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Conserved domains on  [gi|160298187|ref|NP_034406|]
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GTP-binding protein GEM [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, ...
75-295 1.69e-143

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: 402.55  E-value: 1.69e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFAGvHDSMDSDCEVLGEDTYERTLVVDGESATIILLDMWENKGeNEWLHDHCMQVGDAYLI 154
Cdd:cd04148    1 YRVVLLGDSGVGKSSLANIFTA-GVYEDSAYEASGDDTYERTVSVDGEEATLVVYDHWEQED-GMWLEDSCMQVGDAYVI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 155 VYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEGI 234
Cdd:cd04148   79 VYSVTDRSSFEKASELRIQLRRARQAEDIPIILVGNKSDLVRSREVSVQEGRACAVVFDCKFIETSAALQHNVDELFEGI 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160298187 235 VRQVRLRRDSKEKNERRLAYQKRRESIPRKARRFWGKIVAKNNKNMAFKLKSKSCHDLSVL 295
Cdd:cd04148  159 VRQVRLRRDSKEKNTRRMASRKRRESITKKAKRFLSKIVAKNNKGMAFKQKSKSCHDLSVL 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, ...
75-295 1.69e-143

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: 402.55  E-value: 1.69e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFAGvHDSMDSDCEVLGEDTYERTLVVDGESATIILLDMWENKGeNEWLHDHCMQVGDAYLI 154
Cdd:cd04148    1 YRVVLLGDSGVGKSSLANIFTA-GVYEDSAYEASGDDTYERTVSVDGEEATLVVYDHWEQED-GMWLEDSCMQVGDAYVI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 155 VYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEGI 234
Cdd:cd04148   79 VYSVTDRSSFEKASELRIQLRRARQAEDIPIILVGNKSDLVRSREVSVQEGRACAVVFDCKFIETSAALQHNVDELFEGI 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160298187 235 VRQVRLRRDSKEKNERRLAYQKRRESIPRKARRFWGKIVAKNNKNMAFKLKSKSCHDLSVL 295
Cdd:cd04148  159 VRQVRLRRDSKEKNTRRMASRKRRESITKKAKRFLSKIVAKNNKGMAFKQKSKSCHDLSVL 219
small_GTPase smart00010
Small GTPase of the Ras superfamily; ill-defined subfamily; SMART predicts Ras-like small ...
75-241 1.85e-44

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: 148.48  E-value: 1.85e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187    75 YRVVLIGEQGVGKSTL-----ANIFAGVHDSMDsdcevlgEDTYERTLVVDGESATIILLDmweNKGENEW--LHDHCMQ 147
Cdd:smart00010   3 YKLVVLGGGGVGKSALtiqfvQGHFVDEYDPTI-------EDSYRKQIEIDGEVCLLDILD---TAGQEEFsaMRDQYMR 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187   148 VGDAYLIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNV 227
Cdd:smart00010  73 TGEGFLLVYSITDRQSFEEIAKFREQILRVKDRDDVPIVLVGNKCDLENERVVSTEEGKELARQWGCPFLETSAKERINV 152
                          170
                   ....*....|....
gi 160298187   228 KELFEGIVRQVRLR 241
Cdd:smart00010 153 DEAFYDLVREIRKS 166
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
76-239 1.25e-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: 136.11  E-value: 1.25e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187   76 RVVLIGEQGVGKSTLA-----NIFAGVHDSmdsdceVLGEDTYERTLVVDGEsatIILLDMWENKGENEW--LHDHCMQV 148
Cdd:pfam00071   1 KLVLVGDGGVGKSSLLirftqNKFPEEYIP------TIGVDFYTKTIEVDGK---TVKLQIWDTAGQERFraLRPLYYRG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  149 GDAYLIVYSITDRASFEKASELRIQLRRARQtEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVK 228
Cdd:pfam00071  72 ADGFLLVYDITSRDSFENVKKWVEEILRHAD-ENVPIVLVGNKCDLEDQRVVSTEEGEALAKELGLPFMETSAKTNENVE 150
                         170
                  ....*....|.
gi 160298187  229 ELFEGIVRQVR 239
Cdd:pfam00071 151 EAFEELAREIL 161
PTZ00369 PTZ00369
Ras-like protein; Provisional
73-251 3.26e-35

Ras-like protein; Provisional


Pssm-ID: 240385 [Multi-domain]  Cd Length: 189  Bit Score: 125.75  E-value: 3.26e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  73 TYYRVVLIGEQGVGKSTLANIFAGVHDSMDSDCEVlgEDTYERTLVVDGESAtiiLLDMWENKGENEW--LHDHCMQVGD 150
Cdd:PTZ00369   4 TEYKLVVVGGGGVGKSALTIQFIQNHFIDEYDPTI--EDSYRKQCVIDEETC---LLDILDTAGQEEYsaMRDQYMRTGQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 151 AYLIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKEL 230
Cdd:PTZ00369  79 GFLCVYSITSRSSFEEIASFREQILRVKDKDRVPMILVGNKCDLDSERQVSTGEGQELAKSFGIPFLETSAKQRVNVDEA 158
                        170       180
                 ....*....|....*....|...
gi 160298187 231 FEGIVRQVR--LRRDSKEKNERR 251
Cdd:PTZ00369 159 FYELVREIRkyLKEDMPSQKQKK 181
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
76-246 2.72e-13

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 66.54  E-value: 2.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  76 RVVLIGEQGVGKSTLANIFAGVHDSMDSDCEVLGEDTYERTLVVDGESATIILLDMwenKGENE----------WLHDHc 145
Cdd:COG1100    5 KIVVVGTGGVGKTSLVNRLVGDIFSLEKYLSTNGVTIDKKELKLDGLDVDLVIWDT---PGQDEfretrqfyarQLTGA- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 146 mqvgDAYLIVYSITDRASFEKASELRIQLRRARqtEDIPIILVGNKSDLVRCREVsVSEGRACAVVFDCKF---IETSAA 222
Cdd:COG1100   81 ----SLYLFVVDGTREETLQSLYELLESLRRLG--KKSPIILVLNKIDLYDEEEI-EDEERLKEALSEDNIvevVATSAK 153
                        170       180
                 ....*....|....*....|....
gi 160298187 223 VQHNVKELFEGIVRQVRLRRDSKE 246
Cdd:COG1100  154 TGEGVEELFAALAEILRGEGDSLD 177
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
74-236 1.61e-12

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: 64.32  E-value: 1.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187   74 YYRVVLIGEQGVGKSTLANIFAGVHDSMDSDCEVLGEDTYERTLVVDGESATIILLDMwenKGENEW--LHDHCMQVGDA 151
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYVTTVIEEDGKTYKFNLLDT---AGQEDYdaIRRLYYPQVER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  152 YLIVYSITDRA-SFEKASEL-RIQLRRARqTEDIPIILVGNKSDLvRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKE 229
Cdd:TIGR00231  78 SLRVFDIVILVlDVEEILEKqTKEIIHHA-DSGVPIILVGNKIDL-KDADLKTHVASEFAKLNGEPIIPLSAETGKNIDS 155

                  ....*..
gi 160298187  230 LFEGIVR 236
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, ...
75-295 1.69e-143

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: 402.55  E-value: 1.69e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFAGvHDSMDSDCEVLGEDTYERTLVVDGESATIILLDMWENKGeNEWLHDHCMQVGDAYLI 154
Cdd:cd04148    1 YRVVLLGDSGVGKSSLANIFTA-GVYEDSAYEASGDDTYERTVSVDGEEATLVVYDHWEQED-GMWLEDSCMQVGDAYVI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 155 VYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEGI 234
Cdd:cd04148   79 VYSVTDRSSFEKASELRIQLRRARQAEDIPIILVGNKSDLVRSREVSVQEGRACAVVFDCKFIETSAALQHNVDELFEGI 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160298187 235 VRQVRLRRDSKEKNERRLAYQKRRESIPRKARRFWGKIVAKNNKNMAFKLKSKSCHDLSVL 295
Cdd:cd04148  159 VRQVRLRRDSKEKNTRRMASRKRRESITKKAKRFLSKIVAKNNKGMAFKQKSKSCHDLSVL 219
Ras cd00876
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ...
76-238 2.46e-57

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: 181.57  E-value: 2.46e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  76 RVVLIGEQGVGKSTLANIFAGVHDSMDSDCEVlgEDTYERTLVVDGESATIILLDMWENkGENEWLHDHCMQVGDAYLIV 155
Cdd:cd00876    1 KLVVLGAGGVGKSALTIRFVSGEFVEEYDPTI--EDSYRKQIVVDGETYTLDILDTAGQ-EEFSAMRDQYIRNGDGFILV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 156 YSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEGIV 235
Cdd:cd00876   78 YSITSRESFEEIKNIREQILRVKDKEDVPIVLVGNKCDLENERQVSTEEGEALAEEWGCPFLETSAKTNINIDELFNTLV 157

                 ...
gi 160298187 236 RQV 238
Cdd:cd00876  158 REI 160
small_GTPase smart00010
Small GTPase of the Ras superfamily; ill-defined subfamily; SMART predicts Ras-like small ...
75-241 1.85e-44

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: 148.48  E-value: 1.85e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187    75 YRVVLIGEQGVGKSTL-----ANIFAGVHDSMDsdcevlgEDTYERTLVVDGESATIILLDmweNKGENEW--LHDHCMQ 147
Cdd:smart00010   3 YKLVVLGGGGVGKSALtiqfvQGHFVDEYDPTI-------EDSYRKQIEIDGEVCLLDILD---TAGQEEFsaMRDQYMR 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187   148 VGDAYLIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNV 227
Cdd:smart00010  73 TGEGFLLVYSITDRQSFEEIAKFREQILRVKDRDDVPIVLVGNKCDLENERVVSTEEGKELARQWGCPFLETSAKERINV 152
                          170
                   ....*....|....
gi 160298187   228 KELFEGIVRQVRLR 241
Cdd:smart00010 153 DEAFYDLVREIRKS 166
RAS smart00173
Ras subfamily of RAS small GTPases; Similar in fold and function to the bacterial EF-Tu GTPase. ...
75-239 4.69e-44

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: 147.70  E-value: 4.69e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187    75 YRVVLIGEQGVGKSTL-----ANIFAGVHDSMDsdcevlgEDTYERTLVVDGESATIILLDmweNKGENEW--LHDHCMQ 147
Cdd:smart00173   1 YKLVVLGSGGVGKSALtiqfiQGHFVDDYDPTI-------EDSYRKQIEIDGEVCLLDILD---TAGQEEFsaMRDQYMR 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187   148 VGDAYLIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNV 227
Cdd:smart00173  71 TGEGFLLVYSITDRQSFEEIKKFREQILRVKDRDDVPIVLVGNKCDLESERVVSTEEGKELARQWGCPFLETSAKERVNV 150
                          170
                   ....*....|..
gi 160298187   228 KELFEGIVRQVR 239
Cdd:smart00173 151 DEAFYDLVREIR 162
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
76-239 1.25e-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: 136.11  E-value: 1.25e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187   76 RVVLIGEQGVGKSTLA-----NIFAGVHDSmdsdceVLGEDTYERTLVVDGEsatIILLDMWENKGENEW--LHDHCMQV 148
Cdd:pfam00071   1 KLVLVGDGGVGKSSLLirftqNKFPEEYIP------TIGVDFYTKTIEVDGK---TVKLQIWDTAGQERFraLRPLYYRG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  149 GDAYLIVYSITDRASFEKASELRIQLRRARQtEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVK 228
Cdd:pfam00071  72 ADGFLLVYDITSRDSFENVKKWVEEILRHAD-ENVPIVLVGNKCDLEDQRVVSTEEGEALAKELGLPFMETSAKTNENVE 150
                         170
                  ....*....|.
gi 160298187  229 ELFEGIVRQVR 239
Cdd:pfam00071 151 EAFEELAREIL 161
Rit_Rin_Ric cd04141
Ras-like protein in all tissues (Rit), Ras-like protein in neurons (Rin) and Ras-related ...
75-239 4.00e-38

