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Conserved domains on  [gi|17541992|ref|NP_502959|]
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Ras-like GTP-binding protein rhoA [Caenorhabditis elegans]

Protein Classification

RhoA_like domain-containing protein (domain architecture ID 10111594)

RhoA_like domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RhoA_like cd01870
Ras homology family A (RhoA)-like includes RhoA, RhoB and RhoC; The RhoA subfamily consists of ...
5-179 1.59e-135

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: 380.62  E-value: 1.59e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   5 RKKLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCF 84
Cdd:cd01870   1 RKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  85 SIDSPDSLENIPEKWTPEVRHFCPNVPIILVGNKRDLRSDPQTVRELAKMKQEPVKPEQGRAIAEQIGAFAYLECSAKTK 164
Cdd:cd01870  81 SIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRNDEHTIRELAKMKQEPVKPEEGRAMAEKIGAFGYLECSAKTK 160
                       170
                ....*....|....*
gi 17541992 165 DGIREVFEKATQAAL 179
Cdd:cd01870 161 EGVREVFEMATRAAL 175
 
Name Accession Description Interval E-value
RhoA_like cd01870
Ras homology family A (RhoA)-like includes RhoA, RhoB and RhoC; The RhoA subfamily consists of ...
5-179 1.59e-135

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: 380.62  E-value: 1.59e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   5 RKKLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCF 84
Cdd:cd01870   1 RKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  85 SIDSPDSLENIPEKWTPEVRHFCPNVPIILVGNKRDLRSDPQTVRELAKMKQEPVKPEQGRAIAEQIGAFAYLECSAKTK 164
Cdd:cd01870  81 SIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRNDEHTIRELAKMKQEPVKPEEGRAMAEKIGAFGYLECSAKTK 160
                       170
                ....*....|....*
gi 17541992 165 DGIREVFEKATQAAL 179
Cdd:cd01870 161 EGVREVFEMATRAAL 175
RHO smart00174
Rho (Ras homology) subfamily of Ras-like small GTPases; Members of this subfamily of Ras-like ...
8-181 1.54e-123

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: 349.99  E-value: 1.54e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992      8 LVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSID 87
Cdd:smart00174   1 LVVVGDGAVGKTCLLIVYTTNAFPEDYVPTVFENYSADVEVDGKPVELGLWDTAGQEDYDRLRPLSYPDTDVFLICFSVD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992     88 SPDSLENIPEKWTPEVRHFCPNVPIILVGNKRDLRSDPQTVRELAKMKQEPVKPEQGRAIAEQIGAFAYLECSAKTKDGI 167
Cdd:smart00174  81 SPASFENVKEKWYPEVKHFCPNVPIILVGTKLDLRNDKSTLEELSKKKQEPVTYEQGQALAKRIGAVKYLECSALTQEGV 160
                          170
                   ....*....|....
gi 17541992    168 REVFEKATQAALQQ 181
Cdd:smart00174 161 REVFEEAIRAALNK 174
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
7-180 7.76e-77

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: 306559  Cd Length: 162  Bit Score: 230.85  E-value: 7.76e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992     7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTV-FENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:pfam00071   1 KLVLVGDGGVGKSSLLIRFTQNKFPEEYIPTIgVDFYTKTVEVDGKTVKLQIWDTAGQERFRALRPLYYRGADGFLLVYD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992    86 IDSPDSLENIPeKWTPEVRHFCP-NVPIILVGNKRDLRSdpqtvrelakmkQEPVKPEQGRAIAEQIGaFAYLECSAKTK 164
Cdd:pfam00071  81 ITSRDSFENVK-KWVEEILRHADeNVPIVLVGNKCDLED------------QRVVSTEEGEALAKELG-LPFMETSAKTN 146
                         170
                  ....*....|....*.
gi 17541992   165 DGIREVFEKATQAALQ 180
Cdd:pfam00071 147 ENVEEAFEELAREILK 162
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
5-159 2.84e-50

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


Pssm-ID: 272973  Cd Length: 162  Bit Score: 162.93  E-value: 2.84e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992     5 RKKLVIVGDGACGKTCLLIVFSKDQ-FPDVYVPTVFENYVAD-IEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILM 82
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKgSITEYYPGTTRNYVTTvIEEDGKTYKFNLLDTAGQEDYDAIRRLYYPQVERSLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992    83 CFSIDSP-DSLENIPEKWTPEVRHFCP-NVPIILVGNKRDLRS---DPQTVRELAKMKQEPVKPEQGRAIAEQIGAFAYL 157
Cdd:TIGR00231  81 VFDIVILvLDVEEILEKQTKEIIHHADsGVPIILVGNKIDLKDadlKTHVASEFAKLNGEPIIPLSAETGKNIDSAFKIV 160

                  ..
gi 17541992   158 EC 159
Cdd:TIGR00231 161 EA 162
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
4-181 7.31e-46

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 224025  Cd Length: 219  Bit Score: 153.58  E-value: 7.31e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   4 IRKKLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVA-DIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILM 82
Cdd:COG1100   4 KEFKIVVLGDGGVGKTTLLNRLVGDEFPEGYPPTIGNLDPAkTIEPYRRNIKLQLWDTAGQEEYRSLRPEYYRGANGILI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  83 CFSIDSPDSLENIPEKWTPEVRHFCP-NVPIILVGNKRDLRSDPQTVRELAK--MKQEPVKPEQGRAIAEQIGAFAYLEC 159
Cdd:COG1100  84 VYDSTLRESSDELTEEWLEELRELAPdDVPILLVGNKIDLFDEQSSSEEILNqlNREVVLLVLAPKAVLPEVANPALLET 163
                       170       180
                ....*....|....*....|....
gi 17541992 160 SAK--TKDGIREVFEKATQAALQQ 181
Cdd:COG1100 164 SAKslTGPNVNELFKELLRKLLEE 187
PLN03118 PLN03118
Rab family protein; Provisional
7-173 2.21e-25

Rab family protein; Provisional


Pssm-ID: 215587  Cd Length: 211  Bit Score: 99.36  E-value: 2.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992    7 KLVIVGDGACGKTCLLIVFSKDQFPDVyVPTVFENY-VADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:PLN03118  16 KILLIGDSGVGKSSLLVSFISSSVEDL-APTIGVDFkIKQLTVGGKRLKLTIWDTAGQERFRTLTSSYYRNAQGIILVYD 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   86 IDSPDSLENIPEKWTPEVRHFCPNVPII--LVGNKRDLRSDPQTVRelakmkqepvkpEQGRAIAEQIGAfAYLECSAKT 163
Cdd:PLN03118  95 VTRRETFTNLSDVWGKEVELYSTNQDCVkmLVGNKVDRESERDVSR------------EEGMALAKEHGC-LFLECSAKT 161
                        170
                 ....*....|
gi 17541992  164 KDGIREVFEK 173
Cdd:PLN03118 162 RENVEQCFEE 171
 
Name Accession Description Interval E-value
RhoA_like cd01870
Ras homology family A (RhoA)-like includes RhoA, RhoB and RhoC; The RhoA subfamily consists of ...
5-179 1.59e-135

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: 380.62  E-value: 1.59e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   5 RKKLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCF 84
Cdd:cd01870   1 RKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  85 SIDSPDSLENIPEKWTPEVRHFCPNVPIILVGNKRDLRSDPQTVRELAKMKQEPVKPEQGRAIAEQIGAFAYLECSAKTK 164
Cdd:cd01870  81 SIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRNDEHTIRELAKMKQEPVKPEEGRAMAEKIGAFGYLECSAKTK 160
                       170
                ....*....|....*
gi 17541992 165 DGIREVFEKATQAAL 179
Cdd:cd01870 161 EGVREVFEMATRAAL 175
RHO smart00174
Rho (Ras homology) subfamily of Ras-like small GTPases; Members of this subfamily of Ras-like ...
8-181 1.54e-123

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: 349.99  E-value: 1.54e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992      8 LVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSID 87
Cdd:smart00174   1 LVVVGDGAVGKTCLLIVYTTNAFPEDYVPTVFENYSADVEVDGKPVELGLWDTAGQEDYDRLRPLSYPDTDVFLICFSVD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992     88 SPDSLENIPEKWTPEVRHFCPNVPIILVGNKRDLRSDPQTVRELAKMKQEPVKPEQGRAIAEQIGAFAYLECSAKTKDGI 167
Cdd:smart00174  81 SPASFENVKEKWYPEVKHFCPNVPIILVGTKLDLRNDKSTLEELSKKKQEPVTYEQGQALAKRIGAVKYLECSALTQEGV 160
                          170
                   ....*....|....
gi 17541992    168 REVFEKATQAALQQ 181
Cdd:smart00174 161 REVFEEAIRAALNK 174
Rho cd00157
Ras homology family (Rho) of small guanosine triphosphatases (GTPases); Members of the Rho ...
7-177 4.31e-107

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: 307.93  E-value: 4.31e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSI 86
Cdd:cd00157   2 KIVVVGDGAVGKTCLLISYTTNKFPTEYVPTVFDNYSANVTVDGKQVNLGLWDTAGQEEYDRLRPLSYPQTDVFLLCFSV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  87 DSPDSLENIPEKWTPEVRHFCPNVPIILVGNKRDLRSDPQTVRELAKmKQEPVKPEQGRAIAEQIGAFAYLECSAKTKDG 166
Cdd:cd00157  82 DSPSSFENVKTKWYPEIKHYCPNVPIILVGTKIDLRDDGNTLKKLEK-KQKPITPEEGEKLAKEIGAVKYMECSALTQEG 160
                       170
                ....*....|.
gi 17541992 167 IREVFEKATQA 177
Cdd:cd00157 161 LKEVFDEAIRA 171
Rho4_like cd04132
Ras homology family 4 (Rho4) of small guanosine triphosphatases (GTPases)-like; Rho4 is a ...
4-181 3.29e-105

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: 304.26  E-value: 3.29e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   4 IRKKLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEV-DGKQVELALWDTAGQEDYDRLRPLSYPDTDVILM 82
Cdd:cd04132   2 LKVKIVVVGDGGCGKTCLLMVYAQGSFPEEYVPTVFENYVTTLQVpNGKIIELALWDTAGQEDYDRLRPLSYPDVDVILI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  83 CFSIDSPDSLENIPEKWTPEVRHFCPNVPIILVGNKRDLRSDPQTVRELAKMKQEPVKPEQGRAIAEQIGAFAYLECSAK 162
Cdd:cd04132  82 CYSVDNPTSLDNVEDKWYPEVNHFCPGTPIVLVGLKTDLRKDKNSVSKLRAQGLEPVTPEQGESVAKSIGAVAYIECSAK 161
                       170
                ....*....|....*....
gi 17541992 163 TKDGIREVFEKATQAALQQ 181
Cdd:cd04132 162 LMENVDEVFDAAINVALSK 180
RhoG cd01875
Ras homolog family, member G (RhoG) of small guanosine triphosphatases (GTPases); RhoG is a ...
7-179 9.17e-88

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: 259.94  E-value: 9.17e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSI 86
Cdd:cd01875   5 KCVVVGDGAVGKTCLLICYTTNAFPKEYIPTVFDNYSAQTAVDGRTVSLNLWDTAGQEEYDRLRTLSYPQTNVFIICFSI 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  87 DSPDSLENIPEKWTPEVRHFCPNVPIILVGNKRDLRSDPQTVRELAKMKQEPVKPEQGRAIAEQIGAFAYLECSAKTKDG 166
Cdd:cd01875  85 ASPSSYENVRHKWHPEVCHHCPNVPILLVGTKKDLRNDADTLKKLKEQGQAPITPQQGGALAKQIHAVKYLECSALNQDG 164
                       170
                ....*....|...
gi 17541992 167 IREVFEKATQAAL 179
Cdd:cd01875 165 VKEVFAEAVRAVL 177
Rnd cd04131
Rho family GTPase subfamily Rnd includes Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8; The Rnd ...
5-179 1.74e-85

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: 253.51  E-value: 1.74e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   5 RKKLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCF 84
Cdd:cd04131   1 RCKIVLVGDSQCGKTALLQVFAKDSFPENYVPTVFENYTASFEVDKQRIELSLWDTSGSPYYDNVRPLSYPDSDAVLICF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  85 SIDSPDSLENIPEKWTPEVRHFCPNVPIILVGNKRDLRSDPQTVRELAKMKQEPVKPEQGRAIAEQIGAFAYLECSAKTK 164
Cdd:cd04131  81 DISRPETLDSVLKKWKGEVREFCPNTPVLLVGCKSDLRTDLSTLTELSNKRQIPVSHEQGRNLAKQIGAAAYVECSAKTS 160
                       170
                ....*....|....*.
gi 17541992 165 D-GIREVFEKATQAAL 179
Cdd:cd04131 161 EnSVRDVFEMATLACL 176
Rho2 cd04129
Ras homology family 2 (Rho2) of small guanosine triphosphatases (GTPases); Rho2 is a fungal ...
5-179 9.27e-84

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  Cd Length: 190  Bit Score: 249.75  E-value: 9.27e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   5 RKKLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCF 84
Cdd:cd04129   1 RRKLVIVGDGACGKTSLLYVFTLGEFPEEYHPTVFENYVTDCRVDGKPVQLALWDTAGQEEYERLRPLSYSKAHVILIGF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  85 SIDSPDSLENIPEKWTPEVRHFCPNVPIILVGNKRDLRSDPQTVRELAkmKQEPVKPEQGRAIAEQIGAFAYLECSAKTK 164
Cdd:cd04129  81 AIDTPDSLENVRTKWIEEVRRYCPNVPVILVGLKKDLRQEAVAKGNYA--TDEFVPIQQAKLVARAIGAKKYMECSALTG 158
                       170
                ....*....|....*
gi 17541992 165 DGIREVFEKATQAAL 179
Cdd:cd04129 159 EGVDDVFEAATRAAL 173
Rac1_like cd01871
Ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1)-like ...
7-177 9.86e-83

