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Conserved domains on  [gi|1907154220|ref|XP_036019576|]
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GTP-binding protein GEM isoform X1 [Mus musculus]

Protein Classification

RGK family GTP-binding protein( domain architecture ID 10134947)

RGK (Rem, Rem2, Rad, Gem/Kir) family GTP-binding protein binds 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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RGK cd04148
Rem, Rem2, Rad, Gem/Kir (RGK) subfamily of Ras GTPases; RGK subfamily. The RGK (Rem, Rem2, Rad, ...
75-281 1.70e-137

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


:

Pssm-ID: 206715 [Multi-domain]  Cd Length: 219  Bit Score: 386.76  E-value: 1.70e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFA-------------EDTYERTLVVDGESATIILLDMWENKGeNEWLHDHCMQVGDAYLIV 141
Cdd:cd04148     1 YRVVLLGDSGVGKSSLANIFTagvyedsayeasgDDTYERTVSVDGEEATLVVYDHWEQED-GMWLEDSCMQVGDAYVIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 142 YSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEGIV 221
Cdd:cd04148    80 YSVTDRSSFEKASELRIQLRRARQAEDIPIILVGNKSDLVRSREVSVQEGRACAVVFDCKFIETSAALQHNVDELFEGIV 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 222 RQVRLRRDSKEKNERRLAYQKRRESIPRKARRFWGKIVAKNNKNMAFKLKSKSCHDLSVL 281
Cdd:cd04148   160 RQVRLRRDSKEKNTRRMASRKRRESITKKAKRFLSKIVAKNNKGMAFKQKSKSCHDLSVL 219
 
Name Accession Description Interval E-value
RGK cd04148
Rem, Rem2, Rad, Gem/Kir (RGK) subfamily of Ras GTPases; RGK subfamily. The RGK (Rem, Rem2, Rad, ...
75-281 1.70e-137

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


Pssm-ID: 206715 [Multi-domain]  Cd Length: 219  Bit Score: 386.76  E-value: 1.70e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFA-------------EDTYERTLVVDGESATIILLDMWENKGeNEWLHDHCMQVGDAYLIV 141
Cdd:cd04148     1 YRVVLLGDSGVGKSSLANIFTagvyedsayeasgDDTYERTVSVDGEEATLVVYDHWEQED-GMWLEDSCMQVGDAYVIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 142 YSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEGIV 221
Cdd:cd04148    80 YSVTDRSSFEKASELRIQLRRARQAEDIPIILVGNKSDLVRSREVSVQEGRACAVVFDCKFIETSAALQHNVDELFEGIV 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 222 RQVRLRRDSKEKNERRLAYQKRRESIPRKARRFWGKIVAKNNKNMAFKLKSKSCHDLSVL 281
Cdd:cd04148   160 RQVRLRRDSKEKNTRRMASRKRRESITKKAKRFLSKIVAKNNKGMAFKQKSKSCHDLSVL 219
small_GTPase smart00010
Small GTPase of the Ras superfamily; ill-defined subfamily; SMART predicts Ras-like small ...
75-227 1.54e-45

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 [Multi-domain]  Cd Length: 166  Bit Score: 150.79  E-value: 1.54e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220   75 YRVVLIGEQGVGKSTL-----ANIFA-------EDTYERTLVVDGESATIILLDmweNKGENEW--LHDHCMQVGDAYLI 140
Cdd:smart00010   3 YKLVVLGGGGVGKSALtiqfvQGHFVdeydptiEDSYRKQIEIDGEVCLLDILD---TAGQEEFsaMRDQYMRTGEGFLL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  141 VYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEGI 220
Cdd:smart00010  80 VYSITDRQSFEEIAKFREQILRVKDRDDVPIVLVGNKCDLENERVVSTEEGKELARQWGCPFLETSAKERINVDEAFYDL 159

                   ....*..
gi 1907154220  221 VRQVRLR 227
Cdd:smart00010 160 VREIRKS 166
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
76-225 9.48e-39

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


Pssm-ID: 425451 [Multi-domain]  Cd Length: 162  Bit Score: 133.41  E-value: 9.48e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTLANIFAEDT-------------YERTLVVDGEsatIILLDMWENKGENEW--LHDHCMQVGDAYLI 140
Cdd:pfam00071   1 KLVLVGDGGVGKSSLLIRFTQNKfpeeyiptigvdfYTKTIEVDGK---TVKLQIWDTAGQERFraLRPLYYRGADGFLL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 141 VYSITDRASFEKASELRIQLRRARQtEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEGI 220
Cdd:pfam00071  78 VYDITSRDSFENVKKWVEEILRHAD-ENVPIVLVGNKCDLEDQRVVSTEEGEALAKELGLPFMETSAKTNENVEEAFEEL 156

                  ....*
gi 1907154220 221 VRQVR 225
Cdd:pfam00071 157 AREIL 161
PTZ00369 PTZ00369
Ras-like protein; Provisional
73-237 1.78e-34

Ras-like protein; Provisional


Pssm-ID: 240385 [Multi-domain]  Cd Length: 189  Bit Score: 123.44  E-value: 1.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  73 TYYRVVLIGEQGVGKSTLA-----NIFA-------EDTYERTLVVDGESAtiiLLDMWENKGENEW--LHDHCMQVGDAY 138
Cdd:PTZ00369    4 TEYKLVVVGGGGVGKSALTiqfiqNHFIdeydptiEDSYRKQCVIDEETC---LLDILDTAGQEEYsaMRDQYMRTGQGF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 139 LIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFE 218
Cdd:PTZ00369   81 LCVYSITSRSSFEEIASFREQILRVKDKDRVPMILVGNKCDLDSERQVSTGEGQELAKSFGIPFLETSAKQRVNVDEAFY 160
                         170       180
                  ....*....|....*....|.
gi 1907154220 219 GIVRQVR--LRRDSKEKNERR 237
Cdd:PTZ00369  161 ELVREIRkyLKEDMPSQKQKK 181
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
76-232 2.89e-13

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 66.54  E-value: 2.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTLAN-----IFAEDTYERT---------LVVDGESATIILLDMwenKGENE----------WLHDHc 131
Cdd:COG1100     5 KIVVVGTGGVGKTSLVNrlvgdIFSLEKYLSTngvtidkkeLKLDGLDVDLVIWDT---PGQDEfretrqfyarQLTGA- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 132 mqvgDAYLIVYSITDRASFEKASELRIQLRRARqtEDIPIILVGNKSDLVRCREVsVSEGRACAVVFDCKF---IETSAA 208
Cdd:COG1100    81 ----SLYLFVVDGTREETLQSLYELLESLRRLG--KKSPIILVLNKIDLYDEEEI-EDEERLKEALSEDNIvevVATSAK 153
                         170       180
                  ....*....|....*....|....
gi 1907154220 209 VQHNVKELFEGIVRQVRLRRDSKE 232
Cdd:COG1100   154 TGEGVEELFAALAEILRGEGDSLD 177
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
74-222 1.77e-08

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


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 52.76  E-value: 1.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  74 YYRVVLIGEQGVGKSTLANIFA-------------EDTYERTLV-VDGESATIILLDMwenKGENEW--LHDHCMQVGDA 137
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLgnkgsiteyypgtTRNYVTTVIeEDGKTYKFNLLDT---AGQEDYdaIRRLYYPQVER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 138 YLIVYSITDRA-SFEKASEL-RIQLRRARqTEDIPIILVGNKSDLvRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKE 215
Cdd:TIGR00231  78 SLRVFDIVILVlDVEEILEKqTKEIIHHA-DSGVPIILVGNKIDL-KDADLKTHVASEFAKLNGEPIIPLSAETGKNIDS 155

                  ....*..
gi 1907154220 216 LFEGIVR 222
Cdd:TIGR00231 156 AFKIVEA 162
 
Name Accession Description Interval E-value
RGK cd04148
Rem, Rem2, Rad, Gem/Kir (RGK) subfamily of Ras GTPases; RGK subfamily. The RGK (Rem, Rem2, Rad, ...
75-281 1.70e-137

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


Pssm-ID: 206715 [Multi-domain]  Cd Length: 219  Bit Score: 386.76  E-value: 1.70e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFA-------------EDTYERTLVVDGESATIILLDMWENKGeNEWLHDHCMQVGDAYLIV 141
Cdd:cd04148     1 YRVVLLGDSGVGKSSLANIFTagvyedsayeasgDDTYERTVSVDGEEATLVVYDHWEQED-GMWLEDSCMQVGDAYVIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 142 YSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEGIV 221
Cdd:cd04148    80 YSVTDRSSFEKASELRIQLRRARQAEDIPIILVGNKSDLVRSREVSVQEGRACAVVFDCKFIETSAALQHNVDELFEGIV 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 222 RQVRLRRDSKEKNERRLAYQKRRESIPRKARRFWGKIVAKNNKNMAFKLKSKSCHDLSVL 281
Cdd:cd04148   160 RQVRLRRDSKEKNTRRMASRKRRESITKKAKRFLSKIVAKNNKGMAFKQKSKSCHDLSVL 219
Ras cd00876
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ...
76-224 2.99e-58

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


Pssm-ID: 206642 [Multi-domain]  Cd Length: 160  Bit Score: 183.11  E-value: 2.99e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTLA-----NIF-------AEDTYERTLVVDGESATIILLDMWENkGENEWLHDHCMQVGDAYLIVYS 143
Cdd:cd00876     1 KLVVLGAGGVGKSALTirfvsGEFveeydptIEDSYRKQIVVDGETYTLDILDTAGQ-EEFSAMRDQYIRNGDGFILVYS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 144 ITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEGIVRQ 223
Cdd:cd00876    80 ITSRESFEEIKNIREQILRVKDKEDVPIVLVGNKCDLENERQVSTEEGEALAEEWGCPFLETSAKTNINIDELFNTLVRE 159

                  .
gi 1907154220 224 V 224
Cdd:cd00876   160 I 160
small_GTPase smart00010
Small GTPase of the Ras superfamily; ill-defined subfamily; SMART predicts Ras-like small ...
75-227 1.54e-45

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 [Multi-domain]  Cd Length: 166  Bit Score: 150.79  E-value: 1.54e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220   75 YRVVLIGEQGVGKSTL-----ANIFA-------EDTYERTLVVDGESATIILLDmweNKGENEW--LHDHCMQVGDAYLI 140
Cdd:smart00010   3 YKLVVLGGGGVGKSALtiqfvQGHFVdeydptiEDSYRKQIEIDGEVCLLDILD---TAGQEEFsaMRDQYMRTGEGFLL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  141 VYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEGI 220
Cdd:smart00010  80 VYSITDRQSFEEIAKFREQILRVKDRDDVPIVLVGNKCDLENERVVSTEEGKELARQWGCPFLETSAKERINVDEAFYDL 159

                   ....*..
gi 1907154220  221 VRQVRLR 227
Cdd:smart00010 160 VREIRKS 166
RAS smart00173
Ras subfamily of RAS small GTPases; Similar in fold and function to the bacterial EF-Tu GTPase. ...
75-225 4.46e-45

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 [Multi-domain]  Cd Length: 164  Bit Score: 149.63  E-value: 4.46e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220   75 YRVVLIGEQGVGKSTL-----ANIFA-------EDTYERTLVVDGESATIILLDmweNKGENEW--LHDHCMQVGDAYLI 140
Cdd:smart00173   1 YKLVVLGSGGVGKSALtiqfiQGHFVddydptiEDSYRKQIEIDGEVCLLDILD---TAGQEEFsaMRDQYMRTGEGFLL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  141 VYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEGI 220
Cdd:smart00173  78 VYSITDRQSFEEIKKFREQILRVKDRDDVPIVLVGNKCDLESERVVSTEEGKELARQWGCPFLETSAKERVNVDEAFYDL 157

                   ....*
gi 1907154220  221 VRQVR 225
Cdd:smart00173 158 VREIR 162
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
76-225 9.48e-39

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


Pssm-ID: 425451 [Multi-domain]  Cd Length: 162  Bit Score: 133.41  E-value: 9.48e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTLANIFAEDT-------------YERTLVVDGEsatIILLDMWENKGENEW--LHDHCMQVGDAYLI 140
Cdd:pfam00071   1 KLVLVGDGGVGKSSLLIRFTQNKfpeeyiptigvdfYTKTIEVDGK---TVKLQIWDTAGQERFraLRPLYYRGADGFLL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 141 VYSITDRASFEKASELRIQLRRARQtEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEGI 220
Cdd:pfam00071  78 VYDITSRDSFENVKKWVEEILRHAD-ENVPIVLVGNKCDLEDQRVVSTEEGEALAKELGLPFMETSAKTNENVEEAFEEL 156

