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Conserved domains on  [gi|50741401|ref|XP_419573|]
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PREDICTED: ras-related protein Rab-4A isoform X3 [Gallus gallus]

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Rab4 cd04113
Rab GTPase family 4 (Rab4); Rab4 subfamily. Rab4 has been implicated in numerous functions ...
14-174 5.39e-118

Rab GTPase family 4 (Rab4); Rab4 subfamily. Rab4 has been implicated in numerous functions within the cell. It helps regulate endocytosis through the sorting, recycling, and degradation of early endosomes. Mammalian Rab4 is involved in the regulation of many surface proteins including G-protein-coupled receptors, transferrin receptor, integrins, and surfactant protein A. Experimental data implicate Rab4 in regulation of the recycling of internalized receptors back to the plasma membrane. It is also believed to influence receptor-mediated antigen processing in B-lymphocytes, in calcium-dependent exocytosis in platelets, in alpha-amylase secretion in pancreatic cells, and in insulin-induced translocation of Glut4 from internal vesicles to the cell surface. Rab4 is known to share effector proteins with Rab5 and Rab11. 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: 206696  Cd Length: 161  Bit Score: 335.56  E-value: 5.39e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:cd04113   1 FKFLIIGSAGTGKSCLLHQFIENKFKQDSNHTIGVEFGSRVVNVGGKSVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  94 DITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCARK 173
Cdd:cd04113  81 DITSRESFNALTNWLTDARTLASPDIVIILVGNKKDLEDDREVTFLEASRFAQENGLLFLETSALTGENVEEAFLKCARS 160

                .
gi 50741401 174 I 174
Cdd:cd04113 161 I 161
PLN03108 PLN03108
Rab family protein; Provisional
9-218 2.24e-82

Rab family protein; Provisional


:

Pssm-ID: 178655 [Multi-domain]  Cd Length: 210  Bit Score: 246.78  E-value: 2.24e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401    9 TYDFLFKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAG 88
Cdd:PLN03108   2 SYAYLFKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARMITIDNKPIKLQIWDTAGQESFRSITRSYYRGAAG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401   89 ALLVYDITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFV 168
Cdd:PLN03108  82 ALLVYDITRRETFNHLASWLEDARQHANANMTIMLIGNKCDLAHRRAVSTEEGEQFAKEHGLIFMEASAKTAQNVEEAFI 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 50741401  169 QCARKILNKIESGELDPERMGSGIQYGDAALRQLRSPRraQAQSAQECGC 218
Cdd:PLN03108 162 KTAAKIYKKIQDGVFDVSNESYGIKVGYGAIPGASGGR--DGTSSQGGGC 209
 
Name Accession Description Interval E-value
Rab4 cd04113
Rab GTPase family 4 (Rab4); Rab4 subfamily. Rab4 has been implicated in numerous functions ...
14-174 5.39e-118

Rab GTPase family 4 (Rab4); Rab4 subfamily. Rab4 has been implicated in numerous functions within the cell. It helps regulate endocytosis through the sorting, recycling, and degradation of early endosomes. Mammalian Rab4 is involved in the regulation of many surface proteins including G-protein-coupled receptors, transferrin receptor, integrins, and surfactant protein A. Experimental data implicate Rab4 in regulation of the recycling of internalized receptors back to the plasma membrane. It is also believed to influence receptor-mediated antigen processing in B-lymphocytes, in calcium-dependent exocytosis in platelets, in alpha-amylase secretion in pancreatic cells, and in insulin-induced translocation of Glut4 from internal vesicles to the cell surface. Rab4 is known to share effector proteins with Rab5 and Rab11. 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: 206696  Cd Length: 161  Bit Score: 335.56  E-value: 5.39e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:cd04113   1 FKFLIIGSAGTGKSCLLHQFIENKFKQDSNHTIGVEFGSRVVNVGGKSVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  94 DITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCARK 173
Cdd:cd04113  81 DITSRESFNALTNWLTDARTLASPDIVIILVGNKKDLEDDREVTFLEASRFAQENGLLFLETSALTGENVEEAFLKCARS 160

                .
gi 50741401 174 I 174
Cdd:cd04113 161 I 161
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
14-177 7.28e-97

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


Pssm-ID: 197555  Cd Length: 164  Bit Score: 282.09  E-value: 7.28e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401     14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:smart00175   1 FKIILIGDSGVGKSSLLSRFTDGKFSEQYKSTIGVDFKTKTIEVDGKRVKLQIWDTAGQERFRSITSSYYRGAVGALLVY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401     94 DITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCARK 173
Cdd:smart00175  81 DITNRESFENLENWLKELREYASPNVVIMLVGNKSDLEEQRQVSREEAEAFAEEHGLPFFETSAKTNTNVEEAFEELARE 160

                   ....
gi 50741401    174 ILNK 177
Cdd:smart00175 161 ILKR 164
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
15-176 6.46e-87

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: 249560  Cd Length: 162  Bit Score: 256.66  E-value: 6.46e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401    15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYD 94
Cdd:pfam00071   1 KLVLVGDGGVGKSSLLIRFTQNKFPEEYIPTIGVDFYTKTIEVDGKTVKLQIWDTAGQERFRALRPLYYRGAQGFLLVYD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401    95 ITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCARKI 174
Cdd:pfam00071  81 ITSRDSFENVKKWLEEILRHADDNVPIVLVGNKCDLEDQRVVSTEEGEALAKELGLPFMETSAKTNENVEEAFEELAREI 160

                  ..
gi 50741401   175 LN 176
Cdd:pfam00071 161 LK 162
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
14-167 1.69e-33

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: 232886  Cd Length: 162  Bit Score: 119.40  E-value: 1.69e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401    14 FKFLVIGNAGTGKSCLLHQFIEKK-FKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLV 92
Cdd:TIGR00231   2 IKIVIVGDPNVGKSTLLNRLLGNKiSITEYKPGTTRNYVTTVIEEDGKTYKFNLLDTAGQEDYDAIRRLYYRAVESSLRV 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50741401    93 YDITSR--ETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFlEASRFAQENELMFLETSALTGENVEEAF 167
Cdd:TIGR00231  82 FDIVILvlDVEEILEKQTKEIIHHAESGVPIILVGNKIDLRDAKLKTH-VAFLFAKLNGEPIIPLSAETGKNIDSAF 157
PLN03071 PLN03071
GTP-binding nuclear protein Ran; Provisional
1-185 2.18e-26

GTP-binding nuclear protein Ran; Provisional


Pssm-ID: 178620  Cd Length: 219  Bit Score: 102.14  E-value: 2.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401    1 MSQAAMSETYDFLFKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVE------FGSKiinvgGKyVKLQIWDTAGQER 74
Cdd:PLN03071   1 MALPNQQTVDYPSFKLVIVGDGGTGKTTFVKRHLTGEFEKKYEPTIGVEvhpldfFTNC-----GK-IRFYCWDTAGQEK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401   75 FRSVTRSYYRGAAGALLVYDITSRETYNALTNWLTDARMLaSQNIVIILCGNKKDLdADREVtflEASR--FAQENELMF 152
Cdd:PLN03071  75 FGGLRDGYYIHGQCAIIMFDVTARLTYKNVPTWHRDLCRV-CENIPIVLCGNKVDV-KNRQV---KAKQvtFHRKKNLQY 149
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 50741401  153 LETSALTGENVEEAFVQCARKI-----LNKIESGELDP 185
Cdd:PLN03071 150 YEISAKSNYNFEKPFLYLARKLagdpnLHFVESPALAP 187
PTZ00369 PTZ00369
Ras-like protein; Provisional
14-174 4.70e-26

Ras-like protein; Provisional


Pssm-ID: 240385  Cd Length: 189  Bit Score: 100.32  E-value: 4.70e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401   14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFgSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:PTZ00369   6 YKLVVVGGGGVGKSALTIQFIQNHFIDEYDPTIEDSY-RKQCVIDEETCLLDILDTAGQEEYSAMRDQYMRTGQGFLCVY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401   94 DITSRETYNALTNWLTDA-RMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCAR 172
Cdd:PTZ00369  85 SITSRSSFEEIASFREQIlRVKDKDRVPMILVGNKCDLDSERQVSTGEGQELAKSFGIPFLETSAKQRVNVDEAFYELVR 164

                 ..
gi 50741401  173 KI 174
Cdd:PTZ00369 165 EI 166
COG2229 COG2229
Predicted GTPase [General function prediction only]
15-166 3.18e-08

Predicted GTPase [General function prediction only]


Pssm-ID: 225138  Cd Length: 187  Bit Score: 50.54  E-value: 3.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEK------------KFKDDSNHTIGVEFGSkiINVGGKYvKLQIWDTAGQERFRSVTRSY 82
Cdd:COG2229  12 KIVVIGPVGAGKTTFVRALSDKplviteadassvSGKGKRPTTVAMDFGS--IELDEDT-GVHLFGTPGQERFKFMWEIL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  83 YRGAAGALLVYDITSRETYNAltnwLTDARMLASQNIVIILCG-NKKDL-DADREVTFLEASRFAQENELMFlETSALTG 160
Cdd:COG2229  89 SRGAVGAIVLVDSSRPITFHA----EEIIDFLTSRNPIPVVVAiNKQDLfDALPPEKIREALKLELLSVPVI-EIDATEG 163

                ....*.
gi 50741401 161 ENVEEA 166
Cdd:COG2229 164 EGARDQ 169
PLN03108 PLN03108
Rab family protein; Provisional
9-218 2.24e-82

Rab family protein; Provisional


Pssm-ID: 178655 [Multi-domain]  Cd Length: 210  Bit Score: 246.78  E-value: 2.24e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401    9 TYDFLFKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAG 88
Cdd:PLN03108   2 SYAYLFKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARMITIDNKPIKLQIWDTAGQESFRSITRSYYRGAAG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401   89 ALLVYDITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFV 168
Cdd:PLN03108  82 ALLVYDITRRETFNHLASWLEDARQHANANMTIMLIGNKCDLAHRRAVSTEEGEQFAKEHGLIFMEASAKTAQNVEEAFI 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 50741401  169 QCARKILNKIESGELDPERMGSGIQYGDAALRQLRSPRraQAQSAQECGC 218
Cdd:PLN03108 162 KTAAKIYKKIQDGVFDVSNESYGIKVGYGAIPGASGGR--DGTSSQGGGC 209
COG1100 COG1100
GTPase SAR1 and related small G proteins [General function prediction only]
14-186 3.61e-44

GTPase SAR1 and related small G proteins [General function prediction only]


Pssm-ID: 224025 [Multi-domain]  Cd Length: 219  Bit Score: 148.96  E-value: 3.61e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:COG1100   6 FKIVVLGDGGVGKTTLLNRLVGDEFPEGYPPTIGNLDPAKTIEPYRRNIKLQLWDTAGQEEYRSLRPEYYRGANGILIVY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  94 DITSRE-TYNALTNWLTDARMLASQNIVIILCGNKKDLDAD------------REVTFLEASRFAQENE---LMFLETSA 157
Cdd:COG1100  86 DSTLREsSDELTEEWLEELRELAPDDVPILLVGNKIDLFDEqssseeilnqlnREVVLLVLAPKAVLPEvanPALLETSA 165
                       170       180       190
                ....*....|....*....|....*....|.
gi 50741401 158 --LTGENVEEAFVQCARKILNKIESGELDPE 186
Cdd:COG1100 166 ksLTGPNVNELFKELLRKLLEEIEKLVLKNE 196
PTZ00099 PTZ00099
rab6; Provisional
38-176 4.93e-33

rab6; Provisional


Pssm-ID: 185444 [Multi-domain]  Cd Length: 176  Bit Score: 118.69  E-value: 4.93e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401   38 FKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYDITSRETYNALTNWLTDARMLASQ 117
Cdd:PTZ00099   5 FDNNYQSTIGIDFLSKTLYLDEGPVRLQLWDTAGQERFRSLIPSYIRDSAAAIVVYDITNRQSFENTTKWIQDILNERGK 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 50741401  118 NIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCARKILN 176
Cdd:PTZ00099  85 DVIIALVGNKTDLGDLRKVTYEEGMQKAQEYNTMFHETSAKAGHNIKVLFKKIAAKLPN 143
RAN smart00176
Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases; Ran is involved in the ...
19-175 8.18e-27

Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases; Ran is involved in the active transport of proteins through nuclear pores.


Pssm-ID: 128473 [Multi-domain]  Cd Length: 200  Bit Score: 102.78  E-value: 8.18e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401     19 IGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYDITSR 98
Cdd:smart00176   1 VGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIRFNVWDTAGQEKFGGLRDGYYIQGQCAIIMFDVTAR 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50741401     99 ETYNALTNWLTD-ARMlaSQNIVIILCGNKKDLDaDREVTfLEASRFAQENELMFLETSALTGENVEEAFVQCARKIL 175
Cdd:smart00176  81 VTYKNVPNWHRDlVRV--CENIPIVLCGNKVDVK-DRKVK-AKSITFHRKKNLQYYDISAKSNYNFEKPFLWLARKLI 154
 
Name Accession Description Interval E-value
Rab4 cd04113
Rab GTPase family 4 (Rab4); Rab4 subfamily. Rab4 has been implicated in numerous functions ...
14-174 5.39e-118

Rab GTPase family 4 (Rab4); Rab4 subfamily. Rab4 has been implicated in numerous functions within the cell. It helps regulate endocytosis through the sorting, recycling, and degradation of early endosomes. Mammalian Rab4 is involved in the regulation of many surface proteins including G-protein-coupled receptors, transferrin receptor, integrins, and surfactant protein A. Experimental data implicate Rab4 in regulation of the recycling of internalized receptors back to the plasma membrane. It is also believed to influence receptor-mediated antigen processing in B-lymphocytes, in calcium-dependent exocytosis in platelets, in alpha-amylase secretion in pancreatic cells, and in insulin-induced translocation of Glut4 from internal vesicles to the cell surface. Rab4 is known to share effector proteins with Rab5 and Rab11. 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: 206696  Cd Length: 161  Bit Score: 335.56  E-value: 5.39e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:cd04113   1 FKFLIIGSAGTGKSCLLHQFIENKFKQDSNHTIGVEFGSRVVNVGGKSVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  94 DITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCARK 173
Cdd:cd04113  81 DITSRESFNALTNWLTDARTLASPDIVIILVGNKKDLEDDREVTFLEASRFAQENGLLFLETSALTGENVEEAFLKCARS 160

                .
gi 50741401 174 I 174
Cdd:cd04113 161 I 161
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
14-177 7.28e-97

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


Pssm-ID: 197555  Cd Length: 164  Bit Score: 282.09  E-value: 7.28e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401     14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:smart00175   1 FKIILIGDSGVGKSSLLSRFTDGKFSEQYKSTIGVDFKTKTIEVDGKRVKLQIWDTAGQERFRSITSSYYRGAVGALLVY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401     94 DITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCARK 173
Cdd:smart00175  81 DITNRESFENLENWLKELREYASPNVVIMLVGNKSDLEEQRQVSREEAEAFAEEHGLPFFETSAKTNTNVEEAFEELARE 160

                   ....
gi 50741401    174 ILNK 177
Cdd:smart00175 161 ILKR 164
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
14-172 4.54e-90

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  Cd Length: 159  Bit Score: 264.32  E-value: 4.54e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:cd00154   1 FKIVLIGDSGVGKTSLLLRFVDNKFSENYKSTIGVDFKSKTIEVDGKKVKLQIWDTAGQERFRSITSSYYRGAHGAILVY 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50741401  94 DITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCAR 172
Cdd:cd00154  81 DVTNRESFENLDKWLNELKEYAPPNIPIILVGNKSDLEDERQVSTEEAQQFAKENGLLFFETSAKTGENVDEAFESLAR 159
Rab14 cd04122
Rab GTPase family 14 (Rab14); Rab14 GTPases are localized to biosynthetic compartments, ...
12-177 1.67e-88

Rab GTPase family 14 (Rab14); Rab14 GTPases are localized to biosynthetic compartments, including the rough ER, the Golgi complex, and the trans-Golgi network, and to endosomal compartments, including early endosomal vacuoles and associated vesicles. Rab14 is believed to function in both the biosynthetic and recycling pathways between the Golgi and endosomal compartments. Rab14 has also been identified on GLUT4 vesicles, and has been suggested to help regulate GLUT4 translocation. In addition, Rab14 is believed to play a role in the regulation of phagocytosis. 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: 133322  Cd Length: 166  Bit Score: 260.92  E-value: 1.67e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  12 FLFKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALL 91
Cdd:cd04122   1 YIFKYIIIGDMGVGKSCLLHQFTEKKFMADCPHTIGVEFGTRIIEVNGQKIKLQIWDTAGQERFRAVTRSYYRGAAGALM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  92 VYDITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCA 171
Cdd:cd04122  81 VYDITRRSTYNHLSSWLTDARNLTNPNTVIFLIGNKADLEAQRDVTYEEAKQFADENGLLFLECSAKTGENVEDAFLETA 160

                ....*.
gi 50741401 172 RKILNK 177
Cdd:cd04122 161 KKIYQN 166
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
15-176 6.46e-87

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: 249560  Cd Length: 162  Bit Score: 256.66  E-value: 6.46e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401    15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYD 94
Cdd:pfam00071   1 KLVLVGDGGVGKSSLLIRFTQNKFPEEYIPTIGVDFYTKTIEVDGKTVKLQIWDTAGQERFRALRPLYYRGAQGFLLVYD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401    95 ITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCARKI 174
Cdd:pfam00071  81 ITSRDSFENVKKWLEEILRHADDNVPIVLVGNKCDLEDQRVVSTEEGEALAKELGLPFMETSAKTNENVEEAFEELAREI 160

                  ..
gi 50741401   175 LN 176
Cdd:pfam00071 161 LK 162
Rab2 cd01866
Rab GTPase family 2 (Rab2); Rab2 is localized on cis-Golgi membranes and interacts with Golgi ...
10-177 6.12e-84

Rab GTPase family 2 (Rab2); Rab2 is localized on cis-Golgi membranes and interacts with Golgi matrix proteins. Rab2 is also implicated in the maturation of vesicular tubular clusters (VTCs), which are microtubule-associated intermediates in transport between the ER and Golgi apparatus. In plants, Rab2 regulates vesicle trafficking between the ER and the Golgi bodies and is important to pollen tube growth. 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: 206658  Cd Length: 168  Bit Score: 249.26  E-value: 6.12e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  10 YDFLFKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGA 89
Cdd:cd01866   1 YAYLFKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARMITIDGKQIKLQIWDTAGQESFRSITRSYYRGAAGA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  90 LLVYDITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQ 169
Cdd:cd01866  81 LLVYDITRRETFNHLTSWLEDARQHSNSNMTIMLIGNKCDLESRREVSYEEGEAFAREHGLIFMETSAKTASNVEEAFIN 160

                ....*...
gi 50741401 170 CARKILNK 177
Cdd:cd01866 161 TAKEIYDK 168
Rab11_like cd01868
Rab GTPase family 11 (Rab11)-like includes Rab11a, Rab11b, and Rab25; Rab11a, Rab11b, and ...
11-178 1.16e-78

Rab GTPase family 11 (Rab11)-like includes Rab11a, Rab11b, and Rab25; Rab11a, Rab11b, and Rab25 are closely related, evolutionary conserved Rab proteins that are differentially expressed. Rab11a is ubiquitously synthesized, Rab11b is enriched in brain and heart and Rab25 is only found in epithelia. Rab11/25 proteins seem to regulate recycling pathways from endosomes to the plasma membrane and to the trans-Golgi network. Furthermore, Rab11a is thought to function in the histamine-induced fusion of tubulovesicles containing H+, K+ ATPase with the plasma membrane in gastric parietal cells and in insulin-stimulated insertion of GLUT4 in the plasma membrane of cardiomyocytes. Overexpression of Rab25 has recently been observed in ovarian cancer and breast cancer, and has been correlated with worsened outcomes in both diseases. In addition, Rab25 overexpression has also been observed in prostate cancer, transitional cell carcinoma of the bladder, and invasive breast tumor cells. 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: 206660  Cd Length: 165  Bit Score: 235.53  E-value: 1.16e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  11 DFLFKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGAL 90
Cdd:cd01868   1 DYLFKIVLIGDSGVGKSNLLSRFTRNEFNLDSKSTIGVEFATRTIQIDGKTIKAQIWDTAGQERYRAITSAYYRGAVGAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  91 LVYDITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQc 170
Cdd:cd01868  81 LVYDITKKSTFENVERWLKELRDHADSNIVIMLVGNKSDLRHLRAVPTEEAKAFAEKNGLSFIETSALDGTNVEEAFKQ- 159

