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Conserved domains on  [gi|1791034378|ref|NP_001364293|]
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NF-kappa-B inhibitor-interacting Ras-like protein 1 isoform 1 [Homo sapiens]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
6-168 1.91e-40

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


The actual alignment was detected with superfamily member cd00876:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 160  Bit Score: 134.58  E-value: 1.91e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYgNHTIGMEDcETMEDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVLV 85
Cdd:cd00876     1 KLVVLGAGGVGKSALTIRFVS-GEFVEEYD-PTIEDSYRKQIVVD-GETYTLDILDTAGQEEFSAMRDQYIRNGDGFILV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  86 YSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIEPFTLLA 165
Cdd:cd00876    78 YSITSRESFEEIKNIREQILRVKDKEDVPIVLVGNKCDLENERQVSTEEGEALAEEWGCPFLETSAKTNINIDELFNTLV 157

                  ...
gi 1791034378 166 SKL 168
Cdd:cd00876   158 REI 160
 
Name Accession Description Interval E-value
Ras cd00876
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ...
6-168 1.91e-40

Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the Ras superfamily includes classical N-Ras, H-Ras, and K-Ras, as well as R-Ras, Rap, Ral, Rheb, Rhes, ARHI, RERG, Rin/Rit, RSR1, RRP22, Ras2, Ras-dva, and RGK proteins. Ras proteins regulate cell growth, proliferation and differentiation. Ras is activated by guanine nucleotide exchange factors (GEFs) that release GDP and allow GTP binding. Many RasGEFs have been identified. These are sequestered in the cytosol until activation by growth factors triggers recruitment to the plasma membrane or Golgi, where the GEF colocalizes with Ras. Active GTP-bound Ras interacts with several effector proteins: among the best characterized are the Raf kinases, phosphatidylinositol 3-kinase (PI3K), RalGEFs and NORE/MST1. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206642 [Multi-domain]  Cd Length: 160  Bit Score: 134.58  E-value: 1.91e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYgNHTIGMEDcETMEDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVLV 85
Cdd:cd00876     1 KLVVLGAGGVGKSALTIRFVS-GEFVEEYD-PTIEDSYRKQIVVD-GETYTLDILDTAGQEEFSAMRDQYIRNGDGFILV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  86 YSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIEPFTLLA 165
Cdd:cd00876    78 YSITSRESFEEIKNIREQILRVKDKEDVPIVLVGNKCDLENERQVSTEEGEALAEEWGCPFLETSAKTNINIDELFNTLV 157

                  ...
gi 1791034378 166 SKL 168
Cdd:cd00876   158 REI 160
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
6-168 5.06e-30

Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop motif with GTP_EFTU, arf and myosin_head. See pfam00009 pfam00025, pfam00063. As regards Rab GTPases, these are important regulators of vesicle formation, motility and fusion. They share a fold in common with all Ras GTPases: this is a six-stranded beta-sheet surrounded by five alpha-helices.


Pssm-ID: 425451 [Multi-domain]  Cd Length: 162  Bit Score: 107.99  E-value: 5.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYG------NHTIGmedcetmEDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFA 79
Cdd:pfam00071   1 KLVLVGDGGVGKSSLLIRFTQNkfpeeyIPTIG-------VDFYTKTIEVD-GKTVKLQIWDTAGQERFRALRPLYYRGA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  80 DGFVLVYSVNNLESFQRVELLKKEIDKFKDKkEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIE 159
Cdd:pfam00071  73 DGFLLVYDITSRDSFENVKKWVEEILRHADE-NVPIVLVGNKCDLEDQRVVSTEEGEALAKELGLPFMETSAKTNENVEE 151

                  ....*....
gi 1791034378 160 PFTLLASKL 168
Cdd:pfam00071 152 AFEELAREI 160
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
6-168 1.37e-24

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


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 94.11  E-value: 1.37e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378    6 KVVVCGLLSVGKTAILEQLLYGN------HTIGMedcetmeDVYMASVETDrGVKEQLHLYDTRGlQEG-VELPKHYFSF 78
Cdd:smart00175   2 KIILIGDSGVGKSSLLSRFTDGKfseqykSTIGV-------DFKTKTIEVD-GKRVKLQIWDTAG-QERfRSITSSYYRG 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   79 ADGFVLVYSVNNLESFQRVELLKKEIDKFKDKKeVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLI 158
Cdd:smart00175  73 AVGALLVYDITNRESFENLENWLKELREYASPN-VVIMLVGNKSDLEEQRQVSREEAEAFAEEHGLPFFETSAKTNTNVE 151
                          170
                   ....*....|
gi 1791034378  159 EPFTLLASKL 168
Cdd:smart00175 152 EAFEELAREI 161
PTZ00369 PTZ00369
Ras-like protein; Provisional
6-186 1.89e-17

Ras-like protein; Provisional


Pssm-ID: 240385 [Multi-domain]  Cd Length: 189  Bit Score: 76.06  E-value: 1.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYgNHTIGMEDcETMEDVYMASVETDRGVKeQLHLYDTRGLQEGVELPKHYFSFADGFVLV 85
Cdd:PTZ00369    7 KLVVVGGGGVGKSALTIQFIQ-NHFIDEYD-PTIEDSYRKQCVIDEETC-LLDILDTAGQEEYSAMRDQYMRTGQGFLCV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  86 YSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIEPFTLLA 165
Cdd:PTZ00369   84 YSITSRSSFEEIASFREQILRVKDKDRVPMILVGNKCDLDSERQVSTGEGQELAKSFGIPFLETSAKQRVNVDEAFYELV 163
                         170       180
                  ....*....|....*....|.
gi 1791034378 166 SKLSQPQSKSSFPLPGRKNKG 186
Cdd:PTZ00369  164 REIRKYLKEDMPSQKQKKKGG 184
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
6-164 1.47e-16

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: 73.17  E-value: 1.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLyGNHTIGMEDCETMEDVYMASVETDRGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVLV 85
Cdd:TIGR00231   3 KIVIVGHPNVGKSTLLNSLL-GNKGSITEYYPGTTRNYVTTVIEEDGKTYKFNLLDTAGQEDYDAIRRLYYPQVERSLRV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  86 YSVNNL-ESFQRVELL-KKEIDKFKDKKeVAIVVLGNKIDLsEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIEPFTL 163
Cdd:TIGR00231  82 FDIVILvLDVEEILEKqTKEIIHHADSG-VPIILVGNKIDL-KDADLKTHVASEFAKLNGEPIIPLSAETGKNIDSAFKI 159

                  .
gi 1791034378 164 L 164
Cdd:TIGR00231 160 V 160
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
6-170 3.85e-08

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 50.75  E-value: 3.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGnhTIGMEDCETME--DVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHY---FSFAD 80
Cdd:COG1100     5 KIVVVGTGGVGKTSLVNRLVGD--IFSLEKYLSTNgvTIDKKELKLD-GLDVDLVIWDTPGQDEFRETRQFYarqLTGAS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  81 GFVLVYSVNNLESFQRVELLKKEIDKFkdKKEVAIVVLGNKIDL-SEQRQVDAEVAQQWAKSEKVrlWEVTVTDRKT--- 156
Cdd:COG1100    82 LYLFVVDGTREETLQSLYELLESLRRL--GKKSPIILVLNKIDLyDEEEIEDEERLKEALSEDNI--VEVVATSAKTgeg 157
                         170
                  ....*....|....
gi 1791034378 157 LIEPFTLLASKLSQ 170
Cdd:COG1100   158 VEELFAALAEILRG 171
 
Name Accession Description Interval E-value
Ras cd00876
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ...
6-168 1.91e-40

Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the Ras superfamily includes classical N-Ras, H-Ras, and K-Ras, as well as R-Ras, Rap, Ral, Rheb, Rhes, ARHI, RERG, Rin/Rit, RSR1, RRP22, Ras2, Ras-dva, and RGK proteins. Ras proteins regulate cell growth, proliferation and differentiation. Ras is activated by guanine nucleotide exchange factors (GEFs) that release GDP and allow GTP binding. Many RasGEFs have been identified. These are sequestered in the cytosol until activation by growth factors triggers recruitment to the plasma membrane or Golgi, where the GEF colocalizes with Ras. Active GTP-bound Ras interacts with several effector proteins: among the best characterized are the Raf kinases, phosphatidylinositol 3-kinase (PI3K), RalGEFs and NORE/MST1. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206642 [Multi-domain]  Cd Length: 160  Bit Score: 134.58  E-value: 1.91e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYgNHTIGMEDcETMEDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVLV 85
Cdd:cd00876     1 KLVVLGAGGVGKSALTIRFVS-GEFVEEYD-PTIEDSYRKQIVVD-GETYTLDILDTAGQEEFSAMRDQYIRNGDGFILV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  86 YSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIEPFTLLA 165
Cdd:cd00876    78 YSITSRESFEEIKNIREQILRVKDKEDVPIVLVGNKCDLENERQVSTEEGEALAEEWGCPFLETSAKTNINIDELFNTLV 157

                  ...
gi 1791034378 166 SKL 168
Cdd:cd00876   158 REI 160
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
6-168 5.06e-30

Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop motif with GTP_EFTU, arf and myosin_head. See pfam00009 pfam00025, pfam00063. As regards Rab GTPases, these are important regulators of vesicle formation, motility and fusion. They share a fold in common with all Ras GTPases: this is a six-stranded beta-sheet surrounded by five alpha-helices.


Pssm-ID: 425451 [Multi-domain]  Cd Length: 162  Bit Score: 107.99  E-value: 5.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYG------NHTIGmedcetmEDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFA 79
Cdd:pfam00071   1 KLVLVGDGGVGKSSLLIRFTQNkfpeeyIPTIG-------VDFYTKTIEVD-GKTVKLQIWDTAGQERFRALRPLYYRGA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  80 DGFVLVYSVNNLESFQRVELLKKEIDKFKDKkEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIE 159
Cdd:pfam00071  73 DGFLLVYDITSRDSFENVKKWVEEILRHADE-NVPIVLVGNKCDLEDQRVVSTEEGEALAKELGLPFMETSAKTNENVEE 151

                  ....*....
gi 1791034378 160 PFTLLASKL 168
Cdd:pfam00071 152 AFEELAREI 160
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
8-166 7.66e-30

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: 107.54  E-value: 7.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   8 VVCGLLSVGKTAILEQLLYGNHTI--GMEDCETMEDVYMASVETDrgvKEQLHLYDTRGLQEG-----VELPKHYFSFAD 80
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLGGEVGEvsDVPGTTRDPDVYVKELDKG---KVKLVLVDTPGLDEFgglgrEELARLLLRGAD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  81 GFVLVYSVNNLESFQRVELlkkEIDKFKDKKEVAIVVLGNKIDLSEQRQVDAEV-AQQWAKSEKVRLWEVTVTDRKTLIE 159
Cdd:cd00882    78 LILLVVDSTDRESEEDAKL---LILRRLRKEGIPIILVGNKIDLLEEREVEELLrLEELAKILGVPVFEVSAKTGEGVDE 154

                  ....*..
gi 1791034378 160 PFTLLAS 166
Cdd:cd00882   155 LFEKLIE 161
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
5-166 1.63e-28

Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases form the largest family within the Ras superfamily. There are at least 60 Rab genes in the human genome, and a number of Rab GTPases are conserved from yeast to humans. Rab GTPases are small, monomeric proteins that function as molecular switches to regulate vesicle trafficking pathways. The different Rab GTPases are localized to the cytosolic face of specific intracellular membranes, where they regulate distinct steps in membrane traffic pathways. In the GTP-bound form, Rab GTPases recruit specific sets of effector proteins onto membranes. Through their effectors, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which mask C-terminal lipid binding and promote cytosolic localization. While most unicellular organisms possess 5-20 Rab members, several have been found to possess 60 or more Rabs; for many of these Rab isoforms, homologous proteins are not found in other organisms. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Since crystal structures often lack C-terminal residues, the lipid modification site is not available for annotation in many of the CDs in the hierarchy, but is included where possible.


