NCBI Conserved Domain Search

Conserved domains on [gi|349585207|ref|NP_001231817|]

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arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1 isoform 3 [Homo sapiens]

Protein Classification

Centaurin_gamma domain-containing protein( domain architecture ID 10134846)

Centaurin_gamma domain-containing protein

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

Centaurin_gamma

cd04103

Centaurin gamma (CENTG) GTPase; The centaurins (alpha, beta, gamma, and delta) are large, ...

72-229

4.90e-117

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: 337.54 E-value: 4.90e-117

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  72 LKVGIVGNLASGKSALVHRYLTGTYVQEESPEGGRFKKEIVVDGQSYLLLIRDEGGPPEAQFAMWVDAVIFVFSLEDEIS 151
Cdd:cd04103    1 LKLGIVGNLRSGKSALVHRYLTGSYVQLESPEGGRFKKEVLVDGQSHLLLIRDEGGAPDAQFAGWVDAVIFVFSLEDEAS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 349585207 152 FQTVYHYYSRMANYRNTSEIPLVLVGTQDAISSANPRVIDDARARKLSNDLKRCTYYETCATYGLNVERVFQDVAQKI 229
Cdd:cd04103   81 FQTVYRLYHQLSSYRNISEIPLILVGTQDAISASNPRVIDDARARQLCADMKRCSYYETCATYGLNVERVFQEAAQKI 158

Name

Accession

Description

Interval

E-value

Centaurin_gamma

cd04103

Centaurin gamma (CENTG) GTPase; The centaurins (alpha, beta, gamma, and delta) are large, ...

72-229

4.90e-117

Pssm-ID: 133303 Cd Length: 158 Bit Score: 337.54 E-value: 4.90e-117

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  72 LKVGIVGNLASGKSALVHRYLTGTYVQEESPEGGRFKKEIVVDGQSYLLLIRDEGGPPEAQFAMWVDAVIFVFSLEDEIS 151
Cdd:cd04103    1 LKLGIVGNLRSGKSALVHRYLTGSYVQLESPEGGRFKKEVLVDGQSHLLLIRDEGGAPDAQFAGWVDAVIFVFSLEDEAS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 349585207 152 FQTVYHYYSRMANYRNTSEIPLVLVGTQDAISSANPRVIDDARARKLSNDLKRCTYYETCATYGLNVERVFQDVAQKI 229
Cdd:cd04103   81 FQTVYRLYHQLSSYRNISEIPLILVGTQDAISASNPRVIDDARARQLCADMKRCSYYETCATYGLNVERVFQEAAQKI 158

RAS

smart00173

Ras subfamily of RAS small GTPases; Similar in fold and function to the bacterial EF-Tu GTPase. ...

73-235

4.95e-17

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: 77.98 E-value: 4.95e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207    73 KVGIVGNLASGKSALVHRYLTGTYVQEESP--EGGrFKKEIVVDGQSYLLLIRDEGGppEAQF-AM---WV---DAVIFV 143
Cdd:smart00173   2 KLVVLGSGGVGKSALTIQFIQGHFVDDYDPtiEDS-YRKQIEIDGEVCLLDILDTAG--QEEFsAMrdqYMrtgEGFLLV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207   144 FSLEDEISFQTVYHYYSRMANYRNTSEIPLVLVGTQ-DAIssaNPRVIDDARARKLSNDLKrCTYYETCATYGLNVERVF 222
Cdd:smart00173  79 YSITDRQSFEEIKKFREQILRVKDRDDVPIVLVGNKcDLE---SERVVSTEEGKELARQWG-CPFLETSAKERVNVDEAF 154

                          170
                   ....*....|...
gi 349585207   223 QDVAQKIvatRKK 235
Cdd:smart00173 155 YDLVREI---RKK 164

Ras

pfam00071

Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...

73-229

1.91e-16

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: 76.01 E-value: 1.91e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207   73 KVGIVGNLASGKSALVHRYLTGTYVQE-ESPEGGRFK-KEIVVDGQSYLLLIRDEGGPPE-----AQFAMWVDAVIFVFS 145
Cdd:pfam00071   1 KLVLVGDGGVGKSSLLIRFTQNKFPEEyIPTIGVDFYtKTIEVDGKTVKLQIWDTAGQERfralrPLYYRGADGFLLVYD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  146 LEDEISFQTVYHYYSRMANYRNTSeIPLVLVGTQ-DAISSanpRVIDDARARKLSNDLKrCTYYETCATYGLNVERVFQD 224
Cdd:pfam00071  81 ITSRDSFENVKKWVEEILRHADEN-VPIVLVGNKcDLEDQ---RVVSTEEGEALAKELG-LPFMETSAKTNENVEEAFEE 155


                  ....*
gi 349585207  225 VAQKI 229
Cdd:pfam00071 156 LAREI 160

Gem1

COG1100

GTPase SAR1 family domain [General function prediction only];

71-229

7.48e-13

GTPase SAR1 family domain [General function prediction only];

Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 66.54 E-value: 7.48e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  71 ELKVGIVGNLASGKSALVHRYLTGTYVQEE--SPEG-GRFKKEIVVDGQSYLLLIRDEGGPPE-----AQFAMWV---DA 139
Cdd:COG1100    3 EKKIVVVGTGGVGKTSLVNRLVGDIFSLEKylSTNGvTIDKKELKLDGLDVDLVIWDTPGQDEfretrQFYARQLtgaSL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 140 VIFVFSLEDEISFQTVYHYYSRMANYRNTSeiPLVLVGTQ-DAISsaNPRVIDDARARKLSNDLKRCTYYETCATYGLNV 218
Cdd:COG1100   83 YLFVVDGTREETLQSLYELLESLRRLGKKS--PIILVLNKiDLYD--EEEIEDEERLKEALSEDNIVEVVATSAKTGEGV 158

                        170
                 ....*....|.
gi 349585207 219 ERVFQDVAQKI 229
Cdd:COG1100  159 EELFAALAEIL 169

PTZ00369

Ras-like protein; Provisional

71-229

1.26e-08

Ras-like protein; Provisional

Pssm-ID: 240385 [Multi-domain] Cd Length: 189 Bit Score: 54.48 E-value: 1.26e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  71 ELKVGIVGNLASGKSALVHRYLTGTYVQEESPE-GGRFKKEIVVDGQSYLLLIRDEGGPPE-----AQFAMWVDAVIFVF 144
Cdd:PTZ00369   5 EYKLVVVGGGGVGKSALTIQFIQNHFIDEYDPTiEDSYRKQCVIDEETCLLDILDTAGQEEysamrDQYMRTGQGFLCVY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 145 SLEDEISFQTVYHYYSRMANYRNTSEIPLVLVGTQDAISSAnpRVIDDARARKLSNDLKrCTYYETCATYGLNVERVFQD 224
Cdd:PTZ00369  85 SITSRSSFEEIASFREQILRVKDKDRVPMILVGNKCDLDSE--RQVSTGEGQELAKSFG-IPFLETSAKQRVNVDEAFYE 161


                 ....*
gi 349585207 225 VAQKI 229
Cdd:PTZ00369 162 LVREI 166

small_GTP

TIGR00231

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...

71-179

3.94e-05

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: 43.51 E-value: 3.94e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207   71 ELKVGIVGNLASGKSALVHRYLTGTYVQEESPEGGRF---KKEIVVDGQSYLLLIRDEGGpPEAQFAMW------VDAVI 141
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRnyvTTVIEEDGKTYKFNLLDTAG-QEDYDAIRrlyypqVERSL 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 349585207  142 FVFSLED-EISFQTVYHYYSRMANYRNTSEIPLVLVGTQ 179
Cdd:TIGR00231  80 RVFDIVIlVLDVEEILEKQTKEIIHHADSGVPIILVGNK 118

Name

Accession

Description

Interval

E-value

Centaurin_gamma

cd04103

Centaurin gamma (CENTG) GTPase; The centaurins (alpha, beta, gamma, and delta) are large, ...

