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Conserved domains on  [gi|6680730|ref|NP_031513|]
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ADP-ribosylation factor-like protein 4A [Mus musculus]

Protein Classification

ADP-ribosylation factor-like protein 4( domain architecture ID 10134963)

ADP-ribosylation factor-like protein 4 (Arl4), a small GTP-binding protein that is developmentally regulated and localized to nuclei and nucleoli, and which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF)and GTPase-activating proteins (GAP)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Arl4_Arl7 cd04152
Arf-like 4 (Arl4) and 7 (Arl7) GTPases; Arl4 (Arf-like 4) is highly expressed in testicular ...
18-200 1.19e-139

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: 387.23  E-value: 1.19e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   18 FQSFHIVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIKVTLGNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIV 97
Cdd:cd04152   1 FQSLHIVMLGLDSAGKTTVLYRLKFNEFVNTVPTKGFNTEKIKVSLGNAKGVTFHFWDVGGQEKLRPLWKSYTRCTDGIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   98 FVVDSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIEKLLAMGELSSSTPWHLQPTCAIIGDGLKE 177
Cdd:cd04152  81 FVVDSVDVERMEEAKTELHKITKFSENQGVPVLVLANKQDLPNALPVSEVEKLLALHELSSSTPWHVQPACAIIGEGLQE 160
                       170       180
                ....*....|....*....|...
gi 6680730  178 GLEKLHDMIIKRRKMLRQQKKKR 200
Cdd:cd04152 161 GLEKLYEMILKRRKMLRQQKKKR 183
 
Name Accession Description Interval E-value
Arl4_Arl7 cd04152
Arf-like 4 (Arl4) and 7 (Arl7) GTPases; Arl4 (Arf-like 4) is highly expressed in testicular ...
18-200 1.19e-139

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: 387.23  E-value: 1.19e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   18 FQSFHIVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIKVTLGNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIV 97
Cdd:cd04152   1 FQSLHIVMLGLDSAGKTTVLYRLKFNEFVNTVPTKGFNTEKIKVSLGNAKGVTFHFWDVGGQEKLRPLWKSYTRCTDGIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   98 FVVDSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIEKLLAMGELSSSTPWHLQPTCAIIGDGLKE 177
Cdd:cd04152  81 FVVDSVDVERMEEAKTELHKITKFSENQGVPVLVLANKQDLPNALPVSEVEKLLALHELSSSTPWHVQPACAIIGEGLQE 160
                       170       180
                ....*....|....*....|...
gi 6680730  178 GLEKLHDMIIKRRKMLRQQKKKR 200
Cdd:cd04152 161 GLEKLYEMILKRRKMLRQQKKKR 183
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
21-186 7.25e-86

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


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 250.22  E-value: 7.25e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730     21 FHIVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIKVtlgnsKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVV 100
Cdd:pfam00025   1 MRILILGLDNAGKTTILYKLKLGEIVTTIPTIGFNVETVTY-----KNVKFTVWDVGGQESLRPLWRNYFPNTDAVIFVV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730    101 DSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIEKLLAMGELsSSTPWHLQPTCAIIGDGLKEGLE 180
Cdd:pfam00025  76 DSADRDRIEEAKEELHALLNEEELADAPLLILANKQDLPGAMSEAEIRELLGLHEL-KDRPWEIQGCSAVTGEGLDEGLD 154

                  ....*.
gi 6680730    181 KLHDMI 186
Cdd:pfam00025 155 WLSNYI 160
ARF smart00177
ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular ...
11-182 1.89e-56

ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular transport. Activator 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. Contains ATP/GTP-binding motif (P-loop).


Pssm-ID: 128474 [Multi-domain]  Cd Length: 175  Bit Score: 176.27  E-value: 1.89e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730      11 ILSSLPSFQSFHIVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIKVtlgnsKTVTFHFWDVGGQEKLRPLWKSYT 90
Cdd:smart00177   4 LFSKLFGNKEMRILMVGLDAAGKTTILYKLKLGESVTTIPTIGFNVETVTY-----KNISFTVWDVGGQDKIRPLWRHYY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730      91 RCTDGIVFVVDSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIEKLLAMGELSSStPWHLQPTCAI 170
Cdd:smart00177  79 TNTQGLIFVVDSNDRDRIDEAREELHRMLNEDELRDAVILVFANKQDLPDAMKAAEITEKLGLHSIRDR-NWYIQPTCAT 157
                          170
                   ....*....|..
gi 6680730     171 IGDGLKEGLEKL 182
Cdd:smart00177 158 SGDGLYEGLTWL 169
PLN00223 PLN00223
ADP-ribosylation factor; Provisional
9-189 5.00e-55

ADP-ribosylation factor; Provisional


Pssm-ID: 165788  Cd Length: 181  Bit Score: 172.84  E-value: 5.00e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730     9 TSILSSLPSFQSFHIVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIKVtlgnsKTVTFHFWDVGGQEKLRPLWKS 88
Cdd:PLN00223   6 TKLFSRLFAKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEY-----KNISFTVWDVGGQDKIRPLWRH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730    89 YTRCTDGIVFVVDSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIEKLLAMGELSSSTpWHLQPTC 168
Cdd:PLN00223  81 YFQNTQGLIFVVDSNDRDRVVEARDELHRMLNEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRQRH-WYIQSTC 159
                        170       180
                 ....*....|....*....|.
gi 6680730   169 AIIGDGLKEGLEKLHDMIIKR 189
Cdd:PLN00223 160 ATSGEGLYEGLDWLSNNIANK 180
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
23-154 8.64e-23

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: 89.74  E-value: 8.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730     23 IVILGLDCAGKTTVLYRLQFNEFVNT--VPTKGFNTEKIKVTLgNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVV 100
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNKGSITeyYPGTTRNYVTTVIEE-DGKTYKFNLLDTAGQEDYDAIRRLYYPQVERSLRVF 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6680730    101 DSVD-VERMEEAKTELHKITRISENQGVPVLIVANKQDLR-NSLSLSEIEKLLAMG 154
Cdd:TIGR00231  83 DIVIlVLDVEEILEKQTKEIIHHADSGVPIILVGNKIDLKdADLKTHVASEFAKLN 138
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
23-194 2.00e-21

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 86.57  E-value: 2.00e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   23 IVILGLDCAGKTTVLYRLQFNEF--VNTVPTKGFNTEKIKVTLgNSKTVTFHFWDVGGQEKLRPLWKSYTRC---TDGIV 97
Cdd:COG1100   6 IVVVGTGGVGKTSLVNRLVGDIFslEKYLSTNGVTIDKKELKL-DGLDVDLVIWDTPGQDEFRETRQFYARQltgASLYL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   98 FVVDSVDVERMEEAKTELHKITRISENqgVPVLIVANKQDLRNSLSLSEIEKLlaMGELSSSTPWHLQPTCAIIGDGLKE 177
Cdd:COG1100  85 FVVDGTREETLQSLYELLESLRRLGKK--SPIILVLNKIDLYDEEEIEDEERL--KEALSEDNIVEVVATSAKTGEGVEE 160
                       170
                ....*....|....*..
gi 6680730  178 GLEKLHDMIIKRRKMLR 194
Cdd:COG1100 161 LFAALAEILRGEGDSLD 177
 