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: 132.67  E-value: 4.00e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFagVHDSMDSDCEVLGEDTYERTLVVDGESAtiiLLDMWENKGENEW--LHDHCMQVGDAY 152
Cdd:cd04141    3 YKIVMLGAGGVGKSAVTMQF--ISHSFPDYHDPTIEDAYKTQARIDNEPA---LLDILDTAGQAEFtaMRDQYMRCGEGF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 153 LIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFE 232
Cdd:cd04141   78 IICYSVTDRHSFQEASEFKELITRVRLTEDIPLVLVGNKVDLEQQRQVTTEEGRNLAREFNCPFFETSAALRFYIDDAFH 157

                 ....*..
gi 160298187 233 GIVRQVR 239
Cdd:cd04141  158 GLVREIR 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, ...
75-239 1.79e-36

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: 127.92  E-value: 1.79e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFAGVHDSMDSDCEVlgEDTYERTLVVDGESAtiiLLDMWENKGENEW--LHDHCMQVGDAY 152
Cdd:cd04138    2 YKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTI--EDSYRKQVVIDGETC---LLDILDTAGQEEYsaMRDQYMRTGEGF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 153 LIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLvRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFE 232
Cdd:cd04138   77 LCVFAINSRKSFEDIHTYREQIKRVKDSDDVPMVLVGNKCDL-AARTVSTRQGQDLAKSYGIPYIETSAKTRQGVEEAFY 155

                 ....*..
gi 160298187 233 GIVRQVR 239
Cdd:cd04138  156 TLVREIR 162
PTZ00369 PTZ00369
Ras-like protein; Provisional
73-251 3.26e-35

Ras-like protein; Provisional


Pssm-ID: 240385 [Multi-domain]  Cd Length: 189  Bit Score: 125.75  E-value: 3.26e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  73 TYYRVVLIGEQGVGKSTLANIFAGVHDSMDSDCEVlgEDTYERTLVVDGESAtiiLLDMWENKGENEW--LHDHCMQVGD 150
Cdd:PTZ00369   4 TEYKLVVVGGGGVGKSALTIQFIQNHFIDEYDPTI--EDSYRKQCVIDEETC---LLDILDTAGQEEYsaMRDQYMRTGQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 151 AYLIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKEL 230
Cdd:PTZ00369  79 GFLCVYSITSRSSFEEIASFREQILRVKDKDRVPMILVGNKCDLDSERQVSTGEGQELAKSFGIPFLETSAKQRVNVDEA 158
                        170       180
                 ....*....|....*....|...
gi 160298187 231 FEGIVRQVR--LRRDSKEKNERR 251
Cdd:PTZ00369 159 FYELVREIRkyLKEDMPSQKQKK 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, ...
74-239 1.87e-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: 122.90  E-value: 1.87e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  74 YYRVVLIGEQGVGKSTLANIFAGVHDSMDSDCEVlgEDTYERTLVVDGESAtiiLLDMWENKGENEW--LHDHCMQVGDA 151
Cdd:cd04145    2 TYKLVVVGGGGVGKSALTIQFIQSYFVTDYDPTI--EDSYTKQCEIDGQWA---RLDILDTAGQEEFsaMREQYMRTGEG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 152 YLIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELF 231
Cdd:cd04145   77 FLLVFSVTDRGSFEEVDKFHTQILRVKDRDEFPMILVGNKADLEHQRQVSREEGQELARQLKIPYIETSAKDRVNVDKAF 156

                 ....*...
gi 160298187 232 EGIVRQVR 239
Cdd:cd04145  157 HDLVRVIR 164
Ras2 cd04144
Rat sarcoma (Ras) family 2 of small guanosine triphosphatases (GTPases); The Ras2 subfamily, ...
76-242 2.68e-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: 123.03  E-value: 2.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  76 RVVLIGEQGVGKSTLANIFAGVHDSMDSDCEVlgEDTYERTLVVDGESATIILLDmweNKGENEW--LHDHCMQVGDAYL 153
Cdd:cd04144    1 KLVVLGDGGVGKTALTIQLCLNHFVETYDPTI--EDSYRKQVVVDGQPCMLEVLD---TAGQEEYtaLRDQWIREGEGFI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 154 IVYSITDRASFEKASELRIQLRRARQTE--DIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELF 231
Cdd:cd04144   76 LVYSITSRSTFERVERFREQIQRVKDESaaDVPIMIVGNKCDKVYEREVSTEEGAALARRLGCEFIEASAKTNVNVERAF 155
                        170
                 ....*....|.
gi 160298187 232 EGIVRQVRLRR 242
Cdd:cd04144  156 YTLVRALRQQR 166
RalA_RalB cd04139
Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily ...
75-239 1.22e-33

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: 120.61  E-value: 1.22e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFagVHDSMDSDCEVLGEDTYERTLVVDGESatiILLDMWENKGENEW--LHDHCMQVGDAY 152
Cdd:cd04139    1 HKVIMVGSGGVGKSALTLQF--MYDEFVEDYEPTKADSYRKKVVLDGEE---VQLNILDTAGQEDYaaIRDNYFRSGEGF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 153 LIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFE 232
Cdd:cd04139   76 LLVFSITDMESFTALAEFREQILRVKEDDNVPLLLVGNKCDLEDKRQVSVEEAANLAEQWGVNYVETSAKTRANVDKVFF 155

                 ....*..
gi 160298187 233 GIVRQVR 239
Cdd:cd04139  156 DLVREIR 162
Rap_like cd04136
Rap-like family consists of Rap1, Rap2 and RSR1; The Rap subfamily consists of the Rap1, Rap2, ...
75-238 2.19e-31

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: 114.96  E-value: 2.19e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFA-GVH-DSMDSDCEvlgeDTYERTLVVDGESATIILLDmweNKGENEW--LHDHCMQVGD 150
Cdd:cd04136    2 YKLVVLGSGGVGKSALTVQFVqGIFvDKYDPTIE----DSYRKQIEVDCQQCMLEILD---TAGTEQFtaMRDLYIKNGQ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 151 AYLIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVF-DCKFIETSAAVQHNVKE 229
Cdd:cd04136   75 GFALVYSITAQQSFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVSKEEGQNLARQWgNCPFLETSAKSKINVDE 154

                 ....*....
gi 160298187 230 LFEGIVRQV 238
Cdd:cd04136  155 IFYDLVRQI 163
Rap2 cd04176
Rap2 family GTPase consists of Rap2a, Rap2b, and Rap2c; The Rap2 subgroup is part of the Rap ...
75-238 3.35e-30

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: 111.85  E-value: 3.35e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFagVHDSMDSDCEVLGEDTYERTLVVDGESATIILLDmweNKGENEW--LHDHCMQVGDAY 152
Cdd:cd04176    2 YKVVVLGSGGVGKSALTVQF--VSGTFIEKYDPTIEDFYRKEIEVDSSPSVLEILD---TAGTEQFasMRDLYIKNGQGF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 153 LIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFE 232
Cdd:cd04176   77 IVVYSLVNQQTFQDIKPMRDQIVRVKGYEKVPIILVGNKVDLESEREVSSAEGRALAEEWGCPFMETSAKSKTMVNELFA 156

                 ....*.
gi 160298187 233 GIVRQV 238
Cdd:cd04176  157 EIVRQM 162
Rap1 cd04175
Rap1 family GTPase consists of Rap1a and Rap1b isoforms; The Rap1 subgroup is part of the Rap ...
75-238 1.13e-29

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: 110.30  E-value: 1.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLA-----NIFAGVHDSMDsdcevlgEDTYERTLVVDGESATIILLDmweNKGENEW--LHDHCMQ 147
Cdd:cd04175    2 YKLVVLGSGGVGKSALTvqfvqGIFVEKYDPTI-------EDSYRKQVEVDGQQCMLEILD---TAGTEQFtaMRDLYMK 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 148 VGDAYLIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNV 227
Cdd:cd04175   72 NGQGFVLVYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVGKEQGQNLARQWGCAFLETSAKAKINV 151
                        170
                 ....*....|.
gi 160298187 228 KELFEGIVRQV 238
Cdd:cd04175  152 NEIFYDLVRQI 162
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
75-236 1.15e-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: 110.24  E-value: 1.15e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFagVHDSMDSDCEV-LGEDTYERTLVVDGESatiILLDMWenkgenewlhDHCMQ-----V 148
Cdd:cd00154    1 FKIVLIGDSGVGKTSLLLRF--VDNKFSENYKStIGVDFKSKTIEVDGKK---VKLQIW----------DTAGQerfrsI 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 149 GDAY-------LIVYSITDRASFEKASELRIQLRRaRQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSA 221
Cdd:cd00154   66 TSSYyrgahgaILVYDVTNRESFENLDKWLNELKE-YAPPNIPIILVGNKSDLEDERQVSTEEAQQFAKENGLLFFETSA 144
                        170
                 ....*....|....*
gi 160298187 222 AVQHNVKELFEGIVR 236
Cdd:cd00154  145 KTGENVDEAFESLAR 159
RSR1 cd04177
RSR1/Bud1p family GTPase; RSR1/Bud1p is a member of the Rap subfamily of the Ras family that ...
75-239 5.54e-29

RSR1/Bud1p family GTPase; RSR1/Bud1p is a member of the Rap subfamily of the Ras family that is found in fungi. In budding yeasts, RSR1 is involved in selecting a site for bud growth on the cell cortex, which directs the establishment of cell polarization. The Rho family GTPase cdc42 and its GEF, cdc24, then establish an axis of polarized growth by organizing the actin cytoskeleton and secretory apparatus at the bud site. It is believed that cdc42 interacts directly with RSR1 in vivo. In filamentous fungi, polar growth occurs at the tips of hypha and at novel growth sites along the extending hypha. In Ashbya gossypii, RSR1 is a key regulator of hyphal growth, localizing at the tip region and regulating in apical polarization of the actin cytoskeleton. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins.


