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Conserved domains on  [gi|11181618|gb|AAG32662|]
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Rag C [Homo sapiens]

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 ...
 63-237 8.50e-125

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: 357.30  E-value: 8.50e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11181618  63 RILLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKIYKDDISNSSFVNFQIWDFPGQMDFFDPTFDYEMIFRGTGALIY 142
Cdd:cd11385   1 RILLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKITKDDISNSSFVNFQIWDFPGQLDPFDPTLDPEMIFSGCGALVF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11181618 143 VIDAQDDYMEALTRLHITVSKAYKVNPDMNFEVFIHKVDGLSDDHKIETQRDIHQRANDDLADAGLEKLHLSFYLTSIYD 222
Cdd:cd11385  81 VIDAQDDYDEAIARLVETVTKAYKVNPNINFEVFIHKVDGLSEDHKIETQRDIQQRVTDELADAGLEDVQISFYLTSIYD 160

                       170
                ....*....|....*
gi 11181618 223 HSIFEAFSKVVQKLI 237
Cdd:cd11385 161 HSIFEAFSKVVQKLI 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 ...
 63-237 8.50e-125

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: 357.30  E-value: 8.50e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11181618  63 RILLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKIYKDDISNSSFVNFQIWDFPGQMDFFDPTFDYEMIFRGTGALIY 142
Cdd:cd11385   1 RILLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKITKDDISNSSFVNFQIWDFPGQLDPFDPTLDPEMIFSGCGALVF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11181618 143 VIDAQDDYMEALTRLHITVSKAYKVNPDMNFEVFIHKVDGLSDDHKIETQRDIHQRANDDLADAGLEKLHLSFYLTSIYD 222
Cdd:cd11385  81 VIDAQDDYDEAIARLVETVTKAYKVNPNINFEVFIHKVDGLSEDHKIETQRDIQQRVTDELADAGLEDVQISFYLTSIYD 160

                       170
                ....*....|....*
gi 11181618 223 HSIFEAFSKVVQKLI 237
Cdd:cd11385 161 HSIFEAFSKVVQKLI 175
Gtr1_RagA pfam04670
Gtr1/RagA G protein conserved region; GTR1 was first identified in S. cerevisiae as a ...
 63-289 2.20e-118

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: 343.41  E-value: 2.20e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11181618    63 RILLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKIYKDDISNSSFVNFQIWDFPGQMDFFDP--TFDYEMIFRGTGAL 140
Cdd:pfam04670   1 KVLLMGLSGSGKSSMRSVIFSNYSPRDTLRLGATIDVEHSHVRFLGNLVLNLWDCGGQDDFFDNylTFQKEHIFSNVGVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11181618   141 IYVIDAQ-DDYMEALTRLHITVSKAYKVNPDMNFEVFIHKVDGLSDDHKIETQRDIHQRANDDLADAGLEkLHLSFYLTS 219
Cdd:pfam04670  81 IYVFDVQsREYEEDLARLKETIEALYQYSPDAKVFVLIHKMDLIQEDHREEIFRDRKQEIREESEDLGLE-LDLSFFLTS 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 11181618   220 IYDHSIFEAFSKVVQKLIPQLPTLENLLNIFISNSGIEKAFLFDVVSKIYIATDSSP--VDMQSYELCCDMI 289
Cdd:pfam04670 160 IWDESLYKAWSSIVQKLIPNLPTLENLLKVFCSNSDADEVFLFERTTFLVIATDSRSpvDDMQRYEKCSDII 231
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
63-236 1.51e-07

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 51.14  E-value: 1.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11181618  63 RILLMGLRRSGKSS-IQKVVFHKMSPNETLfleSTN--KIYKDDIS-NSSFVNFQIWDFPGQMDFFDPTFDYEMIFRGTG 138
Cdd:COG1100   5 KIVVVGTGGVGKTSlVNRLVGDIFSLEKYL---STNgvTIDKKELKlDGLDVDLVIWDTPGQDEFRETRQFYARQLTGAS 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11181618 139 ALIYVIDA-QDDYMEALTRLHITVSKAYKVNPDMnfeVFIHKVDgLSDDHKIETQrdihqranDDLADAGLEKLHLSFYL 217
Cdd:COG1100  82 LYLFVVDGtREETLQSLYELLESLRRLGKKSPII---LVLNKID-LYDEEEIEDE--------ERLKEALSEDNIVEVVA 149