Name Accession Description Interval E-value
Arl4_Arl7 cd04152
Arf-like 4 (Arl4) and 7 (Arl7) GTPases; Arl4 (Arf-like 4) is highly expressed in testicular ...
18-200 1.19e-139

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: 387.23  E-value: 1.19e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   18 FQSFHIVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIKVTLGNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIV 97
Cdd:cd04152   1 FQSLHIVMLGLDSAGKTTVLYRLKFNEFVNTVPTKGFNTEKIKVSLGNAKGVTFHFWDVGGQEKLRPLWKSYTRCTDGIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   98 FVVDSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIEKLLAMGELSSSTPWHLQPTCAIIGDGLKE 177
Cdd:cd04152  81 FVVDSVDVERMEEAKTELHKITKFSENQGVPVLVLANKQDLPNALPVSEVEKLLALHELSSSTPWHVQPACAIIGEGLQE 160
                       170       180
                ....*....|....*....|...
gi 6680730  178 GLEKLHDMIIKRRKMLRQQKKKR 200
Cdd:cd04152 161 GLEKLYEMILKRRKMLRQQKKKR 183
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
21-186 7.25e-86

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


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 250.22  E-value: 7.25e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730     21 FHIVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIKVtlgnsKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVV 100
Cdd:pfam00025   1 MRILILGLDNAGKTTILYKLKLGEIVTTIPTIGFNVETVTY-----KNVKFTVWDVGGQESLRPLWRNYFPNTDAVIFVV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730    101 DSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIEKLLAMGELsSSTPWHLQPTCAIIGDGLKEGLE 180
Cdd:pfam00025  76 DSADRDRIEEAKEELHALLNEEELADAPLLILANKQDLPGAMSEAEIRELLGLHEL-KDRPWEIQGCSAVTGEGLDEGLD 154

                  ....*.
gi 6680730    181 KLHDMI 186
Cdd:pfam00025 155 WLSNYI 160
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
22-182 4.56e-78

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: 230.54  E-value: 4.56e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   22 HIVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIKVtlgnsKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVVD 101
Cdd:cd00878   1 RILMLGLDGAGKTTILYKLKLGEVVTTIPTIGFNVETVEY-----KNVKFTVWDVGGQDKIRPLWKHYYENTDGLIFVVD 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730  102 SVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIEKLLAMGELSSStPWHLQPTCAIIGDGLKEGLEK 181
Cdd:cd00878  76 SSDRERIEEAKNELHKLLNEEELKGAPLLILANKQDLPGALTESELIELLGLESIKGR-RWHIQPCSAVTGDGLDEGLDW 154

                .
gi 6680730  182 L 182
Cdd:cd00878 155 L 155
ARLTS1 cd04156
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ...
22-185 5.64e-57

Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), also known as Arl11, is a member of the Arf family of small GTPases that is believed to play a major role in apoptotic signaling. ARLTS1 is widely expressed and functions as a tumor suppressor gene in several human cancers. ARLTS1 is a low-penetrance suppressor that accounts for a small percentage of familial melanoma or familial chronic lymphocytic leukemia (CLL). ARLTS1 inactivation seems to occur most frequently through biallelic down-regulation by hypermethylation of the promoter. In breast cancer, ARLTS1 alterations were typically a combination of a hypomorphic polymorphism plus loss of heterozygosity. In a case of thyroid adenoma, ARLTS1 alterations were polymorphism plus promoter hypermethylation. The nonsense polymorphism Trp149Stop occurs with significantly greater frequency in familial cancer cases than in sporadic cancer cases, and the Cys148Arg polymorphism is associated with an increase in high-risk familial breast cancer.


Pssm-ID: 133356 [Multi-domain]  Cd Length: 160  Bit Score: 177.22  E-value: 5.64e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   22 HIVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIKVtlgnSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVVD 101
Cdd:cd04156   1 QVLLLGLDSAGKSTLLYKLKHAELVTTIPTVGFNVEMLQL----EKHLSLTVWDVGGQEKMRTVWKCYLENTDGLVYVVD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730  102 SVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIEKLLAMGELSSSTPWHLQPTCAIIGDGLKEGLEK 181
Cdd:cd04156  77 SSDEARLDESQKELKHILKNEHIKGVPVVLLANKQDLPGALTAEEITRRFKLKKYCSDRDWYVQPCSAVTGEGLAEAFRK 156

                ....
gi 6680730  182 LHDM 185
Cdd:cd04156 157 LASF 160
ARF smart00177
ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular ...
11-182 1.89e-56

ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular transport. Activator 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. Contains ATP/GTP-binding motif (P-loop).


Pssm-ID: 128474 [Multi-domain]  Cd Length: 175  Bit Score: 176.27  E-value: 1.89e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730      11 ILSSLPSFQSFHIVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIKVtlgnsKTVTFHFWDVGGQEKLRPLWKSYT 90
Cdd:smart00177   4 LFSKLFGNKEMRILMVGLDAAGKTTILYKLKLGESVTTIPTIGFNVETVTY-----KNISFTVWDVGGQDKIRPLWRHYY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730      91 RCTDGIVFVVDSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIEKLLAMGELSSStPWHLQPTCAI 170
Cdd:smart00177  79 TNTQGLIFVVDSNDRDRIDEAREELHRMLNEDELRDAVILVFANKQDLPDAMKAAEITEKLGLHSIRDR-NWYIQPTCAT 157
                          170
                   ....*....|..
gi 6680730     171 IGDGLKEGLEKL 182
Cdd:smart00177 158 SGDGLYEGLTWL 169
Arf6 cd04149
ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins ...
12-179 4.48e-56

ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins localize to the plasma membrane, where they perform a wide variety of functions. In its active, GTP-bound form, Arf6 is involved in cell spreading, Rac-induced formation of plasma membrane ruffles, cell migration, wound healing, and Fc-mediated phagocytosis. Arf6 appears to change the actin structure at the plasma membrane by activating Rac, a Rho family protein involved in membrane ruffling. Arf6 is required for and enhances Rac formation of ruffles. Arf6 can regulate dendritic branching in hippocampal neurons, and in yeast it localizes to the growing bud, where it plays a role in polarized growth and bud site selection. In leukocytes, Arf6 is required for chemokine-stimulated migration across endothelial cells. Arf6 also plays a role in down-regulation of beta2-adrenergic receptors and luteinizing hormone receptors by facilitating the release of sequestered arrestin to allow endocytosis. Arf6 is believed to function at multiple sites on the plasma membrane through interaction with a specific set of GEFs, GAPs, and effectors. Arf6 has been implicated in breast cancer and melanoma cell invasion, and in actin remodelling at the invasion site of Chlamydia infection.


