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Conserved domains on  [gi|74831320|emb|CAI39282|]
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rag_C80 [Paramecium tetraurelia]

Protein Classification

GTR/RAG family GTP-binding protein( domain architecture ID 10183650)

GTR/RAG family GTP-binding protein similar to yeast GTP-binding protein GTR1, the GTPase component of the GSE complex, a GTPase complex required for intracellular sorting of GAP1 out of the endosome

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RagA_like cd11384
Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins A and ...
10-298 1.08e-154

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: 434.33  E-value: 1.08e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320  10 KMLLMGQHKVGKTSMHSIIFANTPPNQVMQIGLTVDVNQNSFKFMGNLKINLWDCGGQDKLLQEYFTTQKSTIFSNVEVL 89
Cdd:cd11384   1 KVLLMGKSGSGKTSMRSIIFANYLARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDAFMENYFTSQRDHIFRNVEVL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320  90 IYVFDVDKEGdlFIKELNDFKTTVTSLSECSPGAIVFVLIHKFDKIKESERKIVFERKYKEIIQRADGLNIeikDVFSTS 169
Cdd:cd11384  81 IYVFDVESRE--LEKDLTYFRSCLEALRQNSPDAKVFVLIHKMDLVQEDEREAVFERKEKELRRLSEPLEV---TCFPTS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320 170 IWDETLYKAWSQIVQNLIPNINIIKESLKAFCQTCSCEEVVLFEKSTFLIIDFQETNE--KKDIQKYERLSNIIKQFKLT 247
Cdd:cd11384 156 IWDETLYKAWSSIVYSLIPNIQVLESNLKKFADICEADEVVLFERATFLVISHSSRKEasALDPHRFEKISNIIKQFKLS 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 74831320 248 CMKTQASIQAITVKSEKFTVYIDEFTENTFIMLAYTDPSIYPAAISHNVHH 298
Cdd:cd11384 236 CSKLQASFQSMEVRNSNFSAFIDEFTSNTYIMVVMSDPSIESAAILMNIRN 286
 
Name Accession Description Interval E-value
RagA_like cd11384
Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins A and ...
10-298 1.08e-154

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: 434.33  E-value: 1.08e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320  10 KMLLMGQHKVGKTSMHSIIFANTPPNQVMQIGLTVDVNQNSFKFMGNLKINLWDCGGQDKLLQEYFTTQKSTIFSNVEVL 89
Cdd:cd11384   1 KVLLMGKSGSGKTSMRSIIFANYLARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDAFMENYFTSQRDHIFRNVEVL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320  90 IYVFDVDKEGdlFIKELNDFKTTVTSLSECSPGAIVFVLIHKFDKIKESERKIVFERKYKEIIQRADGLNIeikDVFSTS 169
Cdd:cd11384  81 IYVFDVESRE--LEKDLTYFRSCLEALRQNSPDAKVFVLIHKMDLVQEDEREAVFERKEKELRRLSEPLEV---TCFPTS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320 170 IWDETLYKAWSQIVQNLIPNINIIKESLKAFCQTCSCEEVVLFEKSTFLIIDFQETNE--KKDIQKYERLSNIIKQFKLT 247
Cdd:cd11384 156 IWDETLYKAWSSIVYSLIPNIQVLESNLKKFADICEADEVVLFERATFLVISHSSRKEasALDPHRFEKISNIIKQFKLS 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 74831320 248 CMKTQASIQAITVKSEKFTVYIDEFTENTFIMLAYTDPSIYPAAISHNVHH 298
Cdd:cd11384 236 CSKLQASFQSMEVRNSNFSAFIDEFTSNTYIMVVMSDPSIESAAILMNIRN 286
Gtr1_RagA pfam04670
Gtr1/RagA G protein conserved region; GTR1 was first identified in S. cerevisiae as a ...
10-241 2.04e-112