Pssm-ID: 133377 [Multi-domain]  Cd Length: 168  Bit Score: 108.72  E-value: 5.54e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFagVHDSMDSDCEVLGEDTYERTLVVDGESATIILLDmweNKGENEW--LHDHCMQVGDAY 152
Cdd:cd04177    2 YKIVVLGAGGVGKSALTVQF--VQNVFIESYDPTIEDSYRKQVEIDGRQCDLEILD---TAGTEQFtaMRELYIKSGQGF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 153 LIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVF-DCKFIETSAAVQHNVKELF 231
Cdd:cd04177   77 LLVYSVTSEASLNELGELREQVLRIKDSDNVPMVLVGNKADLEDDRQVSREDGVSLSQQWgNVPFYETSARKRTNVDEVF 156

                 ....*...
gi 160298187 232 EGIVRQVR 239
Cdd:cd04177  157 IDLVRQII 164
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
75-238 9.33e-29

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


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 107.98  E-value: 9.33e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187    75 YRVVLIGEQGVGKSTLANIFagVHDSMDSDCEV-LGEDTYERTLVVDGesaTIILLDMWENKGenewlhdhcmQ-----V 148
Cdd:smart00175   1 FKIILIGDSGVGKSSLLSRF--TDGKFSEQYKStIGVDFKTKTIEVDG---KRVKLQIWDTAG----------QerfrsI 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187   149 GDAY-------LIVYSITDRASFEKASELRIQLRRARQtEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSA 221
Cdd:smart00175  66 TSSYyrgavgaLLVYDITNRESFENLENWLKELREYAS-PNVVIMLVGNKSDLEEQRQVSREEAEAFAEEHGLPFFETSA 144
                          170
                   ....*....|....*..
gi 160298187   222 AVQHNVKELFEGIVRQV 238
Cdd:smart00175 145 KTNTNVEEAFEELAREI 161
ARHI_like cd04140
A Ras homolog member I (ARHI); ARHI (A Ras homolog member I) is a member of the Ras family ...
75-232 1.12e-28

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: 107.61  E-value: 1.12e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFagVHDSMDSDCEVLGEDTYERTLvvdGESATIILLDMWENKGENEW--LHDHCMQVGDAY 152
Cdd:cd04140    2 YRVVVFGAGGVGKSSLVLRF--VKGTFRESYIPTIEDTYRQVI---SCSKSICTLQITDTTGSHQFpaMQRLSISKGHAF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 153 LIVYSITDRASFEKASELRIQLRRAR--QTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKEL 230
Cdd:cd04140   77 ILVYSITSKQSLEELKPIYELICEIKgnNLEKIPIMLVGNKCDESPSREVSSSEGAALARTWNCAFMETSAKTNHNVQEL 156

                 ..
gi 160298187 231 FE 232
Cdd:cd04140  157 FQ 158
RERG_RasL11_like cd04146
Ras-related and Estrogen-Regulated Growth inhibitor (RERG) and Ras-like 11 (RasL11)-like ...
77-239 1.15e-28

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: 107.75  E-value: 1.15e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  77 VVLIGEQGVGKST-----LANIFAGVHDSMDsdcevlgEDTYERTLVVDGESATIILLDM--WENKGENEWLhDHCMQVG 149
Cdd:cd04146    2 IAVLGASGVGKSAltvrfLTKRFIGEYEPNL-------ESLYSRQVTIDGEQVSLEIQDTpgQQQNEDPESL-ERSLRWA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 150 DAYLIVYSITDRASFEKASELRIQLRRARQTE-DIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQ-HNV 227
Cdd:cd04146   74 DGFVLVYSITDRSSFDVVSQLLQLIREIKKRDgEIPVILVGNKADLLHSRQVSTEEGQKLALELGCLFFEVSAAENyLEV 153
                        170
                 ....*....|..
gi 160298187 228 KELFEGIVRQVR 239
Cdd:cd04146  154 QNVFHELCREVR 165
RheB cd04137
Ras Homolog Enriched in Brain (RheB) is a small GTPase; Rheb (Ras Homolog Enriched in Brain) ...
76-251 1.58e-26

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: 102.32  E-value: 1.58e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  76 RVVLIGEQGVGKSTLANIFAGVH--DSMDSDCEvlgeDTYERTLVVDGESATIILLDmweNKGENEW--LHDHCMQVGDA 151
Cdd:cd04137    3 KIAVLGSRSVGKSSLTVQFVEGHfvESYYPTIE----NTFSKIITYKGQEYHLEIVD---TAGQDEYsiLPQKYSIGIHG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 152 YLIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELF 231
Cdd:cd04137   76 YILVYSVTSRKSFEVVKVIYDKILDMLGKESVPIVLVGNKSDLHMERQVSAEEGKKLAESWGAAFLESSAKENENVEEAF 155
                        170       180
                 ....*....|....*....|.
gi 160298187 232 EGIVRQV-RLRRDSKEKNERR 251
Cdd:cd04137  156 ELLIEEIeKVENPLPPGQKSK 176
Rab21 cd04123
Rab GTPase family 21 (Rab21); The localization and function of Rab21 are not clearly defined, ...
75-238 2.87e-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: 2.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFagVHDSMDSDCEVLGEDT-YERTLVVDGESATiilLDMWENKGENEWlhdHCM-----QV 148
Cdd:cd04123    1 FKVVLLGEGRVGKTSLVLRY--VENKFNEKHESTTQASfFQKTVNIGGKRID---LAIWDTAGQERY---HALgpiyyRD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 149 GDAYLIVYSITDRASFEKASELRIQLRRARQtEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVK 228
Cdd:cd04123   73 ADGAILVYDITDADSFQKVKKWIKELKQMRG-NNISLVIVGNKIDLERQRVVSKSEAEEYAKSVGAKHFETSAKTGKGIE 151
                        170
                 ....*....|
gi 160298187 229 ELFEGIVRQV 238
Cdd:cd04123  152 ELFLSLAKRM 161
Rab5_related cd01860
Rab-related GTPase family includes Rab5 and Rab22; regulates early endosome fusion; The ...
75-238 6.59e-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: 94.93  E-value: 6.59e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFagVHDSMDSDCEV-LGEDTYERTLVVDGesaTIILLDMWENKGEnEWLHDHC-MQVGDA- 151
Cdd:cd01860    2 FKLVLLGDSSVGKSSIVLRF--VKNEFSENQEStIGAAFLTQTVNLDD---TTVKFEIWDTAGQ-ERYRSLApMYYRGAa 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 152 -YLIVYSITDRASFEKA----SELRIQLRrarqtEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHN 226
Cdd:cd01860   76 aAIVVYDITSEESFEKAkswvKELQEHGP-----PNIVIALAGNKADLESKRQVSTEEAQEYADENGLLFMETSAKTGEN 150
                        170
                 ....*....|..
gi 160298187 227 VKELFEGIVRQV 238
Cdd:cd01860  151 VNELFTEIARKL 162
Rab6 cd01861
Rab GTPase family 6 (Rab6); Rab6 is involved in microtubule-dependent transport pathways ...
75-234 5.99e-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: 92.30  E-value: 5.99e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFagVHDSMDsdcevlgeDTYERTLVVDGESATI------ILLDMWENKGENE-------WL 141
Cdd:cd01861    1 HKLVFLGDQSVGKTSIITRF--MYDTFD--------NQYQATIGIDFLSKTMyvddktVRLQLWDTAGQERfrslipsYI 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 142 HDHCMQVgdaylIVYSITDRASFEKASELrIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSA 221
Cdd:cd01861   71 RDSSVAV-----VVYDITNRQSFDNTDKW-IDDVRDERGNDVIIVLVGNKTDLSDKRQVSTEEGEKKAKENNAMFIETSA 144
                        170
                 ....*....|...
gi 160298187 222 AVQHNVKELFEGI 234
Cdd:cd01861  145 KAGHNVKQLFKKI 157
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
78-236 4.83e-22

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: 90.21  E-value: 4.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  78 VLIGEQGVGKSTLANIFAGVHDSMDSDCEV--LGEDTYERTLVVDGESATII----LLDmwENKGENEWLHDHCMQVGDA 151
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGttRDPDVYVKELDKGKVKLVLVdtpgLDE--FGGLGREELARLLLRGADL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 152 YLIVYSITDRASFEKASELRIQLRRARqteDIPIILVGNKSDLV-RCREVSVSEGRACAVVFDCKFIETSAAVQHNVKEL 230
Cdd:cd00882   79 ILLVVDSTDRESEEDAKLLILRRLRKE---GIPIILVGNKIDLLeEREVEELLRLEELAKILGVPVFEVSAKTGEGVDEL 155

                 ....*.
gi 160298187 231 FEGIVR 236
Cdd:cd00882  156 FEKLIE 161
Rab11_like cd01868
Rab GTPase family 11 (Rab11)-like includes Rab11a, Rab11b, and Rab25; Rab11a, Rab11b, and ...
75-238 6.09e-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: 89.93  E-value: 6.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFAGVHDSMDSDCEVlGEDTYERTLVVDGEsatIILLDMWENKGENEWLhdhcmQVGDAY-- 152
Cdd:cd01868    4 FKIVLIGDSGVGKSNLLSRFTRNEFNLDSKSTI-GVEFATRTIQIDGK---TIKAQIWDTAGQERYR-----AITSAYyr 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 153 -----LIVYSITDRASFEKA----SELRiqlrrARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAV 223
Cdd:cd01868   75 gavgaLLVYDITKKSTFENVerwlKELR-----DHADSNIVIMLVGNKSDLRHLRAVPTEEAKAFAEKNGLSFIETSALD 149
                        170
                 ....*....|....*
gi 160298187 224 QHNVKELFEGIVRQV 238
Cdd:cd01868  150 GTNVEEAFKQLLTEI 164
Ras_dva cd04147
Ras - dorsal-ventral anterior localization (Ras-dva) family; Ras-dva subfamily. Ras-dva (Ras - ...
76-267 1.93e-21

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: 89.51  E-value: 1.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  76 RVVLIGEQGVGKSTLANIFagVHDSMDSDCEVLGEDTYERTLVVDGESATIILLDmweNKGENEW--LHDHCMQVGDAYL 153
Cdd:cd04147    1 RLVFMGAAGVGKTALIQRF--LYDTFEPKHRRTVEELHSKEYEVAGVKVTIDILD---TSGSYSFpaMRKLSIQNGDAFA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 154 IVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVV-FDCKFIETSAAVQHNVKELFE 232
Cdd:cd04147   76 LVYSVDDPESFEEVKRLREEILEVKEDKFVPIVVVGNKIDSLAERQVEAADALSTVELdWNNGFVEASAKDNENVTEVFK 155
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 160298187 233 GIVRQVRLrrdskeknERRL--AYQKRRESIPRKARR 267
Cdd:cd04147  156 ELLQQANL--------PSWLspALRRRRESAPSEIQR 184
Rab39 cd04111
Rab GTPase family 39 (Rab39); Found in eukaryotes, Rab39 is mainly found in epithelial cell ...
75-246 8.50e-20

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: 85.20  E-value: 8.50e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLAN-----IFAGVHDSmdsdceVLGEDTYERTlvVDGESATIILLDMWENKGENEWlhdhcMQVG 149
Cdd:cd04111    3 FRLIVIGDSTVGKSSLLKrftegRFAEVSDP------TVGVDFFSRL--IEIEPGVRIKLQLWDTAGQERF-----RSIT 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 150 DAY-------LIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAA 222
Cdd:cd04111   70 RSYyrnsvgvLLVFDITNRESFEHVHDWLEEARSHIQPHRPVFILVGHKCDLESQRQVTREEAEKLAKDLGMKYIETSAR 149
                        170       180
                 ....*....|....*....|....
gi 160298187 223 VQHNVKELFEGIVRQVRLRRDSKE 246
Cdd:cd04111  150 TGDNVEEAFELLTQEIYERIKRGE 173
Rab1_Ypt1 cd01869
Rab GTPase family 1 includes the yeast homolog Ypt1; Rab1/Ypt1 subfamily. Rab1 is found in ...
75-241 1.50e-19

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: 83.53  E-value: 1.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFAGvHDSMDSDCEVLGEDTYERTLVVDGEsatIILLDMWENKGENEW--LHDHCMQVGDAY 152
Cdd:cd01869    3 FKLLLIGDSGVGKSCLLLRFAD-DTYTESYISTIGVDFKIRTIELDGK---TVKLQIWDTAGQERFrtITSSYYRGAHGI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 153 LIVYSITDRASFEKASELRIQLRRArQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFE 232
Cdd:cd01869   79 IIVYDVTDQESFNNVKQWLQEIDRY-ASENVNKLLVGNKCDLTDKKVVDYTEAKEFADELGIPFLETSAKNATNVEEAFM 157