Pssm-ID: 206716  Cd Length: 168  Bit Score: 174.96  E-value: 4.48e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   12 LSSLPSFQSFHIVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIKVtlgnsKTVTFHFWDVGGQEKLRPLWKSYTR 91
Cdd:cd04149   1 LSKLFGNKEMRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVETVTY-----KNVKFNVWDVGGQDKIRPLWRHYYT 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   92 CTDGIVFVVDSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIEKLLAMgELSSSTPWHLQPTCAII 171
Cdd:cd04149  76 GTQGLIFVVDSADRDRIDEARQELHRIINDREMRDALLLVFANKQDLPDAMKPHEIQEKLGL-TRIRDRNWYVQPSCATS 154

                ....*...
gi 6680730  172 GDGLKEGL 179
Cdd:cd04149 155 GDGLYEGL 162
Arf1_5_like cd04150
ADP-ribosylation factor-1 (Arf1) and ADP-ribosylation factor-5 (Arf5); The Arf1-Arf5-like ...
23-184 5.68e-56

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: 174.52  E-value: 5.68e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   23 IVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIKVtlgnsKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVVDS 102
Cdd:cd04150   3 ILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEY-----KNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730  103 VDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIEKLLAMGELSSStPWHLQPTCAIIGDGLKEGLEKL 182
Cdd:cd04150  78 NDRERIGEAREELQRMLNEDELRDAVLLVFANKQDLPNAMSAAEVTDKLGLHSLRNR-NWYIQATCATSGDGLYEGLDWL 156

                ..
gi 6680730  183 HD 184
Cdd:cd04150 157 SN 158
Arl1 cd04151
ADP ribosylation factor 1 (Arf1); Arl1 subfamily. Arl1 (Arf-like 1) localizes to the Golgi ...
23-182 2.29e-55

ADP ribosylation factor 1 (Arf1); Arl1 subfamily. Arl1 (Arf-like 1) localizes to the Golgi complex, where it is believed to recruit effector proteins to the trans-Golgi network. Like most members of the Arf family, Arl1 is myristoylated at its N-terminal helix and mutation of the myristoylation site disrupts Golgi targeting. In humans, the Golgi-localized proteins golgin-97 and golgin-245 have been identified as Arl1 effectors. Golgins are large coiled-coil proteins found in the Golgi, and these golgins contain a C-terminal GRIP domain, which is the site of Arl1 binding. Additional Arl1 effectors include the GARP (Golgi-associated retrograde protein)/VFT (Vps53) vesicle-tethering complex and Arfaptin 2. Arl1 is not required for exocytosis, but appears necessary for trafficking from the endosomes to the Golgi. In Drosophila zygotes, mutation of Arl1 is lethal, and in the host-bloodstream form of Trypanosoma brucei, Arl1 is essential for viability.


Pssm-ID: 206718 [Multi-domain]  Cd Length: 158  Bit Score: 172.98  E-value: 2.29e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   23 IVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIKVtlgnsKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVVDS 102
Cdd:cd04151   2 ILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTY-----KNLKFQVWDLGGQTSIRPYWRCYYSNTDAIIYVVDS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730  103 VDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIEKLLAMGELSSSTpWHLQPTCAIIGDGLKEGLEKL 182
Cdd:cd04151  77 TDRDRLGISKSELHAMLEEEELKDAVLLVFANKQDMPGALSEAEVAEKLGLSELKDRT-WQIFKTSATKGEGLDEGMDWL 155
PLN00223 PLN00223
ADP-ribosylation factor; Provisional
9-189 5.00e-55

ADP-ribosylation factor; Provisional


Pssm-ID: 165788  Cd Length: 181  Bit Score: 172.84  E-value: 5.00e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730     9 TSILSSLPSFQSFHIVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIKVtlgnsKTVTFHFWDVGGQEKLRPLWKS 88
Cdd:PLN00223   6 TKLFSRLFAKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEY-----KNISFTVWDVGGQDKIRPLWRH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730    89 YTRCTDGIVFVVDSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIEKLLAMGELSSSTpWHLQPTC 168
Cdd:PLN00223  81 YFQNTQGLIFVVDSNDRDRVVEARDELHRMLNEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRQRH-WYIQSTC 159
                        170       180
                 ....*....|....*....|.
gi 6680730   169 AIIGDGLKEGLEKLHDMIIKR 189
Cdd:PLN00223 160 ATSGEGLYEGLDWLSNNIANK 180
PTZ00133 PTZ00133
ADP-ribosylation factor; Provisional
1-191 8.17e-54

ADP-ribosylation factor; Provisional


Pssm-ID: 173423  Cd Length: 182  Bit Score: 169.64  E-value: 8.17e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730     1 MGNGLSdqtSILSSLPSFQSFHIVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIKVtlgnsKTVTFHFWDVGGQE 80
Cdd:PTZ00133   1 MGLWLS---SAFKSLFGKKEVRILMVGLDAAGKTTILYKLKLGEVVTTIPTIGFNVETVEY-----KNLKFTMWDVGGQD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730    81 KLRPLWKSYTRCTDGIVFVVDSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIEKLLAMGELSSST 160
Cdd:PTZ00133  73 KLRPLWRHYYQNTNGLIFVVDSNDRERIGDAREELERMLSEDELRDAVLLVFANKQDLPNAMSTTEVTEKLGLHSVRQRN 152
                        170       180       190
                 ....*....|....*....|....*....|.
gi 6680730   161 pWHLQPTCAIIGDGLKEGLEKLHDMIIKRRK 191
Cdd:PTZ00133 153 -WYIQGCCATTAQGLYEGLDWLSANIKKSMQ 182
Arl5_Arl8 cd04153
Arf-like 5 (Arl5) and 8 (Arl8) GTPases; Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like ...
9-180 2.07e-53

Arf-like 5 (Arl5) and 8 (Arl8) GTPases; Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like Arl4 and Arl7, are localized to the nucleus and nucleolus. Arl5 is developmentally regulated during embryogenesis in mice. Human Arl5 interacts with the heterochromatin protein 1-alpha (HP1alpha), a nonhistone chromosomal protein that is associated with heterochromatin and telomeres, and prevents telomere fusion. Arl5 may also play a role in embryonic nuclear dynamics and/or signaling cascades. Arl8 was identified from a fetal cartilage cDNA library. It is found in brain, heart, lung, cartilage, and kidney. No function has been assigned for Arl8 to date.


Pssm-ID: 133353 [Multi-domain]  Cd Length: 174  Bit Score: 168.30  E-value: 2.07e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730    9 TSILSSLPSFQSFHIVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIKVtlgnsKTVTFHFWDVGGQEKLRPLWKS 88
Cdd:cd04153   4 SSLWSLFFPRKEYKVIIVGLDNAGKTTILYQFLLGEVVHTSPTIGSNVEEIVY-----KNIRFLMWDIGGQESLRSSWNT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   89 YTRCTDGIVFVVDSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIEKLLAMGELSSSTpWHLQPTC 168
Cdd:cd04153  79 YYTNTDAVILVIDSTDRERLPLTKEELYKMLAHEDLRKAVLLVLANKQDLKGAMTPAEISESLGLTSIRDHT-WHIQGCC 157
                       170
                ....*....|..
gi 6680730  169 AIIGDGLKEGLE 180
Cdd:cd04153 158 ALTGEGLPEGLD 169
Arl3 cd04155
Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most ...
11-180 1.24e-46

Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most Arf family members in the N-terminal extension. In is inactive, GDP-bound form, the N-terminal extension forms an elongated loop that is hydrophobically anchored into the membrane surface; however, it has been proposed that this region might form a helix in the GTP-bound form. The delta subunit of the rod-specific cyclic GMP phosphodiesterase type 6 (PDEdelta) is an Arl3 effector. Arl3 binds microtubules in a regulated manner to alter specific aspects of cytokinesis via interactions with retinitis pigmentosa 2 (RP2). It has been proposed that RP2 functions in concert with Arl3 to link the cell membrane and the cytoskeleton in photoreceptors as part of the cell signaling or vesicular transport machinery. In mice, the absence of Arl3 is associated with abnormal epithelial cell proliferation and cyst formation.