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: 246.26  E-value: 9.86e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSI 86
Cdd:cd01871   3 KCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  87 DSPDSLENIPEKWTPEVRHFCPNVPIILVGNKRDLRSDPQTVRELAKMKQEPVKPEQGRAIAEQIGAFAYLECSAKTKDG 166
Cdd:cd01871  83 VSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLRDDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRG 162
                       170
                ....*....|.
gi 17541992 167 IREVFEKATQA 177
Cdd:cd01871 163 LKTVFDEAIRA 173
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
7-180 7.76e-77

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: 306559  Cd Length: 162  Bit Score: 230.85  E-value: 7.76e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992     7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTV-FENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:pfam00071   1 KLVLVGDGGVGKSSLLIRFTQNKFPEEYIPTIgVDFYTKTVEVDGKTVKLQIWDTAGQERFRALRPLYYRGADGFLLVYD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992    86 IDSPDSLENIPeKWTPEVRHFCP-NVPIILVGNKRDLRSdpqtvrelakmkQEPVKPEQGRAIAEQIGaFAYLECSAKTK 164
Cdd:pfam00071  81 ITSRDSFENVK-KWVEEILRHADeNVPIVLVGNKCDLED------------QRVVSTEEGEALAKELG-LPFMETSAKTN 146
                         170
                  ....*....|....*.
gi 17541992   165 DGIREVFEKATQAALQ 180
Cdd:pfam00071 147 ENVEEAFEELAREILK 162
Cdc42 cd01874
cell division cycle 42 (Cdc42) is a small GTPase of the Rho family; Cdc42 is an essential ...
7-179 8.02e-77

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: 231.30  E-value: 8.02e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSI 86
Cdd:cd01874   3 KCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAGQEDYDRLRPLSYPQTDVFLVCFSV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  87 DSPDSLENIPEKWTPEVRHFCPNVPIILVGNKRDLRSDPQTVRELAKMKQEPVKPEQGRAIAEQIGAFAYLECSAKTKDG 166
Cdd:cd01874  83 VSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLRDDPSTIEKLAKNKQKPITPETGEKLARDLKAVKYVECSALTQKG 162
                       170
                ....*....|...
gi 17541992 167 IREVFEKATQAAL 179
Cdd:cd01874 163 LKNVFDEAILAAL 175
Rnd2_Rho7 cd04173
Rnd2/Rho7 GTPases; Rnd2/Rho7 is a member of the novel Rho subfamily Rnd, together with Rnd1 ...
5-181 1.02e-74

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  Cd Length: 221  Bit Score: 227.60  E-value: 1.02e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   5 RKKLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCF 84
Cdd:cd04173   1 RCKIVVVGDTQCGKTALLHVFAKDNYPESYVPTVFENYTASFEIDKHRIELNMWDTSGSSYYDNVRPLAYPDSDAVLICF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  85 SIDSPDSLENIPEKWTPEVRHFCPNVPIILVGNKRDLRSDPQTVRELAKMKQEPVKPEQGRAIAEQIGAFAYLECSAK-T 163
Cdd:cd04173  81 DISRPETLDSVLKKWQGETQEFCPNAKLVLVGCKLDMRTDLSTLRELSKQRLIPVTHEQGSLLARQLGAVAYVECSSRmS 160
                       170
                ....*....|....*...
gi 17541992 164 KDGIREVFEKATQAALQQ 181
Cdd:cd04173 161 ENSVRDVFHVTTLASVRR 178
Rnd3_RhoE_Rho8 cd04172
Rnd3/RhoE/Rho8 GTPases; Rnd3/RhoE/Rho8 subfamily. Rnd3/RhoE/Rho8 is a member of the novel Rho ...
4-181 2.52e-74

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: 225.32  E-value: 2.52e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   4 IRKKLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMC 83
Cdd:cd04172   4 VKCKIVVVGDSQCGKTALLHVFAKDCFPENYVPTVFENYTASFEIDTQRIELSLWDTSGSPYYDNVRPLSYPDSDAVLIC 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  84 FSIDSPDSLENIPEKWTPEVRHFCPNVPIILVGNKRDLRSDPQTVRELAKMKQEPVKPEQGRAIAEQIGAFAYLECSA-K 162
Cdd:cd04172  84 FDISRPETLDSVLKKWKGEIQEFCPNTKMLLVGCKSDLRTDVSTLVELSNHRQTPVSYDQGANMAKQIGAATYIECSAlQ 163
                       170
                ....*....|....*....
gi 17541992 163 TKDGIREVFEKATQAALQQ 181
Cdd:cd04172 164 SENSVRDIFHVATLACVNK 182
Rho3 cd04134
Ras homology family 3 (Rho3) of small guanosine triphosphatases (GTPases); Rho3 is a member of ...
6-179 4.49e-73

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: 222.04  E-value: 4.49e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   6 KKLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:cd04134   1 RKVVVLGDGACGKTSLLNVFTRGYFPQVYEPTVFENYIHDIFVDGLAVELSLWDTAGQEEFDRLRSLSYADTHVIMLCFS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  86 IDSPDSLENIPEKWTPEVRHFCPNVPIILVGNKRDLRSDPQTVRELAKMKQEpvkpEQGRAIAEQIGAFAYLECSAKTKD 165
Cdd:cd04134  81 VDNPDSLENVESKWLAEIRHHCPGVKLVLVALKCDLREPRNERDRGTHTISY----EEGLAVAKRINACRYLECSAKLNR 156
                       170
                ....*....|....
gi 17541992 166 GIREVFEKATQAAL 179
Cdd:cd04134 157 GVNEAFTEAARVAL 170
Wrch_1 cd04130
Wnt-1 responsive Cdc42 homolog (Wrch-1) is a Rho family GTPase similar to Cdc42; Wrch-1 (Wnt-1 ...
7-178 2.54e-72

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: 219.58  E-value: 2.54e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSI 86
Cdd:cd04130   2 KCVLVGDGAVGKTSLIVSYTTNGYPTEYVPTAFDNFSVVVLVDGKPVRLQLCDTAGQDEFDKLRPLCYPDTDVFLLCFSV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  87 DSPDSLENIPEKWTPEVRHFCPNVPIILVGNKRDLRSDPQTVRELAKMKQEPVKPEQGRAIAEQIGAFAYLECSAKTKDG 166
Cdd:cd04130  82 VNPSSFQNISEKWIPEIRKHNPKAPIILVGTQADLRTDVNVLIQLARYGEKPVSQSRAKALAEKIGACEYIECSALTQKN 161
                       170
                ....*....|..
gi 17541992 167 IREVFEKATQAA 178
Cdd:cd04130 162 LKEVFDTAILAG 173
Tc10 cd04135
Rho GTPase TC10 (Tc10); TC10 is a Rho family protein that has been shown to induce microspike ...
7-179 1.96e-70

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: 214.88  E-value: 1.96e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSI 86
Cdd:cd04135   2 KCVVVGDGAVGKTCLLMSYANDAFPEEYVPTVFDHYAVSVTVGGKQYLLGLYDTAGQEDYDRLRPLSYPMTDVFLICFSV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  87 DSPDSLENIPEKWTPEVRHFCPNVPIILVGNKRDLRSDPQTVRELAKMKQEPVKPEQGRAIAEQIGAFAYLECSAKTKDG 166
Cdd:cd04135  82 VNPASFQNVKEEWVPELKEYAPNVPYLLIGTQIDLRDDPKTLARLNDMKEKPITVEQGQKLAKEIGACCYVECSALTQKG 161
                       170
                ....*....|...
gi 17541992 167 IREVFEKATQAAL 179
Cdd:cd04135 162 LKTVFDEAIIAIL 174
Rnd1_Rho6 cd04174
Rnd1/Rho6 GTPases; Rnd1/Rho6 is a member of the novel Rho subfamily Rnd, together with Rnd2 ...
2-181 1.39e-68

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  Cd Length: 232  Bit Score: 212.23  E-value: 1.39e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   2 AAIRKKLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVIL 81
Cdd:cd04174  10 LVVRCKLVLVGDVQCGKTAMLQVLAKDCYPETYVPTVFENYTACLETEEQRVELSLWDTSGSPYYDNVRPLCYSDSDAVL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  82 MCFSIDSPDSLENIPEKWTPEVRHFCPNVPIILVGNKRDLRSDPQTVRELAKMKQEPVKPEQGRAIAEQIGAFAYLECSA 161
Cdd:cd04174  90 LCFDISRPEIFDSALKKWRAEILDYCPSTRILLIGCKTDLRTDLSTLMELSNQKQAPISYEQGCAMAKQLGAEAYLECSA 169
                       170       180
                ....*....|....*....|.
gi 17541992 162 KTKD-GIREVFEKATQAALQQ 181
Cdd:cd04174 170 FTSEkSIHSIFRTASLLCINK 190
Rop_like cd04133
Rho-related protein from plants (Rop)-like; The Rop (Rho-related protein from plants) ...
7-179 6.73e-65

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: 200.84  E-value: 6.73e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSI 86
Cdd:cd04133   3 KCVTVGDGAVGKTCMLISYTSNTFPTDYVPTVFDNFSANVVVDGNTVNLGLWDTAGQEDYNRLRPLSYRGADVFLLAFSL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  87 DSPDSLENIPEKWTPEVRHFCPNVPIILVGNKRDLRSDPQTVRELAKMKqePVKPEQGRAIAEQIGAFAYLECSAKTKDG 166
Cdd:cd04133  83 ISKASYENVLKKWIPELRHYAPGVPIVLVGTKLDLRDDKQFFADHPGAV--PITTAQGEELRKQIGAAAYIECSSKTQQN 160
                       170
                ....*....|...
gi 17541992 167 IREVFEKATQAAL 179
Cdd:cd04133 161 VKAVFDAAIKVVL 173
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
7-176 2.33e-52

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: 168.02  E-value: 2.33e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVA-DIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:cd00154   2 KIVLIGDSGVGKTSLLLRFVDNKFSENYKSTIGVDFKSkTIEVDGKKVKLQIWDTAGQERFRSITSSYYRGAHGAILVYD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  86 IDSPDSLENIpEKWTPEVRHFCP-NVPIILVGNKRDLRSDPQtvrelakmkqepVKPEQGRAIAEQIGAFaYLECSAKTK 164
Cdd:cd00154  82 VTNRESFENL-DKWLNELKEYAPpNIPIILVGNKSDLEDERQ------------VSTEEAQQFAKENGLL-FFETSAKTG 147
                       170
                ....*....|..
gi 17541992 165 DGIREVFEKATQ 176
Cdd:cd00154 148 ENVDEAFESLAR 159
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
5-159 2.84e-50

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


Pssm-ID: 272973  Cd Length: 162  Bit Score: 162.93  E-value: 2.84e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992     5 RKKLVIVGDGACGKTCLLIVFSKDQ-FPDVYVPTVFENYVAD-IEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILM 82
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKgSITEYYPGTTRNYVTTvIEEDGKTYKFNLLDTAGQEDYDAIRRLYYPQVERSLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992    83 CFSIDSP-DSLENIPEKWTPEVRHFCP-NVPIILVGNKRDLRS---DPQTVRELAKMKQEPVKPEQGRAIAEQIGAFAYL 157
Cdd:TIGR00231  81 VFDIVILvLDVEEILEKQTKEIIHHADsGVPIILVGNKIDLKDadlKTHVASEFAKLNGEPIIPLSAETGKNIDSAFKIV 160

                  ..
gi 17541992   158 EC 159
Cdd:TIGR00231 161 EA 162
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
4-181 7.31e-46

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 224025  Cd Length: 219  Bit Score: 153.58  E-value: 7.31e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   4 IRKKLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVA-DIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILM 82
Cdd:COG1100   4 KEFKIVVLGDGGVGKTTLLNRLVGDEFPEGYPPTIGNLDPAkTIEPYRRNIKLQLWDTAGQEEYRSLRPEYYRGANGILI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  83 CFSIDSPDSLENIPEKWTPEVRHFCP-NVPIILVGNKRDLRSDPQTVRELAK--MKQEPVKPEQGRAIAEQIGAFAYLEC 159
Cdd:COG1100  84 VYDSTLRESSDELTEEWLEELRELAPdDVPILLVGNKIDLFDEQSSSEEILNqlNREVVLLVLAPKAVLPEVANPALLET 163
                       170       180
                ....*....|....*....|....
gi 17541992 160 SAK--TKDGIREVFEKATQAALQQ 181
Cdd:COG1100 164 SAKslTGPNVNELFKELLRKLLEE 187
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
7-181 3.48e-41

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


Pssm-ID: 197555  Cd Length: 164  Bit Score: 139.57  E-value: 3.48e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992      7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTV-FENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:smart00175   2 KIILIGDSGVGKSSLLSRFTDGKFSEQYKSTIgVDFKTKTIEVDGKRVKLQIWDTAGQERFRSITSSYYRGAVGALLVYD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992     86 IDSPDSLENIpEKWTPEVRHFC-PNVPIILVGNKRDLRSDPQtvrelakmkqepVKPEQGRAIAEQIGAFaYLECSAKTK 164
Cdd:smart00175  82 ITNRESFENL-ENWLKELREYAsPNVVIMLVGNKSDLEEQRQ------------VSREEAEAFAEEHGLP-FFETSAKTN 147
                          170
                   ....*....|....*..
gi 17541992    165 DGIREVFEKATQAALQQ 181
Cdd:smart00175 148 TNVEEAFEELAREILKR 164
Ras cd00876
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ...
7-172 9.02e-38

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: 130.72  E-value: 9.02e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSI 86
Cdd:cd00876   1 KLVVLGAGGVGKSALTIRFVSGEFVEEYDPTIEDSYRKQIVVDGETYTLDILDTAGQEEFSAMRDQYIRNGDGFILVYSI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  87 DSPDSLENIPE--KWTPEVRHfCPNVPIILVGNKRDLrsdpQTVRElakmkqepVKPEQGRAIAEQIGAfAYLECSAKTK 164
Cdd:cd00876  81 TSRESFEEIKNirEQILRVKD-KEDVPIVLVGNKCDL----ENERQ--------VSTEEGEALAEEWGC-PFLETSAKTN 146

                ....*...
gi 17541992 165 DGIREVFE 172
Cdd:cd00876 147 INIDELFN 154
RhoBTB cd01873
RhoBTB protein is an atypical member of the Rho family of small GTPases; Members of the RhoBTB ...
7-178 9.84e-38

RhoBTB protein is an atypical member of the Rho family of small GTPases; Members of the RhoBTB subfamily of Rho GTPases are present in vertebrates, Drosophila, and Dictyostelium. RhoBTB proteins are characterized by a modular organization, consisting of a GTPase domain, a proline rich region, a tandem of two BTB (Broad-Complex, Tramtrack, and Bric a brac) domains, and a C-terminal region of unknown function. RhoBTB proteins may act as docking points for multiple components participating in signal transduction cascades. RhoBTB genes appeared upregulated in some cancer cell lines, suggesting a participation of RhoBTB proteins in the pathogenesis of particular tumors. Note that the Dictyostelium RacA GTPase domain is more closely related to Rac proteins than to RhoBTB proteins, where RacA actually belongs. Thus, the Dictyostelium RacA is not included here. Most Rho proteins contain a lipid modification site at the C-terminus; however, RhoBTB is one of few Rho subfamilies that lack this feature.


