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Conserved domains on  [gi|2092472343|gb|KAG9609085|]
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TOR1 phosphatidylinositol 3-kinase, partial [Aureobasidium melanogenum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FAT pfam02259
FAT domain; The FAT domain is named after FRAP, ATM and TRRAP.
 48-421 7.22e-115

FAT domain; The FAT domain is named after FRAP, ATM and TRRAP.


:

Pssm-ID: 396714 [Multi-domain]  Cd Length: 342  Bit Score: 348.96  E-value: 7.22e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343  48 WGMGQWELMDGYLSVMKLHSPDRSFFGAILSIHRNQFDDAQLHINKAREGLDTELSALLGESYTRAYSVIVRVQMLAELE 127
Cdd:pfam02259   9 WRLGQWDLMREYLSLMKKDSPDKAFFEAILALHRNQFDEAERYIEKARQLLDTELSALSGESYNRAYPLLVRLQQLAELE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343 128 EIIAYKQ-SSSDPHKQERMRLTWTKRLKGCQKNVEVWQRMLKVRALVISPPEN-------AEMYIKFASICRKAQRNGLA 199
Cdd:pfam02259  89 EIIQYKQkLGQSSEELKSLLQTWRNRLPGCQDDVEIWQDILTVRSLVLSPIEDvylggyhAEMWLKFANLARKSGRFSLA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343 200 EKSLNSLLGWQGSLMTPEgqertlhapypVQYAVYKYMWSNGYSSGALTGLRDFTERLridYEQRSLavtnpGTNGMNGM 279
Cdd:pfam02259 169 EKALLKLLGEDPEEWLPE-----------VVYAYAKYLWPTGEQQEALLKLREFLSCY---LQKNGE-----LLSGLEVI 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343 280 NGTNgvngtqfpaagvspqisekdvaqLADWQKLLARCYLKQGDWLSlQMRGEWDAHRVHEIRSSYKAATHYNQDWYKAW 359
Cdd:pfam02259 230 NPTN-----------------------LEEFTELLARCYLLKGKWQA-ALGQNWAEEKSEEILQAYLLATQFDPSWYKAW 285

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2092472343 360 HAWALANFEVVTALTANKDRgeadgMQRRYIHDYVVPAIQGFFKSIALSSSSSLQDTLRLLT 421
Cdd:pfam02259 286 HTWALFNFEVLRKEEQGKEE-----EGPEDLSRYVVPAVEGYLRSLSLSSENSLQDTLRLLT 342
FRB_dom pfam08771
FKBP12-rapamycin binding domain; The macrolide antibiotic rapamycin and the cytosol protein ...
 528-624 1.07e-57

FKBP12-rapamycin binding domain; The macrolide antibiotic rapamycin and the cytosol protein FKBP12 can form a complex which specifically inhibits the TORC1 complex, leading to growth arrest. The FKBP12-rapamycin complex interferes with TORC1 function by binding to the FKBP12-rapamycin binding domain (FRB) of the TOR proteins. This entry represents the FRB domain.


:

Pssm-ID: 462596  Cd Length: 98  Bit Score: 190.10  E-value: 1.07e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343 528 ELIRIAVLWHEQWHEGLEEASRLYFGDHDIDGMLRTLEPLHRMLDEGPETLREISFIQSFGRDLAEARDWCNNFKRTNEV 607
Cdd:pfam08771   1 ELIRVAILWHELWYEGLEEASRLYFGEKNIEGMLKILEPLHEMLEKGPETLREISFAQAFGRDLQEAREWLKRYRKTGDE 80

                          90
                  ....*....|....*..
gi 2092472343 608 GDLNQAWDLYYGVFKRI 624
Cdd:pfam08771  81 EDLNQAWDIYYSVFRRI 97
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
 666-702 4.88e-12

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd05169:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 279  Bit Score: 67.12  E-value: 4.88e-12
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2092472343 666 ILSFDPSSTVIQSKQRPRKLTVTGSDGGTYQYVLKGH 702
Cdd:cd05169     1 ISSFDPTLEVITSKQRPRKLTIVGSDGKEYKFLLKGH 37
 
Name Accession Description Interval E-value
FAT pfam02259
FAT domain; The FAT domain is named after FRAP, ATM and TRRAP.
 48-421 7.22e-115

FAT domain; The FAT domain is named after FRAP, ATM and TRRAP.