Pssm-ID: 206721 [Multi-domain]  Cd Length: 174  Bit Score: 151.40  E-value: 1.24e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   11 ILSSLPSFQSF-----HIVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIkvtlgNSKTVTFHFWDVGGQEKLRPL 85
Cdd:cd04155   1 LLSILRKLKPSsrqevRILLLGLDNAGKTTILKQLASEDISHITPTQGFNIKNV-----QADGFKLNVWDIGGQRKIRPY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   86 WKSYTRCTDGIVFVVDSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIEKLLAMGELSSSTpWHLQ 165
Cdd:cd04155  76 WRNYFENTDVLIYVIDSADRKRFEEAGQELVELLEEEKLAGVPVLVFANKQDLLTAAPAEEVAEALNLHDIRDRS-WHIQ 154
                       170
                ....*....|....*
gi 6680730  166 PTCAIIGDGLKEGLE 180
Cdd:cd04155 155 ACSAKTGEGLQEGMN 169
Arl2 cd04154
Arf-like 2 (Arl2) GTPase; Arl2 (Arf-like 2) GTPases are members of the Arf family that bind ...
23-182 2.84e-44

Arf-like 2 (Arl2) GTPase; Arl2 (Arf-like 2) GTPases are members of the Arf family that bind GDP and GTP with very low affinity. Unlike most Arf family proteins, Arl2 is not myristoylated at its N-terminal helix. The protein PDE-delta, first identified in photoreceptor rod cells, binds specifically to Arl2 and is structurally very similar to RhoGDI. Despite the high structural similarity between Arl2 and Rho proteins and between PDE-delta and RhoGDI, the interactions between the GTPases and their effectors are very different. In its GTP bound form, Arl2 interacts with the protein Binder of Arl2 (BART), and the complex is believed to play a role in mitochondrial adenine nucleotide transport. In its GDP bound form, Arl2 interacts with tubulin- folding Cofactor D; this interaction is believed to play a role in regulation of microtubule dynamics that impact the cytoskeleton, cell division, and cytokinesis.


Pssm-ID: 206720 [Multi-domain]  Cd Length: 173  Bit Score: 145.16  E-value: 2.84e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   23 IVILGLDCAGKTTVLYRLQfNEFVNTV-PTKGFNTEKIKVtlgnsKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVVD 101
Cdd:cd04154  17 ILMLGLDNAGKTTILKKFN-GEDISTIsPTLGFNIKTLEY-----NGYKLNIWDVGGQKSLRSYWRNYFESTDALIWVVD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730  102 SVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIEKLLAMGELSSSTpWHLQPTCAIIGDGLKEGLEK 181
Cdd:cd04154  91 SSDRARLEDCKRELQKLLVEERLAGATLLIFANKQDLPGALSPEEIREVLELDSIKSHH-WRIFGCSAVTGENLLDGIDW 169

                .
gi 6680730  182 L 182
Cdd:cd04154 170 L 170
Arfrp1 cd04160
Arf-related protein 1 (Arfrp1); Arfrp1 (Arf-related protein 1), formerly known as ARP, is a ...
23-184 3.80e-40

Arf-related protein 1 (Arfrp1); Arfrp1 (Arf-related protein 1), formerly known as ARP, is a membrane-associated Arf family member that lacks the N-terminal myristoylation motif. Arfrp1 is mainly associated with the trans-Golgi compartment and the trans-Golgi network, where it regulates the targeting of Arl1 and the GRIP domain-containing proteins, golgin-97 and golgin-245, onto Golgi membranes. It is also involved in the anterograde transport of the vesicular stomatitis virus G protein from the Golgi to the plasma membrane, and in the retrograde transport of TGN38 and Shiga toxin from endosomes to the trans-Golgi network. Arfrp1 also inhibits Arf/Sec7-dependent activation of phospholipase D. Deletion of Arfrp1 in mice causes embryonic lethality at the gastrulation stage and apoptosis of mesodermal cells, indicating its importance in development.


Pssm-ID: 206725 [Multi-domain]  Cd Length: 168  Bit Score: 134.39  E-value: 3.80e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   23 IVILGLDCAGKTTVLYRLQfNEFvnTVPTKGFNTEKIKVTLG-NSKTVTF-----HFWDVGGQEKLRPLWKSYTRCTDGI 96
Cdd:cd04160   2 VLILGLDNAGKTTFLEQTK-TKF--SKNYKGLNPSKITPTVGlNIGTIEVgkarlMFWDLGGQEELRSLWDKYYAESHGV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   97 VFVVDSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIEKLL-AMGELSSSTPWHLQPTCAIIGDGL 175
Cdd:cd04160  79 IYVIDSTDRERFNESKSAFEKVINNEALEGVPLLVLANKQDLPDALSVAEIKEVFdDCIALIGRRDCLVQPVSALEGEGV 158

                ....*....
gi 6680730  176 KEGLEKLHD 184
Cdd:cd04160 159 EEGIEWLVD 167
Arl6 cd04157
Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small ...
22-185 1.72e-39

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: 132.55  E-value: 1.72e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   22 HIVILGLDCAGKTTVLYRLQFNEF--VNTVPTKGFNTEKIKvtlgnSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFV 99
Cdd:cd04157   1 NILVLGLDNSGKTTIINQLKPSNAqsQNIVPTVGFNVESFK-----KGNLSFTAFDMSGQGKYRGLWEHYYKNIQGIIFV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730  100 VDSVDVERMEEAKTELHKITRISE--NQGVPVLIVANKQDLRNSLSLSEIEKLLAMgELSSSTPWHLQPTCAIIGDGLKE 177
Cdd:cd04157  76 IDSSDRLRMVVAKDELELLLNHPDikHRRIPILFYANKMDLPDALTAVKITQLLCL-ENIKDKPWHIFASSALTGEGLDE 154

                ....*...
gi 6680730  178 GLEKLHDM 185
Cdd:cd04157 155 GVDWLQAQ 162
ARD1 cd04158
(ADP-ribosylation factor domain protein 1 (ARD1); ARD1 (ADP-ribosylation factor domain protein ...
23-187 3.76e-39

(ADP-ribosylation factor domain protein 1 (ARD1); ARD1 (ADP-ribosylation factor domain protein 1) is an unusual member of the Arf family. In addition to the C-terminal Arf domain, ARD1 has an additional 46-kDa N-terminal domain that contains a RING finger domain, two predicted B-Boxes, and a coiled-coil protein interaction motif. This domain belongs to the TRIM (tripartite motif) or RBCC (RING, B-Box, coiled-coil) family. Like most Arfs, the ARD1 Arf domain lacks detectable GTPase activity. However, unlike most Arfs, the full-length ARD1 protein has significant GTPase activity due to the GAP (GTPase-activating protein) activity exhibited by the 46-kDa N-terminal domain. The GAP domain of ARD1 is specific for its own Arf domain and does not bind other Arfs. The rate of GDP dissociation from the ARD1 Arf domain is slowed by the adjacent 15 amino acids, which act as a GDI (GDP-dissociation inhibitor) domain. ARD1 is ubiquitously expressed in cells and localizes to the Golgi and to the lysosomal membrane. Two Tyr-based motifs in the Arf domain are responsible for Golgi localization, while the GAP domain controls lysosomal localization.