Pssm-ID: 206640 [Multi-domain]  Cd Length: 159  Bit Score: 104.07  E-value: 1.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   5 CKVVVCGLLSVGKTAILEQLLYG------NHTIGMedcetmeDVYMASVETDrGVKEQLHLYDTRGlQE-GVELPKHYFS 77
Cdd:cd00154     1 FKIVLIGDSGVGKTSLLLRFVDNkfsenyKSTIGV-------DFKSKTIEVD-GKKVKLQIWDTAG-QErFRSITSSYYR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  78 FADGFVLVYSVNNLESFQRVELLKKEIDKFKDKKeVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTL 157
Cdd:cd00154    72 GAHGAILVYDVTNRESFENLDKWLNELKEYAPPN-IPIILVGNKSDLEDERQVSTEEAQQFAKENGLLFFETSAKTGENV 150

                  ....*....
gi 1791034378 158 IEPFTLLAS 166
Cdd:cd00154   151 DEAFESLAR 159
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
6-168 1.37e-24

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


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 94.11  E-value: 1.37e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378    6 KVVVCGLLSVGKTAILEQLLYGN------HTIGMedcetmeDVYMASVETDrGVKEQLHLYDTRGlQEG-VELPKHYFSF 78
Cdd:smart00175   2 KIILIGDSGVGKSSLLSRFTDGKfseqykSTIGV-------DFKTKTIEVD-GKRVKLQIWDTAG-QERfRSITSSYYRG 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   79 ADGFVLVYSVNNLESFQRVELLKKEIDKFKDKKeVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLI 158
Cdd:smart00175  73 AVGALLVYDITNRESFENLENWLKELREYASPN-VVIMLVGNKSDLEEQRQVSREEAEAFAEEHGLPFFETSAKTNTNVE 151
                          170
                   ....*....|
gi 1791034378  159 EPFTLLASKL 168
Cdd:smart00175 152 EAFEELAREI 161
RAS smart00173
Ras subfamily of RAS small GTPases; Similar in fold and function to the bacterial EF-Tu GTPase. ...
6-164 7.56e-24

Ras subfamily of RAS small GTPases; Similar in fold and function to the bacterial EF-Tu GTPase. p21Ras couples receptor Tyr kinases and G protein receptors to protein kinase cascades


Pssm-ID: 214541 [Multi-domain]  Cd Length: 164  Bit Score: 92.23  E-value: 7.56e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378    6 KVVVCGLLSVGKTAILEQLLYGnhtIGMEDCE-TMEDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVL 84
Cdd:smart00173   2 KLVVLGSGGVGKSALTIQFIQG---HFVDDYDpTIEDSYRKQIEID-GEVCLLDILDTAGQEEFSAMRDQYMRTGEGFLL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   85 VYSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIEPFTLL 164
Cdd:smart00173  78 VYSITDRQSFEEIKKFREQILRVKDRDDVPIVLVGNKCDLESERVVSTEEGKELARQWGCPFLETSAKERVNVDEAFYDL 157
small_GTPase smart00010
Small GTPase of the Ras superfamily; ill-defined subfamily; SMART predicts Ras-like small ...
6-164 1.40e-23

Small GTPase of the Ras superfamily; ill-defined subfamily; SMART predicts Ras-like small GTPases of the ARF, RAB, RAN, RAS, and SAR subfamilies. Others that could not be classified in this way are predicted to be members of the small GTPase superfamily without predictions of the subfamily.


Pssm-ID: 197466 [Multi-domain]  Cd Length: 166  Bit Score: 91.47  E-value: 1.40e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378    6 KVVVCGLLSVGKTAILEQLLYGnhtIGMEDCE-TMEDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVL 84
Cdd:smart00010   4 KLVVLGGGGVGKSALTIQFVQG---HFVDEYDpTIEDSYRKQIEID-GEVCLLDILDTAGQEEFSAMRDQYMRTGEGFLL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   85 VYSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIEPFTLL 164
Cdd:smart00010  80 VYSITDRQSFEEIAKFREQILRVKDRDDVPIVLVGNKCDLENERVVSTEEGKELARQWGCPFLETSAKERINVDEAFYDL 159
H_N_K_Ras_like cd04138
Ras GTPase family containing H-Ras,N-Ras and K-Ras4A/4B; H-Ras/N-Ras/K-Ras subfamily. H-Ras, ...
6-165 3.16e-21

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


Pssm-ID: 133338 [Multi-domain]  Cd Length: 162  Bit Score: 85.16  E-value: 3.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYgNHTIGMEDcETMEDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVLV 85
Cdd:cd04138     3 KLVVVGAGGVGKSALTIQLIQ-NHFVDEYD-PTIEDSYRKQVVID-GETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  86 YSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKIDLsEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIEPFTLLA 165
Cdd:cd04138    80 FAINSRKSFEDIHTYREQIKRVKDSDDVPMVLVGNKCDL-AARTVSTRQGQDLAKSYGIPYIETSAKTRQGVEEAFYTLV 158
RSR1 cd04177
RSR1/Bud1p family GTPase; RSR1/Bud1p is a member of the Rap subfamily of the Ras family that ...
6-161 1.53e-20

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


Pssm-ID: 133377 [Multi-domain]  Cd Length: 168  Bit Score: 83.69  E-value: 1.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLygnHTIGMEDCE-TMEDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVL 84
Cdd:cd04177     3 KIVVLGAGGVGKSALTVQFV---QNVFIESYDpTIEDSYRKQVEID-GRQCDLEILDTAGTEQFTAMRELYIKSGQGFLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  85 VYSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKIDLSEQRQVDAE----VAQQWAkseKVRLWEVTVTDRKTLIEP 160
Cdd:cd04177    79 VYSVTSEASLNELGELREQVLRIKDSDNVPMVLVGNKADLEDDRQVSREdgvsLSQQWG---NVPFYETSARKRTNVDEV 155

                  .
gi 1791034378 161 F 161
Cdd:cd04177   156 F 156
RalA_RalB cd04139
Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily ...
6-170 1.86e-20

Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily consists of the highly homologous RalA and RalB. Ral proteins are believed to play a crucial role in tumorigenesis, metastasis, endocytosis, and actin cytoskeleton dynamics. Despite their high sequence similarity (>80% sequence identity), nonoverlapping and opposing functions have been assigned to RalA and RalBs in tumor migration. In human bladder and prostate cancer cells, RalB promotes migration while RalA inhibits it. A Ral-specific set of GEFs has been identified that are activated by Ras binding. This RalGEF activity is enhanced by Ras binding to another of its target proteins, phosphatidylinositol 3-kinase (PI3K). Ral effectors include RLIP76/RalBP1, a Rac/cdc42 GAP, and the exocyst (Sec6/8) complex, a heterooctomeric protein complex that is involved in tethering vesicles to specific sites on the plasma membrane prior to exocytosis. In rat kidney cells, RalB is required for functional assembly of the exocyst and for localizing the exocyst to the leading edge of migrating cells. In human cancer cells, RalA is required to support anchorage-independent proliferation and RalB is required to suppress apoptosis. RalA has been shown to localize to the plasma membrane while RalB is localized to the intracellular vesicles. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206710 [Multi-domain]  Cd Length: 163  Bit Score: 83.24  E-value: 1.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGNHtigMEDCE-TMEDVYMASVeTDRGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVL 84
Cdd:cd04139     2 KVIMVGSGGVGKSALTLQFMYDEF---VEDYEpTKADSYRKKV-VLDGEEVQLNILDTAGQEDYAAIRDNYFRSGEGFLL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  85 VYSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIEPFTLL 164
Cdd:cd04139    78 VFSITDMESFTALAEFREQILRVKEDDNVPLLLVGNKCDLEDKRQVSVEEAANLAEQWGVNYVETSAKTRANVDKVFFDL 157

                  ....*.
gi 1791034378 165 ASKLSQ 170
Cdd:cd04139   158 VREIRQ 163
RheB cd04137
Ras Homolog Enriched in Brain (RheB) is a small GTPase; Rheb (Ras Homolog Enriched in Brain) ...
6-164 2.20e-20

Ras Homolog Enriched in Brain (RheB) is a small GTPase; Rheb (Ras Homolog Enriched in Brain) subfamily. Rheb was initially identified in rat brain, where its expression is elevated by seizures or by long-term potentiation. It is expressed ubiquitously, with elevated levels in muscle and brain. Rheb functions as an important mediator between the tuberous sclerosis complex proteins, TSC1 and TSC2, and the mammalian target of rapamycin (TOR) kinase to stimulate cell growth. TOR kinase regulates cell growth by controlling nutrient availability, growth factors, and the energy status of the cell. TSC1 and TSC2 form a dimeric complex that has tumor suppressor activity, and TSC2 is a GTPase activating protein (GAP) for Rheb. The TSC1/TSC2 complex inhibits the activation of TOR kinase through Rheb. Rheb has also been shown to induce the formation of large cytoplasmic vacuoles in a process that is dependent on the GTPase cycle of Rheb, but independent of the TOR kinase, suggesting Rheb plays a role in endocytic trafficking that leads to cell growth and cell-cycle progression. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins.


Pssm-ID: 206709 [Multi-domain]  Cd Length: 180  Bit Score: 83.45  E-value: 2.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGNHTIGMEdcETMEDVYMASVeTDRGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVLV 85
Cdd:cd04137     3 KIAVLGSRSVGKSSLTVQFVEGHFVESYY--PTIENTFSKII-TYKGQEYHLEIVDTAGQDEYSILPQKYSIGIHGYILV 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1791034378  86 YSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIEPFTLL 164
Cdd:cd04137    80 YSVTSRKSFEVVKVIYDKILDMLGKESVPIVLVGNKSDLHMERQVSAEEGKKLAESWGAAFLESSAKENENVEEAFELL 158
Rab21 cd04123
Rab GTPase family 21 (Rab21); The localization and function of Rab21 are not clearly defined, ...
6-169 2.53e-20

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


Pssm-ID: 133323 [Multi-domain]  Cd Length: 162  Bit Score: 83.04  E-value: 2.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGNHTIGMEdcETMEDVYMASVETDRGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVLV 85
Cdd:cd04123     2 KVVLLGEGRVGKTSLVLRYVENKFNEKHE--STTQASFFQKTVNIGGKRIDLAIWDTAGQERYHALGPIYYRDADGAILV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  86 YSVNNLESFQRVELLKKEIDKFKDKKeVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIEPFTLLA 165
Cdd:cd04123    80 YDITDADSFQKVKKWIKELKQMRGNN-ISLVIVGNKIDLERQRVVSKSEAEEYAKSVGAKHFETSAKTGKGIEELFLSLA 158

                  ....
gi 1791034378 166 SKLS 169
Cdd:cd04123   159 KRMI 162
Ras_dva cd04147
Ras - dorsal-ventral anterior localization (Ras-dva) family; Ras-dva subfamily. Ras-dva (Ras - ...
6-149 5.90e-20

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: 82.96  E-value: 5.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYgnHTIGMEDCETMEDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVLV 85
Cdd:cd04147     1 RLVFMGAAGVGKTALIQRFLY--DTFEPKHRRTVEELHSKEYEVA-GVKVTIDILDTSGSYSFPAMRKLSIQNGDAFALV 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1791034378  86 YSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKIDLSEQRQVDAE-----VAQQW-------AKSEKVRLWEV 149
Cdd:cd04147    78 YSVDDPESFEEVKRLREEILEVKEDKFVPIVVVGNKIDSLAERQVEAAdalstVELDWnngfveaSAKDNENVTEV 153
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, ...
6-161 1.28e-19

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


Pssm-ID: 133345 [Multi-domain]  Cd Length: 164  Bit Score: 81.30  E-value: 1.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLygnHTIGMEDCE-TMEDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVL 84
Cdd:cd04145     4 KLVVVGGGGVGKSALTIQFI---QSYFVTDYDpTIEDSYTKQCEID-GQWARLDILDTAGQEEFSAMREQYMRTGEGFLL 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1791034378  85 VYSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIEPF 161
Cdd:cd04145    80 VFSVTDRGSFEEVDKFHTQILRVKDRDEFPMILVGNKADLEHQRQVSREEGQELARQLKIPYIETSAKDRVNVDKAF 156
Rap2 cd04176
Rap2 family GTPase consists of Rap2a, Rap2b, and Rap2c; The Rap2 subgroup is part of the Rap ...
6-138 6.33e-19

Rap2 family GTPase consists of Rap2a, Rap2b, and Rap2c; The Rap2 subgroup is part of the Rap subfamily of the Ras family. It consists of Rap2a, Rap2b, and Rap2c. Both isoform 3 of the human mitogen-activated protein kinase kinase kinase kinase 4 (MAP4K4) and Traf2- and Nck-interacting kinase (TNIK) are putative effectors of Rap2 in mediating the activation of c-Jun N-terminal kinase (JNK) to regulate the actin cytoskeleton. In human platelets, Rap2 was shown to interact with the cytoskeleton by binding the actin filaments. In embryonic Xenopus development, Rap2 is necessary for the Wnt/beta-catenin signaling pathway. The Rap2 interacting protein 9 (RPIP9) is highly expressed in human breast carcinomas and correlates with a poor prognosis, suggesting a role for Rap2 in breast cancer oncogenesis. Rap2b, but not Rap2a, Rap2c, Rap1a, or Rap1b, is expressed in human red blood cells, where it is believed to be involved in vesiculation. A number of additional effector proteins for Rap2 have been identified, including the RalGEFs RalGDS, RGL, and Rlf, which also interact with Rap1 and Ras. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 133376 [Multi-domain]  Cd Length: 163  Bit Score: 79.50  E-value: 6.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGNHtIGMEDcETMEDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVLV 85
Cdd:cd04176     3 KVVVLGSGGVGKSALTVQFVSGTF-IEKYD-PTIEDFYRKEIEVD-SSPSVLEILDTAGTEQFASMRDLYIKNGQGFIVV 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1791034378  86 YSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKIDLSEQRQVDAE----VAQQW 138
Cdd:cd04176    80 YSLVNQQTFQDIKPMRDQIVRVKGYEKVPIILVGNKVDLESEREVSSAegraLAEEW 136
Rap1 cd04175
Rap1 family GTPase consists of Rap1a and Rap1b isoforms; The Rap1 subgroup is part of the Rap ...
6-140 1.78e-17