                 ....*....
gi 160298187 233 GIVRQVRLR 241
Cdd:cd01869  158 TMAREIKKR 166
Rab8_Rab10_Rab13_like cd01867
Rab GTPase families 8, 10, 13 (Rab8, Rab10, Rab13); Rab8/Sec4/Ypt2 are known or suspected to ...
75-241 2.78e-18

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: 80.00  E-value: 2.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLanIFAGVHDSM-DSDCEVLGEDTYERTLVVDGESatiILLDMWENKGEnEWLHdhcmQVGDAY- 152
Cdd:cd01867    4 FKLLLIGDSGVGKSCL--LLRFSEDSFnPSFISTIGIDFKIRTIELDGKK---IKLQIWDTAGQ-ERFR----TITTSYy 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 153 ------LIVYSITDRASFEkasELRIQLRRARQ--TEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQ 224
Cdd:cd01867   74 rgamgiILVYDITDEKSFE---NIKNWMRNIDEhaSEDVERMLVGNKCDMEEKRVVSKEEGEALAREYGIKFLETSAKAN 150
                        170
                 ....*....|....*..
gi 160298187 225 HNVKELFEGIVRQVRLR 241
Cdd:cd01867  151 INVEEAFLTLAKDILKK 167
Rab9 cd04116
Rab GTPase family 9 (Rab9); Rab9 is found in late endosomes, together with mannose 6-phosphate ...
76-238 8.19e-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: 8.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  76 RVVLIGEQGVGKSTLANIFagVHDSMDSDC-EVLGEDTYERTLVVDGESATiilLDMWENKGENEW--LHDHCMQVGDAY 152
Cdd:cd04116    7 KVILLGDGGVGKSSLMNRY--VTNKFDTQLfHTIGVEFLNKDLEVDGHFVT---LQIWDTAGQERFrsLRTPFYRGSDCC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 153 LIVYSITDRASFEKASELR---IQLRRARQTEDIPIILVGNKSDLVRcREVSVSEGRA-CAVVFDCKFIETSAAVQHNVK 228
Cdd:cd04116   82 LLTFSVDDSQSFQNLSNWKkefIYYADVKEPESFPFVILGNKIDIPE-RQVSTEEAQAwCRDNGDYPYFETSAKDATNVA 160
                        170
                 ....*....|
gi 160298187 229 ELFEGIVRQV 238
Cdd:cd04116  161 AAFEEAVRRV 170
PLN03110 PLN03110
Rab GTPase; Provisional
75-238 4.24e-17

Rab GTPase; Provisional


Pssm-ID: 178657 [Multi-domain]  Cd Length: 216  Bit Score: 78.05  E-value: 4.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFAGVHDSMDSDcEVLGEDTYERTLVVDGESatiILLDMWENKGENEWlhdhcMQVGDAY-- 152
Cdd:PLN03110  13 FKIVLIGDSGVGKSNILSRFTRNEFCLESK-STIGVEFATRTLQVEGKT---VKAQIWDTAGQERY-----RAITSAYyr 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 153 -----LIVYSITDRASFEKASELriqLRRARQTED--IPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQH 225
Cdd:PLN03110  84 gavgaLLVYDITKRQTFDNVQRW---LRELRDHADsnIVIMMAGNKSDLNHLRSVAEEDGQALAEKEGLSFLETSALEAT 160
                        170
                 ....*....|...
gi 160298187 226 NVKELFEGIVRQV 238
Cdd:PLN03110 161 NVEKAFQTILLEI 173
Rho cd00157
Ras homology family (Rho) of small guanosine triphosphatases (GTPases); Members of the Rho ...
77-236 2.66e-16

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: 74.89  E-value: 2.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  77 VVLIGEQGVGKSTLANIFAgvhdsmdSDcEVLGE------DTYERTLVVDGESatiILLDMWENKGENEwlHDH----CM 146
Cdd:cd00157    3 IVVVGDGAVGKTCLLISYT-------TN-KFPTEyvptvfDNYSANVTVDGKQ---VNLGLWDTAGQEE--YDRlrplSY 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 147 QVGDAYLIVYSITDRASFEKAS-----ELRiqlrraRQTEDIPIILVGNKSDLvrcRE--------------VSVSEGRA 207
Cdd:cd00157   70 PQTDVFLLCFSVDSPSSFENVKtkwypEIK------HYCPNVPIILVGTKIDL---RDdgntlkklekkqkpITPEEGEK 140
                        170       180       190
                 ....*....|....*....|....*....|
gi 160298187 208 CAVVFDC-KFIETSAAVQHNVKELFEGIVR 236
Cdd:cd00157  141 LAKEIGAvKYMECSALTQEGLKEVFDEAIR 170
PLN03118 PLN03118
Rab family protein; Provisional
67-262 2.76e-16

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 75.86  E-value: 2.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  67 SSESGNTY---YRVVLIGEQGVGKSTLANIFagVHDSMDSDCEVLGEDTYERTLVVDGESatiILLDMWENKGENEW--L 141
Cdd:PLN03118   4 SSGQSSGYdlsFKILLIGDSGVGKSSLLVSF--ISSSVEDLAPTIGVDFKIKQLTVGGKR---LKLTIWDTAGQERFrtL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 142 HDHCMQVGDAYLIVYSITDRASFEKASEL---RIQLRRARQteDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIE 218
Cdd:PLN03118  79 TSSYYRNAQGIILVYDVTRRETFTNLSDVwgkEVELYSTNQ--DCVKMLVGNKVDRESERDVSREEGMALAKEHGCLFLE 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 160298187 219 TSAAVQHNVKELFEGIVRQV----RLRRDSKEKNERRLAYQKRRESIP 262
Cdd:PLN03118 157 CSAKTRENVEQCFEELALKImevpSLLEEGSTAVKRNILKQKPEHQPP 204
Rab2 cd01866
Rab GTPase family 2 (Rab2); Rab2 is localized on cis-Golgi membranes and interacts with Golgi ...
75-231 3.41e-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: 3.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLA-----NIFAGVHDSmdsdceVLGEDTYERTLVVDGESatiILLDMWENKGENEWlhdhcMQVG 149
Cdd:cd01866    5 FKYIIIGDTGVGKSCLLlqftdKRFQPVHDL------TIGVEFGARMITIDGKQ---IKLQIWDTAGQESF-----RSIT 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 150 DAY-------LIVYSITDRASFEKaseLRIQLRRARQ--TEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETS 220
Cdd:cd01866   71 RSYyrgaagaLLVYDITRRETFNH---LTSWLEDARQhsNSNMTIMLIGNKCDLESRREVSYEEGEAFAREHGLIFMETS 147
                        170
                 ....*....|.
gi 160298187 221 AAVQHNVKELF 231
Cdd:cd01866  148 AKTASNVEEAF 158
Miro1 cd01893
Mitochondrial Rho family 1 (Miro1), N-terminal; Miro1 subfamily. Miro (mitochondrial Rho) ...
76-231 8.74e-16

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: 73.53  E-value: 8.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  76 RVVLIGEQGVGKSTLANIFAGvhdsmdsdcEVLGEDTYER----TLVVDG--ESATIILLDMWENKGENEWLHDHCMQvG 149
Cdd:cd01893    4 RIVLIGDEGVGKSSLIMSLVS---------EEFPENVPRVlpeiTIPADVtpERVPTTIVDTSSRPQDRANLAAEIRK-A 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 150 DAYLIVYSITDRASFEKASELRIQLRRaRQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIET----SAAVQH 225
Cdd:cd01893   74 NVICLVYSVDRPSTLERIRTKWLPLIR-RLGVKVPIILVGNKSDLRDGSSQAGLEEEMLPIMNEFREIETcvecSAKTLI 152

                 ....*.
gi 160298187 226 NVKELF 231
Cdd:cd01893  153 NVSEVF 158
RabL4 cd04101
Rab GTPase-like family 4 (Rab-like4); RabL4 (Rab-like4) subfamily. RabL4s are novel proteins ...
76-237 1.10e-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: 72.95  E-value: 1.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  76 RVVLIGEQGVGKSTLANIFA--GVH----DSMDSDCEVLgedtyERTLVVDGESATIILLdMWENKGENEW--LHDHCMQ 147
Cdd:cd04101    2 QCAVVGDPAVGKSALVQMFHsdGATfqknYTMTTGCDLV-----VKTVPVPDTSDSVELF-IFDSAGQELFsdMVENVWE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 148 VGDAYLIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNV 227
Cdd:cd04101   76 QPAVVCVVYDVTNEVSFNNCSRWINRVRTHSHGLHTPGVLVGNKCDLTDRREVDAAQAQALAQANTLKFYETSAKEGVGY 155
                        170
                 ....*....|
gi 160298187 228 KELFEGIVRQ 237
Cdd:cd04101  156 EAPFLSLARA 165
Rab18 cd01863
Rab GTPase family 18 (Rab18); Rab18 subfamily. Mammalian Rab18 is implicated in endocytic ...
75-238 4.23e-15

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: 71.19  E-value: 4.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFagVHDSMDSDCEV-LGEDTYERTLVVDGesaTIILLDMWENKGENEW--LHDHCMQVGDA 151
Cdd:cd01863    1 LKILLIGDSGVGKSSLLLRF--TDDTFDEDLSStIGVDFKVKTVTVDG---KKVKLAIWDTAGQERFrtLTSSYYRGAQG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 152 YLIVYSITDRASFEKaseLRIQLRRAR---QTEDIPIILVGNKSDLVRcREVSVSEGRACAVVFDCKFIETSAAVQHNVK 228
Cdd:cd01863   76 VILVYDVTRRDTFDN---LDTWLNELDtysTNPDAVKMLVGNKIDKEN-REVTREEGQKFARKHNMLFIETSAKTRIGVQ 151
                        170
                 ....*....|
gi 160298187 229 ELFEGIVRQV 238
Cdd:cd01863  152 QAFEELVEKI 161
PLN03108 PLN03108
Rab family protein; Provisional
75-231 4.94e-14

Rab family protein; Provisional


Pssm-ID: 178655 [Multi-domain]  Cd Length: 210  Bit Score: 69.58  E-value: 4.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLA-----NIFAGVHDSmdsdceVLGEDTYERTLVVDGESatiILLDMWENKGENEWlhdhcMQVG 149
Cdd:PLN03108   7 FKYIIIGDTGVGKSCLLlqftdKRFQPVHDL------TIGVEFGARMITIDNKP---IKLQIWDTAGQESF-----RSIT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 150 DAY-------LIVYSITDRASFekaSELRIQLRRARQ--TEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETS 220
Cdd:PLN03108  73 RSYyrgaagaLLVYDITRRETF---NHLASWLEDARQhaNANMTIMLIGNKCDLAHRRAVSTEEGEQFAKEHGLIFMEAS 149
                        170
                 ....*....|.
gi 160298187 221 AAVQHNVKELF 231
Cdd:PLN03108 150 AKTAQNVEEAF 160
Rab7 cd01862
Rab GTPase family 7 (Rab7); Rab7 subfamily. Rab7 is a small Rab GTPase that regulates ...
75-236 8.20e-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: 68.07  E-value: 8.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFagVHDSMDSDCE-VLGEDTYERTLVVDGESATiilLDMWENKGenewlHDHCMQVG---- 149
Cdd:cd01862    1 LKVIILGDSGVGKTSLMNQY--VNKKFSNQYKaTIGADFLTKEVTVDDRLVT---LQIWDTAG-----QERFQSLGvafy 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 150 ---DAYLIVYSITDRASFEKAS----ELRIQLRrARQTEDIPIILVGNKSDLVRCREVSVSEGRA-CAVVFDCKFIETSA 221
Cdd:cd01862   71 rgaDCCVLVYDVTNPKSFESLDswrdEFLIQAS-PRDPENFPFVVLGNKIDLEEKRQVSTKKAQQwCKSKGNIPYFETSA 149
                        170
                 ....*....|....*
gi 160298187 222 AVQHNVKELFEGIVR 236
Cdd:cd01862  150 KEAINVDQAFETIAR 164
Rab19 cd01864
Rab GTPase family 19 (Rab19); Rab19 subfamily. Rab19 proteins are associated with Golgi stacks. ...
75-238 1.35e-13