Pssm-ID: 206723 [Multi-domain]  Cd Length: 169  Bit Score: 132.07  E-value: 3.76e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   23 IVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIKVtlgnsKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVVDS 102
Cdd:cd04158   2 VVTLGLDGAGKTTILFKLKQDEFMQPIPTIGFNVETVEY-----KNLKFTIWDVGGKHKLRPLWKHYYLNTQAVVFVIDS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730  103 VDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIEKLLAMGELSSSTPWHLQPTCAIIGDGLKEGLEKL 182
Cdd:cd04158  77 SHRDRVSEAHSELAKLLTEKELRDALLLIFANKQDVAGALSVEEMTELLSLHKLCCGRSWYIQGCDARSGMGLYEGLDWL 156

                ....*
gi 6680730  183 HDMII 187
Cdd:cd04158 157 SRQLV 161
Sar1 cd00879
Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII ...
9-151 5.97e-39

Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII vesicle coats involved in export of cargo from the ER. The GTPase activity of Sar1 functions as a molecular switch to control protein-protein and protein-lipid interactions that direct vesicle budding from the ER. Activation of the GDP to the GTP-bound form of Sar1 involves the membrane-associated guanine nucleotide exchange factor (GEF) Sec12. Sar1 is unlike all Ras superfamily GTPases that use either myristoyl or prenyl groups to direct membrane association and function, in that Sar1 lacks such modification. Instead, Sar1 contains a unique nine-amino-acid N-terminal extension. This extension contains an evolutionarily conserved cluster of bulky hydrophobic amino acids, referred to as the Sar1-N-terminal activation recruitment (STAR) motif. The STAR motif mediates the recruitment of Sar1 to ER membranes and facilitates its interaction with mammalian Sec12 GEF leading to activation.


Pssm-ID: 206645 [Multi-domain]  Cd Length: 191  Bit Score: 132.02  E-value: 5.97e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730    9 TSILSSLPSFQ-SFHIVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIkvTLGNsktVTFHFWDVGGQEKLRPLWK 87
Cdd:cd00879   7 YNVLSSLGLYKkEAKIVFLGLDNAGKTTLLHMLKDDRLAQHVPTLHPTSEEL--TIGN---VKFTTFDLGGHEQARRVWK 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6680730   88 SYTRCTDGIVFVVDSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIEKLL 151
Cdd:cd00879  82 DYFPEVDGIVFLVDAADPERFQESKEELDSLLNDEELANVPILILGNKIDKPGAVSEEELREAL 145
Arl9_Arfrp2_like cd04162
Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first ...
23-186 7.15e-36

Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first identified as part of the Human Cancer Genome Project. It maps to chromosome 4q12 and is sometimes referred to as Arfrp2 (Arf-related protein 2). This is a novel subfamily identified in human cancers that is uncharacterized to date.


Pssm-ID: 133362 [Multi-domain]  Cd Length: 164  Bit Score: 123.33  E-value: 7.15e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   23 IVILGLDCAGKTTVLYRLQFNEFV-NTVPTKGFNTEKIkvtlgNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVVD 101
Cdd:cd04162   2 ILVLGLDGAGKTSLLHSLSSERSLeSVVPTTGFNSVAI-----PTQDAIMELLEIGGSQNLRKYWKRYLSGSQGLIFVVD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730  102 SVDVERMEEAKTELHKItrISENQGVPVLIVANKQDLRNSLSLSEIEKLLAMGELSSSTPWHLQPTcAIIGDGLKEGLEK 181
Cdd:cd04162  77 SADSERLPLARQELHQL--LQHPPDLPLVVLANKQDLPAARSVQEIHKELELEPIARGRRWILQGT-SLDDDGSPSRMEA 153

                ....*
gi 6680730  182 LHDMI 186
Cdd:cd04162 154 VKDLL 158
Arl10_like cd04159
Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from ...
23-150 5.02e-33

Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from a human cancer-derived EST dataset. No functional information about the subfamily is available at the current time, but crystal structures of human Arl10b and Arl10c have been solved.


Pssm-ID: 206724 [Multi-domain]  Cd Length: 159  Bit Score: 115.88  E-value: 5.02e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   23 IVILGLDCAGKTTVLYRLQFNEFV-NTVPTKGFNTEKikVTLGNsktVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVVD 101
Cdd:cd04159   2 ITLVGLQNSGKTTLVNVIASGQFSeDTIPTVGFNMRK--VTKGN---VTIKVWDLGGQPRFRSMWERYCRGVNAIVYVVD 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6680730  102 SVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSE-IEKL 150
Cdd:cd04159  77 AADREKLEVAKNELHDLLEKPSLEGIPLLVLGNKNDLPGALSVDElIEQM 126
Arl2l1_Arl13_like cd04161
Arl2-like protein 1 (Arl2l1) and Arl13; Arl2l1 (Arl2-like protein 1) and Arl13 form a ...
23-189 1.21e-28

Arl2-like protein 1 (Arl2l1) and Arl13; Arl2l1 (Arl2-like protein 1) and Arl13 form a subfamily of the Arf family of small GTPases. Arl2l1 was identified in human cells during a search for the gene(s) responsible for Bardet-Biedl syndrome (BBS). Like Arl6, the identified BBS gene, Arl2l1 is proposed to have cilia-specific functions. Arl13 is found on the X chromosome, but its expression has not been confirmed; it may be a pseudogene.


Pssm-ID: 133361 [Multi-domain]  Cd Length: 167  Bit Score: 104.78  E-value: 1.21e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   23 IVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFntEKIKVTLGNSKTVTFhfwDVGGQEKLRPLWKSYTRCTDGIVFVVDS 102
Cdd:cd04161   2 LLTVGLDNAGKTTLVSALQGEIPKKVAPTVGF--TPTKLRLDKYEVCIF---DLGGGANFRGIWVNYYAEAHGLVFVVDS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730  103 VDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIEKLLAMGEL--SSSTPWHLQPTCAIigdglkEGLE 180
Cdd:cd04161  77 SDDDRVQEVKEILRELLQHPRVSGKPILVLANKQDKKNALLGADVIEYLSLEKLvnENKSLCHIEPCSAI------EGLG 150

                ....*....
gi 6680730  181 KLHDMIIKR 189
Cdd:cd04161 151 KKIDPSIVE 159
SAR smart00178
Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene ...
11-159 6.83e-25

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: 95.77  E-value: 6.83e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730      11 ILSSLPSFQSF-HIVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIkvTLGNSKTVTFhfwDVGGQEKLRPLWKSY 89
Cdd:smart00178   7 ILASLGLWNKHaKILFLGLDNAGKTTLLHMLKNDRLAQHQPTQHPTSEEL--AIGNIKFTTF---DLGGHQQARRLWKDY 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730      90 TRCTDGIVFVVDSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIEKLLAMGELSSS 159
Cdd:smart00178  82 FPEVNGIVYLVDAYDKERFAESKRELDALLSDEELATVPFLILGNKIDAPYAASEDELRYALGLTNTTTG 151
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
23-154 8.64e-23

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: 89.74  E-value: 8.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730     23 IVILGLDCAGKTTVLYRLQFNEFVNT--VPTKGFNTEKIKVTLgNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVV 100
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNKGSITeyYPGTTRNYVTTVIEE-DGKTYKFNLLDTAGQEDYDAIRRLYYPQVERSLRVF 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6680730    101 DSVD-VERMEEAKTELHKITRISENQGVPVLIVANKQDLR-NSLSLSEIEKLLAMG 154
Cdd:TIGR00231  83 DIVIlVLDVEEILEKQTKEIIHHADSGVPIILVGNKIDLKdADLKTHVASEFAKLN 138
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
23-194 2.00e-21