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: 325.31  E-value: 2.04e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320    10 KMLLMGQHKVGKTSMHSIIFANTPPNQVMQIGLTVDVNQNSFKFMGNLKINLWDCGGQDKLLQEYFTTQKSTIFSNVEVL 89
Cdd:pfam04670   1 KVLLMGLSGSGKSSMRSVIFSNYSPRDTLRLGATIDVEHSHVRFLGNLVLNLWDCGGQDDFFDNYLTFQKEHIFSNVGVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320    90 IYVFDVdkEGDLFIKELNDFKTTVTSLSECSPGAIVFVLIHKFDKIKESERKIVFERKYKEIIQRADGLNIEIK-DVFST 168
Cdd:pfam04670  81 IYVFDV--QSREYEEDLARLKETIEALYQYSPDAKVFVLIHKMDLIQEDHREEIFRDRKQEIREESEDLGLELDlSFFLT 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74831320   169 SIWDETLYKAWSQIVQNLIPNINIIKESLKAFCQTCSCEEVVLFEKSTFLIIDFQETNEKKDIQKYERLSNII 241
Cdd:pfam04670 159 SIWDESLYKAWSSIVQKLIPNLPTLENLLKVFCSNSDADEVFLFERTTFLVIATDSRSPVDDMQRYEKCSDII 231
PLN03118 PLN03118
Rab family protein; Provisional
10-145 1.13e-05

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 45.43  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320   10 KMLLMGQHKVGKTSMHSIIFANTPPNQVMQIGLTVDVNQNSFKfMGNLKINLWDCGGqdkllQEYFTTQKSTIFSNVEVL 89
Cdd:PLN03118  16 KILLIGDSGVGKSSLLVSFISSSVEDLAPTIGVDFKIKQLTVG-GKRLKLTIWDTAG-----QERFRTLTSSYYRNAQGI 89
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74831320   90 IYVFDVDKE------GDLFIKELNDFKTTvtslSECspgaIVFVLIHKFDkiKESERKIVFE 145
Cdd:PLN03118  90 ILVYDVTRRetftnlSDVWGKEVELYSTN----QDC----VKMLVGNKVD--RESERDVSRE 141
ARF smart00177
ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular ...
6-83 5.26e-04

ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular transport. Activator 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. Contains ATP/GTP-binding motif (P-loop).


Pssm-ID: 128474 [Multi-domain]  Cd Length: 175  Bit Score: 40.29  E-value: 5.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320      6 NKLKKMLLMGQHKVGKTSmhsiIFANTPPNQVMQIGLTVDVNQNSFKFMgNLKINLWDCGGQDK---LLQEYFTTQKSTI 82
Cdd:smart00177  11 NKEMRILMVGLDAAGKTT----ILYKLKLGESVTTIPTIGFNVETVTYK-NISFTVWDVGGQDKirpLWRHYYTNTQGLI 85

                   .
gi 74831320     83 F 83
Cdd:smart00177  86 F 86
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
9-126 9.17e-04

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 39.58  E-value: 9.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320   9 KKMLLMGQHKVGKTS-----MHSIIFANT--PPN--QVMQIGLTVDVnqnsfkfmGNLKINLWDCGGQDkllqEYFTTQK 79
Cdd:COG1100   4 KKIVVVGTGGVGKTSlvnrlVGDIFSLEKylSTNgvTIDKKELKLDG--------LDVDLVIWDTPGQD----EFRETRQ 71
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 74831320  80 S--TIFSNVEVLIYVFDVDKEGDLfiKELNDFKTTVTSLSECSPGAIVF 126
Cdd:COG1100  72 FyaRQLTGASLYLFVVDGTREETL--QSLYELLESLRRLGKKSPIILVL 118
 
Name Accession Description Interval E-value
RagA_like cd11384
Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins A and ...
10-298 1.08e-154