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: 67.46  E-value: 1.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIF-AGVHdsMDSDCEVLGEDTYERTLVVDGESatiILLDMWENKGENEW--LHDHCMQVGDA 151
Cdd:cd01864    4 FKIILIGDSNVGKTCVVQRFkSGTF--SERQGNTIGVDFTMKTLEIQGKR---VKLQIWDTAGQERFrtITQSYYRSANG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 152 YLIVYSITDRASFEKASELrIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKF-IETSAAVQHNVKEL 230
Cdd:cd01864   79 AIIAYDITRRSSFESVPHW-IEEVEKYGASNVVLLLIGNKCDLEEQREVLFEEACTLAEHYGILAvLETSAKESSNVEEA 157

                 ....*...
gi 160298187 231 FEGIVRQV 238
Cdd:cd01864  158 FLLMATEL 165
PTZ00099 PTZ00099
rab6; Provisional
110-238 2.27e-13

rab6; Provisional


Pssm-ID: 185444 [Multi-domain]  Cd Length: 176  Bit Score: 67.08  E-value: 2.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 110 EDTYERTLVVDGESATIIL------LDMWENKGENEW--LHDHCMQVGDAYLIVYSITDRASFEKASELrIQLRRARQTE 181
Cdd:PTZ00099   6 DNNYQSTIGIDFLSKTLYLdegpvrLQLWDTAGQERFrsLIPSYIRDSAAAIVVYDITNRQSFENTTKW-IQDILNERGK 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 160298187 182 DIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEGIVRQV 238
Cdd:PTZ00099  85 DVIIALVGNKTDLGDLRKVTYEEGMQKAQEYNTMFHETSAKAGHNIKVLFKKIAAKL 141
Wrch_1 cd04130
Wnt-1 responsive Cdc42 homolog (Wrch-1) is a Rho family GTPase similar to Cdc42; Wrch-1 (Wnt-1 ...
78-232 2.62e-13

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


Pssm-ID: 133330 [Multi-domain]  Cd Length: 173  Bit Score: 66.66  E-value: 2.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  78 VLIGEQGVGKSTLanIFAGVHDSMDSDCEVLGEDTYERTLVVDGesaTIILLDMWENKGENEW--LHDHCMQVGDAYLIV 155
Cdd:cd04130    4 VLVGDGAVGKTSL--IVSYTTNGYPTEYVPTAFDNFSVVVLVDG---KPVRLQLCDTAGQDEFdkLRPLCYPDTDVFLLC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 156 YSITDRASFEKASELRIQLRRARQTEdIPIILVGNKSDLV----------RCREVSVSEGRACAV---VFDCKFIETSAA 222
Cdd:cd04130   79 FSVVNPSSFQNISEKWIPEIRKHNPK-APIILVGTQADLRtdvnvliqlaRYGEKPVSQSRAKALaekIGACEYIECSAL 157
                        170
                 ....*....|
gi 160298187 223 VQHNVKELFE 232
Cdd:cd04130  158 TQKNLKEVFD 167
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
76-246 2.72e-13

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 66.54  E-value: 2.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  76 RVVLIGEQGVGKSTLANIFAGVHDSMDSDCEVLGEDTYERTLVVDGESATIILLDMwenKGENE----------WLHDHc 145
Cdd:COG1100    5 KIVVVGTGGVGKTSLVNRLVGDIFSLEKYLSTNGVTIDKKELKLDGLDVDLVIWDT---PGQDEfretrqfyarQLTGA- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 146 mqvgDAYLIVYSITDRASFEKASELRIQLRRARqtEDIPIILVGNKSDLVRCREVsVSEGRACAVVFDCKF---IETSAA 222
Cdd:COG1100   81 ----SLYLFVVDGTREETLQSLYELLESLRRLG--KKSPIILVLNKIDLYDEEEI-EDEERLKEALSEDNIvevVATSAK 153
                        170       180
                 ....*....|....*....|....
gi 160298187 223 VQHNVKELFEGIVRQVRLRRDSKE 246
Cdd:COG1100  154 TGEGVEELFAALAEILRGEGDSLD 177
RJL cd04119
Rab GTPase family J-like (RabJ-like); RJLs are found in many protists and as chimeras with ...
150-238 2.79e-13

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: 66.61  E-value: 2.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 150 DAYLIVYSITDRASFEKAS----ELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQH 225
Cdd:cd04119   74 QGVLLVYDVTDRQSFEALDswlkEMKQEGGPHGNMENIVVVVCANKIDLTKHRAVSEDEGRLWAESKGFKYFETSACTGE 153
                         90
                 ....*....|...
gi 160298187 226 NVKELFEGIVRQV 238
Cdd:cd04119  154 GVNEMFQTLFSSI 166
Rhes_like cd04143
Ras homolog enriched in striatum (Rhes) and activator of G-protein signaling 1 (Dexras1/AGS1); ...
75-232 3.02e-13

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


Pssm-ID: 133343 [Multi-domain]  Cd Length: 247  Bit Score: 67.85  E-value: 3.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFAGvhDSMDSDCEVLGEDTYERTLVVDGEsatIILLDMWENKGENEW--LHDHCMQVGDAY 152
Cdd:cd04143    1 YRMVVLGASKVGKTAIVSRFLG--GRFEEQYTPTIEDFHRKLYSIRGE---VYQLDILDTSGNHPFpaMRRLSILTGDVF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 153 LIVYSITDRASFEKASELRIQ--------LRRARQTEDIPIILVGNKSDLVRCREVSVSEGRAC-AVVFDCKFIETSAAV 223
Cdd:cd04143   76 ILVFSLDNRESFEEVCRLREQiletksclKNKTKENVKIPMVICGNKADRDFPREVQRDEVEQLvGGDENCAYFEVSAKK 155

                 ....*....
gi 160298187 224 QHNVKELFE 232
Cdd:cd04143  156 NSNLDEMFR 164
Rab4 cd04113
Rab GTPase family 4 (Rab4); Rab4 subfamily. Rab4 has been implicated in numerous functions ...
75-238 4.71e-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: 4.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFagVHDSMDSDCE-VLGEDTYERTLVVDGESatiILLDMWENKGENEWlhdhcMQVGDAY- 152
Cdd:cd04113    1 FKFLIIGSAGTGKSCLLHQF--IENKFKQDSNhTIGVEFGSRVVNVGGKS---VKLQIWDTAGQERF-----RSVTRSYy 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 153 ------LIVYSITDRASFEKASELrIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHN 226
Cdd:cd04113   71 rgaagaLLVYDITSRESFNALTNW-LTDARTLASPDIVIILVGNKKDLEDDREVTFLEASRFAQENGLLFLETSALTGEN 149
                        170
                 ....*....|..
gi 160298187 227 VKELFEGIVRQV 238
Cdd:cd04113  150 VEEAFLKCARSI 161
Rab33B_Rab33A cd04115
Rab GTPase family 33 includes Rab33A and Rab33B; Rab33B/Rab33A subfamily. Rab33B is ...
75-221 1.15e-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: 64.77  E-value: 1.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFAGvHDSMDSDCEVLGEDTYERTLVVDGESatiILLDMWENKGENEWLH---DHCMQVGDA 151
Cdd:cd04115    3 FKIIVIGDSNVGKTCLTYRFCA-GRFPERTEATIGVDFRERTVEIDGER---IKVQLWDTAGQERFRKsmvQHYYRNVHA 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 152 YLIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSA 221
Cdd:cd04115   79 VVFVYDVTNMASFHSLPSWIEECEQHSLPNEVPRILVGNKCDLREQIQVPTDLAQRFADAHSMPLFETSA 148
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
74-236 1.61e-12

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: 64.32  E-value: 1.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187   74 YYRVVLIGEQGVGKSTLANIFAGVHDSMDSDCEVLGEDTYERTLVVDGESATIILLDMwenKGENEW--LHDHCMQVGDA 151
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYVTTVIEEDGKTYKFNLLDT---AGQEDYdaIRRLYYPQVER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  152 YLIVYSITDRA-SFEKASEL-RIQLRRARqTEDIPIILVGNKSDLvRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKE 229
Cdd:TIGR00231  78 SLRVFDIVILVlDVEEILEKqTKEIIHHA-DSGVPIILVGNKIDL-KDADLKTHVASEFAKLNGEPIIPLSAETGKNIDS 155

                  ....*..
gi 160298187  230 LFEGIVR 236
Cdd:TIGR00231 156 AFKIVEA 162
Rab30 cd04114
Rab GTPase family 30 (Rab30); Rab30 subfamily. Rab30 appears to be associated with the Golgi ...
75-234 5.53e-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: 62.99  E-value: 5.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFA-GVHDSMDSdcEVLGEDTYERTLVVDGESatiILLDMWENKGENEW--LHDHCMQVGDA 151
Cdd:cd04114    8 FKIVLIGNAGVGKTCLVRRFTqGLFPPGQG--ATIGVDFMIKTVEIKGEK---IKLQIWDTAGQERFrsITQSYYRSANA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 152 YLIVYSITDRASFEKASELriqLRRARQ--TEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKE 229
Cdd:cd04114   83 LILTYDITCEESFRCLPEW---LREIEQyaNNKVITILVGNKIDLAERREVSQQRAEEFSDAQDMYYLETSAKESDNVEK 159

                 ....*
gi 160298187 230 LFEGI 234
Cdd:cd04114  160 LFLDL 164
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
76-193 1.01e-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: 60.60  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187   76 RVVLIGEQGVGKSTLANIFagVHDSMDSDCE-VLGEDTYERTLVVDGESATIILLDMWENKGENEW--LHDHCMQVGDAY 152
Cdd:pfam08477   1 KVVLLGDSGVGKTSLLKRF--VDDTFDPKYKsTIGVDFKTKTVLENDDNGKKIKLNIWDTAGQERFrsLHPFYYRGAAAA 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 160298187  153 LIVYsitDRASFEKaseLRIQLRRARQ-TEDIPIILVGNKSD 193
Cdd:pfam08477  79 LLVY---DSRTFSN---LKYWLRELKKyAGNSPVILVGNKID 114
RHO smart00174
Rho (Ras homology) subfamily of Ras-like small GTPases; Members of this subfamily of Ras-like ...
77-238 1.05e-11

