ID A0A2A4JTT6_HELVI Unreviewed; 2425 AA.
AC A0A2A4JTT6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN ORFNames=B5V51_12056 {ECO:0000313|EMBL:PCG75229.1};
OS Heliothis virescens (Tobacco budworm moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Heliothinae; Heliothis.
OX NCBI_TaxID=7102 {ECO:0000313|EMBL:PCG75229.1, ECO:0000313|Proteomes:UP000218220};
RN [1] {ECO:0000313|EMBL:PCG75229.1, ECO:0000313|Proteomes:UP000218220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HvINT- {ECO:0000313|EMBL:PCG75229.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:PCG75229.1};
RA Fritz M.L., Deyonke A.M., Papanicolaou A., Micinski S., Westbrook J.,
RA Gould F.;
RT "Contemporary evolution of a Lepidopteran species, Heliothis virescens, in
RT response to modern agricultural practices.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PCG75229.1}.
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DR EMBL; NWSH01000622; PCG75229.1; -; Genomic_DNA.
DR Proteomes; UP000218220; 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:UP000218220};
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 1336..1876
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2050..2360
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2393..2425
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2425 AA; 276459 MW; 702A5C5AADE52468 CRC64;
MSNQVGAFVA GLKSRNVDVQ IKTARELYHF AKTELREVPQ EELTQFLDEF NHQIFEMVSS
NDVHEKKGGV LAIVCLIGGD CDTTKTRITR FANYLRNLLP SSDVGVMELA AKTVGRLATV
SGVKRAEYVE FEVKRAFEWL SEERNEGRRH SAVLLLKELA IAMPTYFYQQ VSGFFDHILV
ALKDPKPQIR EAAAKALRAG LVVTAQRETA KQSTAKPQWY MQCYEEAMLS FEDIPLKEKG
MTKEDRVHGG LLILNELLRC SNAVWEKKYS YLMQSLDTQK DITVSDDIIF ISTKLHSPSV
KRGYLCDGFK TENVTYPVPI YESEVCRKLL TEKFERLCRD VMSQRMLKTQ GVPQILLVII
PRLAAFNKNY FLDKYLISTM NYLISCLRSR EKDRNMAFTT LGLMAAALEN DIKKYIPSIM
EVIKQTLPIR DSQTKKRVWI DPSIFACITL LGSAVKDLVL TDIKELLDAM FATGLSPSLT
ICLRELSNNL PSLRTEISEG LLNMLSLVLR NKPFLHPGVP RSLEQQMSNM SLVMEPQDTA
SIVLALRTLG TFNFEGQHSL LTFVRRCADH FLQSDQQEIR LEAVKTAAKL LADATVRTMK
TPSRTLTLLT AEVIGKLLVV TVTDPDYEVR YWVLESLYNI FDIHLAQIEN LSFLFMAMND
EHLAIRELAI CTVGRLSVVN PAYVMPGLRK TLIQYLTELE HSGMSRNKEQ AARMLDNLIR
HAPKLVKPYM ETILNVLVPK LRESDSNPGV VISVLKAVGD LADVHGDNSG LKKWLPELLS
ILLELLSDAS ATEKRSVALW AFGQLISATG YVVAPYTEYP TLMDVLLNFL KTEQQPKDRR
ETIRVLGLLG ALDPYKHKIT RGLIGEQPDS SLVPVADSKA EENNFDMTTS EMLVNMSSPV
LDEYYPAIVI STLMRILRDP TLQQHHTSVV QAVTFIFQSL GIKCVPYISR VTPSLLYVAR
ATDNNNFREF LFTQLARLIA IVKQHIRNYL DKIFDLIREF WTPNSPFQPT LILLVEYIAV
ALGSEFKVYL PQLMPQILRV LAHDTSKDRI VTEKLLYALQ KFEDNLDDYM HLVIPSIVKL
FDASDCPINV AKVAMETVDY LSDSLNYSEL VSRIIHPLVR SLDTCAALRP TAMDTLCALI
VQLGRKFTDF IPLVQKVVVR HKIQHQNYEL LLSRMQSSQT LAMDEFLQST RRKPRNHTQE
PRIGYNCDTS QSIRKLCVNA HNLKLAWTVS SRVSKDDWLE WLRRFSIGLL TESHSPALRA
CLALAHNYSQ LLRDLFNAAF VSCWTELDKT SRAELSNALE QALTAPDAPE LAHTVLNLAE
FMEHCEGGTL PISTHLLGER AMHCRAYAKA LHYKEEEFRN GATSQVVEAL IHINNKLQQK
EAAEGLLERV MAQREAGDAT LKVQIRWYEK LHNWEKALDL YGEKLNEDVG DMDSYLGELR
CFEALGEWVE LYNTVSKKWV KMSNDERFKA ARLAAAAAWG LNEWDSMAKY VRFLPENTQD
GAFYRAVLNI HNGEFDLSKQ YIDQARTLLD SELTAVAGES YQRAYGALVN AQLLAELEEV
ITYKSVMERR ESIRQAWWTR LQGGQRLVED WRRILQVRSL VLTPQEDMAT WLKFASLCRK
SGAPRQAHKT LVMLLGTDPS QNRDMPLPTH EPRLTLAYAK HLWVAGDKQL AYDQLQRYVD
TTETGDAEHC RLLARCHLKL GSWCESLLGI NELSIPEILR NYAAATDLSS DWYKAWHAWA
YMNFETVLFY KHQDANITGG QAERRPSPEC IQQHTVPAVE GFFKSIKLSH GSSLQDTLRL
LTLWFDYGHY PAVHEALVEG IRTIEINVWL QVIPQLIARI DTPRALVGKL IHSLLIDIGK
SHPQALVYPL TVASKSSFIA RKNAANQILK SMCTHSSNLV NQAAMISEEL IRVAILWHEQ
WHEALEEASR LYFSENDVNA MFKTLEPLHA MLERGPQTLK EVSFSQAYGR DLNEAQEWCN
RYKESGLVRD LNQAWDLYYH VFRRISRQLP QLTSLELQYV SPRLLNCRDL ELAVPGSYVP
DQDLIRIAHI QSSLQVITSK QRPRRLCIRG SNGKDYIFLL KGHEDLRQDE RVMQLFGLVN
TLLQADPDTF RRDLAIQRYA VIPLSTNSGL IGWVPHCDTL HSLIREKRKC LLNIEHRIMQ
RMASDLDKLM LMQKVEVFEH ALEHTAGDDL AKLLWLKSPS SEVWFERRTN YTRSLAVMSM
VGYILGLGDR HPSNIMLDRV TGKFLHIDFG DCFEVAVTRD KFPEKIPFRL TRMLINAMEV
TGIEGTYRRT CESVMEVLHR HKDSVMAVLE AFVYDPLLNW RLIDAGRRSR ADAEVCSTSD
PASSPQPSRS RVHIGLNDAL DQPAETNLNK RALAIVNRVR DKLTGRDFPH IDEIVSVQKQ
VDLLIQQATS NENLCQCYVG WCPFW
//