                  ....*
gi 1907154220 221 VRQVR 225
Cdd:pfam00071 157 AREIL 161
Rit_Rin_Ric cd04141
Ras-like protein in all tissues (Rit), Ras-like protein in neurons (Rin) and Ras-related ...
75-225 1.15e-37

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 [Multi-domain]  Cd Length: 172  Bit Score: 131.13  E-value: 1.15e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFA------------EDTYERTLVVDGESAtiiLLDMWENKGENEW--LHDHCMQVGDAYLI 140
Cdd:cd04141     3 YKIVMLGAGGVGKSAVTMQFIshsfpdyhdptiEDAYKTQARIDNEPA---LLDILDTAGQAEFtaMRDQYMRCGEGFII 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 141 VYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEGI 220
Cdd:cd04141    80 CYSVTDRHSFQEASEFKELITRVRLTEDIPLVLVGNKVDLEQQRQVTTEEGRNLAREFNCPFFETSAALRFYIDDAFHGL 159

                  ....*
gi 1907154220 221 VRQVR 225
Cdd:cd04141   160 VREIR 164
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, ...
75-225 8.62e-37

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 [Multi-domain]  Cd Length: 162  Bit Score: 128.31  E-value: 8.62e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLA-----NIFA-------EDTYERTLVVDGESAtiiLLDMWENKGENEW--LHDHCMQVGDAYLI 140
Cdd:cd04138     2 YKLVVVGAGGVGKSALTiqliqNHFVdeydptiEDSYRKQVVIDGETC---LLDILDTAGQEEYsaMRDQYMRTGEGFLC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 141 VYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLvRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEGI 220
Cdd:cd04138    79 VFAINSRKSFEDIHTYREQIKRVKDSDDVPMVLVGNKCDL-AARTVSTRQGQDLAKSYGIPYIETSAKTRQGVEEAFYTL 157

                  ....*
gi 1907154220 221 VRQVR 225
Cdd:cd04138   158 VREIR 162
Ras2 cd04144
Rat sarcoma (Ras) family 2 of small guanosine triphosphatases (GTPases); The Ras2 subfamily, ...
76-245 1.65e-34

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 [Multi-domain]  Cd Length: 190  Bit Score: 123.42  E-value: 1.65e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTLA-----NIFAE-------DTYERTLVVDGESATIILLDmweNKGENEW--LHDHCMQVGDAYLIV 141
Cdd:cd04144     1 KLVVLGDGGVGKTALTiqlclNHFVEtydptieDSYRKQVVVDGQPCMLEVLD---TAGQEEYtaLRDQWIREGEGFILV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 142 YSITDRASFEKASELRIQLRRARQTE--DIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEG 219
Cdd:cd04144    78 YSITSRSTFERVERFREQIQRVKDESaaDVPIMIVGNKCDKVYEREVSTEEGAALARRLGCEFIEASAKTNVNVERAFYT 157
                         170       180
                  ....*....|....*....|....*.
gi 1907154220 220 IVRQVRLRRDSKEKNERRLAYQKRRE 245
Cdd:cd04144   158 LVRALRQQRQGGQGPKGGPTKKKEKK 183
PTZ00369 PTZ00369
Ras-like protein; Provisional
73-237 1.78e-34

Ras-like protein; Provisional


Pssm-ID: 240385 [Multi-domain]  Cd Length: 189  Bit Score: 123.44  E-value: 1.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  73 TYYRVVLIGEQGVGKSTLA-----NIFA-------EDTYERTLVVDGESAtiiLLDMWENKGENEW--LHDHCMQVGDAY 138
Cdd:PTZ00369    4 TEYKLVVVGGGGVGKSALTiqfiqNHFIdeydptiEDSYRKQCVIDEETC---LLDILDTAGQEEYsaMRDQYMRTGQGF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 139 LIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFE 218
Cdd:PTZ00369   81 LCVYSITSRSSFEEIASFREQILRVKDKDRVPMILVGNKCDLDSERQVSTGEGQELAKSFGIPFLETSAKQRVNVDEAFY 160
                         170       180
                  ....*....|....*....|.
gi 1907154220 219 GIVRQVR--LRRDSKEKNERR 237
Cdd:PTZ00369  161 ELVREIRkyLKEDMPSQKQKK 181
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, ...
74-225 5.72e-34

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 [Multi-domain]  Cd Length: 164  Bit Score: 120.98  E-value: 5.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  74 YYRVVLIGEQGVGKSTLANIF------------AEDTYERTLVVDGESAtiiLLDMWENKGENEW--LHDHCMQVGDAYL 139
Cdd:cd04145     2 TYKLVVVGGGGVGKSALTIQFiqsyfvtdydptIEDSYTKQCEIDGQWA---RLDILDTAGQEEFsaMREQYMRTGEGFL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 140 IVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEG 219
Cdd:cd04145    79 LVFSVTDRGSFEEVDKFHTQILRVKDRDEFPMILVGNKADLEHQRQVSREEGQELARQLKIPYIETSAKDRVNVDKAFHD 158

                  ....*.
gi 1907154220 220 IVRQVR 225
Cdd:cd04145   159 LVRVIR 164
Rap_like cd04136
Rap-like family consists of Rap1, Rap2 and RSR1; The Rap subfamily consists of the Rap1, Rap2, ...
75-224 7.26e-32

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 [Multi-domain]  Cd Length: 164  Bit Score: 115.73  E-value: 7.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFA------------EDTYERTLVVDGESATIILLDmweNKGENEW--LHDHCMQVGDAYLI 140
Cdd:cd04136     2 YKLVVLGSGGVGKSALTVQFVqgifvdkydptiEDSYRKQIEVDCQQCMLEILD---TAGTEQFtaMRDLYIKNGQGFAL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 141 VYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVF-DCKFIETSAAVQHNVKELFEG 219
Cdd:cd04136    79 VYSITAQQSFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVSKEEGQNLARQWgNCPFLETSAKSKINVDEIFYD 158

                  ....*
gi 1907154220 220 IVRQV 224
Cdd:cd04136   159 LVRQI 163
RalA_RalB cd04139
Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily ...
75-225 1.52e-31

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 [Multi-domain]  Cd Length: 163  Bit Score: 114.83  E-value: 1.52e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIF------------AEDTYERTLVVDGESatiILLDMWENKGENEW--LHDHCMQVGDAYLI 140
Cdd:cd04139     1 HKVIMVGSGGVGKSALTLQFmydefvedyeptKADSYRKKVVLDGEE---VQLNILDTAGQEDYaaIRDNYFRSGEGFLL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 141 VYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEGI 220
Cdd:cd04139    78 VFSITDMESFTALAEFREQILRVKEDDNVPLLLVGNKCDLEDKRQVSVEEAANLAEQWGVNYVETSAKTRANVDKVFFDL 157

                  ....*
gi 1907154220 221 VRQVR 225
Cdd:cd04139   158 VREIR 162
Rap2 cd04176
Rap2 family GTPase consists of Rap2a, Rap2b, and Rap2c; The Rap2 subgroup is part of the Rap ...
75-224 4.22e-31

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 [Multi-domain]  Cd Length: 163  Bit Score: 113.78  E-value: 4.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFA------------EDTYERTLVVDGESATIILLDmweNKGENEW--LHDHCMQVGDAYLI 140
Cdd:cd04176     2 YKVVVLGSGGVGKSALTVQFVsgtfiekydptiEDFYRKEIEVDSSPSVLEILD---TAGTEQFasMRDLYIKNGQGFIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 141 VYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEGI 220
Cdd:cd04176    79 VYSLVNQQTFQDIKPMRDQIVRVKGYEKVPIILVGNKVDLESEREVSSAEGRALAEEWGCPFMETSAKSKTMVNELFAEI 158

                  ....
gi 1907154220 221 VRQV 224
Cdd:cd04176   159 VRQM 162
Rap1 cd04175
Rap1 family GTPase consists of Rap1a and Rap1b isoforms; The Rap1 subgroup is part of the Rap ...
75-224 1.47e-30

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 [Multi-domain]  Cd Length: 164  Bit Score: 112.23  E-value: 1.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLA-----NIFA-------EDTYERTLVVDGESATIILLDmweNKGENEW--LHDHCMQVGDAYLI 140
Cdd:cd04175     2 YKLVVLGSGGVGKSALTvqfvqGIFVekydptiEDSYRKQVEVDGQQCMLEILD---TAGTEQFtaMRDLYMKNGQGFVL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 141 VYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEGI 220
Cdd:cd04175    79 VYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVGKEQGQNLARQWGCAFLETSAKAKINVNEIFYDL 158

                  ....
gi 1907154220 221 VRQV 224
Cdd:cd04175   159 VRQI 162
RERG_RasL11_like cd04146
Ras-related and Estrogen-Regulated Growth inhibitor (RERG) and Ras-like 11 (RasL11)-like ...
77-225 2.00e-30

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 [Multi-domain]  Cd Length: 166  Bit Score: 111.99  E-value: 2.00e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  77 VVLIGEQGVGKSTLANIF------------AEDTYERTLVVDGESATIILLDM--WENKGENEWLhDHCMQVGDAYLIVY 142
Cdd:cd04146     2 IAVLGASGVGKSALTVRFltkrfigeyepnLESLYSRQVTIDGEQVSLEIQDTpgQQQNEDPESL-ERSLRWADGFVLVY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 143 SITDRASFEKASELRIQLRRARQTE-DIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQ-HNVKELFEGI 220
Cdd:cd04146    81 SITDRSSFDVVSQLLQLIREIKKRDgEIPVILVGNKADLLHSRQVSTEEGQKLALELGCLFFEVSAAENyLEVQNVFHEL 160

                  ....*
gi 1907154220 221 VRQVR 225
Cdd:cd04146   161 CREVR 165
ARHI_like cd04140
A Ras homolog member I (ARHI); ARHI (A Ras homolog member I) is a member of the Ras family ...
75-218 2.65e-30

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 [Multi-domain]  Cd Length: 165  Bit Score: 111.46  E-value: 2.65e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFA------------EDTYERTLvvdGESATIILLDMWENKGENEW--LHDHCMQVGDAYLI 140
Cdd:cd04140     2 YRVVVFGAGGVGKSSLVLRFVkgtfresyiptiEDTYRQVI---SCSKSICTLQITDTTGSHQFpaMQRLSISKGHAFIL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 141 VYSITDRASFEKASELRIQLRRAR--QTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFE 218
Cdd:cd04140    79 VYSITSKQSLEELKPIYELICEIKgnNLEKIPIMLVGNKCDESPSREVSSSEGAALARTWNCAFMETSAKTNHNVQELFQ 158
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
75-222 1.68e-29

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


Pssm-ID: 206640 [Multi-domain]  Cd Length: 159  Bit Score: 109.08  E-value: 1.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFAEDTYER----TLVVDGESATIILldmwenKGENewlhdHCMQVGD-------------- 136
Cdd:cd00154     1 FKIVLIGDSGVGKTSLLLRFVDNKFSEnyksTIGVDFKSKTIEV------DGKK-----VKLQIWDtagqerfrsitssy 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 137 -----AYLIVYSITDRASFEKASELRIQLRRaRQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQH 211
Cdd:cd00154    70 yrgahGAILVYDVTNRESFENLDKWLNELKE-YAPPNIPIILVGNKSDLEDERQVSTEEAQQFAKENGLLFFETSAKTGE 148
                         170
                  ....*....|.
gi 1907154220 212 NVKELFEGIVR 222
Cdd:cd00154   149 NVDEAFESLAR 159
RSR1 cd04177
RSR1/Bud1p family GTPase; RSR1/Bud1p is a member of the Rap subfamily of the Ras family that ...
75-225 1.11e-28

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 [Multi-domain]  Cd Length: 168  Bit Score: 107.57  E-value: 1.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLA-----NIFA-------EDTYERTLVVDGESATIILLDmweNKGENEW--LHDHCMQVGDAYLI 140
Cdd:cd04177     2 YKIVVLGAGGVGKSALTvqfvqNVFIesydptiEDSYRKQVEIDGRQCDLEILD---TAGTEQFtaMRELYIKSGQGFLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 141 VYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVF-DCKFIETSAAVQHNVKELFEG 219
Cdd:cd04177    79 VYSVTSEASLNELGELREQVLRIKDSDNVPMVLVGNKADLEDDRQVSREDGVSLSQQWgNVPFYETSARKRTNVDEVFID 158