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: 62.25  E-value: 1.05e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187    77 VVLIGEQGVGKSTLANIFAgvhdsmdSDC-------EVLgeDTYERTLVVDGEsatIILLDMWENKGENEW--LHDHCMQ 147
Cdd:smart00174   1 LVVVGDGAVGKTCLLIVYT-------TNAfpedyvpTVF--ENYSADVEVDGK---PVELGLWDTAGQEDYdrLRPLSYP 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187   148 VGDAYLIVYSITDRASFEKAS-----ELRiqlrraRQTEDIPIILVGNKSDL----------VRCREVSVSEGRACAVVF 212
Cdd:smart00174  69 DTDVFLICFSVDSPASFENVKekwypEVK------HFCPNVPIILVGTKLDLrndkstleelSKKKQEPVTYEQGQALAK 142
                          170       180
                   ....*....|....*....|....*....
gi 160298187   213 D---CKFIETSAAVQHNVKELFEGIVRQV 238
Cdd:smart00174 143 RigaVKYLECSALTQEGVREVFEEAIRAA 171
Rab27A cd04127
Rab GTPase family 27a (Rab27a); The Rab27a subfamily consists of Rab27a and its highly ...
80-241 1.26e-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: 62.13  E-value: 1.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  80 IGEQGVGKSTLA-----NIFAGVHDSmdsdceVLGEDTYERTLVVDGES-------ATIILLDMWENKGENEWLHDHCMQ 147
Cdd:cd04127   10 LGDSGVGKTTFLyrytdNKFNPKFIT------TVGIDFREKRVVYNSQGpdgtsgkAFRVHLQLWDTAGQERFRSLTTAF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 148 VGDA--YLIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQH 225
Cdd:cd04127   84 FRDAmgFLLMFDLTSEQSFLNVRNWMSQLQAHAYCENPDIVLIGNKADLPDQREVSERQARELADKYGIPYFETSAATGQ 163
                        170
                 ....*....|....*.
gi 160298187 226 NVKELFEGIVRQVRLR 241
Cdd:cd04127  164 NVEKAVETLLDLIMKR 179
Rab15 cd04117
Rab GTPase family 15 (Rab15); Rab15 colocalizes with the transferrin receptor in early ...
75-241 1.29e-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: 61.92  E-value: 1.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFAGvHDSMDSDCEVLGEDTYERTLVVDGESATIillDMWENKGENEW--LHDHCMQVGDAY 152
Cdd:cd04117    1 FRLLLIGDSGVGKTCLLCRFTD-NEFHSSHISTIGVDFKMKTIEVDGIKVRI---QIWDTAGQERYqtITKQYYRRAQGI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 153 LIVYSITDRASFEK----ASELRiqlrrARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVK 228
Cdd:cd04117   77 FLVYDISSERSYQHimkwVSDVD-----EYAPEGVQKILIGNKADEEQKRQVGDEQGNKLAKEYGMDFFETSACTNKNIK 151
                        170
                 ....*....|...
gi 160298187 229 ELFEGIvRQVRLR 241
Cdd:cd04117  152 ESFTRL-TELVLQ 163
Rab14 cd04122
Rab GTPase family 14 (Rab14); Rab14 GTPases are localized to biosynthetic compartments, ...
75-238 1.38e-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: 61.78  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFAgvHDSMDSDC-EVLGEDTYERTLVVDGESatiILLDMWENKGENEWlhdhcMQVGDAY- 152
Cdd:cd04122    3 FKYIIIGDMGVGKSCLLHQFT--EKKFMADCpHTIGVEFGTRIIEVNGQK---IKLQIWDTAGQERF-----RAVTRSYy 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 153 ------LIVYSITDRASFEKASELrIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHN 226
Cdd:cd04122   73 rgaagaLMVYDITRRSTYNHLSSW-LTDARNLTNPNTVIFLIGNKADLEAQRDVTYEEAKQFADENGLLFLECSAKTGEN 151
                        170
                 ....*....|..
gi 160298187 227 VKELFEGIVRQV 238
Cdd:cd04122  152 VEDAFLETAKKI 163
Rab26 cd04112
Rab GTPase family 26 (Rab26); Rab26 subfamily. First identified in rat pancreatic acinar cells, ...
75-241 1.83e-11

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: 61.81  E-value: 1.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFAGVHDSMDSDCEVLGEDTYERTLVVDGesaTIILLDMWENKGENEWlhdhcMQVGDAY-- 152
Cdd:cd04112    1 FKVMLVGDSGVGKTCLLVRFKDGAFLAGSFIATVGIQFTNKVVTVDG---VKVKLQIWDTAGQERF-----RSVTHAYyr 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 153 -----LIVYSITDRASFEKASELRIQLRRARQtEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNV 227
Cdd:cd04112   73 dahalLLLYDVTNKSSFDNIRAWLTEILEYAQ-SDVVIMLLGNKADMSGERVVKREDGERLAKEYGVPFMETSAKTGLNV 151
                        170
                 ....*....|....
gi 160298187 228 KELFEGIVRQVRLR 241
Cdd:cd04112  152 ELAFTAVAKELKHR 165
Rab23_like cd04106
Rab GTPase family 23 (Rab23)-like; Rab23-like subfamily. Rab23 is a member of the Rab family ...
76-232 6.71e-11

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: 59.76  E-value: 6.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  76 RVVLIGEQGVGKSTLANIFAGvHDSMDSDCEVLGEDTYERTLVVDGESATIILLdMWENKGENEW--LHDHCMQVGDAYL 153
Cdd:cd04106    2 KVIVVGNGNVGKSSMIQRFVK-GIFTKDYKKTIGVDFLEKQIFLRQSDEDVRLM-LWDTAGQEEFdaITKAYYRGAQACI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 154 IVYSITDRASFEKASELRiqlRRA-RQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFE 232
Cdd:cd04106   80 LVFSTTDRESFEAIESWK---EKVeAECGDIPMVLVQTKIDLLDQAVITNEEAEALAKRLQLPLFRTSVKDDFNVTELFE 156
RRP22 cd04142
Ras-related protein on chromosome 22 (RRP22) family; RRP22 (Ras-related protein on chromosome ...
75-242 1.16e-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: 59.88  E-value: 1.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKST-----LANIFAGVHDSMDsdcevlGEDTYERTLVVDGESATIILLDM-----WENKGENEWLHDH 144
Cdd:cd04142    1 VRVAVLGAPGVGKTAivrqfLAQEFPEEYIPTE------HRRLYRPAVVLSGRVYDLHILDVpnmqrYPGTAGQEWMDPR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 145 C--MQVGDAYLIVYSITDRASFEKASELRIQLRRARQ--TEDIPIILVGNKSDLVRCRevsVSEGRACAVV----FDCKF 216
Cdd:cd04142   75 FrgLRNSRAFILVYDICSPDSFHYVKLLRQQILETRPagNKEPPIVVVGNKRDQQRHR---FAPRHVLSVLvrksWKCGY 151
                        170       180
                 ....*....|....*....|....*.
gi 160298187 217 IETSAAVQHNVKELFEGIVRQVRLRR 242
Cdd:cd04142  152 LECSAKYNWHILLLFKELLISATTRG 177
Centaurin_gamma cd04103
Centaurin gamma (CENTG) GTPase; The centaurins (alpha, beta, gamma, and delta) are large, ...
113-238 6.28e-10

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: 56.73  E-value: 6.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 113 YERTLVVDGESATIILLDmwenkgENEWLHDHCMQVGDAYLIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKS 192
Cdd:cd04103   36 FKKEVLVDGQSHLLLIRD------EGGAPDAQFAGWVDAVIFVFSLEDEASFQTVYRLYHQLSSYRNISEIPLILVGTQD 109
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 160298187 193 DL--VRCREVSVSEGRA-CAVVFDCKFIETSAAVQHNVKELFEGIVRQV 238
Cdd:cd04103  110 AIsaSNPRVIDDARARQlCADMKRCSYYETCATYGLNVERVFQEAAQKI 158
Rab3 cd01865
Rab GTPase family 3 contains Rab3A, Rab3B, Rab3C and Rab3D; The Rab3 subfamily contains Rab3A, ...
75-235 8.01e-10

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: 56.84  E-value: 8.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLanIFAGVHDSMDSdcevlgedTYERTLVVDGESATI------ILLDMWENKGENEW--LHDHCM 146
Cdd:cd01865    2 FKLLIIGNSSVGKTSF--LFRYADDSFTS--------AFVSTVGIDFKVKTVyrndkrIKLQIWDTAGQERYrtITTAYY 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 147 QVGDAYLIVYSITDRASFEKASELRIQLRrARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHN 226
Cdd:cd01865   72 RGAMGFILMYDITNEESFNAVQDWSTQIK-TYSWDNAQVILVGNKCDMEDERVVSAERGRQLADQLGFEFFEASAKENIN 150

                 ....*....
gi 160298187 227 VKELFEGIV 235
Cdd:cd01865  151 VKQVFERLV 159
Rab12 cd04120
Rab GTPase family 12 (Rab12); Rab12 was first identified in canine cells, where it was ...
76-262 2.24e-09

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: 56.17  E-value: 2.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  76 RVVLIGEQGVGKSTLANIFAGvhdsmDSDCEV----LGEDTYERTLVVDGESatiILLDMWENKGENEWlhdhcMQVGDA 151
Cdd:cd04120    2 QVIIIGSRGVGKTSLMERFTD-----DTFCEAckstVGVDFKIKTVELRGKK---IRLQIWDTAGQERF-----NSITSA 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 152 Y-------LIVYSITDRASFEKASELrIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEG-RACAVVFDCKFIETSAAV 223
Cdd:cd04120   69 YyrsakgiILVYDITKKETFDDLPKW-MKMIDKYASEDAELLLVGNKLDCETDREITRQQGeKFAQQITGMRFCEASAKD 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 160298187 224 QHNVKELF----EGIVRQVRLRRDSKEKNERRLAYQKRRESIP 262
Cdd:cd04120  148 NFNVDEIFlklvDDILKKMPLDILRNELSNSILSLQPEPEIPP 190
Rab35 cd04110
Rab GTPase family 35 (Rab35); Rab35 is one of several Rab proteins to be found to participate ...
75-251 2.62e-09

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: 56.02  E-value: 2.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLA-----NIFAGvhdsmdSDCEVLGEDTYERTLVVDGESatiILLDMWENKGENEWlhdhcMQVG 149
Cdd:cd04110    7 FKLLIIGDSGVGKSSLLlrfadNTFSG------SYITTIGVDFKIRTVEINGER---VKLQIWDTAGQERF-----RTIT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 150 DAY-------LIVYSITDRASFekaSELRIQLRRARQT-EDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSA 221
Cdd:cd04110   73 STYyrgthgvIVVYDVTNGESF---VNVKRWLQEIEQNcDDVCKVLVGNKNDDPERKVVETEDAYKFAGQMGISLFETSA 149
                        170       180       190
                 ....*....|....*....|....*....|
gi 160298187 222 AVQHNVKELFEGIVRQVRLRRDSKEKNERR 251
Cdd:cd04110  150 KENINVEEMFNCITELVLRAKKDNLAKQQQ 179
Rab28 cd04109
Rab GTPase family 28 (Rab28); Rab28 subfamily. First identified in maize, Rab28 has been shown ...
75-238 2.96e-09

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: 55.96  E-value: 2.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFAgvHDSMD-SDCEVLGEDTYERTLVVDGESAtiILLDMWENKGEN---EWLhDHCMQVGD 150
Cdd:cd04109    1 IKIVVLGDGASGKTSLIRRFA--QEGFGkSYKQTIGLDFFSRRITLPGSLN--VTLQVWDIGGQQiggKML-DKYIYGAQ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 151 AYLIVYSITDRASFEKASELRIQLRRARQTEDIP--IILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVK 228
Cdd:cd04109   76 AVCLVYDITNSQSFENLEDWLSVVKKVNEESETKpkMVLVGNKTDLEHNRQVTAEKHARFAQENDMESIFVSAKTGDRVF 155
                        170
                 ....*....|
gi 160298187 229 ELFEGIVRQV 238
Cdd:cd04109  156 LCFQRIAAEL 165
Rac1_like cd01871
Ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1)-like ...
76-238 3.63e-09