72-229

4.90e-117

Pssm-ID: 133303 Cd Length: 158 Bit Score: 337.54 E-value: 4.90e-117

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  72 LKVGIVGNLASGKSALVHRYLTGTYVQEESPEGGRFKKEIVVDGQSYLLLIRDEGGPPEAQFAMWVDAVIFVFSLEDEIS 151
Cdd:cd04103    1 LKLGIVGNLRSGKSALVHRYLTGSYVQLESPEGGRFKKEVLVDGQSHLLLIRDEGGAPDAQFAGWVDAVIFVFSLEDEAS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 349585207 152 FQTVYHYYSRMANYRNTSEIPLVLVGTQDAISSANPRVIDDARARKLSNDLKRCTYYETCATYGLNVERVFQDVAQKI 229
Cdd:cd04103   81 FQTVYRLYHQLSSYRNISEIPLILVGTQDAISASNPRVIDDARARQLCADMKRCSYYETCATYGLNVERVFQEAAQKI 158

Ras

cd00876

Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ...

73-229

1.97e-22

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: 92.97 E-value: 1.97e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  73 KVGIVGNLASGKSALVHRYLTGTYVQEESP-EGGRFKKEIVVDGQSYLLLI-----RDEGGPPEAQFAMWVDAVIFVFSL 146
Cdd:cd00876    1 KLVVLGAGGVGKSALTIRFVSGEFVEEYDPtIEDSYRKQIVVDGETYTLDIldtagQEEFSAMRDQYIRNGDGFILVYSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 147 EDEISFQTVYHYYSRMANYRNTSEIPLVLVGTQdaISSANPRVIDDARARKLSNDLKrCTYYETCATYGLNVERVFQDVA 226
Cdd:cd00876   81 TSRESFEEIKNIREQILRVKDKEDVPIVLVGNK--CDLENERQVSTEEGEALAEEWG-CPFLETSAKTNINIDELFNTLV 157


                 ...
gi 349585207 227 QKI 229
Cdd:cd00876  158 REI 160

Rab

cd00154

Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...

72-227

1.24e-18

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: 82.12 E-value: 1.24e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  72 LKVGIVGNLASGKSALVHRYLTGTYVQEESPE-GGRFK-KEIVVDGQSYLLLIRDEGGppeaQ--F----AMW---VDAV 140
Cdd:cd00154    1 FKIVLIGDSGVGKTSLLLRFVDNKFSENYKSTiGVDFKsKTIEVDGKKVKLQIWDTAG----QerFrsitSSYyrgAHGA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 141 IFVFSLEDEISFQTVYHYYSrMANYRNTSEIPLVLVGTQdaISSANPRVIDDARARKLSNDLKrCTYYETCATYGLNVER 220
Cdd:cd00154   77 ILVYDVTNRESFENLDKWLN-ELKEYAPPNIPIILVGNK--SDLEDERQVSTEEAQQFAKENG-LLFFETSAKTGENVDE 152


                 ....*..
gi 349585207 221 VFQDVAQ 227
Cdd:cd00154  153 AFESLAR 159

RheB

cd04137

Ras Homolog Enriched in Brain (RheB) is a small GTPase; Rheb (Ras Homolog Enriched in Brain) ...

73-229

2.74e-17

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: 79.21 E-value: 2.74e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  73 KVGIVGNLASGKSALVHRYLTGTYVQEESP--EGgRFKKEIVVDGQSYLLLIRDEGGPPE-----AQFAMWVDAVIFVFS 145
Cdd:cd04137    3 KIAVLGSRSVGKSSLTVQFVEGHFVESYYPtiEN-TFSKIITYKGQEYHLEIVDTAGQDEysilpQKYSIGIHGYILVYS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 146 LEDEISFQTVYHYYSRMANYRNTSEIPLVLVGTQDAISSAnpRVIDDARARKLSNDLKrCTYYETCATYGLNVERVFQDV 225
Cdd:cd04137   82 VTSRKSFEVVKVIYDKILDMLGKESVPIVLVGNKSDLHME--RQVSAEEGKKLAESWG-AAFLESSAKENENVEEAFELL 158


                 ....
gi 349585207 226 AQKI 229
Cdd:cd04137  159 IEEI 162

RSR1

cd04177

RSR1/Bud1p family GTPase; RSR1/Bud1p is a member of the Rap subfamily of the Ras family that ...

71-232

2.90e-17

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: 78.68 E-value: 2.90e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  71 ELKVGIVGNLASGKSALVHRYLTGTYVQEESPE-GGRFKKEIVVDGQSYLLLIRDEGGppEAQF-AM---WVDA---VIF 142
Cdd:cd04177    1 DYKIVVLGAGGVGKSALTVQFVQNVFIESYDPTiEDSYRKQVEIDGRQCDLEILDTAG--TEQFtAMrelYIKSgqgFLL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 143 VFSLEDEISFQTVYHYYSRMANYRNTSEIPLVLVGTQ-DAIssaNPRVIDDARARKLSNDLKRCTYYETCATYGLNVERV 221
Cdd:cd04177   79 VYSVTSEASLNELGELREQVLRIKDSDNVPMVLVGNKaDLE---DDRQVSREDGVSLSQQWGNVPFYETSARKRTNVDEV 155

                        170
                 ....*....|.
gi 349585207 222 FQDVAQKIVAT 232
Cdd:cd04177  156 FIDLVRQIICV 166

RAS

smart00173

Ras subfamily of RAS small GTPases; Similar in fold and function to the bacterial EF-Tu GTPase. ...

73-235

4.95e-17

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: 77.98 E-value: 4.95e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207    73 KVGIVGNLASGKSALVHRYLTGTYVQEESP--EGGrFKKEIVVDGQSYLLLIRDEGGppEAQF-AM---WV---DAVIFV 143
Cdd:smart00173   2 KLVVLGSGGVGKSALTIQFIQGHFVDDYDPtiEDS-YRKQIEIDGEVCLLDILDTAG--QEEFsAMrdqYMrtgEGFLLV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207   144 FSLEDEISFQTVYHYYSRMANYRNTSEIPLVLVGTQ-DAIssaNPRVIDDARARKLSNDLKrCTYYETCATYGLNVERVF 222
Cdd:smart00173  79 YSITDRQSFEEIKKFREQILRVKDRDDVPIVLVGNKcDLE---SERVVSTEEGKELARQWG-CPFLETSAKERVNVDEAF 154

                          170
                   ....*....|...
gi 349585207   223 QDVAQKIvatRKK 235
Cdd:smart00173 155 YDLVREI---RKK 164

Rap_like

cd04136

Rap-like family consists of Rap1, Rap2 and RSR1; The Rap subfamily consists of the Rap1, Rap2, ...

71-229

1.36e-16

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: 76.83 E-value: 1.36e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  71 ELKVGIVGNLASGKSALVHRYLTGTYVQEESPE-GGRFKKEIVVDGQSYLLLIRDEGGppEAQFAMWVD-------AVIF 142
Cdd:cd04136    1 EYKLVVLGSGGVGKSALTVQFVQGIFVDKYDPTiEDSYRKQIEVDCQQCMLEILDTAG--TEQFTAMRDlyikngqGFAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 143 VFSLEDEISFQTVYHYYSRMANYRNTSEIPLVLVGTQdaISSANPRVIDDARARKLSNDLKRCTYYETCATYGLNVERVF 222
Cdd:cd04136   79 VYSITAQQSFNDLQDLREQILRVKDTEDVPMILVGNK--CDLEDERVVSKEEGQNLARQWGNCPFLETSAKSKINVDEIF 156


                 ....*..
gi 349585207 223 QDVAQKI 229
Cdd:cd04136  157 YDLVRQI 163

small_GTPase

smart00010

Small GTPase of the Ras superfamily; ill-defined subfamily; SMART predicts Ras-like small ...