                ....*...
gi 50741401 171 arkILNKI 178
Cdd:cd01868 160 ---LLTEI 164
Rab39 cd04111
Rab GTPase family 39 (Rab39); Found in eukaryotes, Rab39 is mainly found in epithelial cell ...
14-218 2.80e-67

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: 208.46  E-value: 2.80e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVG-GKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLV 92
Cdd:cd04111   3 FRLIVIGDSTVGKSSLLKRFTEGRFAEVSDPTVGVDFFSRLIEIEpGVRIKLQLWDTAGQERFRSITRSYYRNSVGVLLV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  93 YDITSRETYNALTNWLTDARM-LASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCA 171
Cdd:cd04111  83 FDITNRESFEHVHDWLEEARShIQPHRPVFILVGHKCDLESQRQVTREEAEKLAKDLGMKYIETSARTGDNVEEAFELLT 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 50741401 172 RKILNKIESGELDPERMGSGIQYGDAALRQLRSPRRA--QAQSAQECGC 218
Cdd:cd04111 163 QEIYERIKRGELCALDGWDGVKSGFPAGRAFSLEERSptFASPEKSCCC 211
Rab8_Rab10_Rab13_like cd01867
Rab GTPase families 8, 10, 13 (Rab8, Rab10, Rab13); Rab8/Sec4/Ypt2 are known or suspected to ...
11-177 6.19e-67

Rab GTPase families 8, 10, 13 (Rab8, Rab10, Rab13); Rab8/Sec4/Ypt2 are known or suspected to be involved in post-Golgi transport to the plasma membrane. It is likely that these Rabs have functions that are specific to the mammalian lineage and have no orthologs in plants. Rab8 modulates polarized membrane transport through reorganization of actin and microtubules, induces the formation of new surface extensions, and has an important role in directed membrane transport to cell surfaces. The Ypt2 gene of the fission yeast Schizosaccharomyces pombe encodes a member of the Ypt/Rab family of small GTP-binding proteins, related in sequence to Sec4p of Saccharomyces cerevisiae but closer to mammalian Rab8. 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: 206659  Cd Length: 167  Bit Score: 205.96  E-value: 6.19e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  11 DFLFKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGAL 90
Cdd:cd01867   1 DYLFKLLLIGDSGVGKSCLLLRFSEDSFNPSFISTIGIDFKIRTIELDGKKIKLQIWDTAGQERFRTITTSYYRGAMGII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  91 LVYDITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQC 170
Cdd:cd01867  81 LVYDITDEKSFENIKNWMRNIDEHASEDVERMLVGNKCDMEEKRVVSKEEGEALAREYGIKFLETSAKANINVEEAFLTL 160

                ....*..
gi 50741401 171 ARKILNK 177
Cdd:cd01867 161 AKDILKK 167
Rab1_Ypt1 cd01869
Rab GTPase family 1 includes the yeast homolog Ypt1; Rab1/Ypt1 subfamily. Rab1 is found in ...
12-177 1.91e-66

Rab GTPase family 1 includes the yeast homolog Ypt1; Rab1/Ypt1 subfamily. Rab1 is found in every eukaryote and is a key regulatory component for the transport of vesicles from the ER to the Golgi apparatus. Studies on mutations of Ypt1, the yeast homolog of Rab1, showed that this protein is necessary for the budding of vesicles of the ER as well as for their transport to, and fusion with, the Golgi apparatus. 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: 206661  Cd Length: 166  Bit Score: 204.48  E-value: 1.91e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  12 FLFKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALL 91
Cdd:cd01869   1 YLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTVKLQIWDTAGQERFRTITSSYYRGAHGIII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  92 VYDITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCA 171
Cdd:cd01869  81 VYDVTDQESFNNVKQWLQEIDRYASENVNKLLVGNKCDLTDKKVVDYTEAKEFADELGIPFLETSAKNATNVEEAFMTMA 160

                ....*.
gi 50741401 172 RKILNK 177
Cdd:cd01869 161 REIKKR 166
Rab5_related cd01860
Rab-related GTPase family includes Rab5 and Rab22; regulates early endosome fusion; The ...
14-175 6.70e-66

Rab-related GTPase family includes Rab5 and Rab22; regulates early endosome fusion; The Rab5-related subfamily includes Rab5 and Rab22 of mammals, Ypt51/Ypt52/Ypt53 of yeast, and RabF of plants. The members of this subfamily are involved in endocytosis and endocytic-sorting pathways. In mammals, Rab5 GTPases localize to early endosomes and regulate fusion of clathrin-coated vesicles to early endosomes and fusion between early endosomes. In yeast, Ypt51p family members similarly regulate membrane trafficking through prevacuolar compartments. 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: 206653  Cd Length: 163  Bit Score: 203.17  E-value: 6.70e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:cd01860   2 FKLVLLGDSSVGKSSIVLRFVKNEFSENQESTIGAAFLTQTVNLDDTTVKFEIWDTAGQERYRSLAPMYYRGAAAAIVVY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  94 DITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCARK 173
Cdd:cd01860  82 DITSEESFEKAKSWVKELQEHGPPNIVIALAGNKADLESKRQVSTEEAQEYADENGLLFMETSAKTGENVNELFTEIARK 161

                ..
gi 50741401 174 IL 175
Cdd:cd01860 162 LP 163
Rab18 cd01863
Rab GTPase family 18 (Rab18); Rab18 subfamily. Mammalian Rab18 is implicated in endocytic ...
14-174 1.70e-61

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  Cd Length: 161  Bit Score: 191.76  E-value: 1.70e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:cd01863   1 LKILLIGDSGVGKSSLLLRFTDDTFDEDLSSTIGVDFKVKTVTVDGKKVKLAIWDTAGQERFRTLTSSYYRGAQGVILVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  94 DITSRETYNALTNWLTDARMLA-SQNIVIILCGNKKDLdADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCAR 172
Cdd:cd01863  81 DVTRRDTFDNLDTWLNELDTYStNPDAVKMLVGNKIDK-ENREVTREEGQKFARKHNMLFIETSAKTRIGVQQAFEELVE 159

                ..
gi 50741401 173 KI 174
Cdd:cd01863 160 KI 161
Rab19 cd01864
Rab GTPase family 19 (Rab19); Rab19 subfamily. Rab19 proteins are associated with Golgi stacks. ...
11-174 5.06e-60

Rab GTPase family 19 (Rab19); Rab19 subfamily. Rab19 proteins are associated with Golgi stacks. Similarity analysis indicated that Rab41 is closely related to Rab19. However, the function of these Rabs is not yet characterized. 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: 133267  Cd Length: 165  Bit Score: 188.03  E-value: 5.06e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  11 DFLFKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGAL 90
Cdd:cd01864   1 DFLFKIILIGDSNVGKTCVVQRFKSGTFSERQGNTIGVDFTMKTLEIEGKRVKLQIWDTAGQERFRTITQSYYRSANGAI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  91 LVYDITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMF-LETSALTGENVEEAFVQ 169
Cdd:cd01864  81 IAYDITRRSSFESVPHWIEEVEKYGASNVVLLLIGNKCDLEEQREVLFEEACTLAEKNGMLAvLETSAKESQNVEEAFLL 160

                ....*
gi 50741401 170 CARKI 174
Cdd:cd01864 161 MATEL 165
Rab6 cd01861
Rab GTPase family 6 (Rab6); Rab6 is involved in microtubule-dependent transport pathways ...
14-174 7.00e-58

Rab GTPase family 6 (Rab6); Rab6 is involved in microtubule-dependent transport pathways through the Golgi and from endosomes to the Golgi. Rab6A of mammals is implicated in retrograde transport through the Golgi stack, and is also required for a slow, COPI-independent, retrograde transport pathway from the Golgi to the endoplasmic reticulum (ER). This pathway may allow Golgi residents to be recycled through the ER for scrutiny by ER quality-control systems. Yeast Ypt6p, the homolog of the mammalian Rab6 GTPase, is not essential for cell viability. Ypt6p acts in endosome-to-Golgi, in intra-Golgi retrograde transport, and possibly also in Golgi-to-ER trafficking. 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: 206654  Cd Length: 161  Bit Score: 182.44  E-value: 7.00e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:cd01861   1 HKLVFLGDQSVGKTSIITRFMYDTFDNQYQATIGIDFLSKTMYVDDKTVRLQLWDTAGQERFRSLIPSYIRDSSVAVVVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  94 DITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCARK 173
Cdd:cd01861  81 DITNRQSFDNTDKWIDDVRDERGNDVIIVLVGNKTDLSDKRQVSTEEGEKKAKENNAMFIETSAKAGHNVKQLFKKIAQA 160

                .
gi 50741401 174 I 174
Cdd:cd01861 161 L 161
Rab30 cd04114
Rab GTPase family 30 (Rab30); Rab30 subfamily. Rab30 appears to be associated with the Golgi ...
8-175 1.54e-57

Rab GTPase family 30 (Rab30); Rab30 subfamily. Rab30 appears to be associated with the Golgi stack. It is expressed in a wide variety of tissue types and in humans maps to chromosome 11. 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: 133314  Cd Length: 169  Bit Score: 182.02  E-value: 1.54e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401   8 ETYDFLFKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAA 87
Cdd:cd04114   2 EDYDFLFKIVLIGNAGVGKTCLVRRFTQGLFPPGQGATIGVDFMIKTVEIKGEKIKLQIWDTAGQERFRSITQSYYRSAN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  88 GALLVYDITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAF 167
Cdd:cd04114  82 ALILTYDITCEESFRCLPEWLREIEQYANNKVITILVGNKIDLAERREVSQQRAEEFSDAQDMYYLETSAKESDNVEKLF 161

                ....*...
gi 50741401 168 VQCARKIL 175
Cdd:cd04114 162 LDLACRLI 169
Rab7 cd01862
Rab GTPase family 7 (Rab7); Rab7 subfamily. Rab7 is a small Rab GTPase that regulates ...
14-177 2.92e-49

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  Cd Length: 172  Bit Score: 160.52  E-value: 2.92e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:cd01862   1 LKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVTVDDRLVTLQIWDTAGQERFQSLGVAFYRGADCCVLVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  94 DITSRETYNALTNWLTDARMLASQN------IVIIlcGNKKDLDADREVTFLEASRFAQENELM-FLETSALTGENVEEA 166
Cdd:cd01862  81 DVTNPKSFESLDSWRDEFLIQASPRdpenfpFVVL--GNKIDLEEKRQVSTKKAQQWCKSKGNIpYFETSAKEAINVDQA 158
                       170
                ....*....|.
gi 50741401 167 FVQCARKILNK 177
Cdd:cd01862 159 FETIARLALEQ 169
Rab26 cd04112
Rab GTPase family 26 (Rab26); Rab26 subfamily. First identified in rat pancreatic acinar cells, ...
14-174 1.88e-46

Rab GTPase family 26 (Rab26); Rab26 subfamily. First identified in rat pancreatic acinar cells, Rab26 is believed to play a role in recruiting mature granules to the plasma membrane upon beta-adrenergic stimulation. Rab26 belongs to the Rab functional group III, which are considered key regulators of intracellular vesicle transport during exocytosis. 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: 206695  Cd Length: 191  Bit Score: 153.87  E-value: 1.88e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDS-NHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLV 92
Cdd:cd04112   1 FKVMLVGDSGVGKTCLLVRFKDGAFLAGSfIATVGIQFTNKVVTVDGVKVKLQIWDTAGQERFRSVTHAYYRDAHALLLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  93 YDITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCAR 172
Cdd:cd04112  81 YDVTNKSSFDNIRAWLTEILEYAQSDVVIMLLGNKADMSGERVVKREDGERLAKEYGVPFMETSAKTGLNVELAFTAVAK 160

                ..
gi 50741401 173 KI 174
Cdd:cd04112 161 EL 162
Rab21 cd04123
Rab GTPase family 21 (Rab21); The localization and function of Rab21 are not clearly defined, ...
14-175 6.13e-46

Rab GTPase family 21 (Rab21); The localization and function of Rab21 are not clearly defined, with conflicting data reported. Rab21 has been reported to localize in the ER in human intestinal epithelial cells, with partial colocalization with alpha-glucosidase, a late endosomal/lysosomal marker. More recently, Rab21 was shown to colocalize with and affect the morphology of early endosomes. In Dictyostelium, GTP-bound Rab21, together with two novel LIM domain proteins, LimF and ChLim, has been shown to regulate phagocytosis. 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: 133323  Cd Length: 162  Bit Score: 151.61  E-value: 6.13e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:cd04123   1 FKVVLLGEGRVGKTSLVLRYVENKFNEKHESTTQASFFQKTVNIGGKRIDLAIWDTAGQERYHALGPIYYRDADGAILVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  94 DITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCARK 173
Cdd:cd04123  81 DITDADSFQKVKKWIKELKQMRGNNISLVIVGNKIDLERQRVVSKSEAEEYAKSVGAKHFETSAKTGKGIEELFLSLAKR 160

                ..
gi 50741401 174 IL 175
Cdd:cd04123 161 MI 162
Rab12 cd04120
Rab GTPase family 12 (Rab12); Rab12 was first identified in canine cells, where it was ...
17-178 6.49e-46

Rab GTPase family 12 (Rab12); Rab12 was first identified in canine cells, where it was localized to the Golgi complex. The specific function of Rab12 remains unknown, and inconsistent results about its cellular localization have been reported. More recent studies have identified Rab12 associated with post-Golgi vesicles, or with other small vesicle-like structures but not with the Golgi complex. 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. 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: 206699 [Multi-domain]  Cd Length: 202  Bit Score: 152.86  E-value: 6.49e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  17 LVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYDIT 96
Cdd:cd04120   4 IIIGSRGVGKTSLMERFTDDTFCEACKSTVGVDFKIKTVELRGKKIRLQIWDTAGQERFNSITSAYYRSAKGIILVYDIT 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  97 SRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELM-FLETSALTGENVEEAFVQCARKIL 175
Cdd:cd04120  84 KKETFDDLPKWMKMIDKYASEDAELLLVGNKLDCETDREITRQQGEKFAQQITGMrFCEASAKDNFNVDEIFLKLVDDIL 163

                ...
gi 50741401 176 NKI 178
Cdd:cd04120 164 KKM 166
Rab32_Rab38 cd04107
Rab GTPase families 18 (Rab18) and 32 (Rab32); Rab38/Rab32 subfamily. Rab32 and Rab38 are ...
14-192 1.53e-45

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: 152.08  E-value: 1.53e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINV-GGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLV 92
Cdd:cd04107   1 FKVLVIGDLGVGKTSIIKRYVHGVFSQHYKATIGVDFALKVIEWdPNTVVRLQLWDIAGQERFGGMTRVYYKGAVGAIIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  93 YDITSRETYNALTNWLTD----ARMLASQNIVIILCGNKKDLDADRE-VTFLEASRFAQENELM-FLETSALTGENVEEA 166
Cdd:cd04107  81 FDVTRPSTFEAVLKWKADldskVTLPNGEPIPALLLANKCDLKKERLaKDPEQMDQFCKENGFIgWFETSAKENINIEEA 160
                       170       180
                ....*....|....*....|....*.
gi 50741401 167 FVQCARKILNKIESGELDPERMGSGI 192
Cdd:cd04107 161 MRFLVKNILKNDKGLQSPEPDEDNVI 186
Rab35 cd04110
Rab GTPase family 35 (Rab35); Rab35 is one of several Rab proteins to be found to participate ...
10-175 1.54e-45

Rab GTPase family 35 (Rab35); Rab35 is one of several Rab proteins to be found to participate in the regulation of osteoclast cells in rats. In addition, Rab35 has been identified as a protein that interacts with nucleophosmin-anaplastic lymphoma kinase (NPM-ALK) in human cells. Overexpression of NPM-ALK is a key oncogenic event in some anaplastic large-cell lymphomas; since Rab35 interacts with N|PM-ALK, it may provide a target for cancer treatments. 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: 133310 [Multi-domain]  Cd Length: 199  Bit Score: 151.93  E-value: 1.54e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  10 YDFLFKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGA 89
Cdd:cd04110   3 YDHLFKLLIIGDSGVGKSSLLLRFADNTFSGSYITTIGVDFKIRTVEINGERVKLQIWDTAGQERFRTITSTYYRGTHGV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  90 LLVYDITSRETYNALTNWLTDARmlasQN---IVIILCGNKKDlDADREVTFLE-ASRFAQENELMFLETSALTGENVEE 165
Cdd:cd04110  83 IVVYDVTNGESFVNVKRWLQEIE----QNcddVCKVLVGNKND-DPERKVVETEdAYKFAGQMGISLFETSAKENINVEE 157
                       170
                ....*....|
gi 50741401 166 AFVQCARKIL 175
Cdd:cd04110 158 MFNCITELVL 167
Rab15 cd04117
Rab GTPase family 15 (Rab15); Rab15 colocalizes with the transferrin receptor in early ...
14-175 2.54e-44

Rab GTPase family 15 (Rab15); Rab15 colocalizes with the transferrin receptor in early endosome compartments, but not with late endosomal markers. It codistributes with Rab4 and Rab5 on early/sorting endosomes, and with Rab11 on pericentriolar recycling endosomes. It is believed to function as an inhibitory GTPase that regulates distinct steps in early endocytic trafficking. 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: 206698  Cd Length: 164  Bit Score: 147.82  E-value: 2.54e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:cd04117   1 FRLLLIGDSGVGKTCLLCRFTDNEFHSSHISTIGVDFKMKTIEVDGIKVRIQIWDTAGQERYQTITKQYYRRAQGIFLVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  94 DITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCARK 173
Cdd:cd04117  81 DISSERSYQHIMKWVSDVDEYAPEGVQKILIGNKADEEQKRQVGDEQGNKLAKEYGMDFFETSACTNKNIKESFTRLTEL 160

                ..
gi 50741401 174 IL 175
Cdd:cd04117 161 VL 162
Rab27A cd04127
Rab GTPase family 27a (Rab27a); The Rab27a subfamily consists of Rab27a and its highly ...
10-166 3.50e-43

Rab GTPase family 27a (Rab27a); The Rab27a subfamily consists of Rab27a and its highly homologous isoform, Rab27b. Unlike most Rab proteins whose functions remain poorly defined, Rab27a has many known functions. Rab27a has multiple effector proteins, and depending on which effector it binds, Rab27a has different functions as well as tissue distribution and/or cellular localization. Putative functions have been assigned to Rab27a when associated with the effector proteins Slp1, Slp2, Slp3, Slp4, Slp5, DmSlp, rabphilin, Dm/Ce-rabphilin, Slac2-a, Slac2-b, Slac2-c, Noc2, JFC1, and Munc13-4. Rab27a has been associated with several human diseases, including hemophagocytic syndrome (Griscelli syndrome or GS), Hermansky-Pudlak syndrome, and choroidermia. In the case of GS, a rare, autosomal recessive disease, a Rab27a mutation is directly responsible for the disorder. When Rab27a is localized to the secretory granules of pancreatic beta cells, it is believed to mediate glucose-stimulated insulin secretion, making it a potential target for diabetes therapy. When bound to JFC1 in prostate cells, Rab27a is believed to regulate the exocytosis of prostate- specific markers. 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: 206700  Cd Length: 180  Bit Score: 145.34  E-value: 3.50e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  10 YDFLFKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKII--------NVGGK--YVKLQIWDTAGQERFRSVT 79
Cdd:cd04127   1 YDYLIKLLALGDSGVGKTTFLYRYTDNKFNPKFITTVGIDFREKRVvynsqgpdGTSGKafRVHLQLWDTAGQERFRSLT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  80 RSYYRGAAGALLVYDITSRETYNALTNWLTDARMLA-SQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSAL 158
Cdd:cd04127  81 TAFFRDAMGFLLMFDLTSEQSFLNVRNWMSQLQAHAyCENPDIVLIGNKADLPDQREVSERQARELADKYGIPYFETSAA 160

                ....*...
gi 50741401 159 TGENVEEA 166
Cdd:cd04127 161 TGQNVEKA 168
Ras cd00876
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ...
15-174 6.10e-43

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  Cd Length: 160  Bit Score: 143.82  E-value: 6.10e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGvEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYD 94
Cdd:cd00876   1 KLVVLGAGGVGKSALTIRFVSGEFVEEYDPTIE-DSYRKQIVVDGETYTLDILDTAGQEEFSAMRDQYIRNGDGFILVYS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  95 ITSRETYNALTNWLTD-ARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCARK 173
Cdd:cd00876  80 ITSRESFEEIKNIREQiLRVKDKEDVPIVLVGNKCDLENERQVSTEEGEALAEEWGCPFLETSAKTNINIDELFNTLVRE 159

                .
gi 50741401 174 I 174
Cdd:cd00876 160 I 160
Rab33B_Rab33A cd04115
Rab GTPase family 33 includes Rab33A and Rab33B; Rab33B/Rab33A subfamily. Rab33B is ...
14-174 7.32e-43

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  Cd Length: 170  Bit Score: 144.12  E-value: 7.32e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFR-SVTRSYYRGAAGALLV 92
Cdd:cd04115   3 FKIIVIGDSNVGKTCLTYRFCAGRFPERTEATIGVDFRERTVEIDGERIKVQLWDTAGQERFRkSMVQHYYRNVHAVVFV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  93 YDITSRETYNALTNWLTDARMLASQNIVI-ILCGNKKDLDADREVTFLEASRFAQENELMFLETSA---LTGENVEEAFV 168
Cdd:cd04115  83 YDVTNMASFHSLPSWIEECEQHSLPNEVPrILVGNKCDLREQIQVPTDLAQRFADAHSMPLFETSAkdpSENDHVEAIFM 162

                ....*.
gi 50741401 169 QCARKI 174
Cdd:cd04115 163 TLAHKL 168
RJL cd04119
Rab GTPase family J-like (RabJ-like); RJLs are found in many protists and as chimeras with ...
15-167 2.91e-42

Rab GTPase family J-like (RabJ-like); RJLs are found in many protists and as chimeras with C-terminal DNAJ domains in deuterostome metazoa. They are not found in plants, fungi, and protostome metazoa, suggesting a horizontal gene transfer between protists and deuterostome metazoa. RJLs lack any known membrane targeting signal and contain a degenerate phosphate/magnesium-binding 3 (PM3) motif, suggesting an impaired ability to hydrolyze GTP. 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.


