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Database: UniProt
Entry: A0A2A4JT56_HELVI
LinkDB: A0A2A4JT56_HELVI
Original site: A0A2A4JT56_HELVI 
ID   A0A2A4JT56_HELVI        Unreviewed;      2774 AA.
AC   A0A2A4JT56;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
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_12054 {ECO:0000313|EMBL:PCG75225.1};
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:PCG75225.1, ECO:0000313|Proteomes:UP000218220};
RN   [1] {ECO:0000313|EMBL:PCG75225.1, ECO:0000313|Proteomes:UP000218220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HvINT- {ECO:0000313|EMBL:PCG75225.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:PCG75225.1};
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:PCG75225.1}.
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DR   EMBL; NWSH01000622; PCG75225.1; -; Genomic_DNA.
DR   STRING; 7102.A0A2A4JT56; -.
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; 2.
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; 2.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
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; 2.
DR   Pfam; PF00454; PI3_PI4_kinase; 2.
DR   SMART; SM01346; DUF3385; 1.
DR   SMART; SM01343; FATC; 1.
DR   SMART; SM00146; PI3Kc; 2.
DR   SMART; SM01345; Rapamycin_bind; 2.
DR   SUPFAM; SSF48371; ARM repeat; 2.
DR   SUPFAM; SSF47212; FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP); 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   PROSITE; PS51189; FAT; 1.
DR   PROSITE; PS51190; FATC; 1.
DR   PROSITE; PS00915; PI3_4_KINASE_1; 2.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 2.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 2.
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          1325..1870
FT                   /note="FAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51189"
FT   DOMAIN          2040..2359
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          2396..2709
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          2742..2774
FT                   /note="FATC"
FT                   /evidence="ECO:0000259|PROSITE:PS51190"
SQ   SEQUENCE   2774 AA;  319635 MW;  376C3E9E885A0C02 CRC64;
     MKMTSFQVSD LVSGLKSRHA ETRHKAIREL LHFTKTDLRE MSQESLRQVL DDFNQQIHAL
     TSSYDNNEKK AGILTIVCLI GGDTETTKTR NIRYAYYLRN VFPSTDYNVL ELGAKTMGRL
     AVTLGIKRGE YVESELKRAY EWLAEERNEG KRLSAVMILR ELAICMPSYF FQHINGFFNY
     IMIPLRDPKE QIREAAAKAL RAALVITSQR EIPEQSNKAH WYIQCYEQSM LSFAEQPGRE
     RGLSRDDHVH GALLILNELL RCSNATWEKK YTTLMQKLDA EQDISDEMTS LSSKVQNSWT
     AQHFPDDKSQ QTLVYESSIC KKLIEEQYEK ICSDVMAQQI SRAHNVHQML LLMIPRLAAF
     NREAFAKRHL KSTINHLITF LRGREKEKAM AFTTLGLICV AVESDVQQYL GRIIEIIKLT
     LPLKDTPKKR NGSDTPLFNC VTLLGFAMKE DVANEVKELL DPMCATGLSP QLTTCFKELS