                  ....*.
gi 1907154220 220 IVRQVR 225
Cdd:cd04177   159 LVRQII 164
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
75-224 2.58e-28

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


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 106.44  E-value: 2.58e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220   75 YRVVLIGEQGVGKSTLANIFAEDTYE-------------RTLVVDGesaTIILLDMWENKGenewlhdhcmQ-----VGD 136
Cdd:smart00175   1 FKIILIGDSGVGKSSLLSRFTDGKFSeqykstigvdfktKTIEVDG---KRVKLQIWDTAG----------QerfrsITS 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  137 AY-------LIVYSITDRASFEKASELRIQLRRARQtEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAV 209
Cdd:smart00175  68 SYyrgavgaLLVYDITNRESFENLENWLKELREYAS-PNVVIMLVGNKSDLEEQRQVSREEAEAFAEEHGLPFFETSAKT 146
                          170
                   ....*....|....*
gi 1907154220  210 QHNVKELFEGIVRQV 224
Cdd:smart00175 147 NTNVEEAFEELAREI 161
RheB cd04137
Ras Homolog Enriched in Brain (RheB) is a small GTPase; Rheb (Ras Homolog Enriched in Brain) ...
76-237 8.89e-27

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 [Multi-domain]  Cd Length: 180  Bit Score: 102.71  E-value: 8.89e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTLA-----NIFA-------EDTYERTLVVDGESATIILLDmweNKGENEW--LHDHCMQVGDAYLIV 141
Cdd:cd04137     3 KIAVLGSRSVGKSSLTvqfveGHFVesyyptiENTFSKIITYKGQEYHLEIVD---TAGQDEYsiLPQKYSIGIHGYILV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 142 YSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEGIV 221
Cdd:cd04137    80 YSVTSRKSFEVVKVIYDKILDMLGKESVPIVLVGNKSDLHMERQVSAEEGKKLAESWGAAFLESSAKENENVEEAFELLI 159
                         170
                  ....*....|....*..
gi 1907154220 222 RQV-RLRRDSKEKNERR 237
Cdd:cd04137   160 EEIeKVENPLPPGQKSK 176
Rab21 cd04123
Rab GTPase family 21 (Rab21); The localization and function of Rab21 are not clearly defined, ...
75-224 2.48e-25

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 [Multi-domain]  Cd Length: 162  Bit Score: 98.45  E-value: 2.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFAEDT-------------YERTLVVDGESATiilLDMWENKGENEWlhdHCM-----QVGD 136
Cdd:cd04123     1 FKVVLLGEGRVGKTSLVLRYVENKfnekhesttqasfFQKTVNIGGKRID---LAIWDTAGQERY---HALgpiyyRDAD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 137 AYLIVYSITDRASFEKASELRIQLRRARQtEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKEL 216
Cdd:cd04123    75 GAILVYDITDADSFQKVKKWIKELKQMRG-NNISLVIVGNKIDLERQRVVSKSEAEEYAKSVGAKHFETSAKTGKGIEEL 153

                  ....*...
gi 1907154220 217 FEGIVRQV 224
Cdd:cd04123   154 FLSLAKRM 161
Rab5_related cd01860
Rab-related GTPase family includes Rab5 and Rab22; regulates early endosome fusion; The ...
75-224 3.96e-24

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 [Multi-domain]  Cd Length: 163  Bit Score: 95.31  E-value: 3.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFAEDTYE-------------RTLVVDGesaTIILLDMWENKGEnEWLHDHC-MQVGDA--Y 138
Cdd:cd01860     2 FKLVLLGDSSVGKSSIVLRFVKNEFSenqestigaafltQTVNLDD---TTVKFEIWDTAGQ-ERYRSLApMYYRGAaaA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 139 LIVYSITDRASFEKA----SELRIQLRrarqtEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVK 214
Cdd:cd01860    78 IVVYDITSEESFEKAkswvKELQEHGP-----PNIVIALAGNKADLESKRQVSTEEAQEYADENGLLFMETSAKTGENVN 152
                         170
                  ....*....|
gi 1907154220 215 ELFEGIVRQV 224
Cdd:cd01860   153 ELFTEIARKL 162
Rab6 cd01861
Rab GTPase family 6 (Rab6); Rab6 is involved in microtubule-dependent transport pathways ...
75-220 2.22e-23

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 [Multi-domain]  Cd Length: 161  Bit Score: 93.46  E-value: 2.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFAEDT----YERTLVVDGESATI------ILLDMWENKGENE-------WLHDHCMQVgda 137
Cdd:cd01861     1 HKLVFLGDQSVGKTSIITRFMYDTfdnqYQATIGIDFLSKTMyvddktVRLQLWDTAGQERfrslipsYIRDSSVAV--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 138 ylIVYSITDRASFEKASELrIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELF 217
Cdd:cd01861    78 --VVYDITNRQSFDNTDKW-IDDVRDERGNDVIIVLVGNKTDLSDKRQVSTEEGEKKAKENNAMFIETSAKAGHNVKQLF 154

                  ...
gi 1907154220 218 EGI 220
Cdd:cd01861   155 KKI 157
Ras_dva cd04147
Ras - dorsal-ventral anterior localization (Ras-dva) family; Ras-dva subfamily. Ras-dva (Ras - ...
76-253 7.19e-23

Ras - dorsal-ventral anterior localization (Ras-dva) family; Ras-dva subfamily. Ras-dva (Ras - dorsal-ventral anterior localization) subfamily consists of a set of proteins characterized only in Xenopus leavis, to date. In Xenopus Ras-dva expression is activated by the transcription factor Otx2 and begins during gastrulation throughout the anterior ectoderm. Ras-dva expression is inhibited in the anterior neural plate by factor Xanf1. Downregulation of Ras-dva results in head development abnormalities through the inhibition of several regulators of the anterior neural plate and folds patterning, including Otx2, BF-1, Xag2, Pax6, Slug, and Sox9. Downregulation of Ras-dva also interferes with the FGF-8a signaling within the anterior ectoderm. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins.


Pssm-ID: 206714 [Multi-domain]  Cd Length: 197  Bit Score: 92.98  E-value: 7.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTLANIFAEDTYE----RTL--------VVDGESATIILLDmweNKGENEW--LHDHCMQVGDAYLIV 141
Cdd:cd04147     1 RLVFMGAAGVGKTALIQRFLYDTFEpkhrRTVeelhskeyEVAGVKVTIDILD---TSGSYSFpaMRKLSIQNGDAFALV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 142 YSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVV-FDCKFIETSAAVQHNVKELFEGI 220
Cdd:cd04147    78 YSVDDPESFEEVKRLREEILEVKEDKFVPIVVVGNKIDSLAERQVEAADALSTVELdWNNGFVEASAKDNENVTEVFKEL 157
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907154220 221 VRQVRLrrdskeknERRL--AYQKRRESIPRKARR 253
Cdd:cd04147   158 LQQANL--------PSWLspALRRRRESAPSEIQR 184
Rab11_like cd01868
Rab GTPase family 11 (Rab11)-like includes Rab11a, Rab11b, and Rab25; Rab11a, Rab11b, and ...
75-224 3.00e-22

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 [Multi-domain]  Cd Length: 165  Bit Score: 90.31  E-value: 3.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFAEDTYE-------------RTLVVDGEsatIILLDMWENKGENEWLhdhcmQVGDAY--- 138
Cdd:cd01868     4 FKIVLIGDSGVGKSNLLSRFTRNEFNldskstigvefatRTIQIDGK---TIKAQIWDTAGQERYR-----AITSAYyrg 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 139 ----LIVYSITDRASFEKA----SELRiqlrrARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQ 210
Cdd:cd01868    76 avgaLLVYDITKKSTFENVerwlKELR-----DHADSNIVIMLVGNKSDLRHLRAVPTEEAKAFAEKNGLSFIETSALDG 150
                         170
                  ....*....|....
gi 1907154220 211 HNVKELFEGIVRQV 224
Cdd:cd01868   151 TNVEEAFKQLLTEI 164
Rab1_Ypt1 cd01869
Rab GTPase family 1 includes the yeast homolog Ypt1; Rab1/Ypt1 subfamily. Rab1 is found in ...
75-227 3.98e-21

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 [Multi-domain]  Cd Length: 166  Bit Score: 87.38  E-value: 3.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFAEDTYE-------------RTLVVDGEsatIILLDMWENKGENEW--LHDHCMQVGDAYL 139
Cdd:cd01869     3 FKLLLIGDSGVGKSCLLLRFADDTYTesyistigvdfkiRTIELDGK---TVKLQIWDTAGQERFrtITSSYYRGAHGII 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 140 IVYSITDRASFEKASELRIQLRRArQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEG 219
Cdd:cd01869    80 IVYDVTDQESFNNVKQWLQEIDRY-ASENVNKLLVGNKCDLTDKKVVDYTEAKEFADELGIPFLETSAKNATNVEEAFMT 158

                  ....*...
gi 1907154220 220 IVRQVRLR 227
Cdd:cd01869   159 MAREIKKR 166
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
78-222 9.51e-21

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 86.36  E-value: 9.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  78 VLIGEQGVGKSTLANIFAEDTYERTLVVDGESATIILLDMWENKGE------------------NEWLHDHCMQVGDAYL 139
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYVKELDKGKvklvlvdtpgldefgglgREELARLLLRGADLIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 140 IVYSITDRASFEKASELRIQLRRARqteDIPIILVGNKSDLV-RCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFE 218
Cdd:cd00882    81 LVVDSTDRESEEDAKLLILRRLRKE---GIPIILVGNKIDLLeEREVEELLRLEELAKILGVPVFEVSAKTGEGVDELFE 157

                  ....
gi 1907154220 219 GIVR 222
Cdd:cd00882   158 KLIE 161
Rab8_Rab10_Rab13_like cd01867
Rab GTPase families 8, 10, 13 (Rab8, Rab10, Rab13); Rab8/Sec4/Ypt2 are known or suspected to ...
75-227 8.90e-20

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 [Multi-domain]  Cd Length: 167  Bit Score: 83.86  E-value: 8.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFAED----TYERTLVVDGESATI------ILLDMWENKGEnEWLHdhcmQVGDAY------ 138
Cdd:cd01867     4 FKLLLIGDSGVGKSCLLLRFSEDsfnpSFISTIGIDFKIRTIeldgkkIKLQIWDTAGQ-ERFR----TITTSYyrgamg 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 139 -LIVYSITDRASFEkasELRIQLRRARQ--TEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKE 215
Cdd:cd01867    79 iILVYDITDEKSFE---NIKNWMRNIDEhaSEDVERMLVGNKCDMEEKRVVSKEEGEALAREYGIKFLETSAKANINVEE 155
                         170
                  ....*....|..
gi 1907154220 216 LFEGIVRQVRLR 227
Cdd:cd01867   156 AFLTLAKDILKK 167
Rab39 cd04111
Rab GTPase family 39 (Rab39); Found in eukaryotes, Rab39 is mainly found in epithelial cell ...
75-232 4.72e-19

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


Pssm-ID: 133311 [Multi-domain]  Cd Length: 211  Bit Score: 83.27  E-value: 4.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFAE-------------DTYERTlvVDGESATIILLDMWENKGENEWlhdhcMQVGDAY--- 138
Cdd:cd04111     3 FRLIVIGDSTVGKSSLLKRFTEgrfaevsdptvgvDFFSRL--IEIEPGVRIKLQLWDTAGQERF-----RSITRSYyrn 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 139 ----LIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVK 214
Cdd:cd04111    76 svgvLLVFDITNRESFEHVHDWLEEARSHIQPHRPVFILVGHKCDLESQRQVTREEAEKLAKDLGMKYIETSARTGDNVE 155
                         170
                  ....*....|....*...
gi 1907154220 215 ELFEGIVRQVRLRRDSKE 232
Cdd:cd04111   156 EAFELLTQEIYERIKRGE 173
Rho cd00157
Ras homology family (Rho) of small guanosine triphosphatases (GTPases); Members of the Rho ...
77-222 1.07e-18

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 [Multi-domain]  Cd Length: 171  Bit Score: 81.05  E-value: 1.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  77 VVLIGEQGVGKSTLANIFAE------------DTYERTLVVDGESatiILLDMWENKGENEwlHDH----CMQVGDAYLI 140
Cdd:cd00157     3 IVVVGDGAVGKTCLLISYTTnkfpteyvptvfDNYSANVTVDGKQ---VNLGLWDTAGQEE--YDRlrplSYPQTDVFLL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 141 VYSITDRASFEKAS-----ELRiqlrraRQTEDIPIILVGNKSDLvrcRE--------------VSVSEGRACAVVFDC- 200
Cdd:cd00157    78 CFSVDSPSSFENVKtkwypEIK------HYCPNVPIILVGTKIDL---RDdgntlkklekkqkpITPEEGEKLAKEIGAv 148
                         170       180
                  ....*....|....*....|..
gi 1907154220 201 KFIETSAAVQHNVKELFEGIVR 222
Cdd:cd00157   149 KYMECSALTQEGLKEVFDEAIR 170
Miro1 cd01893
Mitochondrial Rho family 1 (Miro1), N-terminal; Miro1 subfamily. Miro (mitochondrial Rho) ...
76-217 2.49e-18

