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Conserved domains on  [gi|339469074|gb|EGP84174|]
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hypothetical protein MYCGRDRAFT_49226 [Zymoseptoria tritici IPO323]

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
SCOP:  4005007

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 ...
 4-173 2.15e-87

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: 259.46  E-value: 2.15e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339469074   4 YTDNHHRSGKSSIQKVIFEKYSPAETLYLEPTTKIETATMD--SFMTFEALELPSTTLTAPlSTHDS--LFATAGSLIWV 79
Cdd:cd11385    3 LLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKITKDDISnsSFVNFQIWDFPGQLDPFD-PTLDPemIFSGCGALVFV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339469074  80 LDMQDEYFASISLLIQTAVHLLQYHPRINFEVFIHKTDGLSEEYKYDTFRDVRQRVTDELADAGYGDRGIAFYQTSIFDH 159
Cdd:cd11385   82 IDAQDDYDEAIARLVETVTKAYKVNPNINFEVFIHKVDGLSEDHKIETQRDIQQRVTDELADAGLEDVQISFYLTSIYDH 161

                        170
                 ....*....|....
gi 339469074 160 SVYEAMSKVVQKLV 173
Cdd:cd11385  162 SIFEAFSKVVQKLI 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 ...
 4-173 2.15e-87

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: 259.46  E-value: 2.15e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339469074   4 YTDNHHRSGKSSIQKVIFEKYSPAETLYLEPTTKIETATMD--SFMTFEALELPSTTLTAPlSTHDS--LFATAGSLIWV 79
Cdd:cd11385    3 LLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKITKDDISnsSFVNFQIWDFPGQLDPFD-PTLDPemIFSGCGALVFV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339469074  80 LDMQDEYFASISLLIQTAVHLLQYHPRINFEVFIHKTDGLSEEYKYDTFRDVRQRVTDELADAGYGDRGIAFYQTSIFDH 159
Cdd:cd11385   82 IDAQDDYDEAIARLVETVTKAYKVNPNINFEVFIHKVDGLSEDHKIETQRDIQQRVTDELADAGLEDVQISFYLTSIYDH 161

                        170
                 ....*....|....
gi 339469074 160 SVYEAMSKVVQKLV 173
Cdd:cd11385  162 SIFEAFSKVVQKLI 175
Gtr1_RagA pfam04670
Gtr1/RagA G protein conserved region; GTR1 was first identified in S. cerevisiae as a ...
 8-224 7.98e-69

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: 213.98  E-value: 7.98e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339469074    8 HHRSGKSSIQKVIFEKYSPAETLYLEPTTKIETATMD--SFMTFEALELPSTT--LTAPLSTH-DSLFATAGSLIWVLDM 82
Cdd:pfam04670   7 LSGSGKSSMRSVIFSNYSPRDTLRLGATIDVEHSHVRflGNLVLNLWDCGGQDdfFDNYLTFQkEHIFSNVGVLIYVFDV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339469074   83 Q-DEYFASISLLIQTAVHLLQYHPRINFEVFIHKTDGLSEEYKYDTFRDVRQRVTDELADAGYGDRgIAFYQTSIFDHSV 161
Cdd:pfam04670  87 QsREYEEDLARLKETIEALYQYSPDAKVFVLIHKMDLIQEDHREEIFRDRKQEIREESEDLGLELD-LSFFLTSIWDESL 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339469074  162 YEAMSKVVQKLVPQLPAMEALLNKLCSACRIQKAYLFDTVSKIYLATDASPTF--LKDYEACADY 224
Cdd:pfam04670 166 YKAWSSIVQKLIPNLPTLENLLKVFCSNSDADEVFLFERTTFLVIATDSRSPVddMQRYEKCSDI 230
 
Name Accession Description Interval E-value
RagC_like cd11385
Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins C and ...
 4-173 2.15e-87

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: 259.46  E-value: 2.15e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339469074   4 YTDNHHRSGKSSIQKVIFEKYSPAETLYLEPTTKIETATMD--SFMTFEALELPSTTLTAPlSTHDS--LFATAGSLIWV 79
Cdd:cd11385    3 LLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKITKDDISnsSFVNFQIWDFPGQLDPFD-PTLDPemIFSGCGALVFV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339469074  80 LDMQDEYFASISLLIQTAVHLLQYHPRINFEVFIHKTDGLSEEYKYDTFRDVRQRVTDELADAGYGDRGIAFYQTSIFDH 159
Cdd:cd11385   82 IDAQDDYDEAIARLVETVTKAYKVNPNINFEVFIHKVDGLSEDHKIETQRDIQQRVTDELADAGLEDVQISFYLTSIYDH 161