Pssm-ID: 133319  Cd Length: 168  Bit Score: 142.49  E-value: 2.91e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYD 94
Cdd:cd04119   2 KVISMGNSGVGKSCIIKRYCEGRFVSKYLPTIGIDYGVKKVSVRNKEVRVNFFDLSGHPEYLEVRNEFYKDTQGVLLVYD 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50741401  95 ITSRETYNALTNWLTDA-----RMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAF 167
Cdd:cd04119  82 VTDRQSFEALDSWLKEMkqeggPHGNMENIVVVVCANKIDLTKHRAVSEDEGRLWAESKGFKYFETSACTGEGVNEMF 159
Rab3 cd01865
Rab GTPase family 3 contains Rab3A, Rab3B, Rab3C and Rab3D; The Rab3 subfamily contains Rab3A, ...
13-177 3.09e-41

Rab GTPase family 3 contains Rab3A, Rab3B, Rab3C and Rab3D; The Rab3 subfamily contains Rab3A, Rab3B, Rab3C, and Rab3D. All four isoforms were found in mouse brain and endocrine tissues, with varying levels of expression. Rab3A, Rab3B, and Rab3C localized to synaptic and secretory vesicles; Rab3D was expressed at high levels only in adipose tissue, exocrine glands, and the endocrine pituitary, where it is localized to cytoplasmic secretory granules. Rab3 appears to control Ca2+-regulated exocytosis. The appropriate GDP/GTP exchange cycle of Rab3A is required for Ca2+-regulated exocytosis to occur, and interaction of the GTP-bound form of Rab3A with effector molecule(s) is widely believed to be essential for this process. Functionally, most studies point toward a role for Rab3 in the secretion of hormones and neurotransmitters. 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: 206657  Cd Length: 165  Bit Score: 139.66  E-value: 3.09e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  13 LFKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLV 92
Cdd:cd01865   1 MFKLLIIGNSSVGKTSFLFRYADDSFTSAFVSTVGIDFKVKTVYRNDKRIKLQIWDTAGQERYRTITTAYYRGAMGFILM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  93 YDITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCAR 172
Cdd:cd01865  81 YDITNEESFNAVQDWSTQIKTYSWDNAQVILVGNKCDMEDERVVSAERGRQLADQLGFEFFEASAKENINVKQVFERLVD 160

                ....*
gi 50741401 173 KILNK 177
Cdd:cd01865 161 IICDK 165
small_GTPase smart00010
Small GTPase of the Ras superfamily; ill-defined subfamily; SMART predicts Ras-like small ...
14-174 5.67e-36

Small GTPase of the Ras superfamily; ill-defined subfamily; SMART predicts Ras-like small GTPases of the ARF, RAB, RAN, RAS, and SAR subfamilies. Others that could not be classified in this way are predicted to be members of the small GTPase superfamily without predictions of the subfamily.


Pssm-ID: 197466  Cd Length: 166  Bit Score: 126.14  E-value: 5.67e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401     14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGvEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:smart00010   3 YKLVVLGGGGVGKSALTIQFVQGHFVDEYDPTIE-DSYRKQIEIDGEVCLLDILDTAGQEEFSAMRDQYMRTGEGFLLVY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401     94 DITSRETYNALTNWLTD-ARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCAR 172
Cdd:smart00010  82 SITDRQSFEEIAKFREQiLRVKDRDDVPIVLVGNKCDLENERVVSTEEGKELARQWGCPFLETSAKERINVDEAFYDLVR 161

                   ..
gi 50741401    173 KI 174
Cdd:smart00010 162 EI 163
RAS smart00173
Ras subfamily of RAS small GTPases; Similar in fold and function to the bacterial EF-Tu GTPase. ...
14-174 7.33e-36

Ras subfamily of RAS small GTPases; Similar in fold and function to the bacterial EF-Tu GTPase. p21Ras couples receptor Tyr kinases and G protein receptors to protein kinase cascades


Pssm-ID: 214541  Cd Length: 164  Bit Score: 125.75  E-value: 7.33e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401     14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGvEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:smart00173   1 YKLVVLGSGGVGKSALTIQFIQGHFVDDYDPTIE-DSYRKQIEIDGEVCLLDILDTAGQEEFSAMRDQYMRTGEGFLLVY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401     94 DITSRETYNALTNWLTD-ARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCAR 172
Cdd:smart00173  80 SITDRQSFEEIKKFREQiLRVKDRDDVPIVLVGNKCDLESERVVSTEEGKELARQWGCPFLETSAKERVNVDEAFYDLVR 159

                   ..
gi 50741401    173 KI 174
Cdd:smart00173 160 EI 161
Rab40 cd04121
Rab GTPase family 40 (Rab40) contains Rab40a, Rab40b and Rab40c; The Rab40 subfamily contains ...
8-177 2.88e-35

Rab GTPase family 40 (Rab40) contains Rab40a, Rab40b and Rab40c; The Rab40 subfamily contains Rab40a, Rab40b, and Rab40c, which are all highly homologous. In rat, Rab40c is localized to the perinuclear recycling compartment (PRC), and is distributed in a tissue-specific manor, with high expression in brain, heart, kidney, and testis, low expression in lung and liver, and no expression in spleen and skeletal muscle. Rab40c is highly expressed in differentiated oligodendrocytes but minimally expressed in oligodendrocyte progenitors, suggesting a role in the vesicular transport of myelin components. Unlike most other Ras-superfamily proteins, Rab40c was shown to have a much lower affinity for GTP, and an affinity for GDP that is lower than for GTP. 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: 133321 [Multi-domain]  Cd Length: 189  Bit Score: 125.05  E-value: 2.88e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401   8 ETYDFLFKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAA 87
Cdd:cd04121   1 KAYDYLLKFLLVGDSDVGKGEILASLQDGSTESPYGYNMGIDYKTTTILLDGRRVKLQLWDTSGQGRFCTIFRSYSRGAQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  88 GALLVYDITSRETYNALTNWLTDARMLASqNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAF 167
Cdd:cd04121  81 GIILVYDITNRWSFDGIDRWIKEIDEHAP-GVPKILVGNRLHLAFKRQVATEQAQAYAERNGMTFFEVSPLCNFNITESF 159
                       170
                ....*....|
gi 50741401 168 VQCARKILNK 177
Cdd:cd04121 160 TELARIVLMR 169
Rab9 cd04116
Rab GTPase family 9 (Rab9); Rab9 is found in late endosomes, together with mannose 6-phosphate ...
13-174 3.63e-35

Rab GTPase family 9 (Rab9); Rab9 is found in late endosomes, together with mannose 6-phosphate receptors (MPRs) and the tail-interacting protein of 47 kD (TIP47). Rab9 is a key mediator of vesicular transport from late endosomes to the trans-Golgi network (TGN) by redirecting the MPRs. Rab9 has been identified as a key component for the replication of several viruses, including HIV1, Ebola, Marburg, and measles, making it a potential target for inhibiting a variety of viruses. 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: 206697  Cd Length: 170  Bit Score: 124.22  E-value: 3.63e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  13 LFKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLV 92
Cdd:cd04116   5 LLKVILLGDGGVGKSSLMNRYVTNKFDTQLFHTIGVEFLNKDLEVDGHFVTLQIWDTAGQERFRSLRTPFYRGSDCCLLT 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  93 YDITSRETYNALTNW----LTDARMLASQNIVIILCGNKKDLdADREVTFLEASRFAQENELM-FLETSALTGENVEEAF 167
Cdd:cd04116  85 FSVDDSQSFQNLSNWkkefIYYADVKEPESFPFVILGNKIDI-PERQVSTEEAQAWCRDNGDYpYFETSAKDATNVAAAF 163

                ....*..
gi 50741401 168 VQCARKI 174
Cdd:cd04116 164 EEAVRRV 170
Rab23_like cd04106
Rab GTPase family 23 (Rab23)-like; Rab23-like subfamily. Rab23 is a member of the Rab family ...
15-173 1.30e-34

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  Cd Length: 162  Bit Score: 122.16  E-value: 1.30e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSK--IINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLV 92
Cdd:cd04106   2 KVIVVGNGNVGKSSMIQRFVKGIFTKDYKKTIGVDFLEKqiFLRQSDEDVRLMLWDTAGQEEFDAITKAYYRGAQACILV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  93 YDITSRETYNALTNWLTDARMLASqNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCAR 172
Cdd:cd04106  82 FSTTDRESFEAIESWKEKVEAECG-DIPMVLVQTKIDLLDQAVITNEEAEALAKRLQLPLFRTSVKDDFNVTELFEYLAE 160

                .
gi 50741401 173 K 173
Cdd:cd04106 161 K 161
Rab24 cd04118
Rab GTPase family 24 (Rab24); Rab24 is distinct from other Rabs in several ways. It exists ...
15-171 6.14e-34

Rab GTPase family 24 (Rab24); Rab24 is distinct from other Rabs in several ways. It exists primarily in the GTP-bound state, having a low intrinsic GTPase activity; it is not efficiently geranyl-geranylated at the C-terminus; it does not form a detectable complex with Rab GDP-dissociation inhibitors (GDIs); and it has recently been shown to undergo tyrosine phosphorylation when overexpressed in vitro. The specific function of Rab24 still remains unknown. It is found in a transport route between ER-cis-Golgi and late endocytic compartments. It is putatively involved in an autophagic pathway, possibly directing misfolded proteins in the ER to degradative pathways. 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: 133318  Cd Length: 193  Bit Score: 121.51  E-value: 6.14e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNH-TIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:cd04118   2 KVVMLGKESVGKTSLVERYVHHRFLVGPYQnTIGAAFVAKRMVVGERVVTLGIWDTAGSERYEAMSRIYYRGAKAAIVCY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  94 DITSRETYNALTNWLTDARMLaSQNIVIILCGNKKDL---DAD-REVTFLEASRFAQENELMFLETSALTGENVEEAFVQ 169
Cdd:cd04118  82 DLTDSSSFERAKFWVKELQNL-EEHCKIYLCGTKSDLieqDRSlRQVDFHDVQDFADEIKAQHFETSSKTGQNVDELFQK 160

                ..
gi 50741401 170 CA 171
Cdd:cd04118 161 VA 162
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
14-167 1.69e-33

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: 232886  Cd Length: 162  Bit Score: 119.40  E-value: 1.69e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401    14 FKFLVIGNAGTGKSCLLHQFIEKK-FKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLV 92
Cdd:TIGR00231   2 IKIVIVGDPNVGKSTLLNRLLGNKiSITEYKPGTTRNYVTTVIEEDGKTYKFNLLDTAGQEDYDAIRRLYYRAVESSLRV 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50741401    93 YDITSR--ETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFlEASRFAQENELMFLETSALTGENVEEAF 167
Cdd:TIGR00231  82 FDIVILvlDVEEILEKQTKEIIHHAESGVPIILVGNKIDLRDAKLKTH-VAFLFAKLNGEPIIPLSAETGKNIDSAF 157
RalA_RalB cd04139
Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily ...
14-174 1.46e-32

Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily consists of the highly homologous RalA and RalB. Ral proteins are believed to play a crucial role in tumorigenesis, metastasis, endocytosis, and actin cytoskeleton dynamics. Despite their high sequence similarity (>80% sequence identity), nonoverlapping and opposing functions have been assigned to RalA and RalBs in tumor migration. In human bladder and prostate cancer cells, RalB promotes migration while RalA inhibits it. A Ral-specific set of GEFs has been identified that are activated by Ras binding. This RalGEF activity is enhanced by Ras binding to another of its target proteins, phosphatidylinositol 3-kinase (PI3K). Ral effectors include RLIP76/RalBP1, a Rac/cdc42 GAP, and the exocyst (Sec6/8) complex, a heterooctomeric protein complex that is involved in tethering vesicles to specific sites on the plasma membrane prior to exocytosis. In rat kidney cells, RalB is required for functional assembly of the exocyst and for localizing the exocyst to the leading edge of migrating cells. In human cancer cells, RalA is required to support anchorage-independent proliferation and RalB is required to suppress apoptosis. RalA has been shown to localize to the plasma membrane while RalB is localized to the intracellular vesicles. 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: 206710  Cd Length: 163  Bit Score: 117.14  E-value: 1.46e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFgSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:cd04139   1 HKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSY-RKKVVLDGEEVQLNILDTAGQEDYAAIRDNYFRSGEGFLLVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  94 DITSRETYNALTN-WLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCAR 172
Cdd:cd04139  80 SITDMESFTALAEfREQILRVKEDDNVPLLLVGNKCDLEDKRQVSVEEAANLAEQWGVNYVETSAKTRANVDKVFFDLVR 159

                ..
gi 50741401 173 KI 174
Cdd:cd04139 160 EI 161
Ran cd00877
Ras-related nuclear proteins (Ran)/TC4 family of small GTPases; Ran GTPase is involved in ...
14-178 5.82e-32

Ras-related nuclear proteins (Ran)/TC4 family of small GTPases; Ran GTPase is involved in diverse biological functions, such as nuclear transport, spindle formation during mitosis, DNA replication, and cell division. Among the Ras superfamily, Ran is a unique small G protein. It does not have a lipid modification motif at the C-terminus to bind to the membrane, which is often observed within the Ras superfamily. Ran may therefore interact with a wide range of proteins in various intracellular locations. Like other GTPases, Ran exists in GTP- and GDP-bound conformations that interact differently with effectors. Conversion between these forms and the assembly or disassembly of effector complexes requires the interaction of regulator proteins. The intrinsic GTPase activity of Ran is very low, but it is greatly stimulated by a GTPase-activating protein (RanGAP1) located in the cytoplasm. By contrast, RCC1, a guanine nucleotide exchange factor that generates RanGTP, is bound to chromatin and confined to the nucleus. Ran itself is mobile and is actively imported into the nucleus by a mechanism involving NTF-2. Together with the compartmentalization of its regulators, this is thought to produce a relatively high concentration of RanGTP in the nucleus.


Pssm-ID: 206643  Cd Length: 166  Bit Score: 115.48  E-value: 5.82e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:cd00877   1 FKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLDFHTNRGKIRFNVWDTAGQEKFGGLRDGYYIQGQCAIIMF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  94 DITSRETYNALTNWLTDARMLaSQNIVIILCGNKKDLdADREVtflEAS--RFAQENELMFLETSALTGENVEEAFVQCA 171
Cdd:cd00877  81 DVTSRVTYKNVPNWHRDLVRV-CENIPIVLCGNKVDI-KDRKV---KPKqiTFHRKKNLQYYEISAKSNYNFEKPFLWLA 155

                ....*..
gi 50741401 172 RKILNKI 178
Cdd:cd00877 156 RKLLGNP 162
M_R_Ras_like cd04145
R-Ras2/TC21, M-Ras/R-Ras3; The M-Ras/R-Ras-like subfamily contains R-Ras2/TC21, M-Ras/R-Ras3, ...
14-174 1.38e-31

R-Ras2/TC21, M-Ras/R-Ras3; The M-Ras/R-Ras-like subfamily contains R-Ras2/TC21, M-Ras/R-Ras3, and related members of the Ras family. M-Ras is expressed in lympho-hematopoetic cells. It interacts with some of the known Ras effectors, but appears to also have its own effectors. Expression of mutated M-Ras leads to transformation of several types of cell lines, including hematopoietic cells, mammary epithelial cells, and fibroblasts. Overexpression of M-Ras is observed in carcinomas from breast, uterus, thyroid, stomach, colon, kidney, lung, and rectum. In addition, expression of a constitutively active M-Ras mutant in murine bone marrow induces a malignant mast cell leukemia that is distinct from the monocytic leukemia induced by H-Ras. TC21, along with H-Ras, has been shown to regulate the branching morphogenesis of ureteric bud cell branching in mice. 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: 133345  Cd Length: 164  Bit Score: 114.43  E-value: 1.38e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFgSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:cd04145   3 YKLVVVGGGGVGKSALTIQFIQSYFVTDYDPTIEDSY-TKQCEIDGQWAILDILDTAGQEEFSAMREQYMRTGEGFLLVF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  94 DITSRETYNALTNWLTDA-RMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCAR 172
Cdd:cd04145  82 SVTDRGSFEEVDKFHTQIlRVKDRDEFPMILVGNKADLEHQRKVSREEGQELARKLKIPYIETSAKDRLNVDKAFHDLVR 161

                ..
gi 50741401 173 KI 174
Cdd:cd04145 162 VI 163
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
17-172 8.15e-31

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: 112.16  E-value: 8.15e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  17 LVIGNAGTGKSCLLHQFIEKKFKDDSN---HTIGVEFGSKIINVGGkyVKLQIWDTAGQERF-----RSVTRSYYRGAAG 88
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVGEVSDvpgTTRDPDVYVKELDKGK--VKLVLVDTPGLDEFgglgrEELARLLLRGADL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  89 ALLVYDITSRET-YNALTNWLtdaRMLASQNIVIILCGNKKDLDADREVTFLEASRF-AQENELMFLETSALTGENVEEA 166
Cdd:cd00882  79 ILLVVDSTDRESeEDAKLLIL---RRLRKEGIPIILVGNKIDLLEEREVEELLRLEElAKILGVPVFEVSAKTGEGVDEL 155

                ....*.
gi 50741401 167 FVQCAR 172
Cdd:cd00882 156 FEKLIE 161
Rab28 cd04109
Rab GTPase family 28 (Rab28); Rab28 subfamily. First identified in maize, Rab28 has been shown ...
14-184 7.06e-30