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 [Multi-domain]  Cd Length: 168  Bit Score: 80.07  E-value: 2.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTLANIFAEDTY---------ERTLVVDG--ESATIILLDMWENKGENEWLHDHCMQvGDAYLIVYSI 144
Cdd:cd01893     4 RIVLIGDEGVGKSSLIMSLVSEEFpenvprvlpEITIPADVtpERVPTTIVDTSSRPQDRANLAAEIRK-ANVICLVYSV 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907154220 145 TDRASFEKASELRIQLRRaRQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIET----SAAVQHNVKELF 217
Cdd:cd01893    83 DRPSTLERIRTKWLPLIR-RLGVKVPIILVGNKSDLRDGSSQAGLEEEMLPIMNEFREIETcvecSAKTLINVSEVF 158
Rab9 cd04116
Rab GTPase family 9 (Rab9); Rab9 is found in late endosomes, together with mannose 6-phosphate ...
76-224 6.41e-18

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 [Multi-domain]  Cd Length: 170  Bit Score: 79.15  E-value: 6.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTLANIFAEDTYE-------------RTLVVDGESATiilLDMWENKGENEW--LHDHCMQVGDAYLI 140
Cdd:cd04116     7 KVILLGDGGVGKSSLMNRYVTNKFDtqlfhtigveflnKDLEVDGHFVT---LQIWDTAGQERFrsLRTPFYRGSDCCLL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 141 VYSITDRASFEKASELR---IQLRRARQTEDIPIILVGNKSDLVRcREVSVSEGRA-CAVVFDCKFIETSAAVQHNVKEL 216
Cdd:cd04116    84 TFSVDDSQSFQNLSNWKkefIYYADVKEPESFPFVILGNKIDIPE-RQVSTEEAQAwCRDNGDYPYFETSAKDATNVAAA 162

                  ....*...
gi 1907154220 217 FEGIVRQV 224
Cdd:cd04116   163 FEEAVRRV 170
PLN03110 PLN03110
Rab GTPase; Provisional
75-224 1.71e-16

Rab GTPase; Provisional


Pssm-ID: 178657 [Multi-domain]  Cd Length: 216  Bit Score: 76.12  E-value: 1.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFAEDTY-------------ERTLVVDGESatiILLDMWENKGENEWlhdhcMQVGDAY--- 138
Cdd:PLN03110   13 FKIVLIGDSGVGKSNILSRFTRNEFcleskstigvefaTRTLQVEGKT---VKAQIWDTAGQERY-----RAITSAYyrg 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 139 ----LIVYSITDRASFEKASELriqLRRARQTED--IPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHN 212
Cdd:PLN03110   85 avgaLLVYDITKRQTFDNVQRW---LRELRDHADsnIVIMMAGNKSDLNHLRSVAEEDGQALAEKEGLSFLETSALEATN 161
                         170
                  ....*....|..
gi 1907154220 213 VKELFEGIVRQV 224
Cdd:PLN03110  162 VEKAFQTILLEI 173
Rab18 cd01863
Rab GTPase family 18 (Rab18); Rab18 subfamily. Mammalian Rab18 is implicated in endocytic ...
75-224 2.63e-16

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


Pssm-ID: 206656 [Multi-domain]  Cd Length: 161  Bit Score: 74.27  E-value: 2.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFAEDTYE-------------RTLVVDGesaTIILLDMWENKGENEW--LHDHCMQVGDAYL 139
Cdd:cd01863     1 LKILLIGDSGVGKSSLLLRFTDDTFDedlsstigvdfkvKTVTVDG---KKVKLAIWDTAGQERFrtLTSSYYRGAQGVI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 140 IVYSITDRASFEKaseLRIQLRRAR---QTEDIPIILVGNKSDLVRcREVSVSEGRACAVVFDCKFIETSAAVQHNVKEL 216
Cdd:cd01863    78 LVYDVTRRDTFDN---LDTWLNELDtysTNPDAVKMLVGNKIDKEN-REVTREEGQKFARKHNMLFIETSAKTRIGVQQA 153

                  ....*...
gi 1907154220 217 FEGIVRQV 224
Cdd:cd01863   154 FEELVEKI 161
Rab2 cd01866
Rab GTPase family 2 (Rab2); Rab2 is localized on cis-Golgi membranes and interacts with Golgi ...
75-217 3.24e-16

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 [Multi-domain]  Cd Length: 168  Bit Score: 74.38  E-value: 3.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFAEDTYE-------------RTLVVDGESatiILLDMWENKGENEWlhdhcMQVGDAY--- 138
Cdd:cd01866     5 FKYIIIGDTGVGKSCLLLQFTDKRFQpvhdltigvefgaRMITIDGKQ---IKLQIWDTAGQESF-----RSITRSYyrg 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 139 ----LIVYSITDRASFEKaseLRIQLRRARQ--TEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHN 212
Cdd:cd01866    77 aagaLLVYDITRRETFNH---LTSWLEDARQhsNSNMTIMLIGNKCDLESRREVSYEEGEAFAREHGLIFMETSAKTASN 153

                  ....*
gi 1907154220 213 VKELF 217
Cdd:cd01866   154 VEEAF 158
RabL4 cd04101
Rab GTPase-like family 4 (Rab-like4); RabL4 (Rab-like4) subfamily. RabL4s are novel proteins ...
76-223 1.32e-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 [Multi-domain]  Cd Length: 167  Bit Score: 72.56  E-value: 1.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTLANIFAED--TYERT--------LVV-------DGESATIILLDMwENKGENEWLHDHCMQVGDAY 138
Cdd:cd04101     2 QCAVVGDPAVGKSALVQMFHSDgaTFQKNytmttgcdLVVktvpvpdTSDSVELFIFDS-AGQELFSDMVENVWEQPAVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 139 LIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFE 218
Cdd:cd04101    81 CVVYDVTNEVSFNNCSRWINRVRTHSHGLHTPGVLVGNKCDLTDRREVDAAQAQALAQANTLKFYETSAKEGVGYEAPFL 160

                  ....*
gi 1907154220 219 GIVRQ 223
Cdd:cd04101   161 SLARA 165
PLN03118 PLN03118
Rab family protein; Provisional
67-248 7.51e-15

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 71.63  E-value: 7.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  67 SSESGNTY---YRVVLIGEQGVGKSTLANIFAEDTYE------------RTLVVDGESatiILLDMWENKGENEW--LHD 129
Cdd:PLN03118    4 SSGQSSGYdlsFKILLIGDSGVGKSSLLVSFISSSVEdlaptigvdfkiKQLTVGGKR---LKLTIWDTAGQERFrtLTS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 130 HCMQVGDAYLIVYSITDRASFEKASEL---RIQLRRARQteDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETS 206
Cdd:PLN03118   81 SYYRNAQGIILVYDVTRRETFTNLSDVwgkEVELYSTNQ--DCVKMLVGNKVDRESERDVSREEGMALAKEHGCLFLECS 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907154220 207 AAVQHNVKELFEGIVRQV----RLRRDSKEKNERRLAYQKRRESIP 248
Cdd:PLN03118  159 AKTRENVEQCFEELALKImevpSLLEEGSTAVKRNILKQKPEHQPP 204
Wrch_1 cd04130
Wnt-1 responsive Cdc42 homolog (Wrch-1) is a Rho family GTPase similar to Cdc42; Wrch-1 (Wnt-1 ...
78-218 7.75e-15

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 [Multi-domain]  Cd Length: 173  Bit Score: 70.51  E-value: 7.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  78 VLIGEQGVGKSTL-----ANIF-------AEDTYERTLVVDGesaTIILLDMWENKGENEW--LHDHCMQVGDAYLIVYS 143
Cdd:cd04130     4 VLVGDGAVGKTSLivsytTNGYpteyvptAFDNFSVVVLVDG---KPVRLQLCDTAGQDEFdkLRPLCYPDTDVFLLCFS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 144 ITDRASFEKASELRIQLRRARQTEdIPIILVGNKSDLV----------RCREVSVSEGRACAV---VFDCKFIETSAAVQ 210
Cdd:cd04130    81 VVNPSSFQNISEKWIPEIRKHNPK-APIILVGTQADLRtdvnvliqlaRYGEKPVSQSRAKALaekIGACEYIECSALTQ 159

                  ....*...
gi 1907154220 211 HNVKELFE 218
Cdd:cd04130   160 KNLKEVFD 167
RJL cd04119
Rab GTPase family J-like (RabJ-like); RJLs are found in many protists and as chimeras with ...
76-224 1.69e-14

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 [Multi-domain]  Cd Length: 168  Bit Score: 69.69  E-value: 1.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTLANIFAE----DTYERTLVVD-GESATI-----ILLDMWENKGE-------NEWLHDhcmqvGDAY 138
Cdd:cd04119     2 KVISMGNSGVGKSCIIKRYCEgrfvSKYLPTIGIDyGVKKVSvrnkeVRVNFFDLSGHpeylevrNEFYKD-----TQGV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 139 LIVYSITDRASFEKAS----ELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVK 214
Cdd:cd04119    77 LLVYDVTDRQSFEALDswlkEMKQEGGPHGNMENIVVVVCANKIDLTKHRAVSEDEGRLWAESKGFKYFETSACTGEGVN 156
                         170
                  ....*....|
gi 1907154220 215 ELFEGIVRQV 224
Cdd:cd04119   157 EMFQTLFSSI 166
Rab7 cd01862
Rab GTPase family 7 (Rab7); Rab7 subfamily. Rab7 is a small Rab GTPase that regulates ...
75-222 3.14e-14

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


Pssm-ID: 206655 [Multi-domain]  Cd Length: 172  Bit Score: 68.85  E-value: 3.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFAEDTYE-------------RTLVVDGESATiilLDMWENKGenewlHDHCMQVG------ 135
Cdd:cd01862     1 LKVIILGDSGVGKTSLMNQYVNKKFSnqykatigadfltKEVTVDDRLVT---LQIWDTAG-----QERFQSLGvafyrg 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 136 -DAYLIVYSITDRASFEKAS----ELRIQLRrARQTEDIPIILVGNKSDLVRCREVSVSEGRA-CAVVFDCKFIETSAAV 209
Cdd:cd01862    73 aDCCVLVYDVTNPKSFESLDswrdEFLIQAS-PRDPENFPFVVLGNKIDLEEKRQVSTKKAQQwCKSKGNIPYFETSAKE 151
                         170
                  ....*....|...
gi 1907154220 210 QHNVKELFEGIVR 222
Cdd:cd01862   152 AINVDQAFETIAR 164
RHO smart00174
Rho (Ras homology) subfamily of Ras-like small GTPases; Members of this subfamily of Ras-like ...
77-224 3.70e-14

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 [Multi-domain]  Cd Length: 174  Bit Score: 68.79  E-value: 3.70e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220   77 VVLIGEQGVGKSTLANIFAEDT------------YERTLVVDGEsatIILLDMWENKGENEW--LHDHCMQVGDAYLIVY 142
Cdd:smart00174   1 LVVVGDGAVGKTCLLIVYTTNAfpedyvptvfenYSADVEVDGK---PVELGLWDTAGQEDYdrLRPLSYPDTDVFLICF 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  143 SITDRASFEKAS-----ELRiqlrraRQTEDIPIILVGNKSDL----------VRCREVSVSEGRACAVVFD---CKFIE 204
Cdd:smart00174  78 SVDSPASFENVKekwypEVK------HFCPNVPIILVGTKLDLrndkstleelSKKKQEPVTYEQGQALAKRigaVKYLE 151
                          170       180
                   ....*....|....*....|
gi 1907154220  205 TSAAVQHNVKELFEGIVRQV 224
Cdd:smart00174 152 CSALTQEGVREVFEEAIRAA 171
Rhes_like cd04143
Ras homolog enriched in striatum (Rhes) and activator of G-protein signaling 1 (Dexras1/AGS1); ...
75-218 4.18e-14

Ras homolog enriched in striatum (Rhes) and activator of G-protein signaling 1 (Dexras1/AGS1); This subfamily includes Rhes (Ras homolog enriched in striatum) and Dexras1/AGS1 (activator of G-protein signaling 1). These proteins are homologous, but exhibit significant differences in tissue distribution and subcellular localization. Rhes is found primarily in the striatum of the brain, but is also expressed in other areas of the brain, such as the cerebral cortex, hippocampus, inferior colliculus, and cerebellum. Rhes expression is controlled by thyroid hormones. In rat PC12 cells, Rhes is farnesylated and localizes to the plasma membrane. Rhes binds and activates PI3K, and plays a role in coupling serpentine membrane receptors with heterotrimeric G-protein signaling. Rhes has recently been shown to be reduced under conditions of dopamine supersensitivity and may play a role in determining dopamine receptor sensitivity. Dexras1/AGS1 is a dexamethasone-induced Ras protein that is expressed primarily in the brain, with low expression levels in other tissues. Dexras1 localizes primarily to the cytoplasm, and is a critical regulator of the circadian master clock to photic and nonphotic input. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins.


