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Conserved domains on  [gi|24659726|ref|NP_648073|]
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uncharacterized protein Dmel_CG8641, isoform A [Drosophila melanogaster]

Protein Classification

RasD family small GTPase( domain architecture ID 10134938)

RasD family small GTPase such as GTP-binding protein Rhes (Ras homolog enriched in striatum), a GTPase that regulates signaling pathways involving G-protein-coupled receptor, and Dexras1 (Dexamethasone-induced Ras-related protein 1), which interacts with FE65 to regulate FE65-amyloid precursor protein-dependent transcription

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Rhes_like cd04143
Ras homolog enriched in striatum (Rhes) and activator of G-protein signaling 1 (Dexras1/AGS1); ...
167-434 1.71e-148

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: 421.85  E-value: 1.71e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFS 246
Cdd:cd04143   1 YRMVVLGASKVGKTAIVSRFLGGRFEEQYTPTIEDFHRKLYSIRGEVYQLDILDTSGNHPFPAMRRLSILTGDVFILVFS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 247 MDSRESFEEVVRLRENILETKWAALNpgsgfKKKSLPKIPMILAGNKCDRDF-KTVQVDEVMGYIAGqDNCCTFVECSAR 325
Cdd:cd04143  81 LDNRESFEEVCRLREQILETKSCLKN-----KTKENVKIPMVICGNKADRDFpREVQRDEVEQLVGG-DENCAYFEVSAK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 326 QNYRIDDLFHSLFTVSNLPLEMTPNHHRRLVSVFGAPSPLPPHGsavggtkknaLSIKRRFSDACGVVTPNARRPSIRTD 405
Cdd:cd04143 155 KNSNLDEMFRALFSLAKLPNEMSPSLHRKISVQYGDALHKKSRG----------GSRKRKEGDACGAVAPFARRPSVHSD 224
                       250       260
                ....*....|....*....|....*....
gi 24659726 406 LNLMRSKTMALnegegvRSPSRWNRCALM 434
Cdd:cd04143 225 LRYIRSKSTGG------GQSKDKERCQIQ 247
 
Name Accession Description Interval E-value
Rhes_like cd04143
Ras homolog enriched in striatum (Rhes) and activator of G-protein signaling 1 (Dexras1/AGS1); ...
167-434 1.71e-148

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: 421.85  E-value: 1.71e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFS 246
Cdd:cd04143   1 YRMVVLGASKVGKTAIVSRFLGGRFEEQYTPTIEDFHRKLYSIRGEVYQLDILDTSGNHPFPAMRRLSILTGDVFILVFS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 247 MDSRESFEEVVRLRENILETKWAALNpgsgfKKKSLPKIPMILAGNKCDRDF-KTVQVDEVMGYIAGqDNCCTFVECSAR 325
Cdd:cd04143  81 LDNRESFEEVCRLREQILETKSCLKN-----KTKENVKIPMVICGNKADRDFpREVQRDEVEQLVGG-DENCAYFEVSAK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 326 QNYRIDDLFHSLFTVSNLPLEMTPNHHRRLVSVFGAPSPLPPHGsavggtkknaLSIKRRFSDACGVVTPNARRPSIRTD 405
Cdd:cd04143 155 KNSNLDEMFRALFSLAKLPNEMSPSLHRKISVQYGDALHKKSRG----------GSRKRKEGDACGAVAPFARRPSVHSD 224
                       250       260
                ....*....|....*....|....*....
gi 24659726 406 LNLMRSKTMALnegegvRSPSRWNRCALM 434
Cdd:cd04143 225 LRYIRSKSTGG------GQSKDKERCQIQ 247
RAS smart00173
Ras subfamily of RAS small GTPases; Similar in fold and function to the bacterial EF-Tu GTPase. ...
167-338 5.32e-59

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: 190.07  E-value: 5.32e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726    167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFS 246
Cdd:smart00173   1 YKLVVLGSGGVGKSALTIQFIQGHFVDDYDPTIEDSYRKQIEIDGEVCLLDILDTAGQEEFSAMRDQYMRTGEGFLLVYS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726    247 MDSRESFEEVVRLRENILETkwaalnpgsgfkkKSLPKIPMILAGNKCDRDFK-TVQVDEvmGY-IAGQDNcCTFVECSA 324
Cdd:smart00173  81 ITDRQSFEEIKKFREQILRV-------------KDRDDVPIVLVGNKCDLESErVVSTEE--GKeLARQWG-CPFLETSA 144
                          170
                   ....*....|....
gi 24659726    325 RQNYRIDDLFHSLF 338
Cdd:smart00173 145 KERVNVDEAFYDLV 158
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
168-337 2.64e-36

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: 130.71  E-value: 2.64e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726   168 RLVMLGSSRAGKSSIVARFLGNRFEEAYTPTI-EEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFS 246
Cdd:pfam00071   1 KLVLVGDGGVGKSSLLIRFTQNKFPEEYIPTIgVDFYTKTIEVDGKTVKLQIWDTAGQERFRALRPLYYRGADGFLLVYD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726   247 MDSRESFEEVVRLRENILETKWaalnpgsgfkkkslPKIPMILAGNKCD-RDFKTVQVDEVMGYiaGQDNCCTFVECSAR 325
Cdd:pfam00071  81 ITSRDSFENVKKWVEEILRHAD--------------ENVPIVLVGNKCDlEDQRVVSTEEGEAL--AKELGLPFMETSAK 144
                         170
                  ....*....|..
gi 24659726   326 QNYRIDDLFHSL 337
Cdd:pfam00071 145 TNENVEEAFEEL 156
PTZ00369 PTZ00369
Ras-like protein; Provisional
163-337 4.11e-32

Ras-like protein; Provisional


Pssm-ID: 240385 [Multi-domain]  Cd Length: 189  Bit Score: 120.74  E-value: 4.11e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726  163 AKNCYRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFI 242
Cdd:PTZ00369   2 ASTEYKLVVVGGGGVGKSALTIQFIQNHFIDEYDPTIEDSYRKQCVIDEETCLLDILDTAGQEEYSAMRDQYMRTGQGFL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726  243 LVFSMDSRESFEEVVRLRENILetkwaalnpgsgfKKKSLPKIPMILAGNKCDRDFKTvQVDEVMGYIAGQDNCCTFVEC 322
Cdd:PTZ00369  82 CVYSITSRSSFEEIASFREQIL-------------RVKDKDRVPMILVGNKCDLDSER-QVSTGEGQELAKSFGIPFLET 147
                        170
                 ....*....|....*
gi 24659726  323 SARQNYRIDDLFHSL 337
Cdd:PTZ00369 148 SAKQRVNVDEAFYEL 162
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
166-334 6.44e-19

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: 83.58  E-value: 6.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726   166 CYRLVMLGSSRAGKSSIVARFLGN-RFEEAYTPTIEEFHRK-LYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFIL 243
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNkGSITEYYPGTTRNYVTtVIEEDGKTYKFNLLDTAGQEDYDAIRRLYYPQVERSLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726   244 VFSMDSR-ESFEEVVRLRENILEtkwaalnpgsGFKKKslpKIPMILAGNKCdrDFKTVQVDEVMGYIAGQDNCCTFVEC 322
Cdd:TIGR00231  81 VFDIVILvLDVEEILEKQTKEII----------HHADS---GVPIILVGNKI--DLKDADLKTHVASEFAKLNGEPIIPL 145
                         170
                  ....*....|..
gi 24659726   323 SARQNYRIDDLF 334
Cdd:TIGR00231 146 SAETGKNIDSAF 157
 
Name Accession Description Interval E-value
Rhes_like cd04143
Ras homolog enriched in striatum (Rhes) and activator of G-protein signaling 1 (Dexras1/AGS1); ...
167-434 1.71e-148

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: 421.85  E-value: 1.71e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFS 246
Cdd:cd04143   1 YRMVVLGASKVGKTAIVSRFLGGRFEEQYTPTIEDFHRKLYSIRGEVYQLDILDTSGNHPFPAMRRLSILTGDVFILVFS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 247 MDSRESFEEVVRLRENILETKWAALNpgsgfKKKSLPKIPMILAGNKCDRDF-KTVQVDEVMGYIAGqDNCCTFVECSAR 325
Cdd:cd04143  81 LDNRESFEEVCRLREQILETKSCLKN-----KTKENVKIPMVICGNKADRDFpREVQRDEVEQLVGG-DENCAYFEVSAK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 326 QNYRIDDLFHSLFTVSNLPLEMTPNHHRRLVSVFGAPSPLPPHGsavggtkknaLSIKRRFSDACGVVTPNARRPSIRTD 405
Cdd:cd04143 155 KNSNLDEMFRALFSLAKLPNEMSPSLHRKISVQYGDALHKKSRG----------GSRKRKEGDACGAVAPFARRPSVHSD 224
                       250       260
                ....*....|....*....|....*....
gi 24659726 406 LNLMRSKTMALnegegvRSPSRWNRCALM 434
Cdd:cd04143 225 LRYIRSKSTGG------GQSKDKERCQIQ 247
RAS smart00173
Ras subfamily of RAS small GTPases; Similar in fold and function to the bacterial EF-Tu GTPase. ...
167-338 5.32e-59

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: 190.07  E-value: 5.32e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726    167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFS 246
Cdd:smart00173   1 YKLVVLGSGGVGKSALTIQFIQGHFVDDYDPTIEDSYRKQIEIDGEVCLLDILDTAGQEEFSAMRDQYMRTGEGFLLVYS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726    247 MDSRESFEEVVRLRENILETkwaalnpgsgfkkKSLPKIPMILAGNKCDRDFK-TVQVDEvmGY-IAGQDNcCTFVECSA 324
Cdd:smart00173  81 ITDRQSFEEIKKFREQILRV-------------KDRDDVPIVLVGNKCDLESErVVSTEE--GKeLARQWG-CPFLETSA 144
                          170
                   ....*....|....
gi 24659726    325 RQNYRIDDLFHSLF 338
Cdd:smart00173 145 KERVNVDEAFYDLV 158
small_GTPase smart00010
Small GTPase of the Ras superfamily; ill-defined subfamily; SMART predicts Ras-like small ...
165-338 1.25e-58

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: 189.31  E-value: 1.25e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726    165 NCYRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILV 244
Cdd:smart00010   1 REYKLVVLGGGGVGKSALTIQFVQGHFVDEYDPTIEDSYRKQIEIDGEVCLLDILDTAGQEEFSAMRDQYMRTGEGFLLV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726    245 FSMDSRESFEEVVRLRENILETkwaalnpgsgfkkKSLPKIPMILAGNKCDRDFK-TVQVDEvmGY-IAGQDNcCTFVEC 322
Cdd:smart00010  81 YSITDRQSFEEIAKFREQILRV-------------KDRDDVPIVLVGNKCDLENErVVSTEE--GKeLARQWG-CPFLET 144
                          170
                   ....*....|....*.
gi 24659726    323 SARQNYRIDDLFHSLF 338
Cdd:smart00010 145 SAKERINVDEAFYDLV 160
Ras cd00876
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ...
168-339 2.36e-54