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: 55.20  E-value: 3.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  76 RVVLIGEQGVGKSTL-----ANIFAGvhdsmdsdcEVLGE--DTYERTLVVDGESatiILLDMWENKGENEW--LHDHCM 146
Cdd:cd01871    3 KCVVVGDGAVGKTCLlisytTNAFPG---------EYIPTvfDNYSANVMVDGKP---VNLGLWDTAGQEDYdrLRPLSY 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 147 QVGDAYLIVYSITDRASFEKASElRIQLRRARQTEDIPIILVGNKSDL-------VRCRE-----VSVSEGRACAV-VFD 213
Cdd:cd01871   71 PQTDVFLICFSLVSPASFENVRA-KWYPEVRHHCPNTPIILVGTKLDLrddkdtiEKLKEkkltpITYPQGLAMAKeIGA 149
                        170       180
                 ....*....|....*....|....*
gi 160298187 214 CKFIETSAAVQHNVKELFEGIVRQV 238
Cdd:cd01871  150 VKYLECSALTQRGLKTVFDEAIRAV 174
RabL2 cd04124
Rab GTPase-like family 2 (Rab-like2); RabL2 (Rab-like2) subfamily. RabL2s are novel Rab ...
76-236 1.74e-08

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: 52.94  E-value: 1.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  76 RVVLIGEQGVGKSTLANIFAgvhdsMDsDCEVLGEDTYERTL-----VVDGESatiILLDMWENKGENEW--LHDHCMQV 148
Cdd:cd04124    2 KIILLGDSAVGKSKLVERFL-----MD-GYEPQQLSTYALTLykhnaKFEGKT---ILVDFWDTAGQERFqtMHASYYHK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 149 GDAYLIVYSITDRASFEKASELRIQLRRARqtEDIPIILVGNKSDLvrcrEVSVSE-GRACAVVFDCKFIETSAAVQHNV 227
Cdd:cd04124   73 AHACILVFDVTRKITYKNLSKWYEELREYR--PEIPCIVVANKIDL----DPSVTQkKFNFAEKHNLPLYYVSAADGTNV 146

                 ....*....
gi 160298187 228 KELFEGIVR 236
Cdd:cd04124  147 VKLFQDAIK 155
Rop_like cd04133
Rho-related protein from plants (Rop)-like; The Rop (Rho-related protein from plants) ...
78-239 2.11e-08

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: 52.93  E-value: 2.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  78 VLIGEQGVGKSTLANIFAGVHDSMDSDCEVLgeDTYERTLVVDGesaTIILLDMWENKGENEW--LHDHCMQVGDAYLIV 155
Cdd:cd04133    5 VTVGDGAVGKTCMLISYTSNTFPTDYVPTVF--DNFSANVVVDG---NTVNLGLWDTAGQEDYnrLRPLSYRGADVFLLA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 156 YSITDRASFEKASELRI-QLRRArqTEDIPIILVGNKSDLVRCRE--------VSVSEGRACAVVFD---CKFIETSAAV 223
Cdd:cd04133   80 FSLISKASYENVLKKWIpELRHY--APGVPIVLVGTKLDLRDDKQffadhpgaVPITTAQGEELRKQigaAAYIECSSKT 157
                        170
                 ....*....|....*.
gi 160298187 224 QHNVKELFEGIVRQVR 239
Cdd:cd04133  158 QQNVKAVFDAAIKVVL 173
Rab40 cd04121
Rab GTPase family 40 (Rab40) contains Rab40a, Rab40b and Rab40c; The Rab40 subfamily contains ...
76-241 2.91e-08

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: 52.63  E-value: 2.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  76 RVVLIGEQGVGK-STLANIFAGVHDSMDSDCevLGEDTYERTLVVDGESatiILLDMWENKGENEW--LHDHCMQVGDAY 152
Cdd:cd04121    8 KFLLVGDSDVGKgEILASLQDGSTESPYGYN--MGIDYKTTTILLDGRR---VKLQLWDTSGQGRFctIFRSYSRGAQGI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 153 LIVYSITDRASFEKASelriqlRRARQTED----IPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVK 228
Cdd:cd04121   83 ILVYDITNRWSFDGID------RWIKEIDEhapgVPKILVGNRLHLAFKRQVATEQAQAYAERNGMTFFEVSPLCNFNIT 156
                        170
                 ....*....|...
gi 160298187 229 ELFEGIVRQVRLR 241
Cdd:cd04121  157 ESFTELARIVLMR 169
Rab24 cd04118
Rab GTPase family 24 (Rab24); Rab24 is distinct from other Rabs in several ways. It exists ...
76-234 6.46e-08

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: 51.79  E-value: 6.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  76 RVVLIGEQGVGKSTLANIFagVHDS-MDSDCE-VLGEDTYERTLVVDGesaTIILLDMWENKGENEWlhdHCMQV----- 148
Cdd:cd04118    2 KVVMLGKESVGKTSLVERY--VHHRfLVGPYQnTIGAAFVAKRMVVGE---RVVTLGIWDTAGSERY---EAMSRiyyrg 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 149 GDAYLIVYSITDRASFEKASELRIQLRRARqtEDIPIILVGNKSDLV----RCREVSVSEGRACAVVFDCKFIETSAAVQ 224
Cdd:cd04118   74 AKAAIVCYDLTDSSSFERAKFWVKELQNLE--EHCKIYLCGTKSDLIeqdrSLRQVDFHDVQDFADEIKAQHFETSSKTG 151
                        170
                 ....*....|
gi 160298187 225 HNVKELFEGI 234
Cdd:cd04118  152 QNVDELFQKV 161
Rab32_Rab38 cd04107
Rab GTPase families 18 (Rab18) and 32 (Rab32); Rab38/Rab32 subfamily. Rab32 and Rab38 are ...
75-238 1.30e-07

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: 51.16  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLANIFagVHDSMDSDCEV-LGEDTYERTLVVDgeSATIILLDMWENKGenewlHDHCMQVGDAY- 152
Cdd:cd04107    1 FKVLVIGDLGVGKTSIIKRY--VHGVFSQHYKAtIGVDFALKVIEWD--PNTVVRLQLWDIAG-----QERFGGMTRVYy 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 153 ------LIVYSITDRASFEKASELRIQLRRARQTED---IPIILVGNKSDLVRCREvSVSEGRACAVVFDCKFI---ETS 220
Cdd:cd04107   72 kgavgaIIVFDVTRPSTFEAVLKWKADLDSKVTLPNgepIPALLLANKCDLKKERL-AKDPEQMDQFCKENGFIgwfETS 150
                        170
                 ....*....|....*...
gi 160298187 221 AAVQHNVKELFEGIVRQV 238
Cdd:cd04107  151 AKENINIEEAMRFLVKNI 168
Rho4_like cd04132
Ras homology family 4 (Rho4) of small guanosine triphosphatases (GTPases)-like; Rho4 is a ...
76-251 5.47e-07

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: 49.26  E-value: 5.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  76 RVVLIGEQGVGKSTLANIFAgvHDSMDSDCEVLGEDTYERTLVVdgESATIILLDMWENKGENEW--LHDHCMQVGDAYL 153
Cdd:cd04132    5 KIVVVGDGGCGKTCLLMVYA--QGSFPEEYVPTVFENYVTTLQV--PNGKIIELALWDTAGQEDYdrLRPLSYPDVDVIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 154 IVYSITDRASFEKaselrIQLRRARQT----EDIPIILVGNKSDLVRCRE------------VSVSEG-RACAVVFDCKF 216
Cdd:cd04132   81 ICYSVDNPTSLDN-----VEDKWYPEVnhfcPGTPIVLVGLKTDLRKDKNsvsklraqglepVTPEQGeSVAKSIGAVAY 155
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 160298187 217 IETSAAVQHNVKELFEGIVRQVrLRRDSKEKNERR 251
Cdd:cd04132  156 IECSAKLMENVDEVFDAAINVA-LSKSGRAARKKK 189
RhoG cd01875
Ras homolog family, member G (RhoG) of small guanosine triphosphatases (GTPases); RhoG is a ...
76-238 1.05e-06

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: 48.08  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  76 RVVLIGEQGVGKSTLANIFAGVHDSMDSDCEVLgeDTYERTLVVDGESATiilLDMWENKGENEW--LHDHCMQVGDAYL 153
Cdd:cd01875    5 KCVVVGDGAVGKTCLLICYTTNAFPKEYIPTVF--DNYSAQTAVDGRTVS---LNLWDTAGQEEYdrLRTLSYPQTNVFI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 154 IVYSITDRASFEKASElRIQLRRARQTEDIPIILVGNKSDL-------VRCREVSVS-----EGRACA-VVFDCKFIETS 220
Cdd:cd01875   80 ICFSIASPSSYENVRH-KWHPEVCHHCPNVPILLVGTKKDLrndadtlKKLKEQGQApitpqQGGALAkQIHAVKYLECS 158
                        170
                 ....*....|....*...
gi 160298187 221 AAVQHNVKELFEGIVRQV 238
Cdd:cd01875  159 ALNQDGVKEVFAEAVRAV 176
Rho2 cd04129
Ras homology family 2 (Rho2) of small guanosine triphosphatases (GTPases); Rho2 is a fungal ...
76-248 1.12e-06

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: 47.91  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  76 RVVLIGEQGVGKSTLANIFAGVHDSMDSDCEVLgeDTYERTLVVDGESatiILLDMWENKGENEWLHDHCMQVGDAY--L 153
Cdd:cd04129    3 KLVIVGDGACGKTSLLYVFTLGEFPEEYHPTVF--ENYVTDCRVDGKP---VQLALWDTAGQEEYERLRPLSYSKAHviL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 154 IVYSITDRASFEKASELRIQLRRaRQTEDIPIILVGNKSDLvrcREVSVSEG--------------RACAVVFDCKFIET 219
Cdd:cd04129   78 IGFAIDTPDSLENVRTKWIEEVR-RYCPNVPVILVGLKKDL---RQEAVAKGnyatdefvpiqqakLVARAIGAKKYMEC 153
                        170       180
                 ....*....|....*....|....*....
gi 160298187 220 SAAVQHNVKELFEGIVRQVRLRRDSKEKN 248
Cdd:cd04129  154 SALTGEGVDDVFEAATRAALLVRKSGKEE 182
Spg1 cd04128
Septum-promoting GTPase (Spg1); Spg1p. Spg1p (septum-promoting GTPase) was first identified in ...
76-238 6.03e-06

