NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1229014703|ref|XP_022072769|]
View 

ras-related GTP-binding protein A [Acanthochromis polyacanthus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 9-292 0e+00

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: 584.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   9 KVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDTFMENYFTSQRDNIFRNVEVL 88
Cdd:cd11384     1 KVLLMGKSGSGKTSMRSIIFANYLARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDAFMENYFTSQRDHIFRNVEVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703  89 IYVFDVESRELEKDMHYYQSCLEAILQNSPDAKVFCLVHKMDLVQEDQRDLIFKEREEDLKRLSRPLACTCFRTSIWDET 168
Cdd:cd11384    81 IYVFDVESRELEKDLTYFRSCLEALRQNSPDAKVFVLIHKMDLVQEDEREAVFERKEKELRRLSEPLEVTCFPTSIWDET 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703 169 LYKAWSSIVYQLIPNVQQLETNLRNFAQIIEADEVLLFERATFLVISHYQCKEQ--RDAHRFEKISNIIKQFKLSCSKLA 246
Cdd:cd11384   161 LYKAWSSIVYSLIPNIQVLESNLKKFADICEADEVVLFERATFLVISHSSRKEAsaLDPHRFEKISNIIKQFKLSCSKLQ 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1229014703 247 ASFQSMEVRNSNFAAFIDVFTSNTYVMVIMSDPSIPSAATLINIRN 292
Cdd:cd11384   241 ASFQSMEVRNSNFSAFIDEFTSNTYIMVVMSDPSIESAAILMNIRN 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 ...
 9-292 0e+00

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: 584.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   9 KVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDTFMENYFTSQRDNIFRNVEVL 88
Cdd:cd11384     1 KVLLMGKSGSGKTSMRSIIFANYLARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDAFMENYFTSQRDHIFRNVEVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703  89 IYVFDVESRELEKDMHYYQSCLEAILQNSPDAKVFCLVHKMDLVQEDQRDLIFKEREEDLKRLSRPLACTCFRTSIWDET 168
Cdd:cd11384    81 IYVFDVESRELEKDLTYFRSCLEALRQNSPDAKVFVLIHKMDLVQEDEREAVFERKEKELRRLSEPLEVTCFPTSIWDET 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703 169 LYKAWSSIVYQLIPNVQQLETNLRNFAQIIEADEVLLFERATFLVISHYQCKEQ--RDAHRFEKISNIIKQFKLSCSKLA 246
Cdd:cd11384   161 LYKAWSSIVYSLIPNIQVLESNLKKFADICEADEVVLFERATFLVISHSSRKEAsaLDPHRFEKISNIIKQFKLSCSKLQ 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1229014703 247 ASFQSMEVRNSNFAAFIDVFTSNTYVMVIMSDPSIPSAATLINIRN 292
Cdd:cd11384   241 ASFQSMEVRNSNFSAFIDEFTSNTYIMVVMSDPSIESAAILMNIRN 286
Gtr1_RagA pfam04670
Gtr1/RagA G protein conserved region; GTR1 was first identified in S. cerevisiae as a ...
 9-235 1.20e-134

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: 381.16  E-value: 1.20e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   9 KVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDTFMENYFTSQRDNIFRNVEVL 88
Cdd:pfam04670   1 KVLLMGLSGSGKSSMRSVIFSNYSPRDTLRLGATIDVEHSHVRFLGNLVLNLWDCGGQDDFFDNYLTFQKEHIFSNVGVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703  89 IYVFDVESRELEKDMHYYQSCLEAILQNSPDAKVFCLVHKMDLVQEDQRDLIFKEREEDLKRLSRPLA----CTCFRTSI 164
Cdd:pfam04670  81 IYVFDVQSREYEEDLARLKETIEALYQYSPDAKVFVLIHKMDLIQEDHREEIFRDRKQEIREESEDLGleldLSFFLTSI 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229014703 165 WDETLYKAWSSIVYQLIPNVQQLETNLRNFAQIIEADEVLLFERATFLVISHYQCKEQRDAHRFEKISNII 235
Cdd:pfam04670 161 WDESLYKAWSSIVQKLIPNLPTLENLLKVFCSNSDADEVFLFERTTFLVIATDSRSPVDDMQRYEKCSDII 231
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
7-163 3.18e-09

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 55.37  E-value: 3.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   7 KKKVLLMGKSGSGKTSmrsiiFANYIARDT---RRLGATIDVEHSHVRF---LGNLVLNLWDCGGQDTFMEnyFTSQRDN 80
Cdd:COG1100     3 EKKIVVVGTGGVGKTS-----LVNRLVGDIfslEKYLSTNGVTIDKKELkldGLDVDLVIWDTPGQDEFRE--TRQFYAR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703  81 IFRNVEVLIYVFDVesrELEKDMHYYQSCLEAILQNSPDAKVFCLVHKMDLVQEDQRdlifKEREEDLKRLSRPLACTCF 160
Cdd:COG1100    76 QLTGASLYLFVVDG---TREETLQSLYELLESLRRLGKKSPIILVLNKIDLYDEEEI----EDEERLKEALSEDNIVEVV 148


                  ...
gi 1229014703 161 RTS 163
Cdd:COG1100   149 ATS 151
PLN03118 PLN03118
Rab family protein; Provisional
 9-163 5.64e-07