Rab GTPase family 28 (Rab28); Rab28 subfamily. First identified in maize, Rab28 has been shown to be a late embryogenesis-abundant (Lea) protein that is regulated by the plant hormone abcisic acid (ABA). In Arabidopsis, Rab28 is expressed during embryo development and is generally restricted to provascular tissues in mature embryos. Unlike maize Rab28, it is not ABA-inducible. Characterization of the human Rab28 homolog revealed two isoforms, which differ by a 95-base pair insertion, producing an alternative sequence for the 30 amino acids at the C-terminus. The two human isoforms are presumably the result of alternative splicing. Since they differ at the C-terminus but not in the GTP-binding region, they are predicted to be targeted to different cellular locations. 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: 206694 [Multi-domain]  Cd Length: 213  Bit Score: 111.43  E-value: 7.06e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINV-GGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLV 92
Cdd:cd04109   1 IKIVVLGDGASGKTSLIRRFAQEGFGKSYKQTIGLDFFSRRITLpGSLNVTLQVWDIGGQQIGGKMLDKYIYGAQAVCLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  93 YDITSRETYNALTNWLTDARMLASQNIV---IILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQ 169
Cdd:cd04109  81 YDITNSQSFENLEDWLSVVKKVNEESETkpkMVLVGNKTDLEHNRQVTAEKHARFAQENDMESIFVSAKTGDRVFLCFQR 160
                       170
                ....*....|....*.
gi 50741401 170 CARKILN-KIESGELD 184
Cdd:cd04109 161 IAAELLGvKLSQAELE 176
Rap2 cd04176
Rap2 family GTPase consists of Rap2a, Rap2b, and Rap2c; The Rap2 subgroup is part of the Rap ...
14-175 4.85e-29

Rap2 family GTPase consists of Rap2a, Rap2b, and Rap2c; The Rap2 subgroup is part of the Rap subfamily of the Ras family. It consists of Rap2a, Rap2b, and Rap2c. Both isoform 3 of the human mitogen-activated protein kinase kinase kinase kinase 4 (MAP4K4) and Traf2- and Nck-interacting kinase (TNIK) are putative effectors of Rap2 in mediating the activation of c-Jun N-terminal kinase (JNK) to regulate the actin cytoskeleton. In human platelets, Rap2 was shown to interact with the cytoskeleton by binding the actin filaments. In embryonic Xenopus development, Rap2 is necessary for the Wnt/beta-catenin signaling pathway. The Rap2 interacting protein 9 (RPIP9) is highly expressed in human breast carcinomas and correlates with a poor prognosis, suggesting a role for Rap2 in breast cancer oncogenesis. Rap2b, but not Rap2a, Rap2c, Rap1a, or Rap1b, is expressed in human red blood cells, where it is believed to be involved in vesiculation. A number of additional effector proteins for Rap2 have been identified, including the RalGEFs RalGDS, RGL, and Rlf, which also interact with Rap1 and Ras. 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: 133376  Cd Length: 163  Bit Score: 107.62  E-value: 4.85e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGvEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:cd04176   2 YKVVVLGSGGVGKSALTVQFVSGTFIEKYDPTIE-DFYRKEIEVDSSPSVLEILDTAGTEQFASMRDLYIKNGQGFIVVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  94 DITSRETYNALTNWLTD-ARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCAR 172
Cdd:cd04176  81 SLVNQQTFQDIKPMRDQiVRVKGYEKVPIILVGNKVDLESEREVSSAEGRALAEEWGCPFMETSAKSKTMVNELFAEIVR 160

                ...
gi 50741401 173 KIL 175
Cdd:cd04176 161 QMN 163
RheB cd04137
Ras Homolog Enriched in Brain (RheB) is a small GTPase; Rheb (Ras Homolog Enriched in Brain) ...
15-182 6.39e-29

Ras Homolog Enriched in Brain (RheB) is a small GTPase; Rheb (Ras Homolog Enriched in Brain) subfamily. Rheb was initially identified in rat brain, where its expression is elevated by seizures or by long-term potentiation. It is expressed ubiquitously, with elevated levels in muscle and brain. Rheb functions as an important mediator between the tuberous sclerosis complex proteins, TSC1 and TSC2, and the mammalian target of rapamycin (TOR) kinase to stimulate cell growth. TOR kinase regulates cell growth by controlling nutrient availability, growth factors, and the energy status of the cell. TSC1 and TSC2 form a dimeric complex that has tumor suppressor activity, and TSC2 is a GTPase activating protein (GAP) for Rheb. The TSC1/TSC2 complex inhibits the activation of TOR kinase through Rheb. Rheb has also been shown to induce the formation of large cytoplasmic vacuoles in a process that is dependent on the GTPase cycle of Rheb, but independent of the TOR kinase, suggesting Rheb plays a role in endocytic trafficking that leads to cell growth and cell-cycle progression. 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.


Pssm-ID: 206709  Cd Length: 180  Bit Score: 107.72  E-value: 6.39e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFgSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYD 94
Cdd:cd04137   3 KIAVLGSRSVGKSSLTVQFVEGHFVESYYPTIENTF-SKIITYKGQEYHLEIVDTAGQDEYSILPQKYSIGIHGYILVYS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  95 ITSRETYNALTNwLTDA--RMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFvqcaR 172
Cdd:cd04137  82 VTSRKSFEVVKV-IYDKilDMLGKESVPIVLVGNKSDLHMERQVSAEEGKKLAESWGAAFLESSAKENENVEEAF----E 156
                       170
                ....*....|
gi 50741401 173 KILNKIESGE 182
Cdd:cd04137 157 LLIEEIEKVE 166
Rab36_Rab34 cd04108
Rab GTPase families 34 (Rab34) and 36 (Rab36); Rab34/Rab36 subfamily. Rab34, found primarily ...
15-171 7.95e-29

Rab GTPase families 34 (Rab34) and 36 (Rab36); Rab34/Rab36 subfamily. Rab34, found primarily in the Golgi, interacts with its effector, Rab-interacting lysosomal protein (RILP). This enables its participation in microtubular dynenin-dynactin-mediated repositioning of lysosomes from the cell periphery to the Golgi. A Rab34 (Rah) isoform that lacks the consensus GTP-binding region has been identified in mice. This isoform is associated with membrane ruffles and promotes macropinosome formation. Rab36 has been mapped to human chromosome 22q11.2, a region that is homozygously deleted in malignant rhabdoid tumors (MRTs). However, experimental assessments do not implicate Rab36 as a tumor suppressor that would enable tumor formation through a loss-of-function mechanism. 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: 206693  Cd Length: 170  Bit Score: 107.27  E-value: 7.95e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYD 94
Cdd:cd04108   2 KVIVVGDLSVGKTCLINRFCKDVFDKNYKATIGVDFEMERFEVLGVPFSLQLWDTAGQERFKCIASTYYRGAQAIIIVFD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  95 ITSRETYNALTNWLTDA-RMLASQNIVIILCGNKKDLDADREVTFLE--ASRFAQENELMFLETSALTGENVEEAFVQCA 171
Cdd:cd04108  82 LTDVASLEHTRQWLEDAlKENDPSSVLLFLVGTKKDLSSPAQYALMEqdAIKLAREMKAEYWAVSALTGENVRDFFFRVA 161
RSR1 cd04177
RSR1/Bud1p family GTPase; RSR1/Bud1p is a member of the Rap subfamily of the Ras family that ...
14-178 9.52e-29

RSR1/Bud1p family GTPase; RSR1/Bud1p is a member of the Rap subfamily of the Ras family that is found in fungi. In budding yeasts, RSR1 is involved in selecting a site for bud growth on the cell cortex, which directs the establishment of cell polarization. The Rho family GTPase cdc42 and its GEF, cdc24, then establish an axis of polarized growth by organizing the actin cytoskeleton and secretory apparatus at the bud site. It is believed that cdc42 interacts directly with RSR1 in vivo. In filamentous fungi, polar growth occurs at the tips of hypha and at novel growth sites along the extending hypha. In Ashbya gossypii, RSR1 is a key regulator of hyphal growth, localizing at the tip region and regulating in apical polarization of the actin cytoskeleton. 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.


Pssm-ID: 133377  Cd Length: 168  Bit Score: 107.18  E-value: 9.52e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFgSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:cd04177   2 YKIVVLGAGGVGKSALTVQFVQNVFIESYDPTIEDSY-RKQVEIDGRQCDLEILDTAGTEQFTAMRELYIKSGQGFLLVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  94 DITSRETYNALTNwLTDA--RMLASQNIVIILCGNKKDLDADREVTFLEASRFAQE-NELMFLETSALTGENVEEAFVQC 170
Cdd:cd04177  81 SVTSEASLNELGE-LREQvlRIKDSDNVPMVLVGNKADLEDDRQVSREDGVSLSQQwGNVPFYETSARKRTNVDEVFIDL 159

                ....*...
gi 50741401 171 ARKILNKI 178
Cdd:cd04177 160 VRQIICVI 167
Rho cd00157
Ras homology family (Rho) of small guanosine triphosphatases (GTPases); Members of the Rho ...
15-172 1.47e-28

Ras homology family (Rho) of small guanosine triphosphatases (GTPases); Members of the Rho (Ras homology) family include RhoA, Cdc42, Rac, Rnd, Wrch1, RhoBTB, and Rop. There are 22 human Rho family members identified currently. These proteins are all involved in the reorganization of the actin cytoskeleton in response to external stimuli. They also have roles in cell transformation by Ras in cytokinesis, in focal adhesion formation and in the stimulation of stress-activated kinase. These various functions are controlled through distinct effector proteins and mediated through a GTP-binding/GTPase cycle involving three classes of regulating proteins: GAPs (GTPase-activating proteins), GEFs (guanine nucleotide exchange factors), and GDIs (guanine nucleotide dissociation inhibitors). 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. Since crystal structures often lack C-terminal residues, this feature is not available for annotation in many of the CDs in the hierarchy.


Pssm-ID: 206641  Cd Length: 171  Bit Score: 106.47  E-value: 1.47e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIgVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYD 94
Cdd:cd00157   2 KIVVVGDGAVGKTCLLISYTTNKFPTEYVPTV-FDNYSANVTVDGKQVNLGLWDTAGQEEYDRLRPLSYPQTDVFLLCFS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  95 ITSRETY-NALTNWLTDARmLASQNIVIILCGNKKDLDADRE-----------VTFLEASRFAQE-NELMFLETSALTGE 161
Cdd:cd00157  81 VDSPSSFeNVKTKWYPEIK-HYCPNVPIILVGTKIDLRDDGNtlkklekkqkpITPEEGEKLAKEiGAVKYMECSALTQE 159
                       170
                ....*....|.
gi 50741401 162 NVEEAFVQCAR 172
Cdd:cd00157 160 GLKEVFDEAIR 170
H_N_K_Ras_like cd04138
Ras GTPase family containing H-Ras,N-Ras and K-Ras4A/4B; H-Ras/N-Ras/K-Ras subfamily. H-Ras, ...
14-174 3.05e-28

Ras GTPase family containing H-Ras,N-Ras and K-Ras4A/4B; H-Ras/N-Ras/K-Ras subfamily. H-Ras, N-Ras, and K-Ras4A/4B are the prototypical members of the Ras family. These isoforms generate distinct signal outputs despite interacting with a common set of activators and effectors, and are strongly associated with oncogenic progression in tumor initiation. Mutated versions of Ras that are insensitive to GAP stimulation (and are therefore constitutively active) are found in a significant fraction of human cancers. Many Ras guanine nucleotide exchange factors (GEFs) have been identified. They 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 that stimulate a variety of diverse cytoplasmic signaling activities. Some are known to positively mediate the oncogenic properties of Ras, including Raf, phosphatidylinositol 3-kinase (PI3K), RalGEFs, and Tiam1. Others are proposed to play negative regulatory roles in oncogenesis, including RASSF 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: 133338  Cd Length: 162  Bit Score: 105.58  E-value: 3.05e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFgSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:cd04138   2 YKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSY-RKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  94 DITSRETYNALTNWLTDA-RMLASQNIVIILCGNKKDLdADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCAR 172
Cdd:cd04138  81 AINSRKSFEDIHTYREQIkRVKDSDDVPMVLVGNKCDL-AARTVSSRQGQDLAKSYGIPYIETSAKTRQGVEEAFYTLVR 159

                ..
gi 50741401 173 KI 174
Cdd:cd04138 160 EI 161
PLN03071 PLN03071
GTP-binding nuclear protein Ran; Provisional
1-185 2.18e-26

GTP-binding nuclear protein Ran; Provisional


Pssm-ID: 178620  Cd Length: 219  Bit Score: 102.14  E-value: 2.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401    1 MSQAAMSETYDFLFKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVE------FGSKiinvgGKyVKLQIWDTAGQER 74
Cdd:PLN03071   1 MALPNQQTVDYPSFKLVIVGDGGTGKTTFVKRHLTGEFEKKYEPTIGVEvhpldfFTNC-----GK-IRFYCWDTAGQEK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401   75 FRSVTRSYYRGAAGALLVYDITSRETYNALTNWLTDARMLaSQNIVIILCGNKKDLdADREVtflEASR--FAQENELMF 152
Cdd:PLN03071  75 FGGLRDGYYIHGQCAIIMFDVTARLTYKNVPTWHRDLCRV-CENIPIVLCGNKVDV-KNRQV---KAKQvtFHRKKNLQY 149
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 50741401  153 LETSALTGENVEEAFVQCARKI-----LNKIESGELDP 185
Cdd:PLN03071 150 YEISAKSNYNFEKPFLYLARKLagdpnLHFVESPALAP 187
PTZ00369 PTZ00369
Ras-like protein; Provisional
14-174 4.70e-26

Ras-like protein; Provisional


Pssm-ID: 240385  Cd Length: 189  Bit Score: 100.32  E-value: 4.70e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401   14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFgSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:PTZ00369   6 YKLVVVGGGGVGKSALTIQFIQNHFIDEYDPTIEDSY-RKQCVIDEETCLLDILDTAGQEEYSAMRDQYMRTGQGFLCVY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401   94 DITSRETYNALTNWLTDA-RMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCAR 172
Cdd:PTZ00369  85 SITSRSSFEEIASFREQIlRVKDKDRVPMILVGNKCDLDSERQVSTGEGQELAKSFGIPFLETSAKQRVNVDEAFYELVR 164

                 ..
gi 50741401  173 KI 174
Cdd:PTZ00369 165 EI 166
Rap_like cd04136
Rap-like family consists of Rap1, Rap2 and RSR1; The Rap subfamily consists of the Rap1, Rap2, ...
14-174 1.73e-25

Rap-like family consists of Rap1, Rap2 and RSR1; The Rap subfamily consists of the Rap1, Rap2, and RSR1. Rap subfamily proteins perform different cellular functions, depending on the isoform and its subcellular localization. For example, in rat salivary gland, neutrophils, and platelets, Rap1 localizes to secretory granules and is believed to regulate exocytosis or the formation of secretory granules. Rap1 has also been shown to localize in the Golgi of rat fibroblasts, zymogen granules, plasma membrane, and microsomal membrane of the pancreatic acini, as well as in the endocytic compartment of skeletal muscle cells and fibroblasts. Rap1 localizes in the nucleus of human oropharyngeal squamous cell carcinomas (SCCs) and cell lines. Rap1 plays a role in phagocytosis by controlling the binding of adhesion receptors (typically integrins) to their ligands. In yeast, Rap1 has been implicated in multiple functions, including activation and silencing of transcription and maintenance of telomeres. Rap2 is involved in multiple functions, including activation of c-Jun N-terminal kinase (JNK) to regulate the actin cytoskeleton and activation of the Wnt/beta-catenin signaling pathway in embryonic Xenopus. A number of effector proteins for Rap2 have been identified, including isoform 3 of the human mitogen-activated protein kinase kinase kinase kinase 4 (MAP4K4) and Traf2- and Nck-interacting kinase (TNIK), and the RalGEFs RalGDS, RGL, and Rlf, which also interact with Rap1 and Ras. RSR1 is the fungal homolog of Rap1 and Rap2. In budding yeasts, it is involved in selecting a site for bud growth, which directs the establishment of cell polarization. The Rho family GTPase Cdc42 and its GEF, Cdc24, then establish an axis of polarized growth. It is believed that Cdc42 interacts directly with RSR1 in vivo. In filamentous fungi such as Ashbya gossypii, RSR1 is a key regulator of polar growth in the hypha. 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: 206708  Cd Length: 164  Bit Score: 98.40  E-value: 1.73e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGvEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:cd04136   2 YKLVVLGSGGVGKSALTVQFVQGIFVDKYDPTIE-DSYRKQIEVDCQQCMLEILDTAGTEQFTAMRDLYIKNGQGFALVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  94 DITSRETYNALTNwLTDA--RMLASQNIVIILCGNKKDLDADREVTFLEASRFAQE-NELMFLETSALTGENVEEAFVQC 170
Cdd:cd04136  81 SITAQQSFNDLQD-LREQilRVKDTEDVPMILVGNKCDLEDERVVSKEEGQNLARQwGNCPFLETSAKSKINVDEIFYDL 159

                ....
gi 50741401 171 ARKI 174
Cdd:cd04136 160 VRQI 163
RabL4 cd04101
Rab GTPase-like family 4 (Rab-like4); RabL4 (Rab-like4) subfamily. RabL4s are novel proteins ...
15-172 3.72e-25

Rab GTPase-like family 4 (Rab-like4); RabL4 (Rab-like4) subfamily. RabL4s 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, RabL4 lacks a prenylation site at the C-terminus. The specific function of RabL4 remains unknown.


Pssm-ID: 206688  Cd Length: 167  Bit Score: 97.60  E-value: 3.72e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEK--KFKDDSNHTIGVEFGSKIINV--GGKYVKLQIWDTAGQERFRSVTRSYYRGAAGAL 90
Cdd:cd04101   2 QCAVVGDPAVGKSALVQMFHSDgaTFQKNYTMTTGCDLVVKTVPVpdTSDSVELFIFDSAGQELFSDMVENVWEQPAVVC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  91 LVYDITSRETYNALTNWLTDARMLASQ-NIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQ 169
Cdd:cd04101  82 VVYDVTNEVSFNNCSRWINRVRTHSHGlHTPGVLVGNKCDLTDRREVDAAQAQALAQANTLKFYETSAKEGVGYEAPFLS 161

                ...
gi 50741401 170 CAR 172
Cdd:cd04101 162 LAR 164
Rap1 cd04175
Rap1 family GTPase consists of Rap1a and Rap1b isoforms; The Rap1 subgroup is part of the Rap ...
14-174 6.47e-24

Rap1 family GTPase consists of Rap1a and Rap1b isoforms; The Rap1 subgroup is part of the Rap subfamily of the Ras family. It can be further divided into the Rap1a and Rap1b isoforms. In humans, Rap1a and Rap1b share 95% sequence homology, but are products of two different genes located on chromosomes 1 and 12, respectively. Rap1a is sometimes called smg p21 or Krev1 in the older literature. Rap1 proteins are believed to perform different cellular functions, depending on the isoform, its subcellular localization, and the effector proteins it binds. For example, in rat salivary gland, neutrophils, and platelets, Rap1 localizes to secretory granules and is believed to regulate exocytosis or the formation of secretory granules. Rap1 has also been shown to localize in the Golgi of rat fibroblasts, zymogen granules, plasma membrane, and the microsomal membrane of pancreatic acini, as well as in the endocytic compartment of skeletal muscle cells and fibroblasts. High expression of Rap1 has been observed in the nucleus of human oropharyngeal squamous cell carcinomas (SCCs) and cell lines; interestingly, in the SCCs, the active GTP-bound form localized to the nucleus, while the inactive GDP-bound form localized to the cytoplasm. Rap1 plays a role in phagocytosis by controlling the binding of adhesion receptors (typically integrins) to their ligands. In yeast, Rap1 has been implicated in multiple functions, including activation and silencing of transcription and maintenance of telomeres. Rap1a, which is stimulated by T-cell receptor (TCR) activation, is a positive regulator of T cells by directing integrin activation and augmenting lymphocyte responses. In murine hippocampal neurons, Rap1b determines which neurite will become the axon and directs the recruitment of Cdc42, which is required for formation of dendrites and axons. In murine platelets, Rap1b is required for normal homeostasis in vivo and is involved in integrin activation. 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: 133375  Cd Length: 164  Bit Score: 94.12  E-value: 6.47e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFgSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:cd04175   2 YKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSY-RKQVEVDGQQCMLEILDTAGTEQFTAMRDLYMKNGQGFVLVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  94 DITSRETYNALTNwLTDA--RMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCA 171
Cdd:cd04175  81 SITAQSTFNDLQD-LREQilRVKDTEDVPMILVGNKCDLEDERVVGKEQGQNLARQWGCAFLETSAKAKINVNEIFYDLV 159

                ...
gi 50741401 172 RKI 174
Cdd:cd04175 160 RQI 162
Ras2 cd04144
Rat sarcoma (Ras) family 2 of small guanosine triphosphatases (GTPases); The Ras2 subfamily, ...
15-174 5.43e-23

Rat sarcoma (Ras) family 2 of small guanosine triphosphatases (GTPases); The Ras2 subfamily, found exclusively in fungi, was first identified in Ustilago maydis. In U. maydis, Ras2 is regulated by Sql2, a protein that is homologous to GEFs (guanine nucleotide exchange factors) of the CDC25 family. Ras2 has been shown to induce filamentous growth, but the signaling cascade through which Ras2 and Sql2 regulate cell morphology is not known. 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.