Pssm-ID: 133275  Cd Length: 195  Bit Score: 131.63  E-value: 9.84e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLI------VFSKDQFPDVYVPTVF--ENYVADIEV--------DGKQVELALWDTAGqeDYDRLR 70
Cdd:cd01873   4 KCVVVGDNAVGKTRLICaracnkTLTQYQLLATHVPTVWaiDQYRVCQEVlersrdvvDGVSVSLRLWDTFG--DHDKDR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  71 PLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVRHFCPNVPIILVGNKRDLR-----SDPQTVRELAK--MKQEPVKPEQ 143
Cdd:cd01873  82 RFAYGRSDVVLLCFSIASPNSLRNVKTMWYPEIRHFCPRVPVILVGCKLDLRyadldEVNRARRPLARpiKNADILPPET 161
                       170       180       190
                ....*....|....*....|....*....|....*
gi 17541992 144 GRAIAEQIGaFAYLECSAKTKDGIREVFEKATQAA 178
Cdd:cd01873 162 GRAVAKELG-IPYYETSVVTQFGVKDVFDNAIRAA 195
small_GTPase smart00010
Small GTPase of the Ras superfamily; ill-defined subfamily; SMART predicts Ras-like small ...
7-172 5.37e-34

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: 120.74  E-value: 5.37e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992      7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSI 86
Cdd:smart00010   4 KLVVLGGGGVGKSALTIQFVQGHFVDEYDPTIEDSYRKQIEIDGEVCLLDILDTAGQEEFSAMRDQYMRTGEGFLLVYSI 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992     87 DSPDSLENIPEKWTP--EVRHfCPNVPIILVGNKRDLRSDPQtvrelakmkqepVKPEQGRAIAEQIGAfAYLECSAKTK 164
Cdd:smart00010  84 TDRQSFEEIAKFREQilRVKD-RDDVPIVLVGNKCDLENERV------------VSTEEGKELARQWGC-PFLETSAKER 149

                   ....*...
gi 17541992    165 DGIREVFE 172
Cdd:smart00010 150 INVDEAFY 157
RAS smart00173
Ras subfamily of RAS small GTPases; Similar in fold and function to the bacterial EF-Tu GTPase. ...
7-172 5.87e-34

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: 120.74  E-value: 5.87e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992      7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSI 86
Cdd:smart00173   2 KLVVLGSGGVGKSALTIQFIQGHFVDDYDPTIEDSYRKQIEIDGEVCLLDILDTAGQEEFSAMRDQYMRTGEGFLLVYSI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992     87 DSPDSLENIPE--KWTPEVRHfCPNVPIILVGNKRDLRSDPQtvrelakmkqepVKPEQGRAIAEQIGAfAYLECSAKTK 164
Cdd:smart00173  82 TDRQSFEEIKKfrEQILRVKD-RDDVPIVLVGNKCDLESERV------------VSTEEGKELARQWGC-PFLETSAKER 147

                   ....*...
gi 17541992    165 DGIREVFE 172
Cdd:smart00173 148 VNVDEAFY 155
Rab21 cd04123
Rab GTPase family 21 (Rab21); The localization and function of Rab21 are not clearly defined, ...
7-172 3.23e-32

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: 116.17  E-value: 3.23e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVAD-IEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:cd04123   2 KVVLLGEGRVGKTSLVLRYVENKFNEKHESTTQASFFQKtVNIGGKRIDLAIWDTAGQERYHALGPIYYRDADGAILVYD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  86 IDSPDSLENIpEKWTPEVRHFC-PNVPIILVGNKRDLRsdpqtvrelakmKQEPVKPEQGRAIAEQIGAfAYLECSAKTK 164
Cdd:cd04123  82 ITDADSFQKV-KKWIKELKQMRgNNISLVIVGNKIDLE------------RQRVVSKSEAEEYAKSVGA-KHFETSAKTG 147

                ....*...
gi 17541992 165 DGIREVFE 172
Cdd:cd04123 148 KGIEELFL 155
Rab5_related cd01860
Rab-related GTPase family includes Rab5 and Rab22; regulates early endosome fusion; The ...
7-172 1.12e-31

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: 114.96  E-value: 1.12e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTV---FENYVadIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMC 83
Cdd:cd01860   3 KLVLLGDSSVGKSSIVLRFVKNEFSENQESTIgaaFLTQT--VNLDDTTVKFEIWDTAGQERYRSLAPMYYRGAAAAIVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  84 FSIDSPDSLENIpEKWTPEVR-HFCPNVPIILVGNKRDLRSDpqtvRElakmkqepVKPEQGRAIAEQIGAFaYLECSAK 162
Cdd:cd01860  81 YDITSEESFEKA-KSWVKELQeHGPPNIVIALAGNKADLESK----RQ--------VSTEEAQEYADENGLL-FMETSAK 146
                       170
                ....*....|
gi 17541992 163 TKDGIREVFE 172
Cdd:cd01860 147 TGENVNELFT 156
Rab18 cd01863
Rab GTPase family 18 (Rab18); Rab18 subfamily. Mammalian Rab18 is implicated in endocytic ...
7-172 1.40e-30

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: 112.02  E-value: 1.40e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENY-VADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:cd01863   2 KILLIGDSGVGKSSLLLRFTDDTFDEDLSSTIGVDFkVKTVTVDGKKVKLAIWDTAGQERFRTLTSSYYRGAQGVILVYD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  86 IDSPDSLENIpEKWTPEVRHFC--PNVPIILVGNKRDLRSdpqtvRELAKmkqepvkpEQGRAIAEQIGAFaYLECSAKT 163
Cdd:cd01863  82 VTRRDTFDNL-DTWLNELDTYStnPDAVKMLVGNKIDKEN-----REVTR--------EEGQKFARKHNML-FIETSAKT 146

                ....*....
gi 17541992 164 KDGIREVFE 172
Cdd:cd01863 147 RIGVQQAFE 155
Rab6 cd01861
Rab GTPase family 6 (Rab6); Rab6 is involved in microtubule-dependent transport pathways ...
6-177 3.15e-30

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: 110.79  E-value: 3.15e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   6 KKLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADI-EVDGKQVELALWDTAGQEDYDRLRPlSY-PDTDVILMC 83
Cdd:cd01861   1 HKLVFLGDQSVGKTSIITRFMYDTFDNQYQATIGIDFLSKTmYVDDKTVRLQLWDTAGQERFRSLIP-SYiRDSSVAVVV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  84 FSIDSPDSLENIpEKWTPEVRHFCPNVPII-LVGNKRDLRSDPQtvrelakmkqepVKPEQGRAIAEQIGAFaYLECSAK 162
Cdd:cd01861  80 YDITNRQSFDNT-DKWIDDVRDERGNDVIIvLVGNKTDLSDKRQ------------VSTEEGEKKAKENNAM-FIETSAK 145
                       170
                ....*....|....*
gi 17541992 163 TKDGIREVFEKATQA 177
Cdd:cd01861 146 AGHNVKQLFKKIAQA 160
Rab8_Rab10_Rab13_like cd01867
Rab GTPase families 8, 10, 13 (Rab8, Rab10, Rab13); Rab8/Sec4/Ypt2 are known or suspected to ...
7-172 2.03e-29

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: 108.89  E-value: 2.03e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTV---FEnyVADIEVDGKQVELALWDTAGQEdydRLRPLS---YPDTDVI 80
Cdd:cd01867   5 KLLLIGDSGVGKSCLLLRFSEDSFNPSFISTIgidFK--IRTIELDGKKIKLQIWDTAGQE---RFRTITtsyYRGAMGI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  81 LMCFSIDSPDSLENIpEKWTPEV-RHFCPNVPIILVGNKRDLRSDPQtvrelakmkqepVKPEQGRAIAEQIGaFAYLEC 159
Cdd:cd01867  80 ILVYDITDEKSFENI-KNWMRNIdEHASEDVERMLVGNKCDMEEKRV------------VSKEEGEALAREYG-IKFLET 145
                       170
                ....*....|...
gi 17541992 160 SAKTKDGIREVFE 172
Cdd:cd01867 146 SAKANINVEEAFL 158
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
7-120 2.57e-29

Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial Rho proteins (Miro-1, and Miro-2) and atypical Rho GTPases. Full-length proteins have a unique domain 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: 312094  Cd Length: 114  Bit Score: 107.21  E-value: 2.57e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992     7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVA----DIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILM 82
Cdd:pfam08477   1 KIVLLGDSGVGKTSLLKRFVDDTFDPKYQSTIGVDFKTktvlENDDNGKKVKLNIWDTAGQERFRSLHPFYYRGAAAALL 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 17541992    83 CFSIDSPDSLenipEKWTPEVRHFCPNVPIILVGNKRD 120
Cdd:pfam08477  81 VYDSRTFSNL----KYWLRELREYAGNSPVILVGNKID 114
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
9-176 1.06e-28

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  Cd Length: 161  Bit Score: 107.16  E-value: 1.06e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   9 VIVGDGACGKTCLLIVFSKDQF---PDVYVPTVFENYVaDIEVDGKQVELALWDTAGQEDYDRLRP-----LSYPDTDVI 80
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVgevSDVPGTTRDPDVY-VKELDKGKVKLVLVDTPGLDEFGGLGReelarLLLRGADLI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  81 LMCFSIDSPDSLENIpeKWTPEVRHFCPNVPIILVGNKRDLRSDpqtvrelakmkqEPVKPEQGRAIAEQIGAFAYLECS 160
Cdd:cd00882  80 LLVVDSTDRESEEDA--KLLILRRLRKEGIPIILVGNKIDLLEE------------REVEELLRLEELAKILGVPVFEVS 145
                       170
                ....*....|....*.
gi 17541992 161 AKTKDGIREVFEKATQ 176
Cdd:cd00882 146 AKTGEGVDELFEKLIE 161
Rab1_Ypt1 cd01869
Rab GTPase family 1 includes the yeast homolog Ypt1; Rab1/Ypt1 subfamily. Rab1 is found in ...
7-177 1.81e-28

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: 106.64  E-value: 1.81e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENY-VADIEVDGKQVELALWDTAGQEdydRLRPLS---YPDTDVILM 82
Cdd:cd01869   4 KLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFkIRTIELDGKTVKLQIWDTAGQE---RFRTITssyYRGAHGIII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  83 CFSIDSPDSLENIPEkWTPEVRHF-CPNVPIILVGNKRDLRSdpqtvrelakmkQEPVKPEQGRAIAEQIGaFAYLECSA 161
Cdd:cd01869  81 VYDVTDQESFNNVKQ-WLQEIDRYaSENVNKLLVGNKCDLTD------------KKVVDYTEAKEFADELG-IPFLETSA 146
                       170
                ....*....|....*.
gi 17541992 162 KTKDGIREVFEKATQA 177
Cdd:cd01869 147 KNATNVEEAFMTMARE 162
RalA_RalB cd04139
Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily ...
7-171 9.99e-28

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: 104.43  E-value: 9.99e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSI 86
Cdd:cd04139   2 KVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGEEVQLNILDTAGQEDYAAIRDNYFRSGEGFLLVFSI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  87 DSPDSLENIPEKWTPEVRH-FCPNVPIILVGNKRDL---RSDPQtvrelakmkqepvkpEQGRAIAEQIGAfAYLECSAK 162
Cdd:cd04139  82 TDMESFTALAEFREQILRVkEDDNVPLLLVGNKCDLedkRQVSV---------------EEAANLAEQWGV-NYVETSAK 145

                ....*....
gi 17541992 163 TKDGIREVF 171
Cdd:cd04139 146 TRANVDKVF 154
RSR1 cd04177
RSR1/Bud1p family GTPase; RSR1/Bud1p is a member of the Rap subfamily of the Ras family that ...
7-171 7.41e-27