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 49.28  E-value: 5.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   9 KVLLMGKSGSGKTSMrsiiFANYIARDTRRLGATIDVEHSHVRFL---GNLVLNLWDCGGQDTFmeNYFTSqrdNIFRNV 85
Cdd:PLN03118   16 KILLIGDSGVGKSSL----LVSFISSSVEDLAPTIGVDFKIKQLTvggKRLKLTIWDTAGQERF--RTLTS---SYYRNA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703  86 EVLIYVFDVESREL--------EKDMHYY---QSCLEAILQNSPDakvfclvhkmdlvQEDQRDLifkEREEDLKrLSRP 154
Cdd:PLN03118   87 QGIILVYDVTRRETftnlsdvwGKEVELYstnQDCVKMLVGNKVD-------------RESERDV---SREEGMA-LAKE 149


                  ....*....
gi 1229014703 155 LACTCFRTS 163
Cdd:PLN03118  150 HGCLFLECS 158
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 8-135 2.17e-06

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 46.98  E-value: 2.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   8 KKVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATIDVEHSHVRFLG-NLVLNLWDCGGQDTF--MENYFTSQRDNIFRN 84
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYVTTVIEEDGkTYKFNLLDTAGQEDYdaIRRLYYPQVERSLRV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1229014703  85 VEVLIYVFDVESRELEKDMhyyqsclEAILQNSPDAKVFCLVHKMDLVQED 135
Cdd:TIGR00231  82 FDIVILVLDVEEILEKQTK-------EIIHHADSGVPIILVGNKIDLKDAD 125
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
 9-163 5.86e-03

Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 36.72  E-value: 5.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703    9 KVLLMGKSGSGKTS-MRSiiFANYIARDTRRlgATIDVEHShVRFL---GNLV-LNLWDCGGQDTfmenyFTSQRDNIFR 83
Cdd:smart00175   2 KIILIGDSGVGKSSlLSR--FTDGKFSEQYK--STIGVDFK-TKTIevdGKRVkLQIWDTAGQER-----FRSITSSYYR 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   84 NVEVLIYVFDVESRELEKDMhyyQSCLEAILQNSPDAKVFCLV-HKMDLvqEDQRDLifkeREEDLKRLSRPLACTCFRT 162
Cdd:smart00175  72 GAVGALLVYDITNRESFENL---ENWLKELREYASPNVVIMLVgNKSDL--EEQRQV----SREEAEAFAEEHGLPFFET 142


                   .
gi 1229014703  163 S 163
Cdd:smart00175 143 S 143
 
Name Accession Description Interval E-value
RagA_like cd11384
Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins A and ...
 9-292 0e+00

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: 584.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   9 KVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDTFMENYFTSQRDNIFRNVEVL 88
Cdd:cd11384     1 KVLLMGKSGSGKTSMRSIIFANYLARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDAFMENYFTSQRDHIFRNVEVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703  89 IYVFDVESRELEKDMHYYQSCLEAILQNSPDAKVFCLVHKMDLVQEDQRDLIFKEREEDLKRLSRPLACTCFRTSIWDET 168
Cdd:cd11384    81 IYVFDVESRELEKDLTYFRSCLEALRQNSPDAKVFVLIHKMDLVQEDEREAVFERKEKELRRLSEPLEVTCFPTSIWDET 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703 169 LYKAWSSIVYQLIPNVQQLETNLRNFAQIIEADEVLLFERATFLVISHYQCKEQ--RDAHRFEKISNIIKQFKLSCSKLA 246
Cdd:cd11384   161 LYKAWSSIVYSLIPNIQVLESNLKKFADICEADEVVLFERATFLVISHSSRKEAsaLDPHRFEKISNIIKQFKLSCSKLQ 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1229014703 247 ASFQSMEVRNSNFAAFIDVFTSNTYVMVIMSDPSIPSAATLINIRN 292
Cdd:cd11384   241 ASFQSMEVRNSNFSAFIDEFTSNTYIMVVMSDPSIESAAILMNIRN 286
Gtr1_RagA pfam04670
Gtr1/RagA G protein conserved region; GTR1 was first identified in S. cerevisiae as a ...
 9-235 1.20e-134

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: 381.16  E-value: 1.20e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   9 KVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDTFMENYFTSQRDNIFRNVEVL 88
Cdd:pfam04670   1 KVLLMGLSGSGKSSMRSVIFSNYSPRDTLRLGATIDVEHSHVRFLGNLVLNLWDCGGQDDFFDNYLTFQKEHIFSNVGVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703  89 IYVFDVESRELEKDMHYYQSCLEAILQNSPDAKVFCLVHKMDLVQEDQRDLIFKEREEDLKRLSRPLA----CTCFRTSI 164
Cdd:pfam04670  81 IYVFDVQSREYEEDLARLKETIEALYQYSPDAKVFVLIHKMDLIQEDHREEIFRDRKQEIREESEDLGleldLSFFLTSI 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229014703 165 WDETLYKAWSSIVYQLIPNVQQLETNLRNFAQIIEADEVLLFERATFLVISHYQCKEQRDAHRFEKISNII 235
Cdd:pfam04670 161 WDESLYKAWSSIVQKLIPNLPTLENLLKVFCSNSDADEVFLFERTTFLVIATDSRSPVDDMQRYEKCSDII 231
Rag cd09915
Rag GTPase subfamily of Ras-related GTPases; Rag GTPases (ras-related GTP-binding proteins) ...
 9-181 4.65e-50

