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Conserved domains on  [gi|194363764|ref|NP_001123915.1|]
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GTPase HRas isoform 1

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List of domain hits

Name Accession Description Interval E-value
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, ...
3-164 5.79e-115

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  Cd Length: 162  Bit Score: 326.68  E-value: 5.79e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764   3 EYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVF 82
Cdd:cd04138    1 EYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  83 AINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVRE 162
Cdd:cd04138   81 AINSRKSFEDIHTYREQIKRVKDSDDVPMVLVGNKCDLAARTVSSRQGQDLAKSYGIPYIETSAKTRQGVEEAFYTLVRE 160

                 ..
gi 194363764 163 IR 164
Cdd:cd04138  161 IR 162
PTZ00369 PTZ00369
Ras-like protein; Provisional
1-184 4.02e-83

Ras-like protein; Provisional


:

Pssm-ID: 240385 [Multi-domain]  Cd Length: 189  Bit Score: 246.70  E-value: 4.02e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764   1 MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLC 80
Cdd:PTZ00369   3 STEYKLVVVGGGGVGKSALTIQFIQNHFIDEYDPTIEDSYRKQCVIDEETCLLDILDTAGQEEYSAMRDQYMRTGQGFLC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  81 VFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDL-AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTL 159
Cdd:PTZ00369  83 VYSITSRSSFEEIASFREQILRVKDKDRVPMILVGNKCDLdSERQVSTGEGQELAKSFGIPFLETSAKQRVNVDEAFYEL 162
                        170       180
                 ....*....|....*....|....*
gi 194363764 160 VREIRQHkLRKLNPPDESGPGCMSC 184
Cdd:PTZ00369 163 VREIRKY-LKEDMPSQKQKKKGGLC 186
 
Name Accession Description Interval E-value
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, ...
3-164 5.79e-115

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  Cd Length: 162  Bit Score: 326.68  E-value: 5.79e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764   3 EYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVF 82
Cdd:cd04138    1 EYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  83 AINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVRE 162
Cdd:cd04138   81 AINSRKSFEDIHTYREQIKRVKDSDDVPMVLVGNKCDLAARTVSSRQGQDLAKSYGIPYIETSAKTRQGVEEAFYTLVRE 160

                 ..
gi 194363764 163 IR 164
Cdd:cd04138  161 IR 162
RAS smart00173
Ras subfamily of RAS small GTPases; Similar in fold and function to the bacterial EF-Tu GTPase. ...
16-166 1.04e-101

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  Cd Length: 164  Bit Score: 292.92  E-value: 1.04e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764    16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQ 95
Cdd:smart00173  13 KSALTIQFIQGHFVDDYDPTIEDSYRKQIEIDGEVCLLDILDTAGQEEFSAMRDQYMRTGEGFLLVYSITDRQSFEEIKK 92
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194363764    96 YREQIKRVKDSDDVPMVLVGNKCDLAA-RTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQH 166
Cdd:smart00173  93 FREQILRVKDRDDVPIVLVGNKCDLESeRVVSTEEGKELARQWGCPFLETSAKERVNVDEAFYDLVREIRKK 164
Miro pfam08477
Miro-like protein; Mitochondrial Rho proteins (Miro-1 and Miro-2), are atypical Rho GTPases. ...
16-119 8.88e-13

Miro-like protein; Mitochondrial Rho proteins (Miro-1 and Miro-2), are atypical Rho GTPases. They have a unique domain organisation, 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: 254820  Cd Length: 118  Bit Score: 61.29  E-value: 8.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764   16 KSALTIQLIQNHFVDE-YDPTIEDSYRKQ-VVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDI 93
Cdd:pfam08477  12 KSSLLSQLVGGEFPPEiPEEIQGDTLAVDtLEVDGDTELLHIWDFGGREELKFEHIIFMKTADAILLVYDLTDRESLNRV 91
                          90       100
                  ....*....|....*....|....*..
gi 194363764   94 HQYREQIKRVKDSD-DVPMVLVGNKCD 119
Cdd:pfam08477  92 SRLIAWLPHLRKLGkKIPVILVGNKFD 118
PLN03071 PLN03071
GTP-binding nuclear protein Ran; Provisional
4-163 9.08e-13

GTP-binding nuclear protein Ran; Provisional


Pssm-ID: 178620  Cd Length: 219  Bit Score: 62.85  E-value: 9.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764   4 YKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIE-DSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVF 82
Cdd:PLN03071  14 FKLVIVGDGGTGKTTFVKRHLTGEFEKKYEPTIGvEVHPLDFFTNCGKIRFYCWDTAGQEKFGGLRDGYYIHGQCAIIMF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  83 AINNTKSFEDIHQYREQIKRVkdSDDVPMVLVGNKCDLAARTVESRQAQdLARSYGIPYIETSAKTRQGVEDAFYTLVRE 162
Cdd:PLN03071  94 DVTARLTYKNVPTWHRDLCRV--CENIPIVLCGNKVDVKNRQVKAKQVT-FHRKKNLQYYEISAKSNYNFEKPFLYLARK 170

                 .
gi 194363764 163 I 163
Cdd:PLN03071 171 L 171
COG2229 COG2229
Predicted GTPase [General function prediction only]
1-159 7.56e-06

Predicted GTPase [General function prediction only]


Pssm-ID: 225138  Cd Length: 187  Bit Score: 43.22  E-value: 7.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764   1 MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYR----KQVVIDGETCLLD------ILDTAGQEEYSAMRDQ 70
Cdd:COG2229    8 MIETKIVVIGPVGAGKTTFVRALSDKPLVITEADASSVSGKgkrpTTVAMDFGSIELDedtgvhLFGTPGQERFKFMWEI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  71 YMRTGEGFLCVFAINNTKSFEDihqyREQIKRVKDSDDVPMVLVGNKCDLA-ARTVES-RQAQDLARSyGIPYIETSAKT 148
Cdd:COG2229   88 LSRGAVGAIVLVDSSRPITFHA----EEIIDFLTSRNPIPVVVAINKQDLFdALPPEKiREALKLELL-SVPVIEIDATE 162
                        170
                 ....*....|.
gi 194363764 149 RQGVEDAFYTL 159
Cdd:COG2229  163 GEGARDQLDVL 173
PTZ00369 PTZ00369
Ras-like protein; Provisional
1-184 4.02e-83

Ras-like protein; Provisional


Pssm-ID: 240385 [Multi-domain]  Cd Length: 189  Bit Score: 246.70  E-value: 4.02e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764   1 MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLC 80
Cdd:PTZ00369   3 STEYKLVVVGGGGVGKSALTIQFIQNHFIDEYDPTIEDSYRKQCVIDEETCLLDILDTAGQEEYSAMRDQYMRTGQGFLC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  81 VFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDL-AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTL 159
Cdd:PTZ00369  83 VYSITSRSSFEEIASFREQILRVKDKDRVPMILVGNKCDLdSERQVSTGEGQELAKSFGIPFLETSAKQRVNVDEAFYEL 162
                        170       180
                 ....*....|....*....|....*
gi 194363764 160 VREIRQHkLRKLNPPDESGPGCMSC 184
Cdd:PTZ00369 163 VREIRKY-LKEDMPSQKQKKKGGLC 186
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
16-165 7.47e-78

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: 249560 [Multi-domain]  Cd Length: 162  Bit Score: 232.40  E-value: 7.47e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764   16 KSALTIQLIQNHFVDEYDPTI-EDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:pfam00071  12 KSSLLIRFTQNKFPEEYIPTIgVDFYTKTIEVDGKTVKLQIWDTAGQERFRALRPLYYRGAQGFLLVYDITSRDSFENVK 91
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194363764   95 QYREQIKRVKDsDDVPMVLVGNKCDLAA-RTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQ 165
Cdd:pfam00071  92 KWLEEILRHAD-DNVPIVLVGNKCDLEDqRVVSTEEGEALAKELGLPFMETSAKTNENVEEAFEELAREILK 162
GTP-binding_protein_placental_isoform TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
16-161 3.26e-46

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: 151.37  E-value: 3.26e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764   16 KSALTIQLIQNH-FVDEYDPTIEDSYRKQVV-IDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINN-TKSFED 92
Cdd:TIGR00231  14 KSTLLNSLLGNKgSITEYYPGTTRNYVTTVIeEDGKTYKFNLLDTAGQEDYDAIRRLYYPQVERSLRVFDIVIlVLDVEE 93
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764   93 IHQ-YREQIKRVKDSdDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVR 161
Cdd:TIGR00231  94 ILEkQTKEIIHHADS-GVPIILVGNKIDLKDADLKTHVASEFAKLNGEPIIPLSAETGKNIDSAFKIVEA 162
COG1100 COG1100
GTPase SAR1 and related small G proteins [General function prediction only]
16-165 1.61e-25

GTPase SAR1 and related small G proteins [General function prediction only]


Pssm-ID: 224025 [Multi-domain]  Cd Length: 219  Bit Score: 98.88  E-value: 1.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYRKQ-VVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:COG1100   18 KTTLLNRLVGDEFPEGYPPTIGNLDPAKtIEPYRRNIKLQLWDTAGQEEYRSLRPEYYRGANGILIVYDSTLRESSDELT 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  95 QYREQIKRVKDSDDVPMVLVGNKCDLAARTVESR----------------QAQDLARSYGIPYIETSAK--TRQGVEDAF 156
Cdd:COG1100   98 EEWLEELRELAPDDVPILLVGNKIDLFDEQSSSEeilnqlnrevvllvlaPKAVLPEVANPALLETSAKslTGPNVNELF 177

                 ....*....
gi 194363764 157 YTLVREIRQ 165
Cdd:COG1100  178 KELLRKLLE 186
PLN03108 PLN03108
Rab family protein; Provisional
16-165 4.45e-23

Rab family protein; Provisional


Pssm-ID: 178655 [Multi-domain]  Cd Length: 210  Bit Score: 91.93  E-value: 4.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSY-RKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:PLN03108  19 KSCLLLQFTDKRFQPVHDLTIGVEFgARMITIDNKPIKLQIWDTAGQESFRSITRSYYRGAAGALLVYDITRRETFNHLA 98
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194363764  95 QYREQIKRVKDSdDVPMVLVGNKCDLA-ARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQ 165
Cdd:PLN03108  99 SWLEDARQHANA-NMTIMLIGNKCDLAhRRAVSTEEGEQFAKEHGLIFMEASAKTAQNVEEAFIKTAAKIYK 169
RAN smart00176
Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases; Ran is involved in the ...
53-163 4.23e-13

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: 63.49  E-value: 4.23e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764    53 LDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVkdSDDVPMVLVGNKCDLAARTVESRQAQd 132
Cdd:smart00176  46 FNVWDTAGQEKFGGLRDGYYIQGQCAIIMFDVTARVTYKNVPNWHRDLVRV--CENIPIVLCGNKVDVKDRKVKAKSIT- 122
                           90       100       110
                   ....*....|....*....|....*....|.
gi 194363764   133 LARSYGIPYIETSAKTRQGVEDAFYTLVREI 163
Cdd:smart00176 123 FHRKKNLQYYDISAKSNYNFEKPFLWLARKL 153
PRK00098 PRK00098
GTPase RsgA; Reviewed
108-154 3.51e-05

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 41.73  E-value: 3.51e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 194363764 108 DVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVED 154
Cdd:PRK00098 111 GIKPIIVLNKIDLLDDLEEARELLALYRAIGYDVLELSAKEGEGLDE 157
 
Name Accession Description Interval E-value
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, ...
3-164 5.79e-115

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  Cd Length: 162  Bit Score: 326.68  E-value: 5.79e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764   3 EYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVF 82
Cdd:cd04138    1 EYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  83 AINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVRE 162
Cdd:cd04138   81 AINSRKSFEDIHTYREQIKRVKDSDDVPMVLVGNKCDLAARTVSSRQGQDLAKSYGIPYIETSAKTRQGVEEAFYTLVRE 160

                 ..
gi 194363764 163 IR 164
Cdd:cd04138  161 IR 162
RAS smart00173
Ras subfamily of RAS small GTPases; Similar in fold and function to the bacterial EF-Tu GTPase. ...
16-166 1.04e-101

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  Cd Length: 164  Bit Score: 292.92  E-value: 1.04e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764    16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQ 95
Cdd:smart00173  13 KSALTIQFIQGHFVDDYDPTIEDSYRKQIEIDGEVCLLDILDTAGQEEFSAMRDQYMRTGEGFLLVYSITDRQSFEEIKK 92
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194363764    96 YREQIKRVKDSDDVPMVLVGNKCDLAA-RTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQH 166
Cdd:smart00173  93 FREQILRVKDRDDVPIVLVGNKCDLESeRVVSTEEGKELARQWGCPFLETSAKERVNVDEAFYDLVREIRKK 164
small_GTPase smart00010
Small GTPase of the Ras superfamily; ill-defined subfamily; SMART predicts Ras-like small ...
16-166 1.81e-101

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  Cd Length: 166  Bit Score: 292.54  E-value: 1.81e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764    16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQ 95
Cdd:smart00010  15 KSALTIQFVQGHFVDEYDPTIEDSYRKQIEIDGEVCLLDILDTAGQEEFSAMRDQYMRTGEGFLLVYSITDRQSFEEIAK 94
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194363764    96 YREQIKRVKDSDDVPMVLVGNKCDLAA-RTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQH 166
Cdd:smart00010  95 FREQILRVKDRDDVPIVLVGNKCDLENeRVVSTEEGKELARQWGCPFLETSAKERINVDEAFYDLVREIRKS 166
Ras cd00876
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ...
16-163 1.44e-86

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  Cd Length: 160  Bit Score: 254.37  E-value: 1.44e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQ 95
Cdd:cd00876   12 KSALTIRFVSGEFVEEYDPTIEDSYRKQIVVDGETYTLDILDTAGQEEFSAMRDQYIRNGDGFILVYSITSRESFEEIKN 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194363764  96 YREQIKRVKDSDDVPMVLVGNKCDLAA-RTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREI 163
Cdd:cd00876   92 IREQILRVKDKEDVPIVLVGNKCDLENeRQVSTEEGEALAEEWGCPFLETSAKTNINIDELFNTLVREI 160
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, ...
16-164 1.10e-77