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: 102.18  E-value: 7.41e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSI 86
Cdd:cd04177   3 KIVVLGAGGVGKSALTVQFVQNVFIESYDPTIEDSYRKQVEIDGRQCDLEILDTAGTEQFTAMRELYIKSGQGFLLVYSV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  87 DSPDSLENIPEKWTPEVR-HFCPNVPIILVGNKRDLRSDPQtvrelakmkqepVKPEQGRAIAEQIGAFAYLECSAKTKD 165
Cdd:cd04177  83 TSEASLNELGELREQVLRiKDSDNVPMVLVGNKADLEDDRQ------------VSREDGVSLSQQWGNVPFYETSARKRT 150

                ....*.
gi 17541992 166 GIREVF 171
Cdd:cd04177 151 NVDEVF 156
Rab39 cd04111
Rab GTPase family 39 (Rab39); Found in eukaryotes, Rab39 is mainly found in epithelial cell ...
7-176 1.09e-25

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  Cd Length: 211  Bit Score: 100.22  E-value: 1.09e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTV---FENYVADIEvDGKQVELALWDTAGQEdydRLRPL--SYPDTDV-I 80
Cdd:cd04111   4 RLIVIGDSTVGKSSLLKRFTEGRFAEVSDPTVgvdFFSRLIEIE-PGVRIKLQLWDTAGQE---RFRSItrSYYRNSVgV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  81 LMCFSIDSPDSLENIPEkWTPEVR-HFCPNVPI-ILVGNKRDLRSDPQtvrelakmkqepVKPEQGRAIAEQIGaFAYLE 158
Cdd:cd04111  80 LLVFDITNRESFEHVHD-WLEEARsHIQPHRPVfILVGHKCDLESQRQ------------VTREEAEKLAKDLG-MKYIE 145
                       170
                ....*....|....*...
gi 17541992 159 CSAKTKDGIREVFEKATQ 176
Cdd:cd04111 146 TSARTGDNVEEAFELLTQ 163
RheB cd04137
Ras Homolog Enriched in Brain (RheB) is a small GTPase; Rheb (Ras Homolog Enriched in Brain) ...
6-173 1.51e-25

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: 99.24  E-value: 1.51e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   6 KKLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLrPLSYpDTDV--ILMC 83
Cdd:cd04137   2 RKIAVLGSRSVGKSSLTVQFVEGHFVESYYPTIENTFSKIITYKGQEYHLEIVDTAGQDEYSIL-PQKY-SIGIhgYILV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  84 FSIDSPDSLENIPEKWTPEVRHF-CPNVPIILVGNKRDLRSdpqtvrelakmkQEPVKPEQGRAIAEQIGAfAYLECSAK 162
Cdd:cd04137  80 YSVTSRKSFEVVKVIYDKILDMLgKESVPIVLVGNKSDLHM------------ERQVSAEEGKKLAESWGA-AFLESSAK 146
                       170
                ....*....|.
gi 17541992 163 TKDGIREVFEK 173
Cdd:cd04137 147 ENENVEEAFEL 157
Rab7 cd01862
Rab GTPase family 7 (Rab7); Rab7 subfamily. Rab7 is a small Rab GTPase that regulates ...
7-181 1.51e-25

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: 98.89  E-value: 1.51e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVA-DIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:cd01862   2 KVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTkEVTVDDRLVTLQIWDTAGQERFQSLGVAFYRGADCCVLVYD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  86 IDSPDSLENIpEKWTPEVR-HFCP----NVPIILVGNKRDLRSDPQtvrelakmkqepVKPEQGRAIAEQIGAFAYLECS 160
Cdd:cd01862  82 VTNPKSFESL-DSWRDEFLiQASPrdpeNFPFVVLGNKIDLEEKRQ------------VSTKKAQQWCKSKGNIPYFETS 148
                       170       180
                ....*....|....*....|.
gi 17541992 161 AKTKDGIREVFEKATQAALQQ 181
Cdd:cd01862 149 AKEAINVDQAFETIARLALEQ 169
PLN03118 PLN03118
Rab family protein; Provisional
7-173 2.21e-25

Rab family protein; Provisional


Pssm-ID: 215587  Cd Length: 211  Bit Score: 99.36  E-value: 2.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992    7 KLVIVGDGACGKTCLLIVFSKDQFPDVyVPTVFENY-VADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:PLN03118  16 KILLIGDSGVGKSSLLVSFISSSVEDL-APTIGVDFkIKQLTVGGKRLKLTIWDTAGQERFRTLTSSYYRNAQGIILVYD 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   86 IDSPDSLENIPEKWTPEVRHFCPNVPII--LVGNKRDLRSDPQTVRelakmkqepvkpEQGRAIAEQIGAfAYLECSAKT 163
Cdd:PLN03118  95 VTRRETFTNLSDVWGKEVELYSTNQDCVkmLVGNKVDRESERDVSR------------EEGMALAKEHGC-LFLECSAKT 161
                        170
                 ....*....|
gi 17541992  164 KDGIREVFEK 173
Cdd:PLN03118 162 RENVEQCFEE 171
Rab2 cd01866
Rab GTPase family 2 (Rab2); Rab2 is localized on cis-Golgi membranes and interacts with Golgi ...
7-171 2.36e-25

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: 98.26  E-value: 2.36e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVAD-IEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:cd01866   6 KYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARmITIDGKQIKLQIWDTAGQESFRSITRSYYRGAAGALLVYD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  86 IDSPDSLENIPeKWTPEVR-HFCPNVPIILVGNKRDLRSDpqtvRElakmkqepVKPEQGRAIAEQIGAFaYLECSAKTK 164
Cdd:cd01866  86 ITRRETFNHLT-SWLEDARqHSNSNMTIMLIGNKCDLESR----RE--------VSYEEGEAFAREHGLI-FMETSAKTA 151

                ....*..
gi 17541992 165 DGIREVF 171
Cdd:cd01866 152 SNVEEAF 158
Rab11_like cd01868
Rab GTPase family 11 (Rab11)-like includes Rab11a, Rab11b, and Rab25; Rab11a, Rab11b, and ...
7-173 2.71e-25

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: 98.02  E-value: 2.71e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTV---FENYVadIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMC 83
Cdd:cd01868   5 KIVLIGDSGVGKSNLLSRFTRNEFNLDSKSTIgveFATRT--IQIDGKTIKAQIWDTAGQERYRAITSAYYRGAVGALLV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  84 FSIDSPDSLENIpEKWTPEVRHFC-PNVPIILVGNKRDLRSDpqtvRElakmkqepVKPEQGRAIAEQIGAFaYLECSAK 162
Cdd:cd01868  83 YDITKKSTFENV-ERWLKELRDHAdSNIVIMLVGNKSDLRHL----RA--------VPTEEAKAFAEKNGLS-FIETSAL 148
                       170
                ....*....|.
gi 17541992 163 TKDGIREVFEK 173
Cdd:cd01868 149 DGTNVEEAFKQ 159
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, ...
7-171 6.86e-25

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: 96.72  E-value: 6.86e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSI 86
Cdd:cd04138   3 KLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  87 DSPDSLENIPEKWTPEVR-HFCPNVPIILVGNKRDLRSdpqtvrelakmkqEPVKPEQGRAIAEQIGAfAYLECSAKTKD 165
Cdd:cd04138  83 NSRKSFEDIHTYREQIKRvKDSDDVPMVLVGNKCDLAA-------------RTVSSRQGQDLAKSYGI-PYIETSAKTRQ 148

                ....*.
gi 17541992 166 GIREVF 171
Cdd:cd04138 149 GVEEAF 154
Rab15 cd04117
Rab GTPase family 15 (Rab15); Rab15 colocalizes with the transferrin receptor in early ...
7-180 7.26e-25

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: 96.97  E-value: 7.26e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENY-VADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:cd04117   2 RLLLIGDSGVGKTCLLCRFTDNEFHSSHISTIGVDFkMKTIEVDGIKVRIQIWDTAGQERYQTITKQYYRRAQGIFLVYD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  86 IDSPDSLENIpEKWTPEVRHFCPN-VPIILVGNKrdlrSDPQTVRELAKmkqepvkpEQGRAIAEQIGaFAYLECSAKTK 164
Cdd:cd04117  82 ISSERSYQHI-MKWVSDVDEYAPEgVQKILIGNK----ADEEQKRQVGD--------EQGNKLAKEYG-MDFFETSACTN 147
                       170
                ....*....|....*.
gi 17541992 165 DGIREVFEKATQAALQ 180
Cdd:cd04117 148 KNIKESFTRLTELVLQ 163
Rab19 cd01864
Rab GTPase family 19 (Rab19); Rab19 subfamily. Rab19 proteins are associated with Golgi stacks. ...
7-173 8.47e-25

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: 96.73  E-value: 8.47e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENY-VADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:cd01864   5 KIILIGDSNVGKTCVVQRFKSGTFSERQGNTIGVDFtMKTLEIEGKRVKLQIWDTAGQERFRTITQSYYRSANGAIIAYD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  86 IDSPDSLENIPeKWTPEVRHF-CPNVPIILVGNKRDLRsdpqtvrelakmKQEPVKPEQGRAIAEQIGAFAYLECSAKTK 164
Cdd:cd01864  85 ITRRSSFESVP-HWIEEVEKYgASNVVLLLIGNKCDLE------------EQREVLFEEACTLAEKNGMLAVLETSAKES 151

                ....*....
gi 17541992 165 DGIREVFEK 173
Cdd:cd01864 152 QNVEEAFLL 160
Rap1 cd04175
Rap1 family GTPase consists of Rap1a and Rap1b isoforms; The Rap1 subgroup is part of the Rap ...
7-171 1.19e-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: 96.43  E-value: 1.19e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSI 86
Cdd:cd04175   3 KLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDGQQCMLEILDTAGTEQFTAMRDLYMKNGQGFVLVYSI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  87 DSPDSLENIPEKWTPEVR-HFCPNVPIILVGNKRDLRSdpqtvrelakmkQEPVKPEQGRAIAEQIGAfAYLECSAKTKD 165
Cdd:cd04175  83 TAQSTFNDLQDLREQILRvKDTEDVPMILVGNKCDLED------------ERVVGKEQGQNLARQWGC-AFLETSAKAKI 149

                ....*.
gi 17541992 166 GIREVF 171
Cdd:cd04175 150 NVNEIF 155
Rap_like cd04136
Rap-like family consists of Rap1, Rap2 and RSR1; The Rap subfamily consists of the Rap1, Rap2, ...
7-171 1.32e-24

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: 96.09  E-value: 1.32e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSI 86
Cdd:cd04136   3 KLVVLGSGGVGKSALTVQFVQGIFVDKYDPTIEDSYRKQIEVDCQQCMLEILDTAGTEQFTAMRDLYIKNGQGFALVYSI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  87 DSPDSLENIPEKWTPEVR-HFCPNVPIILVGNKRDLRSDpqtvRELAKmkqepvkpEQGRAIAEQIGAFAYLECSAKTKD 165
Cdd:cd04136  83 TAQQSFNDLQDLREQILRvKDTEDVPMILVGNKCDLEDE----RVVSK--------EEGQNLARQWGNCPFLETSAKSKI 150

                ....*.
gi 17541992 166 GIREVF 171
Cdd:cd04136 151 NVDEIF 156
Miro1 cd01893
Mitochondrial Rho family 1 (Miro1), N-terminal; Miro1 subfamily. Miro (mitochondrial Rho) ...
7-179 3.61e-24

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: 95.10  E-value: 3.61e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVyVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSI 86
Cdd:cd01893   4 RIVLIGDEGVGKSSLIMSLVSEEFPEN-VPRVLPEITIPADVTPERVPTTIVDTSSRPQDRANLAAEIRKANVICLVYSV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  87 DSPDSLENIPEKWTPEVRHFCPNVPIILVGNKRDLRSDPQTVRELAKMkqEPVKpEQGRAIAeqigafAYLECSAKTKDG 166
Cdd:cd01893  83 DRPSTLERIRTKWLPLIRRLGVKVPIILVGNKSDLRDGSSQAGLEEEM--LPIM-NEFREIE------TCVECSAKTLIN 153
                       170
                ....*....|...
gi 17541992 167 IREVFEKATQAAL 179
Cdd:cd01893 154 VSEVFYYAQKAVL 166
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, ...
7-172 6.99e-24

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: 94.40  E-value: 6.99e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSI 86
Cdd:cd04145   4 KLVVVGGGGVGKSALTIQFIQSYFVTDYDPTIEDSYTKQCEIDGQWAILDILDTAGQEEFSAMREQYMRTGEGFLLVFSV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  87 DSPDSLENIPEKWTPEVR-HFCPNVPIILVGNKRDLrsdpqtvrelakMKQEPVKPEQGRAIAEQIgAFAYLECSAKTKD 165
Cdd:cd04145  84 TDRGSFEEVDKFHTQILRvKDRDEFPMILVGNKADL------------EHQRKVSREEGQELARKL-KIPYIETSAKDRL 150

                ....*..
gi 17541992 166 GIREVFE 172
Cdd:cd04145 151 NVDKAFH 157
Ras2 cd04144
Rat sarcoma (Ras) family 2 of small guanosine triphosphatases (GTPases); The Ras2 subfamily, ...
7-181 2.43e-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: 93.37  E-value: 2.43e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSI 86
Cdd:cd04144   1 KLVVLGDGGVGKTALTIQLCLNHFVETYDPTIEDSYRKQVVVDGQPCMLEVLDTAGQEEYTALRDQWIREGEGFILVYSI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  87 DSPDSLENIpEKWTPEVR----HFCPNVPIILVGNKrdlrSDPQTVRELAKmkqepvkpEQGRAIAEQIGAfAYLECSAK 162
Cdd:cd04144  81 TSRSTFERV-ERFREQIQrvkdESAADVPIMIVGNK----CDKVYEREVST--------EEGAALARRLGC-EFIEASAK 146
                       170
                ....*....|....*....
gi 17541992 163 TKDGIREVFEKATQAALQQ 181
Cdd:cd04144 147 TNVNVERAFYTLVRALRQQ 165
Rap2 cd04176
Rap2 family GTPase consists of Rap2a, Rap2b, and Rap2c; The Rap2 subgroup is part of the Rap ...
7-176 3.18e-23