Pssm-ID: 133343 [Multi-domain]  Cd Length: 247  Bit Score: 70.16  E-value: 4.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFA----EDTYERTL--------VVDGEsatIILLDMWENKGENEW--LHDHCMQVGDAYLI 140
Cdd:cd04143     1 YRMVVLGASKVGKTAIVSRFLggrfEEQYTPTIedfhrklySIRGE---VYQLDILDTSGNHPFpaMRRLSILTGDVFIL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 141 VYSITDRASFEKASELRIQ--------LRRARQTEDIPIILVGNKSDLVRCREVSVSEGRAC-AVVFDCKFIETSAAVQH 211
Cdd:cd04143    78 VFSLDNRESFEEVCRLREQiletksclKNKTKENVKIPMVICGNKADRDFPREVQRDEVEQLvGGDENCAYFEVSAKKNS 157

                  ....*..
gi 1907154220 212 NVKELFE 218
Cdd:cd04143   158 NLDEMFR 164
PLN03108 PLN03108
Rab family protein; Provisional
75-217 1.23e-13

Rab family protein; Provisional


Pssm-ID: 178655 [Multi-domain]  Cd Length: 210  Bit Score: 68.04  E-value: 1.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFAEDTYE-------------RTLVVDGESatiILLDMWENKGENEWlhdhcMQVGDAY--- 138
Cdd:PLN03108    7 FKYIIIGDTGVGKSCLLLQFTDKRFQpvhdltigvefgaRMITIDNKP---IKLQIWDTAGQESF-----RSITRSYyrg 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 139 ----LIVYSITDRASFekaSELRIQLRRARQ--TEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHN 212
Cdd:PLN03108   79 aagaLLVYDITRRETF---NHLASWLEDARQhaNANMTIMLIGNKCDLAHRRAVSTEEGEQFAKEHGLIFMEASAKTAQN 155

                  ....*
gi 1907154220 213 VKELF 217
Cdd:PLN03108  156 VEEAF 160
PTZ00099 PTZ00099
rab6; Provisional
96-224 2.16e-13

rab6; Provisional


Pssm-ID: 185444 [Multi-domain]  Cd Length: 176  Bit Score: 66.69  E-value: 2.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  96 EDTYERTLVVDGESATIIL------LDMWENKGENEW--LHDHCMQVGDAYLIVYSITDRASFEKASELrIQLRRARQTE 167
Cdd:PTZ00099    6 DNNYQSTIGIDFLSKTLYLdegpvrLQLWDTAGQERFrsLIPSYIRDSAAAIVVYDITNRQSFENTTKW-IQDILNERGK 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907154220 168 DIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEGIVRQV 224
Cdd:PTZ00099   85 DVIIALVGNKTDLGDLRKVTYEEGMQKAQEYNTMFHETSAKAGHNIKVLFKKIAAKL 141
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
76-232 2.89e-13

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 66.54  E-value: 2.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTLAN-----IFAEDTYERT---------LVVDGESATIILLDMwenKGENE----------WLHDHc 131
Cdd:COG1100     5 KIVVVGTGGVGKTSLVNrlvgdIFSLEKYLSTngvtidkkeLKLDGLDVDLVIWDT---PGQDEfretrqfyarQLTGA- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 132 mqvgDAYLIVYSITDRASFEKASELRIQLRRARqtEDIPIILVGNKSDLVRCREVsVSEGRACAVVFDCKF---IETSAA 208
Cdd:COG1100    81 ----SLYLFVVDGTREETLQSLYELLESLRRLG--KKSPIILVLNKIDLYDEEEI-EDEERLKEALSEDNIvevVATSAK 153
                         170       180
                  ....*....|....*....|....
gi 1907154220 209 VQHNVKELFEGIVRQVRLRRDSKE 232
Cdd:COG1100   154 TGEGVEELFAALAEILRGEGDSLD 177
Rab4 cd04113
Rab GTPase family 4 (Rab4); Rab4 subfamily. Rab4 has been implicated in numerous functions ...
75-224 4.38e-13

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 [Multi-domain]  Cd Length: 161  Bit Score: 65.53  E-value: 4.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFAEDTYE-------------RTLVVDGESatiILLDMWENKGENEWlhdhcMQVGDAY--- 138
Cdd:cd04113     1 FKFLIIGSAGTGKSCLLHQFIENKFKqdsnhtigvefgsRVVNVGGKS---VKLQIWDTAGQERF-----RSVTRSYyrg 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 139 ----LIVYSITDRASFEKASELrIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVK 214
Cdd:cd04113    73 aagaLLVYDITSRESFNALTNW-LTDARTLASPDIVIILVGNKKDLEDDREVTFLEASRFAQENGLLFLETSALTGENVE 151
                         170
                  ....*....|
gi 1907154220 215 ELFEGIVRQV 224
Cdd:cd04113   152 EAFLKCARSI 161
Rab23_like cd04106
Rab GTPase family 23 (Rab23)-like; Rab23-like subfamily. Rab23 is a member of the Rab family ...
76-218 6.64e-13

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


Pssm-ID: 133306 [Multi-domain]  Cd Length: 162  Bit Score: 65.16  E-value: 6.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTL-----ANIFAEDtYERTLVVD--------GESATIILLDMWENKGENEW--LHDHCMQVGDAYLI 140
Cdd:cd04106     2 KVIVVGNGNVGKSSMiqrfvKGIFTKD-YKKTIGVDflekqiflRQSDEDVRLMLWDTAGQEEFdaITKAYYRGAQACIL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907154220 141 VYSITDRASFEKASELRiqlRRA-RQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFE 218
Cdd:cd04106    81 VFSTTDRESFEAIESWK---EKVeAECGDIPMVLVQTKIDLLDQAVITNEEAEALAKRLQLPLFRTSVKDDFNVTELFE 156
Rab19 cd01864
Rab GTPase family 19 (Rab19); Rab19 subfamily. Rab19 proteins are associated with Golgi stacks. ...
75-224 2.31e-12

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 [Multi-domain]  Cd Length: 165  Bit Score: 63.61  E-value: 2.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFAEDTYE-------------RTLVVDGESatiILLDMWENKGENEW--LHDHCMQVGDAYL 139
Cdd:cd01864     4 FKIILIGDSNVGKTCVVQRFKSGTFSerqgntigvdftmKTLEIQGKR---VKLQIWDTAGQERFrtITQSYYRSANGAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 140 IVYSITDRASFEKASELrIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKF-IETSAAVQHNVKELFE 218
Cdd:cd01864    81 IAYDITRRSSFESVPHW-IEEVEKYGASNVVLLLIGNKCDLEEQREVLFEEACTLAEHYGILAvLETSAKESSNVEEAFL 159

                  ....*.
gi 1907154220 219 GIVRQV 224
Cdd:cd01864   160 LMATEL 165
Rab33B_Rab33A cd04115
Rab GTPase family 33 includes Rab33A and Rab33B; Rab33B/Rab33A subfamily. Rab33B is ...
75-207 5.67e-12

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


Pssm-ID: 133315 [Multi-domain]  Cd Length: 170  Bit Score: 62.84  E-value: 5.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTL-----ANIFAE--------DTYERTLVVDGESatiILLDMWENKGENEWLH---DHCMQVGDAY 138
Cdd:cd04115     3 FKIIVIGDSNVGKTCLtyrfcAGRFPErteatigvDFRERTVEIDGER---IKVQLWDTAGQERFRKsmvQHYYRNVHAV 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907154220 139 LIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSA 207
Cdd:cd04115    80 VFVYDVTNMASFHSLPSWIEECEQHSLPNEVPRILVGNKCDLREQIQVPTDLAQRFADAHSMPLFETSA 148
Rab30 cd04114
Rab GTPase family 30 (Rab30); Rab30 subfamily. Rab30 appears to be associated with the Golgi ...
75-220 6.11e-12

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 [Multi-domain]  Cd Length: 169  Bit Score: 62.61  E-value: 6.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFAEDtyertLVVDGESATI---------------ILLDMWENKGENEW--LHDHCMQVGDA 137
Cdd:cd04114     8 FKIVLIGNAGVGKTCLVRRFTQG-----LFPPGQGATIgvdfmiktveikgekIKLQIWDTAGQERFrsITQSYYRSANA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 138 YLIVYSITDRASFEKASELriqLRRARQ--TEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKE 215
Cdd:cd04114    83 LILTYDITCEESFRCLPEW---LREIEQyaNNKVITILVGNKIDLAERREVSQQRAEEFSDAQDMYYLETSAKESDNVEK 159

                  ....*
gi 1907154220 216 LFEGI 220
Cdd:cd04114   160 LFLDL 164
Rab3 cd01865
Rab GTPase family 3 contains Rab3A, Rab3B, Rab3C and Rab3D; The Rab3 subfamily contains Rab3A, ...
75-221 9.49e-12

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 [Multi-domain]  Cd Length: 165  Bit Score: 61.85  E-value: 9.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFAEDTYERTLV----VDGESATI------ILLDMWENKGENEW--LHDHCMQVGDAYLIVY 142
Cdd:cd01865     2 FKLLIIGNSSVGKTSFLFRYADDSFTSAFVstvgIDFKVKTVyrndkrIKLQIWDTAGQERYrtITTAYYRGAMGFILMY 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907154220 143 SITDRASFEKASELRIQLRrARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEGIV 221
Cdd:cd01865    82 DITNEESFNAVQDWSTQIK-TYSWDNAQVILVGNKCDMEDERVVSAERGRQLADQLGFEFFEASAKENINVKQVFERLV 159
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
76-179 1.13e-11

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


Pssm-ID: 462490 [Multi-domain]  Cd Length: 114  Bit Score: 60.21  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTLANIFAEDTYE-------------RTLVVDGESATIILLDMWENKGENEW--LHDHCMQVGDAYLI 140
Cdd:pfam08477   1 KVVLLGDSGVGKTSLLKRFVDDTFDpkykstigvdfktKTVLENDDNGKKIKLNIWDTAGQERFrsLHPFYYRGAAAALL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907154220 141 VYsitDRASFEKaseLRIQLRRARQ-TEDIPIILVGNKSD 179
Cdd:pfam08477  81 VY---DSRTFSN---LKYWLRELKKyAGNSPVILVGNKID 114
Rab14 cd04122
Rab GTPase family 14 (Rab14); Rab14 GTPases are localized to biosynthetic compartments, ...
75-224 1.46e-11

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 [Multi-domain]  Cd Length: 166  Bit Score: 61.39  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFAEDTY-------------ERTLVVDGESatiILLDMWENKGENEWlhdhcMQVGDAY--- 138
Cdd:cd04122     3 FKYIIIGDMGVGKSCLLHQFTEKKFmadcphtigvefgTRIIEVNGQK---IKLQIWDTAGQERF-----RAVTRSYyrg 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 139 ----LIVYSITDRASFEKASELrIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVK 214
Cdd:cd04122    75 aagaLMVYDITRRSTYNHLSSW-LTDARNLTNPNTVIFLIGNKADLEAQRDVTYEEAKQFADENGLLFLECSAKTGENVE 153
                         170
                  ....*....|
gi 1907154220 215 ELFEGIVRQV 224
Cdd:cd04122   154 DAFLETAKKI 163
Rab27A cd04127
Rab GTPase family 27a (Rab27a); The Rab27a subfamily consists of Rab27a and its highly ...
80-227 2.81e-11

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 [Multi-domain]  Cd Length: 180  Bit Score: 60.98  E-value: 2.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  80 IGEQGVGKSTLA-----NIFAE--------DTYERTLVVDGES-------ATIILLDMWENKGENEWLHDHCMQVGDA-- 137
Cdd:cd04127    10 LGDSGVGKTTFLyrytdNKFNPkfittvgiDFREKRVVYNSQGpdgtsgkAFRVHLQLWDTAGQERFRSLTTAFFRDAmg 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 138 YLIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELF 217
Cdd:cd04127    90 FLLMFDLTSEQSFLNVRNWMSQLQAHAYCENPDIVLIGNKADLPDQREVSERQARELADKYGIPYFETSAATGQNVEKAV 169
                         170
                  ....*....|
gi 1907154220 218 EGIVRQVRLR 227
Cdd:cd04127   170 ETLLDLIMKR 179
Rab12 cd04120
Rab GTPase family 12 (Rab12); Rab12 was first identified in canine cells, where it was ...
76-248 3.77e-11

Rab GTPase family 12 (Rab12); Rab12 was first identified in canine cells, where it was localized to the Golgi complex. The specific function of Rab12 remains unknown, and inconsistent results about its cellular localization have been reported. More recent studies have identified Rab12 associated with post-Golgi vesicles, or with other small vesicle-like structures but not with the Golgi complex. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins.