                       170       180
                ....*....|....*....|
gi 11181618 218 TSIYD-HSIFEAFSKVVQKL 236
Cdd:COG1100 150 TSAKTgEGVEELFAALAEIL 169
 
Name Accession Description Interval E-value
RagC_like cd11385
Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins C and ...
 63-237 8.50e-125

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: 357.30  E-value: 8.50e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11181618  63 RILLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKIYKDDISNSSFVNFQIWDFPGQMDFFDPTFDYEMIFRGTGALIY 142
Cdd:cd11385   1 RILLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKITKDDISNSSFVNFQIWDFPGQLDPFDPTLDPEMIFSGCGALVF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11181618 143 VIDAQDDYMEALTRLHITVSKAYKVNPDMNFEVFIHKVDGLSDDHKIETQRDIHQRANDDLADAGLEKLHLSFYLTSIYD 222
Cdd:cd11385  81 VIDAQDDYDEAIARLVETVTKAYKVNPNINFEVFIHKVDGLSEDHKIETQRDIQQRVTDELADAGLEDVQISFYLTSIYD 160

                       170
                ....*....|....*
gi 11181618 223 HSIFEAFSKVVQKLI 237
Cdd:cd11385 161 HSIFEAFSKVVQKLI 175
Gtr1_RagA pfam04670
Gtr1/RagA G protein conserved region; GTR1 was first identified in S. cerevisiae as a ...
 63-289 2.20e-118

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: 343.41  E-value: 2.20e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11181618    63 RILLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKIYKDDISNSSFVNFQIWDFPGQMDFFDP--TFDYEMIFRGTGAL 140
Cdd:pfam04670   1 KVLLMGLSGSGKSSMRSVIFSNYSPRDTLRLGATIDVEHSHVRFLGNLVLNLWDCGGQDDFFDNylTFQKEHIFSNVGVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11181618   141 IYVIDAQ-DDYMEALTRLHITVSKAYKVNPDMNFEVFIHKVDGLSDDHKIETQRDIHQRANDDLADAGLEkLHLSFYLTS 219
Cdd:pfam04670  81 IYVFDVQsREYEEDLARLKETIEALYQYSPDAKVFVLIHKMDLIQEDHREEIFRDRKQEIREESEDLGLE-LDLSFFLTS 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 11181618   220 IYDHSIFEAFSKVVQKLIPQLPTLENLLNIFISNSGIEKAFLFDVVSKIYIATDSSP--VDMQSYELCCDMI 289
Cdd:pfam04670 160 IWDESLYKAWSSIVQKLIPNLPTLENLLKVFCSNSDADEVFLFERTTFLVIATDSRSpvDDMQRYEKCSDII 231
Rag cd09915
Rag GTPase subfamily of Ras-related GTPases; Rag GTPases (ras-related GTP-binding proteins) ...
 63-237 2.83e-100

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: 295.24  E-value: 2.83e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11181618  63 RILLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKIYKDDISNSSFVNFQIWDFPGQMDFFDPTFDYEMIFRGTGALIY 142
Cdd:cd09915   1 KLLL*GRRRSGKSSIRKVVFHNYSPFDTLRLESTIDVEHSHLSFLGN*TLNLWDCPGQDVFFEPTKDKEHIFQ*VGALIY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11181618 143 VIDAQDDYMEALTRLHITVSKAYKVNPDMNFEVFIHKVDGLSDDHKIETQRDIHQRANDDLADAGLEKLHLSFYLTSIYD 222
Cdd:cd09915  81 VIDVQDEYLKAITILAKALKQAYKVNPDANIEVLIHKVDGLSLDKKEELQRDI*QRLSETLSEFGLEFPNLSFYLTSIWD 160