70-229

1.50e-16

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: 76.44 E-value: 1.50e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207    70 PELKVGIVGNLASGKSALVHRYLTGTYVQEESP--EGGrFKKEIVVDGQSYLLLIRDEGGppEAQF-AMW------VDAV 140
Cdd:smart00010   1 REYKLVVLGGGGVGKSALTIQFVQGHFVDEYDPtiEDS-YRKQIEIDGEVCLLDILDTAG--QEEFsAMRdqymrtGEGF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207   141 IFVFSLEDEISFQTVYHYYSRMANYRNTSEIPLVLVGTQ-DAIssaNPRVIDDARARKLSNDLKrCTYYETCATYGLNVE 219
Cdd:smart00010  78 LLVYSITDRQSFEEIAKFREQILRVKDRDDVPIVLVGNKcDLE---NERVVSTEEGKELARQWG-CPFLETSAKERINVD 153

                          170
                   ....*....|
gi 349585207   220 RVFQDVAQKI 229
Cdd:smart00010 154 EAFYDLVREI 163

Ras

pfam00071

Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...

73-229

1.91e-16

Pssm-ID: 425451 [Multi-domain] Cd Length: 162 Bit Score: 76.01 E-value: 1.91e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207   73 KVGIVGNLASGKSALVHRYLTGTYVQE-ESPEGGRFK-KEIVVDGQSYLLLIRDEGGPPE-----AQFAMWVDAVIFVFS 145
Cdd:pfam00071   1 KLVLVGDGGVGKSSLLIRFTQNKFPEEyIPTIGVDFYtKTIEVDGKTVKLQIWDTAGQERfralrPLYYRGADGFLLVYD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  146 LEDEISFQTVYHYYSRMANYRNTSeIPLVLVGTQ-DAISSanpRVIDDARARKLSNDLKrCTYYETCATYGLNVERVFQD 224
Cdd:pfam00071  81 ITSRDSFENVKKWVEEILRHADEN-VPIVLVGNKcDLEDQ---RVVSTEEGEALAKELG-LPFMETSAKTNENVEEAFEE 155


                  ....*
gi 349585207  225 VAQKI 229
Cdd:pfam00071 156 LAREI 160

RERG_RasL11_like

cd04146

Ras-related and Estrogen-Regulated Growth inhibitor (RERG) and Ras-like 11 (RasL11)-like ...

73-229

1.30e-15

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: 73.85 E-value: 1.30e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  73 KVGIVGNLASGKSALVHRYLTGTYVQE-ESPEGGRFKKEIVVDGQSYLLLIRDEGGP--PEAQFAM-----WVDAVIFVF 144
Cdd:cd04146    1 KIAVLGASGVGKSALTVRFLTKRFIGEyEPNLESLYSRQVTIDGEQVSLEIQDTPGQqqNEDPESLerslrWADGFVLVY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 145 SLEDEISFQTVYHYYSRMANY-RNTSEIPLVLVGT-QDAissANPRVIDDARARKLSNDLkRCTYYE--TCATYgLNVER 220
Cdd:cd04146   81 SITDRSSFDVVSQLLQLIREIkKRDGEIPVILVGNkADL---LHSRQVSTEEGQKLALEL-GCLFFEvsAAENY-LEVQN 155


                 ....*....
gi 349585207 221 VFQDVAQKI 229
Cdd:cd04146  156 VFHELCREV 164

RAB

smart00175

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

72-232

4.77e-15

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

Pssm-ID: 197555 [Multi-domain] Cd Length: 164 Bit Score: 72.16 E-value: 4.77e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207    72 LKVGIVGNLASGKSALVHRYLTGTYVQEESPEGG-RFK-KEIVVDGQSYLLLIRDEGGppeaQ---------FAMWVDAV 140
Cdd:smart00175   1 FKIILIGDSGVGKSSLLSRFTDGKFSEQYKSTIGvDFKtKTIEVDGKRVKLQIWDTAG----QerfrsitssYYRGAVGA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207   141 IFVFSLEDEISFQTVYHYYSRMANYRNtSEIPLVLVGTQdaISSANPRVIDDARARKLSNDLKrCTYYETCATYGLNVER 220
Cdd:smart00175  77 LLVYDITNRESFENLENWLKELREYAS-PNVVIMLVGNK--SDLEEQRQVSREEAEAFAEEHG-LPFFETSAKTNTNVEE 152

                          170
                   ....*....|..
gi 349585207   221 VFQDVAQKIVAT 232
Cdd:smart00175 153 AFEELAREILKR 164

Ras_like_GTPase

cd00882

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...

75-227

9.96e-15

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: 71.33 E-value: 9.96e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  75 GIVGNLASGKSALVHRYLTGTYVQEESPEG---GRFKKEIVVDGQSYLLLIRDEGGPPEA----------QFAMWVDAVI 141
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGttrDPDVYVKELDKGKVKLVLVDTPGLDEFgglgreelarLLLRGADLIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 142 FVFSLEDEISFQTVYHYYSRMANYRNtseIPLVLVGTQdaISSANPRVIDDARARKLSNDLKRCTYYETCATYGLNVERV 221
Cdd:cd00882   81 LVVDSTDRESEEDAKLLILRRLRKEG---IPIILVGNK--IDLLEEREVEELLRLEELAKILGVPVFEVSAKTGEGVDEL 155


                 ....*.
gi 349585207 222 FQDVAQ 227
Cdd:cd00882  156 FEKLIE 161

Rap1

cd04175

Rap1 family GTPase consists of Rap1a and Rap1b isoforms; The Rap1 subgroup is part of the Rap ...

71-229

1.02e-14

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: 71.39 E-value: 1.02e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  71 ELKVGIVGNLASGKSALVHRYLTGTYVQEESPE-GGRFKKEIVVDGQSYLLLIRDEGGppEAQFAMWVD-------AVIF 142
Cdd:cd04175    1 EYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTiEDSYRKQVEVDGQQCMLEILDTAG--TEQFTAMRDlymkngqGFVL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 143 VFSLEDEISFQTVYHYYSRMANYRNTSEIPLVLVGTQDAISSAnpRVIDDARARKLSNDLKrCTYYETCATYGLNVERVF 222
Cdd:cd04175   79 VYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDE--RVVGKEQGQNLARQWG-CAFLETSAKAKINVNEIF 155


                 ....*..
gi 349585207 223 QDVAQKI 229
Cdd:cd04175  156 YDLVRQI 162

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, ...

71-229

2.17e-13

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: 67.44 E-value: 2.17e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  71 ELKVGIVGNLASGKSALVHRYLTGTYVQEESPE-GGRFKKEIVVDGQSYLLLIRDEGGPPE-----AQFAMWVDAVIFVF 144
Cdd:cd04138    1 EYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTiEDSYRKQVVIDGETCLLDILDTAGQEEysamrDQYMRTGEGFLCVF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 145 SLEDEISFQTVYHYYSRMANYRNTSEIPLVLVGTQDAISSanpRVIDDARARKLSNDLKrCTYYETCATYGLNVERVFQD 224
Cdd:cd04138   81 AINSRKSFEDIHTYREQIKRVKDSDDVPMVLVGNKCDLAA---RTVSTRQGQDLAKSYG-IPYIETSAKTRQGVEEAFYT 156


                 ....*
gi 349585207 225 VAQKI 229
Cdd:cd04138  157 LVREI 161

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, ...