Pssm-ID: 396714 [Multi-domain]  Cd Length: 342  Bit Score: 348.96  E-value: 7.22e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343  48 WGMGQWELMDGYLSVMKLHSPDRSFFGAILSIHRNQFDDAQLHINKAREGLDTELSALLGESYTRAYSVIVRVQMLAELE 127
Cdd:pfam02259   9 WRLGQWDLMREYLSLMKKDSPDKAFFEAILALHRNQFDEAERYIEKARQLLDTELSALSGESYNRAYPLLVRLQQLAELE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343 128 EIIAYKQ-SSSDPHKQERMRLTWTKRLKGCQKNVEVWQRMLKVRALVISPPEN-------AEMYIKFASICRKAQRNGLA 199
Cdd:pfam02259  89 EIIQYKQkLGQSSEELKSLLQTWRNRLPGCQDDVEIWQDILTVRSLVLSPIEDvylggyhAEMWLKFANLARKSGRFSLA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343 200 EKSLNSLLGWQGSLMTPEgqertlhapypVQYAVYKYMWSNGYSSGALTGLRDFTERLridYEQRSLavtnpGTNGMNGM 279
Cdd:pfam02259 169 EKALLKLLGEDPEEWLPE-----------VVYAYAKYLWPTGEQQEALLKLREFLSCY---LQKNGE-----LLSGLEVI 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343 280 NGTNgvngtqfpaagvspqisekdvaqLADWQKLLARCYLKQGDWLSlQMRGEWDAHRVHEIRSSYKAATHYNQDWYKAW 359
Cdd:pfam02259 230 NPTN-----------------------LEEFTELLARCYLLKGKWQA-ALGQNWAEEKSEEILQAYLLATQFDPSWYKAW 285

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2092472343 360 HAWALANFEVVTALTANKDRgeadgMQRRYIHDYVVPAIQGFFKSIALSSSSSLQDTLRLLT 421
Cdd:pfam02259 286 HTWALFNFEVLRKEEQGKEE-----EGPEDLSRYVVPAVEGYLRSLSLSSENSLQDTLRLLT 342
TEL1 COG5032
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
1-702 1.97e-104

Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];


Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 350.62  E-value: 1.97e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343    1 FEVIMGKMRCLHALGEWEVLSSLAQEKWMHASSENRKSIAALAAAAAWGMGQWELMDGYLSVMKLHSPDRSFF--GAILS 78
Cdd:COG5032   1114 FAISFTKLRNVDALGKLELYSSLAEIDMFLSLHRRRKLLETLVATAYEQVGEWYKAQQLYEVAQRKARSKEFPfsLQYLY 1193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343   79 IHRNQFDDAQLHI-NKAREGLDTELSAL-LGESYTRAYSVIVRVQMLAELEEIIA--YKQSSSDPHKQER--MRLTWTKR 152
Cdd:COG5032   1194 WHINDIDCADKLQsVLAELSLVTGISELlLEESWRRALFSNIKDSLESELEEIIDgmYKSNEDFGALMLLslSAELWDKI 1273

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343  153 LKG---CQKNVEVWQRMLKVRALVISPPENAEMYIKFASICRKAQ-RNGLAEKSLNSLLGwqgslmtpEGQERT------ 222
Cdd:COG5032   1274 LEGrssCSKSIKLSLNIWLDLSIVVSPKDEPELFIKFVELCEASSiRSKLLEKNIQELLE--------KLEEIKsplgtl 1345