                       170
                ....*....|....*
gi 11181618 223 HSIFEAFSKVVQKLI 237
Cdd:cd09915 161 HSIYEAFSQIVQKLI 175
RagA_like cd11384
Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins A and ...
 64-283 3.00e-18

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: 84.19  E-value: 3.00e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11181618  64 ILLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKIykddisNSSFVNF------QIWDFPGQMDFFDPTFDY--EMIFR 135
Cdd:cd11384   2 VLLMGKSGSGKTSMRSIIFANYLARDTRRLGATIDV------EHSHVRFlgnlvlNLWDCGGQDAFMENYFTSqrDHIFR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11181618 136 GTGALIYVIDAQDDYMEA-LTRLHITVSKAYKVNPDMNFEVFIHKVDGLSDDHK----IETQRDIHQRANDdladaglek 210
Cdd:cd11384  76 NVEVLIYVFDVESRELEKdLTYFRSCLEALRQNSPDAKVFVLIHKMDLVQEDEReavfERKEKELRRLSEP--------- 146

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11181618 211 LHLSFYLTSIYDHSIFEAFSKVVQKLIPQLPTLENLLNIFISNSGIEKAFLFDVVSKIYIATDSSP----VDMQSYE 283
Cdd:cd11384 147 LEVTCFPTSIWDETLYKAWSSIVYSLIPNIQVLESNLKKFADICEADEVVLFERATFLVISHSSRKeasaLDPHRFE 223
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 65-234 3.01e-11

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: 61.32  E-value: 3.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11181618  65 LLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKIYKDDISNSS-FVNFQIWDFPGQMDFFDPTF--DYEMIFRGTGALI 141
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYVKELDKgKVKLVLVDTPGLDEFGGLGReeLARLLLRGADLIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11181618 142 YVIDAQDDYMEALTRLHItvsKAYKVNPDMNFEVFIHKVDGLSDDHKIEtqrdihqranDDLADAGLEKLHLSFYLTSIY 221
Cdd:cd00882  81 LVVDSTDRESEEDAKLLI---LRRLRKEGIPIILVGNKIDLLEEREVEE----------LLRLEELAKILGVPVFEVSAK 147

                       170
                ....*....|....
gi 11181618 222 DHS-IFEAFSKVVQ 234
Cdd:cd00882 148 TGEgVDELFEKLIE 161
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
63-236 1.51e-07

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 51.14  E-value: 1.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11181618  63 RILLMGLRRSGKSS-IQKVVFHKMSPNETLfleSTN--KIYKDDIS-NSSFVNFQIWDFPGQMDFFDPTFDYEMIFRGTG 138
Cdd:COG1100   5 KIVVVGTGGVGKTSlVNRLVGDIFSLEKYL---STNgvTIDKKELKlDGLDVDLVIWDTPGQDEFRETRQFYARQLTGAS 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11181618 139 ALIYVIDA-QDDYMEALTRLHITVSKAYKVNPDMnfeVFIHKVDgLSDDHKIETQrdihqranDDLADAGLEKLHLSFYL 217
Cdd:COG1100  82 LYLFVVDGtREETLQSLYELLESLRRLGKKSPII---LVLNKID-LYDEEEIEDE--------ERLKEALSEDNIVEVVA 149

                       170       180
                ....*....|....*....|
gi 11181618 218 TSIYD-HSIFEAFSKVVQKL 236
Cdd:COG1100 150 TSAKTgEGVEELFAALAEIL 169
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
 63-158 7.59e-06

ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions.