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  Cd Length: 164  Bit Score: 231.91  E-value: 1.10e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQ 95
Cdd:cd04145   15 KSALTIQFIQSYFVTDYDPTIEDSYTKQCEIDGQWAILDILDTAGQEEFSAMREQYMRTGEGFLLVFSVTDRGSFEEVDK 94
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  96 YREQIKRVKDSDDVPMVLVGNKCDL-AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIR 164
Cdd:cd04145   95 FHTQILRVKDRDEFPMILVGNKADLeHQRKVSREEGQELARKLKIPYIETSAKDRLNVDKAFHDLVRVIR 164
RalA_RalB cd04139
Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily ...
16-165 2.12e-76

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  Cd Length: 163  Bit Score: 228.85  E-value: 2.12e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQ 95
Cdd:cd04139   13 KSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGEEVQLNILDTAGQEDYAAIRDNYFRSGEGFLLVFSITDMESFTALAE 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194363764  96 YREQIKRVKDSDDVPMVLVGNKCDLA-ARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQ 165
Cdd:cd04139   93 FREQILRVKEDDNVPLLLVGNKCDLEdKRQVSVEEAANLAEQWGVNYVETSAKTRANVDKVFFDLVREIRQ 163
Ras2 cd04144
Rat sarcoma (Ras) family 2 of small guanosine triphosphatases (GTPases); The Ras2 subfamily, ...
16-167 2.02e-71

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  Cd Length: 190  Bit Score: 217.02  E-value: 2.02e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQ 95
Cdd:cd04144   12 KTALTIQLCLNHFVETYDPTIEDSYRKQVVVDGQPCMLEVLDTAGQEEYTALRDQWIREGEGFILVYSITSRSTFERVER 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194363764  96 YREQIKRVKDSD--DVPMVLVGNKCD-LAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHK 167
Cdd:cd04144   92 FREQIQRVKDESaaDVPIMIVGNKCDkVYEREVSTEEGAALARRLGCEFIEASAKTNVNVERAFYTLVRALRQQR 166
Rap1 cd04175
Rap1 family GTPase consists of Rap1a and Rap1b isoforms; The Rap1 subgroup is part of the Rap ...
3-163 5.01e-66

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  Cd Length: 164  Bit Score: 202.36  E-value: 5.01e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764   3 EYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVF 82
Cdd:cd04175    1 EYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDGQQCMLEILDTAGTEQFTAMRDLYMKNGQGFVLVY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  83 AINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDL-AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVR 161
Cdd:cd04175   81 SITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDLeDERVVGKEQGQNLARQWGCAFLETSAKAKINVNEIFYDLVR 160

                 ..
gi 194363764 162 EI 163
Cdd:cd04175  161 QI 162
RSR1 cd04177
RSR1/Bud1p family GTPase; RSR1/Bud1p is a member of the Rap subfamily of the Ras family that ...
3-164 1.13e-61

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  Cd Length: 168  Bit Score: 191.16  E-value: 1.13e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764   3 EYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVF 82
Cdd:cd04177    1 DYKIVVLGAGGVGKSALTVQFVQNVFIESYDPTIEDSYRKQVEIDGRQCDLEILDTAGTEQFTAMRELYIKSGQGFLLVY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  83 AINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDL-AARTVESRQAQDLARSYG-IPYIETSAKTRQGVEDAFYTLV 160
Cdd:cd04177   81 SVTSEASLNELGELREQVLRIKDSDNVPMVLVGNKADLeDDRQVSREDGVSLSQQWGnVPFYETSARKRTNVDEVFIDLV 160

                 ....
gi 194363764 161 REIR 164
Cdd:cd04177  161 RQII 164
Rap_like cd04136
Rap-like family consists of Rap1, Rap2 and RSR1; The Rap subfamily consists of the Rap1, Rap2, ...
3-163 1.10e-60

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  Cd Length: 164  Bit Score: 188.54  E-value: 1.10e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764   3 EYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVF 82
Cdd:cd04136    1 EYKLVVLGSGGVGKSALTVQFVQGIFVDKYDPTIEDSYRKQIEVDCQQCMLEILDTAGTEQFTAMRDLYIKNGQGFALVY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  83 AINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDL-AARTVESRQAQDLARSYG-IPYIETSAKTRQGVEDAFYTLV 160
Cdd:cd04136   81 SITAQQSFNDLQDLREQILRVKDTEDVPMILVGNKCDLeDERVVSKEEGQNLARQWGnCPFLETSAKSKINVDEIFYDLV 160

                 ...
gi 194363764 161 REI 163
Cdd:cd04136  161 RQI 163
Rit_Rin_Ric cd04141
Ras-like protein in all tissues (Rit), Ras-like protein in neurons (Rin) and Ras-related ...
3-170 1.26e-57

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  Cd Length: 172  Bit Score: 181.21  E-value: 1.26e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764   3 EYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVF 82
Cdd:cd04141    2 EYKIVMLGAGGVGKSAVTMQFISHSFPDYHDPTIEDAYKTQARIDNEPALLDILDTAGQAEFTAMRDQYMRCGEGFIICY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  83 AINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAA-RTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVR 161
Cdd:cd04141   82 SVTDRHSFQEASEFKELITRVRLTEDIPLVLVGNKVDLEQqRQVTTEEGRNLAREFNCPFFETSAALRFYIDDAFHGLVR 161

                 ....*....
gi 194363764 162 EIRQHKLRK 170
Cdd:cd04141  162 EIRRKESMP 170
Rap2 cd04176
Rap2 family GTPase consists of Rap2a, Rap2b, and Rap2c; The Rap2 subgroup is part of the Rap ...
3-163 1.76e-57

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  Cd Length: 163  Bit Score: 180.42  E-value: 1.76e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764   3 EYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVF 82
Cdd:cd04176    1 EYKVVVLGSGGVGKSALTVQFVSGTFIEKYDPTIEDFYRKEIEVDSSPSVLEILDTAGTEQFASMRDLYIKNGQGFIVVY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  83 AINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAA-RTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVR 161
Cdd:cd04176   81 SLVNQQTFQDIKPMRDQIVRVKGYEKVPIILVGNKVDLESeREVSSAEGRALAEEWGCPFMETSAKSKTMVNELFAEIVR 160

                 ..
gi 194363764 162 EI 163
Cdd:cd04176  161 QM 162
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
16-161 4.33e-47

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  Cd Length: 159  Bit Score: 153.38  E-value: 4.33e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTI-EDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:cd00154   13 KTSLLLRFVDNKFSENYKSTIgVDFKSKTIEVDGKKVKLQIWDTAGQERFRSITSSYYRGAHGAILVYDVTNRESFENLD 92
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194363764  95 QYREQIKRvKDSDDVPMVLVGNKCDLAA-RTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVR 161
Cdd:cd00154   93 KWLNELKE-YAPPNIPIILVGNKSDLEDeRQVSTEEAQQFAKENGLLFFETSAKTGENVDEAFESLAR 159
RheB cd04137
Ras Homolog Enriched in Brain (RheB) is a small GTPase; Rheb (Ras Homolog Enriched in Brain) ...
16-183 1.71e-44

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  Cd Length: 180  Bit Score: 147.39  E-value: 1.71e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQ 95
Cdd:cd04137   14 KSSLTVQFVEGHFVESYYPTIENTFSKIITYKGQEYHLEIVDTAGQDEYSILPQKYSIGIHGYILVYSVTSRKSFEVVKV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  96 YREQIKRVKDSDDVPMVLVGNKCDL-AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIrqHKLRKLNPP 174
Cdd:cd04137   94 IYDKILDMLGKESVPIVLVGNKSDLhMERQVSAEEGKKLAESWGAAFLESSAKENENVEEAFELLIEEI--EKVENPLPP 171

                 ....*....
gi 194363764 175 DESGPGCMS 183
Cdd:cd04137  172 GQKSKCSVM 180
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
16-163 9.75e-41

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


Pssm-ID: 197555  Cd Length: 164  Bit Score: 137.25  E-value: 9.75e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764    16 KSALTIQLIQNHFVDEYDPTIEDSYR-KQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:smart00175  13 KSSLLSRFTDGKFSEQYKSTIGVDFKtKTIEVDGKRVKLQIWDTAGQERFRSITSSYYRGAVGALLVYDITNRESFENLE 92
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764    95 QYREQIkRVKDSDDVPMVLVGNKCDLAA-RTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREI 163
Cdd:smart00175  93 NWLKEL-REYASPNVVIMLVGNKSDLEEqRQVSREEAEAFAEEHGLPFFETSAKTNTNVEEAFEELAREI 161
RERG_RasL11_like cd04146
Ras-related and Estrogen-Regulated Growth inhibitor (RERG) and Ras-like 11 (RasL11)-like ...
16-165 1.95e-37

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  Cd Length: 166  Bit Score: 128.93  E-value: 1.95e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSA--MRDQYMRTGEGFLCVFAINNTKSFEDI 93
Cdd:cd04146   12 KSALTVRFLTKRFIGEYEPNLESLYSRQVTIDGEQVSLEIQDTPGQQQNEDpeSLERSLRWADGFVLVYSITDRSSFDVV 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194363764  94 HQYREQIKRVKDSD-DVPMVLVGNKCDLA-ARTVESRQAQDLARSYGIPYIETSA-KTRQGVEDAFYTLVREIRQ 165
Cdd:cd04146   92 SQLLQLIREIKKRDgEIPVILVGNKADLLhSRQVSTEEGQKLALELGCLFFEVSAaENYLEVQNVFHELCREVRR 166
Rab8_Rab10_Rab13_like cd01867
Rab GTPase families 8, 10, 13 (Rab8, Rab10, Rab13); Rab8/Sec4/Ypt2 are known or suspected to ...
16-165 3.24e-33

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  Cd Length: 167  Bit Score: 117.75  E-value: 3.24e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYR-KQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:cd01867   16 KSCLLLRFSEDSFNPSFISTIGIDFKiRTIELDGKKIKLQIWDTAGQERFRTITTSYYRGAMGIILVYDITDEKSFENIK 95
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194363764  95 QYREQIKRVKdSDDVPMVLVGNKCDLAA-RTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQ 165
Cdd:cd01867   96 NWMRNIDEHA-SEDVERMLVGNKCDMEEkRVVSKEEGEALAREYGIKFLETSAKANINVEEAFLTLAKDILK 166
Rab1_Ypt1 cd01869
Rab GTPase family 1 includes the yeast homolog Ypt1; Rab1/Ypt1 subfamily. Rab1 is found in ...
16-164 8.21e-33

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: 116.66  E-value: 8.21e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYR-KQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:cd01869   15 KSCLLLRFADDTYTESYISTIGVDFKiRTIELDGKTVKLQIWDTAGQERFRTITSSYYRGAHGIIIVYDVTDQESFNNVK 94
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194363764  95 QYREQIKRVKdSDDVPMVLVGNKCDLA-ARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIR 164
Cdd:cd01869   95 QWLQEIDRYA-SENVNKLLVGNKCDLTdKKVVDYTEAKEFADELGIPFLETSAKNATNVEEAFMTMAREIK 164
Rab18 cd01863
Rab GTPase family 18 (Rab18); Rab18 subfamily. Mammalian Rab18 is implicated in endocytic ...
16-163 4.93e-32

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  Cd Length: 161  Bit Score: 114.72  E-value: 4.93e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYR-KQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:cd01863   13 KSSLLLRFTDDTFDEDLSSTIGVDFKvKTVTVDGKKVKLAIWDTAGQERFRTLTSSYYRGAQGVILVYDVTRRDTFDNLD 92
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194363764  95 QYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREI 163
Cdd:cd01863   93 TWLNELDTYSTNPDAVKMLVGNKIDKENREVTREEGQKFARKHNMLFIETSAKTRIGVQQAFEELVEKI 161
Rhes_like cd04143
Ras homolog enriched in striatum (Rhes) and activator of G-protein signaling 1 (Dexras1/AGS1); ...
16-179 1.52e-31

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: 115.62  E-value: 1.52e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQ 95
Cdd:cd04143   13 KTAIVSRFLGGRFEEQYTPTIEDFHRKLYSIRGEVYQLDILDTSGNHPFPAMRRLSILTGDVFILVFSLDNRESFEEVCR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  96 YREQI--------KRVKDSDDVPMVLVGNKCDL-AARTVESRQA-QDLARSYGIPYIETSAKTRQGVEDAFYTLVreirq 165
Cdd:cd04143   93 LREQIletksclkNKTKENVKIPMVICGNKADRdFPREVQRDEVeQLVGGDENCAYFEVSAKKNSNLDEMFRALF----- 167
                        170
                 ....*....|....
gi 194363764 166 hKLRKLnpPDESGP 179
Cdd:cd04143  168 -SLAKL--PNEMSP 178
Rab21 cd04123
Rab GTPase family 21 (Rab21); The localization and function of Rab21 are not clearly defined, ...
16-163 3.05e-30

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  Cd Length: 162  Bit Score: 110.01  E-value: 3.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDS-YRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:cd04123   13 KTSLVLRYVENKFNEKHESTTQASfFQKTVNIGGKRIDLAIWDTAGQERYHALGPIYYRDADGAILVYDITDADSFQKVK 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  95 QYREQIKRVKdSDDVPMVLVGNKCDL-AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREI 163
Cdd:cd04123   93 KWIKELKQMR-GNNISLVIVGNKIDLeRQRVVSKSEAEEYAKSVGAKHFETSAKTGKGIEELFLSLAKRM 161
Rab11_like cd01868
Rab GTPase family 11 (Rab11)-like includes Rab11a, Rab11b, and Rab25; Rab11a, Rab11b, and ...
16-163 3.36e-30