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343  223 -LHAPYPVQYAVYKYMWSngyssgaltglrdfTERLRIDYEQrslavtNPGTNGMNG--MNGTNGVNGTQFpaagVSPQI 299
Cdd:COG5032   1346 rDRLPPPWALLDLKRLLA--------------TWRQNAFLRI------NPELLPLLSslLNLQSSSLSKQL----VSRGS 1401

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343  300 SEKDVAQLADwQKLLARCYLKQGDWL-SLQMRgeWDAHRVHEIRSSYKAATHYNQDWYKAWHA-WALANFEVVtaltanK 377
Cdd:COG5032   1402 SESAISINSF-ASVARKHFLPDNQLKkIYQLS--NILISEAFLLLRYLLLCRLGRRELKAGLNvWNLTNLELF------S 1472

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343  378 DRGEADGMQRRYIHD--YVVPAIQGFFKSIALSSSSSLQDTLRLLTLWFNHGEHQEVTSAVTQGVTTVSIDT-WLEVIPQ 454
Cdd:COG5032   1473 DIQESEFFEWGKNLKllSIIPPIEEIFLSNALSCYLQVKDLLKKLNLFELLGSLLSAKDAAGSYYKNFHIFDlEISVIPF 1552

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343  455 LIARINQPNRLVKESIHHLLCEVGRAHPQALVYPLTVSIKSEDRDRSRAAKDIMTAMEQHSPNLCRQAAVVSHELIRIA- 533
Cdd:COG5032   1553 IPQLLSSLSLLDLNSAQSLLSKIGKEHPQALVFTLRSAIESTALSKESVALSLENKSRTHDPSLVKEALELSDENIRIAy 1632

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343  534 VLWHEQWHEGLEEASRLYFGDHD-IDGMLRTLEPLHRMLDEGPETLREISFIQSFGRDLAEARDWCNNFKRTNEVGDLNQ 612
Cdd:COG5032   1633 PLLHLLFEPILAQLLSRLSSENNkISVALLIDKPLHEERENFPSGLSLSSFQSSFLKELIKKSPRKIRKKFKIDISLLNL 1712

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343  613 AWDLYYGVFKRIARQLPQLANLELQYVSPKLKNVHD-LELALPGTYKSGKEIIRILSFDPSSTVIQS-KQRPRKLTVTGS 690
Cdd:COG5032   1713 SRKLYISVLRSIRKRLKRLLELRLKKVSPKLLLFHAfLEIKLPGQYLLDKPFVLIERFEPEVSVVKShLQRPRRLTIRGS 1792

                          730
                   ....*....|..
gi 2092472343  691 DGGTYQYVLKGH 702
Cdd:COG5032   1793 DGKLYSFIVKGG 1804
FRB_dom pfam08771
FKBP12-rapamycin binding domain; The macrolide antibiotic rapamycin and the cytosol protein ...
 528-624 1.07e-57

FKBP12-rapamycin binding domain; The macrolide antibiotic rapamycin and the cytosol protein FKBP12 can form a complex which specifically inhibits the TORC1 complex, leading to growth arrest. The FKBP12-rapamycin complex interferes with TORC1 function by binding to the FKBP12-rapamycin binding domain (FRB) of the TOR proteins. This entry represents the FRB domain.


Pssm-ID: 462596  Cd Length: 98  Bit Score: 190.10  E-value: 1.07e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343 528 ELIRIAVLWHEQWHEGLEEASRLYFGDHDIDGMLRTLEPLHRMLDEGPETLREISFIQSFGRDLAEARDWCNNFKRTNEV 607
Cdd:pfam08771   1 ELIRVAILWHELWYEGLEEASRLYFGEKNIEGMLKILEPLHEMLEKGPETLREISFAQAFGRDLQEAREWLKRYRKTGDE 80