Rap1 family GTPase consists of Rap1a and Rap1b isoforms; The Rap1 subgroup is part of the Rap subfamily of the Ras family. It can be further divided into the Rap1a and Rap1b isoforms. In humans, Rap1a and Rap1b share 95% sequence homology, but are products of two different genes located on chromosomes 1 and 12, respectively. Rap1a is sometimes called smg p21 or Krev1 in the older literature. Rap1 proteins are believed to perform different cellular functions, depending on the isoform, its subcellular localization, and the effector proteins it binds. For example, in rat salivary gland, neutrophils, and platelets, Rap1 localizes to secretory granules and is believed to regulate exocytosis or the formation of secretory granules. Rap1 has also been shown to localize in the Golgi of rat fibroblasts, zymogen granules, plasma membrane, and the microsomal membrane of pancreatic acini, as well as in the endocytic compartment of skeletal muscle cells and fibroblasts. High expression of Rap1 has been observed in the nucleus of human oropharyngeal squamous cell carcinomas (SCCs) and cell lines; interestingly, in the SCCs, the active GTP-bound form localized to the nucleus, while the inactive GDP-bound form localized to the cytoplasm. Rap1 plays a role in phagocytosis by controlling the binding of adhesion receptors (typically integrins) to their ligands. In yeast, Rap1 has been implicated in multiple functions, including activation and silencing of transcription and maintenance of telomeres. Rap1a, which is stimulated by T-cell receptor (TCR) activation, is a positive regulator of T cells by directing integrin activation and augmenting lymphocyte responses. In murine hippocampal neurons, Rap1b determines which neurite will become the axon and directs the recruitment of Cdc42, which is required for formation of dendrites and axons. In murine platelets, Rap1b is required for normal homeostasis in vivo and is involved in integrin activation. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 133375 [Multi-domain]  Cd Length: 164  Bit Score: 75.63  E-value: 1.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGnhtIGMEDCE-TMEDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVL 84
Cdd:cd04175     3 KLVVLGSGGVGKSALTVQFVQG---IFVEKYDpTIEDSYRKQVEVD-GQQCMLEILDTAGTEQFTAMRDLYMKNGQGFVL 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1791034378  85 VYSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAK 140
Cdd:cd04175    79 VYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVGKEQGQNLAR 134
PTZ00369 PTZ00369
Ras-like protein; Provisional
6-186 1.89e-17

Ras-like protein; Provisional


Pssm-ID: 240385 [Multi-domain]  Cd Length: 189  Bit Score: 76.06  E-value: 1.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYgNHTIGMEDcETMEDVYMASVETDRGVKeQLHLYDTRGLQEGVELPKHYFSFADGFVLV 85
Cdd:PTZ00369    7 KLVVVGGGGVGKSALTIQFIQ-NHFIDEYD-PTIEDSYRKQCVIDEETC-LLDILDTAGQEEYSAMRDQYMRTGQGFLCV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  86 YSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIEPFTLLA 165
Cdd:PTZ00369   84 YSITSRSSFEEIASFREQILRVKDKDRVPMILVGNKCDLDSERQVSTGEGQELAKSFGIPFLETSAKQRVNVDEAFYELV 163
                         170       180
                  ....*....|....*....|.
gi 1791034378 166 SKLSQPQSKSSFPLPGRKNKG 186
Cdd:PTZ00369  164 REIRKYLKEDMPSQKQKKKGG 184
Rap_like cd04136
Rap-like family consists of Rap1, Rap2 and RSR1; The Rap subfamily consists of the Rap1, Rap2, ...
6-140 5.82e-17

Rap-like family consists of Rap1, Rap2 and RSR1; The Rap subfamily consists of the Rap1, Rap2, and RSR1. Rap subfamily proteins perform different cellular functions, depending on the isoform and its subcellular localization. For example, in rat salivary gland, neutrophils, and platelets, Rap1 localizes to secretory granules and is believed to regulate exocytosis or the formation of secretory granules. Rap1 has also been shown to localize in the Golgi of rat fibroblasts, zymogen granules, plasma membrane, and microsomal membrane of the pancreatic acini, as well as in the endocytic compartment of skeletal muscle cells and fibroblasts. Rap1 localizes in the nucleus of human oropharyngeal squamous cell carcinomas (SCCs) and cell lines. Rap1 plays a role in phagocytosis by controlling the binding of adhesion receptors (typically integrins) to their ligands. In yeast, Rap1 has been implicated in multiple functions, including activation and silencing of transcription and maintenance of telomeres. Rap2 is involved in multiple functions, including activation of c-Jun N-terminal kinase (JNK) to regulate the actin cytoskeleton and activation of the Wnt/beta-catenin signaling pathway in embryonic Xenopus. A number of effector proteins for Rap2 have been identified, including isoform 3 of the human mitogen-activated protein kinase kinase kinase kinase 4 (MAP4K4) and Traf2- and Nck-interacting kinase (TNIK), and the RalGEFs RalGDS, RGL, and Rlf, which also interact with Rap1 and Ras. RSR1 is the fungal homolog of Rap1 and Rap2. In budding yeasts, it is involved in selecting a site for bud growth, which directs the establishment of cell polarization. The Rho family GTPase Cdc42 and its GEF, Cdc24, then establish an axis of polarized growth. It is believed that Cdc42 interacts directly with RSR1 in vivo. In filamentous fungi such as Ashbya gossypii, RSR1 is a key regulator of polar growth in the hypha. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206708 [Multi-domain]  Cd Length: 164  Bit Score: 74.13  E-value: 5.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGnhtIGMEDCE-TMEDVYMASVETDRGVKEqLHLYDTRGLQEGVELPKHYFSFADGFVL 84
Cdd:cd04136     3 KLVVLGSGGVGKSALTVQFVQG---IFVDKYDpTIEDSYRKQIEVDCQQCM-LEILDTAGTEQFTAMRDLYIKNGQGFAL 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  85 VYSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKIDLSEQRQVDAE----VAQQWAK 140
Cdd:cd04136    79 VYSITAQQSFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVSKEegqnLARQWGN 138
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
6-164 1.47e-16

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: 73.17  E-value: 1.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLyGNHTIGMEDCETMEDVYMASVETDRGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVLV 85
Cdd:TIGR00231   3 KIVIVGHPNVGKSTLLNSLL-GNKGSITEYYPGTTRNYVTTVIEEDGKTYKFNLLDTAGQEDYDAIRRLYYPQVERSLRV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  86 YSVNNL-ESFQRVELL-KKEIDKFKDKKeVAIVVLGNKIDLsEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIEPFTL 163
Cdd:TIGR00231  82 FDIVILvLDVEEILEKqTKEIIHHADSG-VPIILVGNKIDL-KDADLKTHVASEFAKLNGEPIIPLSAETGKNIDSAFKI 159

                  .
gi 1791034378 164 L 164
Cdd:TIGR00231 160 V 160
Rab18 cd01863
Rab GTPase family 18 (Rab18); Rab18 subfamily. Mammalian Rab18 is implicated in endocytic ...
6-140 2.00e-16

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


Pssm-ID: 206656 [Multi-domain]  Cd Length: 161  Bit Score: 72.73  E-value: 2.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAIL---------EQLLygnHTIGMedcetmeDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYF 76
Cdd:cd01863     2 KILLIGDSGVGKSSLLlrftddtfdEDLS---STIGV-------DFKVKTVTVD-GKKVKLAIWDTAGQERFRTLTSSYY 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1791034378  77 SFADGFVLVYSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKIDLsEQRQVDAEVAQQWAK 140
Cdd:cd01863    71 RGAQGVILVYDVTRRDTFDNLDTWLNELDTYSTNPDAVKMLVGNKIDK-ENREVTREEGQKFAR 133
Rab6 cd01861
Rab GTPase family 6 (Rab6); Rab6 is involved in microtubule-dependent transport pathways ...
5-168 2.98e-16

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


Pssm-ID: 206654 [Multi-domain]  Cd Length: 161  Bit Score: 72.27  E-value: 2.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   5 CKVVVCGLLSVGKTAILEQLLYgnhtigmedcETMEDVYMASVETD--------RGVKEQLHLYDTRGLQEGVELPKHYF 76
Cdd:cd01861     1 HKLVFLGDQSVGKTSIITRFMY----------DTFDNQYQATIGIDflsktmyvDDKTVRLQLWDTAGQERFRSLIPSYI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  77 SFADGFVLVYSVNNLESFQRVEllkKEIDKFKDKK--EVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDR 154
Cdd:cd01861    71 RDSSVAVVVYDITNRQSFDNTD---KWIDDVRDERgnDVIIVLVGNKTDLSDKRQVSTEEGEKKAKENNAMFIETSAKAG 147
                         170
                  ....*....|....
gi 1791034378 155 KTLIEPFTLLASKL 168
Cdd:cd01861   148 HNVKQLFKKIAQAL 161
Rhes_like cd04143
Ras homolog enriched in striatum (Rhes) and activator of G-protein signaling 1 (Dexras1/AGS1); ...
6-166 7.06e-16

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: 72.86  E-value: 7.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGNHTIGMEdcETMEDvYMASVETDRGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVLV 85
Cdd:cd04143     2 RMVVLGASKVGKTAIVSRFLGGRFEEQYT--PTIED-FHRKLYSIRGEVYQLDILDTSGNHPFPAMRRLSILTGDVFILV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  86 YSVNNLESFQRVELLKKEI--------DKFKDKKEVAIVVLGNKIDLSEQRQVDA-EVAQQWAKSEKVRLWEVTVTDRKT 156
Cdd:cd04143    79 FSLDNRESFEEVCRLREQIletksclkNKTKENVKIPMVICGNKADRDFPREVQRdEVEQLVGGDENCAYFEVSAKKNSN 158
                         170
                  ....*....|
gi 1791034378 157 LIEPFTLLAS 166
Cdd:cd04143   159 LDEMFRALFS 168
Rab7 cd01862
Rab GTPase family 7 (Rab7); Rab7 subfamily. Rab7 is a small Rab GTPase that regulates ...
6-141 1.18e-15

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


Pssm-ID: 206655 [Multi-domain]  Cd Length: 172  Bit Score: 70.77  E-value: 1.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQllYGNHTigmedcetMEDVYMASVETDRGVKE--------QLHLYDTRGLQEGVELPKHYFS 77
Cdd:cd01862     2 KVIILGDSGVGKTSLMNQ--YVNKK--------FSNQYKATIGADFLTKEvtvddrlvTLQIWDTAGQERFQSLGVAFYR 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1791034378  78 FADGFVLVYSVNNLESFQRVELLKKEIDK---FKDKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKS 141
Cdd:cd01862    72 GADCCVLVYDVTNPKSFESLDSWRDEFLIqasPRDPENFPFVVLGNKIDLEEKRQVSTKKAQQWCKS 138
Ras2 cd04144
Rat sarcoma (Ras) family 2 of small guanosine triphosphatases (GTPases); The Ras2 subfamily, ...
6-186 1.22e-15

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


Pssm-ID: 133344 [Multi-domain]  Cd Length: 190  Bit Score: 71.42  E-value: 1.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYgNHTIGMEDcETMEDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVLV 85
Cdd:cd04144     1 KLVVLGDGGVGKTALTIQLCL-NHFVETYD-PTIEDSYRKQVVVD-GQPCMLEVLDTAGQEEYTALRDQWIREGEGFILV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  86 YSVNNLESFQRVELLKKEIDKFKDKKE--VAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIEPFTL 163
Cdd:cd04144    78 YSITSRSTFERVERFREQIQRVKDESAadVPIMIVGNKCDKVYEREVSTEEGAALARRLGCEFIEASAKTNVNVERAFYT 157
                         170       180
                  ....*....|....*....|...
gi 1791034378 164 LASKLSQPQSKSSFPLPGRKNKG 186
Cdd:cd04144   158 LVRALRQQRQGGQGPKGGPTKKK 180
Rit_Rin_Ric cd04141
Ras-like protein in all tissues (Rit), Ras-like protein in neurons (Rin) and Ras-related ...
6-176 2.88e-15

Ras-like protein in all tissues (Rit), Ras-like protein in neurons (Rin) and Ras-related protein which interacts with calmodulin (Ric); Rit (Ras-like protein in all tissues), Rin (Ras-like protein in neurons) and Ric (Ras-related protein which interacts with calmodulin) form a subfamily with several unique structural and functional characteristics. These proteins all lack a the C-terminal CaaX lipid-binding motif typical of Ras family proteins, and Rin and Ric contain calmodulin-binding domains. Rin, which is expressed only in neurons, induces neurite outgrowth in rat pheochromocytoma cells through its association with calmodulin and its activation of endogenous Rac/cdc42. Rit, which is ubiquitously expressed in mammals, inhibits growth-factor withdrawl-mediated apoptosis and induces neurite extension in pheochromocytoma cells. Rit and Rin are both able to form a ternary complex with PAR6, a cell polarity-regulating protein, and Rac/cdc42. This ternary complex is proposed to have physiological function in processes such as tumorigenesis. Activated Ric is likely to signal in parallel with the Ras pathway or stimulate the Ras pathway at some upstream point, and binding of calmodulin to Ric may negatively regulate Ric activity.