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: 92.59  E-value: 3.18e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSI 86
Cdd:cd04176   3 KVVVLGSGGVGKSALTVQFVSGTFIEKYDPTIEDFYRKEIEVDSSPSVLEILDTAGTEQFASMRDLYIKNGQGFIVVYSL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  87 DSPDSLENIPEKWTPEVR-HFCPNVPIILVGNKRDLRSdpqtvrelakmkQEPVKPEQGRAIAEQIGAfAYLECSAKTKD 165
Cdd:cd04176  83 VNQQTFQDIKPMRDQIVRvKGYEKVPIILVGNKVDLES------------EREVSSAEGRALAEEWGC-PFMETSAKSKT 149
                       170
                ....*....|.
gi 17541992 166 GIREVFEKATQ 176
Cdd:cd04176 150 MVNELFAEIVR 160
Rab9 cd04116
Rab GTPase family 9 (Rab9); Rab9 is found in late endosomes, together with mannose 6-phosphate ...
7-174 1.21e-22

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: 91.09  E-value: 1.21e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTV-FENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:cd04116   7 KVILLGDGGVGKSSLMNRYVTNKFDTQLFHTIgVEFLNKDLEVDGHFVTLQIWDTAGQERFRSLRTPFYRGSDCCLLTFS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  86 IDSPDSLENIpEKWTPEVRHFC-----PNVPIILVGNKRDlrsdpqtvrelakMKQEPVKPEQGRAIAEQIGAFAYLECS 160
Cdd:cd04116  87 VDDSQSFQNL-SNWKKEFIYYAdvkepESFPFVILGNKID-------------IPERQVSTEEAQAWCRDNGDYPYFETS 152
                       170
                ....*....|....
gi 17541992 161 AKTKDGIREVFEKA 174
Cdd:cd04116 153 AKDATNVAAAFEEA 166
Rab4 cd04113
Rab GTPase family 4 (Rab4); Rab4 subfamily. Rab4 has been implicated in numerous functions ...
7-176 2.83e-22

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: 89.80  E-value: 2.83e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTV---FENYVadIEVDGKQVELALWDTAGQEdydRLRPLS---YPDTDVI 80
Cdd:cd04113   2 KFLIIGSAGTGKSCLLHQFIENKFKQDSNHTIgveFGSRV--VNVGGKSVKLQIWDTAGQE---RFRSVTrsyYRGAAGA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  81 LMCFSIDSPDSLENIpEKWTPEVRHFC-PNVPIILVGNKRDLRSDPQ-TVRELAKMKQEpvkpeqgraiaeqiGAFAYLE 158
Cdd:cd04113  77 LLVYDITSRESFNAL-TNWLTDARTLAsPDIVIILVGNKKDLEDDREvTFLEASRFAQE--------------NGLLFLE 141
                       170
                ....*....|....*...
gi 17541992 159 CSAKTKDGIREVFEKATQ 176
Cdd:cd04113 142 TSALTGENVEEAFLKCAR 159
Rab23_like cd04106
Rab GTPase family 23 (Rab23)-like; Rab23-like subfamily. Rab23 is a member of the Rab family ...
7-172 3.46e-22

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: 89.81  E-value: 3.46e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVA-DIEVD--GKQVELALWDTAGQEDYDRLRPLSYPDTDVILMC 83
Cdd:cd04106   2 KVIVVGNGNVGKSSMIQRFVKGIFTKDYKKTIGVDFLEkQIFLRqsDEDVRLMLWDTAGQEEFDAITKAYYRGAQACILV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  84 FSIDSPDSLENIpEKWTPEVRHFCPNVPIILVGNKRDLrsdpqtvrelakMKQEPVKPEQGRAIAEQIGAFAYLECsakT 163
Cdd:cd04106  82 FSTTDRESFEAI-ESWKEKVEAECGDIPMVLVQTKIDL------------LDQAVITNEEAEALAKRLQLPLFRTS---V 145
                       170
                ....*....|.
gi 17541992 164 KDGI--REVFE 172
Cdd:cd04106 146 KDDFnvTELFE 156
Rab35 cd04110
Rab GTPase family 35 (Rab35); Rab35 is one of several Rab proteins to be found to participate ...
7-179 5.42e-22

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  Cd Length: 199  Bit Score: 89.91  E-value: 5.42e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENY-VADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:cd04110   8 KLLIIGDSGVGKSSLLLRFADNTFSGSYITTIGVDFkIRTVEINGERVKLQIWDTAGQERFRTITSTYYRGTHGVIVVYD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  86 IDSPDSLENIpEKWTPEVRHFCPNVPIILVGNKRDlrsDPQtvrelakmkQEPVKPEQGRAIAEQIGaFAYLECSAKTKD 165
Cdd:cd04110  88 VTNGESFVNV-KRWLQEIEQNCDDVCKVLVGNKND---DPE---------RKVVETEDAYKFAGQMG-ISLFETSAKENI 153
                       170
                ....*....|....
gi 17541992 166 GIREVFEKATQAAL 179
Cdd:cd04110 154 NVEEMFNCITELVL 167
PLN03108 PLN03108
Rab family protein; Provisional
7-181 1.32e-20

Rab family protein; Provisional


Pssm-ID: 178655  Cd Length: 210  Bit Score: 86.15  E-value: 1.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992    7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVAD-IEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:PLN03108   8 KYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARmITIDNKPIKLQIWDTAGQESFRSITRSYYRGAAGALLVYD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   86 IDSPDSLENIPEkWTPEVR-HFCPNVPIILVGNKRDLrsdpqtvrelakMKQEPVKPEQGRAIAEQIGaFAYLECSAKTK 164
Cdd:PLN03108  88 ITRRETFNHLAS-WLEDARqHANANMTIMLIGNKCDL------------AHRRAVSTEEGEQFAKEHG-LIFMEASAKTA 153
                        170
                 ....*....|....*..
gi 17541992  165 DGIREVFEKATQAALQQ 181
Cdd:PLN03108 154 QNVEEAFIKTAAKIYKK 170
Rab3 cd01865
Rab GTPase family 3 contains Rab3A, Rab3B, Rab3C and Rab3D; The Rab3 subfamily contains Rab3A, ...
7-173 2.90e-20

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: 84.58  E-value: 2.90e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENY-VADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:cd01865   3 KLLIIGNSSVGKTSFLFRYADDSFTSAFVSTVGIDFkVKTVYRNDKRIKLQIWDTAGQERYRTITTAYYRGAMGFILMYD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  86 IDSPDSLeNIPEKWTPEVRHFC-PNVPIILVGNKRDLRSDpqtvrelakmkqEPVKPEQGRAIAEQIGaFAYLECSAKTK 164
Cdd:cd01865  83 ITNEESF-NAVQDWSTQIKTYSwDNAQVILVGNKCDMEDE------------RVVSAERGRQLADQLG-FEFFEASAKEN 148

                ....*....
gi 17541992 165 DGIREVFEK 173
Cdd:cd01865 149 INVKQVFER 157
Rab14 cd04122
Rab GTPase family 14 (Rab14); Rab14 GTPases are localized to biosynthetic compartments, ...
7-171 6.44e-20

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: 83.73  E-value: 6.44e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQF-PDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:cd04122   4 KYIIIGDMGVGKSCLLHQFTEKKFmADCPHTIGVEFGTRIIEVNGQKIKLQIWDTAGQERFRAVTRSYYRGAAGALMVYD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  86 IDSPDSLENIpEKWTPEVRHFC-PNVPIILVGNKRDLRSdpqtvrelakmkQEPVKPEQGRAIAEQIGaFAYLECSAKTK 164
Cdd:cd04122  84 ITRRSTYNHL-SSWLTDARNLTnPNTVIFLIGNKADLEA------------QRDVTYEEAKQFADENG-LLFLECSAKTG 149

                ....*..
gi 17541992 165 DGIREVF 171
Cdd:cd04122 150 ENVEDAF 156
Rab30 cd04114
Rab GTPase family 30 (Rab30); Rab30 subfamily. Rab30 appears to be associated with the Golgi ...
7-173 1.56e-19

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: 82.64  E-value: 1.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENY-VADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:cd04114   9 KIVLIGNAGVGKTCLVRRFTQGLFPPGQGATIGVDFmIKTVEIKGEKIKLQIWDTAGQERFRSITQSYYRSANALILTYD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  86 IDSPDSLENIPEkWTPEVRHFCPN-VPIILVGNKRDLRSDpqtvRELakmkqepvkPEQ-GRAIAEQIGAFaYLECSAKT 163
Cdd:cd04114  89 ITCEESFRCLPE-WLREIEQYANNkVITILVGNKIDLAER----REV---------SQQrAEEFSDAQDMY-YLETSAKE 153
                       170
                ....*....|
gi 17541992 164 KDGIREVFEK 173
Cdd:cd04114 154 SDNVEKLFLD 163
Rab33B_Rab33A cd04115
Rab GTPase family 33 includes Rab33A and Rab33B; Rab33B/Rab33A subfamily. Rab33B is ...
7-134 2.18e-19

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: 82.10  E-value: 2.18e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTV---FENYVadIEVDGKQVELALWDTAGQEDYDR-LRPLSYPDTDVILM 82
Cdd:cd04115   4 KIIVIGDSNVGKTCLTYRFCAGRFPERTEATIgvdFRERT--VEIDGERIKVQLWDTAGQERFRKsMVQHYYRNVHAVVF 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 17541992  83 CFSIDSPDSLENIPEkWTPEVRHFC--PNVPIILVGNKRDLRSDPQTVRELAKM 134
Cdd:cd04115  82 VYDVTNMASFHSLPS-WIEECEQHSlpNEVPRILVGNKCDLREQIQVPTDLAQR 134
PTZ00369 PTZ00369
Ras-like protein; Provisional
1-171 7.15e-19

Ras-like protein; Provisional


Pssm-ID: 240385  Cd Length: 189  Bit Score: 81.06  E-value: 7.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992    1 MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVI 80
Cdd:PTZ00369   1 MASTEYKLVVVGGGGVGKSALTIQFIQNHFIDEYDPTIEDSYRKQCVIDEETCLLDILDTAGQEEYSAMRDQYMRTGQGF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   81 LMCFSIDSPDSLENIPEKWTPEVR-HFCPNVPIILVGNKRDLRSDPQtvrelakmkqepVKPEQGRAIAEQIGAfAYLEC 159
Cdd:PTZ00369  81 LCVYSITSRSSFEEIASFREQILRvKDKDRVPMILVGNKCDLDSERQ------------VSTGEGQELAKSFGI-PFLET 147
                        170
                 ....*....|..
gi 17541992  160 SAKTKDGIREVF 171
Cdd:PTZ00369 148 SAKQRVNVDEAF 159
Rab26 cd04112
Rab GTPase family 26 (Rab26); Rab26 subfamily. First identified in rat pancreatic acinar cells, ...
7-163 9.78e-19

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: 80.68  E-value: 9.78e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQF-PDVYVPTV---FENYVadIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILM 82
Cdd:cd04112   2 KVMLVGDSGVGKTCLLVRFKDGAFlAGSFIATVgiqFTNKV--VTVDGVKVKLQIWDTAGQERFRSVTHAYYRDAHALLL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  83 CFSIDSPDSLENIpEKWTPEVRHFCP-NVPIILVGNKRDLRSDPQtvrelakmkqepVKPEQGRAIAEQIGAfAYLECSA 161
Cdd:cd04112  80 LYDVTNKSSFDNI-RAWLTEILEYAQsDVVIMLLGNKADMSGERV------------VKREDGERLAKEYGV-PFMETSA 145

                ..
gi 17541992 162 KT 163
Cdd:cd04112 146 KT 147
PTZ00132 PTZ00132
GTP-binding nuclear protein Ran; Provisional
7-122 3.12e-18

GTP-binding nuclear protein Ran; Provisional


Pssm-ID: 240284  Cd Length: 215  Bit Score: 79.74  E-value: 3.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992    7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTV-FENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:PTZ00132  11 KLILVGDGGVGKTTFVKRHLTGEFEKKYIPTLgVEVHPLKFYTNCGPICFNVWDTAGQEKFGGLRDGYYIKGQCAIIMFD 90
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 17541992   86 IDSPDSLENIPeKWTPEVRHFCPNVPIILVGNKRDLR 122
Cdd:PTZ00132  91 VTSRITYKNVP-NWHRDIVRVCENIPIVLVGNKVDVK 126
RJL cd04119
Rab GTPase family J-like (RabJ-like); RJLs are found in many protists and as chimeras with ...
7-172 3.65e-18

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: 78.55  E-value: 3.65e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENY-VADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:cd04119   2 KVISMGNSGVGKSCIIKRYCEGRFVSKYLPTIGIDYgVKKVSVRNKEVRVNFFDLSGHPEYLEVRNEFYKDTQGVLLVYD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  86 IDSPDSLENIpEKWTPEVRHFC------PNVPIILVGNKRDLrSDPQTVRElakmkqepvkpEQGRAIAEQIGaFAYLEC 159
Cdd:cd04119  82 VTDRQSFEAL-DSWLKEMKQEGgphgnmENIVVVVCANKIDL-TKHRAVSE-----------DEGRLWAESKG-FKYFET 147
                       170
                ....*....|...
gi 17541992 160 SAKTKDGIREVFE 172
Cdd:cd04119 148 SACTGEGVNEMFQ 160
Rab12 cd04120
Rab GTPase family 12 (Rab12); Rab12 was first identified in canine cells, where it was ...
7-181 5.08e-18