70-229

4.49e-13

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: 66.66 E-value: 4.49e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  70 PELKVGIVGNLASGKSALVHRYLTGTYVQEESPE-GGRFKKEIVVDGQSYLLLIRDEGGPPE-----AQFAMWVDAVIFV 143
Cdd:cd04145    1 PTYKLVVVGGGGVGKSALTIQFIQSYFVTDYDPTiEDSYTKQCEIDGQWARLDILDTAGQEEfsamrEQYMRTGEGFLLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 144 FSLEDEISFQTVYHYYSRMANYRNTSEIPLVLVGTQdaISSANPRVIDDARARKLSNDLKrCTYYETCATYGLNVERVFQ 223
Cdd:cd04145   81 FSVTDRGSFEEVDKFHTQILRVKDRDEFPMILVGNK--ADLEHQRQVSREEGQELARQLK-IPYIETSAKDRVNVDKAFH 157


                 ....*.
gi 349585207 224 DVAQKI 229
Cdd:cd04145  158 DLVRVI 163

Gem1

COG1100

GTPase SAR1 family domain [General function prediction only];

71-229

7.48e-13

GTPase SAR1 family domain [General function prediction only];

Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 66.54 E-value: 7.48e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  71 ELKVGIVGNLASGKSALVHRYLTGTYVQEE--SPEG-GRFKKEIVVDGQSYLLLIRDEGGPPE-----AQFAMWV---DA 139
Cdd:COG1100    3 EKKIVVVGTGGVGKTSLVNRLVGDIFSLEKylSTNGvTIDKKELKLDGLDVDLVIWDTPGQDEfretrQFYARQLtgaSL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 140 VIFVFSLEDEISFQTVYHYYSRMANYRNTSeiPLVLVGTQ-DAISsaNPRVIDDARARKLSNDLKRCTYYETCATYGLNV 218
Cdd:COG1100   83 YLFVVDGTREETLQSLYELLESLRRLGKKS--PIILVLNKiDLYD--EEEIEDEERLKEALSEDNIVEVVATSAKTGEGV 158

                        170
                 ....*....|.
gi 349585207 219 ERVFQDVAQKI 229
Cdd:COG1100  159 EELFAALAEIL 169

Rap2

cd04176

Rap2 family GTPase consists of Rap2a, Rap2b, and Rap2c; The Rap2 subgroup is part of the Rap ...

71-229

2.03e-12

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: 64.86 E-value: 2.03e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  71 ELKVGIVGNLASGKSALVHRYLTGTYVQEESPEGGRF-KKEIVVDGQSYLLLIRDEGGppEAQFAMWVD-------AVIF 142
Cdd:cd04176    1 EYKVVVLGSGGVGKSALTVQFVSGTFIEKYDPTIEDFyRKEIEVDSSPSVLEILDTAG--TEQFASMRDlyikngqGFIV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 143 VFSLEDEISFQTVYHYYSRMANYRNTSEIPLVLVGTQDAISSAnpRVIDDARARKLSNDLKrCTYYETCATYGLNVERVF 222
Cdd:cd04176   79 VYSLVNQQTFQDIKPMRDQIVRVKGYEKVPIILVGNKVDLESE--REVSSAEGRALAEEWG-CPFMETSAKSKTMVNELF 155


                 ....*..
gi 349585207 223 QDVAQKI 229
Cdd:cd04176  156 AEIVRQM 162

RalA_RalB

cd04139

Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily ...

73-229

3.24e-12

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: 64.37 E-value: 3.24e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  73 KVGIVGNLASGKSALVHRYLTGTYVQEESP-EGGRFKKEIVVDGQSYLLLIRDEGGppEAQFA------MWV-DAVIFVF 144
Cdd:cd04139    2 KVIMVGSGGVGKSALTLQFMYDEFVEDYEPtKADSYRKKVVLDGEEVQLNILDTAG--QEDYAairdnyFRSgEGFLLVF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 145 SLEDEISFQTVYHYYSRMANYRNTSEIPLVLVGTQDAISSANPRVIDDARARKLSNDLKrctYYETCATYGLNVERVFQD 224
Cdd:cd04139   80 SITDMESFTALAEFREQILRVKEDDNVPLLLVGNKCDLEDKRQVSVEEAANLAEQWGVN---YVETSAKTRANVDKVFFD 156


                 ....*
gi 349585207 225 VAQKI 229
Cdd:cd04139  157 LVREI 161

Rab7

cd01862

Rab GTPase family 7 (Rab7); Rab7 subfamily. Rab7 is a small Rab GTPase that regulates ...

72-234

1.01e-11

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

Pssm-ID: 206655 [Multi-domain] Cd Length: 172 Bit Score: 63.07 E-value: 1.01e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  72 LKVGIVGNLASGKSALVHRYLTGTYVQE-ESPEGGRF-KKEIVVDGQSYLLLIRDEGGPPEAQ-----FAMWVDAVIFVF 144
Cdd:cd01862    1 LKVIILGDSGVGKTSLMNQYVNKKFSNQyKATIGADFlTKEVTVDDRLVTLQIWDTAGQERFQslgvaFYRGADCCVLVY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 145 SLEDEISFQTVYHYYSRM---ANYRNTSEIPLVLVGTQdaISSANPRVIDDARARKLSNDLKRCTYYETCATYGLNVERV 221
Cdd:cd01862   81 DVTNPKSFESLDSWRDEFliqASPRDPENFPFVVLGNK--IDLEEKRQVSTKKAQQWCKSKGNIPYFETSAKEAINVDQA 158

                        170
                 ....*....|...
gi 349585207 222 FQDVAQKIVATRK 234
Cdd:cd01862  159 FETIARLALEQEK 171

Rab9

cd04116

Rab GTPase family 9 (Rab9); Rab9 is found in late endosomes, together with mannose 6-phosphate ...

72-229

8.72e-11

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: 60.27 E-value: 8.72e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  72 LKVGIVGNLASGKSALVHRYLTGTY-VQEESPEGGRF-KKEIVVDGQSYLLLIRDEGGPPEAQ-----FAMWVDAVIFVF 144
Cdd:cd04116    6 LKVILLGDGGVGKSSLMNRYVTNKFdTQLFHTIGVEFlNKDLEVDGHFVTLQIWDTAGQERFRslrtpFYRGSDCCLLTF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 145 SLEDEISFQTVYHYYSRMANY---RNTSEIPLVLVGTQDAISSanpRVIDDARARKLSNDLKRCTYYETCATYGLNVERV 221
Cdd:cd04116   86 SVDDSQSFQNLSNWKKEFIYYadvKEPESFPFVILGNKIDIPE---RQVSTEEAQAWCRDNGDYPYFETSAKDATNVAAA 162


                 ....*...
gi 349585207 222 FQDVAQKI 229
Cdd:cd04116  163 FEEAVRRV 170

Rab23_like

cd04106

Rab GTPase family 23 (Rab23)-like; Rab23-like subfamily. Rab23 is a member of the Rab family ...

72-228

1.68e-10

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

Pssm-ID: 133306 [Multi-domain] Cd Length: 162 Bit Score: 59.38 E-value: 1.68e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  72 LKVGIVGNLASGKSALVHRYLTGTYVQEespeggrFKKEIVVD-----------GQSYLLLIRDEGGPPE-----AQFAM 135
Cdd:cd04106    1 IKVIVVGNGNVGKSSMIQRFVKGIFTKD-------YKKTIGVDflekqiflrqsDEDVRLMLWDTAGQEEfdaitKAYYR 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 136 WVDAVIFVFSLEDEISFQTVYHYYSRMANyrNTSEIPLVLVgtQDAISSANPRVIDDARARKLSNDLKrCTYYETCATYG 215
Cdd:cd04106   74 GAQACILVFSTTDRESFEAIESWKEKVEA--ECGDIPMVLV--QTKIDLLDQAVITNEEAEALAKRLQ-LPLFRTSVKDD 148

                        170
                 ....*....|...
gi 349585207 216 LNVERVFQDVAQK 228
Cdd:cd04106  149 FNVTELFEYLAEK 161

RJL

cd04119

Rab GTPase family J-like (RabJ-like); RJLs are found in many protists and as chimeras with ...

72-231

4.17e-10

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: 58.14 E-value: 4.17e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  72 LKVGIVGNLASGKSALVHRYLTGTYVQEESPEGG---------RFKKEIVVD-----GQSYLLLIRDEggppeaqFAMWV 137
Cdd:cd04119    1 IKVISMGNSGVGKSCIIKRYCEGRFVSKYLPTIGidygvkkvsVRNKEVRVNffdlsGHPEYLEVRNE-------FYKDT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 138 DAVIFVFSLEDEISFQTVYHYYSRMANY----RNTSEIPLVLVGTQdaISSANPRVIDDARARKLSNDLKrCTYYETCAT 213
Cdd:cd04119   74 QGVLLVYDVTDRQSFEALDSWLKEMKQEggphGNMENIVVVVCANK--IDLTKHRAVSEDEGRLWAESKG-FKYFETSAC 150

                        170
                 ....*....|....*...
gi 349585207 214 YGLNVERVFQDVAQKIVA 231
Cdd:cd04119  151 TGEGVNEMFQTLFSSIVD 168

Rit_Rin_Ric

cd04141

Ras-like protein in all tissues (Rit), Ras-like protein in neurons (Rin) and Ras-related ...