Pssm-ID: 206712 [Multi-domain]  Cd Length: 172  Bit Score: 69.88  E-value: 2.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLygNHTIGMEDCETMEDVYMASVETDRGvKEQLHLYDTRGLQEGVELPKHYFSFADGFVLV 85
Cdd:cd04141     4 KIVMLGAGGVGKSAVTMQFI--SHSFPDYHDPTIEDAYKTQARIDNE-PALLDILDTAGQAEFTAMRDQYMRCGEGFIIC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  86 YSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIEPFTLLA 165
Cdd:cd04141    81 YSVTDRHSFQEASEFKELITRVRLTEDIPLVLVGNKVDLEQQRQVTTEEGRNLAREFNCPFFETSAALRFYIDDAFHGLV 160
                         170
                  ....*....|.
gi 1791034378 166 SKLSQPQSKSS 176
Cdd:cd04141   161 REIRRKESMPA 171
Rab15 cd04117
Rab GTPase family 15 (Rab15); Rab15 colocalizes with the transferrin receptor in early ...
6-170 4.67e-15

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


Pssm-ID: 206698 [Multi-domain]  Cd Length: 164  Bit Score: 69.24  E-value: 4.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAIL----EQLLYGNH--TIGMedcetmeDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFA 79
Cdd:cd04117     2 RLLLIGDSGVGKTCLLcrftDNEFHSSHisTIGV-------DFKMKTIEVD-GIKVRIQIWDTAGQERYQTITKQYYRRA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  80 DGFVLVYSVNNLESFQRVELLKKEIDKFKDKKeVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIE 159
Cdd:cd04117    74 QGIFLVYDISSERSYQHIMKWVSDVDEYAPEG-VQKILIGNKADEEQKRQVGDEQGNKLAKEYGMDFFETSACTNKNIKE 152
                         170
                  ....*....|.
gi 1791034378 160 PFTLLASKLSQ 170
Cdd:cd04117   153 SFTRLTELVLQ 163
Rab19 cd01864
Rab GTPase family 19 (Rab19); Rab19 subfamily. Rab19 proteins are associated with Golgi stacks. ...
6-168 1.17e-14

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


Pssm-ID: 133267 [Multi-domain]  Cd Length: 165  Bit Score: 68.23  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGN------HTIGMedcetmeDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFA 79
Cdd:cd01864     5 KIILIGDSNVGKTCVVQRFKSGTfserqgNTIGV-------DFTMKTLEIQ-GKRVKLQIWDTAGQERFRTITQSYYRSA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  80 DGFVLVYSVNNLESFQRVELLKKEIDKFKdKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKS-EKVRLWEVTVTDRKTLI 158
Cdd:cd01864    77 NGAIIAYDITRRSSFESVPHWIEEVEKYG-ASNVVLLLIGNKCDLEEQREVLFEEACTLAEHyGILAVLETSAKESSNVE 155
                         170
                  ....*....|
gi 1791034378 159 EPFTLLASKL 168
Cdd:cd01864   156 EAFLLMATEL 165
Rab33B_Rab33A cd04115
Rab GTPase family 33 includes Rab33A and Rab33B; Rab33B/Rab33A subfamily. Rab33B is ...
6-170 1.50e-14

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


Pssm-ID: 133315 [Multi-domain]  Cd Length: 170  Bit Score: 67.85  E-value: 1.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGNH------TIGMedcetmeDVYMASVETDrGVKEQLHLYDTRGlQEGVE--LPKHYFS 77
Cdd:cd04115     4 KIIVIGDSNVGKTCLTYRFCAGRFperteaTIGV-------DFRERTVEID-GERIKVQLWDTAG-QERFRksMVQHYYR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  78 FADGFVLVYSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKT- 156
Cdd:cd04115    75 NVHAVVFVYDVTNMASFHSLPSWIEECEQHSLPNEVPRILVGNKCDLREQIQVPTDLAQRFADAHSMPLFETSAKDPSEn 154
                         170
                  ....*....|....*.
gi 1791034378 157 --LIEPFTLLASKLSQ 170
Cdd:cd04115   155 dhVEAIFMTLAHKLKS 170
Rab23_like cd04106
Rab GTPase family 23 (Rab23)-like; Rab23-like subfamily. Rab23 is a member of the Rab family ...
6-167 1.59e-14

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


Pssm-ID: 133306 [Multi-domain]  Cd Length: 162  Bit Score: 67.85  E-value: 1.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYG------NHTIGMEDCEtmEDVYMASVETDrgVKeqLHLYDTRGLQEGVELPKHYFSFA 79
Cdd:cd04106     2 KVIVVGNGNVGKSSMIQRFVKGiftkdyKKTIGVDFLE--KQIFLRQSDED--VR--LMLWDTAGQEEFDAITKAYYRGA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  80 DGFVLVYSVNNLESFQRVELLKKEIDKfkDKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIE 159
Cdd:cd04106    76 QACILVFSTTDRESFEAIESWKEKVEA--ECGDIPMVLVQTKIDLLDQAVITNEEAEALAKRLQLPLFRTSVKDDFNVTE 153

                  ....*...
gi 1791034378 160 PFTLLASK 167
Cdd:cd04106   154 LFEYLAEK 161
RERG_RasL11_like cd04146
Ras-related and Estrogen-Regulated Growth inhibitor (RERG) and Ras-like 11 (RasL11)-like ...
6-151 2.41e-14

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


Pssm-ID: 206713 [Multi-domain]  Cd Length: 166  Bit Score: 67.30  E-value: 2.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLygnhT---IGmEDCETMEDVYMASVETDrgvKEQLHL--YDTRGLQ--EGVELPKHYFSF 78
Cdd:cd04146     1 KIAVLGASGVGKSALTVRFL----TkrfIG-EYEPNLESLYSRQVTID---GEQVSLeiQDTPGQQqnEDPESLERSLRW 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1791034378  79 ADGFVLVYSVNNLESFQRVELLKKEIDKFK-DKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTV 151
Cdd:cd04146    73 ADGFVLVYSITDRSSFDVVSQLLQLIREIKkRDGEIPVILVGNKADLLHSRQVSTEEGQKLALELGCLFFEVSA 146
Rab30 cd04114
Rab GTPase family 30 (Rab30); Rab30 subfamily. Rab30 appears to be associated with the Golgi ...
6-168 2.70e-14

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


Pssm-ID: 133314 [Multi-domain]  Cd Length: 169  Bit Score: 67.23  E-value: 2.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYG------NHTIGMedcetmeDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFA 79
Cdd:cd04114     9 KIVLIGNAGVGKTCLVRRFTQGlfppgqGATIGV-------DFMIKTVEIK-GEKIKLQIWDTAGQERFRSITQSYYRSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  80 DGFVLVYSVNNLESFQRVELLKKEIDKFKDKKEVAIVVlGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIE 159
Cdd:cd04114    81 NALILTYDITCEESFRCLPEWLREIEQYANNKVITILV-GNKIDLAERREVSQQRAEEFSDAQDMYYLETSAKESDNVEK 159

                  ....*....
gi 1791034378 160 PFTLLASKL 168
Cdd:cd04114   160 LFLDLACRL 168
Rab39 cd04111
Rab GTPase family 39 (Rab39); Found in eukaryotes, Rab39 is mainly found in epithelial cell ...
6-165 3.20e-14

Rab GTPase family 39 (Rab39); Found in eukaryotes, Rab39 is mainly found in epithelial cell lines, but is distributed widely in various human tissues and cell lines. It is believed to be a novel Rab protein involved in regulating Golgi-associated vesicular transport during cellular endocytosis. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins.


Pssm-ID: 133311 [Multi-domain]  Cd Length: 211  Bit Score: 67.86  E-value: 3.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGNH------TIGMedcetmeDVYMASVETDRGVKEQLHLYDTRGLQEGVELPKHYFSFA 79
Cdd:cd04111     4 RLIVIGDSTVGKSSLLKRFTEGRFaevsdpTVGV-------DFFSRLIEIEPGVRIKLQLWDTAGQERFRSITRSYYRNS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  80 DGFVLVYSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIE 159
Cdd:cd04111    77 VGVLLVFDITNRESFEHVHDWLEEARSHIQPHRPVFILVGHKCDLESQRQVTREEAEKLAKDLGMKYIETSARTGDNVEE 156

                  ....*.
gi 1791034378 160 PFTLLA 165
Cdd:cd04111   157 AFELLT 162
Rab9 cd04116
Rab GTPase family 9 (Rab9); Rab9 is found in late endosomes, together with mannose 6-phosphate ...
6-144 2.45e-13

Rab GTPase family 9 (Rab9); Rab9 is found in late endosomes, together with mannose 6-phosphate receptors (MPRs) and the tail-interacting protein of 47 kD (TIP47). Rab9 is a key mediator of vesicular transport from late endosomes to the trans-Golgi network (TGN) by redirecting the MPRs. Rab9 has been identified as a key component for the replication of several viruses, including HIV1, Ebola, Marburg, and measles, making it a potential target for inhibiting a variety of viruses. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206697 [Multi-domain]  Cd Length: 170  Bit Score: 64.89  E-value: 2.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGN------HTIGMEdcetmedVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFA 79
Cdd:cd04116     7 KVILLGDGGVGKSSLMNRYVTNKfdtqlfHTIGVE-------FLNKDLEVD-GHFVTLQIWDTAGQERFRSLRTPFYRGS 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1791034378  80 DGFVLVYSVNNLESFQRVELLKKEIDKFKDKKEV---AIVVLGNKIDLsEQRQVDAEVAQQWAKSEKV 144
Cdd:cd04116    79 DCCLLTFSVDDSQSFQNLSNWKKEFIYYADVKEPesfPFVILGNKIDI-PERQVSTEEAQAWCRDNGD 145
Rab4 cd04113
Rab GTPase family 4 (Rab4); Rab4 subfamily. Rab4 has been implicated in numerous functions ...
6-168 9.00e-13

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


Pssm-ID: 206696 [Multi-domain]  Cd Length: 161  Bit Score: 63.22  E-value: 9.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYG------NHTIGMEDCETMEDVymasveTDRGVKeqLHLYDTRGLQEGVELPKHYFSFA 79
Cdd:cd04113     2 KFLIIGSAGTGKSCLLHQFIENkfkqdsNHTIGVEFGSRVVNV------GGKSVK--LQIWDTAGQERFRSVTRSYYRGA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  80 DGFVLVYSVNNLESFQRVEllkkeiDKFKDKKEVA-----IVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDR 154
Cdd:cd04113    74 AGALLVYDITSRESFNALT------NWLTDARTLAspdivIILVGNKKDLEDDREVTFLEASRFAQENGLLFLETSALTG 147
                         170
                  ....*....|....
gi 1791034378 155 KTLIEPFTLLASKL 168
Cdd:cd04113   148 ENVEEAFLKCARSI 161
RJL cd04119
Rab GTPase family J-like (RabJ-like); RJLs are found in many protists and as chimeras with ...
6-149 9.98e-13

Rab GTPase family J-like (RabJ-like); RJLs are found in many protists and as chimeras with C-terminal DNAJ domains in deuterostome metazoa. They are not found in plants, fungi, and protostome metazoa, suggesting a horizontal gene transfer between protists and deuterostome metazoa. RJLs lack any known membrane targeting signal and contain a degenerate phosphate/magnesium-binding 3 (PM3) motif, suggesting an impaired ability to hydrolyze GTP. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization.