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 86.57  E-value: 2.00e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   23 IVILGLDCAGKTTVLYRLQFNEF--VNTVPTKGFNTEKIKVTLgNSKTVTFHFWDVGGQEKLRPLWKSYTRC---TDGIV 97
Cdd:COG1100   6 IVVVGTGGVGKTSLVNRLVGDIFslEKYLSTNGVTIDKKELKL-DGLDVDLVIWDTPGQDEFRETRQFYARQltgASLYL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   98 FVVDSVDVERMEEAKTELHKITRISENqgVPVLIVANKQDLRNSLSLSEIEKLlaMGELSSSTPWHLQPTCAIIGDGLKE 177
Cdd:COG1100  85 FVVDGTREETLQSLYELLESLRRLGKK--SPIILVLNKIDLYDEEEIEDEERL--KEALSEDNIVEVVATSAKTGEGVEE 160
                       170
                ....*....|....*..
gi 6680730  178 GLEKLHDMIIKRRKMLR 194
Cdd:COG1100 161 LFAALAEILRGEGDSLD 177
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
23-137 8.31e-19

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: 77.93  E-value: 8.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730     23 IVILGLDCAGKTTVLYRLQFNEFV-NTVPTKG--FNTEKIKVTLGNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFV 99
Cdd:pfam08477   2 VVLLGDSGVGKTSLLKRFVDDTFDpKYKSTIGvdFKTKTVLENDDNGKKIKLNIWDTAGQERFRSLHPFYYRGAAAALLV 81
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 6680730    100 VDSVDVERMEEAKTELHKItriseNQGVPVLIVANKQD 137
Cdd:pfam08477  82 YDSRTFSNLKYWLRELKKY-----AGNSPVILVGNKID 114
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
24-182 2.45e-17

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: 75.19  E-value: 2.45e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   24 VILGLDCAGKTTVLYRLqFNEFVNTV-----PTKGFNTEKIKVtlgNSKTVTFHFWDVGGQEKLRPLW-----KSYTRCT 93
Cdd:cd00882   1 VVVGRGGVGKSSLLNAL-LGGEVGEVsdvpgTTRDPDVYVKEL---DKGKVKLVLVDTPGLDEFGGLGreelaRLLLRGA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   94 DGIVFVVDSVDVERMEEAKTELHKITRiseNQGVPVLIVANKQDLRNSlslSEIEKLLAMGELSSSTPWHLQPTCAIIGD 173
Cdd:cd00882  77 DLILLVVDSTDRESEEDAKLLILRRLR---KEGIPIILVGNKIDLLEE---REVEELLRLEELAKILGVPVFEVSAKTGE 150

                ....*....
gi 6680730  174 GLKEGLEKL 182
Cdd:cd00882 151 GVDELFEKL 159
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
22-151 1.18e-16

Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.


Pssm-ID: 206691 [Multi-domain]  Cd Length: 202  Bit Score: 74.67  E-value: 1.18e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   22 HIVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIKvtLGNSKTVTFHFWDVGGQEKLRP-LWKSYTRCTDGIVFVV 100
Cdd:cd04105   2 TVLLLGPSDSGKTALFTKLTTGKVRSTVTSIEPNVASFY--SNSSKGKKLTLVDVPGHEKLRDkLLEYLKASLKAIVFVV 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 6680730  101 DSVDVER-MEEAKTELHKITRISEN--QGVPVLIVANKQDLRNSLSLSEIEKLL 151
Cdd:cd04105  80 DSATFQKnIRDVAEFLYDILTDLEKikNKIPILIACNKQDLFTAKPAKKIKELL 133
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
23-140 2.20e-16

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


Pssm-ID: 425451 [Multi-domain]  Cd Length: 162  Bit Score: 72.93  E-value: 2.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730     23 IVILGLDCAGKTTVLYRLQFNEFVNT-VPTKGFNtEKIKVTLGNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVVD 101
Cdd:pfam00071   2 LVLVGDGGVGKSSLLIRFTQNKFPEEyIPTIGVD-FYTKTIEVDGKTVKLQIWDTAGQERFRALRPLYYRGADGFLLVYD 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 6680730    102 SVDVERMEEAKTELHKITRISENqGVPVLIVANKQDLRN 140
Cdd:pfam00071  81 ITSRDSFENVKKWVEEILRHADE-NVPIVLVGNKCDLED 118
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
21-140 4.57e-16

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: 71.72  E-value: 4.57e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLYRLQFNEFV-NTVPTKG--FNTEKIKVtlgNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIV 97
Cdd:cd00154   1 FKIVLIGDSGVGKTSLLLRFVDNKFSeNYKSTIGvdFKSKTIEV---DGKKVKLQIWDTAGQERFRSITSSYYRGAHGAI 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 6680730   98 FVVDSVDVERMEEAKTELHKITRISeNQGVPVLIVANKQDLRN 140
Cdd:cd00154  78 LVYDVTNRESFENLDKWLNELKEYA-PPNIPIILVGNKSDLED 119
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
21-160 9.53e-14

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


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 65.99  E-value: 9.53e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730      21 FHIVILGLDCAGKTTVLYRLQFNEFVN-TVPTKG--FNTEKIKVtlgNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIV 97
Cdd:smart00175   1 FKIILIGDSGVGKSSLLSRFTDGKFSEqYKSTIGvdFKTKTIEV---DGKRVKLQIWDTAGQERFRSITSSYYRGAVGAL 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6680730      98 FVVDSVDVERMEEAKTELHKItRISENQGVPVLIVANKQDLRNS--------LSLSEIEKLLAMgELSSST 160
Cdd:smart00175  78 LVYDITNRESFENLENWLKEL-REYASPNVVIMLVGNKSDLEEQrqvsreeaEAFAEEHGLPFF-ETSAKT 146
Rab5_related cd01860
Rab-related GTPase family includes Rab5 and Rab22; regulates early endosome fusion; The ...
20-141 8.22e-12

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: 60.64  E-value: 8.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   20 SFHIVILGLDCAGKTTVLYRLQFNEFV-NTVPTKG--FNTEKIKVtlgNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGI 96
Cdd:cd01860   1 QFKLVLLGDSSVGKSSIVLRFVKNEFSeNQESTIGaaFLTQTVNL---DDTTVKFEIWDTAGQERYRSLAPMYYRGAAAA 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 6680730   97 VFVVDSVDVERMEEAKT---ELHKitriSENQGVPVLIVANKQDLRNS 141
Cdd:cd01860  78 IVVYDITSEESFEKAKSwvkELQE----HGPPNIVIALAGNKADLESK 121
Rab1_Ypt1 cd01869
Rab GTPase family 1 includes the yeast homolog Ypt1; Rab1/Ypt1 subfamily. Rab1 is found in ...
21-141 1.03e-11