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: 178.10  E-value: 2.36e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 168 RLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFSM 247
Cdd:cd00876   1 KLVVLGAGGVGKSALTIRFVSGEFVEEYDPTIEDSYRKQIVVDGETYTLDILDTAGQEEFSAMRDQYIRNGDGFILVYSI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 248 DSRESFEEVVRLRENILETkwaalnpgsgfkkKSLPKIPMILAGNKCD-RDFKTVQVDEVMGYiAGQDNcCTFVECSARQ 326
Cdd:cd00876  81 TSRESFEEIKNIREQILRV-------------KDKEDVPIVLVGNKCDlENERQVSTEEGEAL-AEEWG-CPFLETSAKT 145
                       170
                ....*....|...
gi 24659726 327 NYRIDDLFHSLFT 339
Cdd:cd00876 146 NINIDELFNTLVR 158
Ras_dva cd04147
Ras - dorsal-ventral anterior localization (Ras-dva) family; Ras-dva subfamily. Ras-dva (Ras - ...
168-382 1.73e-44

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: 153.84  E-value: 1.73e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 168 RLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFSM 247
Cdd:cd04147   1 RLVFMGAAGVGKTALIQRFLYDTFEPKHRRTVEELHSKEYEVAGVKVTIDILDTSGSYSFPAMRKLSIQNGDAFALVYSV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 248 DSRESFEEVVRLRENILETKwaalnpGSGFkkkslpkIPMILAGNKCDRDFKTVQVDEVMGYIAGQDNCCTFVECSARQN 327
Cdd:cd04147  81 DDPESFEEVKRLREEILEVK------EDKF-------VPIVVVGNKIDSLAERQVEAADALSTVELDWNNGFVEASAKDN 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24659726 328 YRIDDLFHSLFTVSNLPLEMTPNHHRRlvsvfgaPSPLPP-HGSAVGGTKKNALSI 382
Cdd:cd04147 148 ENVTEVFKELLQQANLPSWLSPALRRR-------RESAPSeIQRRPPMNKTNSCSV 196
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
168-337 2.64e-36

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: 130.71  E-value: 2.64e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726   168 RLVMLGSSRAGKSSIVARFLGNRFEEAYTPTI-EEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFS 246
Cdd:pfam00071   1 KLVLVGDGGVGKSSLLIRFTQNKFPEEYIPTIgVDFYTKTIEVDGKTVKLQIWDTAGQERFRALRPLYYRGADGFLLVYD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726   247 MDSRESFEEVVRLRENILETKWaalnpgsgfkkkslPKIPMILAGNKCD-RDFKTVQVDEVMGYiaGQDNCCTFVECSAR 325
Cdd:pfam00071  81 ITSRDSFENVKKWVEEILRHAD--------------ENVPIVLVGNKCDlEDQRVVSTEEGEAL--AKELGLPFMETSAK 144
                         170
                  ....*....|..
gi 24659726   326 QNYRIDDLFHSL 337
Cdd:pfam00071 145 TNENVEEAFEEL 156
ARHI_like cd04140
A Ras homolog member I (ARHI); ARHI (A Ras homolog member I) is a member of the Ras family ...
167-337 1.43e-35

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: 129.18  E-value: 1.43e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFS 246
Cdd:cd04140   2 YRVVVFGAGGVGKSSLVLRFVKGTFRESYIPTIEDTYRQVISCSKSICTLQITDTTGSHQFPAMQRLSISKGHAFILVYS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 247 MDSRESFEEVVRLRENILEtkwaalnpgsgFKKKSLPKIPMILAGNKCDrDFKTVQVDEVMGYIAGQDNCCTFVECSARQ 326
Cdd:cd04140  82 ITSKQSLEELKPIYELICE-----------IKGNNLEKIPIMLVGNKCD-ESPSREVSSSEGAALARTWNCAFMETSAKT 149
                       170
                ....*....|.
gi 24659726 327 NYRIDDLFHSL 337
Cdd:cd04140 150 NHNVQELFQEL 160
Rap1 cd04175
Rap1 family GTPase consists of Rap1a and Rap1b isoforms; The Rap1 subgroup is part of the Rap ...
167-337 3.75e-34

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: 125.32  E-value: 3.75e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFS 246
Cdd:cd04175   2 YKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDGQQCMLEILDTAGTEQFTAMRDLYMKNGQGFVLVYS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 247 MDSRESFEEVVRLRENILetkwaalnpgsgfKKKSLPKIPMILAGNKCDRDFKTVqVDEVMGYIAGQDNCCTFVECSARQ 326
Cdd:cd04175  82 ITAQSTFNDLQDLREQIL-------------RVKDTEDVPMILVGNKCDLEDERV-VGKEQGQNLARQWGCAFLETSAKA 147
                       170
                ....*....|.
gi 24659726 327 NYRIDDLFHSL 337
Cdd:cd04175 148 KINVNEIFYDL 158
Rap_like cd04136
Rap-like family consists of Rap1, Rap2 and RSR1; The Rap subfamily consists of the Rap1, Rap2, ...
167-337 1.48e-33

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: 123.44  E-value: 1.48e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFS 246
Cdd:cd04136   2 YKLVVLGSGGVGKSALTVQFVQGIFVDKYDPTIEDSYRKQIEVDCQQCMLEILDTAGTEQFTAMRDLYIKNGQGFALVYS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 247 MDSRESFEEVVRLRENILetkwaalnpgsgfKKKSLPKIPMILAGNKCDRDFKTVQVDEVMGYIAGQDNCCTFVECSARQ 326
Cdd:cd04136  82 ITAQQSFNDLQDLREQIL-------------RVKDTEDVPMILVGNKCDLEDERVVSKEEGQNLARQWGNCPFLETSAKS 148
                       170
                ....*....|.
gi 24659726 327 NYRIDDLFHSL 337
Cdd:cd04136 149 KINVDEIFYDL 159
Rap2 cd04176
Rap2 family GTPase consists of Rap2a, Rap2b, and Rap2c; The Rap2 subgroup is part of the Rap ...
167-334 1.03e-32

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: 121.48  E-value: 1.03e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFS 246
Cdd:cd04176   2 YKVVVLGSGGVGKSALTVQFVSGTFIEKYDPTIEDFYRKEIEVDSSPSVLEILDTAGTEQFASMRDLYIKNGQGFIVVYS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 247 MDSRESFEEVVRLRENILetkwaalnpgsgfKKKSLPKIPMILAGNKCDRDFKTvQVDEVMGYIAGQDNCCTFVECSARQ 326
Cdd:cd04176  82 LVNQQTFQDIKPMRDQIV-------------RVKGYEKVPIILVGNKVDLESER-EVSSAEGRALAEEWGCPFMETSAKS 147

                ....*...
gi 24659726 327 NYRIDDLF 334
Cdd:cd04176 148 KTMVNELF 155
RSR1 cd04177
RSR1/Bud1p family GTPase; RSR1/Bud1p is a member of the Rap subfamily of the Ras family that ...
167-337 1.16e-32

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: 121.44  E-value: 1.16e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFS 246
Cdd:cd04177   2 YKIVVLGAGGVGKSALTVQFVQNVFIESYDPTIEDSYRKQVEIDGRQCDLEILDTAGTEQFTAMRELYIKSGQGFLLVYS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 247 MDSRESFEEVVRLRENILetkwaalnpgsgfKKKSLPKIPMILAGNKCD-RDFKTVQVDEVMGyIAGQDNCCTFVECSAR 325
Cdd:cd04177  82 VTSEASLNELGELREQVL-------------RIKDSDNVPMVLVGNKADlEDDRQVSREDGVS-LSQQWGNVPFYETSAR 147
                       170
                ....*....|..
gi 24659726 326 QNYRIDDLFHSL 337
Cdd:cd04177 148 KRTNVDEVFIDL 159
H_N_K_Ras_like cd04138
Ras GTPase family containing H-Ras,N-Ras and K-Ras4A/4B; H-Ras/N-Ras/K-Ras subfamily. H-Ras, ...
167-337 1.94e-32

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: 120.60  E-value: 1.94e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFS 246
Cdd:cd04138   2 YKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 247 MDSRESFEEVVRLRENILetkwaalnpgsgfKKKSLPKIPMILAGNKCDRDFKTVQVDEVMGyIAGQDNcCTFVECSARQ 326
Cdd:cd04138  82 INSRKSFEDIHTYREQIK-------------RVKDSDDVPMVLVGNKCDLAARTVSTRQGQD-LAKSYG-IPYIETSAKT 146
                       170
                ....*....|.
gi 24659726 327 NYRIDDLFHSL 337
Cdd:cd04138 147 RQGVEEAFYTL 157
PTZ00369 PTZ00369
Ras-like protein; Provisional
163-337 4.11e-32

Ras-like protein; Provisional


Pssm-ID: 240385 [Multi-domain]  Cd Length: 189  Bit Score: 120.74  E-value: 4.11e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726  163 AKNCYRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFI 242
Cdd:PTZ00369   2 ASTEYKLVVVGGGGVGKSALTIQFIQNHFIDEYDPTIEDSYRKQCVIDEETCLLDILDTAGQEEYSAMRDQYMRTGQGFL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726  243 LVFSMDSRESFEEVVRLRENILetkwaalnpgsgfKKKSLPKIPMILAGNKCDRDFKTvQVDEVMGYIAGQDNCCTFVEC 322
Cdd:PTZ00369  82 CVYSITSRSSFEEIASFREQIL-------------RVKDKDRVPMILVGNKCDLDSER-QVSTGEGQELAKSFGIPFLET 147
                        170
                 ....*....|....*
gi 24659726  323 SARQNYRIDDLFHSL 337
Cdd:PTZ00369 148 SAKQRVNVDEAFYEL 162
M_R_Ras_like cd04145
R-Ras2/TC21, M-Ras/R-Ras3; The M-Ras/R-Ras-like subfamily contains R-Ras2/TC21, M-Ras/R-Ras3, ...
167-337 2.35e-31

R-Ras2/TC21, M-Ras/R-Ras3; The M-Ras/R-Ras-like subfamily contains R-Ras2/TC21, M-Ras/R-Ras3, and related members of the Ras family. M-Ras is expressed in lympho-hematopoetic cells. It interacts with some of the known Ras effectors, but appears to also have its own effectors. Expression of mutated M-Ras leads to transformation of several types of cell lines, including hematopoietic cells, mammary epithelial cells, and fibroblasts. Overexpression of M-Ras is observed in carcinomas from breast, uterus, thyroid, stomach, colon, kidney, lung, and rectum. In addition, expression of a constitutively active M-Ras mutant in murine bone marrow induces a malignant mast cell leukemia that is distinct from the monocytic leukemia induced by H-Ras. TC21, along with H-Ras, has been shown to regulate the branching morphogenesis of ureteric bud cell branching in mice. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 133345 [Multi-domain]  Cd Length: 164  Bit Score: 117.51  E-value: 2.35e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFS 246
Cdd:cd04145   3 YKLVVVGGGGVGKSALTIQFIQSYFVTDYDPTIEDSYTKQCEIDGQWARLDILDTAGQEEFSAMREQYMRTGEGFLLVFS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 247 MDSRESFEEVVRLRENILETkwaalnpgsgfkkKSLPKIPMILAGNKCDRDFKTvQVDEVMGYIAGQDNCCTFVECSARQ 326
Cdd:cd04145  83 VTDRGSFEEVDKFHTQILRV-------------KDRDEFPMILVGNKADLEHQR-QVSREEGQELARQLKIPYIETSAKD 148
                       170
                ....*....|.
gi 24659726 327 NYRIDDLFHSL 337
Cdd:cd04145 149 RVNVDKAFHDL 159
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
167-339 4.59e-31

