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Conserved domains on  [gi|4757772|ref|NP_004666|]
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GTP-binding protein Di-Ras3 precursor [Homo sapiens]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
37-200 1.44e-100

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd04140:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 165  Bit Score: 289.03  E-value: 1.44e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   37 DYRVVVVGTAGVGKSTLLHKWASGNFRHEYLPTIENTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVY 116
Cdd:cd04140   1 DYRVVVFGAGGVGKSSLVLRFVKGTFRESYIPTIEDTYRQVISCSKSICTLQITDTTGSHQFPAMQRLSISKGHAFILVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  117 SVTKKETLEELKAFYELICKIKGNNLHKFPIVLVGNKSDDTH-REVALNDGATCAMEWNCAFMEISAKTDVNVQELFHML 195
Cdd:cd04140  81 SITSKQSLEELKPIYELICEIKGNNLEKIPIMLVGNKCDESPsREVSSSEGAALARTWNCAFMETSAKTNHNVQELFQEL 160

                ....*
gi 4757772  196 LNYKK 200
Cdd:cd04140 161 LNLEK 165
 
Name Accession Description Interval E-value
ARHI_like cd04140
A Ras homolog member I (ARHI); ARHI (A Ras homolog member I) is a member of the Ras family ...
37-200 1.44e-100

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: 289.03  E-value: 1.44e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   37 DYRVVVVGTAGVGKSTLLHKWASGNFRHEYLPTIENTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVY 116
Cdd:cd04140   1 DYRVVVFGAGGVGKSSLVLRFVKGTFRESYIPTIEDTYRQVISCSKSICTLQITDTTGSHQFPAMQRLSISKGHAFILVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  117 SVTKKETLEELKAFYELICKIKGNNLHKFPIVLVGNKSDDTH-REVALNDGATCAMEWNCAFMEISAKTDVNVQELFHML 195
Cdd:cd04140  81 SITSKQSLEELKPIYELICEIKGNNLEKIPIMLVGNKCDESPsREVSSSEGAALARTWNCAFMETSAKTNHNVQELFQEL 160

                ....*
gi 4757772  196 LNYKK 200
Cdd:cd04140 161 LNLEK 165
RAS smart00173
Ras subfamily of RAS small GTPases; Similar in fold and function to the bacterial EF-Tu GTPase. ...
50-196 1.10e-36

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: 126.52  E-value: 1.10e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772      50 KSTLLHKWASGNFRHEYLPTIENTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEELKA 129
Cdd:smart00173  13 KSALTIQFIQGHFVDDYDPTIEDSYRKQIEIDGEVCLLDILDTAGQEEFSAMRDQYMRTGEGFLLVYSITDRQSFEEIKK 92
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4757772     130 FYELICKIKGNNlhKFPIVLVGNKSD-DTHREVALNDGATCAMEWNCAFMEISAKTDVNVQELFHMLL 196
Cdd:smart00173  93 FREQILRVKDRD--DVPIVLVGNKCDlESERVVSTEEGKELARQWGCPFLETSAKERVNVDEAFYDLV 158
PTZ00369 PTZ00369
Ras-like protein; Provisional
50-211 1.43e-28

Ras-like protein; Provisional


Pssm-ID: 240385 [Multi-domain]  Cd Length: 189  Bit Score: 106.49  E-value: 1.43e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772    50 KSTLLHKWASGNFRHEYLPTIENTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEELKA 129
Cdd:PTZ00369  18 KSALTIQFIQNHFIDEYDPTIEDSYRKQCVIDEETCLLDILDTAGQEEYSAMRDQYMRTGQGFLCVYSITSRSSFEEIAS 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   130 FYELICKIKGNNlhKFPIVLVGNKSD-DTHREVALNDGATCAMEWNCAFMEISAKTDVNVQELFHMLLNYKKKPTTGLQE 208
Cdd:PTZ00369  98 FREQILRVKDKD--RVPMILVGNKCDlDSERQVSTGEGQELAKSFGIPFLETSAKQRVNVDEAFYELVREIRKYLKEDMP 175

                 ...
gi 4757772   209 PEK 211
Cdd:PTZ00369 176 SQK 178
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
50-196 1.59e-28

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: 105.29  E-value: 1.59e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772     50 KSTLLHKWASGNFRHEYLPTI-ENTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEELK 128
Cdd:pfam00071  12 KSSLLIRFTQNKFPEEYIPTIgVDFYTKTIEVDGKTVKLQIWDTAGQERFRALRPLYYRGADGFLLVYDITSRDSFENVK 91
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4757772    129 AFYELICKIKGNNlhkFPIVLVGNKSD-DTHREVALNDGATCAMEWNCAFMEISAKTDVNVQELFHMLL 196
Cdd:pfam00071  92 KWVEEILRHADEN---VPIVLVGNKCDlEDQRVVSTEEGEALAKELGLPFMETSAKTNENVEEAFEELA 157
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
110-193 1.20e-06

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 47.28  E-value: 1.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  110 HAFVLVYSVTKKETLEelkAFYELICKIKGNNLhKFPIVLVGNKSDDTHREVALNDG---ATCAMEWNCAFMEISAKTDV 186
Cdd:COG1100  81 SLYLFVVDGTREETLQ---SLYELLESLRRLGK-KSPIILVLNKIDLYDEEEIEDEErlkEALSEDNIVEVVATSAKTGE 156

                ....*..
gi 4757772  187 NVQELFH 193
Cdd:COG1100 157 GVEELFA 163
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
50-197 9.89e-04

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: 38.51  E-value: 9.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772     50 KSTLLHKWaSGN--FRHEYLPTIENTY----CQLLGCShgvLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTK-KE 122
Cdd:TIGR00231  14 KSTLLNSL-LGNkgSITEYYPGTTRNYvttvIEEDGKT---YKFNLLDTAGQEDYDAIRRLYYPQVERSLRVFDIVIlVL 89
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4757772    123 TLEELKAFYELIckIKGNNLHKFPIVLVGNKSDDTHREVaLNDGATCAMEWN-CAFMEISAKTDVNVQELFHMLLN 197
Cdd:TIGR00231  90 DVEEILEKQTKE--IIHHADSGVPIILVGNKIDLKDADL-KTHVASEFAKLNgEPIIPLSAETGKNIDSAFKIVEA 162
 
Name Accession Description Interval E-value
ARHI_like cd04140
A Ras homolog member I (ARHI); ARHI (A Ras homolog member I) is a member of the Ras family ...
37-200 1.44e-100

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: 289.03  E-value: 1.44e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   37 DYRVVVVGTAGVGKSTLLHKWASGNFRHEYLPTIENTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVY 116
Cdd:cd04140   1 DYRVVVFGAGGVGKSSLVLRFVKGTFRESYIPTIEDTYRQVISCSKSICTLQITDTTGSHQFPAMQRLSISKGHAFILVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  117 SVTKKETLEELKAFYELICKIKGNNLHKFPIVLVGNKSDDTH-REVALNDGATCAMEWNCAFMEISAKTDVNVQELFHML 195
Cdd:cd04140  81 SITSKQSLEELKPIYELICEIKGNNLEKIPIMLVGNKCDESPsREVSSSEGAALARTWNCAFMETSAKTNHNVQELFQEL 160

                ....*
gi 4757772  196 LNYKK 200
Cdd:cd04140 161 LNLEK 165
Ras cd00876
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ...
50-196 1.10e-47

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: 154.61  E-value: 1.10e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   50 KSTLLHKWASGNFRHEYLPTIENTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEELKA 129
Cdd:cd00876  12 KSALTIRFVSGEFVEEYDPTIEDSYRKQIVVDGETYTLDILDTAGQEEFSAMRDQYIRNGDGFILVYSITSRESFEEIKN 91
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4757772  130 FYELICKIKGNnlHKFPIVLVGNKSD-DTHREVALNDGATCAMEWNCAFMEISAKTDVNVQELFHMLL 196
Cdd:cd00876  92 IREQILRVKDK--EDVPIVLVGNKCDlENERQVSTEEGEALAEEWGCPFLETSAKTNINIDELFNTLV 157
RAS smart00173
Ras subfamily of RAS small GTPases; Similar in fold and function to the bacterial EF-Tu GTPase. ...
50-196 1.10e-36

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: 126.52  E-value: 1.10e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772      50 KSTLLHKWASGNFRHEYLPTIENTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEELKA 129
Cdd:smart00173  13 KSALTIQFIQGHFVDDYDPTIEDSYRKQIEIDGEVCLLDILDTAGQEEFSAMRDQYMRTGEGFLLVYSITDRQSFEEIKK 92
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4757772     130 FYELICKIKGNNlhKFPIVLVGNKSD-DTHREVALNDGATCAMEWNCAFMEISAKTDVNVQELFHMLL 196
Cdd:smart00173  93 FREQILRVKDRD--DVPIVLVGNKCDlESERVVSTEEGKELARQWGCPFLETSAKERVNVDEAFYDLV 158
small_GTPase smart00010
Small GTPase of the Ras superfamily; ill-defined subfamily; SMART predicts Ras-like small ...
36-196 4.28e-35

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: 122.28  E-value: 4.28e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772      36 RDYRVVVVGTAGVGKSTLLHKWASGNFRHEYLPTIENTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLV 115
Cdd:smart00010   1 REYKLVVLGGGGVGKSALTIQFVQGHFVDEYDPTIEDSYRKQIEIDGEVCLLDILDTAGQEEFSAMRDQYMRTGEGFLLV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772     116 YSVTKKETLEELKAFYELICKIKGNNlhKFPIVLVGNKSD-DTHREVALNDGATCAMEWNCAFMEISAKTDVNVQELFHM 194
Cdd:smart00010  81 YSITDRQSFEEIAKFREQILRVKDRD--DVPIVLVGNKCDlENERVVSTEEGKELARQWGCPFLETSAKERINVDEAFYD 158

                   ..
gi 4757772     195 LL 196
Cdd:smart00010 159 LV 160
Ras2 cd04144
Rat sarcoma (Ras) family 2 of small guanosine triphosphatases (GTPases); The Ras2 subfamily, ...
62-229 2.24e-32

Rat sarcoma (Ras) family 2 of small guanosine triphosphatases (GTPases); The Ras2 subfamily, found exclusively in fungi, was first identified in Ustilago maydis. In U. maydis, Ras2 is regulated by Sql2, a protein that is homologous to GEFs (guanine nucleotide exchange factors) of the CDC25 family. Ras2 has been shown to induce filamentous growth, but the signaling cascade through which Ras2 and Sql2 regulate cell morphology is not known. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins.