Pssm-ID: 206699 [Multi-domain]  Cd Length: 202  Bit Score: 61.18  E-value: 3.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTLANIFAEDTY----ERTLVVDGESATI------ILLDMWENKGENEWlhdhcMQVGDAY------- 138
Cdd:cd04120     2 QVIIIGSRGVGKTSLMERFTDDTFceacKSTVGVDFKIKTVelrgkkIRLQIWDTAGQERF-----NSITSAYyrsakgi 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 139 LIVYSITDRASFEKASELrIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEG-RACAVVFDCKFIETSAAVQHNVKELF 217
Cdd:cd04120    77 ILVYDITKKETFDDLPKW-MKMIDKYASEDAELLLVGNKLDCETDREITRQQGeKFAQQITGMRFCEASAKDNFNVDEIF 155
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907154220 218 ----EGIVRQVRLRRDSKEKNERRLAYQKRRESIP 248
Cdd:cd04120   156 lklvDDILKKMPLDILRNELSNSILSLQPEPEIPP 190
Centaurin_gamma cd04103
Centaurin gamma (CENTG) GTPase; The centaurins (alpha, beta, gamma, and delta) are large, ...
76-224 6.28e-11

Centaurin gamma (CENTG) GTPase; The centaurins (alpha, beta, gamma, and delta) are large, multi-domain proteins that all contain an ArfGAP domain and ankyrin repeats, and in some cases, numerous additional domains. Centaurin gamma contains an additional GTPase domain near its N-terminus. The specific function of this GTPase domain has not been well characterized, but centaurin gamma 2 (CENTG2) may play a role in the development of autism. Centaurin gamma 1 is also called PIKE (phosphatidyl inositol (PI) 3-kinase enhancer) and centaurin gamma 2 is also known as AGAP (ArfGAP protein with a GTPase-like domain, ankyrin repeats and a Pleckstrin homology domain) or GGAP. Three isoforms of PIKE have been identified. PIKE-S (short) and PIKE-L (long) are brain-specific isoforms, with PIKE-S restricted to the nucleus and PIKE-L found in multiple cellular compartments. A third isoform, PIKE-A was identified in human glioblastoma brain cancers and has been found in various tissues. GGAP has been shown to have high GTPase activity due to a direct intramolecular interaction between the N-terminal GTPase domain and the C-terminal ArfGAP domain. In human tissue, AGAP mRNA was detected in skeletal muscle, kidney, placenta, brain, heart, colon, and lung. Reduced expression levels were also observed in the spleen, liver, and small intestine.


Pssm-ID: 133303  Cd Length: 158  Bit Score: 59.43  E-value: 6.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTLANIFAEDTY-----------ERTLVVDGESATIILLDmwenkgENEWLHDHCMQVGDAYLIVYSI 144
Cdd:cd04103     2 KLGIVGNLRSGKSALVHRYLTGSYvqlespeggrfKKEVLVDGQSHLLLIRD------EGGAPDAQFAGWVDAVIFVFSL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 145 TDRASFEKASELRIQLRRARQTEDIPIILVGNKSDL--VRCREVSVSEGRA-CAVVFDCKFIETSAAVQHNVKELFEGIV 221
Cdd:cd04103    76 EDEASFQTVYRLYHQLSSYRNISEIPLILVGTQDAIsaSNPRVIDDARARQlCADMKRCSYYETCATYGLNVERVFQEAA 155

                  ...
gi 1907154220 222 RQV 224
Cdd:cd04103   156 QKI 158
Rab15 cd04117
Rab GTPase family 15 (Rab15); Rab15 colocalizes with the transferrin receptor in early ...
75-227 7.72e-11

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 [Multi-domain]  Cd Length: 164  Bit Score: 59.61  E-value: 7.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFAEDTYE----RTLVVDGESATI------ILLDMWENKGENEW--LHDHCMQVGDAYLIVY 142
Cdd:cd04117     1 FRLLLIGDSGVGKTCLLCRFTDNEFHsshiSTIGVDFKMKTIevdgikVRIQIWDTAGQERYqtITKQYYRRAQGIFLVY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 143 SITDRASFEK----ASELRiqlrrARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFE 218
Cdd:cd04117    81 DISSERSYQHimkwVSDVD-----EYAPEGVQKILIGNKADEEQKRQVGDEQGNKLAKEYGMDFFETSACTNKNIKESFT 155

                  ....*....
gi 1907154220 219 GIvRQVRLR 227
Cdd:cd04117   156 RL-TELVLQ 163
Rab28 cd04109
Rab GTPase family 28 (Rab28); Rab28 subfamily. First identified in maize, Rab28 has been shown ...
75-224 8.47e-11

Rab GTPase family 28 (Rab28); Rab28 subfamily. First identified in maize, Rab28 has been shown to be a late embryogenesis-abundant (Lea) protein that is regulated by the plant hormone abcisic acid (ABA). In Arabidopsis, Rab28 is expressed during embryo development and is generally restricted to provascular tissues in mature embryos. Unlike maize Rab28, it is not ABA-inducible. Characterization of the human Rab28 homolog revealed two isoforms, which differ by a 95-base pair insertion, producing an alternative sequence for the 30 amino acids at the C-terminus. The two human isoforms are presumably the result of alternative splicing. Since they differ at the C-terminus but not in the GTP-binding region, they are predicted to be targeted to different cellular locations. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins.


Pssm-ID: 206694 [Multi-domain]  Cd Length: 213  Bit Score: 60.20  E-value: 8.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFAEDT----YERTLVVDGESATI-------ILLDMWENKGEN---EWLhDHCMQVGDAYLI 140
Cdd:cd04109     1 IKIVVLGDGASGKTSLIRRFAQEGfgksYKQTIGLDFFSRRItlpgslnVTLQVWDIGGQQiggKML-DKYIYGAQAVCL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 141 VYSITDRASFEKASELRIQLRRARQTEDIP--IILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFE 218
Cdd:cd04109    80 VYDITNSQSFENLEDWLSVVKKVNEESETKpkMVLVGNKTDLEHNRQVTAEKHARFAQENDMESIFVSAKTGDRVFLCFQ 159

                  ....*.
gi 1907154220 219 GIVRQV 224
Cdd:cd04109   160 RIAAEL 165
Rab26 cd04112
Rab GTPase family 26 (Rab26); Rab26 subfamily. First identified in rat pancreatic acinar cells, ...
75-227 1.74e-10

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 [Multi-domain]  Cd Length: 191  Bit Score: 59.11  E-value: 1.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFAEDTY--------------ERTLVVDGesaTIILLDMWENKGENEWlhdhcMQVGDAY-- 138
Cdd:cd04112     1 FKVMLVGDSGVGKTCLLVRFKDGAFlagsfiatvgiqftNKVVTVDG---VKVKLQIWDTAGQERF-----RSVTHAYyr 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 139 -----LIVYSITDRASFEKASELRIQLRRARQtEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNV 213
Cdd:cd04112    73 dahalLLLYDVTNKSSFDNIRAWLTEILEYAQ-SDVVIMLLGNKADMSGERVVKREDGERLAKEYGVPFMETSAKTGLNV 151
                         170
                  ....*....|....
gi 1907154220 214 KELFEGIVRQVRLR 227
Cdd:cd04112   152 ELAFTAVAKELKHR 165
RRP22 cd04142
Ras-related protein on chromosome 22 (RRP22) family; RRP22 (Ras-related protein on chromosome ...
75-228 2.51e-10

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 [Multi-domain]  Cd Length: 198  Bit Score: 58.73  E-value: 2.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKST-----LANIFAE--------DTYERTLVVDGESATIILLDM-----WENKGENEWLHDHC--MQV 134
Cdd:cd04142     1 VRVAVLGAPGVGKTAivrqfLAQEFPEeyiptehrRLYRPAVVLSGRVYDLHILDVpnmqrYPGTAGQEWMDPRFrgLRN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 135 GDAYLIVYSITDRASFEKASELRIQLRRARQ--TEDIPIILVGNKSDLVRCRevsVSEGRACAVV----FDCKFIETSAA 208
Cdd:cd04142    81 SRAFILVYDICSPDSFHYVKLLRQQILETRPagNKEPPIVVVGNKRDQQRHR---FAPRHVLSVLvrksWKCGYLECSAK 157
                         170       180
                  ....*....|....*....|
gi 1907154220 209 VQHNVKELFEGIVRQVRLRR 228
Cdd:cd04142   158 YNWHILLLFKELLISATTRG 177
Rab35 cd04110
Rab GTPase family 35 (Rab35); Rab35 is one of several Rab proteins to be found to participate ...
75-237 2.67e-10

Rab GTPase family 35 (Rab35); Rab35 is one of several Rab proteins to be found to participate in the regulation of osteoclast cells in rats. In addition, Rab35 has been identified as a protein that interacts with nucleophosmin-anaplastic lymphoma kinase (NPM-ALK) in human cells. Overexpression of NPM-ALK is a key oncogenic event in some anaplastic large-cell lymphomas; since Rab35 interacts with N|PM-ALK, it may provide a target for cancer treatments. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins.


Pssm-ID: 133310 [Multi-domain]  Cd Length: 199  Bit Score: 58.71  E-value: 2.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLANIFAEDTYE-------------RTLVVDGESatiILLDMWENKGENEWlhdhcMQVGDAY--- 138
Cdd:cd04110     7 FKLLIIGDSGVGKSSLLLRFADNTFSgsyittigvdfkiRTVEINGER---VKLQIWDTAGQERF-----RTITSTYyrg 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 139 ----LIVYSITDRASFekaSELRIQLRRARQT-EDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNV 213
Cdd:cd04110    79 thgvIVVYDVTNGESF---VNVKRWLQEIEQNcDDVCKVLVGNKNDDPERKVVETEDAYKFAGQMGISLFETSAKENINV 155
                         170       180
                  ....*....|....*....|....
gi 1907154220 214 KELFEGIVRQVRLRRDSKEKNERR 237
Cdd:cd04110   156 EEMFNCITELVLRAKKDNLAKQQQ 179
Rho4_like cd04132
Ras homology family 4 (Rho4) of small guanosine triphosphatases (GTPases)-like; Rho4 is a ...
76-237 5.68e-10

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


Pssm-ID: 206704 [Multi-domain]  Cd Length: 197  Bit Score: 57.74  E-value: 5.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTLANIFAEDT----YERTLV------VDGESATIILLDMWENKGENEW--LHDHCMQVGDAYLIVYS 143
Cdd:cd04132     5 KIVVVGDGGCGKTCLLMVYAQGSfpeeYVPTVFenyvttLQVPNGKIIELALWDTAGQEDYdrLRPLSYPDVDVILICYS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 144 ITDRASFEKaselrIQLRRARQT----EDIPIILVGNKSDLVRCRE------------VSVSEG-RACAVVFDCKFIETS 206
Cdd:cd04132    85 VDNPTSLDN-----VEDKWYPEVnhfcPGTPIVLVGLKTDLRKDKNsvsklraqglepVTPEQGeSVAKSIGAVAYIECS 159
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1907154220 207 AAVQHNVKELFEGIVRQVrLRRDSKEKNERR 237
Cdd:cd04132   160 AKLMENVDEVFDAAINVA-LSKSGRAARKKK 189
Rac1_like cd01871
Ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1)-like ...
76-224 5.81e-10