Pssm-ID: 133344  Cd Length: 190  Bit Score: 92.22  E-value: 5.43e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIInVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYD 94
Cdd:cd04144   1 KLVVLGDGGVGKTALTIQLCLNHFVETYDPTIEDSYRKQVV-VDGQPCMLEVLDTAGQEEYTALRDQWIREGEGFILVYS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  95 ITSRETYNALTNWLTDARMLASQN---IVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCA 171
Cdd:cd04144  80 ITSRSTFERVERFREQIQRVKDESaadVPIMIVGNKCDKVYEREVSTEEGAALARRLGCEFIEASAKTNVNVERAFYTLV 159

                ...
gi 50741401 172 RKI 174
Cdd:cd04144 160 RAL 162
RabL2 cd04124
Rab GTPase-like family 2 (Rab-like2); RabL2 (Rab-like2) subfamily. RabL2s are novel Rab ...
15-167 5.77e-23

Rab GTPase-like family 2 (Rab-like2); RabL2 (Rab-like2) subfamily. RabL2s are novel Rab proteins identified recently which display features that are distinct from other Rabs, and have been termed Rab-like. RabL2 contains RabL2a and RabL2b, two very similar Rab proteins that share > 98% sequence identity in humans. RabL2b maps to the subtelomeric region of chromosome 22q13.3 and RabL2a maps to 2q13, a region that suggests it is also a subtelomeric gene. Both genes are believed to be expressed ubiquitously, suggesting that RabL2s are the first example of duplicated genes in human proximal subtelomeric regions that are both expressed actively. Like other Rab-like proteins, RabL2s lack a prenylation site at the C-terminus. The specific functions of RabL2a and RabL2b remain unknown. 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.


Pssm-ID: 133324  Cd Length: 161  Bit Score: 91.46  E-value: 5.77e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYD 94
Cdd:cd04124   2 KIILLGDSAVGKSKLVERFLMDGYEPQQLSTYALTLYKHNAKFEGKTILVDFWDTAGQERFQTMHASYYHKAHACILVFD 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50741401  95 ITSRETYNALTNWLTDARMLASQnIVIILCGNKkdLDADREVTfLEASRFAQENELMFLETSALTGENVEEAF 167
Cdd:cd04124  82 VTRKITYKNLSKWYEELREYRPE-IPCIVVANK--IDLDPSVT-QKKFNFAEKHNLPLYYVSAADGTNVVKLF 150
RHO smart00174
Rho (Ras homology) subfamily of Ras-like small GTPases; Members of this subfamily of Ras-like ...
18-177 1.30e-22

Rho (Ras homology) subfamily of Ras-like small GTPases; Members of this subfamily of Ras-like small GTPases include Cdc42 and Rac, as well as Rho isoforms.


Pssm-ID: 197554  Cd Length: 174  Bit Score: 90.75  E-value: 1.30e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401     18 VIGNAGTGKSCLLHQFIEKKFKDD------SNHTIGVEfgskiinVGGKYVKLQIWDTAGQE---RFRSVTrsyYRGAAG 88
Cdd:smart00174   3 VVGDGAVGKTCLLIVYTTNAFPEDyvptvfENYSADVE-------VDGKPVELGLWDTAGQEdydRLRPLS---YPDTDV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401     89 ALLVYDITSRETY-NALTNWLTDARMLAsQNIVIILCGNKKDLDADRE------------VTFLEASRFAQE-NELMFLE 154
Cdd:smart00174  73 FLICFSVDSPASFeNVKEKWYPEVKHFC-PNVPIILVGTKLDLRNDKStleelskkkqepVTYEQGQALAKRiGAVKYLE 151
                          170       180
                   ....*....|....*....|...
gi 50741401    155 TSALTGENVEEAFVQCARKILNK 177
Cdd:smart00174 152 CSALTQEGVREVFEEAIRAALNK 174
Miro pfam08477
Miro-like protein; Mitochondrial Rho proteins (Miro-1 and Miro-2), are atypical Rho GTPases. ...
15-129 5.46e-22

Miro-like protein; Mitochondrial Rho proteins (Miro-1 and Miro-2), are atypical Rho GTPases. They have a unique domain organisation, 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: 254820  Cd Length: 118  Bit Score: 87.48  E-value: 5.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401    15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNH-TIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:pfam08477   1 KVVVIGDKGSGKSSLLSQLVGGEFPPEIPEeIQGDTLAVDTLEVDGDTELLHIWDFGGREELKFEHIIFMKTADAILLVY 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 50741401    94 DITSRETYNALTN---WLTDARMLAsQNIVIILCGNKKD 129
Cdd:pfam08477  81 DLTDRESLNRVSRliaWLPHLRKLG-KKIPVILVGNKFD 118
RERG_RasL11_like cd04146
Ras-related and Estrogen-Regulated Growth inhibitor (RERG) and Ras-like 11 (RasL11)-like ...
15-174 8.96e-22

Ras-related and Estrogen-Regulated Growth inhibitor (RERG) and Ras-like 11 (RasL11)-like families; RERG (Ras-related and Estrogen- Regulated Growth inhibitor) and Ras-like 11 are members of a novel subfamily of Ras that were identified based on their behavior in breast and prostate tumors, respectively. RERG expression was decreased or lost in a significant fraction of primary human breast tumors that lack estrogen receptor and are correlated with poor clinical prognosis. Elevated RERG expression correlated with favorable patient outcome in a breast tumor subtype that is positive for estrogen receptor expression. In contrast to most Ras proteins, RERG overexpression inhibited the growth of breast tumor cells in vitro and in vivo. RasL11 was found to be ubiquitously expressed in human tissue, but down-regulated in prostate tumors. Both RERG and RasL11 lack the C-terminal CaaX prenylation motif, where a = an aliphatic amino acid and X = any amino acid, and are localized primarily in the cytoplasm. Both are believed to have tumor suppressor activity.


Pssm-ID: 206713  Cd Length: 166  Bit Score: 88.10  E-value: 8.96e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFgSKIINVGGKYVKLQIWDTAGQERFRSV--TRSYYRGAAGALLV 92
Cdd:cd04146   1 KIAVLGASGVGKSALTVRFLTKRFIGEYEPNLESLY-SRQVTIDGEQVSLEIQDTPGQQQNEDPesLERSLRWADGFVLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  93 YDITSRETYNALTNWLTDARMLASQ--NIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGEN-VEEAFVQ 169
Cdd:cd04146  80 YSITDRSSFDVVSQLLQLIREIKKRdgEIPVILVGNKADLLHSRQVSTEEGQKLALELGCLFFEVSAAENYLeVQNVFHE 159

                ....*
gi 50741401 170 CARKI 174
Cdd:cd04146 160 LCREV 164
Rab20 cd04126
Rab GTPase family 20 (Rab20); Rab20 is one of several Rab proteins that appear to be ...
15-167 9.06e-22

Rab GTPase family 20 (Rab20); Rab20 is one of several Rab proteins that appear to be restricted in expression to the apical domain of murine polarized epithelial cells. It is expressed on the apical side of polarized kidney tubule and intestinal epithelial cells, and in non-polarized cells. It also localizes to vesico-tubular structures below the apical brush border of renal proximal tubule cells and in the apical region of duodenal epithelial cells. Rab20 has also been shown to colocalize with vacuolar H+-ATPases (V-ATPases) in mouse kidney cells, suggesting a role in the regulation of V-ATPase traffic in specific portions of the nephron. It was also shown to be one of several proteins whose expression is upregulated in human myelodysplastic syndrome (MDS) patients. 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: 133326 [Multi-domain]  Cd Length: 220  Bit Score: 89.20  E-value: 9.06e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDdSNHTIGVEFGSKiinVGGKYvKLQIWDTAGQERFRSVTRSYYRGAAGALLVYD 94
Cdd:cd04126   2 KVVLLGDMNVGKTSLLHRYMERRFKD-TVSTVGGAFYLK---QWGPY-NISIWDTAGREQFHGLGSMYCRGAAAVILTYD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  95 ITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDAD-------------------REVTFLEASRFAQE-------- 147
Cdd:cd04126  77 VSNVQSLEELEDRFLGLTDTANEDCLFAVVGNKLDLTEEgalagqekdagdrvspedqRQVTLEDAKAFYKRinkykmld 156
                       170       180
                ....*....|....*....|....*.
gi 50741401 148 ------NELMFLETSALTGENVEEAF 167
Cdd:cd04126 157 edlspaAEKMCFETSAKTGYNVDELF 182
RGK cd04148
Rem, Rem2, Rad, Gem/Kir (RGK) subfamily of Ras GTPases; RGK subfamily. The RGK (Rem, Rem2, Rad, ...
14-191 1.13e-21

Rem, Rem2, Rad, Gem/Kir (RGK) subfamily of Ras GTPases; RGK subfamily. The RGK (Rem, Rem2, Rad, Gem/Kir) subfamily of Ras GTPases are expressed in a tissue-specific manner and are dynamically regulated by transcriptional and posttranscriptional mechanisms in response to environmental cues. RGK proteins bind to the beta subunit of L-type calcium channels, causing functional down-regulation of these voltage-dependent calcium channels, and either termination of calcium-dependent secretion or modulation of electrical conduction and contractile function. Inhibition of L-type calcium channels by Rem2 may provide a mechanism for modulating calcium-triggered exocytosis in hormone-secreting cells, and has been proposed to influence the secretion of insulin in pancreatic beta cells. RGK proteins also interact with and inhibit the Rho/Rho kinase pathway to modulate remodeling of the cytoskeleton. Two characteristics of RGK proteins cited in the literature are N-terminal and C-terminal extensions beyond the GTPase domain typical of Ras superfamily members. The N-terminal extension is not conserved among family members; the C-terminal extension is reported to be conserved among the family and lack the CaaX prenylation motif typical of membrane-associated Ras proteins. However, a putative CaaX motif has been identified in the alignment of the C-terminal residues of this CD.


Pssm-ID: 206715 [Multi-domain]  Cd Length: 219  Bit Score: 89.00  E-value: 1.13e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:cd04148   1 YRVVLLGDSGVGKSSLANIFTAGVYEDSAYEASGDDTYERTVSVDGEEATLVVYDHWEQEDGMWLEDSCMQVGDAYVIVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  94 DITSRETYNA---LTNWLTDARMLasQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQC 170
Cdd:cd04148  81 SVTDRSSFEKaseLRIQLRRARQA--EDIPIILVGNKSDLVRSREVSVQEGRACAVVFDCKFIETSAALQHNVDELFEGI 158
                       170       180
                ....*....|....*....|.
gi 50741401 171 ARKILNKIESGELDPERMGSG 191
Cdd:cd04148 159 VRQVRLRRDSKEKNTRRMASR 179
ARHI_like cd04140
A Ras homolog member I (ARHI); ARHI (A Ras homolog member I) is a member of the Ras family ...
14-167 1.70e-21

A Ras homolog member I (ARHI); ARHI (A Ras homolog member I) is a member of the Ras family with several unique structural and functional properties. ARHI is expressed in normal human ovarian and breast tissue, but its expression is decreased or eliminated in breast and ovarian cancer. ARHI contains an N-terminal extension of 34 residues (human) that is required to retain its tumor suppressive activity. Unlike most other Ras family members, ARHI is maintained in the constitutively active (GTP-bound) state in resting cells and has modest GTPase activity. ARHI inhibits STAT3 (signal transducers and activators of transcription 3), a latent transcription factor whose abnormal activation plays a critical role in oncogenesis. 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: 206711  Cd Length: 165  Bit Score: 87.58  E-value: 1.70e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFgSKIINVGGKYVKLQIWDTAGQERFRSVTR-SYYRGAAgALLV 92
Cdd:cd04140   2 YRVVVFGAGGVGKSSLVLRFVKGTFRESYIPTIEDTY-RQVISCSKSICTLQITDTTGSHQFPAMQRlSISKGHA-FILV 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50741401  93 YDITSRETYNALTNWLTDARMLAS---QNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAF 167
Cdd:cd04140  80 YSITSKQSLEELKPIYELICEIKGnnlEKIPIMLVGNKCDESPSREVSSSEGAALARTWNCAFMETSAKTNHNVQELF 157
Rho4_like cd04132
Ras homology family 4 (Rho4) of small guanosine triphosphatases (GTPases)-like; Rho4 is a ...
14-177 1.92e-21

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  Cd Length: 197  Bit Score: 87.78  E-value: 1.92e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDD------SNHTIGVEFGSkiinvgGKYVKLQIWDTAGQERFRSVTRSYYRGAA 87
Cdd:cd04132   4 VKIVVVGDGGCGKTCLLMVYAQGSFPEEyvptvfENYVTTLQVPN------GKIIELALWDTAGQEDYDRLRPLSYPDVD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  88 GALLVYDITSRETY-NALTNWLTDARMLAsQNIVIILCGNKKDLDADRE------------VTFLEASRFAQE-NELMFL 153
Cdd:cd04132  78 VILICYSVDNPTSLdNVEDKWYPEVNHFC-PGTPIVLVGLKTDLRKDKNsvsklraqglepVTPEQGESVAKSiGAVAYI 156
                       170       180
                ....*....|....*....|....
gi 50741401 154 ETSALTGENVEEAFVQCARKILNK 177
Cdd:cd04132 157 ECSAKLMENVDEVFDAAINVALSK 180
Rit_Rin_Ric cd04141
Ras-like protein in all tissues (Rit), Ras-like protein in neurons (Rin) and Ras-related ...
14-177 5.57e-20

Ras-like protein in all tissues (Rit), Ras-like protein in neurons (Rin) and Ras-related protein which interacts with calmodulin (Ric); Rit (Ras-like protein in all tissues), Rin (Ras-like protein in neurons) and Ric (Ras-related protein which interacts with calmodulin) form a subfamily with several unique structural and functional characteristics. These proteins all lack a the C-terminal CaaX lipid-binding motif typical of Ras family proteins, and Rin and Ric contain calmodulin-binding domains. Rin, which is expressed only in neurons, induces neurite outgrowth in rat pheochromocytoma cells through its association with calmodulin and its activation of endogenous Rac/cdc42. Rit, which is ubiquitously expressed in mammals, inhibits growth-factor withdrawl-mediated apoptosis and induces neurite extension in pheochromocytoma cells. Rit and Rin are both able to form a ternary complex with PAR6, a cell polarity-regulating protein, and Rac/cdc42. This ternary complex is proposed to have physiological function in processes such as tumorigenesis. Activated Ric is likely to signal in parallel with the Ras pathway or stimulate the Ras pathway at some upstream point, and binding of calmodulin to Ric may negatively regulate Ric activity.


Pssm-ID: 206712  Cd Length: 172  Bit Score: 83.36  E-value: 5.57e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIInVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:cd04141   3 YKIVMLGAGGVGKSAVTMQFISHSFPDYHDPTIEDAYKTQAR-IDNEPALLDILDTAGQAEFTAMRDQYMRCGEGFIICY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  94 DITSRETYNALTNW---LTDARMlaSQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQC 170
Cdd:cd04141  82 SVTDRHSFQEASEFkelITRVRL--TEDIPLVLVGNKVDLEQQRQVTTEEGRNLAREFNCPFFETSAALRFYIDDAFHGL 159

                ....*..
gi 50741401 171 ARKILNK 177
Cdd:cd04141 160 VREIRRK 166
Spg1 cd04128
Septum-promoting GTPase (Spg1); Spg1p. Spg1p (septum-promoting GTPase) was first identified in ...
15-167 1.88e-18

Septum-promoting GTPase (Spg1); Spg1p. Spg1p (septum-promoting GTPase) was first identified in the fission yeast S. pombe, where it regulates septum formation in the septation initiation network (SIN) through the cdc7 protein kinase. Spg1p is an essential gene that localizes to the spindle pole bodies. When GTP-bound, it binds cdc7 and causes it to translocate to spindle poles. Sid4p (septation initiation defective) is required for localization of Spg1p to the spindle pole body, and the ability of Spg1p to promote septum formation from any point in the cell cycle depends on Sid4p. Spg1p is negatively regulated by Byr4 and cdc16, which form a two-component GTPase activating protein (GAP) for Spg1p. The existence of a SIN-related pathway in plants has been proposed. 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.


Pssm-ID: 206701  Cd Length: 182  Bit Score: 79.36  E-value: 1.88e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYD 94
Cdd:cd04128   2 KIGLLGDAQIGKTSLMVKYVEGEFDEEYIQTLGVNFMEKTISIRGTEITFSIWDLGGQREFINMLPLVCKDAVAILFMFD 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50741401  95 ITSRETYNALTNWLTDARMLaSQNIVIILCGNKKDLDAD------REVTfLEASRFAQENELMFLETSALTGENVEEAF 167
Cdd:cd04128  82 LTRKSTLNSIKEWYRQARGF-NKTAIPILVGTKYDLFADlppeeqEEIT-KQARKYAKAMKAPLIFCSTSHSINVQKIF 158
RocCOR cd09914
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ...
15-165 2.23e-18

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  Cd Length: 161  Bit Score: 78.53  E-value: 2.23e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGS-KIINVGGKYVKLQIWDTAGQERFRSV------TRSYYrgaa 87
Cdd:cd09914   3 KLMLVGQGGVGKTSLCKQLIGEKFDGDESSTHGINVQDwKIPAPERKKIRLNVWDFGGQEIYHAThqffltSRSLY---- 78
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50741401  88 gaLLVYDITSRETYNALTNWLTDARMLASQNIVIILcGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEE 165
Cdd:cd09914  79 --LLVFDLRTGDEVSRVPYWLRQIKAFGGVSPVILV-GTHIDESCDEDILKKALNKKFPAIINDIHFVSCKNGKGIAE 153
Rop_like cd04133
Rho-related protein from plants (Rop)-like; The Rop (Rho-related protein from plants) ...
15-175 7.03e-18

Rho-related protein from plants (Rop)-like; The Rop (Rho-related protein from plants) subfamily plays a role in diverse cellular processes, including cytoskeletal organization, pollen and vegetative cell growth, hormone responses, stress responses, and pathogen resistance. Rops are able to regulate several downstream pathways to amplify a specific signal by acting as master switches early in the signaling cascade. They transmit a variety of extracellular and intracellular signals. Rops are involved in establishing cell polarity in root-hair development, root-hair elongation, pollen-tube growth, cell-shape formation, responses to hormones such as abscisic acid (ABA) and auxin, responses to abiotic stresses such as oxygen deprivation, and disease resistance and disease susceptibility. An individual Rop can have a unique function or an overlapping function shared with other Rop proteins; in addition, a given Rop-regulated function can be controlled by one or multiple Rop proteins. For example, Rop1, Rop3, and Rop5 are all involved in pollen-tube growth; Rop2 plays a role in response to low-oxygen environments, cell-morphology, and root-hair development; root-hair development is also regulated by Rop4 and Rop6; Rop6 is also responsible for ABA response, and ABA response is also regulated by Rop10. Plants retain some of the regulatory mechanisms that are shared by other members of the Rho family, but have also developed a number of unique modes for regulating Rops. Unique RhoGEFs have been identified that are exclusively active toward Rop proteins, such as those containing the domain PRONE (plant-specific Rop nucleotide exchanger). 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. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206705  Cd Length: 173  Bit Score: 77.58  E-value: 7.03e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIInVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYD 94
Cdd:cd04133   3 KCVTVGDGAVGKTCMLISYTSNTFPTDYVPTVFDNFSANVV-VDGNTVNLGLWDTAGQEDYNRLRPLSYRGADVFLLAFS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  95 ITSRETY-NALTNWLTDARMLASqNIVIILCGNKKDLDADREVtFLE---ASRF--AQENELMF-------LETSALTGE 161
Cdd:cd04133  82 LISKASYeNVLKKWIPELRHYAP-GVPIVLVGTKLDLRDDKQF-FADhpgAVPIttAQGEELRKqigaaayIECSSKTQQ 159
                       170
                ....*....|....
gi 50741401 162 NVEEAFVQCARKIL 175
Cdd:cd04133 160 NVKAVFDAAIKVVL 173
Rho2 cd04129
Ras homology family 2 (Rho2) of small guanosine triphosphatases (GTPases); Rho2 is a fungal ...
15-167 1.35e-16

Ras homology family 2 (Rho2) of small guanosine triphosphatases (GTPases); Rho2 is a fungal GTPase that plays a role in cell morphogenesis, control of cell wall integrity, control of growth polarity, and maintenance of growth direction. Rho2 activates the protein kinase C homolog Pck2, and Pck2 controls Mok1, the major (1-3) alpha-D-glucan synthase. Together with Rho1 (RhoA), Rho2 regulates the construction of the cell wall. Unlike Rho1, Rho2 is not an essential protein, but its overexpression is lethal. 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 proper intracellular localization via membrane attachment. As with other Rho family GTPases, the GDP/GTP cycling is regulated by GEFs (guanine nucleotide exchange factors), GAPs (GTPase-activating proteins) and GDIs (guanine nucleotide dissociation inhibitors).