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  Cd Length: 165  Bit Score: 109.96  E-value: 3.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTI--EDSYRkQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDI 93
Cdd:cd01868   16 KSNLLSRFTRNEFNLDSKSTIgvEFATR-TIQIDGKTIKAQIWDTAGQERYRAITSAYYRGAVGALLVYDITKKSTFENV 94
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194363764  94 HQYREQIKRVKDSdDVPMVLVGNKCDLAA-RTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREI 163
Cdd:cd01868   95 ERWLKELRDHADS-NIVIMLVGNKSDLRHlRAVPTEEAKAFAEKNGLSFIETSALDGTNVEEAFKQLLTEI 164
Rho cd00157
Ras homology family (Rho) of small guanosine triphosphatases (GTPases); Members of the Rho ...
16-161 6.88e-30

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  Cd Length: 171  Bit Score: 109.17  E-value: 6.88e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRD-QYMRTgEGFLCVFAINNTKSFEDI- 93
Cdd:cd00157   13 KTCLLISYTTNKFPTEYVPTVFDNYSANVTVDGKQVNLGLWDTAGQEEYDRLRPlSYPQT-DVFLLCFSVDSPSSFENVk 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  94 HQYREQIKrvKDSDDVPMVLVGNKCDL------------AARTVESRQAQDLARSYG-IPYIETSAKTRQGVEDAFYTLV 160
Cdd:cd00157   92 TKWYPEIK--HYCPNVPIILVGTKIDLrddgntlkklekKQKPITPEEGEKLAKEIGaVKYMECSALTQEGLKEVFDEAI 169

                 .
gi 194363764 161 R 161
Cdd:cd00157  170 R 170
Rab5_related cd01860
Rab-related GTPase family includes Rab5 and Rab22; regulates early endosome fusion; The ...
16-163 1.04e-29

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  Cd Length: 163  Bit Score: 108.41  E-value: 1.04e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSY-RKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:cd01860   14 KSSIVLRFVKNEFSENQESTIGAAFlTQTVNLDDTTVKFEIWDTAGQERYRSLAPMYYRGAAAAIVVYDITSEESFEKAK 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  95 QYREQIKRVKDSDDVpMVLVGNKCDLAA-RTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREI 163
Cdd:cd01860   94 SWVKELQEHGPPNIV-IALAGNKADLESkRQVSTEEAQEYADENGLLFMETSAKTGENVNELFTEIARKL 162
Rab7 cd01862
Rab GTPase family 7 (Rab7); Rab7 subfamily. Rab7 is a small Rab GTPase that regulates ...
16-161 3.14e-29

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  Cd Length: 172  Bit Score: 107.37  E-value: 3.14e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTI-EDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:cd01862   13 KTSLMNQYVNKKFSNQYKATIgADFLTKEVTVDDRLVTLQIWDTAGQERFQSLGVAFYRGADCCVLVYDVTNPKSFESLD 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194363764  95 QYREQIK---RVKDSDDVPMVLVGNKCDLAA-RTVESRQAQDLARSYG-IPYIETSAKTRQGVEDAFYTLVR 161
Cdd:cd01862   93 SWRDEFLiqaSPRDPENFPFVVLGNKIDLEEkRQVSTKKAQQWCKSKGnIPYFETSAKEAINVDQAFETIAR 164
ARHI_like cd04140
A Ras homolog member I (ARHI); ARHI (A Ras homolog member I) is a member of the Ras family ...
3-160 3.18e-28

A Ras homolog member I (ARHI); ARHI (A Ras homolog member I) is a member of the Ras family with several unique structural and functional properties. ARHI is expressed in normal human ovarian and breast tissue, but its expression is decreased or eliminated in breast and ovarian cancer. ARHI contains an N-terminal extension of 34 residues (human) that is required to retain its tumor suppressive activity. Unlike most other Ras family members, ARHI is maintained in the constitutively active (GTP-bound) state in resting cells and has modest GTPase activity. ARHI inhibits STAT3 (signal transducers and activators of transcription 3), a latent transcription factor whose abnormal activation plays a critical role in oncogenesis. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206711  Cd Length: 165  Bit Score: 104.91  E-value: 3.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764   3 EYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVF 82
Cdd:cd04140    1 DYRVVVFGAGGVGKSSLVLRFVKGTFRESYIPTIEDTYRQVISCSKSICTLQITDTTGSHQFPAMQRLSISKGHAFILVY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  83 AINNTKSFEDIHQYREQIKRVK--DSDDVPMVLVGNKCD-LAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTL 159
Cdd:cd04140   81 SITSKQSLEELKPIYELICEIKgnNLEKIPIMLVGNKCDeSPSREVSSSEGAALARTWNCAFMETSAKTNHNVQELFQEL 160

                 .
gi 194363764 160 V 160
Cdd:cd04140  161 L 161
Ras_dva cd04147
Ras - dorsal-ventral anterior localization (Ras-dva) family; Ras-dva subfamily. Ras-dva (Ras - ...
16-164 1.30e-27

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: 103.76  E-value: 1.30e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQ 95
Cdd:cd04147   12 KTALIQRFLYDTFEPKHRRTVEELHSKEYEVAGVKVTIDILDTSGSYSFPAMRKLSIQNGDAFALVYSVDDPESFEEVKR 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194363764  96 YREQIKRVKDSDDVPMVLVGNKCD-LAARTVESRQAQDLAR-SYGIPYIETSAKTRQGVEDAFYTLVREIR 164
Cdd:cd04147   92 LREEILEVKEDKFVPIVVVGNKIDsLAERQVEAADALSTVElDWNNGFVEASAKDNENVTEVFKELLQQAN 162
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
16-161 1.52e-27

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: 102.92  E-value: 1.52e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFV---DEYDPTI-EDSYRKQvvIDGETCLLDILDTAGQEEYSAMRD-----QYMRTGEGFLCVFAINN 86
Cdd:cd00882   10 KSSLLNALLGGEVGevsDVPGTTRdPDVYVKE--LDKGKVKLVLVDTPGLDEFGGLGReelarLLLRGADLILLVVDSTD 87
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194363764  87 TKSFEDIhqyREQIKRVKDSDDVPMVLVGNKCDLAARTVESR--QAQDLARSYGIPYIETSAKTRQGVEDAFYTLVR 161
Cdd:cd00882   88 RESEEDA---KLLILRRLRKEGIPIILVGNKIDLLEEREVEEllRLEELAKILGVPVFEVSAKTGEGVDELFEKLIE 161
RGK cd04148
Rem, Rem2, Rad, Gem/Kir (RGK) subfamily of Ras GTPases; RGK subfamily. The RGK (Rem, Rem2, Rad, ...
16-176 1.74e-27

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: 104.02  E-value: 1.74e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQN-HFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:cd04148   13 KSSLANIFTAGvYEDSAYEASGDDTYERTVSVDGEEATLVVYDHWEQEDGMWLEDSCMQVGDAYVIVYSVTDRSSFEKAS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  95 QYREQIKRVKDSDDVPMVLVGNKCDLA-ARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRqhklrkLNP 173
Cdd:cd04148   93 ELRIQLRRARQAEDIPIILVGNKSDLVrSREVSVQEGRACAVVFDCKFIETSAALQHNVDELFEGIVRQVR------LRR 166

                 ...
gi 194363764 174 PDE 176
Cdd:cd04148  167 DSK 169
Rab6 cd01861
Rab GTPase family 6 (Rab6); Rab6 is involved in microtubule-dependent transport pathways ...
16-156 2.07e-26

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  Cd Length: 161  Bit Score: 99.62  E-value: 2.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTI-EDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:cd01861   13 KTSIITRFMYDTFDNQYQATIgIDFLSKTMYVDDKTVRLQLWDTAGQERFRSLIPSYIRDSSVAVVVYDITNRQSFDNTD 92
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194363764  95 QYreqIKRVKD--SDDVPMVLVGNKCDLA-ARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAF 156
Cdd:cd01861   93 KW---IDDVRDerGNDVIIVLVGNKTDLSdKRQVSTEEGEKKAKENNAMFIETSAKAGHNVKQLF 154
Rab35 cd04110
Rab GTPase family 35 (Rab35); Rab35 is one of several Rab proteins to be found to participate ...
16-177 4.23e-26

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: 99.93  E-value: 4.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYR-KQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:cd04110   19 KSSLLLRFADNTFSGSYITTIGVDFKiRTVEINGERVKLQIWDTAGQERFRTITSTYYRGTHGVIVVYDVTNGESFVNVK 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  95 QYREQIKrvKDSDDVPMVLVGNKCDLAAR-TVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRklNP 173
Cdd:cd04110   99 RWLQEIE--QNCDDVCKVLVGNKNDDPERkVVETEDAYKFAGQMGISLFETSAKENINVEEMFNCITELVLRAKKD--NL 174

                 ....
gi 194363764 174 PDES 177
Cdd:cd04110  175 AKQQ 178
Rab39 cd04111
Rab GTPase family 39 (Rab39); Found in eukaryotes, Rab39 is mainly found in epithelial cell ...
16-163 6.11e-25

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: 97.14  E-value: 6.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIE-DSYRKQVVI-DGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDI 93
Cdd:cd04111   15 KSSLLKRFTEGRFAEVSDPTVGvDFFSRLIEIePGVRIKLQLWDTAGQERFRSITRSYYRNSVGVLLVFDITNRESFEHV 94
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194363764  94 HQYREQIKR-VKDSDDVpMVLVGNKCDLAA-RTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREI 163
Cdd:cd04111   95 HDWLEEARShIQPHRPV-FILVGHKCDLESqRQVTREEAEKLAKDLGMKYIETSARTGDNVEEAFELLTQEI 165
Rab27A cd04127
Rab GTPase family 27a (Rab27a); The Rab27a subfamily consists of Rab27a and its highly ...
16-160 7.91e-25

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  Cd Length: 180  Bit Score: 96.03  E-value: 7.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYR-KQVVID----------GETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAI 84
Cdd:cd04127   17 KTTFLYRYTDNKFNPKFITTVGIDFReKRVVYNsqgpdgtsgkAFRVHLQLWDTAGQERFRSLTTAFFRDAMGFLLMFDL 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194363764  85 NNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLA-ARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLV 160
Cdd:cd04127   97 TSEQSFLNVRNWMSQLQAHAYCENPDIVLIGNKADLPdQREVSERQARELADKYGIPYFETSAATGQNVEKAVETLL 173
RHO smart00174
Rho (Ras homology) subfamily of Ras-like small GTPases; Members of this subfamily of Ras-like ...
16-161 1.89e-24

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  Cd Length: 174  Bit Score: 94.99  E-value: 1.89e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764    16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRD-QYMRTgEGFLCVFAINNTKSFEDI- 93
Cdd:smart00174  11 KTCLLIVYTTNAFPEDYVPTVFENYSADVEVDGKPVELGLWDTAGQEDYDRLRPlSYPDT-DVFLICFSVDSPASFENVk 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764    94 HQYREQIKrvKDSDDVPMVLVGNKCDLAART-------------VESRQAQDLARSYG-IPYIETSAKTRQGVEDAFYTL 159
Cdd:smart00174  90 EKWYPEVK--HFCPNVPIILVGTKLDLRNDKstleelskkkqepVTYEQGQALAKRIGaVKYLECSALTQEGVREVFEEA 167

                   ..
gi 194363764   160 VR 161
Cdd:smart00174 168 IR 169
Rab9 cd04116
Rab GTPase family 9 (Rab9); Rab9 is found in late endosomes, together with mannose 6-phosphate ...
16-163 1.04e-23

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  Cd Length: 170  Bit Score: 93.01  E-value: 1.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSY-RKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:cd04116   18 KSSLMNRYVTNKFDTQLFHTIGVEFlNKDLEVDGHFVTLQIWDTAGQERFRSLRTPFYRGSDCCLLTFSVDDSQSFQNLS 97
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194363764  95 QYREQI---KRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGI-PYIETSAKTRQGVEDAFYTLVREI 163
Cdd:cd04116   98 NWKKEFiyyADVKEPESFPFVILGNKIDIPERQVSTEEAQAWCRDNGDyPYFETSAKDATNVAAAFEEAVRRV 170
RhoG cd01875
Ras homolog family, member G (RhoG) of small guanosine triphosphatases (GTPases); RhoG is a ...
16-182 3.69e-23

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


Pssm-ID: 133277  Cd Length: 191  Bit Score: 91.99  E-value: 3.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRD-QYMRTGEGFLCvFAINNTKSFEDI- 93
Cdd:cd01875   16 KTCLLICYTTNAFPKEYIPTVFDNYSAQTAVDGRTVSLNLWDTAGQEEYDRLRTlSYPQTNVFIIC-FSIASPSSYENVr 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  94 HQYREQIKRvkDSDDVPMVLVGNKCDLAAR--TVES-----------RQAQDLARSYG-IPYIETSAKTRQGVEDAFYTL 159
Cdd:cd01875   95 HKWHPEVCH--HCPNVPILLVGTKKDLRNDadTLKKlkeqgqapitpQQGGALAKQIHaVKYLECSALNQDGVKEVFAEA 172
                        170       180
                 ....*....|....*....|....
gi 194363764 160 VREIrqhklrkLNP-PDESGPGCM 182
Cdd:cd01875  173 VRAV-------LNPtPIKDTKSCV 189
Rab2 cd01866
Rab GTPase family 2 (Rab2); Rab2 is localized on cis-Golgi membranes and interacts with Golgi ...
16-163 5.39e-23

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  Cd Length: 168  Bit Score: 90.94  E-value: 5.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVV-IDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:cd01866   17 KSCLLLQFTDKRFQPVHDLTIGVEFGARMItIDGKQIKLQIWDTAGQESFRSITRSYYRGAAGALLVYDITRRETFNHLT 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  95 QYREQIkRVKDSDDVPMVLVGNKCDLAA-RTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREI 163
Cdd:cd01866   97 SWLEDA-RQHSNSNMTIMLIGNKCDLESrREVSYEEGEAFAREHGLIFMETSAKTASNVEEAFINTAKEI 165
Rab4 cd04113
Rab GTPase family 4 (Rab4); Rab4 subfamily. Rab4 has been implicated in numerous functions ...
16-163 7.91e-23