Pssm-ID: 133319 [Multi-domain]  Cd Length: 168  Bit Score: 63.14  E-value: 9.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGNHTIGmedcetmedvYMASVETDRGVKE--------QLHLYDTRGLQEGVELPKHYFS 77
Cdd:cd04119     2 KVISMGNSGVGKSCIIKRYCEGRFVSK----------YLPTIGIDYGVKKvsvrnkevRVNFFDLSGHPEYLEVRNEFYK 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1791034378  78 FADGFVLVYSVNNLESFQRVELLKKEIDKF----KDKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEV 149
Cdd:cd04119    72 DTQGVLLVYDVTDRQSFEALDSWLKEMKQEggphGNMENIVVVVCANKIDLTKHRAVSEDEGRLWAESKGFKYFET 147
ARHI_like cd04140
A Ras homolog member I (ARHI); ARHI (A Ras homolog member I) is a member of the Ras family ...
6-164 1.85e-12

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


Pssm-ID: 206711 [Multi-domain]  Cd Length: 165  Bit Score: 62.15  E-value: 1.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGNHTigMEDCETMEDVYMASVETDRGVKeQLHLYDTRGLQEGVELPKHYFSFADGFVLV 85
Cdd:cd04140     3 RVVVFGAGGVGKSSLVLRFVKGTFR--ESYIPTIEDTYRQVISCSKSIC-TLQITDTTGSHQFPAMQRLSISKGHAFILV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  86 YSVNNLESFQRVELLKKEIDKFK--DKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIEPFTL 163
Cdd:cd04140    80 YSITSKQSLEELKPIYELICEIKgnNLEKIPIMLVGNKCDESPSREVSSSEGAALARTWNCAFMETSAKTNHNVQELFQE 159

                  .
gi 1791034378 164 L 164
Cdd:cd04140   160 L 160
Rab1_Ypt1 cd01869
Rab GTPase family 1 includes the yeast homolog Ypt1; Rab1/Ypt1 subfamily. Rab1 is found in ...
6-168 2.04e-12

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: 62.35  E-value: 2.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGNH------TIGMedcetmeDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFA 79
Cdd:cd01869     4 KLLLIGDSGVGKSCLLLRFADDTYtesyisTIGV-------DFKIRTIELD-GKTVKLQIWDTAGQERFRTITSSYYRGA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  80 DGFVLVYSVNNLESFQRVELLKKEIDKFKDkKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIE 159
Cdd:cd01869    76 HGIIIVYDVTDQESFNNVKQWLQEIDRYAS-ENVNKLLVGNKCDLTDKKVVDYTEAKEFADELGIPFLETSAKNATNVEE 154

                  ....*....
gi 1791034378 160 PFTLLASKL 168
Cdd:cd01869   155 AFMTMAREI 163
Rab28 cd04109
Rab GTPase family 28 (Rab28); Rab28 subfamily. First identified in maize, Rab28 has been shown ...
6-141 2.14e-12

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: 62.89  E-value: 2.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILE---QLLYG---NHTIGMedcetmeDVYMASVETDRGVKEQLHLYDTRGLQEGVELPKHYFSFA 79
Cdd:cd04109     2 KIVVLGDGASGKTSLIRrfaQEGFGksyKQTIGL-------DFFSRRITLPGSLNVTLQVWDIGGQQIGGKMLDKYIYGA 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1791034378  80 DGFVLVYSVNNLESFQRVELLKKEIDKFKDKKE--VAIVVLGNKIDLSEQRQVDAEVAQQWAKS 141
Cdd:cd04109    75 QAVCLVYDITNSQSFENLEDWLSVVKKVNEESEtkPKMVLVGNKTDLEHNRQVTAEKHARFAQE 138
RabL4 cd04101
Rab GTPase-like family 4 (Rab-like4); RabL4 (Rab-like4) subfamily. RabL4s are novel proteins ...
6-165 3.04e-12

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


Pssm-ID: 206688 [Multi-domain]  Cd Length: 167  Bit Score: 61.77  E-value: 3.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLlygnHTIGMedceTMEDVYMASVETDRGVKE----------QLHLYDTRGLQEGVELPKHY 75
Cdd:cd04101     2 QCAVVGDPAVGKSALVQMF----HSDGA----TFQKNYTMTTGCDLVVKTvpvpdtsdsvELFIFDSAGQELFSDMVENV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  76 FSFADGFVLVYSVNNLESFqrvELLKKEIDKFK---DKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVT 152
Cdd:cd04101    74 WEQPAVVCVVYDVTNEVSF---NNCSRWINRVRthsHGLHTPGVLVGNKCDLTDRREVDAAQAQALAQANTLKFYETSAK 150
                         170
                  ....*....|...
gi 1791034378 153 DRKTLIEPFTLLA 165
Cdd:cd04101   151 EGVGYEAPFLSLA 163
Rab12 cd04120
Rab GTPase family 12 (Rab12); Rab12 was first identified in canine cells, where it was ...
6-164 9.10e-12

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


Pssm-ID: 206699 [Multi-domain]  Cd Length: 202  Bit Score: 61.18  E-value: 9.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQllYGNHTIgMEDCETME--DVYMASVETdRGVKEQLHLYDTRGLQEGVELPKHYFSFADGFV 83
Cdd:cd04120     2 QVIIIGSRGVGKTSLMER--FTDDTF-CEACKSTVgvDFKIKTVEL-RGKKIRLQIWDTAGQERFNSITSAYYRSAKGII 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  84 LVYSVNNLESFQRVELLKKEIDKFKdKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKS-EKVRLWEVTVTDRKTLIEPFT 162
Cdd:cd04120    78 LVYDITKKETFDDLPKWMKMIDKYA-SEDAELLLVGNKLDCETDREITRQQGEKFAQQiTGMRFCEASAKDNFNVDEIFL 156

                  ..
gi 1791034378 163 LL 164
Cdd:cd04120   157 KL 158
Rab40 cd04121
Rab GTPase family 40 (Rab40) contains Rab40a, Rab40b and Rab40c; The Rab40 subfamily contains ...
6-165 9.43e-12

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: 60.72  E-value: 9.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGNHTIGMEDCetMEDVYMASVETDRGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVLV 85
Cdd:cd04121     8 KFLLVGDSDVGKGEILASLQDGSTESPYGYN--MGIDYKTTTILLDGRRVKLQLWDTSGQGRFCTIFRSYSRGAQGIILV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  86 YSVNNLESFQRVELLKKEIDkfKDKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIEPFTLLA 165
Cdd:cd04121    86 YDITNRWSFDGIDRWIKEID--EHAPGVPKILVGNRLHLAFKRQVATEQAQAYAERNGMTFFEVSPLCNFNITESFTELA 163
RGK cd04148
Rem, Rem2, Rad, Gem/Kir (RGK) subfamily of Ras GTPases; RGK subfamily. The RGK (Rem, Rem2, Rad, ...
6-141 1.55e-11

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: 60.88  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGNHtiGMEDCETM-EDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVL 84
Cdd:cd04148     2 RVVLLGDSGVGKSSLANIFTAGVY--EDSAYEASgDDTYERTVSVD-GEEATLVVYDHWEQEDGMWLEDSCMQVGDAYVI 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1791034378  85 VYSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKS 141
Cdd:cd04148    79 VYSVTDRSSFEKASELRIQLRRARQAEDIPIILVGNKSDLVRSREVSVQEGRACAVV 135
Rab5_related cd01860
Rab-related GTPase family includes Rab5 and Rab22; regulates early endosome fusion; The ...
6-168 3.65e-11

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


Pssm-ID: 206653 [Multi-domain]  Cd Length: 163  Bit Score: 58.72  E-value: 3.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLL------YGNHTIGMedcetmedVYMASVET--DRGVKeqLHLYDTRGlQEGVE-LPKHYF 76
Cdd:cd01860     3 KLVLLGDSSVGKSSIVLRFVknefseNQESTIGA--------AFLTQTVNldDTTVK--FEIWDTAG-QERYRsLAPMYY 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  77 SFADGFVLVYSVNNLESFQRVELLKKEIdKFKDKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKT 156
Cdd:cd01860    72 RGAAAAIVVYDITSEESFEKAKSWVKEL-QEHGPPNIVIALAGNKADLESKRQVSTEEAQEYADENGLLFMETSAKTGEN 150
                         170
                  ....*....|..
gi 1791034378 157 LIEPFTLLASKL 168
Cdd:cd01860   151 VNELFTEIARKL 162
Rab8_Rab10_Rab13_like cd01867
Rab GTPase families 8, 10, 13 (Rab8, Rab10, Rab13); Rab8/Sec4/Ypt2 are known or suspected to ...
6-165 4.13e-11

Rab GTPase families 8, 10, 13 (Rab8, Rab10, Rab13); Rab8/Sec4/Ypt2 are known or suspected to be involved in post-Golgi transport to the plasma membrane. It is likely that these Rabs have functions that are specific to the mammalian lineage and have no orthologs in plants. Rab8 modulates polarized membrane transport through reorganization of actin and microtubules, induces the formation of new surface extensions, and has an important role in directed membrane transport to cell surfaces. The Ypt2 gene of the fission yeast Schizosaccharomyces pombe encodes a member of the Ypt/Rab family of small GTP-binding proteins, related in sequence to Sec4p of Saccharomyces cerevisiae but closer to mammalian Rab8. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206659 [Multi-domain]  Cd Length: 167  Bit Score: 58.82  E-value: 4.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAIL----EQLLYGNH--TIGMedcetmeDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFA 79
Cdd:cd01867     5 KLLLIGDSGVGKSCLLlrfsEDSFNPSFisTIGI-------DFKIRTIELD-GKKIKLQIWDTAGQERFRTITTSYYRGA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  80 DGFVLVYSVNNLESFQRVELLKKEIDKFKDKkEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIE 159
Cdd:cd01867    77 MGIILVYDITDEKSFENIKNWMRNIDEHASE-DVERMLVGNKCDMEEKRVVSKEEGEALAREYGIKFLETSAKANINVEE 155

                  ....*.
gi 1791034378 160 PFTLLA 165
Cdd:cd01867   156 AFLTLA 161
Rab35 cd04110
Rab GTPase family 35 (Rab35); Rab35 is one of several Rab proteins to be found to participate ...
6-175 4.37e-11

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


Pssm-ID: 133310 [Multi-domain]  Cd Length: 199  Bit Score: 59.10  E-value: 4.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAIL----EQLLYGNH--TIGMedcetmeDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFA 79
Cdd:cd04110     8 KLLIIGDSGVGKSSLLlrfaDNTFSGSYitTIGV-------DFKIRTVEIN-GERVKLQIWDTAGQERFRTITSTYYRGT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  80 DGFVLVYSVNNLESFQRVELLKKEIDKFKDkkEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIE 159
Cdd:cd04110    80 HGVIVVYDVTNGESFVNVKRWLQEIEQNCD--DVCKVLVGNKNDDPERKVVETEDAYKFAGQMGISLFETSAKENINVEE 157
                         170       180
                  ....*....|....*....|.
gi 1791034378 160 PFT-----LLASKLSQPQSKS 175
Cdd:cd04110   158 MFNcitelVLRAKKDNLAKQQ 178
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
6-123 4.56e-11

Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial Rho proteins (Miro-1, and Miro-2) and atypical Rho GTPases. Full-length proteins have a unique domain organization, with tandem GTP-binding domains and two EF hand domains (pfam00036) that may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis.