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: 116.79  E-value: 4.59e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTI-EEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRlSFLTG-DLFILV 244
Cdd:cd00154   1 FKIVLIGDSGVGKTSLLLRFVDNKFSENYKSTIgVDFKSKTIEVDGKKVKLQIWDTAGQERFRSITS-SYYRGaHGAILV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 245 FSMDSRESFEEVVRLRENIletkwaalnpgsgfKKKSLPKIPMILAGNKCD-RDFKTVQVDEVMGYIagQDNCCTFVECS 323
Cdd:cd00154  80 YDVTNRESFENLDKWLNEL--------------KEYAPPNIPIILVGNKSDlEDERQVSTEEAQQFA--KENGLLFFETS 143
                       170
                ....*....|....*.
gi 24659726 324 ARQNYRIDDLFHSLFT 339
Cdd:cd00154 144 AKTGENVDEAFESLAR 159
Rit_Rin_Ric cd04141
Ras-like protein in all tissues (Rit), Ras-like protein in neurons (Rin) and Ras-related ...
167-337 6.36e-27

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: 106.09  E-value: 6.36e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFS 246
Cdd:cd04141   3 YKIVMLGAGGVGKSAVTMQFISHSFPDYHDPTIEDAYKTQARIDNEPALLDILDTAGQAEFTAMRDQYMRCGEGFIICYS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 247 MDSRESFEEVVRLRENIletkwaalnpgsgFKKKSLPKIPMILAGNKCD-RDFKTVQVDEvmGYIAGQDNCCTFVECSAR 325
Cdd:cd04141  83 VTDRHSFQEASEFKELI-------------TRVRLTEDIPLVLVGNKVDlEQQRQVTTEE--GRNLAREFNCPFFETSAA 147
                       170
                ....*....|..
gi 24659726 326 QNYRIDDLFHSL 337
Cdd:cd04141 148 LRFYIDDAFHGL 159
RheB cd04137
Ras Homolog Enriched in Brain (RheB) is a small GTPase; Rheb (Ras Homolog Enriched in Brain) ...
168-337 2.92e-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: 104.25  E-value: 2.92e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 168 RLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSG---YHPFPAmrrlSFLTG-DLFIL 243
Cdd:cd04137   3 KIAVLGSRSVGKSSLTVQFVEGHFVESYYPTIENTFSKIITYKGQEYHLEIVDTAGqdeYSILPQ----KYSIGiHGYIL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 244 VFSMDSRESFEEVVRLRENILETKWAAlnpgsgfkkkslpKIPMILAGNKCD-RDFKTVQVDEvmGYIAGQDNCCTFVEC 322
Cdd:cd04137  79 VYSVTSRKSFEVVKVIYDKILDMLGKE-------------SVPIVLVGNKSDlHMERQVSAEE--GKKLAESWGAAFLES 143
                       170
                ....*....|....*
gi 24659726 323 SARQNYRIDDLFHSL 337
Cdd:cd04137 144 SAKENENVEEAFELL 158
RalA_RalB cd04139
Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily ...
167-337 6.85e-26

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: 102.89  E-value: 6.85e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFS 246
Cdd:cd04139   1 HKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGEEVQLNILDTAGQEDYAAIRDNYFRSGEGFLLVFS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 247 MDSRESFEEVVRLRENILetkwaalnpgsgfKKKSLPKIPMILAGNKCDRDFKTVQVDEVMGYIAgQDNCCTFVECSARQ 326
Cdd:cd04139  81 ITDMESFTALAEFREQIL-------------RVKEDDNVPLLLVGNKCDLEDKRQVSVEEAANLA-EQWGVNYVETSAKT 146
                       170
                ....*....|.
gi 24659726 327 NYRIDDLFHSL 337
Cdd:cd04139 147 RANVDKVFFDL 157
Rho cd00157
Ras homology family (Rho) of small guanosine triphosphatases (GTPases); Members of the Rho ...
169-335 2.58e-25

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: 101.47  E-value: 2.58e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 169 LVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFSMD 248
Cdd:cd00157   3 IVVVGDGAVGKTCLLISYTTNKFPTEYVPTVFDNYSANVTVDGKQVNLGLWDTAGQEEYDRLRPLSYPQTDVFLLCFSVD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 249 SRESFEEVvrlrenilETKWaalNPGSgfkKKSLPKIPMILAGNKCD-RD---------FKTVQVDEVMGY-IAGQDNCC 317
Cdd:cd00157  83 SPSSFENV--------KTKW---YPEI---KHYCPNVPIILVGTKIDlRDdgntlkkleKKQKPITPEEGEkLAKEIGAV 148
                       170
                ....*....|....*...
gi 24659726 318 TFVECSARQNYRIDDLFH 335
Cdd:cd00157 149 KYMECSALTQEGLKEVFD 166
Ras2 cd04144
Rat sarcoma (Ras) family 2 of small guanosine triphosphatases (GTPases); The Ras2 subfamily, ...
168-337 1.05e-24

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: 100.31  E-value: 1.05e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 168 RLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFSM 247
Cdd:cd04144   1 KLVVLGDGGVGKTALTIQLCLNHFVETYDPTIEDSYRKQVVVDGQPCMLEVLDTAGQEEYTALRDQWIREGEGFILVYSI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 248 DSRESFEEVVRLRENILETkwaalnpgsgfKKKSLPKIPMILAGNKCDRDF-KTVQVDEvmGYIAGQDNCCTFVECSARQ 326
Cdd:cd04144  81 TSRSTFERVERFREQIQRV-----------KDESAADVPIMIVGNKCDKVYeREVSTEE--GAALARRLGCEFIEASAKT 147
                       170
                ....*....|.
gi 24659726 327 NYRIDDLFHSL 337
Cdd:cd04144 148 NVNVERAFYTL 158
RERG_RasL11_like cd04146
Ras-related and Estrogen-Regulated Growth inhibitor (RERG) and Ras-like 11 (RasL11)-like ...
169-338 4.51e-22

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


Pssm-ID: 206713 [Multi-domain]  Cd Length: 166  Bit Score: 92.34  E-value: 4.51e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 169 LVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRL--SFLTGDLFILVFS 246
Cdd:cd04146   2 IAVLGASGVGKSALTVRFLTKRFIGEYEPNLESLYSRQVTIDGEQVSLEIQDTPGQQQNEDPESLerSLRWADGFVLVYS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 247 MDSRESFEEVVRLRENILETKWAALNpgsgfkkkslpkIPMILAGNKCDRD-FKTVQVDEvmGYIAGQDNCCTFVECSAR 325
Cdd:cd04146  82 ITDRSSFDVVSQLLQLIREIKKRDGE------------IPVILVGNKADLLhSRQVSTEE--GQKLALELGCLFFEVSAA 147
                       170
                ....*....|....
gi 24659726 326 QNY-RIDDLFHSLF 338
Cdd:cd04146 148 ENYlEVQNVFHELC 161
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
170-339 3.64e-21

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


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 89.82  E-value: 3.64e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 170 VMLGSSRAGKSSIVARFLGNRF---EEAYTPTIEEfHRKLYRIRNEVFQLDILDTSG-----YHPFPAMRRLSFLTGDLF 241
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVgevSDVPGTTRDP-DVYVKELDKGKVKLVLVDTPGldefgGLGREELARLLLRGADLI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 242 ILVFSMDSRESFEEVVRLRENILETKwaalnpgsgfkkkslpKIPMILAGNKCDRDFKTVQVDEVMGYIAGQDNCCTFVE 321
Cdd:cd00882  80 LLVVDSTDRESEEDAKLLILRRLRKE----------------GIPIILVGNKIDLLEEREVEELLRLEELAKILGVPVFE 143
                       170
                ....*....|....*...
gi 24659726 322 CSARQNYRIDDLFHSLFT 339
Cdd:cd00882 144 VSAKTGEGVDELFEKLIE 161
RRP22 cd04142
Ras-related protein on chromosome 22 (RRP22) family; RRP22 (Ras-related protein on chromosome ...
167-337 1.04e-20

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: 89.54  E-value: 1.04e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIeefHRKLYR----IRNEVFQLDILDTSGYHPFPA--------MRRLS 234
Cdd:cd04142   1 VRVAVLGAPGVGKTAIVRQFLAQEFPEEYIPTE---HRRLYRpavvLSGRVYDLHILDVPNMQRYPGtagqewmdPRFRG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 235 FLTGDLFILVFSMDSRESFEEVVRLRENILETKWAAlnpgsgfkkksLPKIPMILAGNKCDRDFKTVQVDEVMGYIAGQD 314
Cdd:cd04142  78 LRNSRAFILVYDICSPDSFHYVKLLRQQILETRPAG-----------NKEPPIVVVGNKRDQQRHRFAPRHVLSVLVRKS 146
                       170       180
                ....*....|....*....|...
gi 24659726 315 NCCTFVECSARQNYRIDDLFHSL 337
Cdd:cd04142 147 WKCGYLECSAKYNWHILLLFKEL 169
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
167-337 4.12e-20

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


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 86.79  E-value: 4.12e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726    167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIE-EFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRlSFLTG-DLFILV 244
Cdd:smart00175   1 FKIILIGDSGVGKSSLLSRFTDGKFSEQYKSTIGvDFKTKTIEVDGKRVKLQIWDTAGQERFRSITS-SYYRGaVGALLV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726    245 FSMDSRESFEEVvrlrenileTKWAalnpgSGFKKKSLPKIPMILAGNKCDRDFK-TVQVDEVMGYiaGQDNCCTFVECS 323
Cdd:smart00175  80 YDITNRESFENL---------ENWL-----KELREYASPNVVIMLVGNKSDLEEQrQVSREEAEAF--AEEHGLPFFETS 143
                          170
                   ....*....|....
gi 24659726    324 ARQNYRIDDLFHSL 337
Cdd:smart00175 144 AKTNTNVEEAFEEL 157
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
166-334 6.44e-19

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: 83.58  E-value: 6.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726   166 CYRLVMLGSSRAGKSSIVARFLGN-RFEEAYTPTIEEFHRK-LYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFIL 243
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNkGSITEYYPGTTRNYVTtVIEEDGKTYKFNLLDTAGQEDYDAIRRLYYPQVERSLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726   244 VFSMDSR-ESFEEVVRLRENILEtkwaalnpgsGFKKKslpKIPMILAGNKCdrDFKTVQVDEVMGYIAGQDNCCTFVEC 322
Cdd:TIGR00231  81 VFDIVILvLDVEEILEKQTKEII----------HHADS---GVPIILVGNKI--DLKDADLKTHVASEFAKLNGEPIIPL 145
                         170
                  ....*....|..
gi 24659726   323 SARQNYRIDDLF 334
Cdd:TIGR00231 146 SAETGKNIDSAF 157
Rab5_related cd01860
Rab-related GTPase family includes Rab5 and Rab22; regulates early endosome fusion; The ...
167-335 2.06e-17