71-236

2.14e-09

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: 56.40 E-value: 2.14e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  71 ELKVGIVGNLASGKSALVHRYLTGTYVQEESPE-GGRFKKEIVVDGQSYLLLIRDEGGPPE-----AQFAMWVDAVIFVF 144
Cdd:cd04141    2 EYKIVMLGAGGVGKSAVTMQFISHSFPDYHDPTiEDAYKTQARIDNEPALLDILDTAGQAEftamrDQYMRCGEGFIICY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 145 SLEDEISFQTVYHYYSRMANYRNTSEIPLVLVGTQDAISSAnpRVIDDARARKLSNDLKrCTYYETCATYGLNVERVFQD 224
Cdd:cd04141   82 SVTDRHSFQEASEFKELITRVRLTEDIPLVLVGNKVDLEQQ--RQVTTEEGRNLAREFN-CPFFETSAALRFYIDDAFHG 158

                        170
                 ....*....|..
gi 349585207 225 VAQKIvatRKKQ 236
Cdd:cd04141  159 LVREI---RRKE 167

RabL2

cd04124

Rab GTPase-like family 2 (Rab-like2); RabL2 (Rab-like2) subfamily. RabL2s are novel Rab ...

72-224

4.46e-09

Rab GTPase-like family 2 (Rab-like2); RabL2 (Rab-like2) subfamily. RabL2s are novel Rab proteins identified recently which display features that are distinct from other Rabs, and have been termed Rab-like. RabL2 contains RabL2a and RabL2b, two very similar Rab proteins that share > 98% sequence identity in humans. RabL2b maps to the subtelomeric region of chromosome 22q13.3 and RabL2a maps to 2q13, a region that suggests it is also a subtelomeric gene. Both genes are believed to be expressed ubiquitously, suggesting that RabL2s are the first example of duplicated genes in human proximal subtelomeric regions that are both expressed actively. Like other Rab-like proteins, RabL2s lack a prenylation site at the C-terminus. The specific functions of RabL2a and RabL2b remain unknown. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization.

Pssm-ID: 133324 [Multi-domain] Cd Length: 161 Bit Score: 55.25 E-value: 4.46e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  72 LKVGIVGNLASGKSALVHRYLTGTY--VQEESPEGGRFKKEIVVDGQSYLLLIRDEGGPP-----EAQFAMWVDAVIFVF 144
Cdd:cd04124    1 VKIILLGDSAVGKSKLVERFLMDGYepQQLSTYALTLYKHNAKFEGKTILVDFWDTAGQErfqtmHASYYHKAHACILVF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 145 SLEDEISFQTVYHYYSRMANYRntSEIPLVLVGTQdaiSSANPRVIDDARARKLSNDLkrcTYYETCATYGLNVERVFQD 224
Cdd:cd04124   81 DVTRKITYKNLSKWYEELREYR--PEIPCIVVANK---IDLDPSVTQKKFNFAEKHNL---PLYYVSAADGTNVVKLFQD 152

PTZ00369

Ras-like protein; Provisional

71-229

1.26e-08

Ras-like protein; Provisional

Pssm-ID: 240385 [Multi-domain] Cd Length: 189 Bit Score: 54.48 E-value: 1.26e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  71 ELKVGIVGNLASGKSALVHRYLTGTYVQEESPE-GGRFKKEIVVDGQSYLLLIRDEGGPPE-----AQFAMWVDAVIFVF 144
Cdd:PTZ00369   5 EYKLVVVGGGGVGKSALTIQFIQNHFIDEYDPTiEDSYRKQCVIDEETCLLDILDTAGQEEysamrDQYMRTGQGFLCVY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 145 SLEDEISFQTVYHYYSRMANYRNTSEIPLVLVGTQDAISSAnpRVIDDARARKLSNDLKrCTYYETCATYGLNVERVFQD 224
Cdd:PTZ00369  85 SITSRSSFEEIASFREQILRVKDKDRVPMILVGNKCDLDSE--RQVSTGEGQELAKSFG-IPFLETSAKQRVNVDEAFYE 161


                 ....*
gi 349585207 225 VAQKI 229
Cdd:PTZ00369 162 LVREI 166

RGK

cd04148

Rem, Rem2, Rad, Gem/Kir (RGK) subfamily of Ras GTPases; RGK subfamily. The RGK (Rem, Rem2, Rad, ...

72-229

1.51e-08

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: 54.72 E-value: 1.51e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  72 LKVGIVGNLASGKSALVHRYLTGTY----VQEESPEGGrfKKEIVVDGQSYLLLIRDeggPPEAQFAMWV--------DA 139
Cdd:cd04148    1 YRVVLLGDSGVGKSSLANIFTAGVYedsaYEASGDDTY--ERTVSVDGEEATLVVYD---HWEQEDGMWLedscmqvgDA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 140 VIFVFSLEDEISFQTVYHYYSRMANYRNTSEIPLVLVGTQDaissanprviDDARARKLSNDLKR-------CTYYETCA 212
Cdd:cd04148   76 YVIVYSVTDRSSFEKASELRIQLRRARQAEDIPIILVGNKS----------DLVRSREVSVQEGRacavvfdCKFIETSA 145

                        170
                 ....*....|....*..
gi 349585207 213 TYGLNVERVFQDVAQKI 229
Cdd:cd04148  146 ALQHNVDELFEGIVRQV 162

Wrch_1

cd04130

Wnt-1 responsive Cdc42 homolog (Wrch-1) is a Rho family GTPase similar to Cdc42; Wrch-1 (Wnt-1 ...

72-222

2.35e-08

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: 53.18 E-value: 2.35e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  72 LKVGIVGNLASGKSALVHRYLTGTYVQEESPEG-GRFKKEIVVDGQSYLLLIRDEGGPPEaqFAMW-------VDAVIFV 143
Cdd:cd04130    1 LKCVLVGDGAVGKTSLIVSYTTNGYPTEYVPTAfDNFSVVVLVDGKPVRLQLCDTAGQDE--FDKLrplcypdTDVFLLC 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 144 FSLEDEISFQTV-YHYYSRMANYRNTSeiPLVLVGTQ------------DAISSANPrvIDDARARKLSNDLKRCTYYET 210
Cdd:cd04130   79 FSVVNPSSFQNIsEKWIPEIRKHNPKA--PIILVGTQadlrtdvnvliqLARYGEKP--VSQSRAKALAEKIGACEYIEC 154

                        170
                 ....*....|..
gi 349585207 211 CATYGLNVERVF 222
Cdd:cd04130  155 SALTQKNLKEVF 166

Rho

cd00157

Ras homology family (Rho) of small guanosine triphosphatases (GTPases); Members of the Rho ...

72-227

6.71e-08

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: 51.78 E-value: 6.71e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  72 LKVGIVGNLASGKSALVHRYLTGTYVQEESP---EGgrFKKEIVVDGQSYLLLIRDEGGPPEaqFAMW-------VDAVI 141
Cdd:cd00157    1 IKIVVVGDGAVGKTCLLISYTTNKFPTEYVPtvfDN--YSANVTVDGKQVNLGLWDTAGQEE--YDRLrplsypqTDVFL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 142 FVFSLEDEISFQTVYH-YYSRManYRNTSEIPLVLVGTQ-DAISSANPRVIDDAR--------ARKLSNDLKRCTYYETC 211
Cdd:cd00157   77 LCFSVDSPSSFENVKTkWYPEI--KHYCPNVPIILVGTKiDLRDDGNTLKKLEKKqkpitpeeGEKLAKEIGAVKYMECS 154

                        170
                 ....*....|....*.
gi 349585207 212 ATYGLNVERVFQDVAQ 227
Cdd:cd00157  155 ALTQEGLKEVFDEAIR 170

Spg1

cd04128

Septum-promoting GTPase (Spg1); Spg1p. Spg1p (septum-promoting GTPase) was first identified in ...