Pssm-ID: 133344 [Multi-domain]  Cd Length: 190  Bit Score: 116.10  E-value: 2.24e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   62 FRHEYLPTIENTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEELKAFYELICKIKGNN 141
Cdd:cd04144  24 FVETYDPTIEDSYRKQVVVDGQPCMLEVLDTAGQEEYTALRDQWIREGEGFILVYSITSRSTFERVERFREQIQRVKDES 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  142 LHKFPIVLVGNKSDDTH-REVALNDGATCAMEWNCAFMEISAKTDVNVQELFHMLLNYKKKPTTGLQEPEKKSQMPNTTE 220
Cdd:cd04144 104 AADVPIMIVGNKCDKVYeREVSTEEGAALARRLGCEFIEASAKTNVNVERAFYTLVRALRQQRQGGQGPKGGPTKKKEKK 183

                ....*....
gi 4757772  221 KllDKCIIM 229
Cdd:cd04144 184 K--RKCVIM 190
RheB cd04137
Ras Homolog Enriched in Brain (RheB) is a small GTPase; Rheb (Ras Homolog Enriched in Brain) ...
50-229 4.21e-31

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: 112.72  E-value: 4.21e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   50 KSTLLHKWASGNFRHEYLPTIENTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEELKA 129
Cdd:cd04137  14 KSSLTVQFVEGHFVESYYPTIENTFSKIITYKGQEYHLEIVDTAGQDEYSILPQKYSIGIHGYILVYSVTSRKSFEVVKV 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  130 FYELICKIKGNNlhKFPIVLVGNKSD-DTHREVALNDGATCAMEWNCAFMEISAKTDVNVQELFHMLLNYKKKPTTGLQE 208
Cdd:cd04137  94 IYDKILDMLGKE--SVPIVLVGNKSDlHMERQVSAEEGKKLAESWGAAFLESSAKENENVEEAFELLIEEIEKVENPLPP 171
                       170       180
                ....*....|....*....|.
gi 4757772  209 PEKKsqmpntteklldKCIIM 229
Cdd:cd04137 172 GQKS------------KCSVM 180
Rap2 cd04176
Rap2 family GTPase consists of Rap2a, Rap2b, and Rap2c; The Rap2 subgroup is part of the Rap ...
50-192 3.36e-29

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: 107.23  E-value: 3.36e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   50 KSTLLHKWASGNFRHEYLPTIENTYCQ--LLGCSHGVLslHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEEL 127
Cdd:cd04176  14 KSALTVQFVSGTFIEKYDPTIEDFYRKeiEVDSSPSVL--EILDTAGTEQFASMRDLYIKNGQGFIVVYSLVNQQTFQDI 91
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4757772  128 KAFYELICKIKGnnLHKFPIVLVGNKSD-DTHREVALNDGATCAMEWNCAFMEISAKTDVNVQELF 192
Cdd:cd04176  92 KPMRDQIVRVKG--YEKVPIILVGNKVDlESEREVSSAEGRALAEEWGCPFMETSAKSKTMVNELF 155
PTZ00369 PTZ00369
Ras-like protein; Provisional
50-211 1.43e-28

Ras-like protein; Provisional


Pssm-ID: 240385 [Multi-domain]  Cd Length: 189  Bit Score: 106.49  E-value: 1.43e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772    50 KSTLLHKWASGNFRHEYLPTIENTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEELKA 129
Cdd:PTZ00369  18 KSALTIQFIQNHFIDEYDPTIEDSYRKQCVIDEETCLLDILDTAGQEEYSAMRDQYMRTGQGFLCVYSITSRSSFEEIAS 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   130 FYELICKIKGNNlhKFPIVLVGNKSD-DTHREVALNDGATCAMEWNCAFMEISAKTDVNVQELFHMLLNYKKKPTTGLQE 208
Cdd:PTZ00369  98 FREQILRVKDKD--RVPMILVGNKCDlDSERQVSTGEGQELAKSFGIPFLETSAKQRVNVDEAFYELVREIRKYLKEDMP 175

                 ...
gi 4757772   209 PEK 211
Cdd:PTZ00369 176 SQK 178
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
50-196 1.59e-28

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: 105.29  E-value: 1.59e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772     50 KSTLLHKWASGNFRHEYLPTI-ENTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEELK 128
Cdd:pfam00071  12 KSSLLIRFTQNKFPEEYIPTIgVDFYTKTIEVDGKTVKLQIWDTAGQERFRALRPLYYRGADGFLLVYDITSRDSFENVK 91
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4757772    129 AFYELICKIKGNNlhkFPIVLVGNKSD-DTHREVALNDGATCAMEWNCAFMEISAKTDVNVQELFHMLL 196
Cdd:pfam00071  92 KWVEEILRHADEN---VPIVLVGNKCDlEDQRVVSTEEGEALAKELGLPFMETSAKTNENVEEAFEELA 157
RSR1 cd04177
RSR1/Bud1p family GTPase; RSR1/Bud1p is a member of the Rap subfamily of the Ras family that ...
37-192 8.41e-26

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: 98.71  E-value: 8.41e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   37 DYRVVVVGTAGVGKSTLLHKWASGNFRHEYLPTIENTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVY 116
Cdd:cd04177   1 DYKIVVLGAGGVGKSALTVQFVQNVFIESYDPTIEDSYRKQVEIDGRQCDLEILDTAGTEQFTAMRELYIKSGQGFLLVY 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4757772  117 SVTKKETLEELKAFYELICKIKGNNlhKFPIVLVGNKSD-DTHREVALNDGATCAMEWNCA-FMEISAKTDVNVQELF 192
Cdd:cd04177  81 SVTSEASLNELGELREQVLRIKDSD--NVPMVLVGNKADlEDDRQVSREDGVSLSQQWGNVpFYETSARKRTNVDEVF 156
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, ...
50-195 1.50e-25

Ras GTPase family containing H-Ras,N-Ras and K-Ras4A/4B; H-Ras/N-Ras/K-Ras subfamily. H-Ras, N-Ras, and K-Ras4A/4B are the prototypical members of the Ras family. These isoforms generate distinct signal outputs despite interacting with a common set of activators and effectors, and are strongly associated with oncogenic progression in tumor initiation. Mutated versions of Ras that are insensitive to GAP stimulation (and are therefore constitutively active) are found in a significant fraction of human cancers. Many Ras guanine nucleotide exchange factors (GEFs) have been identified. They are sequestered in the cytosol until activation by growth factors triggers recruitment to the plasma membrane or Golgi, where the GEF colocalizes with Ras. Active (GTP-bound) Ras interacts with several effector proteins that stimulate a variety of diverse cytoplasmic signaling activities. Some are known to positively mediate the oncogenic properties of Ras, including Raf, phosphatidylinositol 3-kinase (PI3K), RalGEFs, and Tiam1. Others are proposed to play negative regulatory roles in oncogenesis, including RASSF and NORE/MST1. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 133338 [Multi-domain]  Cd Length: 162  Bit Score: 97.49  E-value: 1.50e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   50 KSTLLHKWASGNFRHEYLPTIENTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEELKA 129
Cdd:cd04138  14 KSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINSRKSFEDIHT 93
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4757772  130 FYELICKIKgnNLHKFPIVLVGNKSDDTHREVALNDGATCAMEWNCAFMEISAKTDVNVQELFHML 195
Cdd:cd04138  94 YREQIKRVK--DSDDVPMVLVGNKCDLAARTVSTRQGQDLAKSYGIPYIETSAKTRQGVEEAFYTL 157
Rap_like cd04136
Rap-like family consists of Rap1, Rap2 and RSR1; The Rap subfamily consists of the Rap1, Rap2, ...
37-196 1.98e-25

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: 97.63  E-value: 1.98e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   37 DYRVVVVGTAGVGKSTLLHKWASGNFRHEYLPTIENTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVY 116
Cdd:cd04136   1 EYKLVVLGSGGVGKSALTVQFVQGIFVDKYDPTIEDSYRKQIEVDCQQCMLEILDTAGTEQFTAMRDLYIKNGQGFALVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  117 SVTKKETLEELKAFYELICKIKgnNLHKFPIVLVGNKSD-DTHREVALNDGATCAMEW-NCAFMEISAKTDVNVQELFHM 194
Cdd:cd04136  81 SITAQQSFNDLQDLREQILRVK--DTEDVPMILVGNKCDlEDERVVSKEEGQNLARQWgNCPFLETSAKSKINVDEIFYD 158

                ..
gi 4757772  195 LL 196
Cdd:cd04136 159 LV 160
Rap1 cd04175
Rap1 family GTPase consists of Rap1a and Rap1b isoforms; The Rap1 subgroup is part of the Rap ...
37-196 5.54e-25