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  Cd Length: 161  Bit Score: 90.19  E-value: 7.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVV-IDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:cd04113   13 KSCLLHQFIENKFKQDSNHTIGVEFGSRVVnVGGKSVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYDITSRESFNALT 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  95 QYREQIKRVKdSDDVPMVLVGNKCDL-AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREI 163
Cdd:cd04113   93 NWLTDARTLA-SPDIVIILVGNKKDLeDDREVTFLEASRFAQENGLLFLETSALTGENVEEAFLKCARSI 161
Rab19 cd01864
Rab GTPase family 19 (Rab19); Rab19 subfamily. Rab19 proteins are associated with Golgi stacks. ...
28-163 2.47e-22

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  Cd Length: 165  Bit Score: 89.03  E-value: 2.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  28 FVDEYDPTIE-DSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDS 106
Cdd:cd01864   28 FSERQGNTIGvDFTMKTLEIEGKRVKLQIWDTAGQERFRTITQSYYRSANGAIIAYDITRRSSFESVPHWIEEVEKYGAS 107
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 194363764 107 dDVPMVLVGNKCDLAA-RTVESRQAQDLARSYGIPY-IETSAKTRQGVEDAFYTLVREI 163
Cdd:cd01864  108 -NVVLLLIGNKCDLEEqREVLFEEACTLAEKNGMLAvLETSAKESQNVEEAFLLMATEL 165
Rab33B_Rab33A cd04115
Rab GTPase family 33 includes Rab33A and Rab33B; Rab33B/Rab33A subfamily. Rab33B is ...
16-169 2.56e-22

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


Pssm-ID: 133315  Cd Length: 170  Bit Score: 89.03  E-value: 2.56e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYR-KQVVIDGETCLLDILDTAGQEEY-SAMRDQYMRTGEGFLCVFAINNTKSFEDI 93
Cdd:cd04115   15 KTCLTYRFCAGRFPERTEATIGVDFReRTVEIDGERIKVQLWDTAGQERFrKSMVQHYYRNVHAVVFVYDVTNMASFHSL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  94 HQYREQIKRVKDSDDVPMVLVGNKCDL-AARTVESRQAQDLARSYGIPYIETSAK---TRQGVEDAFYTLVreirqHKLR 169
Cdd:cd04115   95 PSWIEECEQHSLPNEVPRILVGNKCDLrEQIQVPTDLAQRFADAHSMPLFETSAKdpsENDHVEAIFMTLA-----HKLK 169
Rab26 cd04112
Rab GTPase family 26 (Rab26); Rab26 subfamily. First identified in rat pancreatic acinar cells, ...
42-176 2.94e-22

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  Cd Length: 191  Bit Score: 89.54  E-value: 2.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  42 KQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKdSDDVPMVLVGNKCDLA 121
Cdd:cd04112   41 KVVTVDGVKVKLQIWDTAGQERFRSVTHAYYRDAHALLLLYDVTNKSSFDNIRAWLTEILEYA-QSDVVIMLLGNKADMS 119
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 194363764 122 A-RTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIrqhKLRKLNPPDE 176
Cdd:cd04112  120 GeRVVKREDGERLAKEYGVPFMETSAKTGLNVELAFTAVAKEL---KHRSVEQPDE 172
Rop_like cd04133
Rho-related protein from plants (Rop)-like; The Rop (Rho-related protein from plants) ...
16-161 3.39e-21

Rho-related protein from plants (Rop)-like; The Rop (Rho-related protein from plants) subfamily plays a role in diverse cellular processes, including cytoskeletal organization, pollen and vegetative cell growth, hormone responses, stress responses, and pathogen resistance. Rops are able to regulate several downstream pathways to amplify a specific signal by acting as master switches early in the signaling cascade. They transmit a variety of extracellular and intracellular signals. Rops are involved in establishing cell polarity in root-hair development, root-hair elongation, pollen-tube growth, cell-shape formation, responses to hormones such as abscisic acid (ABA) and auxin, responses to abiotic stresses such as oxygen deprivation, and disease resistance and disease susceptibility. An individual Rop can have a unique function or an overlapping function shared with other Rop proteins; in addition, a given Rop-regulated function can be controlled by one or multiple Rop proteins. For example, Rop1, Rop3, and Rop5 are all involved in pollen-tube growth; Rop2 plays a role in response to low-oxygen environments, cell-morphology, and root-hair development; root-hair development is also regulated by Rop4 and Rop6; Rop6 is also responsible for ABA response, and ABA response is also regulated by Rop10. Plants retain some of the regulatory mechanisms that are shared by other members of the Rho family, but have also developed a number of unique modes for regulating Rops. Unique RhoGEFs have been identified that are exclusively active toward Rop proteins, such as those containing the domain PRONE (plant-specific Rop nucleotide exchanger). Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206705  Cd Length: 173  Bit Score: 86.05  E-value: 3.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH- 94
Cdd:cd04133   14 KTCMLISYTSNTFPTDYVPTVFDNFSANVVVDGNTVNLGLWDTAGQEDYNRLRPLSYRGADVFLLAFSLISKASYENVLk 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194363764  95 QYREQIKRVkdSDDVPMVLVGNKCDL-----------AARTVESRQAQDLARSYGIP-YIETSAKTRQGVEDAFYTLVR 161
Cdd:cd04133   94 KWIPELRHY--APGVPIVLVGTKLDLrddkqffadhpGAVPITTAQGEELRKQIGAAaYIECSSKTQQNVKAVFDAAIK 170
RabL4 cd04101
Rab GTPase-like family 4 (Rab-like4); RabL4 (Rab-like4) subfamily. RabL4s are novel proteins ...
43-161 9.25e-21

Rab GTPase-like family 4 (Rab-like4); RabL4 (Rab-like4) subfamily. RabL4s are novel proteins that have high sequence similarity with Rab family members, but display features that are distinct from Rabs, and have been termed Rab-like. As in other Rab-like proteins, RabL4 lacks a prenylation site at the C-terminus. The specific function of RabL4 remains unknown.


Pssm-ID: 206688  Cd Length: 167  Bit Score: 84.89  E-value: 9.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  43 QVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAA 122
Cdd:cd04101   45 PVPDTSDSVELFIFDSAGQELFSDMVENVWEQPAVVCVVYDVTNEVSFNNCSRWINRVRTHSHGLHTPGVLVGNKCDLTD 124
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 194363764 123 RT-VESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVR 161
Cdd:cd04101  125 RReVDAAQAQALAQANTLKFYETSAKEGVGYEAPFLSLAR 164
RJL cd04119
Rab GTPase family J-like (RabJ-like); RJLs are found in many protists and as chimeras with ...
16-163 3.91e-20

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  Cd Length: 168  Bit Score: 83.17  E-value: 3.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYR-KQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:cd04119   13 KSCIIKRYCEGRFVSKYLPTIGIDYGvKKVSVRNKEVRVNFFDLSGHPEYLEVRNEFYKDTQGVLLVYDVTDRQSFEALD 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194363764  95 QYREQIK----RVKDSDDVPMVLVGNKCDL-AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREI 163
Cdd:cd04119   93 SWLKEMKqeggPHGNMENIVVVVCANKIDLtKHRAVSEDEGRLWAESKGFKYFETSACTGEGVNEMFQTLFSSI 166
Rab15 cd04117
Rab GTPase family 15 (Rab15); Rab15 colocalizes with the transferrin receptor in early ...
16-164 6.30e-20

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  Cd Length: 164  Bit Score: 82.33  E-value: 6.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYR-KQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:cd04117   13 KTCLLCRFTDNEFHSSHISTIGVDFKmKTIEVDGIKVRIQIWDTAGQERYQTITKQYYRRAQGIFLVYDISSERSYQHIM 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194363764  95 QYREQIKRVKDsDDVPMVLVGNKCDLA-ARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFyTLVREIR 164
Cdd:cd04117   93 KWVSDVDEYAP-EGVQKILIGNKADEEqKRQVGDEQGNKLAKEYGMDFFETSACTNKNIKESF-TRLTELV 161
Rab28 cd04109
Rab GTPase family 28 (Rab28); Rab28 subfamily. First identified in maize, Rab28 has been shown ...
16-170 1.21e-19

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: 82.54  E-value: 1.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIE-DSYRKQVVIDGE-TCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDI 93
Cdd:cd04109   13 KTSLIRRFAQEGFGKSYKQTIGlDFFSRRITLPGSlNVTLQVWDIGGQQIGGKMLDKYIYGAQAVCLVYDITNSQSFENL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  94 HQYREQIKRV-KDSDDVP-MVLVGNKCDLAA-RTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRK 170
Cdd:cd04109   93 EDWLSVVKKVnEESETKPkMVLVGNKTDLEHnRQVTAEKHARFAQENDMESIFVSAKTGDRVFLCFQRIAAELLGVKLSQ 172
Wrch_1 cd04130
Wnt-1 responsive Cdc42 homolog (Wrch-1) is a Rho family GTPase similar to Cdc42; Wrch-1 (Wnt-1 ...
16-156 1.53e-19

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  Cd Length: 173  Bit Score: 81.68  E-value: 1.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDI-H 94
Cdd:cd04130   13 KTSLIVSYTTNGYPTEYVPTAFDNFSVVVLVDGKPVRLQLCDTAGQDEFDKLRPLCYPDTDVFLLCFSVVNPSSFQNIsE 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194363764  95 QYREQIKrvKDSDDVPMVLVGNKCDL-------------AARTVESRQAQDLARSYG-IPYIETSAKTRQGVEDAF 156
Cdd:cd04130   93 KWIPEIR--KHNPKAPIILVGTQADLrtdvnvliqlaryGEKPVSQSRAKALAEKIGaCEYIECSALTQKNLKEVF 166
Rho2 cd04129
Ras homology family 2 (Rho2) of small guanosine triphosphatases (GTPases); Rho2 is a fungal ...
27-161 5.27e-19

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: 80.26  E-value: 5.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  27 HFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQ-YREQIKRVkd 105
Cdd:cd04129   25 EFPEEYHPTVFENYVTDCRVDGKPVQLALWDTAGQEEYERLRPLSYSKAHVILIGFAIDTPDSLENVRTkWIEEVRRY-- 102
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194363764 106 SDDVPMVLVGNKCDL-----------AARTVESRQAQDLARSYGI-PYIETSAKTRQGVEDAFYTLVR 161
Cdd:cd04129  103 CPNVPVILVGLKKDLrqeavakgnyaTDEFVPIQQAKLVARAIGAkKYMECSALTGEGVDDVFEAATR 170
Rab14 cd04122
Rab GTPase family 14 (Rab14); Rab14 GTPases are localized to biosynthetic compartments, ...
16-165 6.02e-19

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  Cd Length: 166  Bit Score: 79.88  E-value: 6.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVV-IDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:cd04122   15 KSCLLHQFTEKKFMADCPHTIGVEFGTRIIeVNGQKIKLQIWDTAGQERFRAVTRSYYRGAAGALMVYDITRRSTYNHLS 94
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194363764  95 QYREQIKRVKDSDDVpMVLVGNKCDL-AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQ 165
Cdd:cd04122   95 SWLTDARNLTNPNTV-IFLIGNKADLeAQRDVTYEEAKQFADENGLLFLECSAKTGENVEDAFLETAKKIYQ 165
Rab23_like cd04106
Rab GTPase family 23 (Rab23)-like; Rab23-like subfamily. Rab23 is a member of the Rab family ...
16-156 3.52e-18

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  Cd Length: 162  Bit Score: 77.48  E-value: 3.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTI-EDSYRKQVVID--GETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFED 92
Cdd:cd04106   13 KSSMIQRFVKGIFTKDYKKTIgVDFLEKQIFLRqsDEDVRLMLWDTAGQEEFDAITKAYYRGAQACILVFSTTDRESFEA 92
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194363764  93 IHQYREQIKRVkdSDDVPMVLVGNKCDLAART-VESRQAQDLARSYGIPYIETSAKTRQGVEDAF 156
Cdd:cd04106   93 IESWKEKVEAE--CGDIPMVLVQTKIDLLDQAvITNEEAEALAKRLQLPLFRTSVKDDFNVTELF 155
Rab3 cd01865
Rab GTPase family 3 contains Rab3A, Rab3B, Rab3C and Rab3D; The Rab3 subfamily contains Rab3A, ...
53-160 9.78e-18

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: 76.49  E-value: 9.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  53 LDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKdSDDVPMVLVGNKCDLA-ARTVESRQAQ 131
Cdd:cd01865   52 LQIWDTAGQERYRTITTAYYRGAMGFILMYDITNEESFNAVQDWSTQIKTYS-WDNAQVILVGNKCDMEdERVVSAERGR 130
                         90       100
                 ....*....|....*....|....*....
gi 194363764 132 DLARSYGIPYIETSAKTRQGVEDAFYTLV 160
Cdd:cd01865  131 QLADQLGFEFFEASAKENINVKQVFERLV 159
Rab12 cd04120
Rab GTPase family 12 (Rab12); Rab12 was first identified in canine cells, where it was ...
42-163 2.86e-17

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: 75.43  E-value: 2.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  42 KQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKdSDDVPMVLVGNKCDLA 121
Cdd:cd04120   40 KTVELRGKKIRLQIWDTAGQERFNSITSAYYRSAKGIILVYDITKKETFDDLPKWMKMIDKYA-SEDAELLLVGNKLDCE 118
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 194363764 122 A-RTVESRQAQDLA-RSYGIPYIETSAKTRQGVEDAFYTLVREI 163
Cdd:cd04120  119 TdREITRQQGEKFAqQITGMRFCEASAKDNFNVDEIFLKLVDDI 162
Rac1_like cd01871
Ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1)-like ...
16-163 3.57e-17

Ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1)-like consists of Rac1, Rac2 and Rac3; The Rac1-like subfamily consists of Rac1, Rac2, and Rac3 proteins, plus the splice variant Rac1b that contains a 19-residue insertion near switch II relative to Rac1. While Rac1 is ubiquitously expressed, Rac2 and Rac3 are largely restricted to hematopoietic and neural tissues respectively. Rac1 stimulates the formation of actin lamellipodia and membrane ruffles. It also plays a role in cell-matrix adhesion and cell anoikis. In intestinal epithelial cells, Rac1 is an important regulator of migration and mediates apoptosis. Rac1 is also essential for RhoA-regulated actin stress fiber and focal adhesion complex formation. In leukocytes, Rac1 and Rac2 have distinct roles in regulating cell morphology, migration, and invasion, but are not essential for macrophage migration or chemotaxis. Rac3 has biochemical properties that are closely related to Rac1, such as effector interaction, nucleotide binding, and hydrolysis; Rac2 has a slower nucleotide association and is more efficiently activated by the RacGEF Tiam1. Both Rac1 and Rac3 have been implicated in the regulation of cell migration and invasion in human metastatic breast cancer. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206663  Cd Length: 174  Bit Score: 74.85  E-value: 3.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH- 94
Cdd:cd01871   14 KTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRa 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  95 QYREQIKRvkDSDDVPMVLVGNKCDL------AARTVESRQA-----QDLARSYGI---PYIETSAKTRQGVEDAFYTLV 160
Cdd:cd01871   94 KWYPEVRH--HCPNTPIILVGTKLDLrddkdtIEKLKEKKLTpitypQGLAMAKEIgavKYLECSALTQRGLKTVFDEAI 171

                 ...
gi 194363764 161 REI 163
Cdd:cd01871  172 RAV 174
Rho4_like cd04132
Ras homology family 4 (Rho4) of small guanosine triphosphatases (GTPases)-like; Rho4 is a ...
11-168 5.41e-17

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  Cd Length: 197  Bit Score: 74.68  E-value: 5.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  11 AGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVI-DGETCLLDILDTAGQEEYSAMRD-QYMRTGEGFLCvFAINNTK 88
Cdd:cd04132   11 DGGCGKTCLLMVYAQGSFPEEYVPTVFENYVTTLQVpNGKIIELALWDTAGQEDYDRLRPlSYPDVDVILIC-YSVDNPT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  89 SFEDIhqyreQIK---RVKD-SDDVPMVLVGNKCDLAA-------------RTVESRQAQDLARSYG-IPYIETSAKTRQ 150
Cdd:cd04132   90 SLDNV-----EDKwypEVNHfCPGTPIVLVGLKTDLRKdknsvsklraqglEPVTPEQGESVAKSIGaVAYIECSAKLME 164
                        170
                 ....*....|....*....
gi 194363764 151 GVEDAFYTLVRE-IRQHKL 168
Cdd:cd04132  165 NVDEVFDAAINVaLSKSGR 183
Cdc42 cd01874
cell division cycle 42 (Cdc42) is a small GTPase of the Rho family; Cdc42 is an essential ...
16-156 1.29e-16

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


Pssm-ID: 206664  Cd Length: 175  Bit Score: 73.37  E-value: 1.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQ 95
Cdd:cd01874   14 KTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAGQEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKE 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194363764  96 -YREQIKRvkDSDDVPMVLVGNKCDL-------------AARTVESRQAQDLARSYG-IPYIETSAKTRQGVEDAF 156
Cdd:cd01874   94 kWVPEITH--HCPKTPFLLVGTQIDLrddpstieklaknKQKPITPETGEKLARDLKaVKYVECSALTQKGLKNVF 167
RhoA_like cd01870
Ras homology family A (RhoA)-like includes RhoA, RhoB and RhoC; The RhoA subfamily consists of ...
16-161 5.95e-16

Ras homology family A (RhoA)-like includes RhoA, RhoB and RhoC; The RhoA subfamily consists of RhoA, RhoB, and RhoC. RhoA promotes the formation of stress fibers and focal adhesions, regulating cell shape, attachment, and motility. RhoA can bind to multiple effector proteins, thereby triggering different downstream responses. In many cell types, RhoA mediates local assembly of the contractile ring, which is necessary for cytokinesis. RhoA is vital for muscle contraction; in vascular smooth muscle cells, RhoA plays a key role in cell contraction, differentiation, migration, and proliferation. RhoA activities appear to be elaborately regulated in a time- and space-dependent manner to control cytoskeletal changes. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. RhoA and RhoC are observed only in geranylgeranylated forms; however, RhoB can be present in palmitoylated, farnesylated, and geranylgeranylated forms. RhoA and RhoC are highly relevant for tumor progression and invasiveness; however, RhoB has recently been suggested to be a tumor suppressor. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206662  Cd Length: 175  Bit Score: 71.31  E-value: 5.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRD-QYMRTGEGFLCvFAINNTKSFEDIH 94
Cdd:cd01870   14 KTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPlSYPDTDVILMC-FSIDSPDSLENIP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  95 QyrEQIKRVKD-SDDVPMVLVGNKCDL----------------AARTVESRQAQDLARSYGipYIETSAKTRQGVEDAFY 157
Cdd:cd01870   93 E--KWTPEVKHfCPNVPIILVGNKKDLrndehtirelakmkqePVKPEEGRAMAEKIGAFG--YLECSAKTKEGVREVFE 168

                 ....
gi 194363764 158 TLVR 161
Cdd:cd01870  169 MATR 172
Ran cd00877
Ras-related nuclear proteins (Ran)/TC4 family of small GTPases; Ran GTPase is involved in ...
54-161 9.27e-16

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  Cd Length: 166  Bit Score: 70.79  E-value: 9.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  54 DILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVkdSDDVPMVLVGNKCDLAARTVESRQAQDL 133
Cdd:cd00877   52 NVWDTAGQEKFGGLRDGYYIQGQCAIIMFDVTSRVTYKNVPNWHRDLVRV--CENIPIVLCGNKVDIKDRKVKPKQITFH 129
                         90       100
                 ....*....|....*....|....*...
gi 194363764 134 aRSYGIPYIETSAKTRQGVEDAFYTLVR 161
Cdd:cd00877  130 -RKKNLQYYEISAKSNYNFEKPFLWLAR 156
Rab30 cd04114
Rab GTPase family 30 (Rab30); Rab30 subfamily. Rab30 appears to be associated with the Golgi ...
42-163 1.31e-15

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  Cd Length: 169  Bit Score: 70.31  E-value: 1.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  42 KQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSdDVPMVLVGNKCDLA 121
Cdd:cd04114   47 KTVEIKGEKIKLQIWDTAGQERFRSITQSYYRSANALILTYDITCEESFRCLPEWLREIEQYANN-KVITILVGNKIDLA 125
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 194363764 122 A-RTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREI 163
Cdd:cd04114  126 ErREVSQQRAEEFSDAQDMYYLETSAKESDNVEKLFLDLACRL 168
Tc10 cd04135
Rho GTPase TC10 (Tc10); TC10 is a Rho family protein that has been shown to induce microspike ...
16-156 1.64e-15

Rho GTPase TC10 (Tc10); TC10 is a Rho family protein that has been shown to induce microspike formation and neurite outgrowth in vitro. Its expression changes dramatically after peripheral nerve injury, suggesting an important role in promoting axonal outgrowth and regeneration. TC10 regulates translocation of insulin-stimulated GLUT4 in adipocytes and has also been shown to bind directly to Golgi COPI coat proteins. GTP-bound TC10 in vitro can bind numerous potential effectors. Depending on its subcellular localization and distinct functional domains, TC10 can differentially regulate two types of filamentous actin in adipocytes. TC10 mRNAs are highly expressed in three types of mouse muscle tissues: leg skeletal muscle, cardiac muscle, and uterus; they were also present in brain, with higher levels in adults than in newborns. TC10 has also been shown to play a role in regulating the expression of cystic fibrosis transmembrane conductance regulator (CFTR) through interactions with CFTR-associated ligand (CAL). The GTP-bound form of TC10 directs the trafficking of CFTR from the juxtanuclear region to the secretory pathway toward the plasma membrane, away from CAL-mediated DFTR degradation in the lysosome. 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: 206707  Cd Length: 174  Bit Score: 70.05  E-value: 1.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQ 95
Cdd:cd04135   13 KTCLLMSYANDAFPEEYVPTVFDHYAVSVTVGGKQYLLGLYDTAGQEDYDRLRPLSYPMTDVFLICFSVVNPASFQNVKE 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194363764  96 yrEQIKRVKD-SDDVPMVLVGNKCDL-------------AARTVESRQAQDLARSYGIP-YIETSAKTRQGVEDAF 156
Cdd:cd04135   93 --EWVPELKEyAPNVPYLLIGTQIDLrddpktlarlndmKEKPITVEQGQKLAKEIGACcYVECSALTQKGLKTVF 166
Rab32_Rab38 cd04107
Rab GTPase families 18 (Rab18) and 32 (Rab32); Rab38/Rab32 subfamily. Rab32 and Rab38 are ...
13-163 3.98e-15

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: 69.26  E-value: 3.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  13 GVGKSALTIQLIQNHFVDEYDPTIE-DSYRKQVVIDGETCL-LDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSF 90
Cdd:cd04107   10 GVGKTSIIKRYVHGVFSQHYKATIGvDFALKVIEWDPNTVVrLQLWDIAGQERFGGMTRVYYKGAVGAIIVFDVTRPSTF 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194363764  91 EDIHQYREQI-KRVK--DSDDVPMVLVGNKCDLAART--VESRQAQDLARSYGIP-YIETSAKTRQGVEDAFYTLVREI 163
Cdd:cd04107   90 EAVLKWKADLdSKVTlpNGEPIPALLLANKCDLKKERlaKDPEQMDQFCKENGFIgWFETSAKENINIEEAMRFLVKNI 168
Rho3 cd04134
Ras homology family 3 (Rho3) of small guanosine triphosphatases (GTPases); Rho3 is a member of ...
16-183 6.60e-15

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


Pssm-ID: 206706  Cd Length: 185  Bit Score: 68.35  E-value: 6.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRD-QYMRTGEGFLCvFAINNTKSFEDIH 94
Cdd:cd04134   13 KTSLLNVFTRGYFPQVYEPTVFENYIHDIFVDGLAVELSLWDTAGQEEFDRLRSlSYADTHVIMLC-FSVDNPDSLENVE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  95 QyrEQIKRVKDS-DDVPMVLVGNKCDL---------AARTVESRQAQDLARSYG-IPYIETSAKTRQGVEDAFYTLVREI 163
Cdd:cd04134   92 S--KWLAEIRHHcPGVKLVLVALKCDLreprnerdrGTHTISYEEGLAVAKRINaCRYLECSAKLNRGVNEAFTEAARVA 169
                        170       180
                 ....*....|....*....|
gi 194363764 164 RQHKlrklnPPDESGPGCMS 183
Cdd:cd04134  170 LNAR-----PPHPHSRACTI 184
Rab40 cd04121
Rab GTPase family 40 (Rab40) contains Rab40a, Rab40b and Rab40c; The Rab40 subfamily contains ...
44-189 7.69e-14

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


Pssm-ID: 133321 [Multi-domain]  Cd Length: 189  Bit Score: 65.34  E-value: 7.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  44 VVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKrvKDSDDVPMVLVGNKCDLA-A 122
Cdd:cd04121   48 ILLDGRRVKLQLWDTSGQGRFCTIFRSYSRGAQGIILVYDITNRWSFDGIDRWIKEID--EHAPGVPKILVGNRLHLAfK 125
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194363764 123 RTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRqhkLRKLNPPDESGPGCMSCKCVLS 189
Cdd:cd04121  126 RQVATEQAQAYAERNGMTFFEVSPLCNFNITESFTELARIVL---MRHGRPPQSPPQNCSRNSCKIS 189
Miro pfam08477
Miro-like protein; Mitochondrial Rho proteins (Miro-1 and Miro-2), are atypical Rho GTPases. ...
16-119 8.88e-13

Miro-like protein; Mitochondrial Rho proteins (Miro-1 and Miro-2), are atypical Rho GTPases. They have a unique domain organisation, 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: 254820  Cd Length: 118  Bit Score: 61.29  E-value: 8.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764   16 KSALTIQLIQNHFVDE-YDPTIEDSYRKQ-VVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDI 93
Cdd:pfam08477  12 KSSLLSQLVGGEFPPEiPEEIQGDTLAVDtLEVDGDTELLHIWDFGGREELKFEHIIFMKTADAILLVYDLTDRESLNRV 91
                          90       100
                  ....*....|....*....|....*..
gi 194363764   94 HQYREQIKRVKDSD-DVPMVLVGNKCD 119
Cdd:pfam08477  92 SRLIAWLPHLRKLGkKIPVILVGNKFD 118
PLN03071 PLN03071
GTP-binding nuclear protein Ran; Provisional
4-163 9.08e-13

GTP-binding nuclear protein Ran; Provisional


Pssm-ID: 178620  Cd Length: 219  Bit Score: 62.85  E-value: 9.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764   4 YKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIE-DSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVF 82
Cdd:PLN03071  14 FKLVIVGDGGTGKTTFVKRHLTGEFEKKYEPTIGvEVHPLDFFTNCGKIRFYCWDTAGQEKFGGLRDGYYIHGQCAIIMF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  83 AINNTKSFEDIHQYREQIKRVkdSDDVPMVLVGNKCDLAARTVESRQAQdLARSYGIPYIETSAKTRQGVEDAFYTLVRE 162
Cdd:PLN03071  94 DVTARLTYKNVPTWHRDLCRV--CENIPIVLCGNKVDVKNRQVKAKQVT-FHRKKNLQYYEISAKSNYNFEKPFLYLARK 170

                 .
gi 194363764 163 I 163
Cdd:PLN03071 171 L 171
Rab24 cd04118
Rab GTPase family 24 (Rab24); Rab24 is distinct from other Rabs in several ways. It exists ...
16-159 3.46e-12

Rab GTPase family 24 (Rab24); Rab24 is distinct from other Rabs in several ways. It exists primarily in the GTP-bound state, having a low intrinsic GTPase activity; it is not efficiently geranyl-geranylated at the C-terminus; it does not form a detectable complex with Rab GDP-dissociation inhibitors (GDIs); and it has recently been shown to undergo tyrosine phosphorylation when overexpressed in vitro. The specific function of Rab24 still remains unknown. It is found in a transport route between ER-cis-Golgi and late endocytic compartments. It is putatively involved in an autophagic pathway, possibly directing misfolded proteins in the ER to degradative pathways. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins.


