ID E0W704_BACDO Unreviewed; 2460 AA.
AC E0W704;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN Name=LOC105222371 {ECO:0000313|RefSeq:NP_001291913.1};
OS Bactrocera dorsalis (Oriental fruit fly) (Dacus dorsalis).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Bactrocera; Bactrocera.
OX NCBI_TaxID=27457 {ECO:0000313|EMBL:ACN38706.1};
RN [1] {ECO:0000313|EMBL:ACN38706.1, ECO:0000313|RefSeq:NP_001291913.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20734415; DOI=10.1002/arch.20383;
RA Suganya R., Chen S.L., Lu K.H.;
RT "Target of rapamycin in the oriental fruit fly Bactrocera dorsalis
RT (Hendel): its cloning and effect on yolk protein expression.";
RL Arch. Insect Biochem. Physiol. 75:45-56(2010).
RN [2] {ECO:0000313|RefSeq:NP_001291913.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26946038;
RA Zheng W., Luo D., Wu F., Wang J., Zhang H.;
RT "RNA sequencing to characterize transcriptional changes of sexual
RT maturation and mating in the female oriental fruit fly Bactrocera
RT dorsalis.";
RL BMC Genomics 17:194-194(2016).
RN [3] {ECO:0000313|RefSeq:NP_001291913.1}
RP IDENTIFICATION.
RG RefSeq;
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; FJ167395; ACN38706.1; -; mRNA.
DR RefSeq; NP_001291913.1; NM_001304984.1.
DR EnsemblMetazoa; NM_001304984.1; NP_001291913.1; LOC105222371.
DR GeneID; 105222371; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000504616; Unplaced.
DR GO; GO:0031931; C:TORC1 complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; 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 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 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 2: Evidence at transcript level;
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:UP000504616};
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 1347..1896
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2070..2397
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2428..2460
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2460 AA; 280164 MW; 3BAA492EDED1B344 CRC64;
MSTAALVQQF VAGLKSRNRN VQNKAAQDLF MYVKTELREM SQEDLVAFFD DFNHQIFSMV
NSADINDKKG AVLAIKCLIS GDVVNTMKRI SPYYNHLRTL LPSNDTTVME IAARTLVKLA
NLPGSKGAES IDFDIKRAFE MLSGDRQEYR RHAAVFILRE LAIAMPTYFY QQISTFFDNI
FNAIFDPKAA IRESAGEALR AALIVTSQRE STKQSTEPQW YKTCYQEASA SFVAEPTGTK
DQKGMTRDDC IHGGLIILNE LFRCSHAAWE RRYATLKSLL PDAQHNKFGE VIHSGSVGSQ