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: 79.13  E-value: 2.06e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTI-EEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVF 245
Cdd:cd01860   2 FKLVLLGDSSVGKSSIVLRFVKNEFSENQESTIgAAFLTQTVNLDDTTVKFEIWDTAGQERYRSLAPMYYRGAAAAIVVY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 246 SMDSRESFEEVVR-LREniletkwaalnpgsgFKKKSLPKIPMILAGNKCD-RDFKTVQVDEVMGYIagQDNCCTFVECS 323
Cdd:cd01860  82 DITSEESFEKAKSwVKE---------------LQEHGPPNIVIALAGNKADlESKRQVSTEEAQEYA--DENGLLFMETS 144
                       170
                ....*....|..
gi 24659726 324 ARQNYRIDDLFH 335
Cdd:cd01860 145 AKTGENVNELFT 156
RHO smart00174
Rho (Ras homology) subfamily of Ras-like small GTPases; Members of this subfamily of Ras-like ...
169-335 4.31e-17

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: 78.42  E-value: 4.31e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726    169 LVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFSMD 248
Cdd:smart00174   1 LVVVGDGAVGKTCLLIVYTTNAFPEDYVPTVFENYSADVEVDGKPVELGLWDTAGQEDYDRLRPLSYPDTDVFLICFSVD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726    249 SRESFeevvrlrENILEtKWAalnpgsGFKKKSLPKIPMILAGNKCD-RDFK--------------TVQVDEVMgyiAGQ 313
Cdd:smart00174  81 SPASF-------ENVKE-KWY------PEVKHFCPNVPIILVGTKLDlRNDKstleelskkkqepvTYEQGQAL---AKR 143
                          170       180
                   ....*....|....*....|..
gi 24659726    314 DNCCTFVECSARQNYRIDDLFH 335
Cdd:smart00174 144 IGAVKYLECSALTQEGVREVFE 165
Rab21 cd04123
Rab GTPase family 21 (Rab21); The localization and function of Rab21 are not clearly defined, ...
167-337 2.49e-16

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: 76.11  E-value: 2.49e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIE-EFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVF 245
Cdd:cd04123   1 FKVVLLGEGRVGKTSLVLRYVENKFNEKHESTTQaSFFQKTVNIGGKRIDLAIWDTAGQERYHALGPIYYRDADGAILVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 246 SMDSRESFEEVvrlRENILETKWAALNpgsgfkkkslpKIPMILAGNKCDRDF-KTVQVDEVMGYiAGQDNCCTFvECSA 324
Cdd:cd04123  81 DITDADSFQKV---KKWIKELKQMRGN-----------NISLVIVGNKIDLERqRVVSKSEAEEY-AKSVGAKHF-ETSA 144
                       170
                ....*....|...
gi 24659726 325 RQNYRIDDLFHSL 337
Cdd:cd04123 145 KTGKGIEELFLSL 157
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
168-295 7.20e-16

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: 73.31  E-value: 7.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726   168 RLVMLGSSRAGKSSIVARFLGNRFEEAYTPTI-EEFHRK---LYRIRNEVFQLDILDTSG---YHpfpAMRRlSFLTG-D 239
Cdd:pfam08477   1 KVVLLGDSGVGKTSLLKRFVDDTFDPKYKSTIgVDFKTKtvlENDDNGKKIKLNIWDTAGqerFR---SLHP-FYYRGaA 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 24659726   240 LFILVFsmDSRESFeevvRLRENILETkwaalnpgsgfkKKSLPKIPMILAGNKCD 295
Cdd:pfam08477  77 AALLVY--DSRTFS----NLKYWLREL------------KKYAGNSPVILVGNKID 114
Rho4_like cd04132
Ras homology family 4 (Rho4) of small guanosine triphosphatases (GTPases)-like; Rho4 is a ...
168-334 1.78e-15

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: 74.68  E-value: 1.78e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 168 RLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRN-EVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFS 246
Cdd:cd04132   5 KIVVVGDGGCGKTCLLMVYAQGSFPEEYVPTVFENYVTTLQVPNgKIIELALWDTAGQEDYDRLRPLSYPDVDVILICYS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 247 MDSRESFEevvrlreNILEtKWAalnPG-SGFkkksLPKIPMILAGNKCD--RDFKTVQVDEVMG-----YIAGQDNC-- 316
Cdd:cd04132  85 VDNPTSLD-------NVED-KWY---PEvNHF----CPGTPIVLVGLKTDlrKDKNSVSKLRAQGlepvtPEQGESVAks 149
                       170       180
                ....*....|....*....|.
gi 24659726 317 ---CTFVECSARQNYRIDDLF 334
Cdd:cd04132 150 igaVAYIECSAKLMENVDEVF 170
Rab9 cd04116
Rab GTPase family 9 (Rab9); Rab9 is found in late endosomes, together with mannose 6-phosphate ...
168-334 2.29e-15

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: 73.75  E-value: 2.29e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 168 RLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIE-EFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFS 246
Cdd:cd04116   7 KVILLGDGGVGKSSLMNRYVTNKFDTQLFHTIGvEFLNKDLEVDGHFVTLQIWDTAGQERFRSLRTPFYRGSDCCLLTFS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 247 MDSRESFEEVVRLRENILetKWAALnpgsgfkkKSLPKIPMILAGNKCDRDFKTVQVDEVMGYIAGQDNCCTFvECSARQ 326
Cdd:cd04116  87 VDDSQSFQNLSNWKKEFI--YYADV--------KEPESFPFVILGNKIDIPERQVSTEEAQAWCRDNGDYPYF-ETSAKD 155

                ....*...
gi 24659726 327 NYRIDDLF 334
Cdd:cd04116 156 ATNVAAAF 163
Rho3 cd04134
Ras homology family 3 (Rho3) of small guanosine triphosphatases (GTPases); Rho3 is a member of ...
168-334 1.66e-14

Ras homology family 3 (Rho3) of small guanosine triphosphatases (GTPases); Rho3 is a member of the Rho family found only in fungi. Rho3 is believed to regulate cell polarity by interacting with the diaphanous/formin family protein For3 to control both the actin cytoskeleton and microtubules. Rho3 is also believed to have a direct role in exocytosis that is independent of its role in regulating actin polarity. The function in exocytosis may be two-pronged: first, in the transport of post-Golgi vesicles from the mother cell to the bud, mediated by myosin (Myo2); second, in the docking and fusion of vesicles to the plasma membrane, mediated by an exocyst (Exo70) protein. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins.


Pssm-ID: 206706 [Multi-domain]  Cd Length: 185  Bit Score: 71.43  E-value: 1.66e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 168 RLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFSM 247
Cdd:cd04134   2 KVVVLGDGACGKTSLLNVFTRGYFPQVYEPTVFENYIHDIFVDGLAVELSLWDTAGQEEFDRLRSLSYADTHVIMLCFSV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 248 DSRESFEEVvrlrenilETKWAalnpgsGFKKKSLPKIPMILAGNKCD---------RDFKTVQVDEVMGyIAGQDNCCT 318
Cdd:cd04134  82 DNPDSLENV--------ESKWL------AEIRHHCPGVKLVLVALKCDlreprnerdRGTHTISYEEGLA-VAKRINACR 146
                       170
                ....*....|....*.
gi 24659726 319 FVECSARQNYRIDDLF 334
Cdd:cd04134 147 YLECSAKLNRGVNEAF 162
Rab18 cd01863
Rab GTPase family 18 (Rab18); Rab18 subfamily. Mammalian Rab18 is implicated in endocytic ...
167-337 2.53e-14

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: 70.42  E-value: 2.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIE-EFHRKLYRIRNEVFQLDILDTSGYHPFpamRRL--SFLTGDL-FI 242
Cdd:cd01863   1 LKILLIGDSGVGKSSLLLRFTDDTFDEDLSSTIGvDFKVKTVTVDGKKVKLAIWDTAGQERF---RTLtsSYYRGAQgVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 243 LVFSMDSRESFEEVVrlreniletKWaaLNPGSGFKKKslPKIPMILAGNKCDRDFKTVQVDEVMGYiaGQDNCCTFVEC 322
Cdd:cd01863  78 LVYDVTRRDTFDNLD---------TW--LNELDTYSTN--PDAVKMLVGNKIDKENREVTREEGQKF--ARKHNMLFIET 142
                       170
                ....*....|....*
gi 24659726 323 SARQNYRIDDLFHSL 337
Cdd:cd01863 143 SAKTRIGVQQAFEEL 157
Rab6 cd01861
Rab GTPase family 6 (Rab6); Rab6 is involved in microtubule-dependent transport pathways ...
167-334 4.76e-14

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: 69.57  E-value: 4.76e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTI-EEFHRKLYRIRNEVFQLDILDTSGYHPF----PAMRRLSFLTgdlf 241
Cdd:cd01861   1 HKLVFLGDQSVGKTSIITRFMYDTFDNQYQATIgIDFLSKTMYVDDKTVRLQLWDTAGQERFrsliPSYIRDSSVA---- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 242 ILVFSMDSRESFEEVvrlrenileTKWAalnpgSGFKKKSLPKIPMILAGNKCDRDFKTVQVDEVMGYIAGQDNcCTFVE 321
Cdd:cd01861  77 VVVYDITNRQSFDNT---------DKWI-----DDVRDERGNDVIIVLVGNKTDLSDKRQVSTEEGEKKAKENN-AMFIE 141
                       170
                ....*....|...
gi 24659726 322 CSARQNYRIDDLF 334
Cdd:cd01861 142 TSAKAGHNVKQLF 154
Rnd3_RhoE_Rho8 cd04172
Rnd3/RhoE/Rho8 GTPases; Rnd3/RhoE/Rho8 subfamily. Rnd3/RhoE/Rho8 is a member of the novel Rho ...
168-335 5.16e-14

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


Pssm-ID: 206735 [Multi-domain]  Cd Length: 182  Bit Score: 70.08  E-value: 5.16e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 168 RLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFSM 247
Cdd:cd04172   7 KIVVVGDSQCGKTALLHVFAKDCFPENYVPTVFENYTASFEIDTQRIELSLWDTSGSPYYDNVRPLSYPDSDAVLICFDI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 248 DSRESFEEVVRlreniletKWaalnpgSGFKKKSLPKIPMILAGNKCD--RDFKTV-----QVDEVMGY-----IAGQDN 315
Cdd:cd04172  87 SRPETLDSVLK--------KW------KGEIQEFCPNTKMLLVGCKSDlrTDVSTLvelsnHRQTPVSYdqganMAKQIG 152
                       170       180
                ....*....|....*....|.
gi 24659726 316 CCTFVECSARQNYR-IDDLFH 335
Cdd:cd04172 153 AATYIECSALQSENsVRDIFH 173
RGK cd04148
Rem, Rem2, Rad, Gem/Kir (RGK) subfamily of Ras GTPases; RGK subfamily. The RGK (Rem, Rem2, Rad, ...
167-334 3.35e-13