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: 45.85  E-value: 6.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  76 RVVLIGEQGVGKSTLANIFagVHDSMDSD-CEVLGEDTYERTLVVDGesaTIILLDMWENKGENEWLHDHCMQVGDAYLI 154
Cdd:cd04128    2 KIGLLGDAQIGKTSLMVKY--VEGEFDEEyIQTLGVNFMEKTISIRG---TEITFSIWDLGGQREFINMLPLVCKDAVAI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 155 VY--SITDRASFEKASELRIQLRRARQTEdIPiILVGNKSDLVR-----CREVSVSEGRACAVVFDCKFIETSAAVQHNV 227
Cdd:cd04128   77 LFmfDLTRKSTLNSIKEWYRQARGFNKTA-IP-ILVGTKYDLFAdlppeEQEEITKQARKYAKAMKAPLIFCSTSHSINV 154
                        170
                 ....*....|.
gi 160298187 228 KELFEGIVRQV 238
Cdd:cd04128  155 QKIFKFVLAKV 165
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
78-238 3.84e-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: 43.00  E-value: 3.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  78 VLIGEQGVGKSTLANIFAGVHDSMDSDceVLGE--DTYERTLVVDGEsATIIL-----LDMWENKGE--NEWLHDHCMQV 148
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVGIVSP--IPGTtrDPVRKEWELLPL-GPVVLidtpgLDEEGGLGRerVEEARQVADRA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 149 gDAYLIVYSITdrasfEKASELRIQLRRARQTEdIPIILVGNKSDLVRCREVSVSEGRAC-AVVFDCKFIETSAAVQHNV 227
Cdd:cd00880   78 -DLVLLVVDSD-----LTPVEEEAKLGLLRERG-KPVLLVLNKIDLVPESEEEELLRERKlELLPDLPVIAVSALPGEGI 150
                        170
                 ....*....|.
gi 160298187 228 KELFEGIVRQV 238
Cdd:cd00880  151 DELRKKIAELL 161
RAN smart00176
Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases; Ran is involved in the ...
80-238 3.99e-05

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: 43.85  E-value: 3.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187    80 IGEQGVGKSTlaniFAGVHDSMDSdcevlgEDTYERTLVVDGESATI------ILLDMWENKGENEW--LHDHCMQVGDA 151
Cdd:smart00176   1 VGDGGTGKTT----FVKRHLTGEF------EKKYVATLGVEVHPLVFhtnrgpIRFNVWDTAGQEKFggLRDGYYIQGQC 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187   152 YLIVYSITDRASFEKASELRIQLrrARQTEDIPIILVGNKSDlVRCREVsvsegRACAVVF----DCKFIETSAAVQHNV 227
Cdd:smart00176  71 AIIMFDVTARVTYKNVPNWHRDL--VRVCENIPIVLCGNKVD-VKDRKV-----KAKSITFhrkkNLQYYDISAKSNYNF 142
                          170
                   ....*....|.
gi 160298187   228 KELFEGIVRQV 238
Cdd:smart00176 143 EKPFLWLARKL 153
RhoA_like cd01870
Ras homology family A (RhoA)-like includes RhoA, RhoB and RhoC; The RhoA subfamily consists of ...
76-232 4.03e-05

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: 43.19  E-value: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  76 RVVLIGEQGVGKSTLANIFagvhdSMDSDCEVLGE---DTYERTLVVDGESatiILLDMWENKGENEW--LHDHCMQVGD 150
Cdd:cd01870    3 KLVIVGDGACGKTCLLIVF-----SKDQFPEVYVPtvfENYVADIEVDGKQ---VELALWDTAGQEDYdrLRPLSYPDTD 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 151 AYLIVYSITDRASFEKASELRIQLRRaRQTEDIPIILVGNKSDL------------VRCREVSVSEGRACAVVFDC-KFI 217
Cdd:cd01870   75 VILMCFSIDSPDSLENIPEKWTPEVK-HFCPNVPIILVGNKKDLrndehtirelakMKQEPVKPEEGRAMAEKIGAfGYL 153
                        170
                 ....*....|....*
gi 160298187 218 ETSAAVQHNVKELFE 232
Cdd:cd01870  154 ECSAKTKEGVREVFE 168
Ran cd00877
Ras-related nuclear proteins (Ran)/TC4 family of small GTPases; Ran GTPase is involved in ...
75-237 4.29e-05

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: 43.06  E-value: 4.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTLAN-IFAGVHdsmdsdcevlgEDTYERTLVVDGESATI------ILLDMWENKGENEW--LHDHC 145
Cdd:cd00877    1 FKLVLVGDGGTGKTTFVKrHLTGEF-----------EKKYVATLGVEVHPLDFhtnrgkIRFNVWDTAGQEKFggLRDGY 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 146 MQVGDAYLIVYSITDRASFEKASELRIQLRRARqtEDIPIILVGNKSDlVRCREVsvsegRACAVVFD----CKFIETSA 221
Cdd:cd00877   70 YIQGQCAIIMFDVTSRVTYKNVPNWHRDLVRVC--ENIPIVLCGNKVD-IKDRKV-----KPKQITFHrkknLQYYEISA 141
                        170
                 ....*....|....*.
gi 160298187 222 AVQHNVKELFEGIVRQ 237
Cdd:cd00877  142 KSNYNFEKPFLWLARK 157
PLN03071 PLN03071
GTP-binding nuclear protein Ran; Provisional
75-231 6.82e-05

GTP-binding nuclear protein Ran; Provisional


Pssm-ID: 178620 [Multi-domain]  Cd Length: 219  Bit Score: 43.20  E-value: 6.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTlaniFAGVHDSMDSdcevlgEDTYERTLVVDgesatIILLDMWENKGE---NEW----------L 141
Cdd:PLN03071  14 FKLVIVGDGGTGKTT----FVKRHLTGEF------EKKYEPTIGVE-----VHPLDFFTNCGKirfYCWdtagqekfggL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 142 HDHCMQVGDAYLIVYSITDRASFEKASELRIQLRRArqTEDIPIILVGNKSDlVRCREVsvsegRACAVVFDCK----FI 217
Cdd:PLN03071  79 RDGYYIHGQCAIIMFDVTARLTYKNVPTWHRDLCRV--CENIPIVLCGNKVD-VKNRQV-----KAKQVTFHRKknlqYY 150
                        170
                 ....*....|....
gi 160298187 218 ETSAAVQHNVKELF 231
Cdd:PLN03071 151 EISAKSNYNFEKPF 164
PTZ00132 PTZ00132
GTP-binding nuclear protein Ran; Provisional
75-200 1.53e-04

GTP-binding nuclear protein Ran; Provisional


Pssm-ID: 240284 [Multi-domain]  Cd Length: 215  Bit Score: 41.99  E-value: 1.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  75 YRVVLIGEQGVGKSTlaniFAGVHdsmdsdceVLGE--DTYERTLVVDGESATI------ILLDMWENKGENEW--LHDH 144
Cdd:PTZ00132  10 FKLILVGDGGVGKTT----FVKRH--------LTGEfeKKYIPTLGVEVHPLKFytncgpICFNVWDTAGQEKFggLRDG 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 160298187 145 CMQVGDAYLIVYSITDRASFEKASELRIQLRRArqTEDIPIILVGNKSDlVRCREV 200
Cdd:PTZ00132  78 YYIKGQCAIIMFDVTSRITYKNVPNWHRDIVRV--CENIPIVLVGNKVD-VKDRQV 130
Rnd cd04131
Rho family GTPase subfamily Rnd includes Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8; The Rnd ...
76-232 1.91e-04

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: 41.26  E-value: 1.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  76 RVVLIGEQGVGKSTLANIFAgvHDSMDSDCEVLGEDTYERTLVVDGESatiILLDMWENKGENEWlhDH----CMQVGDA 151
Cdd:cd04131    3 KIVLVGDSQCGKTALLQVFA--KDSFPENYVPTVFENYTASFEVDKQR---IELSLWDTSGSPYY--DNvrplSYPDSDA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 152 YLIVYSITDRASFEKASE-LRIQLRRArqTEDIPIILVGNKSDL------------VRCREVSVSEGRA-----CAVVfd 213
Cdd:cd04131   76 VLICFDISRPETLDSVLKkWKGEVREF--CPNTPVLLVGCKSDLrtdlstltelsnKRQIPVSHEQGRNlakqiGAAA-- 151
                        170       180
                 ....*....|....*....|
gi 160298187 214 ckFIETSAAVQHN-VKELFE 232
Cdd:cd04131  152 --YVECSAKTSENsVRDVFE 169
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
76-191 1.78e-03

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: 37.21  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187   76 RVVLIGEQGVGKSTLANIFAG----VHDsmdsdceVLGE--DTYERTLVVDGESatIILLD---MWENKGENEWLHDHCM 146
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGakaiVSD-------YPGTtrDPNEGRLELKGKQ--IILVDtpgLIEGASEGEGLGRAFL 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 160298187  147 QVGDAYLIVYsITDRAsfEKASELRIQLRRARQTEDIPIILVGNK 191
Cdd:pfam01926  72 AIIEADLILF-VVDSE--EGITPLDEELLELLRENKKPIILVLNK 113
YeeP COG3596
Predicted GTPase [General function prediction only];
76-270 1.90e-03

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 39.36  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  76 RVVLIGEQGVGKSTLANIFAGVhdsmdSDCEV-LGEDTYERTLVVDGESA---TIILLDMW------ENKGENEWLHDhc 145
Cdd:COG3596   41 VIALVGKTGAGKSSLINALFGA-----EVAEVgVGRPCTREIQRYRLESDglpGLVLLDTPglgevnERDREYRELRE-- 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187 146 mQVGDAYLIVY--SITDRASfekASELRIQLRRARQTEDIPIILVGNKSDLVR-CRE-------------VSVSE----- 204
Cdd:COG3596  114 -LLPEADLILWvvKADDRAL---ATDEEFLQALRAQYPDPPVLVVLTQVDRLEpEREwdppynwpsppkeQNIRRaleai 189
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160298187 205 ----GRACAVVFDckfieTSAA---VQHNVKELFEGIV------RQVRLRRDSKEKNERRLAYQKRRESIPRKARRFWG 270
Cdd:COG3596  190 aeqlGVPIDRVIP-----VSAAedrTGYGLEELVDALAealpeaKRSRLARLLRAKAIDRYTLLAAAAALLAAALLALL 263
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
77-98 2.71e-03

First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 37.79  E-value: 2.71e-03
                         10        20
                 ....*....|....*....|..
gi 160298187  77 VVLIGEQGVGKSTLANIFAGVH 98
Cdd:cd03216   29 HALLGENGAGKSTLMKILSGLY 50
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
76-99 2.92e-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: 37.63  E-value: 2.92e-03
                          10        20
                  ....*....|....*....|....
gi 160298187   76 RVVLIGEQGVGKSTLANIFAGVHD 99
Cdd:pfam00005  13 ILALVGPNGAGKSTLLKLIAGLLS 36
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
76-117 4.12e-03

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 37.83  E-value: 4.12e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 160298187  76 RVVLIGEQGVGKSTLANIFAGVHDSMDSDCEVLGEDTYERTL 117
Cdd:cd03225   29 FVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSL 70
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
77-111 4.22e-03

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 37.84  E-value: 4.22e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 160298187  77 VVLIGEQGVGKSTLANIFAGVHDSMDSDCEVLGED 111
Cdd:PRK10584  39 IALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQP 73
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
77-262 5.18e-03

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 36.52  E-value: 5.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187   77 VVLIGEQGVGKSTLANIFAGVHdsmdsDCEVLGEDTYERTLVVDGESAtiILLDMWENKGENEWLHDHC---MQVGDAYL 153
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEEL-----GAVRLSSDDERKRLFGEGRPS--ISYYTDATDRTYERLHELAriaLRAGRPVI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298187  154 IVYSITDRasfekasELRIQLRRARQTEDIPIILVgnksdlvrcrevsvsegracavvfdckFIETSAAVqhnvkeLFEG 233
Cdd:pfam13671  75 LDATNLRR-------DERARLLALAREYGVPVRIV---------------------------VFEAPEEV------LRER 114
                         170       180
                  ....*....|....*....|....*....
gi 160298187  234 IVRQVRLRRDSKEKNERRLAYQKRRESIP 262
Cdd:pfam13671 115 LAARARAGGDPSDVPEEVLDRQKARFEPP 143
 
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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