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: 164.27  E-value: 4.65e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   9 KVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDTFMEnyFTSQRDNIFRNVEVL 88
Cdd:cd09915     1 KLLL*GRRRSGKSSIRKVVFHNYSPFDTLRLESTIDVEHSHLSFLGN*TLNLWDCPGQDVFFE--PTKDKEHIFQ*VGAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703  89 IYVFDVESrELEKDMHYYQSCLEAILQNSPDAKVFCLVHKMDLVQED-----QRDLIFKEREEDLKRLSRPLACTCFRTS 163
Cdd:cd09915    79 IYVIDVQD-EYLKAITILAKALKQAYKVNPDANIEVLIHKVDGLSLDkkeelQRDI*QRLSETLSEFGLEFPNLSFYLTS 157

                         170
                  ....*....|....*...
gi 1229014703 164 IWDETLYKAWSSIVYQLI 181
Cdd:cd09915   158 IWDHSIYEAFSQIVQKLI 175
RagC_like cd11385
Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins C and ...
 9-181 8.98e-15

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: 71.10  E-value: 8.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   9 KVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDTFMENYFTSqrDNIFRNVEVL 88
Cdd:cd11385     1 RILLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKITKDDISNSSFVNFQIWDFPGQLDPFDPTLDP--EMIFSGCGAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703  89 IYVFDVESrelekdmHYYQSC------LEAILQNSPDAKVFCLVHKMDLVQED-----QRDLIFKEREE--DLKRLSRPL 155
Cdd:cd11385    79 VFVIDAQD-------DYDEAIarlvetVTKAYKVNPNINFEVFIHKVDGLSEDhkietQRDIQQRVTDElaDAGLEDVQI 151

                         170       180
                  ....*....|....*....|....*..
gi 1229014703 156 ActcFR-TSIWDETLYKAWSSIVYQLI 181
Cdd:cd11385   152 S---FYlTSIYDHSIFEAFSKVVQKLI 175
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 11-163 5.77e-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: 60.16  E-value: 5.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703  11 LLMGKSGSGKTSmrsiiFANYIARDT-----RRLGATIDVEHSHVRFLGNLV-LNLWDCGGQDTFMENYFTSQRDNIFRN 84
Cdd:cd00882     1 VVVGRGGVGKSS-----LLNALLGGEvgevsDVPGTTRDPDVYVKELDKGKVkLVLVDTPGLDEFGGLGREELARLLLRG 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229014703  85 VEVLIYVFDVESRELEKDMHYyqscLEAILQNSPDAKVFCLVHKMDLVQEDQRdlifkEREEDLKRLSRPLACTCFRTS 163
Cdd:cd00882    76 ADLILLVVDSTDRESEEDAKL----LILRRLRKEGIPIILVGNKIDLLEEREV-----EELLRLEELAKILGVPVFEVS 145
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
7-163 3.18e-09

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 55.37  E-value: 3.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   7 KKKVLLMGKSGSGKTSmrsiiFANYIARDT---RRLGATIDVEHSHVRF---LGNLVLNLWDCGGQDTFMEnyFTSQRDN 80
Cdd:COG1100     3 EKKIVVVGTGGVGKTS-----LVNRLVGDIfslEKYLSTNGVTIDKKELkldGLDVDLVIWDTPGQDEFRE--TRQFYAR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703  81 IFRNVEVLIYVFDVesrELEKDMHYYQSCLEAILQNSPDAKVFCLVHKMDLVQEDQRdlifKEREEDLKRLSRPLACTCF 160
Cdd:COG1100    76 QLTGASLYLFVVDG---TREETLQSLYELLESLRRLGKKSPIILVLNKIDLYDEEEI----EDEERLKEALSEDNIVEVV 148


                  ...
gi 1229014703 161 RTS 163
Cdd:COG1100   149 ATS 151
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
 9-146 1.60e-07

Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop motif with GTP_EFTU, arf and myosin_head. See pfam00009 pfam00025, pfam00063. As regards Rab GTPases, these are important regulators of vesicle formation, motility and fusion. They share a fold in common with all Ras GTPases: this is a six-stranded beta-sheet surrounded by five alpha-helices.


Pssm-ID: 425451 [Multi-domain]  Cd Length: 162  Bit Score: 50.21  E-value: 1.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   9 KVLLMGKSGSGKTSMRS--------------IIFANYIArdtrrlgaTIDVEHSHVRflgnlvLNLWDCGGQDTfmenyF 74
Cdd:pfam00071   1 KLVLVGDGGVGKSSLLIrftqnkfpeeyiptIGVDFYTK--------TIEVDGKTVK------LQIWDTAGQER-----F 61

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229014703  75 TSQRDNIFRNVEVLIYVFDVESRE-LEKDMHYYQScleaILQNSPDAKVFCLV-HKMDLvqEDQRDLIFKEREE 146
Cdd:pfam00071  62 RALRPLYYRGADGFLLVYDITSRDsFENVKKWVEE----ILRHADENVPIVLVgNKCDL--EDQRVVSTEEGEA 129
PLN03118 PLN03118
Rab family protein; Provisional
 9-163 5.64e-07