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: 68.59  E-value: 3.35e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEE-AYTPTIEEFHRKLYRIRNEVFQLDILDTsgyhpfPAMRRLSFLT------GD 239
Cdd:cd04148   1 YRVVLLGDSGVGKSSLANIFTAGVYEDsAYEASGDDTYERTVSVDGEEATLVVYDH------WEQEDGMWLEdscmqvGD 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 240 LFILVFSMDSRESFEEVVRLRENILETKWAalnpgsgfkkkslPKIPMILAGNKCD--RDfKTVQVDEVMGYIAGQDncC 317
Cdd:cd04148  75 AYVIVYSVTDRSSFEKASELRIQLRRARQA-------------EDIPIILVGNKSDlvRS-REVSVQEGRACAVVFD--C 138
                       170
                ....*....|....*..
gi 24659726 318 TFVECSARQNYRIDDLF 334
Cdd:cd04148 139 KFIETSAALQHNVDELF 155
Rnd cd04131
Rho family GTPase subfamily Rnd includes Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8; The Rnd ...
165-335 4.12e-13

Rho family GTPase subfamily Rnd includes Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8; The Rnd subfamily contains Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8. These novel Rho family proteins have substantial structural differences compared to other Rho members, including N- and C-terminal extensions relative to other Rhos. Rnd3/RhoE is farnesylated at the C-terminal prenylation site, unlike most other Rho proteins that are geranylgeranylated. In addition, Rnd members are unable to hydrolyze GTP and are resistant to GAP activity. They are believed to exist only in the GTP-bound conformation, and are antagonists of RhoA activity. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206703 [Multi-domain]  Cd Length: 176  Bit Score: 67.07  E-value: 4.12e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 165 NCyRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILV 244
Cdd:cd04131   1 RC-KIVLVGDSQCGKTALLQVFAKDSFPENYVPTVFENYTASFEVDKQRIELSLWDTSGSPYYDNVRPLSYPDSDAVLIC 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 245 FSMDSRESFEEVVRlreniletKWaalnpgSGFKKKSLPKIPMILAGNKCD--RDFKTV-----QVDEVMGY-----IAG 312
Cdd:cd04131  80 FDISRPETLDSVLK--------KW------KGEVREFCPNTPVLLVGCKSDlrTDLSTLtelsnKRQIPVSHeqgrnLAK 145
                       170       180
                ....*....|....*....|....
gi 24659726 313 QDNCCTFVECSARQNYR-IDDLFH 335
Cdd:cd04131 146 QIGAAAYVECSAKTSENsVRDVFE 169
Rab39 cd04111
Rab GTPase family 39 (Rab39); Found in eukaryotes, Rab39 is mainly found in epithelial cell ...
167-337 6.80e-13

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: 67.48  E-value: 6.80e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIE-EFHRKLYRIRNEVF-QLDILDTSGYHPFPAMRRLSFLTGDLFILV 244
Cdd:cd04111   3 FRLIVIGDSTVGKSSLLKRFTEGRFAEVSDPTVGvDFFSRLIEIEPGVRiKLQLWDTAGQERFRSITRSYYRNSVGVLLV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 245 FSMDSRESFEEVvrlrENILETKWAALNPGsgfkkkslpKIPMILAGNKCDRDFKTvQVDEVMGYIAGQDNCCTFVECSA 324
Cdd:cd04111  83 FDITNRESFEHV----HDWLEEARSHIQPH---------RPVFILVGHKCDLESQR-QVTREEAEKLAKDLGMKYIETSA 148
                       170
                ....*....|...
gi 24659726 325 RQNYRIDDLFHSL 337
Cdd:cd04111 149 RTGDNVEEAFELL 161
Rho2 cd04129
Ras homology family 2 (Rho2) of small guanosine triphosphatases (GTPases); Rho2 is a fungal ...
168-334 3.86e-12

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: 64.85  E-value: 3.86e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 168 RLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFSM 247
Cdd:cd04129   3 KLVIVGDGACGKTSLLYVFTLGEFPEEYHPTVFENYVTDCRVDGKPVQLALWDTAGQEEYERLRPLSYSKAHVILIGFAI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 248 DSRESFEEVvrlrenilETKWAALnpgsgfKKKSLPKIPMILAGNKCD-RD---FKTVQVDEVM------GYIAGQDNCC 317
Cdd:cd04129  83 DTPDSLENV--------RTKWIEE------VRRYCPNVPVILVGLKKDlRQeavAKGNYATDEFvpiqqaKLVARAIGAK 148
                       170
                ....*....|....*..
gi 24659726 318 TFVECSARQNYRIDDLF 334
Cdd:cd04129 149 KYMECSALTGEGVDDVF 165
RhoA_like cd01870
Ras homology family A (RhoA)-like includes RhoA, RhoB and RhoC; The RhoA subfamily consists of ...
168-334 5.52e-12

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: 63.99  E-value: 5.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 168 RLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFSM 247
Cdd:cd01870   3 KLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 248 DSRESFeevvrlrENILEtKWaalnpgSGFKKKSLPKIPMILAGNKCD--RDFKTVQVDEVMGY----------IAGQDN 315
Cdd:cd01870  83 DSPDSL-------ENIPE-KW------TPEVKHFCPNVPIILVGNKKDlrNDEHTIRELAKMKQepvkpeegraMAEKIG 148
                       170
                ....*....|....*....
gi 24659726 316 CCTFVECSARQNYRIDDLF 334
Cdd:cd01870 149 AFGYLECSAKTKEGVREVF 167
Rab2 cd01866
Rab GTPase family 2 (Rab2); Rab2 is localized on cis-Golgi membranes and interacts with Golgi ...
167-334 6.02e-12

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: 63.60  E-value: 6.02e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIE-EFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVF 245
Cdd:cd01866   5 FKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGvEFGARMITIDGKQIKLQIWDTAGQESFRSITRSYYRGAAGALLVY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 246 SMDSRESFEEVVRLRENIletkwaalnpgsgfKKKSLPKIPMILAGNKCDRDFK-TVQVDEvmGYIAGQDNCCTFVECSA 324
Cdd:cd01866  85 DITRRETFNHLTSWLEDA--------------RQHSNSNMTIMLIGNKCDLESRrEVSYEE--GEAFAREHGLIFMETSA 148
                       170
                ....*....|
gi 24659726 325 RQNYRIDDLF 334
Cdd:cd01866 149 KTASNVEEAF 158
Wrch_1 cd04130
Wnt-1 responsive Cdc42 homolog (Wrch-1) is a Rho family GTPase similar to Cdc42; Wrch-1 (Wnt-1 ...
170-336 6.30e-12

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: 63.58  E-value: 6.30e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 170 VMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFSMDS 249
Cdd:cd04130   4 VLVGDGAVGKTSLIVSYTTNGYPTEYVPTAFDNFSVVVLVDGKPVRLQLCDTAGQDEFDKLRPLCYPDTDVFLLCFSVVN 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 250 RESFEEVvrlrenilETKWAalnPGSgfkKKSLPKIPMILAGNKCD-RDFKTVQVD-----------EVMGYIAGQDNCC 317
Cdd:cd04130  84 PSSFQNI--------SEKWI---PEI---RKHNPKAPIILVGTQADlRTDVNVLIQlarygekpvsqSRAKALAEKIGAC 149
                       170
                ....*....|....*....
gi 24659726 318 TFVECSARQNYRIDDLFHS 336
Cdd:cd04130 150 EYIECSALTQKNLKEVFDT 168
Rab12 cd04120
Rab GTPase family 12 (Rab12); Rab12 was first identified in canine cells, where it was ...
168-367 8.83e-12

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: 63.88  E-value: 8.83e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 168 RLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIE-EFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFS 246
Cdd:cd04120   2 QVIIIGSRGVGKTSLMERFTDDTFCEACKSTVGvDFKIKTVELRGKKIRLQIWDTAGQERFNSITSAYYRSAKGIILVYD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 247 MDSRESFEEVvrlrenileTKWAALnpgsgFKKKSLPKIPMILAGNK--C--DRDFKTVQVDEVMGYIAGQdnccTFVEC 322
Cdd:cd04120  82 ITKKETFDDL---------PKWMKM-----IDKYASEDAELLLVGNKldCetDREITRQQGEKFAQQITGM----RFCEA 143
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 24659726 323 SARQNYRIDDLFHSLF--TVSNLPLEMTPNHHRRLVSVFGAPSPLPP 367
Cdd:cd04120 144 SAKDNFNVDEIFLKLVddILKKMPLDILRNELSNSILSLQPEPEIPP 190
Rab23_like cd04106
Rab GTPase family 23 (Rab23)-like; Rab23-like subfamily. Rab23 is a member of the Rab family ...
168-337 3.08e-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: 61.69  E-value: 3.08e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 168 RLVMLGSSRAGKSSIVARFLGNRFEEAYTPTI-EEFHRK--LYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILV 244
Cdd:cd04106   2 KVIVVGNGNVGKSSMIQRFVKGIFTKDYKKTIgVDFLEKqiFLRQSDEDVRLMLWDTAGQEEFDAITKAYYRGAQACILV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 245 FSMDSRESFEEVVRLRENILETkwaalnpgsgfkkksLPKIPMILAGNKCDRDFKTVQVDEVMGYIAGQDNcCTFVECSA 324
Cdd:cd04106  82 FSTTDRESFEAIESWKEKVEAE---------------CGDIPMVLVQTKIDLLDQAVITNEEAEALAKRLQ-LPLFRTSV 145
                       170
                ....*....|...
gi 24659726 325 RQNYRIDDLFHSL 337
Cdd:cd04106 146 KDDFNVTELFEYL 158
Rab1_Ypt1 cd01869
Rab GTPase family 1 includes the yeast homolog Ypt1; Rab1/Ypt1 subfamily. Rab1 is found in ...
167-337 3.13e-11

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: 61.58  E-value: 3.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIE-EFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVF 245
Cdd:cd01869   3 FKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGvDFKIRTIELDGKTVKLQIWDTAGQERFRTITSSYYRGAHGIIIVY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 246 SMDSRESFEEVVRLRENIletkwaalnpgsgfKKKSLPKIPMILAGNKCD-RDFKTVQVDEVMGYiaGQDNCCTFVECSA 324
Cdd:cd01869  83 DVTDQESFNNVKQWLQEI--------------DRYASENVNKLLVGNKCDlTDKKVVDYTEAKEF--ADELGIPFLETSA 146
                       170
                ....*....|...
gi 24659726 325 RQNYRIDDLFHSL 337
Cdd:cd01869 147 KNATNVEEAFMTM 159
Rab11_like cd01868
Rab GTPase family 11 (Rab11)-like includes Rab11a, Rab11b, and Rab25; Rab11a, Rab11b, and ...
167-339 4.02e-11