72-229

8.19e-08

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: 52.01 E-value: 8.19e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  72 LKVGIVGNLASGKSALVHRYLTGTYVQEESPEGGR--FKKEIVVDGQSYLLLIRDEGGPPE--AQFAMWVD---AVIFVF 144
Cdd:cd04128    1 LKIGLLGDAQIGKTSLMVKYVEGEFDEEYIQTLGVnfMEKTISIRGTEITFSIWDLGGQREfiNMLPLVCKdavAILFMF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 145 SLEDEISFQTVYHYYsRMANYRNTSEIPlVLVGT------------QDAISSanprviddaRARKLSNDLKrCTYYETCA 212
Cdd:cd04128   81 DLTRKSTLNSIKEWY-RQARGFNKTAIP-ILVGTkydlfadlppeeQEEITK---------QARKYAKAMK-APLIFCST 148

                        170
                 ....*....|....*..
gi 349585207 213 TYGLNVERVFQDVAQKI 229
Cdd:cd04128  149 SHSINVQKIFKFVLAKV 165

Ran

cd00877

Ras-related nuclear proteins (Ran)/TC4 family of small GTPases; Ran GTPase is involved in ...

73-230

2.55e-07

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: 49.99 E-value: 2.55e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  73 KVGIVGNLASGKSALVHRYLTGtyvqeespeggRFKKEIV--VDGQSYLLLIRDEGGPpeAQFAMW-------------- 136
Cdd:cd00877    2 KLVLVGDGGTGKTTFVKRHLTG-----------EFEKKYVatLGVEVHPLDFHTNRGK--IRFNVWdtagqekfgglrdg 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 137 ----VDAVIFVFSLEDEISFQTVYHYYSRManYRNTSEIPLVLVGTQDAISSA--NPRVIDDARARKLSndlkrctYYET 210
Cdd:cd00877   69 yyiqGQCAIIMFDVTSRVTYKNVPNWHRDL--VRVCENIPIVLCGNKVDIKDRkvKPKQITFHRKKNLQ-------YYEI 139

                        170       180
                 ....*....|....*....|
gi 349585207 211 CATYGLNVERVFQDVAQKIV 230
Cdd:cd00877  140 SAKSNYNFEKPFLWLARKLL 159

Ras_dva

cd04147

Ras - dorsal-ventral anterior localization (Ras-dva) family; Ras-dva subfamily. Ras-dva (Ras - ...

83-228

3.64e-07

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: 50.22 E-value: 3.64e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  83 GKSALVHRYLTGTYvqeeSPEGGR-----FKKEIVVDGQSYLLLIRDEGGPPE--AQFAMWV---DAVIFVFSLEDEISF 152
Cdd:cd04147   11 GKTALIQRFLYDTF----EPKHRRtveelHSKEYEVAGVKVTIDILDTSGSYSfpAMRKLSIqngDAFALVYSVDDPESF 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 349585207 153 QTVYHYYSRMANYRNTSEIPLVLVGTQdaISSANPRVIDDARARKLSNDLKRCTYYETCATYGLNVERVFQDVAQK 228
Cdd:cd04147   87 EEVKRLREEILEVKEDKFVPIVVVGNK--IDSLAERQVEAADALSTVELDWNNGFVEASAKDNENVTEVFKELLQQ 160

Rhes_like

cd04143

Ras homolog enriched in striatum (Rhes) and activator of G-protein signaling 1 (Dexras1/AGS1); ...

73-223

1.03e-06

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: 49.75 E-value: 1.03e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  73 KVGIVGNLASGKSALVHRYLTGTYVQEESPEGGRF-KKEIVVDGQSYLLLIRDEGG----PPEAQFAMWV-DAVIFVFSL 146
Cdd:cd04143    2 RMVVLGASKVGKTAIVSRFLGGRFEEQYTPTIEDFhRKLYSIRGEVYQLDILDTSGnhpfPAMRRLSILTgDVFILVFSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 147 EDEISF-------QTVYHYYSRMAN-YRNTSEIPLVLVGTQDAISSanPRVIDDARARKLSNDLKRCTYYETCATYGLNV 218
Cdd:cd04143   82 DNRESFeevcrlrEQILETKSCLKNkTKENVKIPMVICGNKADRDF--PREVQRDEVEQLVGGDENCAYFEVSAKKNSNL 159


                 ....*
gi 349585207 219 ERVFQ 223
Cdd:cd04143  160 DEMFR 164

Rab39

cd04111

Rab GTPase family 39 (Rab39); Found in eukaryotes, Rab39 is mainly found in epithelial cell ...

76-241

1.86e-06

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: 48.22 E-value: 1.86e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  76 IVGNLASGKSALVHRYLTGTYVQEESPEGGrfkkeivVDGQSYLLLIRDEggpPEAQFAMWVDA---------------- 139
Cdd:cd04111    7 VIGDSTVGKSSLLKRFTEGRFAEVSDPTVG-------VDFFSRLIEIEPG---VRIKLQLWDTAgqerfrsitrsyyrns 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 140 --VIFVFSLEDEISFQTVYHYYSRMANYRNTSEIPLVLVGTQDAISSAnpRVIDDARARKLSNDLKrCTYYETCATYGLN 217
Cdd:cd04111   77 vgVLLVFDITNRESFEHVHDWLEEARSHIQPHRPVFILVGHKCDLESQ--RQVTREEAEKLAKDLG-MKYIETSARTGDN 153

                        170       180
                 ....*....|....*....|....
gi 349585207 218 VERVFQDVAQKIVATRKKQQLSIG 241
Cdd:cd04111  154 VEEAFELLTQEIYERIKRGELCAL 177

Rab6

cd01861

Rab GTPase family 6 (Rab6); Rab6 is involved in microtubule-dependent transport pathways ...

73-229

4.27e-06

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: 46.46 E-value: 4.27e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  73 KVGIVGNLASGKSALVHRYLTGTYVQEESPEGGR--FKKEIVVDGQSYLLLIRDEGGppEAQFAMWV-------DAVIFV 143
Cdd:cd01861    2 KLVFLGDQSVGKTSIITRFMYDTFDNQYQATIGIdfLSKTMYVDDKTVRLQLWDTAG--QERFRSLIpsyirdsSVAVVV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 144 FSLEDEISFQTVYHYYSRMANYRNtSEIPLVLVGTQdaISSANPRVIDDARARKLSNDLKrCTYYETCATYGLNVERVFQ 223
Cdd:cd01861   80 YDITNRQSFDNTDKWIDDVRDERG-NDVIIVLVGNK--TDLSDKRQVSTEEGEKKAKENN-AMFIETSAKAGHNVKQLFK 155


                 ....*.
gi 349585207 224 DVAQKI 229
Cdd:cd01861  156 KIAQAL 161

Roc

pfam08477

Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...

73-178

4.72e-06

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: 45.19 E-value: 4.72e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207   73 KVGIVGNLASGKSALVHRYLTGTYVQEESPEGGrfkkeivVDGQSYLLLIRDEGGpPEAQFAMW---------------- 136
Cdd:pfam08477   1 KVVLLGDSGVGKTSLLKRFVDDTFDPKYKSTIG-------VDFKTKTVLENDDNG-KKIKLNIWdtagqerfrslhpfyy 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 349585207  137 --VDAVIFVFsleDEISFQTVYHYYSRMANYRNtsEIPLVLVGT 178
Cdd:pfam08477  73 rgAAAALLVY---DSRTFSNLKYWLRELKKYAG--NSPVILVGN 111

Rab24

cd04118

Rab GTPase family 24 (Rab24); Rab24 is distinct from other Rabs in several ways. It exists ...