                          90
                  ....*....|....*..
gi 2092472343 608 GDLNQAWDLYYGVFKRI 624
Cdd:pfam08771  81 EDLNQAWDIYYSVFRRI 97
PIKKc_TOR cd05169
Catalytic domain of Target of Rapamycin; TOR contains a rapamycin binding domain, a catalytic ...
 666-702 4.88e-12

Catalytic domain of Target of Rapamycin; TOR contains a rapamycin binding domain, a catalytic domain, and a FATC (FRAP, ATM and TRRAP, C-terminal) domain at the C-terminus. It is also called FRAP (FK506 binding protein 12-rapamycin associated protein). TOR is a central component of the eukaryotic growth regulatory network. It controls the expression of many genes transcribed by all three RNA polymerases. It associates with other proteins to form two distinct complexes, TORC1 and TORC2. TORC1 is involved in diverse growth-related functions including protein synthesis, nutrient use and transport, autophagy and stress responses. TORC2 is involved in organizing cytoskeletal structures. TOR is a member of the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K, and their large molecular weight (240-470 kDa). The TOR catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270713 [Multi-domain]  Cd Length: 279  Bit Score: 67.12  E-value: 4.88e-12
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2092472343 666 ILSFDPSSTVIQSKQRPRKLTVTGSDGGTYQYVLKGH 702
Cdd:cd05169     1 ISSFDPTLEVITSKQRPRKLTIVGSDGKEYKFLLKGH 37
 
Name Accession Description Interval E-value
FAT pfam02259
FAT domain; The FAT domain is named after FRAP, ATM and TRRAP.
 48-421 7.22e-115

FAT domain; The FAT domain is named after FRAP, ATM and TRRAP.


Pssm-ID: 396714 [Multi-domain]  Cd Length: 342  Bit Score: 348.96  E-value: 7.22e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343  48 WGMGQWELMDGYLSVMKLHSPDRSFFGAILSIHRNQFDDAQLHINKAREGLDTELSALLGESYTRAYSVIVRVQMLAELE 127
Cdd:pfam02259   9 WRLGQWDLMREYLSLMKKDSPDKAFFEAILALHRNQFDEAERYIEKARQLLDTELSALSGESYNRAYPLLVRLQQLAELE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343 128 EIIAYKQ-SSSDPHKQERMRLTWTKRLKGCQKNVEVWQRMLKVRALVISPPEN-------AEMYIKFASICRKAQRNGLA 199
Cdd:pfam02259  89 EIIQYKQkLGQSSEELKSLLQTWRNRLPGCQDDVEIWQDILTVRSLVLSPIEDvylggyhAEMWLKFANLARKSGRFSLA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343 200 EKSLNSLLGWQGSLMTPEgqertlhapypVQYAVYKYMWSNGYSSGALTGLRDFTERLridYEQRSLavtnpGTNGMNGM 279
Cdd:pfam02259 169 EKALLKLLGEDPEEWLPE-----------VVYAYAKYLWPTGEQQEALLKLREFLSCY---LQKNGE-----LLSGLEVI 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343 280 NGTNgvngtqfpaagvspqisekdvaqLADWQKLLARCYLKQGDWLSlQMRGEWDAHRVHEIRSSYKAATHYNQDWYKAW 359
Cdd:pfam02259 230 NPTN-----------------------LEEFTELLARCYLLKGKWQA-ALGQNWAEEKSEEILQAYLLATQFDPSWYKAW 285

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2092472343 360 HAWALANFEVVTALTANKDRgeadgMQRRYIHDYVVPAIQGFFKSIALSSSSSLQDTLRLLT 421
Cdd:pfam02259 286 HTWALFNFEVLRKEEQGKEE-----EGPEDLSRYVVPAVEGYLRSLSLSSENSLQDTLRLLT 342
TEL1 COG5032
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
1-702 1.97e-104

Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];


Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 350.62  E-value: 1.97e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343    1 FEVIMGKMRCLHALGEWEVLSSLAQEKWMHASSENRKSIAALAAAAAWGMGQWELMDGYLSVMKLHSPDRSFF--GAILS 78
Cdd:COG5032   1114 FAISFTKLRNVDALGKLELYSSLAEIDMFLSLHRRRKLLETLVATAYEQVGEWYKAQQLYEVAQRKARSKEFPfsLQYLY 1193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343   79 IHRNQFDDAQLHI-NKAREGLDTELSAL-LGESYTRAYSVIVRVQMLAELEEIIA--YKQSSSDPHKQER--MRLTWTKR 152
Cdd:COG5032   1194 WHINDIDCADKLQsVLAELSLVTGISELlLEESWRRALFSNIKDSLESELEEIIDgmYKSNEDFGALMLLslSAELWDKI 1273

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343  153 LKG---CQKNVEVWQRMLKVRALVISPPENAEMYIKFASICRKAQ-RNGLAEKSLNSLLGwqgslmtpEGQERT------ 222
Cdd:COG5032   1274 LEGrssCSKSIKLSLNIWLDLSIVVSPKDEPELFIKFVELCEASSiRSKLLEKNIQELLE--------KLEEIKsplgtl 1345

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343  223 -LHAPYPVQYAVYKYMWSngyssgaltglrdfTERLRIDYEQrslavtNPGTNGMNG--MNGTNGVNGTQFpaagVSPQI 299
Cdd:COG5032   1346 rDRLPPPWALLDLKRLLA--------------TWRQNAFLRI------NPELLPLLSslLNLQSSSLSKQL----VSRGS 1401

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343  300 SEKDVAQLADwQKLLARCYLKQGDWL-SLQMRgeWDAHRVHEIRSSYKAATHYNQDWYKAWHA-WALANFEVVtaltanK 377
Cdd:COG5032   1402 SESAISINSF-ASVARKHFLPDNQLKkIYQLS--NILISEAFLLLRYLLLCRLGRRELKAGLNvWNLTNLELF------S 1472

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343  378 DRGEADGMQRRYIHD--YVVPAIQGFFKSIALSSSSSLQDTLRLLTLWFNHGEHQEVTSAVTQGVTTVSIDT-WLEVIPQ 454
Cdd:COG5032   1473 DIQESEFFEWGKNLKllSIIPPIEEIFLSNALSCYLQVKDLLKKLNLFELLGSLLSAKDAAGSYYKNFHIFDlEISVIPF 1552

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343  455 LIARINQPNRLVKESIHHLLCEVGRAHPQALVYPLTVSIKSEDRDRSRAAKDIMTAMEQHSPNLCRQAAVVSHELIRIA- 533
Cdd:COG5032   1553 IPQLLSSLSLLDLNSAQSLLSKIGKEHPQALVFTLRSAIESTALSKESVALSLENKSRTHDPSLVKEALELSDENIRIAy 1632

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343  534 VLWHEQWHEGLEEASRLYFGDHD-IDGMLRTLEPLHRMLDEGPETLREISFIQSFGRDLAEARDWCNNFKRTNEVGDLNQ 612
Cdd:COG5032   1633 PLLHLLFEPILAQLLSRLSSENNkISVALLIDKPLHEERENFPSGLSLSSFQSSFLKELIKKSPRKIRKKFKIDISLLNL 1712

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343  613 AWDLYYGVFKRIARQLPQLANLELQYVSPKLKNVHD-LELALPGTYKSGKEIIRILSFDPSSTVIQS-KQRPRKLTVTGS 690
Cdd:COG5032   1713 SRKLYISVLRSIRKRLKRLLELRLKKVSPKLLLFHAfLEIKLPGQYLLDKPFVLIERFEPEVSVVKShLQRPRRLTIRGS 1792

                          730
                   ....*....|..
gi 2092472343  691 DGGTYQYVLKGH 702
Cdd:COG5032   1793 DGKLYSFIVKGG 1804
FRB_dom pfam08771
FKBP12-rapamycin binding domain; The macrolide antibiotic rapamycin and the cytosol protein ...
 528-624 1.07e-57

FKBP12-rapamycin binding domain; The macrolide antibiotic rapamycin and the cytosol protein FKBP12 can form a complex which specifically inhibits the TORC1 complex, leading to growth arrest. The FKBP12-rapamycin complex interferes with TORC1 function by binding to the FKBP12-rapamycin binding domain (FRB) of the TOR proteins. This entry represents the FRB domain.


Pssm-ID: 462596  Cd Length: 98  Bit Score: 190.10  E-value: 1.07e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092472343 528 ELIRIAVLWHEQWHEGLEEASRLYFGDHDIDGMLRTLEPLHRMLDEGPETLREISFIQSFGRDLAEARDWCNNFKRTNEV 607
Cdd:pfam08771   1 ELIRVAILWHELWYEGLEEASRLYFGEKNIEGMLKILEPLHEMLEKGPETLREISFAQAFGRDLQEAREWLKRYRKTGDE 80

                          90
                  ....*....|....*..
gi 2092472343 608 GDLNQAWDLYYGVFKRI 624
Cdd:pfam08771  81 EDLNQAWDIYYSVFRRI 97
PIKKc_TOR cd05169
Catalytic domain of Target of Rapamycin; TOR contains a rapamycin binding domain, a catalytic ...
 666-702 4.88e-12

Catalytic domain of Target of Rapamycin; TOR contains a rapamycin binding domain, a catalytic domain, and a FATC (FRAP, ATM and TRRAP, C-terminal) domain at the C-terminus. It is also called FRAP (FK506 binding protein 12-rapamycin associated protein). TOR is a central component of the eukaryotic growth regulatory network. It controls the expression of many genes transcribed by all three RNA polymerases. It associates with other proteins to form two distinct complexes, TORC1 and TORC2. TORC1 is involved in diverse growth-related functions including protein synthesis, nutrient use and transport, autophagy and stress responses. TORC2 is involved in organizing cytoskeletal structures. TOR is a member of the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K, and their large molecular weight (240-470 kDa). The TOR catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270713 [Multi-domain]  Cd Length: 279  Bit Score: 67.12  E-value: 4.88e-12
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2092472343 666 ILSFDPSSTVIQSKQRPRKLTVTGSDGGTYQYVLKGH 702
Cdd:cd05169     1 ISSFDPTLEVITSKQRPRKLTIVGSDGKEYKFLLKGH 37
PIKKc cd05164
Catalytic domain of Phosphoinositide 3-kinase-related protein kinases; PIKK subfamily members ...
 666-702 1.61e-07

Catalytic domain of Phosphoinositide 3-kinase-related protein kinases; PIKK subfamily members include ATM (Ataxia telangiectasia mutated), ATR (Ataxia telangiectasia and Rad3-related), TOR (Target of rapamycin), SMG-1 (Suppressor of morphogenetic effect on genitalia-1), and DNA-PK (DNA-dependent protein kinase). PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K, and their large molecular weight (240-470 kDa). They show strong preference for phosphorylating serine/threonine residues followed by a glutamine and are also referred to as (S/T)-Q-directed kinases. They all contain a FATC (FRAP, ATM and TRRAP, C-terminal) domain. PIKKs have diverse functions including cell-cycle checkpoints, genome surveillance, mRNA surveillance, and translation control. The PIKK catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270708 [Multi-domain]  Cd Length: 222  Bit Score: 52.66  E-value: 1.61e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2092472343 666 ILSFDPSSTVIQSKQRPRKLTVTGSDGGTYQYVLKGH 702
Cdd:cd05164     1 IASFDPRVRILASLQKPKKITILGSDGKEYPFLVKGD 37
PIKKc_DNA-PK cd05172
Catalytic domain of DNA-dependent protein kinase; DNA-PK is comprised of a regulatory subunit, ...
 666-701 2.10e-06

Catalytic domain of DNA-dependent protein kinase; DNA-PK is comprised of a regulatory subunit, containing the Ku70/80 subunit, and a catalytic subunit, which contains a NUC194 domain of unknown function, a FAT (FRAP, ATM and TRRAP) domain, a catalytic domain, and a FATC domain at the C-terminus. It is part of a multi-component system involved in non-homologous end joining (NHEJ), a process of repairing double strand breaks (DSBs) by joining together two free DNA ends of little homology. DNA-PK functions as a molecular sensor for DNA damage that enhances the signal via phosphorylation of downstream targets. It may also act as a protein scaffold that aids the localization of DNA repair proteins to the site of DNA damage. DNA-PK also plays a role in the maintenance of telomeric stability and the prevention of chromosomal end fusion. DNA-PK is a member of the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K, and their large molecular weight (240-470 kDa). The DNA-PK catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270716 [Multi-domain]  Cd Length: 235  Bit Score: 49.50  E-value: 2.10e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2092472343 666 ILSFDPSSTVIQSKQRPRKLTVTGSDGGTYQYVLKG 701
Cdd:cd05172     1 IVGFDPRVLVLSSKRRPKRITIRGSDEKEYKFLVKG 36
PIKKc_SMG1 cd05170
Catalytic domain of Suppressor of Morphogenetic effect on Genitalia-1; SMG-1 plays a critical ...
 666-702 4.29e-06

Catalytic domain of Suppressor of Morphogenetic effect on Genitalia-1; SMG-1 plays a critical role in the mRNA surveillance mechanism known as non-sense mediated mRNA decay (NMD). NMD protects the cells from the accumulation of aberrant mRNAs with premature termination codons (PTCs) generated by genome mutations and by errors during transcription and splicing. SMG-1 phosphorylates Upf1, another central component of NMD, at the C-terminus upon recognition of PTCs. The phosphorylation/dephosphorylation cycle of Upf1 is essential for promoting NMD. In addition to its catalytic domain, SMG-1 contains a FATC (FRAP, ATM and TRRAP, C-terminal) domain at the C-terminus. SMG-1 is a member of the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K, and their large molecular weight (240-470 kDa). The SMG-1 catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270714  Cd Length: 304  Bit Score: 49.18  E-value: 4.29e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2092472343 666 ILSFDPSSTVIQSKQRPRKLTVTGSDGGTYQYVLKGH 702
Cdd:cd05170     1 IQSVGSTVTVLPTKTKPKKLVFLGSDGKRYPYLFKGL 37
PIKKc_ATR cd00892
Catalytic domain of Ataxia telangiectasia and Rad3-related proteins; ATR is also referred to ...
 666-700 3.38e-05

Catalytic domain of Ataxia telangiectasia and Rad3-related proteins; ATR is also referred to as Mei-41 (Drosophila), Esr1/Mec1p (Saccharomyces cerevisiae), Rad3 (Schizosaccharomyces pombe), and FRAP-related protein (human). ATR contains a UME domain of unknown function, a FAT (FRAP, ATM and TRRAP) domain, a catalytic domain, and a FATC domain at the C-terminus. Together with its downstream effector kinase, Chk1, ATR plays a central role in regulating the replication checkpoint. ATR stabilizes replication forks by promoting the association of DNA polymerases with the fork. Preventing fork collapse is essential in preserving genomic integrity. ATR also plays a role in normal cell growth and in response to DNA damage. ATR is a member of the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K, and their large molecular weight (240-470 kDa). The ATR catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270625 [Multi-domain]  Cd Length: 237  Bit Score: 45.96  E-value: 3.38e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2092472343 666 ILSFDPSSTVIQSKQRPRKLTVTGSDGGTYQYVLK 700
Cdd:cd00892     1 ISGFEDEVEIMPSLQKPKKITLVGSDGKKYPFLCK 35
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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