Pssm-ID: 206702 [Multi-domain]  Cd Length: 190  Bit Score: 74.10  E-value: 1.35e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIiNVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYD 94
Cdd:cd04129   3 KLVIVGDGACGKTSLLYVFTLGEFPEEYHPTVFENYVTDC-RVDGKPVQLALWDTAGQEEYERLRPLSYSKAHVILIGFA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  95 ITSRETY-NALTNWLTDARMLASqNIVIILCGNKKDLDAD----------REVTFLEASRFAQE-NELMFLETSALTGEN 162
Cdd:cd04129  82 IDTPDSLeNVRTKWIEEVRRYCP-NVPVILVGLKKDLRQEavakgnyatdEFVPIQQAKLVARAiGAKKYMECSALTGEG 160

                ....*
gi 50741401 163 VEEAF 167
Cdd:cd04129 161 VDDVF 165
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
17-167 3.01e-16

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: 72.61  E-value: 3.01e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  17 LVIGNAGTGKSCLLHQFIEKKFkdDSNH-TIGveFGSKIINVggKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYDI 95
Cdd:cd00878   3 LMLGLDGAGKTTILYKLKLGEV--VTTIpTIG--FNVETVEY--KNVKFTVWDVGGQDKIRPLWKHYYENTDGLIFVVDS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  96 TSR----ETYNALTNWLTDARMlasQNIVIILCGNKKDL---DADREVT-FLEASRFAQENELMFlETSALTGENVEEAF 167
Cdd:cd00878  77 SDRerieEAKNELHKLLNEEEL---KGAPLLILANKQDLpgaLTESELIeLLGLESIKGRRWHIQ-PCSAVTGDGLDEGL 152
RhoA_like cd01870
Ras homology family A (RhoA)-like includes RhoA, RhoB and RhoC; The RhoA subfamily consists of ...
15-175 4.40e-16

Ras homology family A (RhoA)-like includes RhoA, RhoB and RhoC; The RhoA subfamily consists of RhoA, RhoB, and RhoC. RhoA promotes the formation of stress fibers and focal adhesions, regulating cell shape, attachment, and motility. RhoA can bind to multiple effector proteins, thereby triggering different downstream responses. In many cell types, RhoA mediates local assembly of the contractile ring, which is necessary for cytokinesis. RhoA is vital for muscle contraction; in vascular smooth muscle cells, RhoA plays a key role in cell contraction, differentiation, migration, and proliferation. RhoA activities appear to be elaborately regulated in a time- and space-dependent manner to control cytoskeletal changes. 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. RhoA and RhoC are observed only in geranylgeranylated forms; however, RhoB can be present in palmitoylated, farnesylated, and geranylgeranylated forms. RhoA and RhoC are highly relevant for tumor progression and invasiveness; however, RhoB has recently been suggested to be a tumor suppressor. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206662  Cd Length: 175  Bit Score: 72.08  E-value: 4.40e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIgVEFGSKIINVGGKYVKLQIWDTAGQE---RFRSVTrsyYRGAAGALL 91
Cdd:cd01870   3 KLVIVGDGACGKTCLLIVFSKDQFPEVYVPTV-FENYVADIEVDGKQVELALWDTAGQEdydRLRPLS---YPDTDVILM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  92 VYDITSRETY-NALTNWLTDARMLAsQNIVIILCGNKKDLDADrEVTFLEASRFAQE--------------NELMFLETS 156
Cdd:cd01870  79 CFSIDSPDSLeNIPEKWTPEVKHFC-PNVPIILVGNKKDLRND-EHTIRELAKMKQEpvkpeegramaekiGAFGYLECS 156
                       170
                ....*....|....*....
gi 50741401 157 ALTGENVEEAFVQCARKIL 175
Cdd:cd01870 157 AKTKEGVREVFEMATRAAL 175
RhoG cd01875
Ras homolog family, member G (RhoG) of small guanosine triphosphatases (GTPases); RhoG is a ...
15-176 1.08e-15

Ras homolog family, member G (RhoG) of small guanosine triphosphatases (GTPases); RhoG is a GTPase with high sequence similarity to members of the Rac subfamily, including the regions involved in effector recognition and binding. However, RhoG does not bind to known Rac1 and Cdc42 effectors, including proteins containing a Cdc42/Rac interacting binding (CRIB) motif. Instead, RhoG interacts directly with Elmo, an upstream regulator of Rac1, in a GTP-dependent manner and forms a ternary complex with Dock180 to induce activation of Rac1. The RhoG-Elmo-Dock180 pathway is required for activation of Rac1 and cell spreading mediated by integrin, as well as for neurite outgrowth induced by nerve growth factor. Thus RhoG activates Rac1 through Elmo and Dock180 to control cell morphology. RhoG has also been shown to play a role in caveolar trafficking and has a novel role in signaling the neutrophil respiratory burst stimulated by G protein-coupled receptor (GPCR) agonists. 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: 133277  Cd Length: 191  Bit Score: 71.19  E-value: 1.08e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIInVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYD 94
Cdd:cd01875   5 KCVVVGDGAVGKTCLLICYTTNAFPKEYIPTVFDNYSAQTA-VDGRTVSLNLWDTAGQEEYDRLRTLSYPQTNVFIICFS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  95 ITSRETY-NALTNWLTDARMlASQNIVIILCGNKKDLDADREV------------TFLEASRFAQE-NELMFLETSALTG 160
Cdd:cd01875  84 IASPSSYeNVRHKWHPEVCH-HCPNVPILLVGTKKDLRNDADTlkklkeqgqapiTPQQGGALAKQiHAVKYLECSALNQ 162
                       170
                ....*....|....*.
gi 50741401 161 ENVEEAFVQCARKILN 176
Cdd:cd01875 163 DGVKEVFAEAVRAVLN 178
Ras_dva cd04147
Ras - dorsal-ventral anterior localization (Ras-dva) family; Ras-dva subfamily. Ras-dva (Ras - ...
15-216 3.01e-15

Ras - dorsal-ventral anterior localization (Ras-dva) family; Ras-dva subfamily. Ras-dva (Ras - dorsal-ventral anterior localization) subfamily consists of a set of proteins characterized only in Xenopus leavis, to date. In Xenopus Ras-dva expression is activated by the transcription factor Otx2 and begins during gastrulation throughout the anterior ectoderm. Ras-dva expression is inhibited in the anterior neural plate by factor Xanf1. Downregulation of Ras-dva results in head development abnormalities through the inhibition of several regulators of the anterior neural plate and folds patterning, including Otx2, BF-1, Xag2, Pax6, Slug, and Sox9. Downregulation of Ras-dva also interferes with the FGF-8a signaling within the anterior ectoderm. 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.


Pssm-ID: 206714 [Multi-domain]  Cd Length: 197  Bit Score: 70.25  E-value: 3.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGvEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYD 94
Cdd:cd04147   1 RLVFMGAAGVGKTALIQRFLYDTFEPKHRRTVE-ELHSKEYEVAGVKVTIDILDTSGSYSFPAMRKLSIQNGDAFALVYS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  95 ITSRETY---NALTNWLTDARMLASQNIVIIlcGNKKDLDADREVTFLEASRFAQ-ENELMFLETSALTGENVEEAFvqc 170
Cdd:cd04147  80 VDDPESFeevKRLREEILEVKEDKFVPIVVV--GNKIDSLAERQVEAADALSTVElDWNNGFVEASAKDNENVTEVF--- 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 50741401 171 aRKILNKIESgeldPERMGSgiqygdaALRQLRSP------RRAQAQSAQEC 216
Cdd:cd04147 155 -KELLQQANL----PSWLSP-------ALRRRRESapseiqRRPPMNKTNSC 194
Rhes_like cd04143
Ras homolog enriched in striatum (Rhes) and activator of G-protein signaling 1 (Dexras1/AGS1); ...
14-207 4.46e-14

Ras homolog enriched in striatum (Rhes) and activator of G-protein signaling 1 (Dexras1/AGS1); This subfamily includes Rhes (Ras homolog enriched in striatum) and Dexras1/AGS1 (activator of G-protein signaling 1). These proteins are homologous, but exhibit significant differences in tissue distribution and subcellular localization. Rhes is found primarily in the striatum of the brain, but is also expressed in other areas of the brain, such as the cerebral cortex, hippocampus, inferior colliculus, and cerebellum. Rhes expression is controlled by thyroid hormones. In rat PC12 cells, Rhes is farnesylated and localizes to the plasma membrane. Rhes binds and activates PI3K, and plays a role in coupling serpentine membrane receptors with heterotrimeric G-protein signaling. Rhes has recently been shown to be reduced under conditions of dopamine supersensitivity and may play a role in determining dopamine receptor sensitivity. Dexras1/AGS1 is a dexamethasone-induced Ras protein that is expressed primarily in the brain, with low expression levels in other tissues. Dexras1 localizes primarily to the cytoplasm, and is a critical regulator of the circadian master clock to photic and nonphotic input. 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.


Pssm-ID: 133343 [Multi-domain]  Cd Length: 247  Bit Score: 67.47  E-value: 4.46e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGvEFGSKIINVGGKYVKLQIWDTAGQERFRSVTR-SYYRGAAgALLV 92
Cdd:cd04143   1 YRMVVLGASKVGKTAIVSRFLGGRFEEQYTPTIE-DFHRKLYSIRGEVYQLDILDTSGNHPFPAMRRlSILTGDV-FILV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  93 YDITSRETYNAL---------TNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENEL-MFLETSALTGEN 162
Cdd:cd04143  79 FSLDNRESFEEVcrlreqileTKSCLKNKTKENVKIPMVICGNKADRDFPREVQRDEVEQLVGGDENcAYFEVSAKKNSN 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 50741401 163 VEEAFVQCArkILNKIESgELDPERMGS-GIQYGDA-ALRQLRSPRR 207
Cdd:cd04143 159 LDEMFRALF--SLAKLPN-EMSPSLHRKiSVQYGDAlHKKSRGGSRK 202
Wrch_1 cd04130
Wnt-1 responsive Cdc42 homolog (Wrch-1) is a Rho family GTPase similar to Cdc42; Wrch-1 (Wnt-1 ...
15-167 1.13e-13

Wnt-1 responsive Cdc42 homolog (Wrch-1) is a Rho family GTPase similar to Cdc42; Wrch-1 (Wnt-1 responsive Cdc42 homolog) is a Rho family GTPase that shares significant sequence and functional similarity with Cdc42. Wrch-1 was first identified in mouse mammary epithelial cells, where its transcription is upregulated in Wnt-1 transformation. Wrch-1 contains N- and C-terminal extensions relative to cdc42, suggesting potential differences in cellular localization and function. The Wrch-1 N-terminal extension contains putative SH3 domain-binding motifs and has been shown to bind the SH3 domain-containing protein Grb2, which increases the level of active Wrch-1 in cells. Unlike Cdc42, which localizes to the cytosol and perinuclear membranes, Wrch-1 localizes extensively with the plasma membrane and endosomes. The membrane association, localization, and biological activity of Wrch-1 indicate an atypical model of regulation distinct from other Rho family GTPases. 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. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 133330  Cd Length: 173  Bit Score: 65.12  E-value: 1.13e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFgSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYD 94
Cdd:cd04130   2 KCVLVGDGAVGKTSLIVSYTTNGYPTEYVPTAFDNF-SVVVLVDGKPVRLQLCDTAGQDEFDKLRPLCYPDTDVFLLCFS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  95 ITSRETY-NALTNWLTDARMlASQNIVIILCGNKKDLDAD------------REVTFLEASRFAQE-NELMFLETSALTG 160
Cdd:cd04130  81 VVNPSSFqNISEKWIPEIRK-HNPKAPIILVGTQADLRTDvnvliqlarygeKPVSQSRAKALAEKiGACEYIECSALTQ 159

                ....*..
gi 50741401 161 ENVEEAF 167
Cdd:cd04130 160 KNLKEVF 166
Rnd cd04131
Rho family GTPase subfamily Rnd includes Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8; The Rnd ...
15-167 2.07e-13

Rho family GTPase subfamily Rnd includes Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8; The Rnd subfamily contains Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8. These novel Rho family proteins have substantial structural differences compared to other Rho members, including N- and C-terminal extensions relative to other Rhos. Rnd3/RhoE is farnesylated at the C-terminal prenylation site, unlike most other Rho proteins that are geranylgeranylated. In addition, Rnd members are unable to hydrolyze GTP and are resistant to GAP activity. They are believed to exist only in the GTP-bound conformation, and are antagonists of RhoA activity. 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. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206703  Cd Length: 176  Bit Score: 64.38  E-value: 2.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDD------SNHTIGVEfgskiinVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAG 88
Cdd:cd04131   3 KIVLVGDSQCGKTALLQVFAKDSFPENyvptvfENYTASFE-------VDKQRIELSLWDTSGSPYYDNVRPLSYPDSDA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  89 ALLVYDITSRETY-NALTNWLTDARMLASqNIVIILCGNKKDLDAD------------REVTFLEASRFA-QENELMFLE 154
Cdd:cd04131  76 VLICFDISRPETLdSVLKKWKGEVREFCP-NTPVLLVGCKSDLRTDlstltelsnkrqIPVSHEQGRNLAkQIGAAAYVE 154
                       170
                ....*....|....
gi 50741401 155 TSALTGEN-VEEAF 167
Cdd:cd04131 155 CSAKTSENsVRDVF 168
Rac1_like cd01871
Ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1)-like ...
15-174 1.32e-12

Ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1)-like consists of Rac1, Rac2 and Rac3; The Rac1-like subfamily consists of Rac1, Rac2, and Rac3 proteins, plus the splice variant Rac1b that contains a 19-residue insertion near switch II relative to Rac1. While Rac1 is ubiquitously expressed, Rac2 and Rac3 are largely restricted to hematopoietic and neural tissues respectively. Rac1 stimulates the formation of actin lamellipodia and membrane ruffles. It also plays a role in cell-matrix adhesion and cell anoikis. In intestinal epithelial cells, Rac1 is an important regulator of migration and mediates apoptosis. Rac1 is also essential for RhoA-regulated actin stress fiber and focal adhesion complex formation. In leukocytes, Rac1 and Rac2 have distinct roles in regulating cell morphology, migration, and invasion, but are not essential for macrophage migration or chemotaxis. Rac3 has biochemical properties that are closely related to Rac1, such as effector interaction, nucleotide binding, and hydrolysis; Rac2 has a slower nucleotide association and is more efficiently activated by the RacGEF Tiam1. Both Rac1 and Rac3 have been implicated in the regulation of cell migration and invasion in human metastatic breast cancer. 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. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206663  Cd Length: 174  Bit Score: 62.14  E-value: 1.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIInVGGKYVKLQIWDTAGQE---RFRSVTrsyYRGAAGALL 91
Cdd:cd01871   3 KCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVM-VDGKPVNLGLWDTAGQEdydRLRPLS---YPQTDVFLI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  92 VYDITSRETY-NALTNWLTDARMLASqNIVIILCGNKKDLDADRE------------VTFLEASRFAQE-NELMFLETSA 157
Cdd:cd01871  79 CFSLVSPASFeNVRAKWYPEVRHHCP-NTPIILVGTKLDLRDDKDtieklkekkltpITYPQGLAMAKEiGAVKYLECSA 157
                       170
                ....*....|....*..
gi 50741401 158 LTGENVEEAFVQCARKI 174
Cdd:cd01871 158 LTQRGLKTVFDEAIRAV 174
Miro1 cd01893
Mitochondrial Rho family 1 (Miro1), N-terminal; Miro1 subfamily. Miro (mitochondrial Rho) ...
15-173 1.70e-12

Mitochondrial Rho family 1 (Miro1), N-terminal; Miro1 subfamily. Miro (mitochondrial Rho) proteins have tandem GTP-binding domains separated by a linker region containing putative calcium-binding EF hand motifs. Genes encoding Miro-like proteins were found in several eukaryotic organisms. This CD represents the N-terminal GTPase domain of Miro proteins. These atypical Rho GTPases have roles in mitochondrial homeostasis and apoptosis. Most Rho proteins contain a lipid modification site at the C-terminus; however, Miro is one of few Rho subfamilies that lack this feature.


Pssm-ID: 206680  Cd Length: 168  Bit Score: 61.58  E-value: 1.70e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNH-----TIGVEFGSKiinvggkYVKLQIWDTAGQERFRSVTRSYYRGAAGA 89
Cdd:cd01893   4 RIVLIGDEGVGKSSLIMSLVSEEFPENVPRvlpeiTIPADVTPE-------RVPTTIVDTSSRPQDRANLAAEIRKANVI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  90 LLVYDITSRETYNAL-TNWLTDARMLASqNIVIILCGNKKDLDADREVTFLEASRFAQENEL----MFLETSALTGENVE 164
Cdd:cd01893  77 CLVYSVDRPSTLERIrTKWLPLIRRLGV-KVPIILVGNKSDLRDGSSQAGLEEEMLPIMNEFreieTCVECSAKTLINVS 155

                ....*....
gi 50741401 165 EAFVqCARK 173
Cdd:cd01893 156 EVFY-YAQK 163
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
14-167 6.73e-12

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


Pssm-ID: 249519  Cd Length: 174  Bit Score: 59.94  E-value: 6.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401    14 FKFLVIGNAGTGKSCLLHQFiekKFKDDSNH--TIGveFGSKIINVGGkyVKLQIWDTAGQERFRSVTRSYYRGAAGALL 91
Cdd:pfam00025  15 MRILILGLDNAGKTTILYKL---KLGEIVTTipTIG--FNVETVTYKN--VKFTVWDVGGQESLRPLWRNYFPNTDAVIF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401    92 VYDITSR----ETYNALTNWLTDARMlasQNIVIILCGNKKDLDAD---REVT-FLEASRFAQENELMFlETSALTGENV 163
Cdd:pfam00025  88 VVDSADRdrieEAKEELHALLNEEEL---ADAPLLILANKQDLPGAmseAEIReLLGLHELKDRPWEIQ-GCSAVTGEGL 163

                  ....
gi 50741401   164 EEAF 167
Cdd:pfam00025 164 DEGL 167
ARLTS1 cd04156
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ...
17-167 1.42e-11

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  Cd Length: 160  Bit Score: 58.97  E-value: 1.42e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  17 LVIGNAGTGKSCLLHQFIEKKFKDDSNhTIGveFGSKIINVGgKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYDIT 96
Cdd:cd04156   3 LLLGLDSAGKSTLLYKLKHAELVTTIP-TVG--FNVEMLQLE-KHLSLTVWDVGGQEKMRTVWKCYLENTDGLVYVVDSS 78
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50741401  97 SR----ETYNALTNWLTDARMlasQNIVIILCGNKKDLDAD---REVT-FLEASRFAQENELMFLETSALTGENVEEAF 167
Cdd:cd04156  79 DEarldESQKELKHILKNEHI---KGVPVVLLANKQDLPGAltaEEITrRFKLKKYCSDRDWYVQPCSAVTGEGLAEAF 154
Arfrp1 cd04160
Arf-related protein 1 (Arfrp1); Arfrp1 (Arf-related protein 1), formerly known as ARP, is a ...
17-166 1.47e-11

Arf-related protein 1 (Arfrp1); Arfrp1 (Arf-related protein 1), formerly known as ARP, is a membrane-associated Arf family member that lacks the N-terminal myristoylation motif. Arfrp1 is mainly associated with the trans-Golgi compartment and the trans-Golgi network, where it regulates the targeting of Arl1 and the GRIP domain-containing proteins, golgin-97 and golgin-245, onto Golgi membranes. It is also involved in the anterograde transport of the vesicular stomatitis virus G protein from the Golgi to the plasma membrane, and in the retrograde transport of TGN38 and Shiga toxin from endosomes to the trans-Golgi network. Arfrp1 also inhibits Arf/Sec7-dependent activation of phospholipase D. Deletion of Arfrp1 in mice causes embryonic lethality at the gastrulation stage and apoptosis of mesodermal cells, indicating its importance in development.