Pssm-ID: 133318  Cd Length: 193  Bit Score: 60.65  E-value: 3.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVD-EYDPTIEDSY-RKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDI 93
Cdd:cd04118   13 KTSLVERYVHHRFLVgPYQNTIGAAFvAKRMVVGERVVTLGIWDTAGSERYEAMSRIYYRGAKAAIVCYDLTDSSSFERA 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194363764  94 HQYREQIKRVKdsDDVPMVLVGNKCDL-----AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTL 159
Cdd:cd04118   93 KFWVKELQNLE--EHCKIYLCGTKSDLieqdrSLRQVDFHDVQDFADEIKAQHFETSSKTGQNVDELFQKV 161
RRP22 cd04142
Ras-related protein on chromosome 22 (RRP22) family; RRP22 (Ras-related protein on chromosome ...
14-161 4.70e-12

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  Cd Length: 198  Bit Score: 60.27  E-value: 4.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  14 VGKSALTIQLIQNHFVDEYDPTI-EDSYRKQVVIDGETCLLDILD--------TAGQEEYSAMRDQYMRTGEGFLCVFAI 84
Cdd:cd04142   11 VGKTAIVRQFLAQEFPEEYIPTEhRRLYRPAVVLSGRVYDLHILDvpnmqrypGTAGQEWMDPRFRGLRNSRAFILVYDI 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  85 NNTKSFEDIHQYREQI--KRVKDSDDVPMVLVGNKCDLAARTVESRQAQD--LARSYGIPYIETSAKTRQGVEDAFYTLV 160
Cdd:cd04142   91 CSPDSFHYVKLLRQQIleTRPAGNKEPPIVVVGNKRDQQRHRFAPRHVLSvlVRKSWKCGYLECSAKYNWHILLLFKELL 170

                 .
gi 194363764 161 R 161
Cdd:cd04142  171 I 171
RabL2 cd04124
Rab GTPase-like family 2 (Rab-like2); RabL2 (Rab-like2) subfamily. RabL2s are novel Rab ...
22-167 7.61e-12

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


Pssm-ID: 133324  Cd Length: 161  Bit Score: 59.49  E-value: 7.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  22 QLIQNHFVDEYDPTIEDSY-----RKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAI-------NNTKS 89
Cdd:cd04124   15 KLVERFLMDGYEPQQLSTYaltlyKHNAKFEGKTILVDFWDTAGQERFQTMHASYYHKAHACILVFDVtrkitykNLSKW 94
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194363764  90 FEDIHQYREQIkrvkdsddvPMVLVGNKCDLAARTVEsrQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHK 167
Cdd:cd04124   95 YEELREYRPEI---------PCIVVANKIDLDPSVTQ--KKFNFAEKHNLPLYYVSAADGTNVVKLFQDAIKLAVSYK 161
Centaurin_gamma cd04103
Centaurin gamma (CENTG) GTPase; The centaurins (alpha, beta, gamma, and delta) are large, ...
16-156 9.30e-12

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


Pssm-ID: 133303  Cd Length: 158  Bit Score: 59.04  E-value: 9.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEdSYRKQVVIDGETCLLDILDTAGQEEYsamrdQYMRTGEGFLCVFAINNTKSFEDIHQ 95
Cdd:cd04103   13 KSALVHRYLTGSYVQLESPEGG-RFKKEVLVDGQSHLLLIRDEGGAPDA-----QFASWVDAVIFVFSLENEASFQTVYN 86
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194363764  96 YREQIKRVKDSDDVPMVLVGNKCDLAART------VESRQ-AQDLARSygiPYIETSAKTRQGVEDAF 156
Cdd:cd04103   87 LYHQLSSYRNISEIPLILVGTQDAISESNprviddARARQlCADMKRC---SYYETCATYGLNVERVF 151
Rab36_Rab34 cd04108
Rab GTPase families 34 (Rab34) and 36 (Rab36); Rab34/Rab36 subfamily. Rab34, found primarily ...
16-157 8.61e-11

Rab GTPase families 34 (Rab34) and 36 (Rab36); Rab34/Rab36 subfamily. Rab34, found primarily in the Golgi, interacts with its effector, Rab-interacting lysosomal protein (RILP). This enables its participation in microtubular dynenin-dynactin-mediated repositioning of lysosomes from the cell periphery to the Golgi. A Rab34 (Rah) isoform that lacks the consensus GTP-binding region has been identified in mice. This isoform is associated with membrane ruffles and promotes macropinosome formation. Rab36 has been mapped to human chromosome 22q11.2, a region that is homozygously deleted in malignant rhabdoid tumors (MRTs). However, experimental assessments do not implicate Rab36 as a tumor suppressor that would enable tumor formation through a loss-of-function mechanism. 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: 206693  Cd Length: 170  Bit Score: 56.42  E-value: 8.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIE-DSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:cd04108   13 KTCLINRFCKDVFDKNYKATIGvDFEMERFEVLGVPFSLQLWDTAGQERFKCIASTYYRGAQAIIIVFDLTDVASLEHTR 92
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194363764  95 QYREQIKRVKDSDDVPMVLVGNKCDL---AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFY 157
Cdd:cd04108   93 QWLEDALKENDPSSVLLFLVGTKKDLsspAQYALMEQDAIKLAREMKAEYWAVSALTGENVRDFFF 158
Rnd cd04131
Rho family GTPase subfamily Rnd includes Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8; The Rnd ...
16-158 7.31e-10

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


Pssm-ID: 206703  Cd Length: 176  Bit Score: 53.98  E-value: 7.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDI-H 94
Cdd:cd04131   14 KTALLQVFAKDSFPENYVPTVFENYTASFEVDKQRIELSLWDTSGSPYYDNVRPLSYPDSDAVLICFDISRPETLDSVlK 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194363764  95 QYREQIKRVKDSddVPMVLVGNKCDLAA-------------RTVESRQAQDLARSYG-IPYIETSAKT-RQGVEDAFYT 158
Cdd:cd04131   94 KWKGEVREFCPN--TPVLLVGCKSDLRTdlstltelsnkrqIPVSHEQGRNLAKQIGaAAYVECSAKTsENSVRDVFEM 170
RocCOR cd09914
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ...
3-162 6.57e-08

Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein family is characterized by a superdomain containing a Ras-like GTPase domain, called Roc (Ras of complex proteins), and a characteristic second domain called COR (C-terminal of Roc). A kinase domain and diverse regulatory domains are also often found in Roco proteins. Their functions are diverse; in Dictyostelium discoideum, which encodes 11 Roco proteins, they are involved in cell division, chemotaxis and development, while in human, where 4 Roco proteins (LRRK1, LRRK2, DAPK1, and MFHAS1) are encoded, these proteins are involved in epilepsy and cancer. Mutations in LRRK2 (leucine-rich repeat kinase 2) are known to cause familial Parkinson's disease.


Pssm-ID: 206741  Cd Length: 161  Bit Score: 48.49  E-value: 6.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764   3 EYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPT----IEDSYRKqvVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGF 78
Cdd:cd09914    1 EAKLMLVGQGGVGKTSLCKQLIGEKFDGDESSThginVQDWKIP--APERKKIRLNVWDFGGQEIYHATHQFFLTSRSLY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  79 LCVFAINNTKSFEDIHQYREQIKrvKDSDDVPMVLVGNKCDLAArtvESRQAQDLARSYGIP----YIETSAKTRQGVED 154
Cdd:cd09914   79 LLVFDLRTGDEVSRVPYWLRQIK--AFGGVSPVILVGTHIDESC---DEDILKKALNKKFPAiindIHFVSCKNGKGIAE 153

                 ....*...
gi 194363764 155 AFYTLVRE 162
Cdd:cd09914  154 LKKAIAKE 161
Rnd3_RhoE_Rho8 cd04172
Rnd3/RhoE/Rho8 GTPases; Rnd3/RhoE/Rho8 subfamily. Rnd3/RhoE/Rho8 is a member of the novel Rho ...
16-157 8.09e-08

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  Cd Length: 182  Bit Score: 48.51  E-value: 8.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDI-H 94
Cdd:cd04172   18 KTALLHVFAKDCFPENYVPTVFENYTASFEIDTQRIELSLWDTSGSPYYDNVRPLSYPDSDAVLICFDISRPETLDSVlK 97
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194363764  95 QYREQIKRVkdSDDVPMVLVGNKCDLAA-------------RTVESRQAQDLARSYG-IPYIETSA-KTRQGVEDAFY 157
Cdd:cd04172   98 KWKGEIQEF--CPNTKMLLVGCKSDLRTdvstlvelsnhrqTPVSYDQGANMAKQIGaATYIECSAlQSENSVRDIFH 173
RhoBTB cd01873
RhoBTB protein is an atypical member of the Rho family of small GTPases; Members of the RhoBTB ...
16-161 1.40e-07

RhoBTB protein is an atypical member of the Rho family of small GTPases; Members of the RhoBTB subfamily of Rho GTPases are present in vertebrates, Drosophila, and Dictyostelium. RhoBTB proteins are characterized by a modular organization, consisting of a GTPase domain, a proline rich region, a tandem of two BTB (Broad-Complex, Tramtrack, and Bric a brac) domains, and a C-terminal region of unknown function. RhoBTB proteins may act as docking points for multiple components participating in signal transduction cascades. RhoBTB genes appeared upregulated in some cancer cell lines, suggesting a participation of RhoBTB proteins in the pathogenesis of particular tumors. Note that the Dictyostelium RacA GTPase domain is more closely related to Rac proteins than to RhoBTB proteins, where RacA actually belongs. Thus, the Dictyostelium RacA is not included here. Most Rho proteins contain a lipid modification site at the C-terminus; however, RhoBTB is one of few Rho subfamilies that lack this feature.


Pssm-ID: 133275  Cd Length: 195  Bit Score: 48.04  E-value: 1.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHF-----VDEYDPTIEDSYRKQVVIDGETCLLDILDTAGqEEYSAMRDQYMRTGEGFLCvFAINNTKSF 90
Cdd:cd01873   26 KTLTQYQLLATHVptvwaIDQYRVCQEVLERSRDVVDGVSVSLRLWDTFG-DHDKDRRFAYGRSDVVLLC-FSIASPNSL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  91 EDIHQ-YREQIKRVkdSDDVPMVLVGNKCDL--------------------AARTVESRQAQDLARSYGIPYIETSAKTR 149
Cdd:cd01873  104 RNVKTmWYPEIRHF--CPRVPVILVGCKLDLryadldevnrarrplarpikNADILPPETGRAVAKELGIPYYETSVVTQ 181
                        170
                 ....*....|..
gi 194363764 150 QGVEDAFYTLVR 161
Cdd:cd01873  182 FGVKDVFDNAIR 193
Rnd2_Rho7 cd04173
Rnd2/Rho7 GTPases; Rnd2/Rho7 is a member of the novel Rho subfamily Rnd, together with Rnd1 ...
13-172 1.91e-06

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


Pssm-ID: 206736 [Multi-domain]  Cd Length: 221  Bit Score: 45.40  E-value: 1.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  13 GVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFED 92
Cdd:cd04173   11 QCGKTALLHVFAKDNYPESYVPTVFENYTASFEIDKHRIELNMWDTSGSSYYDNVRPLAYPDSDAVLICFDISRPETLDS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  93 IHQyREQIKRVKDSDDVPMVLVGnkCDLAART---------------VESRQAQDLARSYG-IPYIETSAK-TRQGVEDA 155
Cdd:cd04173   91 VLK-KWQGETQEFCPNAKLVLVG--CKLDMRTdlstlrelskqrlipVTHEQGSLLARQLGaVAYVECSSRmSENSVRDV 167
                        170       180
                 ....*....|....*....|
gi 194363764 156 FY--TLVREIRQHK-LRKLN 172
Cdd:cd04173  168 FHvtTLASVRREHPsLKRST 187
Miro1 cd01893
Mitochondrial Rho family 1 (Miro1), N-terminal; Miro1 subfamily. Miro (mitochondrial Rho) ...
13-157 3.72e-06

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  Cd Length: 168  Bit Score: 43.87  E-value: 3.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  13 GVGKSALTIQLIQNHFVDEYDPTIEDsYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFED 92
Cdd:cd01893   12 GVGKSSLIMSLVSEEFPENVPRVLPE-ITIPADVTPERVPTTIVDTSSRPQDRANLAAEIRKANVICLVYSVDRPSTLER 90
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194363764  93 IHQYR-EQIKRVkdSDDVPMVLVGNKCDLAARTVESRQAQDLA---RSYG--IPYIETSAKTRQGVEDAFY 157
Cdd:cd01893   91 IRTKWlPLIRRL--GVKVPIILVGNKSDLRDGSSQAGLEEEMLpimNEFReiETCVECSAKTLINVSEVFY 159
COG2229 COG2229
Predicted GTPase [General function prediction only]
1-159 7.56e-06

Predicted GTPase [General function prediction only]


Pssm-ID: 225138  Cd Length: 187  Bit Score: 43.22  E-value: 7.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764   1 MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYR----KQVVIDGETCLLD------ILDTAGQEEYSAMRDQ 70
Cdd:COG2229    8 MIETKIVVIGPVGAGKTTFVRALSDKPLVITEADASSVSGKgkrpTTVAMDFGSIELDedtgvhLFGTPGQERFKFMWEI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  71 YMRTGEGFLCVFAINNTKSFEDihqyREQIKRVKDSDDVPMVLVGNKCDLA-ARTVES-RQAQDLARSyGIPYIETSAKT 148
Cdd:COG2229   88 LSRGAVGAIVLVDSSRPITFHA----EEIIDFLTSRNPIPVVVAINKQDLFdALPPEKiREALKLELL-SVPVIEIDATE 162
                        170
                 ....*....|.
gi 194363764 149 RQGVEDAFYTL 159
Cdd:COG2229  163 GEGARDQLDVL 173
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
96-166 1.97e-05

HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment N-terminal of the GTPase domain characterizes the HflX subfamily. The E. coli HflX has been implicated in the control of the lambda cII repressor proteolysis, but the actual biological functions of these GTPases remain unclear. HflX is widespread, but not universally represented in all three superkingdoms.


