ID A0A1Y2GGM1_9FUNG Unreviewed; 2362 AA.
AC A0A1Y2GGM1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN ORFNames=BCR41DRAFT_423880 {ECO:0000313|EMBL:ORZ10331.1};
OS Lobosporangium transversale.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Lobosporangium.
OX NCBI_TaxID=64571 {ECO:0000313|EMBL:ORZ10331.1, ECO:0000313|Proteomes:UP000193648};
RN [1] {ECO:0000313|EMBL:ORZ10331.1, ECO:0000313|Proteomes:UP000193648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3116 {ECO:0000313|EMBL:ORZ10331.1,
RC ECO:0000313|Proteomes:UP000193648};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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:ORZ10331.1}.
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DR EMBL; MCFF01000031; ORZ10331.1; -; Genomic_DNA.
DR STRING; 64571.A0A1Y2GGM1; -.
DR InParanoid; A0A1Y2GGM1; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000193648; Unassembled WGS sequence.
DR GO; GO:0032991; C:protein-containing 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:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; 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 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; PF13513; HEAT_EZ; 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 SUPFAM; SSF48452; TPR-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:UP000193648};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU364109};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364109}.
FT DOMAIN 1247..1801
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 1975..2294
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2330..2362
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 2256..2276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2256..2275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2362 AA; 268407 MW; B94E83AFD62D81BB CRC64;
MSMATAPPSD ILSKLTNDLK SKNEEVRLQS AQALKDHVVV MSRELSGQDL KRFYGEVNSI
IWTLVQSVDN NDKLCGVMII DKLIGIEGEE NTTQETRFAN YLRQLFPADV KTMTVAARAL
GKLAQQGGTF TTEFVEFELK RAIEWLTGDR QEARRHASVL VLAELVRHAD VIVYPFVASI
LEHIWVAFRD PNQNIRVAAA DALSAVLVII ADRDSPYKST WYNRISEEAQ RGLRIASTES
IHGSLLIYRE LLLHAGMFMH ERYKSTGEIV FQYKDHRDGL VRRAVISLIP DLAAYNPQEF
ANVYLHRAMV HILSQLRKDK ERSLMKEKDR SNAFLAIGKI ALVAGADMGE FLDDILICIR
EGLRLKSKNR IQTDTPIFSC ISMLANAVGQ ALTKHMHELL ELMFATGLSE PLRQSLTDLS
NCIPPLLPII QERLLNMLSM ILSGHMYKPL GAPNGARTGL TSSPVRRDIQ SAEPKDVDSI
ILALTTLGSF NFQGHILNEF VRDCCIPFLE DDNPDIRRSA AKTCCQLFVR DPICFQTSAH
AVQVVGEVLE KLLTVGIADP DPEIRRTVME SLDERFDRHL AQAENVRSLF IALNDEIFAI
REHAITIIGR LSMHNPAYVM PSLRKTLIQL LTEIEYSGVS RNKEESARLL ALLVISSQRL
VKPYVESIIK VLLPKAKDQS AGVVSSILAA LGELARVGGE DLLPFMDQLM PLIIDTLQDQ
SSPTKRSAAL KTLGQLASNT GYVIEPYIKY PGLLDTLMNI LKTEQSGNIR KETIKLLGIL
GALDPYRHKQ MAIESVDDNQ ADKSQGSDVS LLMSGLGPSS EDYYPTVVIN ALLKILKDPS
LSQQYQPATQ AILNIFQALQ LKMVPFLPQI MPVYLSIMQS GTVLNLDFYF EKMGFLVMIV
KLHIRPYLPD LLQLVKDNWN HTPLQERIIG LVESIAVALD GEFKAYLPNL LQSFLAVFDT
DLTERHDASI KVLGAFVKFG SNIEEYMHLV IPVLVKTFEK PDAPINLRRA AINTIRELAK
KVNFSDYASR IIHPFARILA LPGPELRMPT MDALCCLVLQ LGQDYVNFIP MIKKVLIRTR
ISHAQYDHLV SQLLKREPLP LELPGLGDDR YVSISDVPQA ESGIRKLPVN QASLRRAWDT
QPRSTKDDWA DWIRRLCLEM LKETPSHALR ACADMANSYH PLARELFNAA FVSCWGELLD
QYQEELARAL VTALVAPNIS PEIIQILLNL AEFMEHDDKP LPIDIRTLGE YAAKSHAFAK
ALHYKELEFL TEPSTNAIEE LIGINNNLQQ PDAAAGILTH AQLHHDFELK EAWYERLQRW
EDALAAYERK QLENPNDLTL TNKRMRCLHA LGEWDQLSSL AQAKWGSAPP QDRRKMASFA
AAAAWGLGQW ELLDEYISAM QENSDRAFFK AILALHRNQF QEAEKYIDKT RNMLDTELTA
LVGESYNRAY ATVVRVQMMA ELEEIIAYKQ YHDQPDRQAT IRRTWMKRLK GCQRNVEVWQ
KLIKVHAIVV TPAQDMEMRI KFMNLCRKNG RLRLAENTMS TLMGPDTANM SFTAMTQVTP
PQIVYAKLKY MWATGVREHT LDCLRQFTER LASDLGLGTV EDAGIAMTGA NQLNGNVVDY
SRLLARCYLK QGEWQFALQD GWTHDSIEDI LTPYLYAKHL DKDWYKAWHT WALANFEVIT
FYEKNPPPNH SGRDPCLQYV IPSIMGFFKS IALSQGNSLQ DTLRLLTLWF KFGHRAEISA
ALSDGFSTVS IDTWLQVIPQ LIARIHAPSP NVQRLIHQLL TDVGKEHPQA LVYSLTVASK
SPSVVRKNAA LAIMEKMRVH SPLLVEQALL VSQELIRVAI LWHEMWHEGL EEASRLYFGD
RNINGMLALL EPLHMMLQRG PETQREIAFN QAFGRDLREA QECCIRYGQT QEINDLNQAW
DIYYQVFRRI AKQLQQLSTL DLPYVSPQLQ GAQDLELAIP GTYKSGEPII KISSFVPTLT
VMTSKQRPRR LTVKGSDGRD YQYLLKGHED LRQDERVMQL FGLVNTLLSI DPETFKRYLG
IQRYPVIPLS PNSGLIGWLP DTDTLHTLIR DYRESRKILL NIEHRIMLQM APDYDNLTLM
QKVEVFEYAL NNTGGQDLYK VLWLKSRNSE AWLDRRTNYT RSLAVMSMVG YILGLGDRHP
SNLMLDRNSG KIVHIDFGDC FEVAMHREKF PEQIPFRLTR MLTNAMEVSG IEGNFRNTCE
NVMRVLRENK ESLMAVLEAF VYDPLINWRI LTTSPRQPME NGQGGNQNAA NESVMDEQAR
NMRRALPSER ELVRDNMKME NQPEQLNQRA VSIINRVTNK LTGRDFKPDK PLDVPSQVEK
LIQQASSYEN LCQCWIGWCA FW
//