72-230

4.84e-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: 46.78 E-value: 4.84e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  72 LKVGIVGNLASGKSALVHRYLTGTYVQE--ESPEGGRF-KKEIVVDGQSYLLLIRDEGGPPEAQfAMWV------DAVIF 142
Cdd:cd04118    1 VKVVMLGKESVGKTSLVERYVHHRFLVGpyQNTIGAAFvAKRMVVGERVVTLGIWDTAGSERYE-AMSRiyyrgaKAAIV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 143 VFSLEDEISFQTVYHYYSRMANyrNTSEIPLVLVGTQ-DAISS-ANPRVIDDARARKLSNDLKrCTYYETCATYGLNVER 220
Cdd:cd04118   80 CYDLTDSSSFERAKFWVKELQN--LEEHCKIYLCGTKsDLIEQdRSLRQVDFHDVQDFADEIK-AQHFETSSKTGQNVDE 156

                        170
                 ....*....|
gi 349585207 221 VFQDVAQKIV 230
Cdd:cd04118  157 LFQKVAEDFV 166

RabL4

cd04101

Rab GTPase-like family 4 (Rab-like4); RabL4 (Rab-like4) subfamily. RabL4s are novel proteins ...

72-230

5.65e-06

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: 46.37 E-value: 5.65e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  72 LKVGIVGNLASGKSALVHRYLT-GTYVQEES--PEGGRF-KKEIVV--DGQSYLLLIRDEGGPPEaqFAMWVD------- 138
Cdd:cd04101    1 AQCAVVGDPAVGKSALVQMFHSdGATFQKNYtmTTGCDLvVKTVPVpdTSDSVELFIFDSAGQEL--FSDMVEnvweqpa 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 139 AVIFVFSLEDEISFQTVYHYYSRMANYRNTSEIPLVLVGTQDAISSAnpRVIDDARARKLS--NDLKrctYYETCATYGL 216
Cdd:cd04101   79 VVCVVYDVTNEVSFNNCSRWINRVRTHSHGLHTPGVLVGNKCDLTDR--REVDAAQAQALAqaNTLK---FYETSAKEGV 153

                        170
                 ....*....|....
gi 349585207 217 NVERVFQDVAQKIV 230
Cdd:cd04101  154 GYEAPFLSLARAFH 167

Rab8_Rab10_Rab13_like

cd01867

Rab GTPase families 8, 10, 13 (Rab8, Rab10, Rab13); Rab8/Sec4/Ypt2 are known or suspected to ...

73-229

2.28e-05

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: 44.57 E-value: 2.28e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  73 KVGIVGNLASGKSALVHRY----LTGTYVqeeSPEGGRFK-KEIVVDGQSYLLLIRDEGGppEAQF----------AMwv 137
Cdd:cd01867    5 KLLLIGDSGVGKSCLLLRFsedsFNPSFI---STIGIDFKiRTIELDGKKIKLQIWDTAG--QERFrtittsyyrgAM-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 138 dAVIFVFSLEDEISFQTVYHYYSRMANYRNtSEIPLVLVGTQDAIssANPRVIDDARARKLSNDLkRCTYYETCATYGLN 217
Cdd:cd01867   78 -GIILVYDITDEKSFENIKNWMRNIDEHAS-EDVERMLVGNKCDM--EEKRVVSKEEGEALAREY-GIKFLETSAKANIN 152

                        170
                 ....*....|..
gi 349585207 218 VERVFQDVAQKI 229
Cdd:cd01867  153 VEEAFLTLAKDI 164

small_GTP

TIGR00231

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...

71-179

3.94e-05

Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 43.51 E-value: 3.94e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207   71 ELKVGIVGNLASGKSALVHRYLTGTYVQEESPEGGRF---KKEIVVDGQSYLLLIRDEGGpPEAQFAMW------VDAVI 141
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRnyvTTVIEEDGKTYKFNLLDTAG-QEDYDAIRrlyypqVERSL 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 349585207  142 FVFSLED-EISFQTVYHYYSRMANYRNTSEIPLVLVGTQ 179
Cdd:TIGR00231  80 RVFDIVIlVLDVEEILEKQTKEIIHHADSGVPIILVGNK 118

Rab28

cd04109

Rab GTPase family 28 (Rab28); Rab28 subfamily. First identified in maize, Rab28 has been shown ...

72-270

4.13e-05

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

Pssm-ID: 206694 [Multi-domain] Cd Length: 213 Bit Score: 44.40 E-value: 4.13e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  72 LKVGIVGNLASGKSALVHRYLTGTYVQEESPEGGR--FKKEIVVDG-QSYLLLIRDEGGPP-----EAQFAMWVDAVIFV 143
Cdd:cd04109    1 IKIVVLGDGASGKTSLIRRFAQEGFGKSYKQTIGLdfFSRRITLPGsLNVTLQVWDIGGQQiggkmLDKYIYGAQAVCLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 144 FSLEDEISFQTVYHYYSRMANYRNTSEIP--LVLVGTQDAISSaNPRVIDDARAR-KLSNDLKRCTyyeTCATYGLNVER 220
Cdd:cd04109   81 YDITNSQSFENLEDWLSVVKKVNEESETKpkMVLVGNKTDLEH-NRQVTAEKHARfAQENDMESIF---VSAKTGDRVFL 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 349585207 221 VFQDVAQKIVATRKKQQ---LSIGPCKSLPNSPSHSSVCSAQVSAVHISQTSN 270
Cdd:cd04109  157 CFQRIAAELLGVKLSQAeleQSQRVVKADVSRYSERTLREPVSRSVNKRSNSM 209

Rab27A

cd04127

Rab GTPase family 27a (Rab27a); The Rab27a subfamily consists of Rab27a and its highly ...

72-220

1.39e-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: 42.49 E-value: 1.39e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  72 LKVGIVGNLASGKSALVHRYLTGTY-VQEESPEGGRFKKEIVV-----------DGQSYLLLIRDEGGppEAQF-----A 134
Cdd:cd04127    5 IKLLALGDSGVGKTTFLYRYTDNKFnPKFITTVGIDFREKRVVynsqgpdgtsgKAFRVHLQLWDTAG--QERFrslttA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 135 MWVDAVIF--VFSLEDEISFQTVYHYYSRMANYRNTSEIPLVLVGTQDAISsaNPRVIDDARARKLSNDLkRCTYYETCA 212
Cdd:cd04127   83 FFRDAMGFllMFDLTSEQSFLNVRNWMSQLQAHAYCENPDIVLIGNKADLP--DQREVSERQARELADKY-GIPYFETSA 159


                 ....*...
gi 349585207 213 TYGLNVER 220
Cdd:cd04127  160 ATGQNVEK 167

PLN03118

Rab family protein; Provisional

72-230

1.66e-04

Rab family protein; Provisional

Pssm-ID: 215587 [Multi-domain] Cd Length: 211 Bit Score: 42.74 E-value: 1.66e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  72 LKVGIVGNLASGKSALVHRYLTGTyVQEESPE-GGRFK-KEIVVDGQSYLLLIRDEGGPPE-----AQFAMWVDAVIFVF 144
Cdd:PLN03118  15 FKILLIGDSGVGKSSLLVSFISSS-VEDLAPTiGVDFKiKQLTVGGKRLKLTIWDTAGQERfrtltSSYYRNAQGIILVY 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 145 SLEDEISFQTVYHYYSRMAN-YRNTSEIPLVLVGTQDAISSAnpRVIDDARARKLSNDLKrCTYYETCATYGLNVERVFQ 223
Cdd:PLN03118  94 DVTRRETFTNLSDVWGKEVElYSTNQDCVKMLVGNKVDRESE--RDVSREEGMALAKEHG-CLFLECSAKTRENVEQCFE 170


                 ....*..
gi 349585207 224 DVAQKIV 230
Cdd:PLN03118 171 ELALKIM 177

Rab35

cd04110

Rab GTPase family 35 (Rab35); Rab35 is one of several Rab proteins to be found to participate ...

73-236

1.97e-04

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

Pssm-ID: 133310 [Multi-domain] Cd Length: 199 Bit Score: 42.15 E-value: 1.97e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  73 KVGIVGNLASGKSALVHRY----LTGTYVqeeSPEGGRFK-KEIVVDGQSYLLLIRDEGGPPE-----AQFAMWVDAVIF 142
Cdd:cd04110    8 KLLIIGDSGVGKSSLLLRFadntFSGSYI---TTIGVDFKiRTVEINGERVKLQIWDTAGQERfrtitSTYYRGTHGVIV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 143 VFSLEDEISFQTVYHYYSRMANyrNTSEIPLVLVGTQDaiSSANPRVIDDARARKLSNDLKrCTYYETCATYGLNVERVF 222
Cdd:cd04110   85 VYDVTNGESFVNVKRWLQEIEQ--NCDDVCKVLVGNKN--DDPERKVVETEDAYKFAGQMG-ISLFETSAKENINVEEMF 159

                        170
                 ....*....|....
gi 349585207 223 QDVAQKIVATRKKQ 236
Cdd:cd04110  160 NCITELVLRAKKDN 173

ARHI_like

cd04140

A Ras homolog member I (ARHI); ARHI (A Ras homolog member I) is a member of the Ras family ...