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 49.28  E-value: 5.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   9 KVLLMGKSGSGKTSMrsiiFANYIARDTRRLGATIDVEHSHVRFL---GNLVLNLWDCGGQDTFmeNYFTSqrdNIFRNV 85
Cdd:PLN03118   16 KILLIGDSGVGKSSL----LVSFISSSVEDLAPTIGVDFKIKQLTvggKRLKLTIWDTAGQERF--RTLTS---SYYRNA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703  86 EVLIYVFDVESREL--------EKDMHYY---QSCLEAILQNSPDakvfclvhkmdlvQEDQRDLifkEREEDLKrLSRP 154
Cdd:PLN03118   87 QGIILVYDVTRRETftnlsdvwGKEVELYstnQDCVKMLVGNKVD-------------RESERDV---SREEGMA-LAKE 149


                  ....*....
gi 1229014703 155 LACTCFRTS 163
Cdd:PLN03118  150 HGCLFLECS 158
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
 9-130 1.42e-06

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: 46.35  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   9 KVLLMGKSGSGKTSmrsiiFANYIARDTR--RLGATIDVEHSHVRFLGN------LVLNLWDCGGQDTF--MENYFtsqr 78
Cdd:pfam08477   1 KVVLLGDSGVGKTS-----LLKRFVDDTFdpKYKSTIGVDFKTKTVLENddngkkIKLNIWDTAGQERFrsLHPFY---- 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1229014703  79 dniFRNVEVLIYVFDVESrelEKDMHYYQSCLEAILQNSPdakVFCLVHKMD 130
Cdd:pfam08477  72 ---YRGAAAALLVYDSRT---FSNLKYWLRELKKYAGNSP---VILVGNKID 114
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 8-135 2.17e-06

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 46.98  E-value: 2.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   8 KKVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATIDVEHSHVRFLG-NLVLNLWDCGGQDTF--MENYFTSQRDNIFRN 84
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYVTTVIEEDGkTYKFNLLDTAGQEDYdaIRRLYYPQVERSLRV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1229014703  85 VEVLIYVFDVESRELEKDMhyyqsclEAILQNSPDAKVFCLVHKMDLVQED 135
Cdd:TIGR00231  82 FDIVILVLDVEEILEKQTK-------EIIHHADSGVPIILVGNKIDLKDAD 125
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
 9-139 2.50e-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: 46.80  E-value: 2.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   9 KVLLMGKSGSGKTSMRsiifaNYIAR-DTRRLGATI-----DVEHSHVRFlgnlvlNLWDCGGQDTFM---ENYftsqrd 79
Cdd:cd00878     1 RILMLGLDGAGKTTIL-----YKLKLgEVVTTIPTIgfnveTVEYKNVKF------TVWDVGGQDKIRplwKHY------ 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229014703  80 niFRNVEVLIYVFDVESRElekdmHYYQSC--LEAILQNSP--DAKVFCLVHKMDL-----VQEDQRDL 139
Cdd:cd00878    64 --YENTDGLIFVVDSSDRE-----RIEEAKneLHKLLNEEElkGAPLLILANKQDLpgaltESELIELL 125
RabL3 cd04102
Rab GTPase-like family 3 (Rab-like3); RabL3 (Rab-like3) subfamily. RabL3s are novel proteins ...
 9-113 5.24e-06

Rab GTPase-like family 3 (Rab-like3); RabL3 (Rab-like3) subfamily. RabL3s are novel proteins that have high sequence similarity with Rab family members, but display features that are distinct from Rabs, and have been termed Rab-like. As in other Rab-like proteins, RabL3 lacks a prenylation site at the C-terminus. The specific function of RabL3 remains unknown.


Pssm-ID: 206689  Cd Length: 204  Bit Score: 46.43  E-value: 5.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   9 KVLLMGKSGSGKTSMRSIIFAN-YIARDTRRLGATIDVEHSHVRFLG----NLVLNLWDCGGQDTFMENYfTSQRDNIFR 83
Cdd:cd04102     2 KVLVLGDSGVGKSSLVHLLCKNqVLGNPSWTVGCSVDVRHHTYGEGTpeekTFYVELWDVGGSVGSAESV-KSTRAVFYN 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1229014703  84 NVEVLIYVFDVESRELEKDMhyYQSCLEAI 113
Cdd:cd04102    81 QINGIIFVHDLTNKKSSQNL--YRWSLEAL 108
Arl3 cd04155
Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most ...
 1-133 2.91e-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: 43.92  E-value: 2.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   1 MSSTAMKKKVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATI-DVEHSHVRflgnlvLNLWDCGGQDT---FMENYfts 76
Cdd:cd04155     9 KPSSRQEVRILLLGLDNAGKTTILKQLASEDISHITPTQGFNIkNVQADGFK------LNVWDIGGQRKirpYWRNY--- 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1229014703  77 qrdniFRNVEVLIYVFDVESRELEKDMHyyqSCLEAILQNSPDAKVFCLV--HKMDLVQ 133
Cdd:cd04155    80 -----FENTDVLIYVIDSADRKRFEEAG---QELVELLEEEKLAGVPVLVfaNKQDLLT 130
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 11-132 1.50e-04

YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.