                        170
                 ....*....|....
gi 339469074 160 SVYEAMSKVVQKLV 173
Cdd:cd11385  162 SIFEAFSKVVQKLI 175
Gtr1_RagA pfam04670
Gtr1/RagA G protein conserved region; GTR1 was first identified in S. cerevisiae as a ...
 8-224 7.98e-69

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: 213.98  E-value: 7.98e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339469074    8 HHRSGKSSIQKVIFEKYSPAETLYLEPTTKIETATMD--SFMTFEALELPSTT--LTAPLSTH-DSLFATAGSLIWVLDM 82
Cdd:pfam04670   7 LSGSGKSSMRSVIFSNYSPRDTLRLGATIDVEHSHVRflGNLVLNLWDCGGQDdfFDNYLTFQkEHIFSNVGVLIYVFDV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339469074   83 Q-DEYFASISLLIQTAVHLLQYHPRINFEVFIHKTDGLSEEYKYDTFRDVRQRVTDELADAGYGDRgIAFYQTSIFDHSV 161
Cdd:pfam04670  87 QsREYEEDLARLKETIEALYQYSPDAKVFVLIHKMDLIQEDHREEIFRDRKQEIREESEDLGLELD-LSFFLTSIWDESL 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339469074  162 YEAMSKVVQKLVPQLPAMEALLNKLCSACRIQKAYLFDTVSKIYLATDASPTF--LKDYEACADY 224
Cdd:pfam04670 166 YKAWSSIVQKLIPNLPTLENLLKVFCSNSDADEVFLFERTTFLVIATDSRSPVddMQRYEKCSDI 230
Rag cd09915
Rag GTPase subfamily of Ras-related GTPases; Rag GTPases (ras-related GTP-binding proteins) ...
 10-173 3.66e-47

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: 156.57  E-value: 3.66e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339469074  10 RSGKSSIQKVIFEKYSPAETLYLEPTTKIETA--TMDSFMTFEALELPST-TLTAPLSTHDSLFATAGSLIWVLDMQDEY 86
Cdd:cd09915    9 RSGKSSIRKVVFHNYSPFDTLRLESTIDVEHShlSFLGN*TLNLWDCPGQdVFFEPTKDKEHIFQ*VGALIYVIDVQDEY 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339469074  87 FASISLLIQTAVHLLQYHPRINFEVFIHKTDGLSEEYKYDTFRDVRQRVTDELADAGYGDRGIAFYQTSIFDHSVYEAMS 166
Cdd:cd09915   89 LKAITILAKALKQAYKVNPDANIEVLIHKVDGLSLDKKEELQRDI*QRLSETLSEFGLEFPNLSFYLTSIWDHSIYEAFS 168


                 ....*..
gi 339469074 167 KVVQKLV 173
Cdd:cd09915  169 QIVQKLI 175
RagA_like cd11384
Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins A and ...
 11-198 1.29e-15

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: 75.71  E-value: 1.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339469074  11 SGKSSIQKVIFEKYSPAETLYLEPTTKIETATM----------------DSFMT--FEalelpsttltaplSTHDSLFAT 72
Cdd:cd11384   10 SGKTSMRSIIFANYLARDTRRLGATIDVEHSHVrflgnlvlnlwdcggqDAFMEnyFT-------------SQRDHIFRN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339469074  73 AGSLIWVLDMQ-DEYFASISLLIQTAVHLLQYHPriNFEVF--IHKTDGLSEEYKYDTFR----DVRQRVtdeladagyG 145
Cdd:cd11384   77 VEVLIYVFDVEsRELEKDLTYFRSCLEALRQNSP--DAKVFvlIHKMDLVQEDEREAVFErkekELRRLS---------E 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 339469074 146 DRGIAFYQTSIFDHSVYEAMSKVVQKLVPQLPAMEALLNKLCSACRIQKAYLF 198
Cdd:cd11384  146 PLEVTCFPTSIWDETLYKAWSSIVYSLIPNIQVLESNLKKFADICEADEVVLF 198
 
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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