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
//