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: 434.33  E-value: 1.08e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320  10 KMLLMGQHKVGKTSMHSIIFANTPPNQVMQIGLTVDVNQNSFKFMGNLKINLWDCGGQDKLLQEYFTTQKSTIFSNVEVL 89
Cdd:cd11384   1 KVLLMGKSGSGKTSMRSIIFANYLARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDAFMENYFTSQRDHIFRNVEVL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320  90 IYVFDVDKEGdlFIKELNDFKTTVTSLSECSPGAIVFVLIHKFDKIKESERKIVFERKYKEIIQRADGLNIeikDVFSTS 169
Cdd:cd11384  81 IYVFDVESRE--LEKDLTYFRSCLEALRQNSPDAKVFVLIHKMDLVQEDEREAVFERKEKELRRLSEPLEV---TCFPTS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320 170 IWDETLYKAWSQIVQNLIPNINIIKESLKAFCQTCSCEEVVLFEKSTFLIIDFQETNE--KKDIQKYERLSNIIKQFKLT 247
Cdd:cd11384 156 IWDETLYKAWSSIVYSLIPNIQVLESNLKKFADICEADEVVLFERATFLVISHSSRKEasALDPHRFEKISNIIKQFKLS 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 74831320 248 CMKTQASIQAITVKSEKFTVYIDEFTENTFIMLAYTDPSIYPAAISHNVHH 298
Cdd:cd11384 236 CSKLQASFQSMEVRNSNFSAFIDEFTSNTYIMVVMSDPSIESAAILMNIRN 286
Gtr1_RagA pfam04670
Gtr1/RagA G protein conserved region; GTR1 was first identified in S. cerevisiae as a ...
10-241 2.04e-112

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: 325.31  E-value: 2.04e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320    10 KMLLMGQHKVGKTSMHSIIFANTPPNQVMQIGLTVDVNQNSFKFMGNLKINLWDCGGQDKLLQEYFTTQKSTIFSNVEVL 89
Cdd:pfam04670   1 KVLLMGLSGSGKSSMRSVIFSNYSPRDTLRLGATIDVEHSHVRFLGNLVLNLWDCGGQDDFFDNYLTFQKEHIFSNVGVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320    90 IYVFDVdkEGDLFIKELNDFKTTVTSLSECSPGAIVFVLIHKFDKIKESERKIVFERKYKEIIQRADGLNIEIK-DVFST 168
Cdd:pfam04670  81 IYVFDV--QSREYEEDLARLKETIEALYQYSPDAKVFVLIHKMDLIQEDHREEIFRDRKQEIREESEDLGLELDlSFFLT 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74831320   169 SIWDETLYKAWSQIVQNLIPNINIIKESLKAFCQTCSCEEVVLFEKSTFLIIDFQETNEKKDIQKYERLSNII 241
Cdd:pfam04670 159 SIWDESLYKAWSSIVQKLIPNLPTLENLLKVFCSNSDADEVFLFERTTFLVIATDSRSPVDDMQRYEKCSDII 231
Rag cd09915
Rag GTPase subfamily of Ras-related GTPases; Rag GTPases (ras-related GTP-binding proteins) ...
10-187 1.10e-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: 124.60  E-value: 1.10e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320  10 KMLLMGQHKVGKTSMHSIIFANTPPNQVMQIGLTVDVNQNSFKFMGNLKINLWDCGGQDKLLQeyFTTQKSTIFSNVEVL 89
Cdd:cd09915   1 KLLL*GRRRSGKSSIRKVVFHNYSPFDTLRLESTIDVEHSHLSFLGN*TLNLWDCPGQDVFFE--PTKDKEHIFQ*VGAL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320  90 IYVFDVDKEgdlFIKELNDFKTTVTSLSECSPGAIVFVLIHKFDKIKESERkivfERKYKEIIQRAD------GLNIEIK 163
Cdd:cd09915  79 IYVIDVQDE---YLKAITILAKALKQAYKVNPDANIEVLIHKVDGLSLDKK----EELQRDI*QRLSetlsefGLEFPNL 151
                       170       180
                ....*....|....*....|....
gi 74831320 164 DVFSTSIWDETLYKAWSQIVQNLI 187
Cdd:cd09915 152 SFYLTSIWDHSIYEAFSQIVQKLI 175
RagC_like cd11385
Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins C and ...
10-187 2.10e-18

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: 81.11  E-value: 2.10e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320  10 KMLLMGQHKVGKTSMHSIIFANTPPNQVMQIGLTVDVNQNSFKFMGNLKINLWDCGGQDKLLQEYFTTQksTIFSNVEVL 89
Cdd:cd11385   1 RILLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKITKDDISNSSFVNFQIWDFPGQLDPFDPTLDPE--MIFSGCGAL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320  90 IYVFDVdkeGDLFIKELNDFKTTVTSLSECSPGAIVFVLIHKFDKIKEsERKIVFERkykEIIQR-----ADGLNIEIKD 164
Cdd:cd11385  79 VFVIDA---QDDYDEAIARLVETVTKAYKVNPNINFEVFIHKVDGLSE-DHKIETQR---DIQQRvtdelADAGLEDVQI 151
                       170       180
                ....*....|....*....|....
gi 74831320 165 VFS-TSIWDETLYKAWSQIVQNLI 187
Cdd:cd11385 152 SFYlTSIYDHSIFEAFSKVVQKLI 175
PLN03118 PLN03118
Rab family protein; Provisional
10-145 1.13e-05

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 45.43  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320   10 KMLLMGQHKVGKTSMHSIIFANTPPNQVMQIGLTVDVNQNSFKfMGNLKINLWDCGGqdkllQEYFTTQKSTIFSNVEVL 89
Cdd:PLN03118  16 KILLIGDSGVGKSSLLVSFISSSVEDLAPTIGVDFKIKQLTVG-GKRLKLTIWDTAG-----QERFRTLTSSYYRNAQGI 89
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74831320   90 IYVFDVDKE------GDLFIKELNDFKTTvtslSECspgaIVFVLIHKFDkiKESERKIVFE 145
Cdd:PLN03118  90 ILVYDVTRRetftnlSDVWGKEVELYSTN----QDC----VKMLVGNKVD--RESERDVSRE 141
Arf6 cd04149
ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins ...
6-83 1.38e-05

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: 44.77  E-value: 1.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320   6 NKLKKMLLMGQHKVGKTSmhsiIFANTPPNQVMQIGLTVDVNQNSFKFMgNLKINLWDCGGQDK---LLQEYFTTQKSTI 82
Cdd:cd04149   7 NKEMRILMLGLDAAGKTT----ILYKLKLGQSVTTIPTVGFNVETVTYK-NVKFNVWDVGGQDKirpLWRHYYTGTQGLI 81

                .
gi 74831320  83 F 83
Cdd:cd04149  82 F 82
Arl3 cd04155
Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most ...
3-94 1.45e-05

Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most Arf family members in the N-terminal extension. In is inactive, GDP-bound form, the N-terminal extension forms an elongated loop that is hydrophobically anchored into the membrane surface; however, it has been proposed that this region might form a helix in the GTP-bound form. The delta subunit of the rod-specific cyclic GMP phosphodiesterase type 6 (PDEdelta) is an Arl3 effector. Arl3 binds microtubules in a regulated manner to alter specific aspects of cytokinesis via interactions with retinitis pigmentosa 2 (RP2). It has been proposed that RP2 functions in concert with Arl3 to link the cell membrane and the cytoskeleton in photoreceptors as part of the cell signaling or vesicular transport machinery. In mice, the absence of Arl3 is associated with abnormal epithelial cell proliferation and cyst formation.


Pssm-ID: 206721 [Multi-domain]  Cd Length: 174  Bit Score: 44.69  E-value: 1.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320   3 SNENKLKKMLLMGQHKVGKTSmhsiIFANTPPNQVMQIGLTVDVNQNSFKFMGnLKINLWDCGGQDKlLQEYFttqkSTI 82
Cdd:cd04155  10 PSSRQEVRILLLGLDNAGKTT----ILKQLASEDISHITPTQGFNIKNVQADG-FKLNVWDIGGQRK-IRPYW----RNY 79
                        90
                ....*....|..
gi 74831320  83 FSNVEVLIYVFD 94
Cdd:cd04155  80 FENTDVLIYVID 91
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
10-98 3.83e-04

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


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 40.29  E-value: 3.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320    10 KMLLMGQHKVGKTSmhsiIFANTPPNQVMQIGLTVDVNQNSFKFmGNLKINLWDCGGQDKlLQEYFttqkSTIFSNVEVL 89
Cdd:pfam00025   2 RILILGLDNAGKTT----ILYKLKLGEIVTTIPTIGFNVETVTY-KNVKFTVWDVGGQES-LRPLW----RNYFPNTDAV 71
                          90
                  ....*....|
gi 74831320    90 IYVFDV-DKE 98
Cdd:pfam00025  72 IFVVDSaDRD 81
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
10-133 4.32e-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: 39.41  E-value: 4.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320    10 KMLLMGQHKVGKTS-MHSIIFANTPPNQVMQIGLTV---DVNQNSFKfMGNLKINLWDCGGQDK---LLQEYFTtqksti 82
Cdd:pfam08477   1 KVVLLGDSGVGKTSlLKRFVDDTFDPKYKSTIGVDFktkTVLENDDN-GKKIKLNIWDTAGQERfrsLHPFYYR------ 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 74831320    83 fsNVEVLIYVFDvdkegdlfIKELNDFKTTVTSLSECSPGAIVFVLIHKFD 133
Cdd:pfam08477  74 --GAAAALLVYD--------SRTFSNLKYWLRELKKYAGNSPVILVGNKID 114
ARF smart00177
ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular ...
6-83 5.26e-04

ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular transport. Activator 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. Contains ATP/GTP-binding motif (P-loop).


Pssm-ID: 128474 [Multi-domain]  Cd Length: 175  Bit Score: 40.29  E-value: 5.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320      6 NKLKKMLLMGQHKVGKTSmhsiIFANTPPNQVMQIGLTVDVNQNSFKFMgNLKINLWDCGGQDK---LLQEYFTTQKSTI 82
Cdd:smart00177  11 NKEMRILMVGLDAAGKTT----ILYKLKLGESVTTIPTIGFNVETVTYK-NISFTVWDVGGQDKirpLWRHYYTNTQGLI 85

                   .
gi 74831320     83 F 83
Cdd:smart00177  86 F 86
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
12-152 7.10e-04

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: 39.75  E-value: 7.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320  12 LLMGQHKVGKTS-----MHSIIFANTPPNQVmqiglTVDVNQNSFKF-MGNLKINLWDCGGQDKLLQEYFTTQKSTIFSN 85
Cdd:cd00882   1 VVVGRGGVGKSSllnalLGGEVGEVSDVPGT-----TRDPDVYVKELdKGKVKLVLVDTPGLDEFGGLGREELARLLLRG 75
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74831320  86 VEVLIYVFDVDKegdlfiKELNDFKTTVTSLSECSPGAIVFVLIHKFDKIKESERKIVFERKYKEII 152
Cdd:cd00882  76 ADLILLVVDSTD------RESEEDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELAKI 136
RocCOR cd09914
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ...
10-68 8.56e-04

Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein family is characterized by a superdomain containing a Ras-like GTPase domain, called Roc (Ras of complex proteins), and a characteristic second domain called COR (C-terminal of Roc). A kinase domain and diverse regulatory domains are also often found in Roco proteins. Their functions are diverse; in Dictyostelium discoideum, which encodes 11 Roco proteins, they are involved in cell division, chemotaxis and development, while in human, where 4 Roco proteins (LRRK1, LRRK2, DAPK1, and MFHAS1) are encoded, these proteins are involved in epilepsy and cancer. Mutations in LRRK2 (leucine-rich repeat kinase 2) are known to cause familial Parkinson's disease.


Pssm-ID: 206741 [Multi-domain]  Cd Length: 161  Bit Score: 39.24  E-value: 8.56e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320  10 KMLLMGQHKVGKTSM-HSIIFANTPPNQVMQIGLTVDVNQNSFKFMGNLKINLWDCGGQD 68
Cdd:cd09914   3 KLMLVGQGGVGKTSLcKQLIGEKFDGDESSTHGINVQDWKIPAPERKKIRLNVWDFGGQE 62
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
9-126 9.17e-04

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 39.58  E-value: 9.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320   9 KKMLLMGQHKVGKTS-----MHSIIFANT--PPN--QVMQIGLTVDVnqnsfkfmGNLKINLWDCGGQDkllqEYFTTQK 79
Cdd:COG1100   4 KKIVVVGTGGVGKTSlvnrlVGDIFSLEKylSTNgvTIDKKELKLDG--------LDVDLVIWDTPGQD----EFRETRQ 71
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 74831320  80 S--TIFSNVEVLIYVFDVDKEGDLfiKELNDFKTTVTSLSECSPGAIVF 126
Cdd:COG1100  72 FyaRQLTGASLYLFVVDGTREETL--QSLYELLESLRRLGKKSPIILVL 118
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
20-98 1.74e-03

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: 38.33  E-value: 1.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320  20 GKTSM-HSIIfantpPNQVMQIGLTVDVNQNSFKFmGNLKINLWDCGGQDKLLQ---EYFTtqkstifsNVEVLIYVFDV 95
Cdd:cd00878  11 GKTTIlYKLK-----LGEVVTTIPTIGFNVETVEY-KNVKFTVWDVGGQDKIRPlwkHYYE--------NTDGLIFVVDS 76

                ....
gi 74831320  96 -DKE 98
Cdd:cd00878  77 sDRE 80
ARLTS1 cd04156
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ...
10-94 4.34e-03

Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), also known as Arl11, is a member of the Arf family of small GTPases that is believed to play a major role in apoptotic signaling. ARLTS1 is widely expressed and functions as a tumor suppressor gene in several human cancers. ARLTS1 is a low-penetrance suppressor that accounts for a small percentage of familial melanoma or familial chronic lymphocytic leukemia (CLL). ARLTS1 inactivation seems to occur most frequently through biallelic down-regulation by hypermethylation of the promoter. In breast cancer, ARLTS1 alterations were typically a combination of a hypomorphic polymorphism plus loss of heterozygosity. In a case of thyroid adenoma, ARLTS1 alterations were polymorphism plus promoter hypermethylation. The nonsense polymorphism Trp149Stop occurs with significantly greater frequency in familial cancer cases than in sporadic cancer cases, and the Cys148Arg polymorphism is associated with an increase in high-risk familial breast cancer.


Pssm-ID: 133356 [Multi-domain]  Cd Length: 160  Bit Score: 37.39  E-value: 4.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320  10 KMLLMGQHKVGKTS-MHSIIFAntppnQVMQIGLTVDVNQNSFKFMGNLKINLWDCGGQDKLLQEYfttqkSTIFSNVEV 88
Cdd:cd04156   1 QVLLLGLDSAGKSTlLYKLKHA-----ELVTTIPTVGFNVEMLQLEKHLSLTVWDVGGQEKMRTVW-----KCYLENTDG 70

                ....*.
gi 74831320  89 LIYVFD 94
Cdd:cd04156  71 LVYVVD 76
Arl5_Arl8 cd04153
Arf-like 5 (Arl5) and 8 (Arl8) GTPases; Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like ...
4-94 7.62e-03

Arf-like 5 (Arl5) and 8 (Arl8) GTPases; Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like Arl4 and Arl7, are localized to the nucleus and nucleolus. Arl5 is developmentally regulated during embryogenesis in mice. Human Arl5 interacts with the heterochromatin protein 1-alpha (HP1alpha), a nonhistone chromosomal protein that is associated with heterochromatin and telomeres, and prevents telomere fusion. Arl5 may also play a role in embryonic nuclear dynamics and/or signaling cascades. Arl8 was identified from a fetal cartilage cDNA library. It is found in brain, heart, lung, cartilage, and kidney. No function has been assigned for Arl8 to date.


Pssm-ID: 133353 [Multi-domain]  Cd Length: 174  Bit Score: 36.56  E-value: 7.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74831320   4 NENKLKKMLLMGQHKVGKTSmhsiIFANTPPNQVMQIGLTVDVNQNSFKFmGNLKINLWDCGGQDKLLQEYfttqkSTIF 83
Cdd:cd04153  11 FPRKEYKVIIVGLDNAGKTT----ILYQFLLGEVVHTSPTIGSNVEEIVY-KNIRFLMWDIGGQESLRSSW-----NTYY 80
                        90
                ....*....|.
gi 74831320  84 SNVEVLIYVFD 94
Cdd:cd04153  81 TNTDAVILVID 91
 
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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