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 [Multi-domain]  Cd Length: 174  Bit Score: 57.13  E-value: 5.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTL-----ANIFAE-------DTYERTLVVDGESatiILLDMWENKGENEW--LHDHCMQVGDAYLIV 141
Cdd:cd01871     3 KCVVVGDGAVGKTCLlisytTNAFPGeyiptvfDNYSANVMVDGKP---VNLGLWDTAGQEDYdrLRPLSYPQTDVFLIC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 142 YSITDRASFEKASElRIQLRRARQTEDIPIILVGNKSDL-------VRCRE-----VSVSEGRACAV-VFDCKFIETSAA 208
Cdd:cd01871    80 FSLVSPASFENVRA-KWYPEVRHHCPNTPIILVGTKLDLrddkdtiEKLKEkkltpITYPQGLAMAKeIGAVKYLECSAL 158
                         170
                  ....*....|....*.
gi 1907154220 209 VQHNVKELFEGIVRQV 224
Cdd:cd01871   159 TQRGLKTVFDEAIRAV 174
RabL2 cd04124
Rab GTPase-like family 2 (Rab-like2); RabL2 (Rab-like2) subfamily. RabL2s are novel Rab ...
76-222 4.33e-09

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 [Multi-domain]  Cd Length: 161  Bit Score: 54.48  E-value: 4.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTLANIFAED--------TYERTL-----VVDGESatiILLDMWENKGENEW--LHDHCMQVGDAYLI 140
Cdd:cd04124     2 KIILLGDSAVGKSKLVERFLMDgyepqqlsTYALTLykhnaKFEGKT---ILVDFWDTAGQERFqtMHASYYHKAHACIL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 141 VYSITDRASFEKASELRIQLRRARqtEDIPIILVGNKSDLvrcrEVSVSE-GRACAVVFDCKFIETSAAVQHNVKELFEG 219
Cdd:cd04124    79 VFDVTRKITYKNLSKWYEELREYR--PEIPCIVVANKIDL----DPSVTQkKFNFAEKHNLPLYYVSAADGTNVVKLFQD 152

                  ...
gi 1907154220 220 IVR 222
Cdd:cd04124   153 AIK 155
RhoG cd01875
Ras homolog family, member G (RhoG) of small guanosine triphosphatases (GTPases); RhoG is a ...
76-224 6.61e-09

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 [Multi-domain]  Cd Length: 191  Bit Score: 54.63  E-value: 6.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTL-----ANIFAE-------DTYERTLVVDGESATiilLDMWENKGENEW--LHDHCMQVGDAYLIV 141
Cdd:cd01875     5 KCVVVGDGAVGKTCLlicytTNAFPKeyiptvfDNYSAQTAVDGRTVS---LNLWDTAGQEEYdrLRTLSYPQTNVFIIC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 142 YSITDRASFEKASElRIQLRRARQTEDIPIILVGNKSDL-------VRCREVSVS-----EGRACA-VVFDCKFIETSAA 208
Cdd:cd01875    82 FSIASPSSYENVRH-KWHPEVCHHCPNVPILLVGTKKDLrndadtlKKLKEQGQApitpqQGGALAkQIHAVKYLECSAL 160
                         170
                  ....*....|....*.
gi 1907154220 209 VQHNVKELFEGIVRQV 224
Cdd:cd01875   161 NQDGVKEVFAEAVRAV 176
Rab40 cd04121
Rab GTPase family 40 (Rab40) contains Rab40a, Rab40b and Rab40c; The Rab40 subfamily contains ...
76-227 8.05e-09

Rab GTPase family 40 (Rab40) contains Rab40a, Rab40b and Rab40c; The Rab40 subfamily contains Rab40a, Rab40b, and Rab40c, which are all highly homologous. In rat, Rab40c is localized to the perinuclear recycling compartment (PRC), and is distributed in a tissue-specific manor, with high expression in brain, heart, kidney, and testis, low expression in lung and liver, and no expression in spleen and skeletal muscle. Rab40c is highly expressed in differentiated oligodendrocytes but minimally expressed in oligodendrocyte progenitors, suggesting a role in the vesicular transport of myelin components. Unlike most other Ras-superfamily proteins, Rab40c was shown to have a much lower affinity for GTP, and an affinity for GDP that is lower than for GTP. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins.


Pssm-ID: 133321 [Multi-domain]  Cd Length: 189  Bit Score: 54.17  E-value: 8.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGK----STLANIFAEDTYERTLVVDGESATIIL------LDMWENKGENEW--LHDHCMQVGDAYLIVYS 143
Cdd:cd04121     8 KFLLVGDSDVGKgeilASLQDGSTESPYGYNMGIDYKTTTILLdgrrvkLQLWDTSGQGRFctIFRSYSRGAQGIILVYD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 144 ITDRASFEKASelriqlRRARQTED----IPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEG 219
Cdd:cd04121    88 ITNRWSFDGID------RWIKEIDEhapgVPKILVGNRLHLAFKRQVATEQAQAYAERNGMTFFEVSPLCNFNITESFTE 161

                  ....*...
gi 1907154220 220 IVRQVRLR 227
Cdd:cd04121   162 LARIVLMR 169
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
74-222 1.77e-08

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


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 52.76  E-value: 1.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  74 YYRVVLIGEQGVGKSTLANIFA-------------EDTYERTLV-VDGESATIILLDMwenKGENEW--LHDHCMQVGDA 137
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLgnkgsiteyypgtTRNYVTTVIeEDGKTYKFNLLDT---AGQEDYdaIRRLYYPQVER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 138 YLIVYSITDRA-SFEKASEL-RIQLRRARqTEDIPIILVGNKSDLvRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKE 215
Cdd:TIGR00231  78 SLRVFDIVILVlDVEEILEKqTKEIIHHA-DSGVPIILVGNKIDL-KDADLKTHVASEFAKLNGEPIIPLSAETGKNIDS 155

                  ....*..
gi 1907154220 216 LFEGIVR 222
Cdd:TIGR00231 156 AFKIVEA 162
Rab32_Rab38 cd04107
Rab GTPase families 18 (Rab18) and 32 (Rab32); Rab38/Rab32 subfamily. Rab32 and Rab38 are ...
75-224 7.37e-08

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


Pssm-ID: 206692 [Multi-domain]  Cd Length: 201  Bit Score: 51.54  E-value: 7.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKSTLA-----NIFAEDtYERTLVVD-------GESATIILLDMWENKGenewlHDHCMQVGDAY---- 138
Cdd:cd04107     1 FKVLVIGDLGVGKTSIIkryvhGVFSQH-YKATIGVDfalkvieWDPNTVVRLQLWDIAG-----QERFGGMTRVYykga 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 139 ---LIVYSITDRASFEKASELRIQLRRARQTED---IPIILVGNKSDLVRCREvSVSEGRACAVVFDCKFI---ETSAAV 209
Cdd:cd04107    75 vgaIIVFDVTRPSTFEAVLKWKADLDSKVTLPNgepIPALLLANKCDLKKERL-AKDPEQMDQFCKENGFIgwfETSAKE 153
                         170
                  ....*....|....*
gi 1907154220 210 QHNVKELFEGIVRQV 224
Cdd:cd04107   154 NINIEEAMRFLVKNI 168
Rop_like cd04133
Rho-related protein from plants (Rop)-like; The Rop (Rho-related protein from plants) ...
78-225 1.02e-07

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 [Multi-domain]  Cd Length: 173  Bit Score: 50.62  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  78 VLIGEQGVGKSTL-----ANIFAED-------TYERTLVVDGesaTIILLDMWENKGENEW--LHDHCMQVGDAYLIVYS 143
Cdd:cd04133     5 VTVGDGAVGKTCMlisytSNTFPTDyvptvfdNFSANVVVDG---NTVNLGLWDTAGQEDYnrLRPLSYRGADVFLLAFS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 144 ITDRASFEKASELRI-QLRRArqTEDIPIILVGNKSDLVRCRE--------VSVSEGRACAVVFD---CKFIETSAAVQH 211
Cdd:cd04133    82 LISKASYENVLKKWIpELRHY--APGVPIVLVGTKLDLRDDKQffadhpgaVPITTAQGEELRKQigaAAYIECSSKTQQ 159
                         170
                  ....*....|....
gi 1907154220 212 NVKELFEGIVRQVR 225
Cdd:cd04133   160 NVKAVFDAAIKVVL 173
Rab24 cd04118
Rab GTPase family 24 (Rab24); Rab24 is distinct from other Rabs in several ways. It exists ...
76-220 2.19e-07

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 [Multi-domain]  Cd Length: 193  Bit Score: 50.25  E-value: 2.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTLA-----NIFAEDTYERTL--------VVDGEsaTIILLDMWENKGENEWlhdHCMQV-----GDA 137
Cdd:cd04118     2 KVVMLGKESVGKTSLVeryvhHRFLVGPYQNTIgaafvakrMVVGE--RVVTLGIWDTAGSERY---EAMSRiyyrgAKA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 138 YLIVYSITDRASFEKASELRIQLRRARqtEDIPIILVGNKSDLV----RCREVSVSEGRACAVVFDCKFIETSAAVQHNV 213
Cdd:cd04118    77 AIVCYDLTDSSSFERAKFWVKELQNLE--EHCKIYLCGTKSDLIeqdrSLRQVDFHDVQDFADEIKAQHFETSSKTGQNV 154

                  ....*..
gi 1907154220 214 KELFEGI 220
Cdd:cd04118   155 DELFQKV 161
Rho2 cd04129
Ras homology family 2 (Rho2) of small guanosine triphosphatases (GTPases); Rho2 is a fungal ...
76-234 6.04e-07

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


Pssm-ID: 206702 [Multi-domain]  Cd Length: 190  Bit Score: 48.68  E-value: 6.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTLANIFA----EDTYERTLV--------VDGESatiILLDMWENKGENEWLHDHCMQVGDAY--LIV 141
Cdd:cd04129     3 KLVIVGDGACGKTSLLYVFTlgefPEEYHPTVFenyvtdcrVDGKP---VQLALWDTAGQEEYERLRPLSYSKAHviLIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 142 YSITDRASFEKASELRIQLRRaRQTEDIPIILVGNKSDLvrcREVSVSEG--------------RACAVVFDCKFIETSA 207
Cdd:cd04129    80 FAIDTPDSLENVRTKWIEEVR-RYCPNVPVILVGLKKDL---RQEAVAKGnyatdefvpiqqakLVARAIGAKKYMECSA 155
                         170       180
                  ....*....|....*....|....*..
gi 1907154220 208 AVQHNVKELFEGIVRQVRLRRDSKEKN 234
Cdd:cd04129   156 LTGEGVDDVFEAATRAALLVRKSGKEE 182
RhoA_like cd01870
Ras homology family A (RhoA)-like includes RhoA, RhoB and RhoC; The RhoA subfamily consists of ...
76-218 2.31e-06

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 [Multi-domain]  Cd Length: 175  Bit Score: 46.65  E-value: 2.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTLANIFAED------------TYERTLVVDGESatiILLDMWENKGENEW--LHDHCMQVGDAYLIV 141
Cdd:cd01870     3 KLVIVGDGACGKTCLLIVFSKDqfpevyvptvfeNYVADIEVDGKQ---VELALWDTAGQEDYdrLRPLSYPDTDVILMC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 142 YSITDRASFEKASELRIQLRRaRQTEDIPIILVGNKSDL------------VRCREVSVSEGRACAVVFDC-KFIETSAA 208
Cdd:cd01870    80 FSIDSPDSLENIPEKWTPEVK-HFCPNVPIILVGNKKDLrndehtirelakMKQEPVKPEEGRAMAEKIGAfGYLECSAK 158
                         170
                  ....*....|
gi 1907154220 209 VQHNVKELFE 218
Cdd:cd01870   159 TKEGVREVFE 168
Ran cd00877
Ras-related nuclear proteins (Ran)/TC4 family of small GTPases; Ran GTPase is involved in ...
75-223 3.12e-06

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 [Multi-domain]  Cd Length: 166  Bit Score: 46.14  E-value: 3.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKST-----LANIFaEDTYERTLVVDGESATI------ILLDMWENKGENEW--LHDHCMQVGDAYLIV 141
Cdd:cd00877     1 FKLVLVGDGGTGKTTfvkrhLTGEF-EKKYVATLGVEVHPLDFhtnrgkIRFNVWDTAGQEKFggLRDGYYIQGQCAIIM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 142 YSITDRASFEKASELRIQLRRARqtEDIPIILVGNKSDlVRCREVsvsegRACAVVFD----CKFIETSAAVQHNVKELF 217
Cdd:cd00877    80 FDVTSRVTYKNVPNWHRDLVRVC--ENIPIVLCGNKVD-IKDRKV-----KPKQITFHrkknLQYYEISAKSNYNFEKPF 151

