., Vo A.,
RA   Wade C., Wang S., Wangchuk T., Wangdi T., Whittaker C., Wilkinson J.,
RA   Wu Y., Wyman D., Yadav S., Yang S., Yang X., Yeager S., Yee E., Young G.,
RA   Zainoun J., Zembeck L., Zimmer A., Zody M., Lander E.;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAVP00000001964.1}
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   Ensembl; ENSCSAVT00000001998.1; ENSCSAVP00000001964.1; ENSCSAVG00000001147.1.
DR   GeneTree; ENSGT00930000151037; -.
DR   Proteomes; UP000007875; 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; 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:UP000007875};
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          1225..1780
FT                   /note="FAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51189"
FT   DOMAIN          1963..2279
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          2312..2344
FT                   /note="FATC"
FT                   /evidence="ECO:0000259|PROSITE:PS51190"
SQ   SEQUENCE   2344 AA;  265806 MW;  73806F57B043F8B2 CRC64;
     MAGGVQTFVQ GLKSRNEETR LATATALQHY INTEVQELSS EQNAEFMNEL NSNIYEMVSS
     SDVNEKKGGL LGIVSQIDID GSHGQLSRFY NLIKSLLPSS DVGVMEMAAQ VMGRMAASSG
     NRTEHIEFQV RRSVEWLGTE KNDLRRNAAV LILREMAISS STIFYQQIQS FFDGIFNVIH
     DSKQSIRECA IEALRVALSL VVQRETKESK HRPIWYEEII QLNIDDRVHS SLLILIELLR
     LNFEFLSHFL QMCQFVLSFR TSRNVMIQHS VMSLLPRLAL FNPVKFTESY LSDSMIFLFA
     CLKKDRDRSA AFLAIGLMSM AVTSAIEPYT PKLFEFIKQY LPPKEPSSKN YVPESSIFGC
     IPMVAKSAPA VAVPYIRDEL LQPMFNVGLN AAVMQSLHDL SRIPSLCQSI HDGVLVTLSS
     VLLPNLHPGG DSNAGNVVLP TLIRFIETTE ISTIILALRT LAMFRFTNNE PRRSKIPPSP
     FMDFCEECST AKYLCHENRE LAASRLLSPK LAKIIQSILN LAISDSDKQV RMHVLTLLDD
     HFDCYLILSE NLNLLFVALH DEAFEVQEIA IQTIGRLSEL NPAYVMPMLR RTHIQLVAEL
     EHSGIGRNKL QASRLIGRLA RNAPSFMHAY VVPTIKTLIT KLKDEEQTVA VSVGMMRTIG
     DLAEVGGHDV SVVIDQLFPI ILSMLQAMSC FTKREVALVT LGKVVESTGY VVEPYFKCPT
     LLDVLLAFLK TEPSLAFRKE VMKVLGLIGT LDPFKHKMNQ CSPEDVSFFP PQIDFNVNDM
     LVSIGTTSED FYPAVAITTL MRVLRDPLLS SHHKDVIQAV NHMFQSLKVK CVPYLPEIIP
     TYLSTIQTCD PSIREFLFKS LGLITSTVKQ HARGFMDRIF AVIKEYWGMG SGMQSTLLSL
     TEEIAAALSS EFKLYLPQII PYALRIFLYD DSPGKTVTLQ LLHALEVFGV NMDDYSHILL
     PPMMQLLRAH DTPINIKSAI LETLSTLCDC IDLREHMSLI VHPLTYILDT TPDLQQPAVR
     ALCAAIKQFG ARFAVLVPMV DQIMLKHKIS STLYETLVSK ITKGMLRSDY DGFMWSGGGI
     SDDKTAQPSD ISLTKKIHIH TSNLQMAWTV TRRVSKDDWL EWLRHLSIAL LKESPSLALK
     ACSAFAKTYT PLASHSYIYS NASFLSCWSE LDEGQQDELI SCVEKALAAP DVPPEVTHTL
     LNLAEFMEHT DKGPLPMCDD NGVMLLGETA SRCRAFAKAL HYKELEFNKN PSSSVIGDLI
     NINSKLGQPE AADGALQCYI NTMQKPNQQH NINVEWYERL HKWEAAKSAY HTKKERITEN
     KIGYMRCLEA LGEWDSLHTY AEEQWSTCNT GDSRKRMARL AAAAAWGLGK WTSMDEYACM
     IPREHYDGTL YRAVIAIHQG HFPQAQECIS EAREILDSEL TALAGESHSR AYPALVNCQL
     LAELEEVIHY KLMPERRAVI RQAWWDRLQG CQRKLEDWQR IIQVRSLVVS PQEDMRTLLK
     FSSLCMKTGR QVLAHKTLVK LLNMDPKKEP NKALPTTYPY VSFAYIKHIW KLGKKEEALS
     RMHKFVATIQ NVPPTLSDAE QRSELKHLLA SKEQNGCFLK KTFHRCFLKL GEWNQNMNGL
     NEQNITQIIN FHKLSTEHDR SWYKAWHSWA VINFECVLQL IQPSHTQQSD YSNSILKYAI
     PSVQGFFHSI ALSHGNSLQD TLRVLTLWFE YGHHHSLHDV LVEGIKSIKI ENWLQVIPQL
     IARIDSPKSL VSSINHHLLT DIGKHHPQAL IYPLAVASKS SISMRNHAAN KILNKMCDHS
     NNLVKQAIMV SEELIRVAIL WHELWHEGLE EASRLYFGER DVRAMLATLE PLHALLERGP
     QTLKEITFHH PSTNIKTFQA YGRDLQEAQD WCRKFTQSSN IKDLNQAWDL YYHVFRRISK
     QLPQLTTIEL QYVSPKLMVC KDLELAVPGT YNTSKPIVCI RSVQHTLQVI TSKQRPRKLS
     IKGSNGKDYT FLLKGHEDLR QDERVMQLFG LVNTLLTMDQ ASSRKNLSIQ RFSVVPLSTN
     SGLIGWVPNC DTLHALIRDY RDKKKILLNI EHRIMLRMAP DYDHLSLMQK VEVFEHAINN
     TAGDDLSRLI WLKSPTSEAW FDRRTNYTRS LAVMSMVGHV LGLGDRHPSN LMLDRVSGKV
     LHIDFGDCFE VAMAREKFPE KIPFRLTRML TNAMEVTGIE GNYKHTCRMV MTVLRQHKES
     VMAVLEAFVY DPLLNWRLVD SNPNITRVNL KAVTNLVGVG HKYSDHNRVL EGGSVSDALG
     TVVARPEVLN KKALAIVNRV RDKLTGCDFS SVPIDVPTQV DYLIKQATSH ENLCQCYIGW
     CPFW
//
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