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  Cd Length: 202  Bit Score: 78.90  E-value: 5.08e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENY-VADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:cd04120   2 QVIIIGSRGVGKTSLMERFTDDTFCEACKSTVGVDFkIKTVELRGKKIRLQIWDTAGQERFNSITSAYYRSAKGIILVYD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  86 IDSPDSLENIPeKWTPEV-RHFCPNVPIILVGNKRDLRSDpqtvRELAKmkqepvkpEQGRAIAEQIGAFAYLECSAKTK 164
Cdd:cd04120  82 ITKKETFDDLP-KWMKMIdKYASEDAELLLVGNKLDCETD----REITR--------QQGEKFAQQITGMRFCEASAKDN 148
                       170
                ....*....|....*..
gi 17541992 165 DGIREVFEKATQAALQQ 181
Cdd:cd04120 149 FNVDEIFLKLVDDILKK 165
RabL2 cd04124
Rab GTPase-like family 2 (Rab-like2); RabL2 (Rab-like2) subfamily. RabL2s are novel Rab ...
7-128 6.67e-18

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: 77.98  E-value: 6.67e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPT-VFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:cd04124   2 KIILLGDSAVGKSKLVERFLMDGYEPQQLSTyALTLYKHNAKFEGKTILVDFWDTAGQERFQTMHASYYHKAHACILVFD 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 17541992  86 IDSPDSLENIpEKWTPEVRHFCPNVPIILVGNKRDLrsDPQTV 128
Cdd:cd04124  82 VTRKITYKNL-SKWYEELREYRPEIPCIVVANKIDL--DPSVT 121
PLN03071 PLN03071
GTP-binding nuclear protein Ran; Provisional
7-123 8.23e-18

GTP-binding nuclear protein Ran; Provisional


Pssm-ID: 178620  Cd Length: 219  Bit Score: 78.64  E-value: 8.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992    7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTV-FENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:PLN03071  15 KLVIVGDGGTGKTTFVKRHLTGEFEKKYEPTIgVEVHPLDFFTNCGKIRFYCWDTAGQEKFGGLRDGYYIHGQCAIIMFD 94
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 17541992   86 IDSPDSLENIPeKWTPEVRHFCPNVPIILVGNKRDLRS 123
Cdd:PLN03071  95 VTARLTYKNVP-TWHRDLCRVCENIPIVLCGNKVDVKN 131
Rit_Rin_Ric cd04141
Ras-like protein in all tissues (Rit), Ras-like protein in neurons (Rin) and Ras-related ...
7-171 9.21e-18

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: 77.59  E-value: 9.21e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSI 86
Cdd:cd04141   4 KIVMLGAGGVGKSAVTMQFISHSFPDYHDPTIEDAYKTQARIDNEPALLDILDTAGQAEFTAMRDQYMRCGEGFIICYSV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  87 DSPDSLENIPE--KWTPEVRHfCPNVPIILVGNKRDLRSdpqtvrelakmkQEPVKPEQGRAIAEQIGAfAYLECSAKTK 164
Cdd:cd04141  84 TDRHSFQEASEfkELITRVRL-TEDIPLVLVGNKVDLEQ------------QRQVTTEEGRNLAREFNC-PFFETSAALR 149

                ....*..
gi 17541992 165 DGIREVF 171
Cdd:cd04141 150 FYIDDAF 156
RERG_RasL11_like cd04146
Ras-related and Estrogen-Regulated Growth inhibitor (RERG) and Ras-like 11 (RasL11)-like ...
7-180 2.00e-17

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: 76.55  E-value: 2.00e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYD----RLRPLSYPDTDVILm 82
Cdd:cd04146   1 KIAVLGASGVGKSALTVRFLTKRFIGEYEPNLESLYSRQVTIDGEQVSLEIQDTPGQQQNEdpesLERSLRWADGFVLV- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  83 cFSIDSPDSLENI-PEKWT-PEVRHFCPNVPIILVGNKRDLrsdpQTVRElakmkqepVKPEQGRAIAEQIGAfAYLECS 160
Cdd:cd04146  80 -YSITDRSSFDVVsQLLQLiREIKKRDGEIPVILVGNKADL----LHSRQ--------VSTEEGQKLALELGC-LFFEVS 145
                       170       180
                ....*....|....*....|.
gi 17541992 161 A-KTKDGIREVFEKATQAALQ 180
Cdd:cd04146 146 AaENYLEVQNVFHELCREVRR 166
Rab36_Rab34 cd04108
Rab GTPase families 34 (Rab34) and 36 (Rab36); Rab34/Rab36 subfamily. Rab34, found primarily ...
7-171 3.81e-17

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: 76.07  E-value: 3.81e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTV---FEnyVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMC 83
Cdd:cd04108   2 KVIVVGDLSVGKTCLINRFCKDVFDKNYKATIgvdFE--MERFEVLGVPFSLQLWDTAGQERFKCIASTYYRGAQAIIIV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  84 FSIDSPDSLENIPEKWTPEVRHFCP-NVPIILVGNKRDLRSDPQtvreLAKMKQEPVKpeqgraIAEQIGAfAYLECSAK 162
Cdd:cd04108  80 FDLTDVASLEHTRQWLEDALKENDPsSVLLFLVGTKKDLSSPAQ----YALMEQDAIK------LAREMKA-EYWAVSAL 148

                ....*....
gi 17541992 163 TKDGIREVF 171
Cdd:cd04108 149 TGENVRDFF 157
PLN03110 PLN03110
Rab GTPase; Provisional
7-179 4.02e-17

Rab GTPase; Provisional


Pssm-ID: 178657  Cd Length: 216  Bit Score: 76.51  E-value: 4.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992    7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTV-FENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:PLN03110  14 KIVLIGDSGVGKSNILSRFTRNEFCLESKSTIgVEFATRTLQVEGKTVKAQIWDTAGQERYRAITSAYYRGAVGALLVYD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   86 IDSPDSLENIpEKWTPEVR-HFCPNVPIILVGNKRDLRSdpqtVRELAKmkqepvkpEQGRAIAEQIGaFAYLECSAKTK 164
Cdd:PLN03110  94 ITKRQTFDNV-QRWLRELRdHADSNIVIMMAGNKSDLNH----LRSVAE--------EDGQALAEKEG-LSFLETSALEA 159
                        170
                 ....*....|....*
gi 17541992  165 DGIrevfEKATQAAL 179
Cdd:PLN03110 160 TNV----EKAFQTIL 170
Ran cd00877
Ras-related nuclear proteins (Ran)/TC4 family of small GTPases; Ran GTPase is involved in ...
7-174 7.27e-17

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: 75.03  E-value: 7.27e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTV-FENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:cd00877   2 KLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLgVEVHPLDFHTNRGKIRFNVWDTAGQEKFGGLRDGYYIQGQCAIIMFD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  86 IDSPDSLENIPeKWTPEVRHFCPNVPIILVGNKRDLrsdpqtvrelakmKQEPVKPEQGRAIAEQIgaFAYLECSAKTKD 165
Cdd:cd00877  82 VTSRVTYKNVP-NWHRDLVRVCENIPIVLCGNKVDI-------------KDRKVKPKQITFHRKKN--LQYYEISAKSNY 145

                ....*....
gi 17541992 166 GirevFEKA 174
Cdd:cd00877 146 N----FEKP 150
Ras_dva cd04147
Ras - dorsal-ventral anterior localization (Ras-dva) family; Ras-dva subfamily. Ras-dva (Ras - ...
7-178 1.36e-16

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  Cd Length: 197  Bit Score: 74.87  E-value: 1.36e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSI 86
Cdd:cd04147   1 RLVFMGAAGVGKTALIQRFLYDTFEPKHRRTVEELHSKEYEVAGVKVTIDILDTSGSYSFPAMRKLSIQNGDAFALVYSV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  87 DSPDSLENIpEKWTPEVRHFCPN--VPIILVGNKRDLRSDPQTVRELAKmkqepvkpeqgrAIAEQIGAFAYLECSAKTK 164
Cdd:cd04147  81 DDPESFEEV-KRLREEILEVKEDkfVPIVVVGNKIDSLAERQVEAADAL------------STVELDWNNGFVEASAKDN 147
                       170
                ....*....|....
gi 17541992 165 DGIREVFEKATQAA 178
Cdd:cd04147 148 ENVTEVFKELLQQA 161
Rab27A cd04127
Rab GTPase family 27a (Rab27a); The Rab27a subfamily consists of Rab27a and its highly ...
7-172 3.46e-16

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: 73.30  E-value: 3.46e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTV----------FENYVADIEVDGKQ-VELALWDTAGQEDYDRLRPLSYP 75
Cdd:cd04127   6 KLLALGDSGVGKTTFLYRYTDNKFNPKFITTVgidfrekrvvYNSQGPDGTSGKAFrVHLQLWDTAGQERFRSLTTAFFR 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  76 DTDVILMCFSIDSPDSLENIPEkWTPEVRH--FCPNVPIILVGNKRDLrsdpqtvrelakMKQEPVKPEQGRAIAEQIGa 153
Cdd:cd04127  86 DAMGFLLMFDLTSEQSFLNVRN-WMSQLQAhaYCENPDIVLIGNKADL------------PDQREVSERQARELADKYG- 151
                       170
                ....*....|....*....
gi 17541992 154 FAYLECSAKTKDGIREVFE 172
Cdd:cd04127 152 IPYFETSAATGQNVEKAVE 170
Rab32_Rab38 cd04107
Rab GTPase families 18 (Rab18) and 32 (Rab32); Rab38/Rab32 subfamily. Rab32 and Rab38 are ...
7-173 6.48e-16

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  Cd Length: 201  Bit Score: 72.73  E-value: 6.48e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTV---FENYVadIEVD-GKQVELALWDTAGQEDYDRLRPLSYPDTDVILM 82
Cdd:cd04107   2 KVLVIGDLGVGKTSIIKRYVHGVFSQHYKATIgvdFALKV--IEWDpNTVVRLQLWDIAGQERFGGMTRVYYKGAVGAII 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  83 CFSIDSPDSLENIpEKWTPEV--RHFCPN---VPIILVGNKRDLRSDPqtvrelakmkqEPVKPEQGRAIAEQIGAFAYL 157
Cdd:cd04107  80 VFDVTRPSTFEAV-LKWKADLdsKVTLPNgepIPALLLANKCDLKKER-----------LAKDPEQMDQFCKENGFIGWF 147
                       170
                ....*....|....*.
gi 17541992 158 ECSAKTKDGIREVFEK 173
Cdd:cd04107 148 ETSAKENINIEEAMRF 163
Rhes_like cd04143
Ras homolog enriched in striatum (Rhes) and activator of G-protein signaling 1 (Dexras1/AGS1); ...
7-172 7.95e-16

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  Cd Length: 247  Bit Score: 72.86  E-value: 7.95e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTV--FENYVADIEvdGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCF 84
Cdd:cd04143   2 RMVVLGASKVGKTAIVSRFLGGRFEEQYTPTIedFHRKLYSIR--GEVYQLDILDTSGNHPFPAMRRLSILTGDVFILVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  85 SIDSPDSLENIPE--------KW-----TPEVrhfcPNVPIILVGNKRDlRSDPQTVRelakmkqepvKPEQGRAIAEQI 151
Cdd:cd04143  80 SLDNRESFEEVCRlreqiletKSclknkTKEN----VKIPMVICGNKAD-RDFPREVQ----------RDEVEQLVGGDE 144
                       170       180
                ....*....|....*....|.
gi 17541992 152 GAfAYLECSAKTKDGIREVFE 172
Cdd:cd04143 145 NC-AYFEVSAKKNSNLDEMFR 164
RocCOR cd09914
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ...
5-169 2.46e-15

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: 70.44  E-value: 2.46e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   5 RKKLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENyVADIEV---DGKQVELALWDTAGQEDYDRLRPLSYPDTDVIL 81
Cdd:cd09914   1 EAKLMLVGQGGVGKTSLCKQLIGEKFDGDESSTHGIN-VQDWKIpapERKKIRLNVWDFGGQEIYHATHQFFLTSRSLYL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  82 MCFSIDSPDSLENIPeKWTPEVRHFCPNVPIILVGNKRDLRSDPQTVRELAKMKQEPvkpeqgrAIAeqigafAYLECSA 161
Cdd:cd09914  80 LVFDLRTGDEVSRVP-YWLRQIKAFGGVSPVILVGTHIDESCDEDILKKALNKKFPA-------IIN------DIHFVSC 145

                ....*...
gi 17541992 162 KTKDGIRE 169
Cdd:cd09914 146 KNGKGIAE 153
RAN smart00176
Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases; Ran is involved in the ...
11-122 4.24e-15

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  Cd Length: 200  Bit Score: 70.43  E-value: 4.24e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992     11 VGDGACGKTCLLIVFSKDQFPDVYVPTV-FENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSP 89
Cdd:smart00176   1 VGDGGTGKTTFVKRHLTGEFEKKYVATLgVEVHPLVFHTNRGPIRFNVWDTAGQEKFGGLRDGYYIQGQCAIIMFDVTAR 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 17541992     90 DSLENIPeKWTPEVRHFCPNVPIILVGNKRDLR 122
Cdd:smart00176  81 VTYKNVP-NWHRDLVRVCENIPIVLCGNKVDVK 112
ARHI_like cd04140
A Ras homolog member I (ARHI); ARHI (A Ras homolog member I) is a member of the Ras family ...
7-172 5.10e-15