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


Pssm-ID: 206661 [Multi-domain]  Cd Length: 166  Bit Score: 60.42  E-value: 1.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLYRLQFNEFVNT-VPTKGFNTeKIKVTLGNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFV 99
Cdd:cd01869   3 FKLLLIGDSGVGKSCLLLRFADDTYTESyISTIGVDF-KIRTIELDGKTVKLQIWDTAGQERFRTITSSYYRGAHGIIIV 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 6680730  100 VDSVDVERMEEAKTELHKITRISeNQGVPVLIVANKQDLRNS 141
Cdd:cd01869  82 YDVTDQESFNNVKQWLQEIDRYA-SENVNKLLVGNKCDLTDK 122
Rab18 cd01863
Rab GTPase family 18 (Rab18); Rab18 subfamily. Mammalian Rab18 is implicated in endocytic ...
21-140 3.38e-11

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: 58.86  E-value: 3.38e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLYRLQFNEFV-NTVPTKG--FNTEKIKVtlgNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIV 97
Cdd:cd01863   1 LKILLIGDSGVGKSSLLLRFTDDTFDeDLSSTIGvdFKVKTVTV---DGKKVKLAIWDTAGQERFRTLTSSYYRGAQGVI 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 6680730   98 FVVDSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRN 140
Cdd:cd01863  78 LVYDVTRRDTFDNLDTWLNELDTYSTNPDAVKMLVGNKIDKEN 120
Ras cd00876
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ...
23-141 6.91e-11

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: 57.92  E-value: 6.91e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   23 IVILGLDCAGKTTVLYRLQFNEFVNT-VPTKG--FNTEkIKVtlgNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFV 99
Cdd:cd00876   2 LVVLGAGGVGKSALTIRFVSGEFVEEyDPTIEdsYRKQ-IVV---DGETYTLDILDTAGQEEFSAMRDQYIRNGDGFILV 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 6680730  100 VDSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNS 141
Cdd:cd00876  78 YSITSRESFEEIKNIREQILRVKDKEDVPIVLVGNKCDLENE 119
Srp102 COG2229
Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, ...
23-189 7.00e-11

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


Pssm-ID: 441830 [Multi-domain]  Cd Length: 189  Bit Score: 58.68  E-value: 7.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   23 IVILGLDCAGKTTvlyrlqfneFVNTV------PTKGFNTEKIKVTLGnSKTVTFHF--WDVG-----------GQEKLR 83
Cdd:COG2229  15 IVYAGPFGAGKTT---------FVRSIseieplSTEGRLTDASLETKT-TTTVAFDFgrLTLGdglrlhlfgtpGQVRFD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   84 PLWKSYTRCTDGIVFVVDSvDVERMEEAKTELHKITRISEnqGVPVLIVANKQDLRNSLSLSEIEKLLAmgelsSSTPWH 163
Cdd:COG2229  85 FMWDILLRGADGVVFLADS-RRLEDSFNAESLDFFEERLE--KLPFVVAVNKRDLPDALSLEELREALD-----LGPDVP 156
                       170       180
                ....*....|....*....|....*.
gi 6680730  164 LQPTCAIIGDGLKEGLEKLHDMIIKR 189
Cdd:COG2229 157 VVEADARDGESVKETLIALLELVLAR 182
RalA_RalB cd04139
Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily ...
21-138 2.82e-10

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: 56.67  E-value: 2.82e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLYRLQFNEFVNTV-PTKGFNTEKiKVTLGnSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGiVFV 99
Cdd:cd04139   1 HKVIMVGSGGVGKSALTLQFMYDEFVEDYePTKADSYRK-KVVLD-GEEVQLNILDTAGQEDYAAIRDNYFRSGEG-FLL 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 6680730  100 VDSVDVERMEEAKTELH-KITRISENQGVPVLIVANKQDL 138
Cdd:cd04139  78 VFSITDMESFTALAEFReQILRVKEDDNVPLLLVGNKCDL 117
Rab21 cd04123
Rab GTPase family 21 (Rab21); The localization and function of Rab21 are not clearly defined, ...
21-150 5.10e-10

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: 55.69  E-value: 5.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLYRLQFNEF-VNTVPT-KGFNTEKIKVTLGnsKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVF 98
Cdd:cd04123   1 FKVVLLGEGRVGKTSLVLRYVENKFnEKHESTtQASFFQKTVNIGG--KRIDLAIWDTAGQERYHALGPIYYRDADGAIL 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 6680730   99 VVDSVDVERMEEAKTELHKITRISENQGVPVlIVANKQDLRN--SLSLSEIEKL 150
Cdd:cd04123  79 VYDITDADSFQKVKKWIKELKQMRGNNISLV-IVGNKIDLERqrVVSKSEAEEY 131
PLN03110 PLN03110
Rab GTPase; Provisional
21-146 6.16e-10

Rab GTPase; Provisional


Pssm-ID: 178657 [Multi-domain]  Cd Length: 216  Bit Score: 56.48  E-value: 6.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730    21 FHIVILGLDCAGKTTVLYRLQFNEF-VNTVPTKG--FNTEKIKVtlgNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIV 97
Cdd:PLN03110  13 FKIVLIGDSGVGKSNILSRFTRNEFcLESKSTIGveFATRTLQV---EGKTVKAQIWDTAGQERYRAITSAYYRGAVGAL 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 6680730    98 FVVDSVDVERMEEAKTELHKItRISENQGVPVLIVANKQDLRNSLSLSE 146
Cdd:PLN03110  90 LVYDITKRQTFDNVQRWLREL-RDHADSNIVIMMAGNKSDLNHLRSVAE 137
RocCOR cd09914
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ...
25-188 7.11e-10

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


Pssm-ID: 206741 [Multi-domain]  Cd Length: 161  Bit Score: 55.42  E-value: 7.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   25 ILGLDCAGKTTVLYRLQFNEFV-NTVPTKGFNTEKIKVTLGNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVVDSV 103
Cdd:cd09914   6 LVGQGGVGKTSLCKQLIGEKFDgDESSTHGINVQDWKIPAPERKKIRLNVWDFGGQEIYHATHQFFLTSRSLYLLVFDLR 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730  104 DVERMEEAKTELHKITRISENQgvPVLIVANKQDlrnSLSLSEIEKLLAMgELSSSTPWHLQPTCAIIGDGLKEglekLH 183
Cdd:cd09914  86 TGDEVSRVPYWLRQIKAFGGVS--PVILVGTHID---ESCDEDILKKALN-KKFPAIINDIHFVSCKNGKGIAE----LK 155

                ....*
gi 6680730  184 DMIIK 188
Cdd:cd09914 156 KAIAK 160
RHO smart00174
Rho (Ras homology) subfamily of Ras-like small GTPases; Members of this subfamily of Ras-like ...
23-140 1.33e-09

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: 54.93  E-value: 1.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730      23 IVILGLDCAGKTTVLYRLQFNEF-VNTVPTKGFN-TEKIKVtlgNSKTVTFHFWDVGGQE---KLRPLwkSYTRcTDG-- 95
Cdd:smart00174   1 LVVVGDGAVGKTCLLIVYTTNAFpEDYVPTVFENySADVEV---DGKPVELGLWDTAGQEdydRLRPL--SYPD-TDVfl 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 6680730      96 IVFVVDSVDveRMEEAKTelHKITRISE-NQGVPVLIVANKQDLRN 140
Cdd:smart00174  75 ICFSVDSPA--SFENVKE--KWYPEVKHfCPNVPIILVGTKLDLRN 116
Rab8_Rab10_Rab13_like cd01867
Rab GTPase families 8, 10, 13 (Rab8, Rab10, Rab13); Rab8/Sec4/Ypt2 are known or suspected to ...
21-138 1.42e-09