Pssm-ID: 206743 [Multi-domain]  Cd Length: 140  Bit Score: 41.17  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703  11 LLMGKSGSGKTSMRSIIFANYIARDTRRLGATIDVeHSHVRFLGNLVLNLWDCGGQDtfmENYFTSQR-----DNIFRNV 85
Cdd:cd11383     1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRAA-QAYVWQTGGDGLVLLDLPGVG---ERGRRDREyeelyRRLLPEA 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1229014703  86 EVLIYVFDVESRELEKDMHYYQSCLEAilqnsPDAKVFCLVHKMDLV 132
Cdd:cd11383    77 DLVLWLLDADDRALAADHDFYLLPLAG-----HDAPLLFVLNQVDPV 118
YeeP COG3596
Predicted GTPase [General function prediction only];
10-211 2.63e-04

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 42.06  E-value: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703  10 VLLMGKSGSGKTSMRSIIFANYIARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDTFMENYFTSQR-DNIFRNVEVL 88
Cdd:COG3596    42 IALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRYRLESDGLPGLVLLDTPGLGEVNERDREYRElRELLPEADLI 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703  89 IYVFDVESRELEKDMHYYQscleAILQNSPDAKVFCLVHKMDLV---QEDQR--DLIFKEREEDLKRL----SRPLACTC 159
Cdd:COG3596   122 LWVVKADDRALATDEEFLQ----ALRAQYPDPPVLVVLTQVDRLepeREWDPpyNWPSPPKEQNIRRAleaiAEQLGVPI 197

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703 160 FR----TSIWDETLY---KAWSSIVYQLIPNVQQ-LETNLRnfAQIIEADEVLLFERATF 211
Cdd:COG3596   198 DRvipvSAAEDRTGYgleELVDALAEALPEAKRSrLARLLR--AKAIDRYTLLAAAAALL 255
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
 9-163 3.47e-04

Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases form the largest family within the Ras superfamily. There are at least 60 Rab genes in the human genome, and a number of Rab GTPases are conserved from yeast to humans. Rab GTPases are small, monomeric proteins that function as molecular switches to regulate vesicle trafficking pathways. The different Rab GTPases are localized to the cytosolic face of specific intracellular membranes, where they regulate distinct steps in membrane traffic pathways. In the GTP-bound form, Rab GTPases recruit specific sets of effector proteins onto membranes. Through their effectors, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which mask C-terminal lipid binding and promote cytosolic localization. While most unicellular organisms possess 5-20 Rab members, several have been found to possess 60 or more Rabs; for many of these Rab isoforms, homologous proteins are not found in other organisms. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Since crystal structures often lack C-terminal residues, the lipid modification site is not available for annotation in many of the CDs in the hierarchy, but is included where possible.


Pssm-ID: 206640 [Multi-domain]  Cd Length: 159  Bit Score: 40.52  E-value: 3.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   9 KVLLMGKSGSGKTsmrSII--FANYIARDTRRlgATIDVEHSH--VRFLGNLV-LNLWDCGGQDTFMenyftSQRDNIFR 83
Cdd:cd00154     2 KIVLIGDSGVGKT---SLLlrFVDNKFSENYK--STIGVDFKSktIEVDGKKVkLQIWDTAGQERFR-----SITSSYYR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703  84 NVEVLIYVFDVESRElekdmhYYQSC---LEAILQNSPDAKVFCLV-HKMDLvqEDQRDLIfkerEEDLKRLSRPLACTC 159
Cdd:cd00154    72 GAHGAILVYDVTNRE------SFENLdkwLNELKEYAPPNIPIILVgNKSDL--EDERQVS----TEEAQQFAKENGLLF 139


                  ....
gi 1229014703 160 FRTS 163
Cdd:cd00154   140 FETS 143
RocCOR cd09914
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ...
 9-130 5.48e-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: 40.01  E-value: 5.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   9 KVLLMGKSGSGKTS-----MRSIIFANYIARDtrrlGATIDVEHSHVRFLGNLVLNLWDCGGQDTFmenYFTSQrdnIF- 82
Cdd:cd09914     3 KLMLVGQGGVGKTSlckqlIGEKFDGDESSTH----GINVQDWKIPAPERKKIRLNVWDFGGQEIY---HATHQ---FFl 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1229014703  83 RNVEVLIYVFDVESRELEKDMHYYQSCLEAilqNSPDAKVFCLVHKMD 130
Cdd:cd09914    73 TSRSLYLLVFDLRTGDEVSRVPYWLRQIKA---FGGVSPVILVGTHID 117
Rho4_like cd04132
Ras homology family 4 (Rho4) of small guanosine triphosphatases (GTPases)-like; Rho4 is a ...
 7-97 6.17e-04

Ras homology family 4 (Rho4) of small guanosine triphosphatases (GTPases)-like; Rho4 is a GTPase that controls septum degradation by regulating secretion of Eng1 or Agn1 during cytokinesis. Rho4 also plays a role in cell morphogenesis. Rho4 regulates septation and cell morphology by controlling the actin cytoskeleton and cytoplasmic microtubules. The localization of Rho4 is modulated by Rdi1, which may function as a GDI, and by Rga9, which is believed to function as a GAP. In S. pombe, both Rho4 deletion and Rho4 overexpression result in a defective cell wall, suggesting a role for Rho4 in maintaining cell wall integrity. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins.