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: 61.04  E-value: 4.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIE-EFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRlSFLTGDL-FILV 244
Cdd:cd01868   4 FKIVLIGDSGVGKSNLLSRFTRNEFNLDSKSTIGvEFATRTIQIDGKTIKAQIWDTAGQERYRAITS-AYYRGAVgALLV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 245 FSMDSRESFEEVVR----LRENiletkwaalnpgsgfkkkSLPKIPMILAGNKCD-RDFKTVQVDEVMGYiaGQDNCCTF 319
Cdd:cd01868  83 YDITKKSTFENVERwlkeLRDH------------------ADSNIVIMLVGNKSDlRHLRAVPTEEAKAF--AEKNGLSF 142
                       170       180
                ....*....|....*....|
gi 24659726 320 VECSARQNYRIDDLFHSLFT 339
Cdd:cd01868 143 IETSALDGTNVEEAFKQLLT 162
Rnd2_Rho7 cd04173
Rnd2/Rho7 GTPases; Rnd2/Rho7 is a member of the novel Rho subfamily Rnd, together with Rnd1 ...
168-354 9.68e-11

Rnd2/Rho7 GTPases; Rnd2/Rho7 is a member of the novel Rho subfamily Rnd, together with Rnd1/Rho6 and Rnd3/RhoE/Rho8. Rnd2/Rho7 is transiently expressed in radially migrating cells in the brain while they are within the subventricular zone of the hippocampus and cerebral cortex. These migrating cells typically develop into pyramidal neurons. Cells that exogenously expressed Rnd2/Rho7 failed to migrate to upper layers of the brain, suggesting that Rnd2/Rho7 plays a role in the radial migration and morphological changes of developing pyramidal neurons, and that Rnd2/Rho7 degradation is necessary for proper cellular migration. The Rnd2/Rho7 GEF Rapostlin is found primarily in the brain and together with Rnd2/Rho7 induces dendrite branching. Unlike Rnd1/Rho6 and Rnd3/RhoE/Rho8, which are RhoA antagonists, Rnd2/Rho7 binds the GEF Pragmin and significantly stimulates RhoA activity and Rho-A mediated cell contraction. Rnd2/Rho7 is also found to be expressed in spermatocytes and early spermatids, with male-germ-cell Rac GTPase-activating protein (MgcRacGAP), where it localizes to the Golgi-derived pro-acrosomal vesicle. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins.


Pssm-ID: 206736 [Multi-domain]  Cd Length: 221  Bit Score: 61.19  E-value: 9.68e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 168 RLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFSM 247
Cdd:cd04173   3 KIVVVGDTQCGKTALLHVFAKDNYPESYVPTVFENYTASFEIDKHRIELNMWDTSGSSYYDNVRPLAYPDSDAVLICFDI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 248 DSRESFEEVVRlreniletKWaalnpgSGFKKKSLPKIPMILAGNKCD--RDFKTVQ----------VDEVMGYIAGQDN 315
Cdd:cd04173  83 SRPETLDSVLK--------KW------QGETQEFCPNAKLVLVGCKLDmrTDLSTLRelskqrlipvTHEQGSLLARQLG 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 24659726 316 CCTFVECSARQNYR-IDDLFH--SLFTVSNLPLEMTPNHHRR 354
Cdd:cd04173 149 AVAYVECSSRMSENsVRDVFHvtTLASVRREHPSLKRSTSRR 190
Rop_like cd04133
Rho-related protein from plants (Rop)-like; The Rop (Rho-related protein from plants) ...
170-334 1.64e-10

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: 59.86  E-value: 1.64e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 170 VMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFSMDS 249
Cdd:cd04133   5 VTVGDGAVGKTCMLISYTSNTFPTDYVPTVFDNFSANVVVDGNTVNLGLWDTAGQEDYNRLRPLSYRGADVFLLAFSLIS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 250 RESFEEVvrLRENILETKWAAlnpgsgfkkkslPKIPMILAGNKCD-RDFK-------------TVQVDEVMGYIAgqdn 315
Cdd:cd04133  85 KASYENV--LKKWIPELRHYA------------PGVPIVLVGTKLDlRDDKqffadhpgavpitTAQGEELRKQIG---- 146
                       170
                ....*....|....*....
gi 24659726 316 CCTFVECSARQNYRIDDLF 334
Cdd:cd04133 147 AAAYIECSSKTQQNVKAVF 165
PLN03110 PLN03110
Rab GTPase; Provisional
167-339 1.99e-10

Rab GTPase; Provisional


Pssm-ID: 178657 [Multi-domain]  Cd Length: 216  Bit Score: 60.33  E-value: 1.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726  167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIE-EFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVF 245
Cdd:PLN03110  13 FKIVLIGDSGVGKSNILSRFTRNEFCLESKSTIGvEFATRTLQVEGKTVKAQIWDTAGQERYRAITSAYYRGAVGALLVY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726  246 SMDSRESFEEVVR-LREniletkwaalnpgsgFKKKSLPKIPMILAGNKCDRD-FKTVQVDEvmGYIAGQDNCCTFVECS 323
Cdd:PLN03110  93 DITKRQTFDNVQRwLRE---------------LRDHADSNIVIMMAGNKSDLNhLRSVAEED--GQALAEKEGLSFLETS 155
                        170
                 ....*....|....*.
gi 24659726  324 ARQNYRIDDLFHSLFT 339
Cdd:PLN03110 156 ALEATNVEKAFQTILL 171
Miro1 cd01893
Mitochondrial Rho family 1 (Miro1), N-terminal; Miro1 subfamily. Miro (mitochondrial Rho) ...
168-335 2.72e-10

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: 58.89  E-value: 2.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 168 RLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEfhrklYRIRNEVF----QLDILDTSGYHPFPAMRRLSFLTGDLFIL 243
Cdd:cd01893   4 RIVLIGDEGVGKSSLIMSLVSEEFPENVPRVLPE-----ITIPADVTpervPTTIVDTSSRPQDRANLAAEIRKANVICL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 244 VFSMDSRESFEevvRLRenileTKWAALNPGSGFkkkslpKIPMILAGNKCD-RDFK-TVQVDEVMGYIAGQ-DNCCTFV 320
Cdd:cd01893  79 VYSVDRPSTLE---RIR-----TKWLPLIRRLGV------KVPIILVGNKSDlRDGSsQAGLEEEMLPIMNEfREIETCV 144
                       170
                ....*....|....*
gi 24659726 321 ECSARQNYRIDDLFH 335
Cdd:cd01893 145 ECSAKTLINVSEVFY 159
PLN03118 PLN03118
Rab family protein; Provisional
167-337 4.23e-10

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 59.30  E-value: 4.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726  167 YRLVMLGSSRAGKSSIVARFLGNRFEEaYTPTIE-EFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVF 245
Cdd:PLN03118  15 FKILLIGDSGVGKSSLLVSFISSSVED-LAPTIGvDFKIKQLTVGGKRLKLTIWDTAGQERFRTLTSSYYRNAQGIILVY 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726  246 SMDSRESFEEVVRLreniletkWAalnpgsgfKKKSL----PKIPMILAGNKCDRDF-KTVQVDEvmGYIAGQDNCCTFV 320
Cdd:PLN03118  94 DVTRRETFTNLSDV--------WG--------KEVELystnQDCVKMLVGNKVDRESeRDVSREE--GMALAKEHGCLFL 155
                        170
                 ....*....|....*..
gi 24659726  321 ECSARQNYRIDDLFHSL 337
Cdd:PLN03118 156 ECSAKTRENVEQCFEEL 172
Ran cd00877
Ras-related nuclear proteins (Ran)/TC4 family of small GTPases; Ran GTPase is involved in ...
167-328 7.54e-10

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: 57.70  E-value: 7.54e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIE-EFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVF 245
Cdd:cd00877   1 FKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGvEVHPLDFHTNRGKIRFNVWDTAGQEKFGGLRDGYYIQGQCAIIMF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 246 SMDSRESFEEV-------VRLRENiletkwaalnpgsgfkkkslpkIPMILAGNKCDRDFKTVQvDEVMGYIAGQdnCCT 318
Cdd:cd00877  81 DVTSRVTYKNVpnwhrdlVRVCEN----------------------IPIVLCGNKVDIKDRKVK-PKQITFHRKK--NLQ 135
                       170
                ....*....|
gi 24659726 319 FVECSARQNY 328
Cdd:cd00877 136 YYEISAKSNY 145
Rab32_Rab38 cd04107
Rab GTPase families 18 (Rab18) and 32 (Rab32); Rab38/Rab32 subfamily. Rab32 and Rab38 are ...
167-337 7.55e-10

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: 58.48  E-value: 7.55e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIE-EFHRKLYRI-RNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILV 244
Cdd:cd04107   1 FKVLVIGDLGVGKTSIIKRYVHGVFSQHYKATIGvDFALKVIEWdPNTVVRLQLWDIAGQERFGGMTRVYYKGAVGAIIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 245 FSMDSRESFEEVVRLRENiLETKwAALNPGSgfkkkslpKIPMILAGNKCDRDFKTVQVD-EVMGYIAGQDNCCTFVECS 323
Cdd:cd04107  81 FDVTRPSTFEAVLKWKAD-LDSK-VTLPNGE--------PIPALLLANKCDLKKERLAKDpEQMDQFCKENGFIGWFETS 150
                       170
                ....*....|....
gi 24659726 324 ARQNYRIDDLFHSL 337
Cdd:cd04107 151 AKENINIEEAMRFL 164
PTZ00132 PTZ00132
GTP-binding nuclear protein Ran; Provisional
167-328 1.07e-09

GTP-binding nuclear protein Ran; Provisional


Pssm-ID: 240284 [Multi-domain]  Cd Length: 215  Bit Score: 58.17  E-value: 1.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726  167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIE-EFHR-KLYRIRNEVfQLDILDTSGYHPFPAMRRLSFLTGDLFILV 244
Cdd:PTZ00132  10 FKLILVGDGGVGKTTFVKRHLTGEFEKKYIPTLGvEVHPlKFYTNCGPI-CFNVWDTAGQEKFGGLRDGYYIKGQCAIIM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726  245 FSMDSRESFEEV-------VRLRENiletkwaalnpgsgfkkkslpkIPMILAGNKCD---RDFKTVQVdevmgyiagqd 314
Cdd:PTZ00132  89 FDVTSRITYKNVpnwhrdiVRVCEN----------------------IPIVLVGNKVDvkdRQVKARQI----------- 135
                        170       180
                 ....*....|....*....|..
gi 24659726  315 nccTF--------VECSARQNY 328
Cdd:PTZ00132 136 ---TFhrkknlqyYDISAKSNY 154
PLN03108 PLN03108
Rab family protein; Provisional
167-334 1.47e-09