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: 96.43  E-value: 5.54e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   37 DYRVVVVGTAGVGKSTLLHKWASGNFRHEYLPTIENTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVY 116
Cdd:cd04175   1 EYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDGQQCMLEILDTAGTEQFTAMRDLYMKNGQGFVLVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  117 SVTKKETLEELKAFYELICKIKgnNLHKFPIVLVGNKSD-DTHREVALNDGATCAMEWNCAFMEISAKTDVNVQELFHML 195
Cdd:cd04175  81 SITAQSTFNDLQDLREQILRVK--DTEDVPMILVGNKCDlEDERVVGKEQGQNLARQWGCAFLETSAKAKINVNEIFYDL 158

                .
gi 4757772  196 L 196
Cdd:cd04175 159 V 159
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, ...
47-195 5.69e-24

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


Pssm-ID: 133345 [Multi-domain]  Cd Length: 164  Bit Score: 93.63  E-value: 5.69e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   47 GVGKSTLLHKWASGNFRHEYLPTIENTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEE 126
Cdd:cd04145  12 GVGKSALTIQFIQSYFVTDYDPTIEDSYTKQCEIDGQWARLDILDTAGQEEFSAMREQYMRTGEGFLLVFSVTDRGSFEE 91
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  127 LKAFYELICKIKgnNLHKFPIVLVGNKSD-DTHREVALNDGATCAMEWNCAFMEISAKTDVNVQELFHML 195
Cdd:cd04145  92 VDKFHTQILRVK--DRDEFPMILVGNKADlEHQRQVSREEGQELARQLKIPYIETSAKDRVNVDKAFHDL 159
Ras_dva cd04147
Ras - dorsal-ventral anterior localization (Ras-dva) family; Ras-dva subfamily. Ras-dva (Ras - ...
50-202 6.99e-23

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


Pssm-ID: 206714 [Multi-domain]  Cd Length: 197  Bit Score: 91.82  E-value: 6.99e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   50 KSTLLHKWASGNFRHEYLPTIENTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEELKA 129
Cdd:cd04147  12 KTALIQRFLYDTFEPKHRRTVEELHSKEYEVAGVKVTIDILDTSGSYSFPAMRKLSIQNGDAFALVYSVDDPESFEEVKR 91
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4757772  130 FYELICKIKGNnlhKF-PIVLVGNKSDD-THREV-ALNDGATCAMEWNCAFMEISAKTDVNVQELFHMLLNYKKKP 202
Cdd:cd04147  92 LREEILEVKED---KFvPIVVVGNKIDSlAERQVeAADALSTVELDWNNGFVEASAKDNENVTEVFKELLQQANLP 164
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
50-195 1.02e-22

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: 90.21  E-value: 1.02e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   50 KSTLLHKWASGNFRHEYLPTIentycqllGCSHGVLSLHItdsksGDGNRALQ----------RHVIA---RG-HAFVLV 115
Cdd:cd00154  13 KTSLLLRFVDNKFSENYKSTI--------GVDFKSKTIEV-----DGKKVKLQiwdtagqerfRSITSsyyRGaHGAILV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  116 YSVTKKETLEELKAFYELICKIKGNNLhkfPIVLVGNKSD-DTHREVALNDGATCAMEWNCAFMEISAKTDVNVQELFHM 194
Cdd:cd00154  80 YDVTNRESFENLDKWLNELKEYAPPNI---PIILVGNKSDlEDERQVSTEEAQQFAKENGLLFFETSAKTGENVDEAFES 156

                .
gi 4757772  195 L 195
Cdd:cd00154 157 L 157
RERG_RasL11_like cd04146
Ras-related and Estrogen-Regulated Growth inhibitor (RERG) and Ras-like 11 (RasL11)-like ...
50-196 2.08e-22

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


Pssm-ID: 206713 [Multi-domain]  Cd Length: 166  Bit Score: 89.64  E-value: 2.08e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   50 KSTLLHKWASGNFRHEYLPTIENTYCQLLGCSHGVLSLHITDSKSGDGNRA---LQRHvIARGHAFVLVYSVTKKETLEE 126
Cdd:cd04146  12 KSALTVRFLTKRFIGEYEPNLESLYSRQVTIDGEQVSLEIQDTPGQQQNEDpesLERS-LRWADGFVLVYSITDRSSFDV 90
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4757772  127 LKAFYELICKIKGNNLhKFPIVLVGNKSDDTH-REVALNDGATCAMEWNCAFMEISAKTDVN-VQELFHMLL 196
Cdd:cd04146  91 VSQLLQLIREIKKRDG-EIPVILVGNKADLLHsRQVSTEEGQKLALELGCLFFEVSAAENYLeVQNVFHELC 161
RalA_RalB cd04139
Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily ...
50-195 1.10e-21

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: 87.48  E-value: 1.10e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   50 KSTLLHKWASGNFRHEYLPTIENTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEELKA 129
Cdd:cd04139  13 KSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGEEVQLNILDTAGQEDYAAIRDNYFRSGEGFLLVFSITDMESFTALAE 92
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4757772  130 FYELICKIKGNNlhKFPIVLVGNKSD-DTHREVALNDGATCAMEWNCAFMEISAKTDVNVQELFHML 195
Cdd:cd04139  93 FREQILRVKEDD--NVPLLLVGNKCDlEDKRQVSVEEAANLAEQWGVNYVETSAKTRANVDKVFFDL 157
Rhes_like cd04143
Ras homolog enriched in striatum (Rhes) and activator of G-protein signaling 1 (Dexras1/AGS1); ...
38-203 1.55e-21

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: 89.42  E-value: 1.55e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   38 YRVVVVGTAGVGKSTLLHKWASGNFRHEYLPTIENTYCQLLGCSHGVLSLHITDSKsgdGNR---ALQRHVIARGHAFVL 114
Cdd:cd04143   1 YRMVVLGASKVGKTAIVSRFLGGRFEEQYTPTIEDFHRKLYSIRGEVYQLDILDTS---GNHpfpAMRRLSILTGDVFIL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  115 VYSVTKKETLEELKAFYELICKIKGNNLHK------FPIVLVGNKSD-DTHREVALNDGATC-AMEWNCAFMEISAKTDV 186
Cdd:cd04143  78 VFSLDNRESFEEVCRLREQILETKSCLKNKtkenvkIPMVICGNKADrDFPREVQRDEVEQLvGGDENCAYFEVSAKKNS 157
                       170
                ....*....|....*..
gi 4757772  187 NVQELFHMLLNYKKKPT 203
Cdd:cd04143 158 NLDEMFRALFSLAKLPN 174
RGK cd04148
Rem, Rem2, Rad, Gem/Kir (RGK) subfamily of Ras GTPases; RGK subfamily. The RGK (Rem, Rem2, Rad, ...
50-225 5.23e-21

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: 87.07  E-value: 5.23e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   50 KSTLLHKWASGNFR-HEYLPTIENTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEelK 128
Cdd:cd04148  13 KSSLANIFTAGVYEdSAYEASGDDTYERTVSVDGEEATLVVYDHWEQEDGMWLEDSCMQVGDAYVIVYSVTDRSSFE--K 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  129 AfYELICKIKGNNLHK-FPIVLVGNKSD-DTHREVALNDGATCAMEWNCAFMEISAKTDVNVQELF-----HMLLNYKKK 201
Cdd:cd04148  91 A-SELRIQLRRARQAEdIPIILVGNKSDlVRSREVSVQEGRACAVVFDCKFIETSAALQHNVDELFegivrQVRLRRDSK 169
                       170       180
                ....*....|....*....|....*.
gi 4757772  202 P--TTGLQEPEKKSQMPNTTEKLLDK 225
Cdd:cd04148 170 EknTRRMASRKRRESITKKAKRFLSK 195
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
50-196 9.27e-19

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


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 79.86  E-value: 9.27e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772      50 KSTLLHKWASGNFRHEYLPTIentycqllGCSHGVLSLHITDSK--------SGDGN-RALQRHVIARGHAFVLVYSVTK 120
Cdd:smart00175  13 KSSLLSRFTDGKFSEQYKSTI--------GVDFKTKTIEVDGKRvklqiwdtAGQERfRSITSSYYRGAVGALLVYDITN 84
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4757772     121 KETLEELKAFYElicKIKGNNLHKFPIVLVGNKSDDTH-REVALNDGATCAMEWNCAFMEISAKTDVNVQELFHMLL 196
Cdd:smart00175  85 RESFENLENWLK---ELREYASPNVVIMLVGNKSDLEEqRQVSREEAEAFAEEHGLPFFETSAKTNTNVEEAFEELA 158
Rab5_related cd01860
Rab-related GTPase family includes Rab5 and Rab22; regulates early endosome fusion; The ...
111-195 2.92e-16

Rab-related GTPase family includes Rab5 and Rab22; regulates early endosome fusion; The Rab5-related subfamily includes Rab5 and Rab22 of mammals, Ypt51/Ypt52/Ypt53 of yeast, and RabF of plants. The members of this subfamily are involved in endocytosis and endocytic-sorting pathways. In mammals, Rab5 GTPases localize to early endosomes and regulate fusion of clathrin-coated vesicles to early endosomes and fusion between early endosomes. In yeast, Ypt51p family members similarly regulate membrane trafficking through prevacuolar compartments. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206653 [Multi-domain]  Cd Length: 163  Bit Score: 73.35  E-value: 2.92e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  111 AFVLVYSVTKKETLEELKAFyelICKIKGNNLHKFPIVLVGNKSD-DTHREVALNDGATCAMEWNCAFMEISAKTDVNVQ 189
Cdd:cd01860  76 AAIVVYDITSEESFEKAKSW---VKELQEHGPPNIVIALAGNKADlESKRQVSTEEAQEYADENGLLFMETSAKTGENVN 152