Pssm-ID: 206725  Cd Length: 168  Bit Score: 59.28  E-value: 1.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  17 LVIGNAGTGKSCLLHQfIEKKFKDDS---NH-----TIGVEFGSkiINVGGkyVKLQIWDTAGQERFRSVTRSYYRGAAG 88
Cdd:cd04160   3 LILGLDNAGKTTFLEQ-TKTKFSKNYkglNPskitpTVGLNIGT--IEVGK--ARLMFWDLGGQEELRSLWDKYYAESHG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  89 ALLVYDITSRETYNALTNWLTdaRMLAS---QNIVIILCGNKKDLD-----ADREVTFLEASRFAQENELMFLETSALTG 160
Cdd:cd04160  78 VIYVIDSTDRERFNESKSAFE--KVINNealEGVPLLVLANKQDLPdalsvAEIKEVFDDCIALIGRRDCLVQPVSALEG 155

                ....*.
gi 50741401 161 ENVEEA 166
Cdd:cd04160 156 EGVEEG 161
Rho3 cd04134
Ras homology family 3 (Rho3) of small guanosine triphosphatases (GTPases); Rho3 is a member of ...
15-176 1.84e-11

Ras homology family 3 (Rho3) of small guanosine triphosphatases (GTPases); Rho3 is a member of the Rho family found only in fungi. Rho3 is believed to regulate cell polarity by interacting with the diaphanous/formin family protein For3 to control both the actin cytoskeleton and microtubules. Rho3 is also believed to have a direct role in exocytosis that is independent of its role in regulating actin polarity. The function in exocytosis may be two-pronged: first, in the transport of post-Golgi vesicles from the mother cell to the bud, mediated by myosin (Myo2); second, in the docking and fusion of vesicles to the plasma membrane, mediated by an exocyst (Exo70) protein. 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: 206706  Cd Length: 185  Bit Score: 59.10  E-value: 1.84e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIgVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYD 94
Cdd:cd04134   2 KVVVLGDGACGKTSLLNVFTRGYFPQVYEPTV-FENYIHDIFVDGLAVELSLWDTAGQEEFDRLRSLSYADTHVIMLCFS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  95 ITSRETY-NALTNWLTDARMlASQNIVIILCGNKKDLDADREVTFLEASRFAQE---------NELMFLETSALTGENVE 164
Cdd:cd04134  81 VDNPDSLeNVESKWLAEIRH-HCPGVKLVLVALKCDLREPRNERDRGTHTISYEeglavakriNACRYLECSAKLNRGVN 159
                       170
                ....*....|..
gi 50741401 165 EAFVQCARKILN 176
Cdd:cd04134 160 EAFTEAARVALN 171
Rnd3_RhoE_Rho8 cd04172
Rnd3/RhoE/Rho8 GTPases; Rnd3/RhoE/Rho8 subfamily. Rnd3/RhoE/Rho8 is a member of the novel Rho ...
15-162 2.45e-11

Rnd3/RhoE/Rho8 GTPases; Rnd3/RhoE/Rho8 subfamily. Rnd3/RhoE/Rho8 is a member of the novel Rho subfamily Rnd, together with Rnd1/Rho6 and Rnd2/Rho7. Rnd3/RhoE is known to bind the serine-threonine kinase ROCK I. Unphosphorylated Rnd3/RhoE associates primarily with membranes, but ROCK I-phosphorylated Rnd3/RhoE localizes in the cytosol. Phosphorylation of Rnd3/RhoE correlates with its activity in disrupting RhoA-induced stress fibers and inhibiting Ras-induced fibroblast transformation. In cells that lack stress fibers, such as macrophages and monocytes, Rnd3/RhoE induces a redistribution of actin, causing morphological changes in the cell. In addition, Rnd3/RhoE has been shown to inhibit cell cycle progression in G1 phase at a point upstream of the pRb family pocket protein checkpoint. Rnd3/RhoE has also been shown to inhibit Ras- and Raf-induced fibroblast transformation. In mammary epithelial tumor cells, Rnd3/RhoE regulates the assembly of the apical junction complex and tight junction formation. Rnd3/RhoE is underexpressed in prostate cancer cells both in vitro and in vivo; re-expression of Rnd3/RhoE suppresses cell cycle progression and increases apoptosis, suggesting it may play a role in tumor suppression. 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. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206735  Cd Length: 182  Bit Score: 58.91  E-value: 2.45e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIgVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYD 94
Cdd:cd04172   7 KIVVVGDSQCGKTALLHVFAKDCFPENYVPTV-FENYTASFEIDTQRIELSLWDTSGSPYYDNVRPLSYPDSDAVLICFD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  95 ITSRETY-NALTNWLTDARMLASqNIVIILCGNKKDLDADReVTFLEASRFAQE--------------NELMFLETSALT 159
Cdd:cd04172  86 ISRPETLdSVLKKWKGEIQEFCP-NTKMLLVGCKSDLRTDV-STLVELSNHRQTpvsydqganmakqiGAATYIECSALQ 163

                ...
gi 50741401 160 GEN 162
Cdd:cd04172 164 SEN 166
ARF smart00177
ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular ...
15-130 6.67e-11

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  Cd Length: 175  Bit Score: 57.62  E-value: 6.67e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401     15 KFLVIGNAGTGKSCLLHqfiekKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYD 94
Cdd:smart00177  15 RILMVGLDAAGKTTILY-----KLKLGESVTTIPTIGFNVETVTYKNISFTVWDVGGQDKIRPLWRHYYTNTQGLIFVVD 89
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 50741401     95 ITSRETYNALTNWLTdaRMLAS---QNIVIILCGNKKDL 130
Cdd:smart00177  90 SNDRDRIDEAREELH--RMLNEdelRDAVILVFANKQDL 126
Tc10 cd04135
Rho GTPase TC10 (Tc10); TC10 is a Rho family protein that has been shown to induce microspike ...
14-167 8.85e-10

Rho GTPase TC10 (Tc10); TC10 is a Rho family protein that has been shown to induce microspike formation and neurite outgrowth in vitro. Its expression changes dramatically after peripheral nerve injury, suggesting an important role in promoting axonal outgrowth and regeneration. TC10 regulates translocation of insulin-stimulated GLUT4 in adipocytes and has also been shown to bind directly to Golgi COPI coat proteins. GTP-bound TC10 in vitro can bind numerous potential effectors. Depending on its subcellular localization and distinct functional domains, TC10 can differentially regulate two types of filamentous actin in adipocytes. TC10 mRNAs are highly expressed in three types of mouse muscle tissues: leg skeletal muscle, cardiac muscle, and uterus; they were also present in brain, with higher levels in adults than in newborns. TC10 has also been shown to play a role in regulating the expression of cystic fibrosis transmembrane conductance regulator (CFTR) through interactions with CFTR-associated ligand (CAL). The GTP-bound form of TC10 directs the trafficking of CFTR from the juxtanuclear region to the secretory pathway toward the plasma membrane, away from CAL-mediated DFTR degradation in the lysosome. 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. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206707  Cd Length: 174  Bit Score: 54.25  E-value: 8.85e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIiNVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:cd04135   1 LKCVVVGDGAVGKTCLLMSYANDAFPEEYVPTVFDHYAVSV-TVGGKQYLLGLYDTAGQEDYDRLRPLSYPMTDVFLICF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  94 DITSRETY-NALTNWLTDARMLASqNIVIILCGNKKDLDAD------------REVTFLEASRFAQE-NELMFLETSALT 159
Cdd:cd04135  80 SVVNPASFqNVKEEWVPELKEYAP-NVPYLLIGTQIDLRDDpktlarlndmkeKPITVEQGQKLAKEiGACCYVECSALT 158

                ....*...
gi 50741401 160 GENVEEAF 167
Cdd:cd04135 159 QKGLKTVF 166
Arl10_like cd04159
Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from ...
18-130 1.11e-09

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  Cd Length: 159  Bit Score: 53.86  E-value: 1.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  18 VIGNAGTGKSCLLHQFIEKKFKDDSNHTIGveFGSKIINVGGkyVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYDITS 97
Cdd:cd04159   4 LVGLQNSGKTTLVNVIASGQFSEDTIPTVG--FNMRKVTKGN--VTIKVWDLGGQPRFRSMWERYCRGVNAIVYVVDAAD 79
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 50741401  98 RETYNALTNWLTD---ARMLASqnIVIILCGNKKDL 130
Cdd:cd04159  80 REKLEVAKNELHDlleKPSLEG--IPLLVLGNKNDL 113
Arl5_Arl8 cd04153
Arf-like 5 (Arl5) and 8 (Arl8) GTPases; Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like ...
14-166 2.54e-09

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  Cd Length: 174  Bit Score: 53.12  E-value: 2.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLHQFIEKkfkdDSNHTiGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:cd04153  16 YKVIIVGLDNAGKTTILYQFLLG----EVVHT-SPTIGSNVEEIVYKNIRFLMWDIGGQESLRSSWNTYYTNTDAVILVI 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  94 DITSRETYNALTNWLtdARMLASQNI---VIILCGNKKDL-DAdreVTFLEASRF-----AQENELMFLETSALTGENVE 164
Cdd:cd04153  91 DSTDRERLPLTKEEL--YKMLAHEDLrkaVLLVLANKQDLkGA---MTPAEISESlgltsIRDHTWHIQGCCALTGEGLP 165

                ..
gi 50741401 165 EA 166
Cdd:cd04153 166 EG 167
RabL3 cd04102
Rab GTPase-like family 3 (Rab-like3); RabL3 (Rab-like3) subfamily. RabL3s are novel proteins ...
15-111 3.56e-09

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: 53.37  E-value: 3.56e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGG-----KYVKLQIWDTAGQ----ERFRSVTRSYYRG 85
Cdd:cd04102   2 KVLVLGDSGVGKSSLVHLLCKNQVLGNPSWTVGCSVDVRHHTYGEgtpeeKTFYVELWDVGGSvgsaESVKSTRAVFYNQ 81
                        90       100
                ....*....|....*....|....*.
gi 50741401  86 AAGALLVYDITSRETYNALTNWLTDA 111
Cdd:cd04102  82 INGIIFVHDLTNKKSSQNLYRWSLEA 107
PLN00023 PLN00023
GTP-binding protein; Provisional
17-107 9.18e-09

GTP-binding protein; Provisional


Pssm-ID: 177661  Cd Length: 334  Bit Score: 52.94  E-value: 9.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401   17 LVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGK---------------YVKLqiWDTAGQERFRSVTRS 81
Cdd:PLN00023  25 LVVGDSGVGKSSLVHLIVKGSSIARPPQTIGCTVGVKHITYGSPgsssnsikgdserdfFVEL--WDVSGHERYKDCRSL 102
                         90       100
                 ....*....|....*....|....*.
gi 50741401   82 YYRGAAGALLVYDITSRETYNALTNW 107
Cdd:PLN00023 103 FYSQINGVIFVHDLSQRRTKTSLQKW 128
Arf6 cd04149
ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins ...
15-167 1.26e-08

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: 50.93  E-value: 1.26e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHqfiekKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYD 94
Cdd:cd04149  11 RILMLGLDAAGKTTILY-----KLKLGQSVTTIPTVGFNVETVTYKNVKFNVWDVGGQDKIRPLWRHYYTGTQGLIFVVD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  95 ITSR----ETYNALTNWLTDARMlasQNIVIILCGNKKDL-DA--DREVT-FLEASRFAQENELMfLETSALTGENVEEA 166
Cdd:cd04149  86 SADRdridEARQELHRIINDREM---RDALLLVFANKQDLpDAmkPHEIQeKLGLTRIRDRNWYV-QPSCATSGDGLYEG 161

                .
gi 50741401 167 F 167
Cdd:cd04149 162 L 162
Rnd2_Rho7 cd04173
Rnd2/Rho7 GTPases; Rnd2/Rho7 is a member of the novel Rho subfamily Rnd, together with Rnd1 ...
15-167 2.50e-08

Rnd2/Rho7 GTPases; Rnd2/Rho7 is a member of the novel Rho subfamily Rnd, together with Rnd1/Rho6 and Rnd3/RhoE/Rho8. Rnd2/Rho7 is transiently expressed in radially migrating cells in the brain while they are within the subventricular zone of the hippocampus and cerebral cortex. These migrating cells typically develop into pyramidal neurons. Cells that exogenously expressed Rnd2/Rho7 failed to migrate to upper layers of the brain, suggesting that Rnd2/Rho7 plays a role in the radial migration and morphological changes of developing pyramidal neurons, and that Rnd2/Rho7 degradation is necessary for proper cellular migration. The Rnd2/Rho7 GEF Rapostlin is found primarily in the brain and together with Rnd2/Rho7 induces dendrite branching. Unlike Rnd1/Rho6 and Rnd3/RhoE/Rho8, which are RhoA antagonists, Rnd2/Rho7 binds the GEF Pragmin and significantly stimulates RhoA activity and Rho-A mediated cell contraction. Rnd2/Rho7 is also found to be expressed in spermatocytes and early spermatids, with male-germ-cell Rac GTPase-activating protein (MgcRacGAP), where it localizes to the Golgi-derived pro-acrosomal vesicle. 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: 206736 [Multi-domain]  Cd Length: 221  Bit Score: 51.18  E-value: 2.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDD------SNHTIGVEfgskiinVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAG 88
Cdd:cd04173   3 KIVVVGDTQCGKTALLHVFAKDNYPESyvptvfENYTASFE-------IDKHRIELNMWDTSGSSYYDNVRPLAYPDSDA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  89 ALLVYDITSRETYNALT-NWLTDARMLASqNIVIILCGNKKDLDAD----RE--------VTFLEASRFAQE-NELMFLE 154
Cdd:cd04173  76 VLICFDISRPETLDSVLkKWQGETQEFCP-NAKLVLVGCKLDMRTDlstlRElskqrlipVTHEQGSLLARQlGAVAYVE 154
                       170
                ....*....|....
gi 50741401 155 TSALTGEN-VEEAF 167
Cdd:cd04173 155 CSSRMSENsVRDVF 168
COG2229 COG2229
Predicted GTPase [General function prediction only]
15-166 3.18e-08

Predicted GTPase [General function prediction only]


Pssm-ID: 225138  Cd Length: 187  Bit Score: 50.54  E-value: 3.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEK------------KFKDDSNHTIGVEFGSkiINVGGKYvKLQIWDTAGQERFRSVTRSY 82
Cdd:COG2229  12 KIVVIGPVGAGKTTFVRALSDKplviteadassvSGKGKRPTTVAMDFGS--IELDEDT-GVHLFGTPGQERFKFMWEIL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  83 YRGAAGALLVYDITSRETYNAltnwLTDARMLASQNIVIILCG-NKKDL-DADREVTFLEASRFAQENELMFlETSALTG 160
Cdd:COG2229  89 SRGAVGAIVLVDSSRPITFHA----EEIIDFLTSRNPIPVVVAiNKQDLfDALPPEKIREALKLELLSVPVI-EIDATEG 163

                ....*.
gi 50741401 161 ENVEEA 166
Cdd:COG2229 164 EGARDQ 169
Arl2 cd04154
Arf-like 2 (Arl2) GTPase; Arl2 (Arf-like 2) GTPases are members of the Arf family that bind ...
14-167 5.92e-08

Arf-like 2 (Arl2) GTPase; Arl2 (Arf-like 2) GTPases are members of the Arf family that bind GDP and GTP with very low affinity. Unlike most Arf family proteins, Arl2 is not myristoylated at its N-terminal helix. The protein PDE-delta, first identified in photoreceptor rod cells, binds specifically to Arl2 and is structurally very similar to RhoGDI. Despite the high structural similarity between Arl2 and Rho proteins and between PDE-delta and RhoGDI, the interactions between the GTPases and their effectors are very different. In its GTP bound form, Arl2 interacts with the protein Binder of Arl2 (BART), and the complex is believed to play a role in mitochondrial adenine nucleotide transport. In its GDP bound form, Arl2 interacts with tubulin- folding Cofactor D; this interaction is believed to play a role in regulation of microtubule dynamics that impact the cytoskeleton, cell division, and cytokinesis.


Pssm-ID: 206720  Cd Length: 173  Bit Score: 49.25  E-value: 5.92e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  14 FKFLVIGNAGTGKSCLLhqfieKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:cd04154  15 MRILMLGLDNAGKTTIL-----KKFNGEDISTISPTLGFNIKTLEYNGYKLNIWDVGGQKSLRSYWRNYFESTDALIWVV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  94 DITSR----ETYNALTNWLTDARMLASQniVIILCgNKKDLDADrevtfLEASRFAQENEL--------MFLETSALTGE 161
Cdd:cd04154  90 DSSDRarleDCKRELQKLLVEERLAGAT--LLIFA-NKQDLPGA-----LSPEEIREVLELdsikshhwRIFGCSAVTGE 161

                ....*.
gi 50741401 162 NVEEAF 167
Cdd:cd04154 162 NLLDGI 167
Cdc42 cd01874
cell division cycle 42 (Cdc42) is a small GTPase of the Rho family; Cdc42 is an essential ...
15-167 1.97e-07

cell division cycle 42 (Cdc42) is a small GTPase of the Rho family; Cdc42 is an essential GTPase that belongs to the Rho family of Ras-like GTPases. These proteins act as molecular switches by responding to exogenous and/or endogenous signals and relaying those signals to activate downstream components of a biological pathway. Cdc42 transduces signals to the actin cytoskeleton to initiate and maintain polarized growth and to mitogen-activated protein morphogenesis. In the budding yeast Saccharomyces cerevisiae, Cdc42 plays an important role in multiple actin-dependent morphogenetic events such as bud emergence, mating-projection formation, and pseudohyphal growth. In mammalian cells, Cdc42 regulates a variety of actin-dependent events and induces the JNK/SAPK protein kinase cascade, which leads to the activation of transcription factors within the nucleus. Cdc42 mediates these processes through interactions with a myriad of downstream effectors, whose number and regulation we are just starting to understand. In addition, Cdc42 has been implicated in a number of human diseases through interactions with its regulators and downstream effectors. 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. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206664  Cd Length: 175  Bit Score: 47.95  E-value: 1.97e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIInVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYD 94
Cdd:cd01874   3 KCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVM-IGGEPYTLGLFDTAGQEDYDRLRPLSYPQTDVFLVCFS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  95 ITSRETY-NALTNWLTDARMlASQNIVIILCGNKKDLDAD------------REVTFLEASRFAQE-NELMFLETSALTG 160
Cdd:cd01874  82 VVSPSSFeNVKEKWVPEITH-HCPKTPFLLVGTQIDLRDDpstieklaknkqKPITPETGEKLARDlKAVKYVECSALTQ 160

                ....*..
gi 50741401 161 ENVEEAF 167
Cdd:cd01874 161 KGLKNVF 167
RRP22 cd04142
Ras-related protein on chromosome 22 (RRP22) family; RRP22 (Ras-related protein on chromosome ...
18-134 2.38e-07

Ras-related protein on chromosome 22 (RRP22) family; RRP22 (Ras-related protein on chromosome 22) subfamily consists of proteins that inhibit cell growth and promote caspase-independent cell death. Unlike most Ras proteins, RRP22 is down-regulated in many human tumor cells due to promoter methylation. RRP22 localizes to the nucleolus in a GTP-dependent manner, suggesting a novel function in modulating transport of nucleolar components. 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. Like most Ras family proteins, RRP22 is farnesylated.