                  ....*.
gi 1907154220 218 EGIVRQ 223
Cdd:cd00877   152 LWLARK 157
RAN smart00176
Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases; Ran is involved in the ...
80-224 3.42e-06

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


Pssm-ID: 128473 [Multi-domain]  Cd Length: 200  Bit Score: 46.54  E-value: 3.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220   80 IGEQGVGKST-----LANIFaEDTYERTLVVDGESATI------ILLDMWENKGENEW--LHDHCMQVGDAYLIVYSITD 146
Cdd:smart00176   1 VGDGGTGKTTfvkrhLTGEF-EKKYVATLGVEVHPLVFhtnrgpIRFNVWDTAGQEKFggLRDGYYIQGQCAIIMFDVTA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  147 RASFEKASELRIQLrrARQTEDIPIILVGNKSDlVRCREVsvsegRACAVVF----DCKFIETSAAVQHNVKELFEGIVR 222
Cdd:smart00176  80 RVTYKNVPNWHRDL--VRVCENIPIVLCGNKVD-VKDRKV-----KAKSITFhrkkNLQYYDISAKSNYNFEKPFLWLAR 151

                   ..
gi 1907154220  223 QV 224
Cdd:smart00176 152 KL 153
Rnd cd04131
Rho family GTPase subfamily Rnd includes Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8; The Rnd ...
76-218 4.85e-06

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 [Multi-domain]  Cd Length: 176  Bit Score: 45.89  E-value: 4.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTLANIFAEDTYERTLV------------VDGESatiILLDMWENKGENEWlhDH----CMQVGDAYL 139
Cdd:cd04131     3 KIVLVGDSQCGKTALLQVFAKDSFPENYVptvfenytasfeVDKQR---IELSLWDTSGSPYY--DNvrplSYPDSDAVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 140 IVYSITDRASFEKASE-LRIQLRRArqTEDIPIILVGNKSDL------------VRCREVSVSEGRA-----CAVVfdck 201
Cdd:cd04131    78 ICFDISRPETLDSVLKkWKGEVREF--CPNTPVLLVGCKSDLrtdlstltelsnKRQIPVSHEQGRNlakqiGAAA---- 151
                         170
                  ....*....|....*...
gi 1907154220 202 FIETSAAVQHN-VKELFE 218
Cdd:cd04131   152 YVECSAKTSENsVRDVFE 169
PLN03071 PLN03071
GTP-binding nuclear protein Ran; Provisional
75-217 4.90e-06

GTP-binding nuclear protein Ran; Provisional


Pssm-ID: 178620 [Multi-domain]  Cd Length: 219  Bit Score: 46.28  E-value: 4.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKST-----LANIFaEDTYERTLVVDgesatIILLDMWENKGE---NEW----------LHDHCMQVGD 136
Cdd:PLN03071   14 FKLVIVGDGGTGKTTfvkrhLTGEF-EKKYEPTIGVE-----VHPLDFFTNCGKirfYCWdtagqekfggLRDGYYIHGQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 137 AYLIVYSITDRASFEKASELRIQLRRArqTEDIPIILVGNKSDlVRCREVsvsegRACAVVFDCK----FIETSAAVQHN 212
Cdd:PLN03071   88 CAIIMFDVTARLTYKNVPTWHRDLCRV--CENIPIVLCGNKVD-VKNRQV-----KAKQVTFHRKknlqYYEISAKSNYN 159

                  ....*
gi 1907154220 213 VKELF 217
Cdd:PLN03071  160 FEKPF 164
PTZ00132 PTZ00132
GTP-binding nuclear protein Ran; Provisional
75-186 5.47e-06

GTP-binding nuclear protein Ran; Provisional


Pssm-ID: 240284 [Multi-domain]  Cd Length: 215  Bit Score: 46.22  E-value: 5.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  75 YRVVLIGEQGVGKST-----LANIFaEDTYERTLVVDGESATI------ILLDMWENKGENEW--LHDHCMQVGDAYLIV 141
Cdd:PTZ00132   10 FKLILVGDGGVGKTTfvkrhLTGEF-EKKYIPTLGVEVHPLKFytncgpICFNVWDTAGQEKFggLRDGYYIKGQCAIIM 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907154220 142 YSITDRASFEKASELRIQLRRArqTEDIPIILVGNKSDlVRCREV 186
Cdd:PTZ00132   89 FDVTSRITYKNVPNWHRDIVRV--CENIPIVLVGNKVD-VKDRQV 130
Rab20 cd04126
Rab GTPase family 20 (Rab20); Rab20 is one of several Rab proteins that appear to be ...
76-252 1.49e-05

Rab GTPase family 20 (Rab20); Rab20 is one of several Rab proteins that appear to be restricted in expression to the apical domain of murine polarized epithelial cells. It is expressed on the apical side of polarized kidney tubule and intestinal epithelial cells, and in non-polarized cells. It also localizes to vesico-tubular structures below the apical brush border of renal proximal tubule cells and in the apical region of duodenal epithelial cells. Rab20 has also been shown to colocalize with vacuolar H+-ATPases (V-ATPases) in mouse kidney cells, suggesting a role in the regulation of V-ATPase traffic in specific portions of the nephron. It was also shown to be one of several proteins whose expression is upregulated in human myelodysplastic syndrome (MDS) patients. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins.


Pssm-ID: 133326 [Multi-domain]  Cd Length: 220  Bit Score: 44.90  E-value: 1.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTLANIFAEDTYERTLVVDGesATIIL-------LDMWENKGEnEWLHD----HCMQVGdAYLIVYSI 144
Cdd:cd04126     2 KVVLLGDMNVGKTSLLHRYMERRFKDTVSTVG--GAFYLkqwgpynISIWDTAGR-EQFHGlgsmYCRGAA-AVILTYDV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 145 TDRASFEKASELRIQLRRArQTEDIPIILVGNKSDLVRC-------------------REVSVSEGRACA------VVFD 199
Cdd:cd04126    78 SNVQSLEELEDRFLGLTDT-ANEDCLFAVVGNKLDLTEEgalagqekdagdrvspedqRQVTLEDAKAFYkrinkyKMLD 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907154220 200 CK--------FIETSAAVQHNVKELFEGIVRQVrLRRDSKEKNERRLAYQKRRESIPRKAR 252
Cdd:cd04126   157 EDlspaaekmCFETSAKTGYNVDELFEYLFNLV-LPLILAQRAEANRTQGTVNLPNPKRSK 216
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
78-224 2.01e-05

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 43.77  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  78 VLIGEQGVGKSTLAN------IFAEDTY-------ERTLVVDGESATIIL-----LDMWENKGE--NEWLHDHCMQVgDA 137
Cdd:cd00880     1 AIFGRPNVGKSSLLNallgqnVGIVSPIpgttrdpVRKEWELLPLGPVVLidtpgLDEEGGLGRerVEEARQVADRA-DL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 138 YLIVYSITDRASFEkasELRIQLRRARQtedIPIILVGNKSDLVRCREVSVSEGRAC-AVVFDCKFIETSAAVQHNVKEL 216
Cdd:cd00880    80 VLLVVDSDLTPVEE---EAKLGLLRERG---KPVLLVLNKIDLVPESEEEELLRERKlELLPDLPVIAVSALPGEGIDEL 153

                  ....*...
gi 1907154220 217 FEGIVRQV 224
Cdd:cd00880   154 RKKIAELL 161
Arl10_like cd04159
Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from ...
77-180 7.71e-05

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


Pssm-ID: 206724 [Multi-domain]  Cd Length: 159  Bit Score: 42.31  E-value: 7.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  77 VVLIGEQGVGKSTLANI-----FAEDTYE----RTLVVDGESATIILLD---------MWENkgenewlhdHCMQVgDAy 138
Cdd:cd04159     2 ITLVGLQNSGKTTLVNViasgqFSEDTIPtvgfNMRKVTKGNVTIKVWDlggqprfrsMWER---------YCRGV-NA- 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1907154220 139 lIVYSI--TDRASFEKASELRIQLRRARQTEDIPIILVGNKSDL 180
Cdd:cd04159    71 -IVYVVdaADREKLEVAKNELHDLLEKPSLEGIPLLVLGNKNDL 113
Spg1 cd04128
Septum-promoting GTPase (Spg1); Spg1p. Spg1p (septum-promoting GTPase) was first identified in ...
76-224 8.14e-05

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 [Multi-domain]  Cd Length: 182  Bit Score: 42.38  E-value: 8.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTLANIFAEDTY-------------ERTLVVDGesaTIILLDMWENKGENEWLHDHCMQVGDAYLIVY 142
Cdd:cd04128     2 KIGLLGDAQIGKTSLMVKYVEGEFdeeyiqtlgvnfmEKTISIRG---TEITFSIWDLGGQREFINMLPLVCKDAVAILF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 143 --SITDRASFEKASELRIQLRRARQTEdIPiILVGNKSDLVR-----CREVSVSEGRACAVVFDCKFIETSAAVQHNVKE 215
Cdd:cd04128    79 mfDLTRKSTLNSIKEWYRQARGFNKTA-IP-ILVGTKYDLFAdlppeEQEEITKQARKYAKAMKAPLIFCSTSHSINVQK 156

                  ....*....
gi 1907154220 216 LFEGIVRQV 224
Cdd:cd04128   157 IFKFVLAKV 165
YeeP COG3596
Predicted GTPase [General function prediction only];
76-256 4.56e-04

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 40.90  E-value: 4.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTLAN-IFAEDTYErtlVVDGESAT---------------IILLDMW------ENKGENEWLHDhcmQ 133
Cdd:COG3596    41 VIALVGKTGAGKSSLINaLFGAEVAE---VGVGRPCTreiqryrlesdglpgLVLLDTPglgevnERDREYRELRE---L 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220 134 VGDAYLIVY--SITDRASfekASELRIQLRRARQTEDIPIILVGNKSDLVR-CRE-------------VSVSE------- 190
Cdd:COG3596   115 LPEADLILWvvKADDRAL---ATDEEFLQALRAQYPDPPVLVVLTQVDRLEpEREwdppynwpsppkeQNIRRaleaiae 191
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907154220 191 --GRACAVVFDckfieTSAA---VQHNVKELFEGIV------RQVRLRRDSKEKNERRLAYQKRRESIPRKARRFWG 256
Cdd:COG3596   192 qlGVPIDRVIP-----VSAAedrTGYGLEELVDALAealpeaKRSRLARLLRAKAIDRYTLLAAAAALLAAALLALL 263
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
76-177 6.16e-04

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 38.75  E-value: 6.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220  76 RVVLIGEQGVGKSTLAN-IFAE------------DTYERTLVVDGESatIILLD---MWENKGENEWLHDHCMQVGDAYL 139
Cdd:pfam01926   1 RVALVGRPNVGKSTLINaLTGAkaivsdypgttrDPNEGRLELKGKQ--IILVDtpgLIEGASEGEGLGRAFLAIIEADL 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907154220 140 IVYsITDRAsfEKASELRIQLRRARQTEDIPIILVGNK 177
Cdd:pfam01926  79 ILF-VVDSE--EGITPLDEELLELLRENKKPIILVLNK 113
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
77-174 1.20e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 38.51  E-value: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154220   77 VVLIGEQGVGKSTLANIFA---EDTYERTLVVDGESATIILLDMWENKGENEwlhdhcmqvgdaylivysitDRASFEKA 153
Cdd:smart00382   5 ILIVGPPGSGKTTLARALArelGPPGGGVIYIDGEDILEEVLDQLLLIIVGG--------------------KKASGSGE 64
                           90       100
                   ....*....|....*....|.
gi 1907154220  154 SELRIQLRRARQtEDIPIILV 174
Cdd:smart00382  65 LRLRLALALARK-LKPDVLIL 84
AAA_24 pfam13479
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
73-108 8.09e-03

AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.


Pssm-ID: 433243  Cd Length: 199  Bit Score: 36.54  E-value: 8.09e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907154220  73 TYYRVVLIGEQGVGKSTLANifaedTYERTLVVDGE 108
Cdd:pfam13479   1 KKLKILIYGPSGIGKTTFAK-----TLPKPLFLDTE 31
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
76-109 8.94e-03

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 36.09  E-value: 8.94e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907154220  76 RVVLIGEQGVGKSTLANIFA--EDTYERTLVVDGES 109
Cdd:pfam00005  13 ILALVGPNGAGKSTLLKLIAglLSPTEGTILLDGQD 48
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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