                ....*.
gi 4757772  190 ELFHML 195
Cdd:cd01860 153 ELFTEI 158
Rab18 cd01863
Rab GTPase family 18 (Rab18); Rab18 subfamily. Mammalian Rab18 is implicated in endocytic ...
50-197 1.12e-15

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


Pssm-ID: 206656 [Multi-domain]  Cd Length: 161  Bit Score: 71.57  E-value: 1.12e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   50 KSTLLHKWASGNFRHEYLPTIENTY-CQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEELK 128
Cdd:cd01863  13 KSSLLLRFTDDTFDEDLSSTIGVDFkVKTVTVDGKKVKLAIWDTAGQERFRTLTSSYYRGAQGVILVYDVTRRDTFDNLD 92
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4757772  129 AFYELICKIKGNnlHKFPIVLVGNKSDDTHREVALNDGATCAMEWNCAFMEISAKTDVNVQELFHMLLN 197
Cdd:cd01863  93 TWLNELDTYSTN--PDAVKMLVGNKIDKENREVTREEGQKFARKHNMLFIETSAKTRIGVQQAFEELVE 159
Rit_Rin_Ric cd04141
Ras-like protein in all tissues (Rit), Ras-like protein in neurons (Rin) and Ras-related ...
36-201 2.30e-15

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: 71.04  E-value: 2.30e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   36 RDYRVVVVGTAGVGKSTLLHKWASGNFRHEYLPTIENTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLV 115
Cdd:cd04141   1 REYKIVMLGAGGVGKSAVTMQFISHSFPDYHDPTIEDAYKTQARIDNEPALLDILDTAGQAEFTAMRDQYMRCGEGFIIC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  116 YSVTKKETLEELKAFYELICKIKGNNlhKFPIVLVGNKSD-DTHREVALNDGATCAMEWNCAFMEISAKTDVNVQELFHM 194
Cdd:cd04141  81 YSVTDRHSFQEASEFKELITRVRLTE--DIPLVLVGNKVDlEQQRQVTTEEGRNLAREFNCPFFETSAALRFYIDDAFHG 158

                ....*..
gi 4757772  195 LLNYKKK 201
Cdd:cd04141 159 LVREIRR 165
Rab6 cd01861
Rab GTPase family 6 (Rab6); Rab6 is involved in microtubule-dependent transport pathways ...
110-195 2.27e-14

Rab GTPase family 6 (Rab6); Rab6 is involved in microtubule-dependent transport pathways through the Golgi and from endosomes to the Golgi. Rab6A of mammals is implicated in retrograde transport through the Golgi stack, and is also required for a slow, COPI-independent, retrograde transport pathway from the Golgi to the endoplasmic reticulum (ER). This pathway may allow Golgi residents to be recycled through the ER for scrutiny by ER quality-control systems. Yeast Ypt6p, the homolog of the mammalian Rab6 GTPase, is not essential for cell viability. Ypt6p acts in endosome-to-Golgi, in intra-Golgi retrograde transport, and possibly also in Golgi-to-ER trafficking. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206654 [Multi-domain]  Cd Length: 161  Bit Score: 68.03  E-value: 2.27e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  110 HAFVLVYSVTKKETLEELKAFYELICKIKGNNLHkfpIVLVGNKSD-DTHREVALNDGATCAMEWNCAFMEISAKTDVNV 188
Cdd:cd01861  74 SVAVVVYDITNRQSFDNTDKWIDDVRDERGNDVI---IVLVGNKTDlSDKRQVSTEEGEKKAKENNAMFIETSAKAGHNV 150

                ....*..
gi 4757772  189 QELFHML 195
Cdd:cd01861 151 KQLFKKI 157
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
50-197 9.71e-14

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: 66.33  E-value: 9.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   50 KSTLLHKWASGNF---RHEYLPTIENTYCQlLGCSHGVLSLHITD-----SKSGDGNRALQRHVIARGHAFVLVYSVTKK 121
Cdd:cd00882  10 KSSLLNALLGGEVgevSDVPGTTRDPDVYV-KELDKGKVKLVLVDtpgldEFGGLGREELARLLLRGADLILLVVDSTDR 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  122 ETLEELKafYELICKIKGNNLhkfPIVLVGNKSDDthREVALNDGATCAMEW----NCAFMEISAKTDVNVQELFHMLLN 197
Cdd:cd00882  89 ESEEDAK--LLILRRLRKEGI---PIILVGNKIDL--LEEREVEELLRLEELakilGVPVFEVSAKTGEGVDELFEKLIE 161
Rab21 cd04123
Rab GTPase family 21 (Rab21); The localization and function of Rab21 are not clearly defined, ...
50-192 2.67e-13

Rab GTPase family 21 (Rab21); The localization and function of Rab21 are not clearly defined, with conflicting data reported. Rab21 has been reported to localize in the ER in human intestinal epithelial cells, with partial colocalization with alpha-glucosidase, a late endosomal/lysosomal marker. More recently, Rab21 was shown to colocalize with and affect the morphology of early endosomes. In Dictyostelium, GTP-bound Rab21, together with two novel LIM domain proteins, LimF and ChLim, has been shown to regulate phagocytosis. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 133323 [Multi-domain]  Cd Length: 162  Bit Score: 65.32  E-value: 2.67e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   50 KSTLLHKWASGNFRHEYLPTIENTYCQ----LLGCShgvLSLHITDSksgdgnrALQRhviaRGHAF-----------VL 114
Cdd:cd04123  13 KTSLVLRYVENKFNEKHESTTQASFFQktvnIGGKR---IDLAIWDT-------AGQE----RYHALgpiyyrdadgaIL 78
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4757772  115 VYSVTKKETLEELKAFYELICKIKGNNLHkfpIVLVGNKSD-DTHREVALNDGATCAMEWNCAFMEISAKTDVNVQELF 192
Cdd:cd04123  79 VYDITDADSFQKVKKWIKELKQMRGNNIS---LVIVGNKIDlERQRVVSKSEAEEYAKSVGAKHFETSAKTGKGIEELF 154
Rab11_like cd01868
Rab GTPase family 11 (Rab11)-like includes Rab11a, Rab11b, and Rab25; Rab11a, Rab11b, and ...
114-197 2.79e-13

Rab GTPase family 11 (Rab11)-like includes Rab11a, Rab11b, and Rab25; Rab11a, Rab11b, and Rab25 are closely related, evolutionary conserved Rab proteins that are differentially expressed. Rab11a is ubiquitously synthesized, Rab11b is enriched in brain and heart and Rab25 is only found in epithelia. Rab11/25 proteins seem to regulate recycling pathways from endosomes to the plasma membrane and to the trans-Golgi network. Furthermore, Rab11a is thought to function in the histamine-induced fusion of tubulovesicles containing H+, K+ ATPase with the plasma membrane in gastric parietal cells and in insulin-stimulated insertion of GLUT4 in the plasma membrane of cardiomyocytes. Overexpression of Rab25 has recently been observed in ovarian cancer and breast cancer, and has been correlated with worsened outcomes in both diseases. In addition, Rab25 overexpression has also been observed in prostate cancer, transitional cell carcinoma of the bladder, and invasive breast tumor cells. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206660 [Multi-domain]  Cd Length: 165  Bit Score: 65.27  E-value: 2.79e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  114 LVYSVTKKET-------LEELKAFYElickikgnnlHKFPIVLVGNKSDDTH-REVALNDGATCAMEWNCAFMEISAKTD 185
Cdd:cd01868  81 LVYDITKKSTfenverwLKELRDHAD----------SNIVIMLVGNKSDLRHlRAVPTEEAKAFAEKNGLSFIETSALDG 150
                        90
                ....*....|..
gi 4757772  186 VNVQELFHMLLN 197
Cdd:cd01868 151 TNVEEAFKQLLT 162
Miro1 cd01893
Mitochondrial Rho family 1 (Miro1), N-terminal; Miro1 subfamily. Miro (mitochondrial Rho) ...
86-194 9.38e-13

Mitochondrial Rho family 1 (Miro1), N-terminal; Miro1 subfamily. Miro (mitochondrial Rho) proteins have tandem GTP-binding domains separated by a linker region containing putative calcium-binding EF hand motifs. Genes encoding Miro-like proteins were found in several eukaryotic organisms. This CD represents the N-terminal GTPase domain of Miro proteins. These atypical Rho GTPases have roles in mitochondrial homeostasis and apoptosis. Most Rho proteins contain a lipid modification site at the C-terminus; however, Miro is one of few Rho subfamilies that lack this feature.