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: 69.86  E-value: 5.10e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSI 86
Cdd:cd04140   3 RVVVFGAGGVGKSSLVLRFVKGTFRESYIPTIEDTYRQVISCSKSICTLQITDTTGSHQFPAMQRLSISKGHAFILVYSI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  87 DSPDSLENIPEKWTpEVRHF----CPNVPIILVGNKrdlrSDPQTVRElakmkqepVKPEQGRAIAEQIGAfAYLECSAK 162
Cdd:cd04140  83 TSKQSLEELKPIYE-LICEIkgnnLEKIPIMLVGNK----CDESPSRE--------VSSSEGAALARTWNC-AFMETSAK 148
                       170
                ....*....|
gi 17541992 163 TKDGIREVFE 172
Cdd:cd04140 149 TNHNVQELFQ 158
Rab24 cd04118
Rab GTPase family 24 (Rab24); Rab24 is distinct from other Rabs in several ways. It exists ...
7-173 5.11e-15

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: 70.28  E-value: 5.11e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPD-VYVPTVFENYVAD-IEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCF 84
Cdd:cd04118   2 KVVMLGKESVGKTSLVERYVHHRFLVgPYQNTIGAAFVAKrMVVGERVVTLGIWDTAGSERYEAMSRIYYRGAKAAIVCY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  85 SIDSPDSLENIpEKWTPEVRHFCPNVPIILVGNKRDLRSDPQTVRElakmkqepVKPEQGRAIAEQIGAFAYlECSAKTK 164
Cdd:cd04118  82 DLTDSSSFERA-KFWVKELQNLEEHCKIYLCGTKSDLIEQDRSLRQ--------VDFHDVQDFADEIKAQHF-ETSSKTG 151

                ....*....
gi 17541992 165 DGIREVFEK 173
Cdd:cd04118 152 QNVDELFQK 160
RabL4 cd04101
Rab GTPase-like family 4 (Rab-like4); RabL4 (Rab-like4) subfamily. RabL4s are novel proteins ...
7-172 5.30e-15

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: 69.86  E-value: 5.30e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKD--QFPDVYVPTVFENYVAD---IEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVIL 81
Cdd:cd04101   2 QCAVVGDPAVGKSALVQMFHSDgaTFQKNYTMTTGCDLVVKtvpVPDTSDSVELFIFDSAGQELFSDMVENVWEQPAVVC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  82 MCFSIDSPDSLENIpEKWTPEVRHFCPNV--PIILVGNKRDLRSdpqtvrelakmKQEpVKPEQGRAIAeQIGAFAYLEC 159
Cdd:cd04101  82 VVYDVTNEVSFNNC-SRWINRVRTHSHGLhtPGVLVGNKCDLTD-----------RRE-VDAAQAQALA-QANTLKFYET 147
                       170
                ....*....|...
gi 17541992 160 SAKTKDGIREVFE 172
Cdd:cd04101 148 SAKEGVGYEAPFL 160
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
7-173 7.91e-14

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  Cd Length: 158  Bit Score: 66.06  E-value: 7.91e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVG-DGAcGKTCLLIVFSKDQFPDVyVPTV-FenyvaDIE-VDGKQVELALWDTAGQedyDRLRPL---SYPDTDVI 80
Cdd:cd00878   1 RILMLGlDGA-GKTTILYKLKLGEVVTT-IPTIgF-----NVEtVEYKNVKFTVWDVGGQ---DKIRPLwkhYYENTDGL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  81 LmcFSIDSPDSlENIPEKWT--------PEVRhfcpNVPIILVGNKRDLRsDPQTVRELAK-MKQEPVKPEQGRAIaeqi 151
Cdd:cd00878  71 I--FVVDSSDR-ERIEEAKNelhkllneEELK----GAPLLILANKQDLP-GALTESELIElLGLESIKGRRWHIQ---- 138
                       170       180
                ....*....|....*....|..
gi 17541992 152 gafaylECSAKTKDGIREVFEK 173
Cdd:cd00878 139 ------PCSAVTGDGLDEGLDW 154
Rab28 cd04109
Rab GTPase family 28 (Rab28); Rab28 subfamily. First identified in maize, Rab28 has been shown ...
7-174 2.99e-13

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  Cd Length: 213  Bit Score: 65.20  E-value: 2.99e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTV-FENYVADIEVDGK-QVELALWDTAGQEDYDRLRPLSYPDTDVILMCF 84
Cdd:cd04109   2 KIVVLGDGASGKTSLIRRFAQEGFGKSYKQTIgLDFFSRRITLPGSlNVTLQVWDIGGQQIGGKMLDKYIYGAQAVCLVY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  85 SIDSPDSLENIpEKWTPEVRHFCPN----VPIILVGNKRDLRsdpqtvrelaKMKQepVKPEQGRAIAEQIGAFAYLeCS 160
Cdd:cd04109  82 DITNSQSFENL-EDWLSVVKKVNEEsetkPKMVLVGNKTDLE----------HNRQ--VTAEKHARFAQENDMESIF-VS 147
                       170
                ....*....|....
gi 17541992 161 AKTKDGIREVFEKA 174
Cdd:cd04109 148 AKTGDRVFLCFQRI 161
Spg1 cd04128
Septum-promoting GTPase (Spg1); Spg1p. Spg1p (septum-promoting GTPase) was first identified in ...
7-171 3.59e-12

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: 61.64  E-value: 3.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENYV-ADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:cd04128   2 KIGLLGDAQIGKTSLMVKYVEGEFDEEYIQTLGVNFMeKTISIRGTEITFSIWDLGGQREFINMLPLVCKDAVAILFMFD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  86 IDSPDSLENIPEkWTPEVRHFCPNVPIILVGNKRDLrsdpqtVRELAKMKQEPVKpEQGRAIAEQIGAFAYLeCSAKTKD 165
Cdd:cd04128  82 LTRKSTLNSIKE-WYRQARGFNKTAIPILVGTKYDL------FADLPPEEQEEIT-KQARKYAKAMKAPLIF-CSTSHSI 152

                ....*.
gi 17541992 166 GIREVF 171
Cdd:cd04128 153 NVQKIF 158
RGK cd04148
Rem, Rem2, Rad, Gem/Kir (RGK) subfamily of Ras GTPases; RGK subfamily. The RGK (Rem, Rem2, Rad, ...
7-172 5.43e-12

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  Cd Length: 219  Bit Score: 61.65  E-value: 5.43e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFS-KDQFPDVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFS 85
Cdd:cd04148   2 RVVLLGDSGVGKSSLANIFTaGVYEDSAYEASGDDTYERTVSVDGEEATLVVYDHWEQEDGMWLEDSCMQVGDAYVIVYS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  86 IDSPDSLENipekwTPEVR------HFCPNVPIILVGNKRDL-RSdpqtvRElakmkqepVKPEQGRAIAEQIGAfAYLE 158
Cdd:cd04148  82 VTDRSSFEK-----ASELRiqlrraRQAEDIPIILVGNKSDLvRS-----RE--------VSVQEGRACAVVFDC-KFIE 142
                       170
                ....*....|....
gi 17541992 159 CSAKTKDGIREVFE 172
Cdd:cd04148 143 TSAALQHNVDELFE 156
Rab40 cd04121
Rab GTPase family 40 (Rab40) contains Rab40a, Rab40b and Rab40c; The Rab40 subfamily contains ...
7-181 1.94e-11

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  Cd Length: 189  Bit Score: 59.56  E-value: 1.94e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLivfSKDQFPDVYVPTVFENYVA----DIEVDGKQVELALWDTAGQEDYDRL-RPLSYPDTDVIL 81
Cdd:cd04121   8 KFLLVGDSDVGKGEIL---ASLQDGSTESPYGYNMGIDykttTILLDGRRVKLQLWDTSGQGRFCTIfRSYSRGAQGIIL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  82 McFSIDSPDSLENIpEKWTPEVRHFCPNVPIILVGNKrdlrsdpqtvRELAKMKQepVKPEQGRAIAEQIGaFAYLECSA 161
Cdd:cd04121  85 V-YDITNRWSFDGI-DRWIKEIDEHAPGVPKILVGNR----------LHLAFKRQ--VATEQAQAYAERNG-MTFFEVSP 149
                       170       180
                ....*....|....*....|
gi 17541992 162 KTKDGIREVFEKATQAALQQ 181
Cdd:cd04121 150 LCNFNITESFTELARIVLMR 169
RRP22 cd04142
Ras-related protein on chromosome 22 (RRP22) family; RRP22 (Ras-related protein on chromosome ...
7-179 3.00e-09

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: 53.72  E-value: 3.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYVPTVF-ENYVADIEVDGKQVELALWD---------TAGQEDYD-RLRPLSyp 75
Cdd:cd04142   2 RVAVLGAPGVGKTAIVRQFLAQEFPEEYIPTEHrRLYRPAVVLSGRVYDLHILDvpnmqrypgTAGQEWMDpRFRGLR-- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  76 DTDVILMCFSIDSPDSLENIP--EKWTPEVRHF-CPNVPIILVGNKRDL---RSDPQtvRELAKMKQEPVKpeqgraiae 149
Cdd:cd04142  80 NSRAFILVYDICSPDSFHYVKllRQQILETRPAgNKEPPIVVVGNKRDQqrhRFAPR--HVLSVLVRKSWK--------- 148
                       170       180       190
                ....*....|....*....|....*....|
gi 17541992 150 qigaFAYLECSAKTKDGIREVFEKATQAAL 179
Cdd:cd04142 149 ----CGYLECSAKYNWHILLLFKELLISAT 174
Rab20 cd04126
Rab GTPase family 20 (Rab20); Rab20 is one of several Rab proteins that appear to be ...
7-172 4.99e-09

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  Cd Length: 220  Bit Score: 53.76  E-value: 4.99e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDvYVPTVFENYVAdievdgKQ---VELALWDTAGQEDYDRLRPLSYPDTDVILMC 83
Cdd:cd04126   2 KVVLLGDMNVGKTSLLHRYMERRFKD-TVSTVGGAFYL------KQwgpYNISIWDTAGREQFHGLGSMYCRGAAAVILT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  84 FSIDSPDSLENIPEKWTPEVRHFCPNVPIILVGNKRDL-------RSDPQTVRELAKMKQEPVKPEQGRAIAEQIGAF-- 154
Cdd:cd04126  75 YDVSNVQSLEELEDRFLGLTDTANEDCLFAVVGNKLDLteegalaGQEKDAGDRVSPEDQRQVTLEDAKAFYKRINKYkm 154
                       170       180
                ....*....|....*....|....*....
gi 17541992 155 -----------AYLECSAKTKDGIREVFE 172
Cdd:cd04126 155 ldedlspaaekMCFETSAKTGYNVDELFE 183
PTZ00099 PTZ00099
rab6; Provisional
28-173 1.00e-08

rab6; Provisional


Pssm-ID: 185444  Cd Length: 176  Bit Score: 52.05  E-value: 1.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   28 DQFPDVYVPTVFENYVAD-IEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIpEKWTPEV-RH 105
Cdd:PTZ00099   3 DTFDNNYQSTIGIDFLSKtLYLDEGPVRLQLWDTAGQERFRSLIPSYIRDSAAAIVVYDITNRQSFENT-TKWIQDIlNE 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17541992  106 FCPNVPIILVGNKRDLrsdpqtvRELAKmkqepVKPEQGRAIAEQIGAFaYLECSAKTKDGIREVFEK 173
Cdd:PTZ00099  82 RGKDVIIALVGNKTDL-------GDLRK-----VTYEEGMQKAQEYNTM-FHETSAKAGHNIKVLFKK 136
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
7-176 1.54e-08

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


Pssm-ID: 306524  Cd Length: 174  Bit Score: 51.46  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992     7 KLVIVG-DGAcGKTCLLIVFSKDQFpDVYVPTVFENyvadIE-VDGKQVELALWDTAGQEdydRLRPL---SYPDTDVIL 81
Cdd:pfam00025  16 RILILGlDNA-GKTTILYKLKLGEI-VTTIPTIGFN----VEtVTYKNVKFTVWDVGGQE---SLRPLwrnYFPNTDGVI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992    82 mcFSIDSPDSlENIPEKWTP--------EVRhfcpNVPIILVGNKRDLRSD--PQTVRE---LAKMKQEPVkpeqgraia 148
Cdd:pfam00025  87 --FVVDSADR-DRIEEAKEElhallneeELA----DAPLLILANKQDLPGAmsEAEIREllgLHELKDRPW--------- 150
                         170       180
                  ....*....|....*....|....*...
gi 17541992   149 eQIGAfayleCSAKTKDGIREVFEKATQ 176
Cdd:pfam00025 151 -EIQG-----CSAVTGEGLDEGLDWLSN 172
Arl4_Arl7 cd04152
Arf-like 4 (Arl4) and 7 (Arl7) GTPases; Arl4 (Arf-like 4) is highly expressed in testicular ...
8-173 4.84e-08

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: 50.18  E-value: 4.84e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   8 LVIVGDGACGKTCLLIVFSKDQFPDVyVPTVFENyVADIEV---DGKQVELALWDTAGQEdydRLRPL--SYPD-TDVIL 81
Cdd:cd04152   6 IVMLGLDSAGKTTVLYRLKFNEFVNT-VPTKGFN-TEKIKVslgNAKGVTFHFWDVGGQE---KLRPLwkSYTRcTDGIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  82 mcFSIDSPDSlENIPEKWTP--EVRHFCPN--VPIILVGNKRDLRSdPQTVRELAKMkqepvkpeqgRAIAEqIGAFA-- 155
Cdd:cd04152  81 --FVVDSVDV-ERMEEAKTElhKITKFSENqgVPVLVLANKQDLPN-ALPVSEVEKL----------LALHE-LSSSTpw 145
                       170
                ....*....|....*....
gi 17541992 156 YLE-CSAKTKDGIREVFEK 173
Cdd:cd04152 146 HVQpACAIIGEGLQEGLEK 164
Arfrp1 cd04160
Arf-related protein 1 (Arfrp1); Arfrp1 (Arf-related protein 1), formerly known as ARP, is a ...
9-169 5.23e-08