Pssm-ID: 206644 [Multi-domain]  Cd Length: 158  Bit Score: 45.65  E-value: 7.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11181618  63 RILLMGLRRSGKSSIqkvvFHKMSPNETLFLESTN--KIYKDDISNssfVNFQIWDFPGQMDFFDPTFDYemiFRGTGAL 140
Cdd:cd00878   1 RILMLGLDGAGKTTI----LYKLKLGEVVTTIPTIgfNVETVEYKN---VKFTVWDVGGQDKIRPLWKHY---YENTDGL 70

                        90       100
                ....*....|....*....|
gi 11181618 141 IYVIDAQD--DYMEALTRLH 158
Cdd:cd00878  71 IFVVDSSDreRIEEAKNELH 90
Arf6 cd04149
ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins ...
 63-158 2.83e-04

ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins localize to the plasma membrane, where they perform a wide variety of functions. In its active, GTP-bound form, Arf6 is involved in cell spreading, Rac-induced formation of plasma membrane ruffles, cell migration, wound healing, and Fc-mediated phagocytosis. Arf6 appears to change the actin structure at the plasma membrane by activating Rac, a Rho family protein involved in membrane ruffling. Arf6 is required for and enhances Rac formation of ruffles. Arf6 can regulate dendritic branching in hippocampal neurons, and in yeast it localizes to the growing bud, where it plays a role in polarized growth and bud site selection. In leukocytes, Arf6 is required for chemokine-stimulated migration across endothelial cells. Arf6 also plays a role in down-regulation of beta2-adrenergic receptors and luteinizing hormone receptors by facilitating the release of sequestered arrestin to allow endocytosis. Arf6 is believed to function at multiple sites on the plasma membrane through interaction with a specific set of GEFs, GAPs, and effectors. Arf6 has been implicated in breast cancer and melanoma cell invasion, and in actin remodelling at the invasion site of Chlamydia infection.


Pssm-ID: 206716  Cd Length: 168  Bit Score: 41.30  E-value: 2.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11181618  63 RILLMGLRRSGKSSIqkvvFHKMSPNE------TLFLESTNKIYKDdisnssfVNFQIWDFPGQmDFFDPTFDYemIFRG 136
Cdd:cd04149  11 RILMLGLDAAGKTTI----LYKLKLGQsvttipTVGFNVETVTYKN-------VKFNVWDVGGQ-DKIRPLWRH--YYTG 76

                        90       100
                ....*....|....*....|....
gi 11181618 137 TGALIYVIDAQD-DYM-EALTRLH 158
Cdd:cd04149  77 TQGLIFVVDSADrDRIdEARQELH 100
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
 63-158 4.12e-04

ADP-ribosylation factor family; Pfam combines a number of different Prosite families together


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 40.67  E-value: 4.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11181618    63 RILLMGLRRSGKSSIqkvvFHKMSPNE------TLFLESTNKIYKDdisnssfVNFQIWDFPGQmDFFDPTF-DYemiFR 135
Cdd:pfam00025   2 RILILGLDNAGKTTI----LYKLKLGEivttipTIGFNVETVTYKN-------VKFTVWDVGGQ-ESLRPLWrNY---FP 66

                          90       100
                  ....*....|....*....|....*
gi 11181618   136 GTGALIYVIDAQDD--YMEALTRLH 158
Cdd:pfam00025  67 NTDAVIFVVDSADRdrIEEAKEELH 91
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
 63-149 8.95e-04

Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial Rho proteins (Miro-1, and Miro-2) and atypical Rho GTPases. Full-length proteins have a unique domain organization, with tandem GTP-binding domains and two EF hand domains (pfam00036) that may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis.


Pssm-ID: 462490 [Multi-domain]  Cd Length: 114  Bit Score: 38.64  E-value: 8.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11181618    63 RILLMGLRRSGKSSI-QKVVFHKMSPNE--TLFLESTNKIYKDDISNSSFVNFQIWDFPGQmDFFDPTFDyeMIFRGTGA 139
Cdd:pfam08477   1 KVVLLGDSGVGKTSLlKRFVDDTFDPKYksTIGVDFKTKTVLENDDNGKKIKLNIWDTAGQ-ERFRSLHP--FYYRGAAA 77

                          90
                  ....*....|
gi 11181618   140 LIYVIDAQDD 149
Cdd:pfam08477  78 ALLVYDSRTF 87
 
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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