Pssm-ID: 206680 [Multi-domain]  Cd Length: 168  Bit Score: 63.90  E-value: 9.38e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   86 SLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEELKAFYELICKIKGNNLhkfPIVLVGNKSD--DTHREVAL 163
Cdd:cd01893  50 PTTIVDTSSRPQDRANLAAEIRKANVICLVYSVDRPSTLERIRTKWLPLIRRLGVKV---PIILVGNKSDlrDGSSQAGL 126
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 4757772  164 NDGATCAMewnCAFMEI------SAKTDVNVQELFHM 194
Cdd:cd01893 127 EEEMLPIM---NEFREIetcvecSAKTLINVSEVFYY 160
RJL cd04119
Rab GTPase family J-like (RabJ-like); RJLs are found in many protists and as chimeras with ...
47-197 3.70e-12

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: 62.37  E-value: 3.70e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   47 GVGKSTLLHKWASGNFRHEYLPTIentycqllGCSHGVLSLHITDSK--------SGDGNRALQRHVIARG-HAFVLVYS 117
Cdd:cd04119  10 GVGKSCIIKRYCEGRFVSKYLPTI--------GIDYGVKKVSVRNKEvrvnffdlSGHPEYLEVRNEFYKDtQGVLLVYD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  118 VTKKETLEELKAFYELICKIKG--NNLHKFPIVLVGNKSDDT-HREVALNDGATCAMEWNCAFMEISAKTDVNVQELFHM 194
Cdd:cd04119  82 VTDRQSFEALDSWLKEMKQEGGphGNMENIVVVVCANKIDLTkHRAVSEDEGRLWAESKGFKYFETSACTGEGVNEMFQT 161

                ...
gi 4757772  195 LLN 197
Cdd:cd04119 162 LFS 164
Rab8_Rab10_Rab13_like cd01867
Rab GTPase families 8, 10, 13 (Rab8, Rab10, Rab13); Rab8/Sec4/Ypt2 are known or suspected to ...
108-201 9.26e-12

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: 61.13  E-value: 9.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  108 RG-HAFVLVYSVTKKETLEELKAFYELICKIKGNNLHKFpivLVGNKSDDTH-REVALNDGATCAMEWNCAFMEISAKTD 185
Cdd:cd01867  74 RGaMGIILVYDITDEKSFENIKNWMRNIDEHASEDVERM---LVGNKCDMEEkRVVSKEEGEALAREYGIKFLETSAKAN 150
                        90
                ....*....|....*..
gi 4757772  186 VNVQELF-HMLLNYKKK 201
Cdd:cd01867 151 INVEEAFlTLAKDILKK 167
Rab1_Ypt1 cd01869
Rab GTPase family 1 includes the yeast homolog Ypt1; Rab1/Ypt1 subfamily. Rab1 is found in ...
108-195 1.05e-11

Rab GTPase family 1 includes the yeast homolog Ypt1; Rab1/Ypt1 subfamily. Rab1 is found in every eukaryote and is a key regulatory component for the transport of vesicles from the ER to the Golgi apparatus. Studies on mutations of Ypt1, the yeast homolog of Rab1, showed that this protein is necessary for the budding of vesicles of the ER as well as for their transport to, and fusion with, the Golgi apparatus. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206661 [Multi-domain]  Cd Length: 166  Bit Score: 61.19  E-value: 1.05e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  108 RG-HAFVLVYSVTKKETLEELKAFYELICKIKGNNLHKfpiVLVGNKSD-DTHREVALNDGATCAMEWNCAFMEISAKTD 185
Cdd:cd01869  73 RGaHGIIIVYDVTDQESFNNVKQWLQEIDRYASENVNK---LLVGNKCDlTDKKVVDYTEAKEFADELGIPFLETSAKNA 149
                        90
                ....*....|
gi 4757772  186 VNVQELFHML 195
Cdd:cd01869 150 TNVEEAFMTM 159
Rab2 cd01866
Rab GTPase family 2 (Rab2); Rab2 is localized on cis-Golgi membranes and interacts with Golgi ...
87-192 1.14e-11

Rab GTPase family 2 (Rab2); Rab2 is localized on cis-Golgi membranes and interacts with Golgi matrix proteins. Rab2 is also implicated in the maturation of vesicular tubular clusters (VTCs), which are microtubule-associated intermediates in transport between the ER and Golgi apparatus. In plants, Rab2 regulates vesicle trafficking between the ER and the Golgi bodies and is important to pollen tube growth. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206658 [Multi-domain]  Cd Length: 168  Bit Score: 60.90  E-value: 1.14e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   87 LHITDSKSGDGNRALQRHVIaRGHA-FVLVYSVTKKETLEELKAFYElICKIKGNNlhKFPIVLVGNKSDDTH-REVALN 164
Cdd:cd01866  55 LQIWDTAGQESFRSITRSYY-RGAAgALLVYDITRRETFNHLTSWLE-DARQHSNS--NMTIMLIGNKCDLESrREVSYE 130
                        90       100
                ....*....|....*....|....*...
gi 4757772  165 DGATCAMEWNCAFMEISAKTDVNVQELF 192
Cdd:cd01866 131 EGEAFAREHGLIFMETSAKTASNVEEAF 158
Rab35 cd04110
Rab GTPase family 35 (Rab35); Rab35 is one of several Rab proteins to be found to participate ...
50-221 3.19e-11

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: 60.25  E-value: 3.19e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   50 KSTLLHKWASGNFRHEYLPTIENTY-CQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEELK 128
Cdd:cd04110  19 KSSLLLRFADNTFSGSYITTIGVDFkIRTVEINGERVKLQIWDTAGQERFRTITSTYYRGTHGVIVVYDVTNGESFVNVK 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  129 AFYELIckikGNNLHKFPIVLVGNKSDDTHREVALN-DGATCAMEWNCAFMEISAKTDVNVQELFHMLlnykkkptTGLQ 207
Cdd:cd04110  99 RWLQEI----EQNCDDVCKVLVGNKNDDPERKVVETeDAYKFAGQMGISLFETSAKENINVEEMFNCI--------TELV 166
                       170
                ....*....|....
gi 4757772  208 EPEKKSQMPNTTEK 221
Cdd:cd04110 167 LRAKKDNLAKQQQQ 180
Rab7 cd01862
Rab GTPase family 7 (Rab7); Rab7 subfamily. Rab7 is a small Rab GTPase that regulates ...
108-193 5.01e-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: 59.22  E-value: 5.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  108 RG-HAFVLVYSVTKKETLEELKAFY-ELICKIKGNNLHKFPIVLVGNKSD-DTHREVALNDgatcAMEW-----NCAFME 179
Cdd:cd01862  71 RGaDCCVLVYDVTNPKSFESLDSWRdEFLIQASPRDPENFPFVVLGNKIDlEEKRQVSTKK----AQQWckskgNIPYFE 146
                        90
                ....*....|....
gi 4757772  180 ISAKTDVNVQELFH 193
Cdd:cd01862 147 TSAKEAINVDQAFE 160
PLN03118 PLN03118
Rab family protein; Provisional
85-195 1.06e-10

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 59.30  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772    85 LSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEELKAFYELICKIKGNNlHKFPIVLVGNKSD-DTHREVAL 163
Cdd:PLN03118  62 LKLTIWDTAGQERFRTLTSSYYRNAQGIILVYDVTRRETFTNLSDVWGKEVELYSTN-QDCVKMLVGNKVDrESERDVSR 140
                         90       100       110
                 ....*....|....*....|....*....|..
gi 4757772   164 NDGATCAMEWNCAFMEISAKTDVNVQELFHML 195
Cdd:PLN03118 141 EEGMALAKEHGCLFLECSAKTRENVEQCFEEL 172
PLN03108 PLN03108
Rab family protein; Provisional
85-192 1.76e-10

Rab family protein; Provisional


Pssm-ID: 178655 [Multi-domain]  Cd Length: 210  Bit Score: 58.41  E-value: 1.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772    85 LSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEELKAFYELICKIKGNNLhkfPIVLVGNKSDDTHRE-VAL 163
Cdd:PLN03108  55 IKLQIWDTAGQESFRSITRSYYRGAAGALLVYDITRRETFNHLASWLEDARQHANANM---TIMLIGNKCDLAHRRaVST 131
                         90       100
                 ....*....|....*....|....*....
gi 4757772   164 NDGATCAMEWNCAFMEISAKTDVNVQELF 192
Cdd:PLN03108 132 EEGEQFAKEHGLIFMEASAKTAQNVEEAF 160
Rab26 cd04112
Rab GTPase family 26 (Rab26); Rab26 subfamily. First identified in rat pancreatic acinar cells, ...
87-226 1.68e-09

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: 55.64  E-value: 1.68e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   87 LHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEELKAFYELICKIKGNNLHkfpIVLVGNKSD-DTHREVALND 165
Cdd:cd04112  52 LQIWDTAGQERFRSVTHAYYRDAHALLLLYDVTNKSSFDNIRAWLTEILEYAQSDVV---IMLLGNKADmSGERVVKRED 128
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4757772  166 GATCAMEWNCAFMEISAKTDVNVQELFHMLLnyKKKPTTGLQEP-EKKSQMPNTTEKLLDKC 226
Cdd:cd04112 129 GERLAKEYGVPFMETSAKTGLNVELAFTAVA--KELKHRSVEQPdEPKFKIQDYVEKQKKSS 188
Rab12 cd04120
Rab GTPase family 12 (Rab12); Rab12 was first identified in canine cells, where it was ...
107-216 3.01e-09

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


Pssm-ID: 206699 [Multi-domain]  Cd Length: 202  Bit Score: 55.02  E-value: 3.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  107 ARGhaFVLVYSVTKKETLEELKAFYELICKIKGNNLHkfpIVLVGNKSD-DTHREVALNDGATCAMEWN-CAFMEISAKT 184
Cdd:cd04120  73 AKG--IILVYDITKKETFDDLPKWMKMIDKYASEDAE---LLLVGNKLDcETDREITRQQGEKFAQQITgMRFCEASAKD 147
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 4757772  185 DVNVQELFHMLLN--YKKKP-----------TTGLQ-EPEKKSQMP 216
Cdd:cd04120 148 NFNVDEIFLKLVDdiLKKMPldilrnelsnsILSLQpEPEIPPELP 193
Rab14 cd04122
Rab GTPase family 14 (Rab14); Rab14 GTPases are localized to biosynthetic compartments, ...
50-192 3.34e-09