Rab family protein; Provisional


Pssm-ID: 178655 [Multi-domain]  Cd Length: 210  Bit Score: 57.64  E-value: 1.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726  167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIE-EFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVF 245
Cdd:PLN03108   7 FKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGvEFGARMITIDNKPIKLQIWDTAGQESFRSITRSYYRGAAGALLVY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726  246 SMDSRESFEEVVRLRENIletkwaalnpgsgfKKKSLPKIPMILAGNKCDRDFK-TVQVDEvmGYIAGQDNCCTFVECSA 324
Cdd:PLN03108  87 DITRRETFNHLASWLEDA--------------RQHANANMTIMLIGNKCDLAHRrAVSTEE--GEQFAKEHGLIFMEASA 150
                        170
                 ....*....|
gi 24659726  325 RQNYRIDDLF 334
Cdd:PLN03108 151 KTAQNVEEAF 160
RJL cd04119
Rab GTPase family J-like (RabJ-like); RJLs are found in many protists and as chimeras with ...
168-338 2.29e-09

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: 56.21  E-value: 2.29e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 168 RLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIE-EFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFS 246
Cdd:cd04119   2 KVISMGNSGVGKSCIIKRYCEGRFVSKYLPTIGiDYGVKKVSVRNKEVRVNFFDLSGHPEYLEVRNEFYKDTQGVLLVYD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 247 MDSRESFEEvvrlreniLEtKWAALNPGSGFKKKSLPKIPMILAGNKCDRDFKTVqVDEVMGYIAGQDNCCTFVECSARQ 326
Cdd:cd04119  82 VTDRQSFEA--------LD-SWLKEMKQEGGPHGNMENIVVVVCANKIDLTKHRA-VSEDEGRLWAESKGFKYFETSACT 151
                       170
                ....*....|..
gi 24659726 327 NYRIDDLFHSLF 338
Cdd:cd04119 152 GEGVNEMFQTLF 163
RhoG cd01875
Ras homolog family, member G (RhoG) of small guanosine triphosphatases (GTPases); RhoG is a ...
168-334 2.49e-09

Ras homolog family, member G (RhoG) of small guanosine triphosphatases (GTPases); RhoG is a GTPase with high sequence similarity to members of the Rac subfamily, including the regions involved in effector recognition and binding. However, RhoG does not bind to known Rac1 and Cdc42 effectors, including proteins containing a Cdc42/Rac interacting binding (CRIB) motif. Instead, RhoG interacts directly with Elmo, an upstream regulator of Rac1, in a GTP-dependent manner and forms a ternary complex with Dock180 to induce activation of Rac1. The RhoG-Elmo-Dock180 pathway is required for activation of Rac1 and cell spreading mediated by integrin, as well as for neurite outgrowth induced by nerve growth factor. Thus RhoG activates Rac1 through Elmo and Dock180 to control cell morphology. RhoG has also been shown to play a role in caveolar trafficking and has a novel role in signaling the neutrophil respiratory burst stimulated by G protein-coupled receptor (GPCR) agonists. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins.


Pssm-ID: 133277 [Multi-domain]  Cd Length: 191  Bit Score: 56.56  E-value: 2.49e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 168 RLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFSM 247
Cdd:cd01875   5 KCVVVGDGAVGKTCLLICYTTNAFPKEYIPTVFDNYSAQTAVDGRTVSLNLWDTAGQEEYDRLRTLSYPQTNVFIICFSI 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 248 DSRESFEEVvrlrenilETKWaalNPGSGfkkKSLPKIPMILAGNKCD--RDFKTVQ----------VDEVMGYIAGQDN 315
Cdd:cd01875  85 ASPSSYENV--------RHKW---HPEVC---HHCPNVPILLVGTKKDlrNDADTLKklkeqgqapiTPQQGGALAKQIH 150
                       170
                ....*....|....*....
gi 24659726 316 CCTFVECSARQNYRIDDLF 334
Cdd:cd01875 151 AVKYLECSALNQDGVKEVF 169
Rab3 cd01865
Rab GTPase family 3 contains Rab3A, Rab3B, Rab3C and Rab3D; The Rab3 subfamily contains Rab3A, ...
167-340 7.29e-09

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: 54.92  E-value: 7.29e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIE-EFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVF 245
Cdd:cd01865   2 FKLLIIGNSSVGKTSFLFRYADDSFTSAFVSTVGiDFKVKTVYRNDKRIKLQIWDTAGQERYRTITTAYYRGAMGFILMY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 246 SMDSRESFEEVvrlrenileTKWAalnpgSGFKKKSLPKIPMILAGNKCD-RDFKTVQVDEvmGYIAGQDNCCTFVECSA 324
Cdd:cd01865  82 DITNEESFNAV---------QDWS-----TQIKTYSWDNAQVILVGNKCDmEDERVVSAER--GRQLADQLGFEFFEASA 145
                       170
                ....*....|....*.
gi 24659726 325 RQNYRIDDLFHSLFTV 340
Cdd:cd01865 146 KENINVKQVFERLVDI 161
Cdc42 cd01874
cell division cycle 42 (Cdc42) is a small GTPase of the Rho family; Cdc42 is an essential ...
168-324 9.08e-09

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


Pssm-ID: 206664 [Multi-domain]  Cd Length: 175  Bit Score: 54.49  E-value: 9.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 168 RLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFSM 247
Cdd:cd01874   3 KCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAGQEDYDRLRPLSYPQTDVFLVCFSV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 248 DSRESFEEVvrlREniletKWAALnpgsgfKKKSLPKIPMILAGNKCD-RDFKTVQ-----------VDEVMGYIAGQDN 315
Cdd:cd01874  83 VSPSSFENV---KE-----KWVPE------ITHHCPKTPFLLVGTQIDlRDDPSTIeklaknkqkpiTPETGEKLARDLK 148

                ....*....
gi 24659726 316 CCTFVECSA 324
Cdd:cd01874 149 AVKYVECSA 157
RAN smart00176
Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases; Ran is involved in the ...
172-334 2.35e-08

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: 53.86  E-value: 2.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726    172 LGSSRAGKSSIVARFLGNRFEEAYTPTIE-EFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFSMDSR 250
Cdd:smart00176   1 VGDGGTGKTTFVKRHLTGEFEKKYVATLGvEVHPLVFHTNRGPIRFNVWDTAGQEKFGGLRDGYYIQGQCAIIMFDVTAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726    251 ESFEEV-------VRLRENiletkwaalnpgsgfkkkslpkIPMILAGNKCDRDFKTVQVDEVMGYiagQDNCCTFVECS 323
Cdd:smart00176  81 VTYKNVpnwhrdlVRVCEN----------------------IPIVLCGNKVDVKDRKVKAKSITFH---RKKNLQYYDIS 135
                          170
                   ....*....|.
gi 24659726    324 ARQNYRIDDLF 334
Cdd:smart00176 136 AKSNYNFEKPF 146
Rab15 cd04117
Rab GTPase family 15 (Rab15); Rab15 colocalizes with the transferrin receptor in early ...
167-337 1.08e-07

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: 51.13  E-value: 1.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIE-EFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVF 245
Cdd:cd04117   1 FRLLLIGDSGVGKTCLLCRFTDNEFHSSHISTIGvDFKMKTIEVDGIKVRIQIWDTAGQERYQTITKQYYRRAQGIFLVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 246 SMDSRESFEEVVrlreniletKWAalnpgSGFKKKSLPKIPMILAGNKCDRDfKTVQVDEVMGYIAGQDNCCTFVECSAR 325
Cdd:cd04117  81 DISSERSYQHIM---------KWV-----SDVDEYAPEGVQKILIGNKADEE-QKRQVGDEQGNKLAKEYGMDFFETSAC 145
                       170
                ....*....|..
gi 24659726 326 QNYRIDDLFHSL 337
Cdd:cd04117 146 TNKNIKESFTRL 157
RabL2 cd04124
Rab GTPase-like family 2 (Rab-like2); RabL2 (Rab-like2) subfamily. RabL2s are novel Rab ...
168-302 1.10e-07

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: 51.40  E-value: 1.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 168 RLVMLGSSRAGKSSIVARFLGNRFEEAYTPTieeFHRKLYR----IRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFIL 243
Cdd:cd04124   2 KIILLGDSAVGKSKLVERFLMDGYEPQQLST---YALTLYKhnakFEGKTILVDFWDTAGQERFQTMHASYYHKAHACIL 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24659726 244 VFSMDSRESFEEVvrlrenileTKWAalnpgsGFKKKSLPKIPMILAGNKCDRDFKTVQ 302
Cdd:cd04124  79 VFDVTRKITYKNL---------SKWY------EELREYRPEIPCIVVANKIDLDPSVTQ 122
PLN03071 PLN03071
GTP-binding nuclear protein Ran; Provisional
167-334 1.47e-07

GTP-binding nuclear protein Ran; Provisional


Pssm-ID: 178620 [Multi-domain]  Cd Length: 219  Bit Score: 52.06  E-value: 1.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726  167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIE------EFHRKLYRIRnevfqLDILDTSGYHPFPAMRRLSFLTGDL 240
Cdd:PLN03071  14 FKLVIVGDGGTGKTTFVKRHLTGEFEKKYEPTIGvevhplDFFTNCGKIR-----FYCWDTAGQEKFGGLRDGYYIHGQC 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726  241 FILVFSMDSRESFEEV-------VRLRENIletkwaalnpgsgfkkkslpkiPMILAGNKCDRDFKTVQVDEVMGYiagQ 313
Cdd:PLN03071  89 AIIMFDVTARLTYKNVptwhrdlCRVCENI----------------------PIVLCGNKVDVKNRQVKAKQVTFH---R 143
                        170       180
                 ....*....|....*....|.
gi 24659726  314 DNCCTFVECSARQNYRIDDLF 334
Cdd:PLN03071 144 KKNLQYYEISAKSNYNFEKPF 164
Rac1_like cd01871
Ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1)-like ...
170-324 1.65e-07

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: 50.97  E-value: 1.65e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 170 VMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFSMDS 249
Cdd:cd01871   5 VVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 250 RESFEEVvrlrenilETKWaalNPGSgfkKKSLPKIPMILAGNKCD-----------RDFKTVQVDEVMGYIAGQD-NCC 317
Cdd:cd01871  85 PASFENV--------RAKW---YPEV---RHHCPNTPIILVGTKLDlrddkdtieklKEKKLTPITYPQGLAMAKEiGAV 150

                ....*..
gi 24659726 318 TFVECSA 324
Cdd:cd01871 151 KYLECSA 157
Rab14 cd04122
Rab GTPase family 14 (Rab14); Rab14 GTPases are localized to biosynthetic compartments, ...
167-334 3.35e-07

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: 49.83  E-value: 3.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIE-EFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVF 245
Cdd:cd04122   3 FKYIIIGDMGVGKSCLLHQFTEKKFMADCPHTIGvEFGTRIIEVNGQKIKLQIWDTAGQERFRAVTRSYYRGAAGALMVY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 246 SMDSRESFEEVvrlrenileTKWAAlnpgsGFKKKSLPKIPMILAGNKCDRD-FKTVQVDEVMGYiaGQDNCCTFVECSA 324
Cdd:cd04122  83 DITRRSTYNHL---------SSWLT-----DARNLTNPNTVIFLIGNKADLEaQRDVTYEEAKQF--ADENGLLFLECSA 146
                       170
                ....*....|
gi 24659726 325 RQNYRIDDLF 334
Cdd:cd04122 147 KTGENVEDAF 156
Rab8_Rab10_Rab13_like cd01867
Rab GTPase families 8, 10, 13 (Rab8, Rab10, Rab13); Rab8/Sec4/Ypt2 are known or suspected to ...
167-337 5.33e-07