Pssm-ID: 206704 [Multi-domain]  Cd Length: 197  Bit Score: 40.02  E-value: 6.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   7 KKKVLLMGKSGSGKTSMRSI-------------IFANYIArdtrrlgaTIDVEHSHVrflgnLVLNLWDCGGQdtfmENY 73
Cdd:cd04132     3 KVKIVVVGDGGCGKTCLLMVyaqgsfpeeyvptVFENYVT--------TLQVPNGKI-----IELALWDTAGQ----EDY 65

                          90       100
                  ....*....|....*....|....
gi 1229014703  74 fTSQRDNIFRNVEVLIYVFDVESR 97
Cdd:cd04132    66 -DRLRPLSYPDVDVILICYSVDNP 88
Rab23_like cd04106
Rab GTPase family 23 (Rab23)-like; Rab23-like subfamily. Rab23 is a member of the Rab family ...
 9-167 7.38e-04

Rab GTPase family 23 (Rab23)-like; Rab23-like subfamily. Rab23 is a member of the Rab family of small GTPases. In mouse, Rab23 has been shown to function as a negative regulator in the sonic hedgehog (Shh) signaling pathway. Rab23 mediates the activity of Gli2 and Gli3, transcription factors that regulate Shh signaling in the spinal cord, primarily by preventing Gli2 activation in the absence of Shh ligand. Rab23 also regulates a step in the cytoplasmic signal transduction pathway that mediates the effect of Smoothened (one of two integral membrane proteins that are essential components of the Shh signaling pathway in vertebrates). In humans, Rab23 is expressed in the retina. Mice contain an isoform that shares 93% sequence identity with the human Rab23 and an alternative splicing isoform that is specific to the brain. This isoform causes the murine open brain phenotype, indicating it may have a role in the development of the central nervous system. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 133306 [Multi-domain]  Cd Length: 162  Bit Score: 39.35  E-value: 7.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   9 KVLLMGKSGSGKTSMRSIIFANYIARDTRRlgaTIDVEHSH----VRFLGNLV-LNLWDCGGQDTfmenyFTSQRDNIFR 83
Cdd:cd04106     2 KVIVVGNGNVGKSSMIQRFVKGIFTKDYKK---TIGVDFLEkqifLRQSDEDVrLMLWDTAGQEE-----FDAITKAYYR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703  84 NVEVLIYVFDVESRELEKDMHYYQSCLEAILQNSPdaKVFCLvHKMDLVqeDQRDLIFKEREEDLKRLSRPLactcFRTS 163
Cdd:cd04106    74 GAQACILVFSTTDRESFEAIESWKEKVEAECGDIP--MVLVQ-TKIDLL--DQAVITNEEAEALAKRLQLPL----FRTS 144


                  ....
gi 1229014703 164 IWDE 167
Cdd:cd04106   145 VKDD 148
Ras cd00876
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ...
 9-163 1.18e-03

Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the Ras superfamily includes classical N-Ras, H-Ras, and K-Ras, as well as R-Ras, Rap, Ral, Rheb, Rhes, ARHI, RERG, Rin/Rit, RSR1, RRP22, Ras2, Ras-dva, and RGK proteins. Ras proteins regulate cell growth, proliferation and differentiation. Ras is activated by guanine nucleotide exchange factors (GEFs) that release GDP and allow GTP binding. Many RasGEFs have been identified. These are sequestered in the cytosol until activation by growth factors triggers recruitment to the plasma membrane or Golgi, where the GEF colocalizes with Ras. Active GTP-bound Ras interacts with several effector proteins: among the best characterized are the Raf kinases, phosphatidylinositol 3-kinase (PI3K), RalGEFs and NORE/MST1. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206642 [Multi-domain]  Cd Length: 160  Bit Score: 39.05  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   9 KVLLMGKSGSGKTS-----MRSIIFANYIAR--DTRRLGATIDVEHSHvrflgnlvLNLWDCGGQDTFmenyfTSQRDNI 81
Cdd:cd00876     1 KLVVLGAGGVGKSAltirfVSGEFVEEYDPTieDSYRKQIVVDGETYT--------LDILDTAGQEEF-----SAMRDQY 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703  82 FRNVEVLIYVFDVESRELEKDMhyyQSCLEAILQNSPDAKVFCLV--HKMDLVqedqrdlifKERE---EDLKRLSRPLA 156
Cdd:cd00876    68 IRNGDGFILVYSITSRESFEEI---KNIREQILRVKDKEDVPIVLvgNKCDLE---------NERQvstEEGEALAEEWG 135


                  ....*..
gi 1229014703 157 CTCFRTS 163
Cdd:cd00876   136 CPFLETS 142
PLN00023 PLN00023
GTP-binding protein; Provisional
 9-97 1.48e-03

GTP-binding protein; Provisional


Pssm-ID: 177661  Cd Length: 334  Bit Score: 39.85  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   9 KVLLMGKSGSGKTSMRSIIF-ANYIARDTRRLGATIDVEHSHVRFLG------------NLVLNLWDCGGQDTFME--NY 73
Cdd:PLN00023   23 RVLVVGDSGVGKSSLVHLIVkGSSIARPPQTIGCTVGVKHITYGSPGsssnsikgdserDFFVELWDVSGHERYKDcrSL 102

                          90       100
                  ....*....|....*....|....
gi 1229014703  74 FTSQRDNIfrnvevlIYVFDVESR 97
Cdd:PLN00023  103 FYSQINGV-------IFVHDLSQR 119
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
 9-133 3.42e-03