Pssm-ID: 462490 [Multi-domain]  Cd Length: 114  Bit Score: 57.13  E-value: 4.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGNH------TIGMedcetmeDVYMASVET--DRGVKEQLHLYDTRGLQEGVELPKHYFS 77
Cdd:pfam08477   1 KVVLLGDSGVGKTSLLKRFVDDTFdpkyksTIGV-------DFKTKTVLEndDNGKKIKLNIWDTAGQERFRSLHPFYYR 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1791034378  78 FADGFVLVYsvnNLESFQRVELLKKEIDKFKDKkeVAIVVLGNKID 123
Cdd:pfam08477  74 GAAAALLVY---DSRTFSNLKYWLRELKKYAGN--SPVILVGNKID 114
RRP22 cd04142
Ras-related protein on chromosome 22 (RRP22) family; RRP22 (Ras-related protein on chromosome ...
6-145 1.18e-10

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


Pssm-ID: 133342 [Multi-domain]  Cd Length: 198  Bit Score: 57.95  E-value: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGNHTigmEDCETME--DVYMASVETDRGVKEqLHLYD--------TRGLQEGVELPKHY 75
Cdd:cd04142     2 RVAVLGAPGVGKTAIVRQFLAQEFP---EEYIPTEhrRLYRPAVVLSGRVYD-LHILDvpnmqrypGTAGQEWMDPRFRG 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1791034378  76 FSFADGFVLVYSVNNLESFQRVELLKKEI--DKFKDKKEVAIVVLGNKIDLSEQRqvdaeVAQQWAKSEKVR 145
Cdd:cd04142    78 LRNSRAFILVYDICSPDSFHYVKLLRQQIleTRPAGNKEPPIVVVGNKRDQQRHR-----FAPRHVLSVLVR 144
Rho cd00157
Ras homology family (Rho) of small guanosine triphosphatases (GTPases); Members of the Rho ...
5-124 1.21e-10

Ras homology family (Rho) of small guanosine triphosphatases (GTPases); Members of the Rho (Ras homology) family include RhoA, Cdc42, Rac, Rnd, Wrch1, RhoBTB, and Rop. There are 22 human Rho family members identified currently. These proteins are all involved in the reorganization of the actin cytoskeleton in response to external stimuli. They also have roles in cell transformation by Ras in cytokinesis, in focal adhesion formation and in the stimulation of stress-activated kinase. These various functions are controlled through distinct effector proteins and mediated through a GTP-binding/GTPase cycle involving three classes of regulating proteins: GAPs (GTPase-activating proteins), GEFs (guanine nucleotide exchange factors), and GDIs (guanine nucleotide dissociation inhibitors). Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Since crystal structures often lack C-terminal residues, this feature is not available for annotation in many of the CDs in the hierarchy.


Pssm-ID: 206641 [Multi-domain]  Cd Length: 171  Bit Score: 57.55  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   5 CKVVVCGLLSVGKTAILeqLLYGNHTIGMEDCETMEDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVL 84
Cdd:cd00157     1 IKIVVVGDGAVGKTCLL--ISYTTNKFPTEYVPTVFDNYSANVTVD-GKQVNLGLWDTAGQEEYDRLRPLSYPQTDVFLL 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1791034378  85 VYSVNNLESFQRVEllKK---EIDKFKDKkeVAIVVLGNKIDL 124
Cdd:cd00157    78 CFSVDSPSSFENVK--TKwypEIKHYCPN--VPIILVGTKIDL 116
PLN03118 PLN03118
Rab family protein; Provisional
6-173 2.51e-10

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 57.37  E-value: 2.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGN-----HTIGMEdcetmedvYMASVETDRGVKEQLHLYDTRGLQEGVELPKHYFSFAD 80
Cdd:PLN03118   16 KILLIGDSGVGKSSLLVSFISSSvedlaPTIGVD--------FKIKQLTVGGKRLKLTIWDTAGQERFRTLTSSYYRNAQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  81 GFVLVYSVNNLESFQR-VELLKKEIDKFKDKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIE 159
Cdd:PLN03118   88 GIILVYDVTRRETFTNlSDVWGKEVELYSTNQDCVKMLVGNKVDRESERDVSREEGMALAKEHGCLFLECSAKTRENVEQ 167
                         170
                  ....*....|....
gi 1791034378 160 PFTLLASKLSQPQS 173
Cdd:PLN03118  168 CFEELALKIMEVPS 181
Rab11_like cd01868
Rab GTPase family 11 (Rab11)-like includes Rab11a, Rab11b, and Rab25; Rab11a, Rab11b, and ...
5-148 3.01e-10

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


Pssm-ID: 206660 [Multi-domain]  Cd Length: 165  Bit Score: 56.41  E-value: 3.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   5 CKVVVCGLLSVGKTAIL------EQLLYGNHTIGMEdcetmedvyMA--SVETD-RGVKEQLhlYDTRGlQEGVE-LPKH 74
Cdd:cd01868     4 FKIVLIGDSGVGKSNLLsrftrnEFNLDSKSTIGVE---------FAtrTIQIDgKTIKAQI--WDTAG-QERYRaITSA 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1791034378  75 YFSFADGFVLVYSVNNLESFQRVELLKKEIDKFKDKKEVAIVVlGNKIDLSEQRQVDAEVAQQWAKSEKVRLWE 148
Cdd:cd01868    72 YYRGAVGALLVYDITKKSTFENVERWLKELRDHADSNIVIMLV-GNKSDLRHLRAVPTEEAKAFAEKNGLSFIE 144
Rab24 cd04118
Rab GTPase family 24 (Rab24); Rab24 is distinct from other Rabs in several ways. It exists ...
6-165 5.76e-10

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


Pssm-ID: 133318 [Multi-domain]  Cd Length: 193  Bit Score: 56.03  E-value: 5.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQllYGNHTIGMEDCE-TMEDVYMASVETDRGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVL 84
Cdd:cd04118     2 KVVMLGKESVGKTSLVER--YVHHRFLVGPYQnTIGAAFVAKRMVVGERVVTLGIWDTAGSERYEAMSRIYYRGAKAAIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  85 VYSVNNLESFQRVELLKKEIDKFKDkkEVAIVVLGNKIDLSEQ----RQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIEP 160
Cdd:cd04118    80 CYDLTDSSSFERAKFWVKELQNLEE--HCKIYLCGTKSDLIEQdrslRQVDFHDVQDFADEIKAQHFETSSKTGQNVDEL 157

                  ....*
gi 1791034378 161 FTLLA 165
Cdd:cd04118   158 FQKVA 162
Rab3 cd01865
Rab GTPase family 3 contains Rab3A, Rab3B, Rab3C and Rab3D; The Rab3 subfamily contains Rab3A, ...
6-153 2.90e-09

Rab GTPase family 3 contains Rab3A, Rab3B, Rab3C and Rab3D; The Rab3 subfamily contains Rab3A, Rab3B, Rab3C, and Rab3D. All four isoforms were found in mouse brain and endocrine tissues, with varying levels of expression. Rab3A, Rab3B, and Rab3C localized to synaptic and secretory vesicles; Rab3D was expressed at high levels only in adipose tissue, exocrine glands, and the endocrine pituitary, where it is localized to cytoplasmic secretory granules. Rab3 appears to control Ca2+-regulated exocytosis. The appropriate GDP/GTP exchange cycle of Rab3A is required for Ca2+-regulated exocytosis to occur, and interaction of the GTP-bound form of Rab3A with effector molecule(s) is widely believed to be essential for this process. Functionally, most studies point toward a role for Rab3 in the secretion of hormones and neurotransmitters. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206657 [Multi-domain]  Cd Length: 165  Bit Score: 53.76  E-value: 2.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILeqLLYGNhtigmedcETMEDVYMASVETDRGVKE--------QLHLYDTRGLQEGVELPKHYFS 77
Cdd:cd01865     3 KLLIIGNSSVGKTSFL--FRYAD--------DSFTSAFVSTVGIDFKVKTvyrndkriKLQIWDTAGQERYRTITTAYYR 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1791034378  78 FADGFVLVYSVNNLESFQRVELLKKEIDKFK-DKKEVAIVvlGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTD 153
Cdd:cd01865    73 GAMGFILMYDITNEESFNAVQDWSTQIKTYSwDNAQVILV--GNKCDMEDERVVSAERGRQLADQLGFEFFEASAKE 147
Rab14 cd04122
Rab GTPase family 14 (Rab14); Rab14 GTPases are localized to biosynthetic compartments, ...
6-170 2.98e-09

Rab GTPase family 14 (Rab14); Rab14 GTPases are localized to biosynthetic compartments, including the rough ER, the Golgi complex, and the trans-Golgi network, and to endosomal compartments, including early endosomal vacuoles and associated vesicles. Rab14 is believed to function in both the biosynthetic and recycling pathways between the Golgi and endosomal compartments. Rab14 has also been identified on GLUT4 vesicles, and has been suggested to help regulate GLUT4 translocation. In addition, Rab14 is believed to play a role in the regulation of phagocytosis. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 133322 [Multi-domain]  Cd Length: 166  Bit Score: 53.69  E-value: 2.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGN------HTIGMEDCETMEDVymasvetdRGVKEQLHLYDTRGLQEGVELPKHYFSFA 79
Cdd:cd04122     4 KYIIIGDMGVGKSCLLHQFTEKKfmadcpHTIGVEFGTRIIEV--------NGQKIKLQIWDTAGQERFRAVTRSYYRGA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  80 DGFVLVYSVNNLESFQRVELLKKEIDKFKDKKEVaIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIE 159
Cdd:cd04122    76 AGALMVYDITRRSTYNHLSSWLTDARNLTNPNTV-IFLIGNKADLEAQRDVTYEEAKQFADENGLLFLECSAKTGENVED 154
                         170
                  ....*....|.
gi 1791034378 160 PFTLLASKLSQ 170
Cdd:cd04122   155 AFLETAKKIYQ 165
Rab26 cd04112
Rab GTPase family 26 (Rab26); Rab26 subfamily. First identified in rat pancreatic acinar cells, ...
6-168 6.37e-09

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


Pssm-ID: 206695 [Multi-domain]  Cd Length: 191  Bit Score: 53.33  E-value: 6.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGNHTIGmEDCETMEDVYMASVETDRGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVLV 85
Cdd:cd04112     2 KVMLVGDSGVGKTCLLVRFKDGAFLAG-SFIATVGIQFTNKVVTVDGVKVKLQIWDTAGQERFRSVTHAYYRDAHALLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  86 YSVNNLESFQRVELLKKEIDKFKdKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIEPFTLLA 165
Cdd:cd04112    81 YDVTNKSSFDNIRAWLTEILEYA-QSDVVIMLLGNKADMSGERVVKREDGERLAKEYGVPFMETSAKTGLNVELAFTAVA 159

                  ...
gi 1791034378 166 SKL 168
Cdd:cd04112   160 KEL 162
PLN03110 PLN03110
Rab GTPase; Provisional
6-189 8.24e-09

Rab GTPase; Provisional


Pssm-ID: 178657 [Multi-domain]  Cd Length: 216  Bit Score: 53.01  E-value: 8.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAIL------EQLLYGNHTIGME-DCETMEdvymasVEtDRGVKEQLhlYDTRGLQEGVELPKHYFSF 78
Cdd:PLN03110   14 KIVLIGDSGVGKSNILsrftrnEFCLESKSTIGVEfATRTLQ------VE-GKTVKAQI--WDTAGQERYRAITSAYYRG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  79 ADGFVLVYSVNNLESFQRVELLKKEIDKFKDKKeVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLI 158
Cdd:PLN03110   85 AVGALLVYDITKRQTFDNVQRWLRELRDHADSN-IVIMMAGNKSDLNHLRSVAEEDGQALAEKEGLSFLETSALEATNVE 163
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1791034378 159 EPFTLLASKLSQPQSKSSfpLPGRKNKGNSN 189
Cdd:PLN03110  164 KAFQTILLEIYHIISKKA--LAAQEAAANSG 192
PLN03108 PLN03108
Rab family protein; Provisional
6-170 1.06e-08

Rab family protein; Provisional


Pssm-ID: 178655 [Multi-domain]  Cd Length: 210  Bit Score: 52.64  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLL------YGNHTIGMEdcetmedvYMASVETDRGVKEQLHLYDTRGLQEGVELPKHYFSFA 79
Cdd:PLN03108    8 KYIIIGDTGVGKSCLLLQFTdkrfqpVHDLTIGVE--------FGARMITIDNKPIKLQIWDTAGQESFRSITRSYYRGA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  80 DGFVLVYSVNNLESFQRVELLKKEIDKFKDKKeVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIE 159
Cdd:PLN03108   80 AGALLVYDITRRETFNHLASWLEDARQHANAN-MTIMLIGNKCDLAHRRAVSTEEGEQFAKEHGLIFMEASAKTAQNVEE 158
                         170
                  ....*....|.
gi 1791034378 160 PFTLLASKLSQ 170
Cdd:PLN03108  159 AFIKTAAKIYK 169
Rho4_like cd04132
Ras homology family 4 (Rho4) of small guanosine triphosphatases (GTPases)-like; Rho4 is a ...
6-137 2.54e-08

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


Pssm-ID: 206704 [Multi-domain]  Cd Length: 197  Bit Score: 51.57  E-value: 2.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILeqLLYGNHTIGMEDCETMEDVYMASVETDRGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVLV 85
Cdd:cd04132     5 KIVVVGDGGCGKTCLL--MVYAQGSFPEEYVPTVFENYVTTLQVPNGKIIELALWDTAGQEDYDRLRPLSYPDVDVILIC 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1791034378  86 YSVNNLESFQRV-ELLKKEIDKFKDKkeVAIVVLGNKIDLSEQRQVDAEVAQQ 137
Cdd:cd04132    83 YSVDNPTSLDNVeDKWYPEVNHFCPG--TPIVLVGLKTDLRKDKNSVSKLRAQ 133
Rab27A cd04127
Rab GTPase family 27a (Rab27a); The Rab27a subfamily consists of Rab27a and its highly ...
6-140 2.59e-08

Rab GTPase family 27a (Rab27a); The Rab27a subfamily consists of Rab27a and its highly homologous isoform, Rab27b. Unlike most Rab proteins whose functions remain poorly defined, Rab27a has many known functions. Rab27a has multiple effector proteins, and depending on which effector it binds, Rab27a has different functions as well as tissue distribution and/or cellular localization. Putative functions have been assigned to Rab27a when associated with the effector proteins Slp1, Slp2, Slp3, Slp4, Slp5, DmSlp, rabphilin, Dm/Ce-rabphilin, Slac2-a, Slac2-b, Slac2-c, Noc2, JFC1, and Munc13-4. Rab27a has been associated with several human diseases, including hemophagocytic syndrome (Griscelli syndrome or GS), Hermansky-Pudlak syndrome, and choroidermia. In the case of GS, a rare, autosomal recessive disease, a Rab27a mutation is directly responsible for the disorder. When Rab27a is localized to the secretory granules of pancreatic beta cells, it is believed to mediate glucose-stimulated insulin secretion, making it a potential target for diabetes therapy. When bound to JFC1 in prostate cells, Rab27a is believed to regulate the exocytosis of prostate- specific markers. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206700 [Multi-domain]  Cd Length: 180  Bit Score: 51.35  E-value: 2.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGNH------TIGMeDCETMEDVYMAS-VETDRGVKEQLHL--YDTRGLQEGVELPKHYF 76
Cdd:cd04127     6 KLLALGDSGVGKTTFLYRYTDNKFnpkfitTVGI-DFREKRVVYNSQgPDGTSGKAFRVHLqlWDTAGQERFRSLTTAFF 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1791034378  77 SFADGFVLVYSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAK 140
Cdd:cd04127    85 RDAMGFLLMFDLTSEQSFLNVRNWMSQLQAHAYCENPDIVLIGNKADLPDQREVSERQARELAD 148
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
6-170 3.85e-08

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 50.75  E-value: 3.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGnhTIGMEDCETME--DVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHY---FSFAD 80
Cdd:COG1100     5 KIVVVGTGGVGKTSLVNRLVGD--IFSLEKYLSTNgvTIDKKELKLD-GLDVDLVIWDTPGQDEFRETRQFYarqLTGAS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  81 GFVLVYSVNNLESFQRVELLKKEIDKFkdKKEVAIVVLGNKIDL-SEQRQVDAEVAQQWAKSEKVrlWEVTVTDRKT--- 156
Cdd:COG1100    82 LYLFVVDGTREETLQSLYELLESLRRL--GKKSPIILVLNKIDLyDEEEIEDEERLKEALSEDNI--VEVVATSAKTgeg 157
                         170
                  ....*....|....
gi 1791034378 157 LIEPFTLLASKLSQ 170
Cdd:COG1100   158 VEELFAALAEILRG 171
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
6-131 1.03e-07

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: 49.11  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGNH-----TIGMedcetmedvymaSVETDRGVKEQLHLYDTRGLQEGVELPKHYFSFAD 80
Cdd:cd00878     1 RILMLGLDGAGKTTILYKLKLGEVvttipTIGF------------NVETVEYKNVKFTVWDVGGQDKIRPLWKHYYENTD 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1791034378  81 GFVLVYSVNNLESFQRVellKKEIDK-FKDK--KEVAIVVLGNKIDLSEQRQVD 131
Cdd:cd00878    69 GLIFVVDSSDRERIEEA---KNELHKlLNEEelKGAPLLILANKQDLPGALTES 119
Rab2 cd01866
Rab GTPase family 2 (Rab2); Rab2 is localized on cis-Golgi membranes and interacts with Golgi ...
6-168 1.16e-07

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


Pssm-ID: 206658 [Multi-domain]  Cd Length: 168  Bit Score: 49.34  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQL----LYGNH--TIGMEdcetmedvYMASVETDRGVKEQLHLYDTRGLQEGVELPKHYFSFA 79
Cdd:cd01866     6 KYIIIGDTGVGKSCLLLQFtdkrFQPVHdlTIGVE--------FGARMITIDGKQIKLQIWDTAGQESFRSITRSYYRGA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  80 DGFVLVYSVNNLESFQRVELLKKEIDKFKDKKeVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIE 159
Cdd:cd01866    78 AGALLVYDITRRETFNHLTSWLEDARQHSNSN-MTIMLIGNKCDLESRREVSYEEGEAFAREHGLIFMETSAKTASNVEE 156

                  ....*....
gi 1791034378 160 PFTLLASKL 168
Cdd:cd01866   157 AFINTAKEI 165
Rab32_Rab38 cd04107
Rab GTPase families 18 (Rab18) and 32 (Rab32); Rab38/Rab32 subfamily. Rab32 and Rab38 are ...
6-141 1.28e-07

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


Pssm-ID: 206692 [Multi-domain]  Cd Length: 201  Bit Score: 49.62  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGNH------TIGMedcetmeDVYMASVETDRGVKEQLHLYDTRGLQEGVELPKHYFSFA 79
Cdd:cd04107     2 KVLVIGDLGVGKTSIIKRYVHGVFsqhykaTIGV-------DFALKVIEWDPNTVVRLQLWDIAGQERFGGMTRVYYKGA 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1791034378  80 DGFVLVYSVNNLESFQRVELLKKEID---KFKDKKEVAIVVLGNKIDLSEQR-QVDAEVAQQWAKS 141
Cdd:cd04107    75 VGAIIVFDVTRPSTFEAVLKWKADLDskvTLPNGEPIPALLLANKCDLKKERlAKDPEQMDQFCKE 140
Wrch_1 cd04130
Wnt-1 responsive Cdc42 homolog (Wrch-1) is a Rho family GTPase similar to Cdc42; Wrch-1 (Wnt-1 ...
6-136 1.18e-06

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


Pssm-ID: 133330 [Multi-domain]  Cd Length: 173  Bit Score: 46.63  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILeqLLYGNHTIGMEDCETMEDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVLV 85
Cdd:cd04130     2 KCVLVGDGAVGKTSLI--VSYTTNGYPTEYVPTAFDNFSVVVLVD-GKPVRLQLCDTAGQDEFDKLRPLCYPDTDVFLLC 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1791034378  86 YSVNNLESFQRVEllKKEIDKF-KDKKEVAIVVLGNKIDLSEQRQVDAEVAQ 136
Cdd:cd04130    79 FSVVNPSSFQNIS--EKWIPEIrKHNPKAPIILVGTQADLRTDVNVLIQLAR 128
Centaurin_gamma cd04103
Centaurin gamma (CENTG) GTPase; The centaurins (alpha, beta, gamma, and delta) are large, ...
6-139 1.81e-06

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: 45.95  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGNHtigmedcetmedVYMASVETDRGVKE-----QLHLYDTRglQEGVELPKHYFSFAD 80
Cdd:cd04103     2 KLGIVGNLRSGKSALVHRYLTGSY------------VQLESPEGGRFKKEvlvdgQSHLLLIR--DEGGAPDAQFAGWVD 67
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1791034378  81 GFVLVYSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLG--NKIDLSEQRQVDAEVAQQWA 139
Cdd:cd04103    68 AVIFVFSLEDEASFQTVYRLYHQLSSYRNISEIPLILVGtqDAISASNPRVIDDARARQLC 128
Tc10 cd04135
Rho GTPase TC10 (Tc10); TC10 is a Rho family protein that has been shown to induce microspike ...
6-126 2.06e-06

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 [Multi-domain]  Cd Length: 174  Bit Score: 45.78  E-value: 2.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILeqLLYGNHTIGMEDCETMEDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVLV 85
Cdd:cd04135     2 KCVVVGDGAVGKTCLL--MSYANDAFPEEYVPTVFDHYAVSVTVG-GKQYLLGLYDTAGQEDYDRLRPLSYPMTDVFLIC 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1791034378  86 YSVNNLESFQRVEllKKEIDKFKD-KKEVAIVVLGNKIDLSE 126
Cdd:cd04135    79 FSVVNPASFQNVK--EEWVPELKEyAPNVPYLLIGTQIDLRD 118
Rab20 cd04126
Rab GTPase family 20 (Rab20); Rab20 is one of several Rab proteins that appear to be ...
6-177 2.14e-06

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: 46.44  E-value: 2.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLlygnhtigmedcetMEDVYMASVETDRG---VKE----QLHLYDTRGLQEGVELPKHYFSF 78
Cdd:cd04126     2 KVVLLGDMNVGKTSLLHRY--------------MERRFKDTVSTVGGafyLKQwgpyNISIWDTAGREQFHGLGSMYCRG 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  79 ADGFVLVYSVNNLESFQRVEllkkeiDKFKDKKEVA-----IVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTD 153
Cdd:cd04126    68 AAAVILTYDVSNVQSLEELE------DRFLGLTDTAnedclFAVVGNKLDLTEEGALAGQEKDAGDRVSPEDQRQVTLED 141
                         170       180
                  ....*....|....*....|....*..
gi 1791034378 154 RKTL---IEPFTLLASKLSQPQSKSSF 177
Cdd:cd04126   142 AKAFykrINKYKMLDEDLSPAAEKMCF 168
Rop_like cd04133
Rho-related protein from plants (Rop)-like; The Rop (Rho-related protein from plants) ...
6-129 2.52e-06

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


Pssm-ID: 206705 [Multi-domain]  Cd Length: 173  Bit Score: 45.61  E-value: 2.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILeqLLYGNHTIGMEDCETMEDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVLV 85
Cdd:cd04133     3 KCVTVGDGAVGKTCML--ISYTSNTFPTDYVPTVFDNFSANVVVD-GNTVNLGLWDTAGQEDYNRLRPLSYRGADVFLLA 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1791034378  86 YSVNNLESFQRVelLKKEIDKFKD-KKEVAIVVLGNKIDLSEQRQ 129
Cdd:cd04133    80 FSLISKASYENV--LKKWIPELRHyAPGVPIVLVGTKLDLRDDKQ 122
RHO smart00174
Rho (Ras homology) subfamily of Ras-like small GTPases; Members of this subfamily of Ras-like ...
7-129 4.42e-06

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


Pssm-ID: 197554 [Multi-domain]  Cd Length: 174  Bit Score: 44.91  E-value: 4.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378    7 VVVCGLLSVGKTAILeqLLYGNHTIGMEDCETMEDVYMASVETDrGVKEQLHLYDTRGlQEGVE--LPKHYfSFADGFVL 84
Cdd:smart00174   1 LVVVGDGAVGKTCLL--IVYTTNAFPEDYVPTVFENYSADVEVD-GKPVELGLWDTAG-QEDYDrlRPLSY-PDTDVFLI 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1791034378   85 VYSVNNLESFQRVelLKK---EIDKFkdKKEVAIVVLGNKIDLSEQRQ 129
Cdd:smart00174  76 CFSVDSPASFENV--KEKwypEVKHF--CPNVPIILVGTKLDLRNDKS 119
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
6-149 9.99e-06

ADP-ribosylation factor family; Pfam combines a number of different Prosite families together


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 43.75  E-value: 9.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYG---NH--TIGMedceTMEDVymasveTDRGVKeqLHLYDTRGLQEGVELPKHYFSFAD 80
Cdd:pfam00025   2 RILILGLDNAGKTTILYKLKLGeivTTipTIGF----NVETV------TYKNVK--FTVWDVGGQESLRPLWRNYFPNTD 69
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1791034378  81 GFVLVYSVNNLEsfqRVELLKKEIDKF---KDKKEVAIVVLGNKIDLSEQRQVdAEVAQQWAKSE-KVRLWEV 149
Cdd:pfam00025  70 AVIFVVDSADRD---RIEEAKEELHALlneEELADAPLLILANKQDLPGAMSE-AEIRELLGLHElKDRPWEI 138
Srp102 COG2229
Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, ...
5-174 1.21e-05

Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441830 [Multi-domain]  Cd Length: 189  Bit Score: 44.04  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   5 CKVVVCGLLSVGKTAILEQLlygnHTIGMEDCE-TMEDVYMASvETDR-----------GVKEQLHLYDTRGlQEgvelp 72
Cdd:COG2229    13 VKIVYAGPFGAGKTTFVRSI----SEIEPLSTEgRLTDASLET-KTTTtvafdfgrltlGDGLRLHLFGTPG-QV----- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  73 khYFSF--------ADGFVLVY------SVNNLESFQRVEllkkeidkfKDKKEVAIVVLGNKIDLSEQRQVDaEVAQQW 138
Cdd:COG2229    82 --RFDFmwdillrgADGVVFLAdsrrleDSFNAESLDFFE---------ERLEKLPFVVAVNKRDLPDALSLE-ELREAL 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1791034378 139 AKSEKVRLWEVTVTDRK----TLIepfTLLASKLSQPQSK 174
Cdd:COG2229   150 DLGPDVPVVEADARDGEsvkeTLI---ALLELVLARLDAR 186
PTZ00099 PTZ00099
rab6; Provisional
56-176 1.97e-05

rab6; Provisional


Pssm-ID: 185444 [Multi-domain]  Cd Length: 176  Bit Score: 43.19  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  56 QLHLYDTRGLQEGVELPKHYFSFADGFVLVYSVNNLESFQRVELLKKEIDKfKDKKEVAIVVLGNKIDLSEQRQVDAEVA 135
Cdd:PTZ00099   30 RLQLWDTAGQERFRSLIPSYIRDSAAAIVVYDITNRQSFENTTKWIQDILN-ERGKDVIIALVGNKTDLGDLRKVTYEEG 108
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1791034378 136 QQWAKSEKVRLWEVTVTDRKTLIEPFTLLASKLSQPQSKSS 176
Cdd:PTZ00099  109 MQKAQEYNTMFHETSAKAGHNIKVLFKKIAAKLPNLDNSNS 149
Arl4_Arl7 cd04152
Arf-like 4 (Arl4) and 7 (Arl7) GTPases; Arl4 (Arf-like 4) is highly expressed in testicular ...
7-142 6.82e-05

Arf-like 4 (Arl4) and 7 (Arl7) GTPases; Arl4 (Arf-like 4) is highly expressed in testicular germ cells, and is found in the nucleus and nucleolus. In mice, Arl4 is developmentally expressed during embryogenesis, and a role in somite formation and central nervous system differentiation has been proposed. Arl7 has been identified as the only Arf/Arl protein to be induced by agonists of liver X-receptor and retinoid X-receptor and by cholesterol loading in human macrophages. Arl7 is proposed to play a role in transport between a perinuclear compartment and the plasma membrane, apparently linked to the ABCA1-mediated cholesterol secretion pathway. Older literature suggests that Arl6 is a part of the Arl4/Arl7 subfamily, but analyses based on more recent sequence data place Arl6 in its own subfamily.


Pssm-ID: 206719 [Multi-domain]  Cd Length: 183  Bit Score: 41.71  E-value: 6.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   7 VVVCGLLSVGKTAILEQLLYGNH-----TIGMeDCETMEdvymASVETDRGVkeQLHLYDTRGLQEGVELPKHYFSFADG 81
Cdd:cd04152     6 IVMLGLDSAGKTTVLYRLKFNEFvntvpTKGF-NTEKIK----VSLGNAKGV--TFHFWDVGGQEKLRPLWKSYTRCTDG 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1791034378  82 FVLVYSVNNLESFQ--RVELLKkeIDKFKDKKEVAIVVLGNKIDLSEQRQVdAEVAQQWAKSE 142
Cdd:cd04152    79 IVFVVDSVDVERMEeaKTELHK--ITKFSENQGVPVLVLANKQDLPNALPV-SEVEKLLALHE 138
Rho3 cd04134
Ras homology family 3 (Rho3) of small guanosine triphosphatases (GTPases); Rho3 is a member of ...
6-130 7.19e-04

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


Pssm-ID: 206706 [Multi-domain]  Cd Length: 185  Bit Score: 38.69  E-value: 7.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGNHTIGMEdcETMEDVYMASVETDrGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVLV 85
Cdd:cd04134     2 KVVVLGDGACGKTSLLNVFTRGYFPQVYE--PTVFENYIHDIFVD-GLAVELSLWDTAGQEEFDRLRSLSYADTHVIMLC 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1791034378  86 YSVNNLESFQRVEllKKEIDKFKDKKE-VAIVVLGNKIDLSEQRQV 130
Cdd:cd04134    79 FSVDNPDSLENVE--SKWLAEIRHHCPgVKLVLVALKCDLREPRNE 122
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
6-135 1.09e-03

Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 38.30  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILeqllygNHTIGmedcetmEDVYMASV--ETDR------GVKEQLHLYDTRGL----QEGVELPK 73
Cdd:cd09912     2 LLAVVGEFSAGKSTLL------NALLG-------EEVLPTGVtpTTAVitvlryGLLKGVVLVDTPGLnstiEHHTEITE 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1791034378  74 HYFSFADGFVLVYSVNNleSFQRVEL--LKKEIDKFKDKkevaIVVLGNKIDLSEQRQVDAEVA 135
Cdd:cd09912    69 SFLPRADAVIFVLSADQ--PLTESERefLKEILKWSGKK----IFFVLNKIDLLSEEELEEVLE 126
SAR smart00178
Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene ...
3-123 1.26e-03

Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene required for transport of secretory proteins from the endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 197556 [Multi-domain]  Cd Length: 184  Bit Score: 37.99  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378    3 KGCKVVVCGLLSVGKTAILeqllygnHTIGMEDCETMEDVYMASVETDRGVKEQLHLYDTRGLQEGVELPKHYFSFADGf 82
Cdd:smart00178  16 KHAKILFLGLDNAGKTTLL-------HMLKNDRLAQHQPTQHPTSEELAIGNIKFTTFDLGGHQQARRLWKDYFPEVNG- 87
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1791034378   83 vLVYSVNNLEsFQRVELLKKEIDKF---KDKKEVAIVVLGNKID 123
Cdd:smart00178  88 -IVYLVDAYD-KERFAESKRELDALlsdEELATVPFLILGNKID 129
Arl6 cd04157
Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small ...
7-124 1.40e-03

Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small GTPases. Arl6 expression is limited to the brain and kidney in adult mice, but it is expressed in the neural plate and somites during embryogenesis, suggesting a possible role for Arl6 in early development. Arl6 is also believed to have a role in cilia or flagella function. Several proteins have been identified that bind Arl6, including Arl6 interacting protein (Arl6ip), and SEC61beta, a subunit of the heterotrimeric conducting channel SEC61p. Based on Arl6 binding to these effectors, Arl6 is also proposed to play a role in protein transport, membrane trafficking, or cell signaling during hematopoietic maturation. At least three specific homozygous Arl6 mutations in humans have been found to cause Bardet-Biedl syndrome, a disorder characterized by obesity, retinopathy, polydactyly, renal and cardiac malformations, learning disabilities, and hypogenitalism. Older literature suggests that Arl6 is a part of the Arl4/Arl7 subfamily, but analyses based on more recent sequence data place Arl6 in its own subfamily.


Pssm-ID: 206722 [Multi-domain]  Cd Length: 162  Bit Score: 37.79  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   7 VVVCGLLSVGKTAILEQLLYGNH-------TIGMedceTMEDVYMASVetdrgvkeQLHLYDTRGLQEGVELPKHYFSFA 79
Cdd:cd04157     2 ILVLGLDNSGKTTIINQLKPSNAqsqnivpTVGF----NVESFKKGNL--------SFTAFDMSGQGKYRGLWEHYYKNI 69
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1791034378  80 DGFVLVY-SVNNLesfqRVELLKKEIDKFKDKKEVA-----IVVLGNKIDL 124
Cdd:cd04157    70 QGIIFVIdSSDRL----RMVVAKDELELLLNHPDIKhrripILFYANKMDL 116
Miro2 cd01892
Mitochondrial Rho family 2 (Miro2), C-terminal; Miro2 subfamily. Miro (mitochondrial Rho) ...
5-130 1.66e-03

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


Pssm-ID: 206679  Cd Length: 180  Bit Score: 37.61  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   5 CKVVvcGLLSVGKTAILEQLLyGNHTIGMEDCETMEDVYMA-SVETdRGVKEQLHLYDTRGLQEGVELPKHYFSFADGFV 83
Cdd:cd01892     7 CFVL--GAKGSGKSALLQAFL-GRSFSQNAYSPTIKPRYAVnTVEV-PGQEKYLILREVGEDEEAILLNDAELAACDVAC 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1791034378  84 LVYSVNNLESFQR-VELLKKeidkFKDKKEVAIVVLGNKIDLSEQRQV 130
Cdd:cd01892    83 LVYDSSDPNSFSYcAEVYKK----YFMLGEIPCLFVAAKADLDEQQQR 126
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
57-138 2.67e-03

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: 36.70  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  57 LHLYDTRGL--------QEGVELPKHYFSFADGFVLVYSVNNLESfqrvELLKKEIDKFKDKKevaIVVLGNKIDLSEQR 128
Cdd:cd04164    53 VRLIDTAGLretedeieKIGIERAREAIEEADLVLLVVDASEGLD----EEDLEILELPAKKP---VIVVLNKSDLLSDA 125
                          90
                  ....*....|
gi 1791034378 129 QVDAEVAQQW 138
Cdd:cd04164   126 EGISELNGKP 135
PTZ00132 PTZ00132
GTP-binding nuclear protein Ran; Provisional
6-172 5.34e-03

GTP-binding nuclear protein Ran; Provisional


Pssm-ID: 240284 [Multi-domain]  Cd Length: 215  Bit Score: 36.21  E-value: 5.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGNH------TIGMEdcetmedVYMASVETDRGvKEQLHLYDTRGLQEGVELPKHYFSFA 79
Cdd:PTZ00132   11 KLILVGDGGVGKTTFVKRHLTGEFekkyipTLGVE-------VHPLKFYTNCG-PICFNVWDTAGQEKFGGLRDGYYIKG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378  80 DGFVLVYSVNNLESFQRVELLKKEIdkFKDKKEVAIVVLGNKIDLSEqRQVDAEVAqQWAKSEKVRLWEVTVTDRKTLIE 159
Cdd:PTZ00132   83 QCAIIMFDVTSRITYKNVPNWHRDI--VRVCENIPIVLVGNKVDVKD-RQVKARQI-TFHRKKNLQYYDISAKSNYNFEK 158
                         170
                  ....*....|....
gi 1791034378 160 PFTLLASKLS-QPQ 172
Cdd:PTZ00132  159 PFLWLARRLTnDPN 172
Arf1_5_like cd04150
ADP-ribosylation factor-1 (Arf1) and ADP-ribosylation factor-5 (Arf5); The Arf1-Arf5-like ...
6-152 9.07e-03

ADP-ribosylation factor-1 (Arf1) and ADP-ribosylation factor-5 (Arf5); The Arf1-Arf5-like subfamily contains Arf1, Arf2, Arf3, Arf4, Arf5, and related proteins. Arfs1-5 are soluble proteins that are crucial for assembling coat proteins during vesicle formation. Each contains an N-terminal myristoylated amphipathic helix that is folded into the protein in the GDP-bound state. GDP/GTP exchange exposes the helix, which anchors to the membrane. Following GTP hydrolysis, the helix dissociates from the membrane and folds back into the protein. A general feature of Arf1-5 signaling may be the cooperation of two Arfs at the same site. Arfs1-5 are generally considered to be interchangeable in function and location, but some specific functions have been assigned. Arf1 localizes to the early/cis-Golgi, where it is activated by GBF1 and recruits the coat protein COPI. It also localizes to the trans-Golgi network (TGN), where it is activated by BIG1/BIG2 and recruits the AP1, AP3, AP4, and GGA proteins. Humans, but not rodents and other lower eukaryotes, lack Arf2. Human Arf3 shares 96% sequence identity with Arf1 and is believed to generally function interchangeably with Arf1. Human Arf4 in the activated (GTP-bound) state has been shown to interact with the cytoplasmic domain of epidermal growth factor receptor (EGFR) and mediate the EGF-dependent activation of phospholipase D2 (PLD2), leading to activation of the activator protein 1 (AP-1) transcription factor. Arf4 has also been shown to recognize the C-terminal sorting signal of rhodopsin and regulate its incorporation into specialized post-Golgi rhodopsin transport carriers (RTCs). There is some evidence that Arf5 functions at the early-Golgi and the trans-Golgi to affect Golgi-associated alpha-adaptin homology Arf-binding proteins (GGAs).


Pssm-ID: 206717 [Multi-domain]  Cd Length: 159  Bit Score: 35.46  E-value: 9.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1791034378   6 KVVVCGLLSVGKTAILEQLLYGN-----HTIGMedcetmedvymaSVETDRGVKEQLHLYDTRGLQEGVELPKHYFSFAD 80
Cdd:cd04150     2 RILMVGLDAAGKTTILYKLKLGEivttiPTIGF------------NVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQ 69
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1791034378  81 GFVLVYSVNNLEsfqRVELLKKEIDKFKDKKEV---AIVVLGNKIDLSeQRQVDAEVAQQWA-KSEKVRLWEVTVT 152
Cdd:cd04150    70 GLIFVVDSNDRE---RIGEAREELQRMLNEDELrdaVLLVFANKQDLP-NAMSAAEVTDKLGlHSLRNRNWYIQAT 141
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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