Pssm-ID: 206666  Cd Length: 204  Bit Score: 42.06  E-value: 1.97e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194363764  96 YREQIKRVKD------SDDVPMVLVGNKCDLaartVESRQAQDLARSYGIPYIETSAKTRQGVEDafytLVREIRQH 166
Cdd:cd01878  135 REEQIETVEEvlkelgADDIPIILVLNKIDL----LDDEELEERLRAGRPDAVFISAKTGEGLDL----LKEAIEEL 203
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
110-165 2.86e-05

Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress response, chromosome partitioning, replication initiation, mycelium development, and sporulation. Obg proteins are among a large group of GTP binding proteins conserved from bacteria to humans. The E. coli homolog, ObgE is believed to function in ribosomal biogenesis. Members of the subfamily contain two equally and highly conserved domains, a C-terminal GTP binding domain and an N-terminal glycine-rich domain.


Pssm-ID: 206685 [Multi-domain]  Cd Length: 170  Bit Score: 41.26  E-value: 2.86e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 194363764 110 PMVLVGNKCDL-AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDafytLVREIRQ 165
Cdd:cd01898  116 PRIVVLNKIDLlDAEERFEKLKELLKELKGKKVFPISALTGEGLDE----LLKKLAK 168
Rnd1_Rho6 cd04174
Rnd1/Rho6 GTPases; Rnd1/Rho6 is a member of the novel Rho subfamily Rnd, together with Rnd2 ...
16-179 3.70e-04

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


Pssm-ID: 206737 [Multi-domain]  Cd Length: 232  Bit Score: 38.89  E-value: 3.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFED-IH 94
Cdd:cd04174   26 KTAMLQVLAKDCYPETYVPTVFENYTACLETEEQRVELSLWDTSGSPYYDNVRPLCYSDSDAVLLCFDISRPEIFDSaLK 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  95 QYREQIkrvkdSDDVP---MVLVGNKCDLaaRT---------------VESRQAQDLARSYGIP-YIETSAKTRqgvEDA 155
Cdd:cd04174  106 KWRAEI-----LDYCPstrILLIGCKTDL--RTdlstlmelsnqkqapISYEQGCAMAKQLGAEaYLECSAFTS---EKS 175
                        170       180
                 ....*....|....*....|....
gi 194363764 156 FYTLVREIRQHKLRKLNPPDESGP 179
Cdd:cd04174  176 IHSIFRTASLLCINKLSPLAKKSP 199
Rab20 cd04126
Rab GTPase family 20 (Rab20); Rab20 is one of several Rab proteins that appear to be ...
55-172 3.80e-04

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


Pssm-ID: 133326 [Multi-domain]  Cd Length: 220  Bit Score: 38.74  E-value: 3.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  55 ILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKdSDDVPMVLVGNKCDL-------------- 120
Cdd:cd04126   48 IWDTAGREQFHGLGSMYCRGAAAVILTYDVSNVQSLEELEDRFLGLTDTA-NEDCLFAVVGNKLDLteegalagqekdag 126
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194363764 121 ------AARTVESRQAQDLAR---SYGI-----------PYIETSAKTRQGVEDAFYTLVREIRQHKLRKLN 172
Cdd:cd04126  127 drvspeDQRQVTLEDAKAFYKrinKYKMldedlspaaekMCFETSAKTGYNVDELFEYLFNLVLPLILAQRA 198
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
109-165 4.22e-04

Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) subfamily. E. coli has an iron(II) transport system, known as feo, which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.


Pssm-ID: 206667 [Multi-domain]  Cd Length: 159  Bit Score: 37.82  E-value: 4.22e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 194363764 109 VPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDafytLVREIRQ 165
Cdd:cd01879  103 LPVVVALNMIDEAEKRGIKIDLDKLSELLGVPVVPTSARKGEGIDE----LLDAIAK 155
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
101-165 4.31e-04

trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 37.86  E-value: 4.31e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194363764 101 KRVKDSDDVPMVLVGNKCDLAARTVESRQAqdlarsYGIPYIETSAKTRQGVEDafytLVREIRQ 165
Cdd:cd04164  102 EILELPAKKPVIVVLNKSDLLSDAEGISEL------NGKPIIAISAKTGEGIDE----LKEALLE 156
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
43-154 5.24e-04

Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.


Pssm-ID: 206674 [Multi-domain]  Cd Length: 169  Bit Score: 37.84  E-value: 5.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  43 QVVIDGETCLLDILDTAGQEEYSAMRdqyMRTGEgfLC-----VFAINNtkSFEDihQYREQIKRVKDSDdVPMVLVGNK 117
Cdd:cd01887   41 QVPIDVKIPGITFIDTPGHEAFTNMR---ARGAS--VTdiailVVAADD--GVMP--QTIEAINHAKAAN-VPIIVAINK 110
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 194363764 118 CDLAARTVES--RQAQDLArSYGI---------PYIETSAKTRQGVED 154
Cdd:cd01887  111 IDKPYGTEADpeRVKNELS-ELGLvgeewggdvSIVPISAKTGEGIDD 157
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
108-163 6.09e-04

Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.


Pssm-ID: 251282  Cd Length: 156  Bit Score: 37.40  E-value: 6.09e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 194363764  108 DVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDafytLVREI 163
Cdd:pfam02421 105 GIPVVLALNMMDEAEKKGIKIDIKKLSKLLGVPVVPTSARKGEGIDE----LKDAI 156
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
112-154 8.14e-04

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 37.38  E-value: 8.14e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 194363764 112 VLVGNKCDLAArTVESRQAQDLARSYGIPYIETSAKTRQGVED 154
Cdd:cd01854   37 VIVLNKADLVD-DEELEELLEIYEKLGYPVLAVSAKTGEGLDE 78
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
13-166 1.21e-03

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


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 36.84  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  13 GVGKSALTIQLIQNHF--VDEYDPTIEDSYRKQVVIDGETcLLDILDTAG--------QEEYSAMRDQYMRTGegfLCVF 82
Cdd:cd00880    7 NVGKSSLLNALLGQNVgiVSPIPGTTRDPVRKEWELLPLG-PVVLIDTPGldeegglgRERVEEARQVADRAD---LVLL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  83 AINNTKSFEDIHQYREQIKRVKdsddVPMVLVGNKCDLAARTVESRQAQDLARSY--GIPYIETSAKTRQGVEdafyTLV 160
Cdd:cd00880   83 VVDSDLTPVEEEAKLGLLRERG----KPVLLVLNKIDLVPESEEEELLRERKLELlpDLPVIAVSALPGEGID----ELR 154

                 ....*.
gi 194363764 161 REIRQH 166
Cdd:cd00880  155 KKIAEL 160
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
98-155 1.40e-03

Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in eukaryotes ranging from trypanosomes to humans. NOG1 is functionally linked to ribosome biogenesis and found in association with the nuclear pore complexes and identified in many preribosomal complexes. Thus, defects in NOG1 can lead to defects in 60S biogenesis. The S. cerevisiae NOG1 gene is essential for cell viability, and mutations in the predicted G motifs abrogate function. It is a member of the ODN family of GTP-binding proteins that also includes the bacterial Obg and DRG proteins.


Pssm-ID: 206684 [Multi-domain]  Cd Length: 167  Bit Score: 36.38  E-value: 1.40e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194363764  98 EQI---KRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSyGIPYIETSAKTRQGVEDA 155
Cdd:cd01897   99 EQLslfKEIKPLFNKPVIVVLNKIDLLTEEDLSEIEKELEKE-GEEVIKISTLTEEGVDEL 158
Spg1 cd04128
Septum-promoting GTPase (Spg1); Spg1p. Spg1p (septum-promoting GTPase) was first identified in ...
16-146 2.03e-03

Septum-promoting GTPase (Spg1); Spg1p. Spg1p (septum-promoting GTPase) was first identified in the fission yeast S. pombe, where it regulates septum formation in the septation initiation network (SIN) through the cdc7 protein kinase. Spg1p is an essential gene that localizes to the spindle pole bodies. When GTP-bound, it binds cdc7 and causes it to translocate to spindle poles. Sid4p (septation initiation defective) is required for localization of Spg1p to the spindle pole body, and the ability of Spg1p to promote septum formation from any point in the cell cycle depends on Sid4p. Spg1p is negatively regulated by Byr4 and cdc16, which form a two-component GTPase activating protein (GAP) for Spg1p. The existence of a SIN-related pathway in plants has been proposed. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization.


Pssm-ID: 206701  Cd Length: 182  Bit Score: 36.22  E-value: 2.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSY-RKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:cd04128   13 KTSLMVKYVEGEFDEEYIQTLGVNFmEKTISIRGTEITFSIWDLGGQREFINMLPLVCKDAVAILFMFDLTRKSTLNSIK 92
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 194363764  95 QYREQIKRVKDSdDVPmVLVGNKCDLAARTVE------SRQAQDLARSYGIPYIETSA 146
Cdd:cd04128   93 EWYRQARGFNKT-AIP-ILVGTKYDLFADLPPeeqeeiTKQARKYAKAMKAPLIFCST 148
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
35-163 2.66e-03

Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.


Pssm-ID: 249504  Cd Length: 185  Bit Score: 35.95  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764   35 TIEDSYrkqVVIDGETCLLDILDTAGQEEYSAMrdqyMRTG----EGFLCVFAINNTKsfedIHQYRE---QIKRVKdsd 107
Cdd:pfam00009  53 TIKIAA---VSFETKKRHINIIDTPGHVDFTKE----MIRGasqaDGAILVVDAVEGV----MPQTREhllLAKTLG--- 118
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194363764  108 dVPMVLVGNKCDLA--ARTVESRQA--QDLARSYG------IPYIETSAKTRQGVEDAFYTLVREI 163
Cdd:pfam00009 119 -VPIIVFINKIDRVddAELEEIVEEisRELLKKYGeggeetVPVVPGSALTGEGIDELLEALDLYL 183
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
13-160 4.75e-03

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


Pssm-ID: 206644 [Multi-domain]  Cd Length: 158  Bit Score: 34.86  E-value: 4.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  13 GVGKSALTIQLIQNHFVDEYdPTI----EDSYRKQVVIdgetcllDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTK 88
Cdd:cd00878    9 GAGKTTILYKLKLGEVVTTI-PTIgfnvETVEYKNVKF-------TVWDVGGQDKIRPLWKHYYENTDGLIFVVDSSDRE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  89 SFEDIhqyREQIKRV---KDSDDVPMVLVGNKCDLAartvESRQAQDLARSYGIPYI--------ETSAKTRQGVEDAFY 157
Cdd:cd00878   81 RIEEA---KNELHKLlneEELKGAPLLILANKQDLP----GALTESELIELLGLESIkgrrwhiqPCSAVTGDGLDEGLD 153

                 ...
gi 194363764 158 TLV 160
Cdd:cd00878  154 WLI 156
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
108-163 7.01e-03

LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.


Pssm-ID: 206677  Cd Length: 179  Bit Score: 34.43  E-value: 7.01e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 194363764 108 DVPMVLVGNKCDLAARTVEsRQAQDLARSYGIP---YIETSAKTRQGVEDAFYTLVREI 163
Cdd:cd01890  119 NLEIIPVINKIDLPAADPD-RVKQEIEDVLGLDaseAILVSAKTGLGVEDLLEAIVERI 176
PTZ00369 PTZ00369
Ras-like protein; Provisional
1-184 4.02e-83

Ras-like protein; Provisional


Pssm-ID: 240385 [Multi-domain]  Cd Length: 189  Bit Score: 246.70  E-value: 4.02e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764   1 MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLC 80
Cdd:PTZ00369   3 STEYKLVVVGGGGVGKSALTIQFIQNHFIDEYDPTIEDSYRKQCVIDEETCLLDILDTAGQEEYSAMRDQYMRTGQGFLC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  81 VFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDL-AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTL 159
Cdd:PTZ00369  83 VYSITSRSSFEEIASFREQILRVKDKDRVPMILVGNKCDLdSERQVSTGEGQELAKSFGIPFLETSAKQRVNVDEAFYEL 162
                        170       180
                 ....*....|....*....|....*
gi 194363764 160 VREIRQHkLRKLNPPDESGPGCMSC 184
Cdd:PTZ00369 163 VREIRKY-LKEDMPSQKQKKKGGLC 186
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
16-165 7.47e-78

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: 249560 [Multi-domain]  Cd Length: 162  Bit Score: 232.40  E-value: 7.47e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764   16 KSALTIQLIQNHFVDEYDPTI-EDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:pfam00071  12 KSSLLIRFTQNKFPEEYIPTIgVDFYTKTIEVDGKTVKLQIWDTAGQERFRALRPLYYRGAQGFLLVYDITSRDSFENVK 91
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194363764   95 QYREQIKRVKDsDDVPMVLVGNKCDLAA-RTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQ 165
Cdd:pfam00071  92 KWLEEILRHAD-DNVPIVLVGNKCDLEDqRVVSTEEGEALAKELGLPFMETSAKTNENVEEAFEELAREILK 162
GTP-binding_protein_placental_isoform TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
16-161 3.26e-46