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


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 37.59  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   9 KVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATID-VEHshvrflGNLVLNLWDCGGQDT---FMENYftsqrdniFRN 84
Cdd:pfam00025   2 RILILGLDNAGKTTILYKLKLGEIVTTIPTIGFNVEtVTY------KNVKFTVWDVGGQESlrpLWRNY--------FPN 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1229014703  85 VEVLIYVFDVESRELEKDMHyyqSCLEAILQNSPDAKVFCLV--HKMDLVQ 133
Cdd:pfam00025  68 TDAVIFVVDSADRDRIEEAK---EELHALLNEEELADAPLLIlaNKQDLPG 115
PTZ00132 PTZ00132
GTP-binding nuclear protein Ran; Provisional
 9-97 4.10e-03

GTP-binding nuclear protein Ran; Provisional


Pssm-ID: 240284 [Multi-domain]  Cd Length: 215  Bit Score: 37.75  E-value: 4.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   9 KVLLMGKSGSGKTSM--RSII--F-ANYIArdtrrlgaTIDVEHSHVRF---LGNLVLNLWDCGGQDTfmenyFTSQRDN 80
Cdd:PTZ00132   11 KLILVGDGGVGKTTFvkRHLTgeFeKKYIP--------TLGVEVHPLKFytnCGPICFNVWDTAGQEK-----FGGLRDG 77

                          90
                  ....*....|....*..
gi 1229014703  81 IFRNVEVLIYVFDVESR 97
Cdd:PTZ00132   78 YYIKGQCAIIMFDVTSR 94
Rab7 cd01862
Rab GTPase family 7 (Rab7); Rab7 subfamily. Rab7 is a small Rab GTPase that regulates ...
 9-146 4.82e-03

Rab GTPase family 7 (Rab7); Rab7 subfamily. Rab7 is a small Rab GTPase that regulates vesicular traffic from early to late endosomal stages of the endocytic pathway. The yeast Ypt7 and mammalian Rab7 are both involved in transport to the vacuole/lysosome, whereas Ypt7 is also required for homotypic vacuole fusion. Mammalian Rab7 is an essential participant in the autophagic pathway for sequestration and targeting of cytoplasmic components to the lytic compartment. Mammalian Rab7 is also proposed to function as a tumor suppressor. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206655 [Multi-domain]  Cd Length: 172  Bit Score: 37.26  E-value: 4.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   9 KVLLMGKSGSGKTSmrsiIFANYI-ARDTRRLGATI--DVEHSHVRFLGNLV-LNLWDCGGQDTFMenyftSQRDNIFRN 84
Cdd:cd01862     2 KVIILGDSGVGKTS----LMNQYVnKKFSNQYKATIgaDFLTKEVTVDDRLVtLQIWDTAGQERFQ-----SLGVAFYRG 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229014703  85 VEVLIYVFDV------ESRELEKDMHYYQSCleailQNSPDAKVFCLV-HKMDLvqEDQRDLIFKEREE 146
Cdd:cd01862    73 ADCCVLVYDVtnpksfESLDSWRDEFLIQAS-----PRDPENFPFVVLgNKIDL--EEKRQVSTKKAQQ 134
Rab39 cd04111
Rab GTPase family 39 (Rab39); Found in eukaryotes, Rab39 is mainly found in epithelial cell ...
 58-151 4.94e-03

Rab GTPase family 39 (Rab39); Found in eukaryotes, Rab39 is mainly found in epithelial cell lines, but is distributed widely in various human tissues and cell lines. It is believed to be a novel Rab protein involved in regulating Golgi-associated vesicular transport during cellular endocytosis. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins.


Pssm-ID: 133311 [Multi-domain]  Cd Length: 211  Bit Score: 37.43  E-value: 4.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703  58 LNLWDCGGQDTfmenyFTSQRDNIFRN-VEVLIyVFDVESRELEKDMHYYQSclEAILQNSPDAKVFCLV-HKMDLvqED 135
Cdd:cd04111    54 LQLWDTAGQER-----FRSITRSYYRNsVGVLL-VFDITNRESFEHVHDWLE--EARSHIQPHRPVFILVgHKCDL--ES 123

                          90
                  ....*....|....*.
gi 1229014703 136 QRDLIFKEREEDLKRL 151
Cdd:cd04111   124 QRQVTREEAEKLAKDL 139
Rab33B_Rab33A cd04115
Rab GTPase family 33 includes Rab33A and Rab33B; Rab33B/Rab33A subfamily. Rab33B is ...
 9-98 5.35e-03

Rab GTPase family 33 includes Rab33A and Rab33B; Rab33B/Rab33A subfamily. Rab33B is ubiquitously expressed in mouse tissues and cells, where it is localized to the medial Golgi cisternae. It colocalizes with alpha-mannose II. Together with the other cisternal Rabs, Rab6A and Rab6A', it is believed to regulate the Golgi response to stress and is likely a molecular target in stress-activated signaling pathways. Rab33A (previously known as S10) is expressed primarily in the brain and immune system cells. In humans, it is located on the X chromosome at Xq26 and its expression is down-regulated in tuberculosis patients. Experimental evidence suggests that Rab33A is a novel CD8+ T cell factor that likely plays a role in tuberculosis disease processes. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 133315 [Multi-domain]  Cd Length: 170  Bit Score: 37.03  E-value: 5.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   9 KVLLMGKSGSGKTSMrsiIFANYIARDTRRLGATIDVEHSH--VRFLG-NLVLNLWDCGGQDTFMEnyftSQRDNIFRNV 85
Cdd:cd04115     4 KIIVIGDSNVGKTCL---TYRFCAGRFPERTEATIGVDFRErtVEIDGeRIKVQLWDTAGQERFRK----SMVQHYYRNV 76