     QNLPSLKKEI TDRLLNMLSL ILRKKPYAPN NGENQIVHMF TTAMLVEPHD ASKLVLALRT
     LGSFDFEWNN TLMSFIRRCT DHYLLSEQHD IRIEAVKTAS KLLIKAVERC AQTNSRTLTV
     IVDESLGKLL SVGRSDFDHE VRYRVLEIFT NPVFDRYLAV EEHLNCLFVA INDSNNDVSE
     LALCLVGRLS NINPSYTIPT LRQLFVQVLM ELQHSESTRN KEQALRMVNN IISHAPRITR
     QFVDTILNVL VPKLKAEADN PTMVATILKA IGDLAEVNGG GTALNKWLPE LMSIQINILS
     DPNQPEKRSV ALWSFGQVVG ATGHVVTPYM EYPHLMDMML NFLKTEQQPR ERRETIRVLG
     LLGALDPYKH KVNQGLIDFQ TVSTLIPVSD STNENIDINI SDMVVNMSPL ILDEFYPAIV
     LTSLMRMLRD PMLTQHHTSV VHSVTFIFQS LGIKCVPYVS RVTPCLLNVI RTTDNSTFRE
     FLLTQLAQLI SVVKIQIRNY LEDIFDIIKE YWTPNSQLQP TLIMLVEHIT VAIGPEFKVY
     LRKILPNILR VLKYDNSKDR VLTEKLLLTI QKFENNLDDV LLSIVPAVTA LFDGRNIPLS
     ISKLAMETME HLCMYLYFRP FSAVIIQALA KVLDNNPSLR QTAMNTLCAL IVQLGREYID
     YIPSVDRILI KHKIQCPNYI VLVTRLQAIS TLASDDDYLD ETRLRLRNQK TDVVGPGDIQ
     TIQKLSLNVS NLRKCWSIKN IVSKEDWMEW LRQLSVAFLT ESNSPAIRAC SSLAQNYPQL
     ASELFNAAFM SCWTELDDKS RKELVQALEH ALTVPDTPEL ALAVLNLAEF LEHCEKGSLP
     IPIKLLGDTA INCRAYAKAL YYKEQEYKRN PSKQVIEALI HINNKLQRNE ASNGLLEKVI
     TQKKSGETSL NVHVRWYEKL HNWDQALELY NKKLEVEPLD EDSRLGMMRC LEALGEWRKI
     YNLTSEQWDN ASEDVRKKSA KIAAAASWGL QEWDSMRKYV EVISEDSHEG AFYRAILAIH
     EGHWPESRHY IDSARSLLDL ELTAVVGESY QRAYGALVNA QLLTELEEVV TYKLVEERRN
     PIRKCWWLRL QGGQRLVEDW RKMLQIRSLV MSPREDFQTW LKFASLCRKT GAFNQAHKIV
     LSILGCDPIT NPDVLLRMQD PRIVLAYSKN LWDAGNKRYA YDVLQRFLDN SEPDNDEHCR
     LLARCHLKLG SWCESLQEIN ELSIPEILRN YESATLLAPD WYKACHAWAC MNFETVLFYK
     QQDNISESSL AGGSGEKKVS RTDFINTHTI PAIEGFFKSI SLSNGSALQD TLRLLTLWFD
     HGHHPAIYDA LFEGIRQIDV KIWLQVIPQL IARIDSPRSL VAKLVHILLI DIGKLHPQAL
     VYPLTVATKS SFVTRKNAAN YILKTMCAHS QNLVNEAAII SEELIKVAIL WHDQVFIALD
     EASSEKDYRG MFKTLDKIHA MLDRPPETLK EVSFLQMYGR DLQEAHRWME LYKESGENRY
     LNEAWDLYYH VVRRITNQFR SLTSLELQYV SKRLHTCKDL ELAVPGSYVP NEKVIRISHI
     HSHLQVIKSK QRPRRLTIQG SDGKQYMFLL KGHEDLRQDE RVMQLFGLVN TLLQADTNTY
     RHDLAIQRYA VIPLSPNSGL IGWVPQCDTL YNLISDYRDK KSNKMALSTE QQIMLRMASD
     YQKLMLKHKV EVFEYTLSQT PGNDLSRLLW LKSPSAEAWF ERRTNYTRSL AVMSMVGYIL
     GLGDRHPSNI MLHRVTGKVL HIDFGDCFEV TQSREKFPEK IPFRLTRMLI NAMEVRLYYS
     EKDYRGMFKT LDKIHAMLDR PPETLKEVSF LQMYGRDLQE AHRWMELYKE SGENRYLNEA
     WDLYYHVVRR ITNQFRSLTS LELQYVSKRL HTCKDLELAV PGSYVPNEKV IRISHIHSHL
     QVIKSKQRPR RLTIQGSDGK QYMFLLKGHE DLRQDERVMQ LFGLVNTLLQ ADTNTYRHDL
     AIQRYAVIPL SPNSGLIGWV PQCDTLYNLI SDYRDKKSNK MALSTEQQIM LRMASDYQKL
     MLKHKVEVFE YTLSQTPGND LSRLLWLKSP SAEAWFERRT NYTRSLAVMS MVGYILGLGD
     RHPSNIMLHR VTGKVLHIDF GDCFEVTQSR EKFPEKIPFR LTRMLINAME VTGIEGTYRS
     TCESVMHVLH KHRDSVMAVL EAFVYDPLLN WRLVDNERHS LSESSFSSDI ESSYTLPSRS
     RNHLHYESLE MPPEANLNKR ALSILNRIRD KLTGRDFPHV EAVVSVPKQV DLLIKQATSN
     ENLCQCYIGW CPYW
//
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