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: 151.37  E-value: 3.26e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764   16 KSALTIQLIQNH-FVDEYDPTIEDSYRKQVV-IDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINN-TKSFED 92
Cdd:TIGR00231  14 KSTLLNSLLGNKgSITEYYPGTTRNYVTTVIeEDGKTYKFNLLDTAGQEDYDAIRRLYYPQVERSLRVFDIVIlVLDVEE 93
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764   93 IHQ-YREQIKRVKDSdDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVR 161
Cdd:TIGR00231  94 ILEkQTKEIIHHADS-GVPIILVGNKIDLKDADLKTHVASEFAKLNGEPIIPLSAETGKNIDSAFKIVEA 162
COG1100 COG1100
GTPase SAR1 and related small G proteins [General function prediction only]
16-165 1.61e-25

GTPase SAR1 and related small G proteins [General function prediction only]


Pssm-ID: 224025 [Multi-domain]  Cd Length: 219  Bit Score: 98.88  E-value: 1.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYRKQ-VVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:COG1100   18 KTTLLNRLVGDEFPEGYPPTIGNLDPAKtIEPYRRNIKLQLWDTAGQEEYRSLRPEYYRGANGILIVYDSTLRESSDELT 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  95 QYREQIKRVKDSDDVPMVLVGNKCDLAARTVESR----------------QAQDLARSYGIPYIETSAK--TRQGVEDAF 156
Cdd:COG1100   98 EEWLEELRELAPDDVPILLVGNKIDLFDEQSSSEeilnqlnrevvllvlaPKAVLPEVANPALLETSAKslTGPNVNELF 177

                 ....*....
gi 194363764 157 YTLVREIRQ 165
Cdd:COG1100  178 KELLRKLLE 186
PLN03108 PLN03108
Rab family protein; Provisional
16-165 4.45e-23

Rab family protein; Provisional


Pssm-ID: 178655 [Multi-domain]  Cd Length: 210  Bit Score: 91.93  E-value: 4.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSY-RKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:PLN03108  19 KSCLLLQFTDKRFQPVHDLTIGVEFgARMITIDNKPIKLQIWDTAGQESFRSITRSYYRGAAGALLVYDITRRETFNHLA 98
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194363764  95 QYREQIKRVKDSdDVPMVLVGNKCDLA-ARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQ 165
Cdd:PLN03108  99 SWLEDARQHANA-NMTIMLIGNKCDLAhRRAVSTEEGEQFAKEHGLIFMEASAKTAQNVEEAFIKTAAKIYK 169
PLN03110 PLN03110
Rab GTPase; Provisional
16-165 4.38e-22

Rab GTPase; Provisional


Pssm-ID: 178657 [Multi-domain]  Cd Length: 216  Bit Score: 89.22  E-value: 4.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHFVDEYDPTIEDSYRKQVV-IDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:PLN03110  25 KSNILSRFTRNEFCLESKSTIGVEFATRTLqVEGKTVKAQIWDTAGQERYRAITSAYYRGAVGALLVYDITKRQTFDNVQ 104
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194363764  95 QYREQIKRVKDSDDVPMvLVGNKCDLA-ARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQ 165
Cdd:PLN03110 105 RWLRELRDHADSNIVIM-MAGNKSDLNhLRSVAEEDGQALAEKEGLSFLETSALEATNVEKAFQTILLEIYH 175
PLN03118 PLN03118
Rab family protein; Provisional
16-165 2.04e-20

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 84.72  E-value: 2.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  16 KSALTIQLIQNHfVDEYDPTIEDSYR-KQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIH 94
Cdd:PLN03118  27 KSSLLVSFISSS-VEDLAPTIGVDFKiKQLTVGGKRLKLTIWDTAGQERFRTLTSSYYRNAQGIILVYDVTRRETFTNLS 105
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194363764  95 Q-YREQIKRVKDSDDVPMVLVGNKCDL-AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQ 165
Cdd:PLN03118 106 DvWGKEVELYSTNQDCVKMLVGNKVDReSERDVSREEGMALAKEHGCLFLECSAKTRENVEQCFEELALKIME 178
PTZ00132 PTZ00132
GTP-binding nuclear protein Ran; Provisional
48-163 6.91e-18

GTP-binding nuclear protein Ran; Provisional


Pssm-ID: 240284 [Multi-domain]  Cd Length: 215  Bit Score: 77.43  E-value: 6.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  48 GETCLlDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVkdSDDVPMVLVGNKCDLAARTVES 127
Cdd:PTZ00132  56 GPICF-NVWDTAGQEKFGGLRDGYYIKGQCAIIMFDVTSRITYKNVPNWHRDIVRV--CENIPIVLVGNKVDVKDRQVKA 132
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 194363764 128 RQAQdLARSYGIPYIETSAKTRQGVEDAFYTLVREI 163
Cdd:PTZ00132 133 RQIT-FHRKKNLQYYDISAKSNYNFEKPFLWLARRL 167
RAN smart00176
Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases; Ran is involved in the ...
53-163 4.23e-13

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: 63.49  E-value: 4.23e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764    53 LDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVkdSDDVPMVLVGNKCDLAARTVESRQAQd 132
Cdd:smart00176  46 FNVWDTAGQEKFGGLRDGYYIQGQCAIIMFDVTARVTYKNVPNWHRDLVRV--CENIPIVLCGNKVDVKDRKVKAKSIT- 122
                           90       100       110
                   ....*....|....*....|....*....|.
gi 194363764   133 LARSYGIPYIETSAKTRQGVEDAFYTLVREI 163
Cdd:smart00176 123 FHRKKNLQYYDISAKSNYNFEKPFLWLARKL 153
PTZ00099 PTZ00099
rab6; Provisional
28-156 7.07e-12

rab6; Provisional


Pssm-ID: 185444 [Multi-domain]  Cd Length: 176  Bit Score: 59.76  E-value: 7.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  28 FVDEYDPTIE-DSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKdS 106
Cdd:PTZ00099   5 FDNNYQSTIGiDFLSKTLYLDEGPVRLQLWDTAGQERFRSLIPSYIRDSAAAIVVYDITNRQSFENTTKWIQDILNER-G 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 194363764 107 DDVPMVLVGNKCDLA-ARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAF 156
Cdd:PTZ00099  84 KDVIIALVGNKTDLGdLRKVTYEEGMQKAQEYNTMFHETSAKAGHNIKVLF 134
PRK00098 PRK00098
GTPase RsgA; Reviewed
108-154 3.51e-05

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 41.73  E-value: 3.51e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 194363764 108 DVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVED 154
Cdd:PRK00098 111 GIKPIIVLNKIDLLDDLEEARELLALYRAIGYDVLELSAKEGEGLDE 157
obgE PRK12299
GTPase CgtA; Reviewed
110-167 4.70e-05

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 41.59  E-value: 4.70e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 194363764 110 PMVLVGNKCD-LAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHK 167
Cdd:PRK12299 273 PRILVLNKIDlLDEEEEREKRAALELAALGGPVFLISAVTGEGLDELLRALWELLEEAR 331
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
110-166 8.65e-05

Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome GTP-binding protein that associates with ribosomal subunits and appears to play a role in ribosomal RNA maturation. This GTPase, related to the nucleolar protein Obg, is designated CgtA in bacteria. Mutations in this gene are pleiotropic, but it appears that effects on cellular functions such as chromosome partition may be secondary to the effect on ribosome structure. Recent work done in Vibrio cholerae shows an essential role in the stringent response, in which RelA-dependent ability to synthesize the alarmone ppGpp is required for deletion of this GTPase to be lethal. [Protein synthesis, Other]


Pssm-ID: 274271 [Multi-domain]  Cd Length: 328  Bit Score: 40.87  E-value: 8.65e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 194363764  110 PMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDafytLVREIRQH 166
Cdd:TIGR02729 275 PRIVVLNKIDLLDEEELEELLKELKKELGKPVFPISALTGEGLDE----LLDALAEL 327
trmE PRK05291
tRNA modification GTPase TrmE; Reviewed
98-166 1.15e-04

tRNA modification GTPase TrmE; Reviewed


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 40.48  E-value: 1.15e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194363764  98 EQIKRVKDSDDVPMVLVGNKCDLAartvesrQAQDLARSYGIPYIETSAKTRQGVEDafytLVREIRQH 166
Cdd:PRK05291 311 EDDEILEELKDKPVIVVLNKADLT-------GEIDLEEENGKPVIRISAKTGEGIDE----LREAIKEL 368
FeoB COG0370
Fe2+ transport system protein B [Inorganic ion transport and metabolism]
109-163 1.84e-04

Fe2+ transport system protein B [Inorganic ion transport and metabolism]


Pssm-ID: 223447 [Multi-domain]  Cd Length: 653  Bit Score: 39.97  E-value: 1.84e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 194363764 109 VPMVLVGNKCDLAART-VESrQAQDLARSYGIPYIETSAKTRQGVEDafytLVREI 163
Cdd:COG0370  109 IPMILALNMIDEAKKRgIRI-DIEKLSKLLGVPVVPTVAKRGEGLEE----LKRAI 159
GTP_HflX TIGR03156
GTP-binding protein HflX; This protein family is one of a number of homologous small, ...
95-153 5.53e-04

GTP-binding protein HflX; This protein family is one of a number of homologous small, well-conserved GTP-binding proteins with pleiotropic effects. Bacterial members are designated HflX, following the naming convention in Escherichia coli where HflX is encoded immediately downstream of the RNA chaperone Hfq, and immediately upstream of HflKC, a membrane-associated protease pair with an important housekeeping function. Over large numbers of other bacterial genomes, the pairing with hfq is more significant than with hflK and hlfC. The gene from Homo sapiens in this family has been named PGPL (pseudoautosomal GTP-binding protein-like). [Unknown function, General]


Pssm-ID: 274455 [Multi-domain]  Cd Length: 351  Bit Score: 38.22  E-value: 5.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194363764   95 QYREQIKRVKD------SDDVPMVLVGNKCDLaartVESRQAQDLARSYGIpYIETSAKTRQGVE 153
Cdd:TIGR03156 282 DREEQIEAVEKvleelgAEDIPQLLVYNKIDL----LDEPRIERLEEGYPE-AVFVSAKTGEGLD 341
hydrogenase_maturation_GTPase_HydF TIGR03918
[FeFe] hydrogenase H-cluster maturation GTPase HydF; This model describes the family of the ...
108-154 7.04e-04

[FeFe] hydrogenase H-cluster maturation GTPase HydF; This model describes the family of the [Fe] hydrogenase maturation protein HypF as characterized in Chlamydomonas reinhardtii and found, in an operon with radical SAM proteins HydE and HydG, in numerous bacteria. It has GTPase activity, can bind an 4Fe-4S cluster, and is essential for hydrogenase activity. [Protein fate, Protein modification and repair]


Pssm-ID: 274853 [Multi-domain]  Cd Length: 391  Bit Score: 38.26  E-value: 7.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 194363764  108 DVPMVLVGNKCDLaarTVESRQAQDLARSYGIPYIETSAKTRQGVED 154
Cdd:TIGR03918 114 KIPYIVVINKIDL---GEESAEKEKLEKKFGLPPIFVSALTGEGIDE 157
HflX COG2262
GTPases [General function prediction only]
96-166 1.30e-03

GTPases [General function prediction only]


Pssm-ID: 225171 [Multi-domain]  Cd Length: 411  Bit Score: 37.25  E-value: 1.30e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194363764  96 YREQIKRVKD------SDDVPMVLVGNKCDLAARTVESRQAQDLARsygiPYIETSAKTRQGVEdafyTLVREIRQH 166
Cdd:COG2262  286 ILEKLEAVEDvlaeigADEIPIILVLNKIDLLEDEEILAELERGSP----NPVFISAKTGEGLD----LLRERIIEL 354
obgE PRK12297
GTPase CgtA; Reviewed
110-176 1.64e-03

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 37.00  E-value: 1.64e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194363764 110 PMVLVGNKCDLAartvESRQA-QDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDE 176
Cdd:PRK12297 276 PQIVVANKMDLP----EAEENlEEFKEKLGPKVFPISALTGQGLDELLYAVAELLEETPEFPLEEEEV 339
obgE PRK12298
GTPase CgtA; Reviewed
110-166 2.67e-03

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 36.38  E-value: 2.67e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 194363764 110 PMVLVGNKCDLAARTVESRQAQDLARSYG--IPYIETSAKTRQGVEDAFYTLVREIRQH 166
Cdd:PRK12298 277 PRWLVFNKIDLLDEEEAEERAKAIVEALGweGPVYLISAASGLGVKELCWDLMTFIEEN 335
PRK04165 PRK04165
acetyl-CoA decarbonylase/synthase complex subunit gamma; Provisional
42-114 7.04e-03

acetyl-CoA decarbonylase/synthase complex subunit gamma; Provisional


Pssm-ID: 235235 [Multi-domain]  Cd Length: 450  Bit Score: 35.22  E-value: 7.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194363764  42 KQVVIDGETCL--------------LDILDTAGQEEYSA-----MRDQYMRTGEgFLCV--FAINNTKsfEDIHQYREQI 100
Cdd:PRK04165  71 RAVKIGGETVLyrhektffnptgiaVDVSDTMDDEEIDArlkkiNNFQFERVGE-ILKLdmVALRNAS--GDPEKFAKAV 147
                         90
                 ....*....|....
gi 194363764 101 KRVKDSDDVPMVLV 114
Cdd:PRK04165 148 KKVAETTDLPLILC 161
Obg COG0536
Predicted GTPase [General function prediction only]
110-179 8.98e-03

Predicted GTPase [General function prediction only]


Pssm-ID: 223610 [Multi-domain]  Cd Length: 369  Bit Score: 34.84  E-value: 8.98e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194363764 110 PMVLVGNKCDLA-ARTVESRQAQDLARSYGIPYIET-SAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGP 179
Cdd:COG0536  277 PRIVVLNKIDLPlDEEELEELKKALAEALGWEVFYLiSALTREGLDELLRALAELLEETKAEAEAAEAEELP 348
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.13
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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