LTTLVPRLKA PFISKLGSTH MHLDHDAQHG GTHKFSSATV LESAYSREIL TENYINICDN
VLEQRTSKSP YVQQALLHIL PRLAAFNREV FVQRYLQECV SHLLSIVPRK EKDRNIAYVT
IGYIAVAVER DIDKHLRTIM CAIKIALPPK ITPSKRKAAI DPAIFHCITL LAHAVKSGIT
EDVRNILEQM FFSGLSPALT VCLRELAENV PHLKSAIAEG LIRVLSQVLM NKPLAIPYQT
LATIPLDPSI NLQHDVPTVV LALKTLGSFN FEEQNMLDFV QRCADHFINH DQQEIRLEAV
QTCTRLLKLA VQSADSTESS NTLSETVSHV IERLLIVAIT DMDCNVRIRI LSSLDETFDA
ELAQPESLSA LFITLNDEIF EIRELAMVTV GRLSAMNPAY VMPKLRKIMI QLLTELEHSG
MSRNKEQSAR MLDHLIISTP RLISSYMHPI LTILVPKLRE ADPNPGVILN VLRAIGDLAE
VNGGSNEMEM WADDLLSILL EMLGDAGSPE KRGVALWTLG QLISATGRVV TPYHKYPGLI
DILINFLKTE QRRSIRRETI RVLGLLGAMD PYKHKMNKGL IDSQKDSVLI SLSDFKMDEN
QDISTAELLV NMSNVLDEYY PAVAIAALMR ILRDPTLSSR HTSVVQAITF IFKSLGIKCV
PYLAQVLPSL LENVRTADIN LREFLFQQLA ILVQIVKQHI ISYMSDIFKL IKEFWTVYTT
LQLTLINLIE QIALALGCEF RNYLSELIPQ ILRVLQHDTS KDRAVTKRLL QALQKFGNTL
DDYLHLIVPP IVKLFDAPYV PQQVSLVALE TIDHLAWILD FTDFSSRIIH PLVRVLEAEP
ELREQAMSTL CSVVIQLGKK YLVFVPLVER TITKHRIVDS KYEKLLTKIQ SNTTMCLDDE
FHMRQTKFKS TELVAPNSGG NFAMKRLIVS TSNLRAAWQV TRRVSKDDWV EWLKRLSIGL
LKESRSQALR ACHVLAQDYD KLLRDLFNAA FISCWTELLQ EHKNELTQSL IQALQVTDMP
EITQTILNLA EFMEHCDTDP IPIETKLLGT RAMACRAYAK ALRYKEEEFQ THKDPQVLES
LILINNKLQQ KEAAEGLLTT YRNASNEFKV QGRWYEKLHN WEQALKHYSG NLKDNSNDLE
ARLGHMRCLE ALGEWSELSS VAKQEWDNLG RDARSRAGPL AAVAAWGLQD WEAMQEYVRC
IPEETQDGSF YRAVLAVHNE DFETAQRLID GTRDLLDTEL TSMAGESYER AYGAMVCVQM
LAELEEVIQY KLIPERREPL KSMWWKRLQG GPRLVEDWRR IIQVHSLVVR PQEDVHTWLK
YASLCRKSGS LHLSHKTLVM LLGTDPSTQP KEQLPYNQPQ VTYAYTKHMA AAENMQGAYE
QLSCFVNAFQ AKLNCIGPEE AAKQDHRLLA RCYLRLGKWQ NKLQSSLEPE IVQGALDCFE
KATENDPTCY KAWHLWAYMN FKVVQAQKQQ LDKLAHTATN GDILQDKEKL IIEHAVQAVD
GFFRSISLIK GNSLQDTLRL LTLWFDYGQY SEVYDALLTG MKTIEINTWL QVIPQLIARI
DTHRKLVNQL IHHLLIDISK YHPQALVYPL TVASKSASVA RKNAAFKILE SMRKHYPTLV
QQAMTCSEEL IRVAILWHEQ WHEGLEEASR LYFADRNVKG MFDILEPLHA LLARGPQTLK
ETSFSQAYGR ELTEAYEWTQ RYKTSSVLMD LDHAWDIYYH VFQKISRQLP QLTSLELPYV
SPKLMTCKNL ELAVPGSYNP NQDLIRIDHI KTNLQVITSK QRPRKLCLRG SNGKDYMYLL
KGHEDLRQDE RVMQLFSLVN TLLLDDPDTF RRNLAIQRYA VIPLSTNSGL IGWVPHCDTL
HTLIRDYRDK RKMLLNQEHR LMLSVSPDYD HLTLMQKVEV FECALAQTQG DDLAKLLWLK
SPSSEVWFER RTNYTRSLAV MSMVGYILGL GDRHPSNLML DRMSGKILHI DFGDCFEVAM
THEKFPEKIP FRLTRMLIKA MEVTGIEGTY RRTCESVMLV LRRNKDSLMA VLEAFVYDPL
LNWRLLDMDK NHRSKSNNDP GGSGMAFGGG NGSLSNSVEE PLLHSQLMSA NRLMGGALMV
ADITNSKASK VIKRVRSKLN GTDFQTQNSV AVPQQVDLLI QQATNNENLC QCYIGWCPFW
//