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: 50.03  E-value: 5.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   9 VIVG-DGAcGKTCLL----IVFSKDQ---FPDVYVPTVFENyVADIEVDGkqVELALWDTAGQEDYDRLRPLSYPDTDVI 80
Cdd:cd04160   3 LILGlDNA-GKTTFLeqtkTKFSKNYkglNPSKITPTVGLN-IGTIEVGK--ARLMFWDLGGQEELRSLWDKYYAESHGV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  81 LmcFSIDSPDSlENIPEKWT--------PEVRhfcpNVPIILVGNKRDLrSDPQTVRELaKMKQEPVKPEQGRAiaeqig 152
Cdd:cd04160  79 I--YVIDSTDR-ERFNESKSafekvinnEALE----GVPLLVLANKQDL-PDALSVAEI-KEVFDDCIALIGRR------ 143
                       170
                ....*....|....*..
gi 17541992 153 AFAYLECSAKTKDGIRE 169
Cdd:cd04160 144 DCLVQPVSALEGEGVEE 160
Miro2 cd01892
Mitochondrial Rho family 2 (Miro2), C-terminal; Miro2 subfamily. Miro (mitochondrial Rho) ...
10-180 2.10e-07

Mitochondrial Rho family 2 (Miro2), C-terminal; Miro2 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 putative GTPase domain in the C terminus 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: 206679  Cd Length: 180  Bit Score: 48.39  E-value: 2.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  10 IVGDGACGKTCLLIVFSKDQF-PDVYVPTVFENYVAD-IEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVIlmCFSID 87
Cdd:cd01892   9 VLGAKGSGKSALLQAFLGRSFsQNAYSPTIKPRYAVNtVEVPGQEKYLILREVGEDEEAILLNDAELAACDVA--CLVYD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  88 S--PDSLENIPEKWTpevRHFC-PNVPIILVGNKRDLrsDPQTVRELakmkqepVKPEQgraIAEQIGAFAYLECSAKTK 164
Cdd:cd01892  87 SsdPNSFSYCAEVYK---KYFMlGEIPCLFVAAKADL--DEQQQRAE-------VQPDE---FCRKLGLPPPLHFSSRLG 151
                       170
                ....*....|....*.
gi 17541992 165 DGIREVFEKATQAALQ 180
Cdd:cd01892 152 DSSNELFTKLATAAQY 167
ARLTS1 cd04156
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ...
7-176 9.38e-06

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: 43.56  E-value: 9.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVyVPTVFENyVADIEVDGKqVELALWDTAGQEdydRLRPL--SY-PDTDVILmc 83
Cdd:cd04156   1 QVLLLGLDSAGKSTLLYKLKHAELVTT-IPTVGFN-VEMLQLEKH-LSLTVWDVGGQE---KMRTVwkCYlENTDGLV-- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  84 FSIDSPDSlENIPEKwTPEVRHFCPN-----VPIILVGNKRDLrSDPQTVRELAKM---------KQEPVKPeqgraiae 149
Cdd:cd04156  73 YVVDSSDE-ARLDES-QKELKHILKNehikgVPVVLLANKQDL-PGALTAEEITRRfklkkycsdRDWYVQP-------- 141
                       170       180
                ....*....|....*....|....*..
gi 17541992 150 qigafayleCSAKTKDGIREVFEKATQ 176
Cdd:cd04156 142 ---------CSAVTGEGLAEAFRKLAS 159
Arl3 cd04155
Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most ...
7-169 1.21e-04

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: 40.84  E-value: 1.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYvPTVFENyVADIEVDGKQveLALWDTAGQEdydRLRPL---SYPDTDVILmc 83
Cdd:cd04155  17 RILLLGLDNAGKTTILKQLASEDISHIT-PTQGFN-IKNVQADGFK--LNVWDIGGQR---KIRPYwrnYFENTDVLI-- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  84 FSIDSPDSlENIPEKWTpEVRHFC-----PNVPIILVGNKRDLrSDPQTVRELAkmkqEPVKPEQGRAIAEQIGAfayle 158
Cdd:cd04155  88 YVIDSADR-KRFEEAGQ-ELVELLeeeklAGVPVLVFANKQDL-LTAAPAEEVA----EALNLHDIRDRSWHIQA----- 155
                       170
                ....*....|.
gi 17541992 159 CSAKTKDGIRE 169
Cdd:cd04155 156 CSAKTGEGLQE 166
Arl10_like cd04159
Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from ...
8-121 1.31e-04

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: 40.38  E-value: 1.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   8 LVIVGDGACGKTCLLIVFSKDQFPDVYVPTVFENyVADIEVDGkqVELALWDTAGQEdydRLRPL--SY-PDTDVILmcF 84
Cdd:cd04159   2 ITLVGLQNSGKTTLVNVIASGQFSEDTIPTVGFN-MRKVTKGN--VTIKVWDLGGQP---RFRSMweRYcRGVNAIV--Y 73
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 17541992  85 SIDSPD---------SLENIPEKwtPEVRHfcpnVPIILVGNKRDL 121
Cdd:cd04159  74 VVDAADreklevaknELHDLLEK--PSLEG----IPLLVLGNKNDL 113
era PRK00089
GTPase Era; Reviewed
76-172 3.02e-04

GTPase Era; Reviewed


Pssm-ID: 234624  Cd Length: 292  Bit Score: 40.42  E-value: 3.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   76 DTDVILMCFSIDspdslenipEKWTPEVRHFC-----PNVPIILVGNKRDLRSDPQTVRELAKmkqepvkpeqgrAIAEQ 150
Cdd:PRK00089  84 DVDLVLFVVDAD---------EKIGPGDEFILeklkkVKTPVILVLNKIDLVKDKEELLPLLE------------ELSEL 142
                         90       100
                 ....*....|....*....|..
gi 17541992  151 IGAFAYLECSAKTKDGIREVFE 172
Cdd:PRK00089 143 MDFAEIVPISALKGDNVDELLD 164
Arf6 cd04149
ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins ...
7-141 1.67e-03

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: 37.45  E-value: 1.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQfPDVYVPTVFENyvadIE-VDGKQVELALWDTAGQedyDRLRPL---SYPDTDVILm 82
Cdd:cd04149  11 RILMLGLDAAGKTTILYKLKLGQ-SVTTIPTVGFN----VEtVTYKNVKFNVWDVGGQ---DKIRPLwrhYYTGTQGLI- 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17541992  83 cFSIDSPDSlENIPEKWTP--------EVRhfcpNVPIILVGNKRDLRS--DPQTVRE---LAKMKQEP--VKP 141
Cdd:cd04149  82 -FVVDSADR-DRIDEARQElhriindrEMR----DALLLVFANKQDLPDamKPHEIQEklgLTRIRDRNwyVQP 149
Arl5_Arl8 cd04153
Arf-like 5 (Arl5) and 8 (Arl8) GTPases; Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like ...
7-169 2.59e-03

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


Pssm-ID: 133353  Cd Length: 174  Bit Score: 36.94  E-value: 2.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVGDGACGKTCLLIVFSKDQFPDVYvPTVFENYVadiEVDGKQVELALWDTAGQEdydRLRP---LSYPDTDVILmc 83
Cdd:cd04153  17 KVIIVGLDNAGKTTILYQFLLGEVVHTS-PTIGSNVE---EIVYKNIRFLMWDIGGQE---SLRSswnTYYTNTDAVI-- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  84 FSIDSPDSlENIPEkwTPEVRHF------CPNVPIILVGNKRDLRsDPQTVRELAkmkqEPVKPEQGRAIAEQIGAfayl 157
Cdd:cd04153  88 LVIDSTDR-ERLPL--TKEELYKmlahedLRKAVLLVLANKQDLK-GAMTPAEIS----ESLGLTSIRDHTWHIQG---- 155
                       170
                ....*....|..
gi 17541992 158 eCSAKTKDGIRE 169
Cdd:cd04153 156 -CCALTGEGLPE 166
PTZ00133 PTZ00133
ADP-ribosylation factor; Provisional
7-90 5.86e-03

ADP-ribosylation factor; Provisional


Pssm-ID: 173423  Cd Length: 182  Bit Score: 35.98  E-value: 5.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992    7 KLVIVGDGACGKTCLLIvfsKDQFPDVY--VPTVFENyvadIE-VDGKQVELALWDTAGQedyDRLRPL---SYPDTDVI 80
Cdd:PTZ00133  19 RILMVGLDAAGKTTILY---KLKLGEVVttIPTIGFN----VEtVEYKNLKFTMWDVGGQ---DKLRPLwrhYYQNTNGL 88
                         90
                 ....*....|
gi 17541992   81 LmcFSIDSPD 90
Cdd:PTZ00133  89 I--FVVDSND 96
PRK09602 PRK09602
translation-associated GTPase; Reviewed
91-173 6.31e-03

translation-associated GTPase; Reviewed


Pssm-ID: 236584  Cd Length: 396  Bit Score: 36.32  E-value: 6.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   91 SLENIPEKWTPE-VRHFCPNV-----PIILVGNKRDLRSDPQTVRELAKMKQEPVKP-----EQGRAIAEQIGAFAYL-- 157
Cdd:PRK09602 193 GLPEDPSKWTDEdLLELARELrkiskPMVIAANKADLPPAEENIERLKEEKYYIVVPtsaeaELALRRAAKAGLIDYIpg 272
                         90       100
                 ....*....|....*....|....*..
gi 17541992  158 --------ECSAKTKDG---IREVFEK 173
Cdd:PRK09602 273 dsdfeilgELSEKQKKAleyIREVLKK 299
Sar1 cd00879
Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII ...
7-172 6.76e-03

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: 36.10  E-value: 6.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992   7 KLVIVG-DGAcGKTCLLIVFsKDQFPDVYVPTVFENyVADIEVDGkqVELALWDTAGQEDYDRLRPLSYPDTDVILmcFS 85
Cdd:cd00879  21 KIVFLGlDNA-GKTTLLHML-KDDRLAQHVPTLHPT-SEELTIGN--VKFTTFDLGGHEQARRVWKDYFPEVDGIV--FL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  86 IDSPDsleniPEKWtPEVR---------HFCPNVPIILVGNKRDLrsdPQTVRElAKMKQE---PVKPEQGRAIAEQIGA 153
Cdd:cd00879  94 VDAAD-----PERF-QESKeeldsllndEELANVPILILGNKIDK---PGAVSE-EELREAlglYGTTTGKGGVSLKVSN 163
                       170       180
                ....*....|....*....|..
gi 17541992 154 FAYLE---CSAKTKDGIREVFE 172
Cdd:cd00879 164 IRPVEvfmCSVVKRQGYGEGFR 185
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
78-167 6.93e-03

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  Cd Length: 159  Bit Score: 35.55  E-value: 6.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992  78 DVILMCFSIDSPDSLENIpekwtpEVRHFCPNVPIILVGNKRDLRSDPQTVRELAKMKQEPVkpeqgraiaeqigafayl 157
Cdd:cd04164  84 DLVLLVVDASEGLDEEDL------EILELPAKKPVIVVLNKSDLLSDAEGISELNGKPIIAI------------------ 139
                        90
                ....*....|
gi 17541992 158 ecSAKTKDGI 167
Cdd:cd04164 140 --SAKTGEGI 147
GTP_HydF TIGR03918
[FeFe] hydrogenase H-cluster maturation GTPase HydF; This model describes the family of the ...
77-173 8.43e-03

[FeFe] hydrogenase H-cluster maturation GTPase HydF; This model describes the family of the [Fe] hydrogenase maturation protein HypF as characterized in Chlamydomonas reinhardtii and found, in an operon with radical SAM proteins HydE and HydG, in numerous bacteria. It has GTPase activity, can bind an 4Fe-4S cluster, and is essential for hydrogenase activity. [Protein fate, Protein modification and repair]


Pssm-ID: 274853  Cd Length: 391  Bit Score: 35.95  E-value: 8.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992    77 TDVILMCfsIDSPDSLENIPEKWTPEVRHfcPNVPIILVGNKRDLRSDPQTVRELAKMKQEPVkpeqgraiaeqigafay 156
Cdd:TIGR03918  86 TDLALLV--VDAEQGPGEYELELIEELKE--RKIPYIVVINKIDLGEESAEKEKLEKKFGLPP----------------- 144
                          90
                  ....*....|....*..
gi 17541992   157 LECSAKTKDGIREVFEK 173
Cdd:TIGR03918 145 IFVSALTGEGIDELKEA 161
DUF258 pfam03193
Protein of unknown function, DUF258;
78-173 8.74e-03

Protein of unknown function, DUF258;


Pssm-ID: 281221  Cd Length: 174  Bit Score: 35.59  E-value: 8.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541992    78 DVILMCFSIDSPDSLENIPEKW--TPEVRhfcpNVPIILVGNKRDLRSDPQTVRELAKmkqepvkpeqgraIAEQIGaFA 155
Cdd:pfam03193  24 DQAVIVFSLKEPDFNLNLLDRFlvLAEAA----GIEPVIVLNKIDLLDEEEELEELLE-------------IYRAIG-YP 85
                          90
                  ....*....|....*...
gi 17541992   156 YLECSAKTKDGIREVFEK 173
Cdd:pfam03193  86 VLFVSAKTGEGLEALKEL 103
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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