Pssm-ID: 133342  Cd Length: 198  Bit Score: 48.32  E-value: 2.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  18 VIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWD---------TAGQE----RFRSVtrsyyR 84
Cdd:cd04142   5 VLGAPGVGKTAIVRQFLAQEFPEEYIPTEHRRLYRPAVVLSGRVYDLHILDvpnmqrypgTAGQEwmdpRFRGL-----R 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 50741401  85 GAAGALLVYDITSRETYN---ALTNWLTDARMLASQNIVIILCGNKKDLDADR 134
Cdd:cd04142  80 NSRAFILVYDICSPDSFHyvkLLRQQILETRPAGNKEPPIVVVGNKRDQQRHR 132
Arl4_Arl7 cd04152
Arf-like 4 (Arl4) and 7 (Arl7) GTPases; Arl4 (Arf-like 4) is highly expressed in testicular ...
17-165 2.66e-07

Arf-like 4 (Arl4) and 7 (Arl7) GTPases; Arl4 (Arf-like 4) is highly expressed in testicular germ cells, and is found in the nucleus and nucleolus. In mice, Arl4 is developmentally expressed during embryogenesis, and a role in somite formation and central nervous system differentiation has been proposed. Arl7 has been identified as the only Arf/Arl protein to be induced by agonists of liver X-receptor and retinoid X-receptor and by cholesterol loading in human macrophages. Arl7 is proposed to play a role in transport between a perinuclear compartment and the plasma membrane, apparently linked to the ABCA1-mediated cholesterol secretion pathway. Older literature suggests that Arl6 is a part of the Arl4/Arl7 subfamily, but analyses based on more recent sequence data place Arl6 in its own subfamily.


Pssm-ID: 206719  Cd Length: 183  Bit Score: 47.87  E-value: 2.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  17 LVIGNAGTGKSCLLHQFiekKFKDDSNH--TIGveFGSKIINVG---GKYVKLQIWDTAGQERFRSVTRSYYRGAAGALL 91
Cdd:cd04152   7 VMLGLDSAGKTTVLYRL---KFNEFVNTvpTKG--FNTEKIKVSlgnAKGVTFHFWDVGGQEKLRPLWKSYTRCTDGIVF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  92 VYDITSRETY-NALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEasRFAQENELM------FLETSALTGENVE 164
Cdd:cd04152  82 VVDSVDVERMeEAKTELHKITKFSENQGVPVLVLANKQDLPNALPVSEVE--KLLALHELSsstpwhVQPACAIIGEGLQ 159

                .
gi 50741401 165 E 165
Cdd:cd04152 160 E 160
PTZ00133 PTZ00133
ADP-ribosylation factor; Provisional
15-130 4.02e-07

ADP-ribosylation factor; Provisional


Pssm-ID: 173423  Cd Length: 182  Bit Score: 47.15  E-value: 4.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401   15 KFLVIGNAGTGKSCLLHqfiekKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYD 94
Cdd:PTZ00133  19 RILMVGLDAAGKTTILY-----KLKLGEVVTTIPTIGFNVETVEYKNLKFTMWDVGGQDKLRPLWRHYYQNTNGLIFVVD 93
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 50741401   95 ITSRETYNALTNWLtdARMLAS---QNIVIILCGNKKDL 130
Cdd:PTZ00133  94 SNDRERIGDAREEL--ERMLSEdelRDAVLLVFANKQDL 130
Sar1 cd00879
Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII ...
16-130 4.65e-07

Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII vesicle coats involved in export of cargo from the ER. The GTPase activity of Sar1 functions as a molecular switch to control protein-protein and protein-lipid interactions that direct vesicle budding from the ER. Activation of the GDP to the GTP-bound form of Sar1 involves the membrane-associated guanine nucleotide exchange factor (GEF) Sec12. Sar1 is unlike all Ras superfamily GTPases that use either myristoyl or prenyl groups to direct membrane association and function, in that Sar1 lacks such modification. Instead, Sar1 contains a unique nine-amino-acid N-terminal extension. This extension contains an evolutionarily conserved cluster of bulky hydrophobic amino acids, referred to as the Sar1-N-terminal activation recruitment (STAR) motif. The STAR motif mediates the recruitment of Sar1 to ER membranes and facilitates its interaction with mammalian Sec12 GEF leading to activation.


Pssm-ID: 206645  Cd Length: 191  Bit Score: 47.27  E-value: 4.65e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  16 FLVIGNAGtgKSCLLHqfiekKFKDDS--NHTIGVEFGSKIINVGGkyVKLQIWDTAGQERFRSVTRSYYRGAAGALLVY 93
Cdd:cd00879  24 FLGLDNAG--KTTLLH-----MLKDDRlaQHVPTLHPTSEELTIGN--VKFTTFDLGGHEQARRVWKDYFPEVDGIVFLV 94
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 50741401  94 D-------ITSRETYNALtnwLTDArMLASQNIVIIlcGNKKDL 130
Cdd:cd00879  95 DaadperfQESKEELDSL---LNDE-ELANVPILIL--GNKIDK 132
Arl9_Arfrp2_like cd04162
Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first ...
17-169 9.47e-07

Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first identified as part of the Human Cancer Genome Project. It maps to chromosome 4q12 and is sometimes referred to as Arfrp2 (Arf-related protein 2). This is a novel subfamily identified in human cancers that is uncharacterized to date.


Pssm-ID: 133362  Cd Length: 164  Bit Score: 45.90  E-value: 9.47e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  17 LVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGveFGSKIINVGGkyVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYDIT 96
Cdd:cd04162   3 LVLGLDGAGKTSLLHSLSSERSLESVVPTTG--FNSVAIPTQD--AIMELLEIGGSQNLRKYWKRYLSGSQGLIFVVDSA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  97 SRETynaltnwLTDARMLASQNI-------VIILcGNKKDLDADREVT----FLEASRFAQENELMFLETSA------LT 159
Cdd:cd04162  79 DSER-------LPLARQELHQLLqhppdlpLVVL-ANKQDLPAARSVQeihkELELEPIARGRRWILQGTSLdddgspSR 150
                       170
                ....*....|
gi 50741401 160 GENVEEAFVQ 169
Cdd:cd04162 151 MEAVKDLLSQ 160
Rnd1_Rho6 cd04174
Rnd1/Rho6 GTPases; Rnd1/Rho6 is a member of the novel Rho subfamily Rnd, together with Rnd2 ...
15-179 1.04e-06

Rnd1/Rho6 GTPases; Rnd1/Rho6 is a member of the novel Rho subfamily Rnd, together with Rnd2/Rho7 and Rnd3/RhoE/Rho8. Rnd1/Rho6 binds GTP but does not hydrolyze it to GDP, indicating that it is constitutively active. In rat, Rnd1/Rho6 is highly expressed in the cerebral cortex and hippocampus during synapse formation, and plays a role in spine formation. Rnd1/Rho6 is also expressed in the liver and in endothelial cells, and is upregulated in uterine myometrial cells during pregnancy. Like Rnd3/RhoE/Rho8, Rnd1/Rho6 is believed to function as an antagonist to RhoA. 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. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206737 [Multi-domain]  Cd Length: 232  Bit Score: 46.59  E-value: 1.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIgVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYD 94
Cdd:cd04174  15 KLVLVGDVQCGKTAMLQVLAKDCYPETYVPTV-FENYTACLETEEQRVELSLWDTSGSPYYDNVRPLCYSDSDAVLLCFD 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  95 ITSRETYN-ALTNWLTDArMLASQNIVIILCGNKKDLDAD------------REVTFLEASRFAQE-NELMFLETSALTG 160
Cdd:cd04174  94 ISRPEIFDsALKKWRAEI-LDYCPSTRILLIGCKTDLRTDlstlmelsnqkqAPISYEQGCAMAKQlGAEAYLECSAFTS 172
                       170       180
                ....*....|....*....|
gi 50741401 161 E-NVEEAFVQCARKILNKIE 179
Cdd:cd04174 173 EkSIHSIFRTASLLCINKLS 192
PLN00223 PLN00223
ADP-ribosylation factor; Provisional
15-130 2.14e-06

ADP-ribosylation factor; Provisional


Pssm-ID: 165788  Cd Length: 181  Bit Score: 45.34  E-value: 2.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401   15 KFLVIGNAGTGKSCLLHqfiekKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYD 94
Cdd:PLN00223  19 RILMVGLDAAGKTTILY-----KLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVD 93
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 50741401   95 ITSRETYNALTNWLtdARMLAS---QNIVIILCGNKKDL 130
Cdd:PLN00223  94 SNDRDRVVEARDEL--HRMLNEdelRDAVLLVFANKQDL 130
Arl3 cd04155
Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most ...
17-165 6.74e-06

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  Cd Length: 174  Bit Score: 43.54  E-value: 6.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  17 LVIGNAGTGKSCLLHQFIEkkfkDDSNHtIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAagALLVYDIT 96
Cdd:cd04155  19 LLLGLDNAGKTTILKQLAS----EDISH-ITPTQGFNIKNVQADGFKLNVWDIGGQRKIRPYWRNYFENT--DVLIYVID 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  97 S------RETYNALTNWLTDARMlasQNIVIILCGNKKDLdadreVTFLEASRFAQENELMFLE--------TSALTGEN 162
Cdd:cd04155  92 SadrkrfEEAGQELVELLEEEKL---AGVPVLVFANKQDL-----LTAAPAEEVAEALNLHDIRdrswhiqaCSAKTGEG 163

                ...
gi 50741401 163 VEE 165
Cdd:cd04155 164 LQE 166
Arl6 cd04157
Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small ...
17-167 9.08e-06

Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small GTPases. Arl6 expression is limited to the brain and kidney in adult mice, but it is expressed in the neural plate and somites during embryogenesis, suggesting a possible role for Arl6 in early development. Arl6 is also believed to have a role in cilia or flagella function. Several proteins have been identified that bind Arl6, including Arl6 interacting protein (Arl6ip), and SEC61beta, a subunit of the heterotrimeric conducting channel SEC61p. Based on Arl6 binding to these effectors, Arl6 is also proposed to play a role in protein transport, membrane trafficking, or cell signaling during hematopoietic maturation. At least three specific homozygous Arl6 mutations in humans have been found to cause Bardet-Biedl syndrome, a disorder characterized by obesity, retinopathy, polydactyly, renal and cardiac malformations, learning disabilities, and hypogenitalism. Older literature suggests that Arl6 is a part of the Arl4/Arl7 subfamily, but analyses based on more recent sequence data place Arl6 in its own subfamily.


Pssm-ID: 206722  Cd Length: 162  Bit Score: 43.19  E-value: 9.08e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  17 LVIGNAGTGKSCLLHQFiekKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYDIT 96
Cdd:cd04157   3 LVLGLDNSGKTTIINQL---KPSNAQSQNIVPTVGFNVESFKKGNLSFTAFDMSGQGKYRGLWEHYYKNIQGIIFVIDSS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  97 SRETYNALTNWL------TDarmLASQNIVIILCGNKKDL-DADREVTFLEASRFAQ--ENELMFLETSALTGENVEEAF 167
Cdd:cd04157  80 DRLRMVVAKDELelllnhPD---IKHRRIPILFYANKMDLpDALTAVKITQLLCLENikDKPWHIFASSALTGEGLDEGV 156
Arl1 cd04151
ADP ribosylation factor 1 (Arf1); Arl1 subfamily. Arl1 (Arf-like 1) localizes to the Golgi ...
60-166 1.83e-05

ADP ribosylation factor 1 (Arf1); Arl1 subfamily. Arl1 (Arf-like 1) localizes to the Golgi complex, where it is believed to recruit effector proteins to the trans-Golgi network. Like most members of the Arf family, Arl1 is myristoylated at its N-terminal helix and mutation of the myristoylation site disrupts Golgi targeting. In humans, the Golgi-localized proteins golgin-97 and golgin-245 have been identified as Arl1 effectors. Golgins are large coiled-coil proteins found in the Golgi, and these golgins contain a C-terminal GRIP domain, which is the site of Arl1 binding. Additional Arl1 effectors include the GARP (Golgi-associated retrograde protein)/VFT (Vps53) vesicle-tethering complex and Arfaptin 2. Arl1 is not required for exocytosis, but appears necessary for trafficking from the endosomes to the Golgi. In Drosophila zygotes, mutation of Arl1 is lethal, and in the host-bloodstream form of Trypanosoma brucei, Arl1 is essential for viability.


Pssm-ID: 206718  Cd Length: 158  Bit Score: 42.01  E-value: 1.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  60 KYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYDITSRETYNALTNWLtdARMLAS---QNIVIILCGNKKDLD---AD 133
Cdd:cd04151  41 KNLKFQVWDLGGQTSIRPYWRCYYSNTDAIIYVVDSTDRDRLGISKSEL--HAMLEEeelKDAVLLVFANKQDMPgalSE 118
                        90       100       110
                ....*....|....*....|....*....|....
gi 50741401 134 REVT-FLEASRFAQENELMFlETSALTGENVEEA 166
Cdd:cd04151 119 AEVAeKLGLSELKDRTWQIF-KTSATKGEGLDEG 151
Arf1_5_like cd04150
ADP-ribosylation factor-1 (Arf1) and ADP-ribosylation factor-5 (Arf5); The Arf1-Arf5-like ...
60-130 2.11e-05

ADP-ribosylation factor-1 (Arf1) and ADP-ribosylation factor-5 (Arf5); The Arf1-Arf5-like subfamily contains Arf1, Arf2, Arf3, Arf4, Arf5, and related proteins. Arfs1-5 are soluble proteins that are crucial for assembling coat proteins during vesicle formation. Each contains an N-terminal myristoylated amphipathic helix that is folded into the protein in the GDP-bound state. GDP/GTP exchange exposes the helix, which anchors to the membrane. Following GTP hydrolysis, the helix dissociates from the membrane and folds back into the protein. A general feature of Arf1-5 signaling may be the cooperation of two Arfs at the same site. Arfs1-5 are generally considered to be interchangeable in function and location, but some specific functions have been assigned. Arf1 localizes to the early/cis-Golgi, where it is activated by GBF1 and recruits the coat protein COPI. It also localizes to the trans-Golgi network (TGN), where it is activated by BIG1/BIG2 and recruits the AP1, AP3, AP4, and GGA proteins. Humans, but not rodents and other lower eukaryotes, lack Arf2. Human Arf3 shares 96% sequence identity with Arf1 and is believed to generally function interchangeably with Arf1. Human Arf4 in the activated (GTP-bound) state has been shown to interact with the cytoplasmic domain of epidermal growth factor receptor (EGFR) and mediate the EGF-dependent activation of phospholipase D2 (PLD2), leading to activation of the activator protein 1 (AP-1) transcription factor. Arf4 has also been shown to recognize the C-terminal sorting signal of rhodopsin and regulate its incorporation into specialized post-Golgi rhodopsin transport carriers (RTCs). There is some evidence that Arf5 functions at the early-Golgi and the trans-Golgi to affect Golgi-associated alpha-adaptin homology Arf-binding proteins (GGAs).


Pssm-ID: 206717  Cd Length: 159  Bit Score: 42.01  E-value: 2.11e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50741401  60 KYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYDITSRETYNALTNWLTdaRMLAS---QNIVIILCGNKKDL 130
Cdd:cd04150  42 KNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERIGEAREELQ--RMLNEdelRDAVLLVFANKQDL 113
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
55-165 6.26e-05

trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 40.56  E-value: 6.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  55 INVGGkyVKLQIWDTAGqerFRS---------VTRSYYRgAAGA---LLVYDITsretyNALTNwLTDARMLASQNIVII 122
Cdd:cd04164  46 IDLGG--IPVRLIDTAG---LREtedeiekigIERAREA-IEEAdlvLLVVDAS-----EGLDE-EDLEILELPAKKPVI 113
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 50741401 123 LCGNKKDLDADREvtfleasRFAQENELMFLETSALTGENVEE 165
Cdd:cd04164 114 VVLNKSDLLSDAE-------GISELNGKPIIAISAKTGEGIDE 149
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
16-165 8.14e-05

GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.


Pssm-ID: 206647 [Multi-domain]  Cd Length: 183  Bit Score: 40.74  E-value: 8.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  16 FLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFG--------------SKIINVGGKYVKLQIWDTAGQERFRSVTRS 81
Cdd:cd00881   2 VGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLdtlkeerergitikTGVVEFEWPKRRINFIDTPGHEDFSKETVR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  82 YYRGAAGALLVYDITSRETYNALTNWLTdarmLASQNIVIILCGNKKDL--DADREVTFLEASRFAQENELMFLE----- 154
Cdd:cd00881  82 GLAQADGALLVVDANEGVEPQTREHLNI----ALAGGLPIIVAVNKIDRvgEEDFDEVLREIKELLKLIGFTFLKgkdvp 157
                       170
                ....*....|....
gi 50741401 155 ---TSALTGENVEE 165
Cdd:cd00881 158 iipISALTGEGIEE 171
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
18-165 9.80e-05

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that 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. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 39.92  E-value: 9.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  18 VIGNAGTGKSCLLHQFIEKKFK--DDSNHT----IGVEFGSKIInvggkyVKLQIWDTAG------QERFRS-VTRSYYR 84
Cdd:cd00880   2 IFGRPNVGKSSLLNALLGQNVGivSPIPGTtrdpVRKEWELLPL------GPVVLIDTPGldeeggLGRERVeEARQVAD 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  85 GAAGALLVYDITSRETynaltNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASR-FAQENELMFLETSALTGENV 163
Cdd:cd00880  76 RADLVLLVVDSDLTPV-----EEEAKLGLLRERGKPVLLVLNKIDLVPESEEEELLRERkLELLPDLPVIAVSALPGEGI 150

                ..
gi 50741401 164 EE 165
Cdd:cd00880 151 DE 152
ARD1 cd04158
(ADP-ribosylation factor domain protein 1 (ARD1); ARD1 (ADP-ribosylation factor domain protein ...
15-132 1.10e-04

(ADP-ribosylation factor domain protein 1 (ARD1); ARD1 (ADP-ribosylation factor domain protein 1) is an unusual member of the Arf family. In addition to the C-terminal Arf domain, ARD1 has an additional 46-kDa N-terminal domain that contains a RING finger domain, two predicted B-Boxes, and a coiled-coil protein interaction motif. This domain belongs to the TRIM (tripartite motif) or RBCC (RING, B-Box, coiled-coil) family. Like most Arfs, the ARD1 Arf domain lacks detectable GTPase activity. However, unlike most Arfs, the full-length ARD1 protein has significant GTPase activity due to the GAP (GTPase-activating protein) activity exhibited by the 46-kDa N-terminal domain. The GAP domain of ARD1 is specific for its own Arf domain and does not bind other Arfs. The rate of GDP dissociation from the ARD1 Arf domain is slowed by the adjacent 15 amino acids, which act as a GDI (GDP-dissociation inhibitor) domain. ARD1 is ubiquitously expressed in cells and localizes to the Golgi and to the lysosomal membrane. Two Tyr-based motifs in the Arf domain are responsible for Golgi localization, while the GAP domain controls lysosomal localization.


Pssm-ID: 206723  Cd Length: 169  Bit Score: 40.01  E-value: 1.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50741401  15 KFLVIGNAGTGKSCLLHqfiekKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYD 94
Cdd:cd04158   1 RVVTLGLDGAGKTTILF-----KLKQDEFMQPIPTIGFNVETVEYKNLKFTIWDVGGKHKLRPLWKHYYLNTQAVVFVID 75
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..