                          90
                  ....*....|...
gi 1229014703  86 EVLIYVFDVESRE 98
Cdd:cd04115    77 HAVVFVYDVTNMA 89
ARLTS1 cd04156
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ...
 9-131 5.69e-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: 37.01  E-value: 5.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   9 KVLLMGKSGSGKTS-MRSIIFANYIARDtrrlgATIDVEHSHVRFLGNLVLNLWDCGGQDTFMENYftsqrDNIFRNVEV 87
Cdd:cd04156     1 QVLLLGLDSAGKSTlLYKLKHAELVTTI-----PTVGFNVEMLQLEKHLSLTVWDVGGQEKMRTVW-----KCYLENTDG 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1229014703  88 LIYVFD-VESRELEKDmhyyQSCLEAILQNS--PDAKVFCLVHKMDL 131
Cdd:cd04156    71 LVYVVDsSDEARLDES----QKELKHILKNEhiKGVPVVLLANKQDL 113
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
 9-163 5.86e-03

Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 36.72  E-value: 5.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703    9 KVLLMGKSGSGKTS-MRSiiFANYIARDTRRlgATIDVEHShVRFL---GNLV-LNLWDCGGQDTfmenyFTSQRDNIFR 83
Cdd:smart00175   2 KIILIGDSGVGKSSlLSR--FTDGKFSEQYK--STIGVDFK-TKTIevdGKRVkLQIWDTAGQER-----FRSITSSYYR 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   84 NVEVLIYVFDVESRELEKDMhyyQSCLEAILQNSPDAKVFCLV-HKMDLvqEDQRDLifkeREEDLKRLSRPLACTCFRT 162
Cdd:smart00175  72 GAVGALLVYDITNRESFENL---ENWLKELREYASPNVVIMLVgNKSDL--EEQRQV----SREEAEAFAEEHGLPFFET 142


                   .
gi 1229014703  163 S 163
Cdd:smart00175 143 S 143
Rab32_Rab38 cd04107
Rab GTPase families 18 (Rab18) and 32 (Rab32); Rab38/Rab32 subfamily. Rab32 and Rab38 are ...
 9-69 6.04e-03

Rab GTPase families 18 (Rab18) and 32 (Rab32); Rab38/Rab32 subfamily. Rab32 and Rab38 are members of the Rab family of small GTPases. Human Rab32 was first identified in platelets but it is expressed in a variety of cell types, where it functions as an A-kinase anchoring protein (AKAP). Rab38 has been shown to be melanocyte-specific. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins.


Pssm-ID: 206692 [Multi-domain]  Cd Length: 201  Bit Score: 37.29  E-value: 6.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229014703   9 KVLLMGKSGSGKTsmrSII--FANYIARDTRRlgATIDVEHShVRFL----GNLV-LNLWDCGGQDTF 69
Cdd:cd04107     2 KVLVIGDLGVGKT---SIIkrYVHGVFSQHYK--ATIGVDFA-LKVIewdpNTVVrLQLWDIAGQERF 63
Rab18 cd01863
Rab GTPase family 18 (Rab18); Rab18 subfamily. Mammalian Rab18 is implicated in endocytic ...
 9-98 6.54e-03

Rab GTPase family 18 (Rab18); Rab18 subfamily. Mammalian Rab18 is implicated in endocytic transport and is expressed most highly in polarized epithelial cells. However, trypanosomal Rab, TbRAB18, is upregulated in the BSF (Blood Stream Form) stage and localized predominantly to elements of the Golgi complex. In human and mouse cells, Rab18 has been identified in lipid droplets, organelles that store neutral lipids. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206656 [Multi-domain]  Cd Length: 161  Bit Score: 36.52  E-value: 6.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703   9 KVLLMGKSGSGKTS-MRSiiFANYIARDtrRLGATIDVEHShVRFLG----NLVLNLWDCGGQDTFmeNYFTSqrdNIFR 83
Cdd:cd01863     2 KILLIGDSGVGKSSlLLR--FTDDTFDE--DLSSTIGVDFK-VKTVTvdgkKVKLAIWDTAGQERF--RTLTS---SYYR 71

                          90
                  ....*....|....*
gi 1229014703  84 NVEVLIYVFDVESRE 98
Cdd:cd01863    72 GAQGVILVYDVTRRD 86
Arl10_like cd04159
Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from ...
 12-98 8.78e-03

Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from a human cancer-derived EST dataset. No functional information about the subfamily is available at the current time, but crystal structures of human Arl10b and Arl10c have been solved.


Pssm-ID: 206724 [Multi-domain]  Cd Length: 159  Bit Score: 36.14  E-value: 8.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229014703  12 LMGKSGSGKTSMRSIIFANYIARDTRrlgATIDVEHSHVRfLGNLVLNLWDCGGQDTfmenyFTSQRDNIFRNVEVLIYV 91
Cdd:cd04159     4 LVGLQNSGKTTLVNVIASGQFSEDTI---PTVGFNMRKVT-KGNVTIKVWDLGGQPR-----FRSMWERYCRGVNAIVYV 74


                  ....*..
gi 1229014703  92 FDVESRE 98
Cdd:cd04159    75 VDAADRE 81
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH