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Conserved domains on  [gi|336370491|gb|EGN98831|]
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hypothetical protein SERLA73DRAFT_181504 [Serpula lacrymans var. lacrymans S7.3]

Protein Classification

GTR/RAG family Ras-related GTP-binding protein( domain architecture ID 10183657)

GTR/RAG family Ras-related GTP-binding protein similar to Homo sapiens RagC, a GTPase involved in activation of the TORC1 signaling pathway, which promotes growth and represses autophagy in nutrient-rich conditions

CATH:  3.40.50.300
EC:  3.6.5.-
Gene Ontology:  GO:0005525|GO:0003924
PubMed:  11073942|16732272|28788436

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RagC_like cd11385
Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins C and ...
 21-191 6.26e-83

Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins C and D; RagC and RagD are closely related Rag GTPases (ras-related GTP-binding protein C and D) that constitute a unique subgroup of the Ras superfamily, and are functional homologs of Saccharomyces cerevisiae Gtr2. These domains form heterodimers with RagA or RagB, and similarly, Gtr2 dimerizes with Gtr1 in order to function. They play an essential role in regulating amino acid-induced target of rapamycin complex 1 (TORC1) kinase signaling, exocytic cargo sorting at endosomes, and epigenetic control of gene expression. In response to amino acids, the Rag GTPases guide the TORC1 complex to activate the platform containing Rheb proto-oncogene by driving the relocalization of mTORC1 from discrete locations in the cytoplasm to a late endosomal and/or lysosomal compartment that is Rheb-enriched and contains Rab-7.


:

Pssm-ID: 206745 [Multi-domain]  Cd Length: 175  Bit Score: 250.60  E-value: 6.26e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336370491  21 KILLMGTKRSGKTSIQQVLFNNLPPKQTFYIEPTKRITKHA-----FDTFIPLEIWDCPGDVTvDSLDTPLSEF--TTIL 93
Cdd:cd11385    1 RILLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKITKDDisnssFVNFQIWDFPGQLDPFD-PTLDPEMIFSgcGALV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336370491  94 FVIDIRALYQEPISKLVEFMVAAHQVNPDINFEVFLHKAEKLMEDDKIEYYRLIHEGVMDRLADESPeyEQVPLNFHLTS 173
Cdd:cd11385   80 FVIDAQDDYDEAIARLVETVTKAYKVNPNINFEVFIHKVDGLSEDHKIETQRDIQQRVTDELADAGL--EDVQISFYLTS 157

                        170
                 ....*....|....*...
gi 336370491 174 VYDHSLQDAFSHVLHKLV 191
Cdd:cd11385  158 IYDHSIFEAFSKVVQKLI 175
 
Name Accession Description Interval E-value
RagC_like cd11385
Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins C and ...
 21-191 6.26e-83

Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins C and D; RagC and RagD are closely related Rag GTPases (ras-related GTP-binding protein C and D) that constitute a unique subgroup of the Ras superfamily, and are functional homologs of Saccharomyces cerevisiae Gtr2. These domains form heterodimers with RagA or RagB, and similarly, Gtr2 dimerizes with Gtr1 in order to function. They play an essential role in regulating amino acid-induced target of rapamycin complex 1 (TORC1) kinase signaling, exocytic cargo sorting at endosomes, and epigenetic control of gene expression. In response to amino acids, the Rag GTPases guide the TORC1 complex to activate the platform containing Rheb proto-oncogene by driving the relocalization of mTORC1 from discrete locations in the cytoplasm to a late endosomal and/or lysosomal compartment that is Rheb-enriched and contains Rab-7.


Pssm-ID: 206745 [Multi-domain]  Cd Length: 175  Bit Score: 250.60  E-value: 6.26e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336370491  21 KILLMGTKRSGKTSIQQVLFNNLPPKQTFYIEPTKRITKHA-----FDTFIPLEIWDCPGDVTvDSLDTPLSEF--TTIL 93
Cdd:cd11385    1 RILLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKITKDDisnssFVNFQIWDFPGQLDPFD-PTLDPEMIFSgcGALV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336370491  94 FVIDIRALYQEPISKLVEFMVAAHQVNPDINFEVFLHKAEKLMEDDKIEYYRLIHEGVMDRLADESPeyEQVPLNFHLTS 173
Cdd:cd11385   80 FVIDAQDDYDEAIARLVETVTKAYKVNPNINFEVFIHKVDGLSEDHKIETQRDIQQRVTDELADAGL--EDVQISFYLTS 157

                        170
                 ....*....|....*...
gi 336370491 174 VYDHSLQDAFSHVLHKLV 191
Cdd:cd11385  158 IYDHSIFEAFSKVVQKLI 175
Gtr1_RagA pfam04670
Gtr1/RagA G protein conserved region; GTR1 was first identified in S. cerevisiae as a ...
 21-243 3.49e-64

Gtr1/RagA G protein conserved region; GTR1 was first identified in S. cerevisiae as a suppressor of a mutation in RCC1. Biochemical analysis revealed that Gtr1 is in fact a G protein of the Ras family. The RagA/B proteins are the human homologs of Gtr1. Included in this family is the human Rag C, a novel protein that has been shown to interact with RagA/B.


Pssm-ID: 398377 [Multi-domain]  Cd Length: 231  Bit Score: 204.74  E-value: 3.49e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336370491   21 KILLMGTKRSGKTSIQQVLFNNLPPKQTFYIEPTKRITKHA--FDTFIPLEIWDCPG-DVTVDSLDTPLSE--FTT---I 92
Cdd:pfam04670   1 KVLLMGLSGSGKSSMRSVIFSNYSPRDTLRLGATIDVEHSHvrFLGNLVLNLWDCGGqDDFFDNYLTFQKEhiFSNvgvL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336370491   93 LFVIDIRA-LYQEPISKLVEFMVAAHQVNPDINFEVFLHKAEKLMEDDKIEYYRLIHEGVMDRLADESPEyeqVPLNFHL 171
Cdd:pfam04670  81 IYVFDVQSrEYEEDLARLKETIEALYQYSPDAKVFVLIHKMDLIQEDHREEIFRDRKQEIREESEDLGLE---LDLSFFL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 336370491  172 TSVYDHSLQDAFSHVLHKLVDSLSFLEDLLNIFCSNTSSPKAFLFDTTSRLYVATD-ASPVDQA-THNLCCDYL 243
Cdd:pfam04670 158 TSIWDESLYKAWSSIVQKLIPNLPTLENLLKVFCSNSDADEVFLFERTTFLVIATDsRSPVDDMqRYEKCSDII 231
 
Name Accession Description Interval E-value
RagC_like cd11385
Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins C and ...
 21-191 6.26e-83

Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins C and D; RagC and RagD are closely related Rag GTPases (ras-related GTP-binding protein C and D) that constitute a unique subgroup of the Ras superfamily, and are functional homologs of Saccharomyces cerevisiae Gtr2. These domains form heterodimers with RagA or RagB, and similarly, Gtr2 dimerizes with Gtr1 in order to function. They play an essential role in regulating amino acid-induced target of rapamycin complex 1 (TORC1) kinase signaling, exocytic cargo sorting at endosomes, and epigenetic control of gene expression. In response to amino acids, the Rag GTPases guide the TORC1 complex to activate the platform containing Rheb proto-oncogene by driving the relocalization of mTORC1 from discrete locations in the cytoplasm to a late endosomal and/or lysosomal compartment that is Rheb-enriched and contains Rab-7.


Pssm-ID: 206745 [Multi-domain]  Cd Length: 175  Bit Score: 250.60  E-value: 6.26e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336370491  21 KILLMGTKRSGKTSIQQVLFNNLPPKQTFYIEPTKRITKHA-----FDTFIPLEIWDCPGDVTvDSLDTPLSEF--TTIL 93
Cdd:cd11385    1 RILLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKITKDDisnssFVNFQIWDFPGQLDPFD-PTLDPEMIFSgcGALV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336370491  94 FVIDIRALYQEPISKLVEFMVAAHQVNPDINFEVFLHKAEKLMEDDKIEYYRLIHEGVMDRLADESPeyEQVPLNFHLTS 173
Cdd:cd11385   80 FVIDAQDDYDEAIARLVETVTKAYKVNPNINFEVFIHKVDGLSEDHKIETQRDIQQRVTDELADAGL--EDVQISFYLTS 157

                        170
                 ....*....|....*...
gi 336370491 174 VYDHSLQDAFSHVLHKLV 191
Cdd:cd11385  158 IYDHSIFEAFSKVVQKLI 175
Gtr1_RagA pfam04670
Gtr1/RagA G protein conserved region; GTR1 was first identified in S. cerevisiae as a ...
 21-243 3.49e-64

Gtr1/RagA G protein conserved region; GTR1 was first identified in S. cerevisiae as a suppressor of a mutation in RCC1. Biochemical analysis revealed that Gtr1 is in fact a G protein of the Ras family. The RagA/B proteins are the human homologs of Gtr1. Included in this family is the human Rag C, a novel protein that has been shown to interact with RagA/B.


Pssm-ID: 398377 [Multi-domain]  Cd Length: 231  Bit Score: 204.74  E-value: 3.49e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336370491   21 KILLMGTKRSGKTSIQQVLFNNLPPKQTFYIEPTKRITKHA--FDTFIPLEIWDCPG-DVTVDSLDTPLSE--FTT---I 92
Cdd:pfam04670   1 KVLLMGLSGSGKSSMRSVIFSNYSPRDTLRLGATIDVEHSHvrFLGNLVLNLWDCGGqDDFFDNYLTFQKEhiFSNvgvL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336370491   93 LFVIDIRA-LYQEPISKLVEFMVAAHQVNPDINFEVFLHKAEKLMEDDKIEYYRLIHEGVMDRLADESPEyeqVPLNFHL 171
Cdd:pfam04670  81 IYVFDVQSrEYEEDLARLKETIEALYQYSPDAKVFVLIHKMDLIQEDHREEIFRDRKQEIREESEDLGLE---LDLSFFL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 336370491  172 TSVYDHSLQDAFSHVLHKLVDSLSFLEDLLNIFCSNTSSPKAFLFDTTSRLYVATD-ASPVDQA-THNLCCDYL 243
Cdd:pfam04670 158 TSIWDESLYKAWSSIVQKLIPNLPTLENLLKVFCSNSDADEVFLFERTTFLVIATDsRSPVDDMqRYEKCSDII 231
Rag cd09915
Rag GTPase subfamily of Ras-related GTPases; Rag GTPases (ras-related GTP-binding proteins) ...
 21-191 1.14e-34

Rag GTPase subfamily of Ras-related GTPases; Rag GTPases (ras-related GTP-binding proteins) constitute a unique subgroup of the Ras superfamily, playing an essential role in regulating amino acid-induced target of rapamycin complex 1 (TORC1) kinase signaling, exocytic cargo sorting at endosomes, and epigenetic control of gene expression. This subfamily consists of RagA and RagB as well as RagC and RagD that are closely related. Saccharomyces cerevisiae encodes single orthologs of metazoan RagA/B and RagC/D, Gtr1 and Gtr2, respectively. Dimer formation is important for their cellular function; these domains form heterodimers, as RagA or RagB dimerizes with RagC or RagD, and similarly, Gtr1 dimerizes with Gtr2. In response to amino acids, the Rag GTPases guide the TORC1 complex to activate the platform containing Rheb proto-oncogene by driving the relocalization of mTORC1 from discrete locations in the cytoplasm to a late endosomal and/or lysosomal compartment that is Rheb-enriched and contains Rab-7.


Pssm-ID: 206742 [Multi-domain]  Cd Length: 175  Bit Score: 126.14  E-value: 1.14e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336370491  21 KILLMGTKRSGKTSIQQVLFNNLPPKQTFYIEPTKRITKHAFDT--FIPLEIWDCPG-----DVTVDSlDTPLSEFTTIL 93
Cdd:cd09915    1 KLLL*GRRRSGKSSIRKVVFHNYSPFDTLRLESTIDVEHSHLSFlgN*TLNLWDCPGqdvffEPTKDK-EHIFQ*VGALI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336370491  94 FVIDIRALYQEPISKLVEFMVAAHQVNPDINFEVFLHKAEKLMEDDKIEYYRLIHEgvmdRLADESPEY--EQVPLNFHL 171
Cdd:cd09915   80 YVIDVQDEYLKAITILAKALKQAYKVNPDANIEVLIHKVDGLSLDKKEELQRDI*Q----RLSETLSEFglEFPNLSFYL 155

                        170       180
                 ....*....|....*....|
gi 336370491 172 TSVYDHSLQDAFSHVLHKLV 191
Cdd:cd09915  156 TSIWDHSIYEAFSQIVQKLI 175
RagA_like cd11384
Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins A and ...
 21-234 1.16e-12

Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins A and B; RagA and RagB are closely related Rag GTPases (ras-related GTP-binding protein A and B) that constitute a unique subgroup of the Ras superfamily, and are functional homologs of Saccharomyces cerevisiae Gtr1. These domains function by forming heterodimers with RagC or RagD, and similarly, Gtr1 dimerizes with Gtr2, through the carboxy-terminal segments. They play an essential role in regulating amino acid-induced target of rapamycin complex 1 (TORC1) kinase signaling, exocytic cargo sorting at endosomes, and epigenetic control of gene expression. In response to amino acids, the Rag GTPases guide the TORC1 complex to activate the platform containing Rheb proto-oncogene by driving the relocalization of mTORC1 from discrete locations in the cytoplasm to a late endosomal and/or lysosomal compartment that is Rheb-enriched and contains Rab-7.


Pssm-ID: 206744  Cd Length: 286  Bit Score: 67.62  E-value: 1.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336370491  21 KILLMGTKRSGKTSIQQVLFNNLPPKQTFYIEPTKRItKHAFDTFI---PLEIWDCPG-DVTVDSL-----DTPLSEFTT 91
Cdd:cd11384    1 KVLLMGKSGSGKTSMRSIIFANYLARDTRRLGATIDV-EHSHVRFLgnlVLNLWDCGGqDAFMENYftsqrDHIFRNVEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336370491  92 ILFVIDIRAlyQEPISKLVEF---MVAAHQVNPDINFEVFLHKAEKLMEDDKIEYYRLihegvmdRLADESPEYEQVPLN 168
Cdd:cd11384   80 LIYVFDVES--RELEKDLTYFrscLEALRQNSPDAKVFVLIHKMDLVQEDEREAVFER-------KEKELRRLSEPLEVT 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 336370491 169 FHLTSVYDHSLQDAFSHVLHKLVDSLSFLEDLLNIFCSNTSSPKAFLFDTTSRLYVATDASPVDQA 234
Cdd:cd11384  151 CFPTSIWDETLYKAWSSIVYSLIPNIQVLESNLKKFADICEADEVVLFERATFLVISHSSRKEASA 216
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 23-149 3.65e-06

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 46.68  E-value: 3.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336370491  23 LLMGTKRSGKTSIQQVLFNNLPPKQTFYIEPTKRITKHAF---DTFIPLEIWDCPGDVTVDSLDTPLSEFTT------IL 93
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYVKeldKGKVKLVLVDTPGLDEFGGLGREELARLLlrgadlIL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 336370491  94 FVIDIRalyQEPISKLVEFMVAAHQVNPDINFEVFLHKAEKLMEDDKIEYYRLIHE 149
Cdd:cd00882   81 LVVDST---DRESEEDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEEL 133
 
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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