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: 54.07  E-value: 3.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   50 KSTLLHKWASGNFRHEYLPTIENTY-CQLLGCSHGVLSLHITDSKSGDGNRALQRHVIaRGHAFVL-VYSVTKKETLEEL 127
Cdd:cd04122  15 KSCLLHQFTEKKFMADCPHTIGVEFgTRIIEVNGQKIKLQIWDTAGQERFRAVTRSYY-RGAAGALmVYDITRRSTYNHL 93
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4757772  128 KAFyelICKIKGNNLHKFPIVLVGNKSD-DTHREVALNDGATCAMEWNCAFMEISAKTDVNVQELF 192
Cdd:cd04122  94 SSW---LTDARNLTNPNTVIFLIGNKADlEAQRDVTYEEAKQFADENGLLFLECSAKTGENVEDAF 156
Rho cd00157
Ras homology family (Rho) of small guanosine triphosphatases (GTPases); Members of the Rho ...
46-198 1.08e-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: 52.93  E-value: 1.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   46 AGVGKSTLLHKWASGNFRHEYLPTIENTYCQLLGCSHGVLSLHITDSkSGDGN----RAL---QRHViarghaFVLVYSV 118
Cdd:cd00157   9 GAVGKTCLLISYTTNKFPTEYVPTVFDNYSANVTVDGKQVNLGLWDT-AGQEEydrlRPLsypQTDV------FLLCFSV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  119 TKKETLEELKA--FYELICkikgnNLHKFPIVLVGNKSD-----DTHREVALN-------DGATCAMEWNC-AFMEISAK 183
Cdd:cd00157  82 DSPSSFENVKTkwYPEIKH-----YCPNVPIILVGTKIDlrddgNTLKKLEKKqkpitpeEGEKLAKEIGAvKYMECSAL 156
                       170
                ....*....|....*
gi 4757772  184 TDVNVQELFHMLLNY 198
Cdd:cd00157 157 TQEGLKEVFDEAIRA 171
RRP22 cd04142
Ras-related protein on chromosome 22 (RRP22) family; RRP22 (Ras-related protein on chromosome ...
50-196 2.14e-08

Ras-related protein on chromosome 22 (RRP22) family; RRP22 (Ras-related protein on chromosome 22) subfamily consists of proteins that inhibit cell growth and promote caspase-independent cell death. Unlike most Ras proteins, RRP22 is down-regulated in many human tumor cells due to promoter methylation. RRP22 localizes to the nucleolus in a GTP-dependent manner, suggesting a novel function in modulating transport of nucleolar components. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Like most Ras family proteins, RRP22 is farnesylated.


Pssm-ID: 133342 [Multi-domain]  Cd Length: 198  Bit Score: 52.56  E-value: 2.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   50 KSTLLHKWASGNFRHEYLPTI-ENTYCQLLGCSHGVLSLHITD---SKSGDGNrALQRHVIAR------GHAFVLVYSVT 119
Cdd:cd04142  13 KTAIVRQFLAQEFPEEYIPTEhRRLYRPAVVLSGRVYDLHILDvpnMQRYPGT-AGQEWMDPRfrglrnSRAFILVYDIC 91
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4757772  120 KKETLEELKAFYELICKIKGNNLHKFPIVLVGNKSDDTHREVA--LNDGATCAMEWNCAFMEISAKTDVNVQELFHMLL 196
Cdd:cd04142  92 SPDSFHYVKLLRQQILETRPAGNKEPPIVVVGNKRDQQRHRFAprHVLSVLVRKSWKCGYLECSAKYNWHILLLFKELL 170
Rab39 cd04111
Rab GTPase family 39 (Rab39); Found in eukaryotes, Rab39 is mainly found in epithelial cell ...
50-195 5.82e-08

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: 51.30  E-value: 5.82e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   50 KSTLLHKWASGNFRHEYLPTIE-NTYCQLLGCSHGV-LSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEEL 127
Cdd:cd04111  15 KSSLLKRFTEGRFAEVSDPTVGvDFFSRLIEIEPGVrIKLQLWDTAGQERFRSITRSYYRNSVGVLLVFDITNRESFEHV 94
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  128 KAFY-ELICKIKGnnlHKFPIVLVGNKSD-DTHREVALNDGATCAMEWNCAFMEISAKTDVNVQELFHML 195
Cdd:cd04111  95 HDWLeEARSHIQP---HRPVFILVGHKCDlESQRQVTREEAEKLAKDLGMKYIETSARTGDNVEEAFELL 161
PTZ00099 PTZ00099
rab6; Provisional
69-192 2.18e-07

rab6; Provisional


Pssm-ID: 185444 [Multi-domain]  Cd Length: 176  Bit Score: 49.36  E-value: 2.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772    69 TIENTYCQLLGCS---------HGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEELKAFYELICKIKG 139
Cdd:PTZ00099   4 TFDNNYQSTIGIDflsktlyldEGPVRLQLWDTAGQERFRSLIPSYIRDSAAAIVVYDITNRQSFENTTKWIQDILNERG 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 4757772   140 NNLhkfPIVLVGNKSD-DTHREVALNDGATCAMEWNCAFMEISAKTDVNVQELF 192
Cdd:PTZ00099  84 KDV---IIALVGNKTDlGDLRKVTYEEGMQKAQEYNTMFHETSAKAGHNIKVLF 134
Rab4 cd04113
Rab GTPase family 4 (Rab4); Rab4 subfamily. Rab4 has been implicated in numerous functions ...
50-192 2.54e-07

Rab GTPase family 4 (Rab4); Rab4 subfamily. Rab4 has been implicated in numerous functions within the cell. It helps regulate endocytosis through the sorting, recycling, and degradation of early endosomes. Mammalian Rab4 is involved in the regulation of many surface proteins including G-protein-coupled receptors, transferrin receptor, integrins, and surfactant protein A. Experimental data implicate Rab4 in regulation of the recycling of internalized receptors back to the plasma membrane. It is also believed to influence receptor-mediated antigen processing in B-lymphocytes, in calcium-dependent exocytosis in platelets, in alpha-amylase secretion in pancreatic cells, and in insulin-induced translocation of Glut4 from internal vesicles to the cell surface. Rab4 is known to share effector proteins with Rab5 and Rab11. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206696 [Multi-domain]  Cd Length: 161  Bit Score: 48.97  E-value: 2.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   50 KSTLLHKWASGNFRHEYLPTIENTY-CQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEELK 128
Cdd:cd04113  13 KSCLLHQFIENKFKQDSNHTIGVEFgSRVVNVGGKSVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYDITSRESFNALT 92
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4757772  129 AFYELICKIKGNNLhkfPIVLVGNKSD-DTHREVALNDGATCAMEWNCAFMEISAKTDVNVQELF 192
Cdd:cd04113  93 NWLTDARTLASPDI---VIILVGNKKDlEDDREVTFLEASRFAQENGLLFLETSALTGENVEEAF 154
Rab3 cd01865
Rab GTPase family 3 contains Rab3A, Rab3B, Rab3C and Rab3D; The Rab3 subfamily contains Rab3A, ...
112-197 4.75e-07

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: 47.98  E-value: 4.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  112 FVLVYSVTKKETLEELKAFYELICKIKGNNLHkfpIVLVGNKSD-DTHREVALNDGATCAMEWNCAFMEISAKTDVNVQE 190
Cdd:cd01865  77 FILMYDITNEESFNAVQDWSTQIKTYSWDNAQ---VILVGNKCDmEDERVVSAERGRQLADQLGFEFFEASAKENINVKQ 153

                ....*..
gi 4757772  191 LFHMLLN 197
Cdd:cd01865 154 VFERLVD 160
Rab9 cd04116
Rab GTPase family 9 (Rab9); Rab9 is found in late endosomes, together with mannose 6-phosphate ...
50-192 5.53e-07

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: 47.95  E-value: 5.53e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   50 KSTLLHKWASGNFRHEYLPTIENTYC-QLLGCSHGVLSLHITDSKSGDGNRALqRHVIARGH-AFVLVYSVTKKETLEEL 127
Cdd:cd04116  18 KSSLMNRYVTNKFDTQLFHTIGVEFLnKDLEVDGHFVTLQIWDTAGQERFRSL-RTPFYRGSdCCLLTFSVDDSQSFQNL 96
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4757772  128 KAFY-ELICKIKGNNLHKFPIVLVGNKSDDTHREVALNDG-ATCAMEWNCAFMEISAKTDVNVQELF 192
Cdd:cd04116  97 SNWKkEFIYYADVKEPESFPFVILGNKIDIPERQVSTEEAqAWCRDNGDYPYFETSAKDATNVAAAF 163
PLN03110 PLN03110
Rab GTPase; Provisional
113-216 7.54e-07

Rab GTPase; Provisional


Pssm-ID: 178657 [Multi-domain]  Cd Length: 216  Bit Score: 48.39  E-value: 7.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   113 VLVYSVTKKETLEELKAFYELICKIKGNNLhkfPIVLVGNKSDDTH-REVALNDGATCAMEWNCAFMEISAKTDVNVQEL 191
Cdd:PLN03110  89 LLVYDITKRQTFDNVQRWLRELRDHADSNI---VIMMAGNKSDLNHlRSVAEEDGQALAEKEGLSFLETSALEATNVEKA 165
                         90       100
                 ....*....|....*....|....*....
gi 4757772   192 FHMLLN--YK--KKPTTGLQEPEKKSQMP 216
Cdd:PLN03110 166 FQTILLeiYHiiSKKALAAQEAAANSGLP 194
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
110-193 1.20e-06

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 47.28  E-value: 1.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  110 HAFVLVYSVTKKETLEelkAFYELICKIKGNNLhKFPIVLVGNKSDDTHREVALNDG---ATCAMEWNCAFMEISAKTDV 186
Cdd:COG1100  81 SLYLFVVDGTREETLQ---SLYELLESLRRLGK-KSPIILVLNKIDLYDEEEIEDEErlkEALSEDNIVEVVATSAKTGE 156

                ....*..
gi 4757772  187 NVQELFH 193
Cdd:COG1100 157 GVEELFA 163
Rab23_like cd04106
Rab GTPase family 23 (Rab23)-like; Rab23-like subfamily. Rab23 is a member of the Rab family ...
46-195 1.54e-06

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: 46.67  E-value: 1.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   46 AGVGKSTLLHKWASGNFRHEYLPTIENTYCQ---LLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKE 122
Cdd:cd04106   9 GNVGKSSMIQRFVKGIFTKDYKKTIGVDFLEkqiFLRQSDEDVRLMLWDTAGQEEFDAITKAYYRGAQACILVFSTTDRE 88
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4757772  123 TLEELKAFYELICKIKGNnlhkFPIVLVGNKSDDTHREVALNDGA-TCAMEWNCAFMEISAKTDVNVQELFHML 195
Cdd:cd04106  89 SFEAIESWKEKVEAECGD----IPMVLVQTKIDLLDQAVITNEEAeALAKRLQLPLFRTSVKDDFNVTELFEYL 158
Ran cd00877
Ras-related nuclear proteins (Ran)/TC4 family of small GTPases; Ran GTPase is involved in ...
50-192 2.07e-06

Ras-related nuclear proteins (Ran)/TC4 family of small GTPases; Ran GTPase is involved in diverse biological functions, such as nuclear transport, spindle formation during mitosis, DNA replication, and cell division. Among the Ras superfamily, Ran is a unique small G protein. It does not have a lipid modification motif at the C-terminus to bind to the membrane, which is often observed within the Ras superfamily. Ran may therefore interact with a wide range of proteins in various intracellular locations. Like other GTPases, Ran exists in GTP- and GDP-bound conformations that interact differently with effectors. Conversion between these forms and the assembly or disassembly of effector complexes requires the interaction of regulator proteins. The intrinsic GTPase activity of Ran is very low, but it is greatly stimulated by a GTPase-activating protein (RanGAP1) located in the cytoplasm. By contrast, RCC1, a guanine nucleotide exchange factor that generates RanGTP, is bound to chromatin and confined to the nucleus. Ran itself is mobile and is actively imported into the nucleus by a mechanism involving NTF-2. Together with the compartmentalization of its regulators, this is thought to produce a relatively high concentration of RanGTP in the nucleus.


Pssm-ID: 206643 [Multi-domain]  Cd Length: 166  Bit Score: 46.14  E-value: 2.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   50 KSTLLHKWASGNFRHEYLPTIE--------NTYCqllgcshGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKK 121
Cdd:cd00877  13 KTTFVKRHLTGEFEKKYVATLGvevhpldfHTNR-------GKIRFNVWDTAGQEKFGGLRDGYYIQGQCAIIMFDVTSR 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4757772  122 ETLEELKAFYELICKIKGNnlhkFPIVLVGNKSDDTHREVALNdGATCAMEWNCAFMEISAKTDVNVQELF 192
Cdd:cd00877  86 VTYKNVPNWHRDLVRVCEN----IPIVLCGNKVDIKDRKVKPK-QITFHRKKNLQYYEISAKSNYNFEKPF 151
Rab30 cd04114
Rab GTPase family 30 (Rab30); Rab30 subfamily. Rab30 appears to be associated with the Golgi ...
85-195 3.38e-06

Rab GTPase family 30 (Rab30); Rab30 subfamily. Rab30 appears to be associated with the Golgi stack. It is expressed in a wide variety of tissue types and in humans maps to chromosome 11. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 133314 [Multi-domain]  Cd Length: 169  Bit Score: 45.66  E-value: 3.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   85 LSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEELKAFYELICKIKGNNLHKfpiVLVGNKSD-DTHREVAL 163
Cdd:cd04114  56 IKLQIWDTAGQERFRSITQSYYRSANALILTYDITCEESFRCLPEWLREIEQYANNKVIT---ILVGNKIDlAERREVSQ 132
                        90       100       110
                ....*....|....*....|....*....|..
gi 4757772  164 NDGATCAMEWNCAFMEISAKTDVNVQELFHML 195
Cdd:cd04114 133 QRAEEFSDAQDMYYLETSAKESDNVEKLFLDL 164
RAN smart00176
Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases; Ran is involved in the ...
49-192 3.47e-06

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


Pssm-ID: 128473 [Multi-domain]  Cd Length: 200  Bit Score: 46.16  E-value: 3.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772      49 GKSTLLHKWASGNFRHEYLPTIE-NTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEEL 127
Cdd:smart00176   7 GKTTFVKRHLTGEFEKKYVATLGvEVHPLVFHTNRGPIRFNVWDTAGQEKFGGLRDGYYIQGQCAIIMFDVTARVTYKNV 86
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4757772     128 KAFYELICKIKGNnlhkFPIVLVGNKSDDTHREVALNDgATCAMEWNCAFMEISAKTDVNVQELF 192
Cdd:smart00176  87 PNWHRDLVRVCEN----IPIVLCGNKVDVKDRKVKAKS-ITFHRKKNLQYYDISAKSNYNFEKPF 146
Rab32_Rab38 cd04107
Rab GTPase families 18 (Rab18) and 32 (Rab32); Rab38/Rab32 subfamily. Rab32 and Rab38 are ...
110-210 3.76e-06

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


Pssm-ID: 206692 [Multi-domain]  Cd Length: 201  Bit Score: 46.15  E-value: 3.76e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  110 HAFVLVYSVTKKETLEE-LKAFYELICKIKGNNLHKFPIVLVGNKSDDTHREVALND---GATCAMEWNCAFMEISAKTD 185
Cdd:cd04107  75 VGAIIVFDVTRPSTFEAvLKWKADLDSKVTLPNGEPIPALLLANKCDLKKERLAKDPeqmDQFCKENGFIGWFETSAKEN 154
                        90       100
                ....*....|....*....|....*
gi 4757772  186 VNVQELFHMLLNYKKKPTTGLQEPE 210
Cdd:cd04107 155 INIEEAMRFLVKNILKNDKGLQSPE 179
Rab19 cd01864
Rab GTPase family 19 (Rab19); Rab19 subfamily. Rab19 proteins are associated with Golgi stacks. ...
46-197 5.70e-06

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: 45.12  E-value: 5.70e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   46 AGVGKSTLLHKWASGNFRHEYLPTIENTYC-QLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETL 124
Cdd:cd01864  12 SNVGKTCVVQRFKSGTFSERQGNTIGVDFTmKTLEIQGKRVKLQIWDTAGQERFRTITQSYYRSANGAIIAYDITRRSSF 91
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4757772  125 EELKAFYELICKIKGNNLhkfPIVLVGNKSD-DTHREVALNDGATCAMEWNC-AFMEISAKTDVNVQELFHMLLN 197
Cdd:cd01864  92 ESVPHWIEEVEKYGASNV---VLLLIGNKCDlEEQREVLFEEACTLAEHYGIlAVLETSAKESSNVEEAFLLMAT 163
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
50-155 7.58e-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: 43.65  E-value: 7.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772     50 KSTLLHKWASGNFRHEYLPTIentycqllGCSHGVLSLHITDSKSGDGN------------RALQRHVIARGHAFVLVYS 117
Cdd:pfam08477  12 KTSLLKRFVDDTFDPKYKSTI--------GVDFKTKTVLENDDNGKKIKlniwdtagqerfRSLHPFYYRGAAAALLVYD 83
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 4757772    118 VTKKETLEElkaFYELICKIKGNNlhkfPIVLVGNKSD 155
Cdd:pfam08477  84 SRTFSNLKY---WLRELKKYAGNS----PVILVGNKID 114
Rab28 cd04109
Rab GTPase family 28 (Rab28); Rab28 subfamily. First identified in maize, Rab28 has been shown ...
110-195 8.53e-06

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: 45.17  E-value: 8.53e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  110 HAFVLVYSVTKKETLEELKAFYELICKIKGNNLHKFPIVLVGNKSDDTH-REVALNDGATCAMEWNCAFMEISAKTDVNV 188
Cdd:cd04109  75 QAVCLVYDITNSQSFENLEDWLSVVKKVNEESETKPKMVLVGNKTDLEHnRQVTAEKHARFAQENDMESIFVSAKTGDRV 154

                ....*..
gi 4757772  189 QELFHML 195
Cdd:cd04109 155 FLCFQRI 161
PLN03071 PLN03071
GTP-binding nuclear protein Ran; Provisional
50-192 2.77e-05

GTP-binding nuclear protein Ran; Provisional


Pssm-ID: 178620 [Multi-domain]  Cd Length: 219  Bit Score: 43.59  E-value: 2.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772    50 KSTLLHKWASGNFRHEYLPTIE-NTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEELK 128
Cdd:PLN03071  26 KTTFVKRHLTGEFEKKYEPTIGvEVHPLDFFTNCGKIRFYCWDTAGQEKFGGLRDGYYIHGQCAIIMFDVTARLTYKNVP 105
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4757772   129 AFYELICKIKGNnlhkFPIVLVGNKSDDTHREVALNDgATCAMEWNCAFMEISAKTDVNVQELF 192
Cdd:PLN03071 106 TWHRDLCRVCEN----IPIVLCGNKVDVKNRQVKAKQ-VTFHRKKNLQYYEISAKSNYNFEKPF 164
RHO smart00174
Rho (Ras homology) subfamily of Ras-like small GTPases; Members of this subfamily of Ras-like ...
46-194 2.87e-05

Rho (Ras homology) subfamily of Ras-like small GTPases; Members of this subfamily of Ras-like small GTPases include Cdc42 and Rac, as well as Rho isoforms.


Pssm-ID: 197554 [Multi-domain]  Cd Length: 174  Bit Score: 42.99  E-value: 2.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772      46 AGVGKSTLLHKWASGNFRHEYLPTIENTYCQLLGCSHGVLSLHITDSkSG----DGNRAL---QRHViarghaFVLVYSV 118
Cdd:smart00174   7 GAVGKTCLLIVYTTNAFPEDYVPTVFENYSADVEVDGKPVELGLWDT-AGqedyDRLRPLsypDTDV------FLICFSV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772     119 TKKETLE--------ELKAFYElickikgnnlhKFPIVLVGNKSD-----DTHRE--------VALNDGATCAMEWN-CA 176
Cdd:smart00174  80 DSPASFEnvkekwypEVKHFCP-----------NVPIILVGTKLDlrndkSTLEElskkkqepVTYEQGQALAKRIGaVK 148
                          170
                   ....*....|....*...
gi 4757772     177 FMEISAKTDVNVQELFHM 194
Cdd:smart00174 149 YLECSALTQEGVREVFEE 166
Wrch_1 cd04130
Wnt-1 responsive Cdc42 homolog (Wrch-1) is a Rho family GTPase similar to Cdc42; Wrch-1 (Wnt-1 ...
49-192 5.74e-05

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: 42.39  E-value: 5.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   49 GKSTLLHKWASGNFRHEYLPTIENTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEELK 128
Cdd:cd04130  12 GKTSLIVSYTTNGYPTEYVPTAFDNFSVVVLVDGKPVRLQLCDTAGQDEFDKLRPLCYPDTDVFLLCFSVVNPSSFQNIS 91
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4757772  129 AFYelICKIKGNNlHKFPIVLVGNKSD-----------DTHRE--VALNDGATCAMEWN-CAFMEISAKTDVNVQELF 192
Cdd:cd04130  92 EKW--IPEIRKHN-PKAPIILVGTQADlrtdvnvliqlARYGEkpVSQSRAKALAEKIGaCEYIECSALTQKNLKEVF 166
Rab27A cd04127
Rab GTPase family 27a (Rab27a); The Rab27a subfamily consists of Rab27a and its highly ...
50-197 8.20e-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: 39.02  E-value: 8.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   50 KSTLLHKWASGNFRHEYLPTIENTYCQ------------LLGCSHGVLsLHITDSKSGDGNRALQRHVIARGHAFVLVYS 117
Cdd:cd04127  17 KTTFLYRYTDNKFNPKFITTVGIDFREkrvvynsqgpdgTSGKAFRVH-LQLWDTAGQERFRSLTTAFFRDAMGFLLMFD 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  118 VTKKETLEELKAFYELICKikgnnlHKF----PIVLVGNKSD-DTHREVALNDGATCAMEWNCAFMEISAKTDVNVQELF 192
Cdd:cd04127  96 LTSEQSFLNVRNWMSQLQA------HAYcenpDIVLIGNKADlPDQREVSERQARELADKYGIPYFETSAATGQNVEKAV 169

                ....*
gi 4757772  193 HMLLN 197
Cdd:cd04127 170 ETLLD 174
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
50-197 9.89e-04

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: 38.51  E-value: 9.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772     50 KSTLLHKWaSGN--FRHEYLPTIENTY----CQLLGCShgvLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTK-KE 122
Cdd:TIGR00231  14 KSTLLNSL-LGNkgSITEYYPGTTRNYvttvIEEDGKT---YKFNLLDTAGQEDYDAIRRLYYPQVERSLRVFDIVIlVL 89
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4757772    123 TLEELKAFYELIckIKGNNLHKFPIVLVGNKSDDTHREVaLNDGATCAMEWN-CAFMEISAKTDVNVQELFHMLLN 197
Cdd:TIGR00231  90 DVEEILEKQTKE--IIHHADSGVPIILVGNKIDLKDADL-KTHVASEFAKLNgEPIIPLSAETGKNIDSAFKIVEA 162
Rnd3_RhoE_Rho8 cd04172
Rnd3/RhoE/Rho8 GTPases; Rnd3/RhoE/Rho8 subfamily. Rnd3/RhoE/Rho8 is a member of the novel Rho ...
50-194 1.14e-03

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


Pssm-ID: 206735 [Multi-domain]  Cd Length: 182  Bit Score: 38.50  E-value: 1.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   50 KSTLLHKWASGNFRHEYLPTIENTYCQLLGCSHGVLSLHITDSKSG---DGNRALQrhvIARGHAFVLVYSVTKKETLEe 126
Cdd:cd04172  18 KTALLHVFAKDCFPENYVPTVFENYTASFEIDTQRIELSLWDTSGSpyyDNVRPLS---YPDSDAVLICFDISRPETLD- 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  127 lkafyELICKIKGnNLHKF----PIVLVGNKSD-----------DTHRE--VALNDGATCAMEWNCA-FMEISAKTDVN- 187
Cdd:cd04172  94 -----SVLKKWKG-EIQEFcpntKMLLVGCKSDlrtdvstlvelSNHRQtpVSYDQGANMAKQIGAAtYIECSALQSENs 167

                ....*..
gi 4757772  188 VQELFHM 194
Cdd:cd04172 168 VRDIFHV 174
Rho4_like cd04132
Ras homology family 4 (Rho4) of small guanosine triphosphatases (GTPases)-like; Rho4 is a ...
46-229 1.19e-03

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


Pssm-ID: 206704 [Multi-domain]  Cd Length: 197  Bit Score: 38.48  E-value: 1.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   46 AGVGKSTLLHKWASGNFRHEYLPTI-ENTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETL 124
Cdd:cd04132  12 GGCGKTCLLMVYAQGSFPEEYVPTVfENYVTTLQVPNGKIIELALWDTAGQEDYDRLRPLSYPDVDVILICYSVDNPTSL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772  125 E--ELKAFYEL--ICKikgnnlhKFPIVLVGNKSD---DTHREVALN----------DGATCAMEWNC-AFMEISAKTDV 186
Cdd:cd04132  92 DnvEDKWYPEVnhFCP-------GTPIVLVGLKTDlrkDKNSVSKLRaqglepvtpeQGESVAKSIGAvAYIECSAKLME 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 4757772  187 NVQELFHMLLN--YKKKpttGLQEPEKKSQmpnttekllDKCIIM 229
Cdd:cd04132 165 NVDEVFDAAINvaLSKS---GRAARKKKKK---------KKCVIL 197
PTZ00132 PTZ00132
GTP-binding nuclear protein Ran; Provisional
49-196 1.96e-03

GTP-binding nuclear protein Ran; Provisional


Pssm-ID: 240284 [Multi-domain]  Cd Length: 215  Bit Score: 38.14  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772    49 GKSTLLHKWASGNFRHEYLPTIENTYCQL-LGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEEL 127
Cdd:PTZ00132  21 GKTTFVKRHLTGEFEKKYIPTLGVEVHPLkFYTNCGPICFNVWDTAGQEKFGGLRDGYYIKGQCAIIMFDVTSRITYKNV 100
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4757772   128 KAFYELICKIKGNnlhkFPIVLVGNKSDDTHREVALNDgATCAMEWNCAFMEISAKTDVNVQELFHMLL 196
Cdd:PTZ00132 101 PNWHRDIVRVCEN----IPIVLVGNKVDVKDRQVKARQ-ITFHRKKNLQYYDISAKSNYNFEKPFLWLA 164
Rab15 cd04117
Rab GTPase family 15 (Rab15); Rab15 colocalizes with the transferrin receptor in early ...
50-192 6.13e-03

Rab GTPase family 15 (Rab15); Rab15 colocalizes with the transferrin receptor in early endosome compartments, but not with late endosomal markers. It codistributes with Rab4 and Rab5 on early/sorting endosomes, and with Rab11 on pericentriolar recycling endosomes. It is believed to function as an inhibitory GTPase that regulates distinct steps in early endocytic trafficking. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206698 [Multi-domain]  Cd Length: 164  Bit Score: 36.11  E-value: 6.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   50 KSTLLHKWASGNFRHEYLPTIENTYCQLLGCSHGV-LSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEELK 128
Cdd:cd04117  13 KTCLLCRFTDNEFHSSHISTIGVDFKMKTIEVDGIkVRIQIWDTAGQERYQTITKQYYRRAQGIFLVYDISSERSYQHIM 92
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4757772  129 AFYELICKIKGNNLHKfpiVLVGNKSDDTH-REVALNDGATCAMEWNCAFMEISAKTDVNVQELF 192
Cdd:cd04117  93 KWVSDVDEYAPEGVQK---ILIGNKADEEQkRQVGDEQGNKLAKEYGMDFFETSACTNKNIKESF 154
Rho2 cd04129
Ras homology family 2 (Rho2) of small guanosine triphosphatases (GTPases); Rho2 is a fungal ...
50-192 8.72e-03

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: 35.96  E-value: 8.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757772   50 KSTLLHKWASGNFRHEYLPTI-EN--TYCQLLGCShgvLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEE 126
Cdd:cd04129  14 KTSLLYVFTLGEFPEEYHPTVfENyvTDCRVDGKP---VQLALWDTAGQEEYERLRPLSYSKAHVILIGFAIDTPDSLEN 90
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4757772  127 LKA-FYELICKIKGNnlhkFPIVLVGNKSD-----------DTHREVALNDGATCAMEWNC-AFMEISAKTDVNVQELF 192
Cdd:cd04129  91 VRTkWIEEVRRYCPN----VPVILVGLKKDlrqeavakgnyATDEFVPIQQAKLVARAIGAkKYMECSALTGEGVDDVF 165
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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