ID A0A158NVZ1_ATTCE Unreviewed; 2437 AA.
AC A0A158NVZ1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN Name=105624966 {ECO:0000313|EnsemblMetazoa:XP_012061699.1};
OS Atta cephalotes (Leafcutter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012061699.1, ECO:0000313|Proteomes:UP000005205};
RN [1] {ECO:0000313|Proteomes:UP000005205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA Weinstock G.M., Gerardo N.M., Currie C.R.;
RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT insights into its obligate symbiotic lifestyle.";
RL PLoS Genet. 7:e1002007-e1002007(2011).
RN [2] {ECO:0000313|EnsemblMetazoa:XP_012061699.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (APR-2016) 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; ADTU01027564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012061699.1; XM_012206309.1.
DR STRING; 12957.A0A158NVZ1; -.
DR EnsemblMetazoa; XM_012206309.1; XP_012061699.1; LOC105624966.
DR GeneID; 105624966; -.
DR KEGG; acep:105624966; -.
DR eggNOG; KOG0891; Eukaryota.
DR InParanoid; A0A158NVZ1; -.
DR OMA; MRQHSAK; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000005205; 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; 5.
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; 2.
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:UP000005205};
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 1319..1876
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2050..2363
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2405..2437
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2437 AA; 277846 MW; D16139A1CC1BEEF7 CRC64;
MSSILMQQFV QRLKSRNEEA RNKAARDLCL YVKRELREAS QEEIIAFMDE FNHHIFEMVS
ASDINEKKGG ILAIVCLIGA DVGNFNTRTV RFANYLRNLI PSNDVGVMQL AAKTVGKLAL
VSGTYTAEYV EFEVKRAFEW LGTDRHEGRK HAAVLVLREL AVSVPTYFFQ QVTPFFELIF
NAIHDPKPAI REGAVEALRA ALVVTAQRET VKQMHKSQWY KQCYDEVIDG FEEIHSKEKG
INRDDRIHGS LLVLNELLRC SNVQWERNYE ALMERLNGST QNENDILSLM PCLRTTIGSK
WAGYCTQNAT ASQHTLYPAH ESTVCRCLMQ DRLDDIYNDV MNQKISRNPH IQHALMMLLP
RLAAFNKEKF IRDHLKESLA YLLLILRSRE KDRYAAFTSI GFIAVAVEDA INPYLPKIME
MIKSLLPSKE TPSKKRTSLE PAVFVCITLL SHAVKQVIAS DVRDLLEPMF QTGLSPILTT
ALRELAHSIP SLQVDISQGL LRMLSQVLMQ KPLRHPGAPW TATSPSSTGD DVSSTVLALK
TLGTFNFDNN PLLQFVKRCA DHFLTSEQAE VRLEAVKTCS RLLRLTLNQS GPTVTTTVST
VLGKLLVVGI TDTDPDVRLW VLASLDDSFD VQLAQAENLS ALFIAMNDEM FEIRELAVRT
VGRLSTLNPA YVMPSLRKTL VQFLTELEHS GMGRNKEQAA RMLDHLVVTA PRLVRPYMEP
ILKVLVPKLK ESDPNPGVVL AVLRAIGDLA EVNGAEMQQW MSELSSILLE MLVDASSPEK
RGVALWVFGQ LVGSTGHVVK PYIQYPTLLD VLINFLKTEQ QPIIRREAIR VLGQLGALDP
YKHKMNIGQI DCQLDTLTSM ADTKNDVENT QDLTTSEMLV NMSPSTLEEF YPAIAITTLM
RIIREPTLSQ HHTMVVQAVT FIFKSLGIKC VPYISQVMPS FLNVVHTADI NFREFLFQQL
AVLIAIVKQH IRNYLDDIFI LIKEFWTVNS PLQSTLILLV EQIAMALGAE FKIYLPQLMP
PILRVLTHDS SKDRAVTVKL LLALQTFGNN LDNYLHLVLP PIVKLFYAND CPIAVNKVAL
ETVDLLADTL DFTDFASRIV HTLVRTLDQC PELRNTAMDT LCAVVMQLGK KYQIFIVLVQ
KVMTKHKIVN SRYDVLVDKI LTDSTAADGE DFLLMRMRHS RNKNREFSLT PSETIKKLNV
SASNLQKAWT ATRRVSKDDW LEWLRCFSIG LLKESPSPAL RSCWALAQTY AVLPRDLFNA
AFVSCWTELA ENYRMELIQT LHQALMVPDL PTEVTQTILN LAEFMEHIDK GPLPLDNKIL
GDTAMHCRAY AKALHYKEDE FHKSRNSSVF ESLISINNKL QQKEAAEGLL EYVMNHNQQD
LKVQIRWYEK LHNWDKALQL YQERLESDSA DVESTLGEMR CLEALGEWGQ LHEVATKQWT
NQTDDTKQRM SRMAAAAAWG LGQWESMQKY VSLIPKDTQD GAFYRAVLAI HDEQYNVAHQ
FIDSARDLLD TELTAMAGES YQRAYNAMVE VQKLAELEEV IQFKLVPERR AAIKAMWWER
LQGGQKIVED WQKIIQVHTL VVSPHDDMYT WLKYASLCRK SGSLMLCHKT LVMLMGTDPS
LTPDQPLPTT HPQVTFAYCK HLWVANKREE AYNQLQRFVQ TYLQPTTAAI INQEDEKQYE
SKKRLLARCY LKLGEWLESL QGINEHSIPA VLSYYAAATE HDPTWYKAWH AFAYTNYETV
LFYKHQQGSD SAPMEAAGNG ARNNLSSSQY ISQFTVPAVE GFFRSINLSD GNSLQDTLRL
LTLWFDYGQW PEVYDAVVEG IRLIEINTWL QVIPQLIARI DTPRALVGRC IHHLLIDIGK
THPQALVYPL TVASKSASHA RKTAANKILK SMCEHSPTLV QQAMMASDEL IRVAILWHEL
WHEGLEEASR LYFGERNVRG MFDTLEPLHA MLERGPQTLK ETSFNQAYGR DLIEAQEWCN
RYKTSRNVRD LNQAWDLYYH VFRRISRQLP QLTSLELQYV SPKLLICRDL ELAVPGSYSP
GQPIVRIASI HSSMQVITSK QRPRKLCIKG SNGKDYMFLL KGHEDLRQDE RVMQLFGLVN
TLLLHDPDTF RRNLTIQRYA VIPLSTNSGL IGWVPHCDTL HTLIRDYREK KKILLNIEHR
IMLRMAPDYD HLILMQKVEV FEHALEHTHG DDLARLLWLK SPSSEVWFDR RTNYTRSLAV
MSMVGYILGL GDRHPSNLML DRLSGKILHI DFGDCFEVAM TREKFPEKIP FRLTRMLINA
MEVTGIEGTY RRTCESVMSV LHRNKDSLMA VLEAFVYDPL LNWRLMDNTM PKGKRSDTQG
MSASSSQEHG DMLDSLTATL PKKGVPCSIE NGADNNQPEA LNKKALTIIT RVRDKLTGRD
FSHEETLSVR QQVDLLIQQA TNNENLCQCY IGWCPFW
//