73-223

3.65e-04

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: 40.97 E-value: 3.65e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  73 KVGIVGNLASGKSALVHRYLTGTYVQEESPE-GGRFKKEIVVDGQSYLLLIRDEGGppEAQF-AMWV------DAVIFVF 144
Cdd:cd04140    3 RVVVFGAGGVGKSSLVLRFVKGTFRESYIPTiEDTYRQVISCSKSICTLQITDTTG--SHQFpAMQRlsiskgHAFILVY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 145 SLEDEISFQTVYHYYSRMANYR--NTSEIPLVLVGTQdaISSANPRVIDDARARKLSNDLKrCTYYETCATYGLNVERVF 222
Cdd:cd04140   81 SITSKQSLEELKPIYELICEIKgnNLEKIPIMLVGNK--CDESPSREVSSSEGAALARTWN-CAFMETSAKTNHNVQELF 157


                 .
gi 349585207 223 Q 223
Cdd:cd04140  158 Q 158

Rab19

cd01864

Rab GTPase family 19 (Rab19); Rab19 subfamily. Rab19 proteins are associated with Golgi stacks. ...

73-229

5.60e-04

Rab GTPase family 19 (Rab19); Rab19 subfamily. Rab19 proteins are associated with Golgi stacks. Similarity analysis indicated that Rab41 is closely related to Rab19. However, the function of these Rabs is not yet characterized. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.

Pssm-ID: 133267 [Multi-domain] Cd Length: 165 Bit Score: 40.50 E-value: 5.60e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  73 KVGIVGNLASGKSALVHRYLTGTYVQ-EESPEGGRFK-KEIVVDGQSYLLLIRDEGGPPE-----AQFAMWVDAVIFVFS 145
Cdd:cd01864    5 KIILIGDSNVGKTCVVQRFKSGTFSErQGNTIGVDFTmKTLEIQGKRVKLQIWDTAGQERfrtitQSYYRSANGAIIAYD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 146 LEDEISFQTVYHYYSRMANYrNTSEIPLVLVGTQDAISSAnpRVIDDARARKLSNDLKRCTYYETCATYGLNVERVFQDV 225
Cdd:cd01864   85 ITRRSSFESVPHWIEEVEKY-GASNVVLLLIGNKCDLEEQ--REVLFEEACTLAEHYGILAVLETSAKESSNVEEAFLLM 161


                 ....
gi 349585207 226 AQKI 229
Cdd:cd01864  162 ATEL 165

Rho2

cd04129

Ras homology family 2 (Rho2) of small guanosine triphosphatases (GTPases); Rho2 is a fungal ...

73-233

6.99e-04

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: 40.59 E-value: 6.99e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  73 KVGIVGNLASGKSALVHRYLTGTYVQEESPE-GGRFKKEIVVDGQSYLLLIRDEGGPPEAQ----FAMWVDAVIFV-FSL 146
Cdd:cd04129    3 KLVIVGDGACGKTSLLYVFTLGEFPEEYHPTvFENYVTDCRVDGKPVQLALWDTAGQEEYErlrpLSYSKAHVILIgFAI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 147 EDEISFQTVYHYYSRMANyRNTSEIPLVLVGT-----QDAISSANP---RVIDDARARKLSNDLKRCTYYETCATYGLNV 218
Cdd:cd04129   83 DTPDSLENVRTKWIEEVR-RYCPNVPVILVGLkkdlrQEAVAKGNYatdEFVPIQQAKLVARAIGAKKYMECSALTGEGV 161

                        170
                 ....*....|....*
gi 349585207 219 ERVFQdvaqkiVATR 233
Cdd:cd04129  162 DDVFE------AATR 170

Rab26

cd04112

Rab GTPase family 26 (Rab26); Rab26 subfamily. First identified in rat pancreatic acinar cells, ...

73-229

9.20e-04

Rab GTPase family 26 (Rab26); Rab26 subfamily. First identified in rat pancreatic acinar cells, Rab26 is believed to play a role in recruiting mature granules to the plasma membrane upon beta-adrenergic stimulation. Rab26 belongs to the Rab functional group III, which are considered key regulators of intracellular vesicle transport during exocytosis. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins.

Pssm-ID: 206695 [Multi-domain] Cd Length: 191 Bit Score: 40.23 E-value: 9.20e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  73 KVGIVGNLASGKSALVHRYLTGTYVqeespeGGRF---------KKEIVVDGQSYLLLIRDEGGppEAQF-----AMWVD 138
Cdd:cd04112    2 KVMLVGDSGVGKTCLLVRFKDGAFL------AGSFiatvgiqftNKVVTVDGVKVKLQIWDTAG--QERFrsvthAYYRD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 139 --AVIFVFSLEDEISFQTVYHYYSRMANYrNTSEIPLVLVGtqDAISSANPRVIDDARARKLSNDLKrCTYYETCATYGL 216
Cdd:cd04112   74 ahALLLLYDVTNKSSFDNIRAWLTEILEY-AQSDVVIMLLG--NKADMSGERVVKREDGERLAKEYG-VPFMETSAKTGL 149

                        170
                 ....*....|...
gi 349585207 217 NVERVFQDVAQKI 229
Cdd:cd04112  150 NVELAFTAVAKEL 162

Rab3

cd01865

Rab GTPase family 3 contains Rab3A, Rab3B, Rab3C and Rab3D; The Rab3 subfamily contains Rab3A, ...

72-223

1.64e-03

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: 39.13 E-value: 1.64e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  72 LKVGIVGNLASGKSALVHRY----LTGTYVqeeSPEGGRFKKEIVVDGQSYL-LLIRDEGGP---PEAQFAMWVDAV--I 141
Cdd:cd01865    2 FKLLIIGNSSVGKTSFLFRYaddsFTSAFV---STVGIDFKVKTVYRNDKRIkLQIWDTAGQeryRTITTAYYRGAMgfI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 142 FVFSLEDEISFQTVYHYYSRMANYRNTSEiPLVLVGTQDAISsaNPRVIDDARARKLSNDLKrCTYYETCATYGLNVERV 221
Cdd:cd01865   79 LMYDITNEESFNAVQDWSTQIKTYSWDNA-QVILVGNKCDME--DERVVSAERGRQLADQLG-FEFFEASAKENINVKQV 154


                 ..
gi 349585207 222 FQ 223
Cdd:cd01865  155 FE 156

Rab14

cd04122

Rab GTPase family 14 (Rab14); Rab14 GTPases are localized to biosynthetic compartments, ...

76-229

3.00e-03

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: 38.28 E-value: 3.00e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207  76 IVGNLASGKSALVHRYLTGTYVQeESPE--GGRFKKEIV-VDGQSYLLLIRDEGGPPEAQ-----FAMWVDAVIFVFSLE 147
Cdd:cd04122    7 IIGDMGVGKSCLLHQFTEKKFMA-DCPHtiGVEFGTRIIeVNGQKIKLQIWDTAGQERFRavtrsYYRGAAGALMVYDIT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349585207 148 DEISFQTVYHYYSRMANYRNTSEIpLVLVGTQDAISSANPRVIDDARARKLSNDLkrcTYYETCATYGLNVERVFQDVAQ 227
Cdd:cd04122   86 RRSTYNHLSSWLTDARNLTNPNTV-IFLIGNKADLEAQRDVTYEEAKQFADENGL---LFLECSAKTGENVEDAFLETAK 161


                 ..
gi 349585207 228 KI 229
Cdd:cd04122  162 KI 163

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