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: 49.19  E-value: 5.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 167 YRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIE-EFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRlSFLTGDL-FILV 244
Cdd:cd01867   4 FKLLLIGDSGVGKSCLLLRFSEDSFNPSFISTIGiDFKIRTIELDGKKIKLQIWDTAGQERFRTITT-SYYRGAMgIILV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 245 FSMDSRESFEEVVRLRENIletkwaalnpgsgfKKKSLPKIPMILAGNKCDRDFKTvQVDEVMGYIAGQDNCCTFVECSA 324
Cdd:cd01867  83 YDITDEKSFENIKNWMRNI--------------DEHASEDVERMLVGNKCDMEEKR-VVSKEEGEALAREYGIKFLETSA 147
                       170
                ....*....|...
gi 24659726 325 RQNYRIDDLFHSL 337
Cdd:cd01867 148 KANINVEEAFLTL 160
Rab24 cd04118
Rab GTPase family 24 (Rab24); Rab24 is distinct from other Rabs in several ways. It exists ...
168-337 2.20e-06

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: 47.94  E-value: 2.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 168 RLVMLGSSRAGKSSIVARFLGNRF-EEAYTPTI-EEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVF 245
Cdd:cd04118   2 KVVMLGKESVGKTSLVERYVHHRFlVGPYQNTIgAAFVAKRMVVGERVVTLGIWDTAGSERYEAMSRIYYRGAKAAIVCY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 246 SMDSRESFEEVvrlrenileTKWAalnpgsgfkkKSL----PKIPMILAGNKCD-----RDFKTVQVDEVMGY---IAGQ 313
Cdd:cd04118  82 DLTDSSSFERA---------KFWV----------KELqnleEHCKIYLCGTKSDlieqdRSLRQVDFHDVQDFadeIKAQ 142
                       170       180
                ....*....|....*....|....
gi 24659726 314 dncctFVECSARQNYRIDDLFHSL 337
Cdd:cd04118 143 -----HFETSSKTGQNVDELFQKV 161
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
168-334 3.08e-06

ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions.


Pssm-ID: 206644 [Multi-domain]  Cd Length: 158  Bit Score: 46.80  E-value: 3.08e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 168 RLVMLGSSRAGKSSIVARFLGNRFEEAyTPTIeEFHRKLYRIRNevFQLDILDTSGYHPFPAMRRLSFLTGDlfILVFSM 247
Cdd:cd00878   1 RILMLGLDGAGKTTILYKLKLGEVVTT-IPTI-GFNVETVEYKN--VKFTVWDVGGQDKIRPLWKHYYENTD--GLIFVV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 248 DS--RESFEEVVRLRENILetkwaalnpgsgfKKKSLPKIPMILAGNKCDR-DFKTVQ-VDEVMGYIAGQDNCCTFVECS 323
Cdd:cd00878  75 DSsdRERIEEAKNELHKLL-------------NEEELKGAPLLILANKQDLpGALTESeLIELLGLESIKGRRWHIQPCS 141
                       170
                ....*....|.
gi 24659726 324 ARQNYRIDDLF 334
Cdd:cd00878 142 AVTGDGLDEGL 152
Rnd1_Rho6 cd04174
Rnd1/Rho6 GTPases; Rnd1/Rho6 is a member of the novel Rho subfamily Rnd, together with Rnd2 ...
161-343 1.25e-05

Rnd1/Rho6 GTPases; Rnd1/Rho6 is a member of the novel Rho subfamily Rnd, together with Rnd2/Rho7 and Rnd3/RhoE/Rho8. Rnd1/Rho6 binds GTP but does not hydrolyze it to GDP, indicating that it is constitutively active. In rat, Rnd1/Rho6 is highly expressed in the cerebral cortex and hippocampus during synapse formation, and plays a role in spine formation. Rnd1/Rho6 is also expressed in the liver and in endothelial cells, and is upregulated in uterine myometrial cells during pregnancy. Like Rnd3/RhoE/Rho8, Rnd1/Rho6 is believed to function as an antagonist to RhoA. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206737 [Multi-domain]  Cd Length: 232  Bit Score: 46.20  E-value: 1.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 161 PSAKNCyRLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDL 240
Cdd:cd04174   9 PLVVRC-KLVLVGDVQCGKTAMLQVLAKDCYPETYVPTVFENYTACLETEEQRVELSLWDTSGSPYYDNVRPLCYSDSDA 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 241 FILVFSMDSRESFEEVV-RLRENILETkwaalnpgsgfkkksLPKIPMILAGNKCD--RDFKTV-----QVDEVMGY--- 309
Cdd:cd04174  88 VLLCFDISRPEIFDSALkKWRAEILDY---------------CPSTRILLIGCKTDlrTDLSTLmelsnQKQAPISYeqg 152
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 24659726 310 --IAGQDNCCTFVECSArqnYRIDDLFHSLFTVSNL 343
Cdd:cd04174 153 caMAKQLGAEAYLECSA---FTSEKSIHSIFRTASL 185
Centaurin_gamma cd04103
Centaurin gamma (CENTG) GTPase; The centaurins (alpha, beta, gamma, and delta) are large, ...
168-293 4.81e-05

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: 43.64  E-value: 4.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 168 RLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIEEFHRKLYrIRNEVFQLDILDTSGYhpfPAMRRLSFLtgDLFILVFSM 247
Cdd:cd04103   2 KLGIVGNLRSGKSALVHRYLTGSYVQLESPEGGRFKKEVL-VDGQSHLLLIRDEGGA---PDAQFAGWV--DAVIFVFSL 75
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 24659726 248 DSRESFEEVVRLRenileTKWAALNPGSGfkkkslpkIPMILAGNK 293
Cdd:cd04103  76 EDEASFQTVYRLY-----HQLSSYRNISE--------IPLILVGTQ 108
RabL4 cd04101
Rab GTPase-like family 4 (Rab-like4); RabL4 (Rab-like4) subfamily. RabL4s are novel proteins ...
168-337 4.91e-05

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: 43.67  E-value: 4.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 168 RLVMLGSSRAGKSSIVARFL--GNRFEEAYTPTIE-EFHRKLYRI---RNEVfQLDILDTSGYHPFPAMRRLSFLTGDLF 241
Cdd:cd04101   2 QCAVVGDPAVGKSALVQMFHsdGATFQKNYTMTTGcDLVVKTVPVpdtSDSV-ELFIFDSAGQELFSDMVENVWEQPAVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 242 ILVFSMDSRESFEEVVRLRENILETkwaalNPGSGfkkkslpkIPMILAGNKCDRDFKTvQVDEVMGYIAGQDNCCTFVE 321
Cdd:cd04101  81 CVVYDVTNEVSFNNCSRWINRVRTH-----SHGLH--------TPGVLVGNKCDLTDRR-EVDAAQAQALAQANTLKFYE 146
                       170
                ....*....|....*.
gi 24659726 322 CSARQNYRIDDLFHSL 337
Cdd:cd04101 147 TSAKEGVGYEAPFLSL 162
Rab27A cd04127
Rab GTPase family 27a (Rab27a); The Rab27a subfamily consists of Rab27a and its highly ...
168-306 1.92e-04

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: 42.10  E-value: 1.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 168 RLVMLGSSRAGKSSIVARFLGNRFEEAYTPTIE-EFHRK--LY--------RIRNEVFQLDILDTSGYHPFPAMRRLSFL 236
Cdd:cd04127   6 KLLALGDSGVGKTTFLYRYTDNKFNPKFITTVGiDFREKrvVYnsqgpdgtSGKAFRVHLQLWDTAGQERFRSLTTAFFR 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24659726 237 TGDLFILVFSMDSRESFEEvVRLRENILETKWAALNPGsgfkkkslpkipMILAGNKCD----RDFKTVQVDEV 306
Cdd:cd04127  86 DAMGFLLMFDLTSEQSFLN-VRNWMSQLQAHAYCENPD------------IVLIGNKADlpdqREVSERQAREL 146
Spg1 cd04128
Septum-promoting GTPase (Spg1); Spg1p. Spg1p (septum-promoting GTPase) was first identified in ...
171-345 2.45e-04

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: 41.61  E-value: 2.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 171 MLGSSRAGKSSIVARFLGNRFEEAYTPTIE-EFHRKLYRIRNEVFQLDILDTSGYHPFPAMRRLSFLTGDLFILVFSMDS 249
Cdd:cd04128   5 LLGDAQIGKTSLMVKYVEGEFDEEYIQTLGvNFMEKTISIRGTEITFSIWDLGGQREFINMLPLVCKDAVAILFMFDLTR 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 250 RESFeevvrlrENILEtkWaaLNPGSGFKKKSLPkipmILAGNKCDR------DFKTVQVDEVMGYiaGQDNCCTFVECS 323
Cdd:cd04128  85 KSTL-------NSIKE--W--YRQARGFNKTAIP----ILVGTKYDLfadlppEEQEEITKQARKY--AKAMKAPLIFCS 147
                       170       180
                ....*....|....*....|...
gi 24659726 324 ARQNYRIDDLFH-SLFTVSNLPL 345
Cdd:cd04128 148 TSHSINVQKIFKfVLAKVFDLPL 170
Miro2 cd01892
Mitochondrial Rho family 2 (Miro2), C-terminal; Miro2 subfamily. Miro (mitochondrial Rho) ...
165-306 4.79e-04

Mitochondrial Rho family 2 (Miro2), C-terminal; Miro2 subfamily. Miro (mitochondrial Rho) proteins have tandem GTP-binding domains separated by a linker region containing putative calcium-binding EF hand motifs. Genes encoding Miro-like proteins were found in several eukaryotic organisms. This CD represents the putative GTPase domain in the C terminus of Miro proteins. These atypical Rho GTPases have roles in mitochondrial homeostasis and apoptosis. Most Rho proteins contain a lipid modification site at the C-terminus; however, Miro is one of few Rho subfamilies that lack this feature.


Pssm-ID: 206679  Cd Length: 180  Bit Score: 40.69  E-value: 4.79e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659726 165 NCYrlvMLGSSRAGKSSIVARFLGNRF-EEAYTPTIEEFH----------RKlYRIRNEVFQLDildtsgyhPFPAMRRL 233
Cdd:cd01892   6 LCF---VLGAKGSGKSALLQAFLGRSFsQNAYSPTIKPRYavntvevpgqEK-YLILREVGEDE--------EAILLNDA 73
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24659726 234 SFLTGDLFILVFSMDSRESFEEVVRLREniletkwaalnpgsgfKKKSLPKIPMILAGNKCDRDfKTVQVDEV 306
Cdd:cd01892  74 ELAACDVACLVYDSSDPNSFSYCAEVYK----------------KYFMLGEIPCLFVAAKADLD-EQQQRAEV 129
 
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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