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: 54.58  E-value: 1.42e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLYRLQFNEFVNT-VPTKGFNTeKIKVTLGNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFV 99
Cdd:cd01867   4 FKLLLIGDSGVGKSCLLLRFSEDSFNPSfISTIGIDF-KIRTIELDGKKIKLQIWDTAGQERFRTITTSYYRGAMGIILV 82
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 6680730  100 VDSVDVERMEEAKTELHKITRISeNQGVPVLIVANKQDL 138
Cdd:cd01867  83 YDITDEKSFENIKNWMRNIDEHA-SEDVERMLVGNKCDM 120
PLN03118 PLN03118
Rab family protein; Provisional
20-148 1.78e-09

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 55.06  E-value: 1.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730    20 SFHIVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIKVTLGnSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFV 99
Cdd:PLN03118  14 SFKILLIGDSGVGKSSLLVSFISSSVEDLAPTIGVDFKIKQLTVG-GKRLKLTIWDTAGQERFRTLTSSYYRNAQGIILV 92
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6680730   100 vdsVDVERmEEAKTEL-----HKITRISENQGVPVLIVANKQDLRNSLSLSEIE 148
Cdd:PLN03118  93 ---YDVTR-RETFTNLsdvwgKEVELYSTNQDCVKMLVGNKVDRESERDVSREE 142
SRPRB pfam09439
Signal recognition particle receptor beta subunit; The beta subunit of the signal recognition ...
23-151 2.30e-09

Signal recognition particle receptor beta subunit; The beta subunit of the signal recognition particle receptor (SRP) is a transmembrane GTPase which anchors the alpha subunit to the endoplasmic reticulum membrane.


Pssm-ID: 462797 [Multi-domain]  Cd Length: 181  Bit Score: 54.37  E-value: 2.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730     23 IVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFN-TEKIKVTLGNSKTVTfhfwDVGGQEKLRPLWKSYTRCTD---GIVF 98
Cdd:pfam09439   6 VIIAGLCDSGKTSLFTLLTTDSVRPTVTSQEPSaAYRYMLNKGNSFTLI----DFPGHVKLRYKLLETLKDSSslkGIVF 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6680730     99 VVDS-VDVERMEEAKTELHKITRISE--NQGVPVLIVANKQDLRNSLSLSEIEKLL 151
Cdd:pfam09439  82 VVDStIFPKEVTDTAEFLYDILSITEllKNGIDILIACNKQESFTARPPKKIKQAL 137
Rho cd00157
Ras homology family (Rho) of small guanosine triphosphatases (GTPases); Members of the Rho ...
23-140 2.96e-09

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: 53.70  E-value: 2.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   23 IVILGLDCAGKTTVLYRLQFNEFVNT-VPTKgFNTEKIKVTLGNsKTVTFHFWDVGGQE---KLRPLwkSYTRcTDG--I 96
Cdd:cd00157   3 IVVVGDGAVGKTCLLISYTTNKFPTEyVPTV-FDNYSANVTVDG-KQVNLGLWDTAGQEeydRLRPL--SYPQ-TDVflL 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6680730   97 VFVVDSvdvermeeaKTELHKITR--ISE----NQGVPVLIVANKQDLRN 140
Cdd:cd00157  78 CFSVDS---------PSSFENVKTkwYPEikhyCPNVPIILVGTKIDLRD 118
Rab11_like cd01868
Rab GTPase family 11 (Rab11)-like includes Rab11a, Rab11b, and Rab25; Rab11a, Rab11b, and ...
21-139 3.96e-09

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: 53.33  E-value: 3.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLYRLQFNEF-VNTVPTKG--FNTEKIKVtlgNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIV 97
Cdd:cd01868   4 FKIVLIGDSGVGKSNLLSRFTRNEFnLDSKSTIGveFATRTIQI---DGKTIKAQIWDTAGQERYRAITSAYYRGAVGAL 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 6680730   98 FVVD---SVDVERMEEAKTELHKITriseNQGVPVLIVANKQDLR 139
Cdd:cd01868  81 LVYDitkKSTFENVERWLKELRDHA----DSNIVIMLVGNKSDLR 121
Rab35 cd04110
Rab GTPase family 35 (Rab35); Rab35 is one of several Rab proteins to be found to participate ...
21-137 7.31e-09

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: 53.32  E-value: 7.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLYRLQFNEFV-NTVPTKGFNTeKIKVTLGNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFV 99
Cdd:cd04110   7 FKLLIIGDSGVGKSSLLLRFADNTFSgSYITTIGVDF-KIRTVEINGERVKLQIWDTAGQERFRTITSTYYRGTHGVIVV 85
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 6680730  100 VDSVDVERMEEAKTELHKITRISENqgVPVLIVANKQD 137
Cdd:cd04110  86 YDVTNGESFVNVKRWLQEIEQNCDD--VCKVLVGNKND 121
Rab33B_Rab33A cd04115
Rab GTPase family 33 includes Rab33A and Rab33B; Rab33B/Rab33A subfamily. Rab33B is ...
21-145 9.93e-09

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: 52.44  E-value: 9.93e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLYRLQFNEFV-NTVPTKG---------FNTEKIKVTLgnsktvtfhfWDVGGQEKLRplwKS-- 88
Cdd:cd04115   3 FKIIVIGDSNVGKTCLTYRFCAGRFPeRTEATIGvdfrertveIDGERIKVQL----------WDTAGQERFR---KSmv 69
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6680730   89 --YTRCTDGIVFVVDSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLS 145
Cdd:cd04115  70 qhYYRNVHAVVFVYDVTNMASFHSLPSWIEECEQHSLPNEVPRILVGNKCDLREQIQVP 128
Rab3 cd01865
Rab GTPase family 3 contains Rab3A, Rab3B, Rab3C and Rab3D; The Rab3 subfamily contains Rab3A, ...
21-145 1.04e-08

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: 52.22  E-value: 1.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLYRLQFNEFVNT-VPTKGFNTeKIKVTLGNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFV 99
Cdd:cd01865   2 FKLLIIGNSSVGKTSFLFRYADDSFTSAfVSTVGIDF-KVKTVYRNDKRIKLQIWDTAGQERYRTITTAYYRGAMGFILM 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 6680730  100 VDSVDVERMEEAKTELHKITRISENQGvPVLIVANKQDLRNSLSLS 145
Cdd:cd01865  81 YDITNEESFNAVQDWSTQIKTYSWDNA-QVILVGNKCDMEDERVVS 125
Rho2 cd04129
Ras homology family 2 (Rho2) of small guanosine triphosphatases (GTPases); Rho2 is a fungal ...
23-139 1.35e-08

Ras homology family 2 (Rho2) of small guanosine triphosphatases (GTPases); Rho2 is a fungal GTPase that plays a role in cell morphogenesis, control of cell wall integrity, control of growth polarity, and maintenance of growth direction. Rho2 activates the protein kinase C homolog Pck2, and Pck2 controls Mok1, the major (1-3) alpha-D-glucan synthase. Together with Rho1 (RhoA), Rho2 regulates the construction of the cell wall. Unlike Rho1, Rho2 is not an essential protein, but its overexpression is lethal. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for proper intracellular localization via membrane attachment. As with other Rho family GTPases, the GDP/GTP cycling is regulated by GEFs (guanine nucleotide exchange factors), GAPs (GTPase-activating proteins) and GDIs (guanine nucleotide dissociation inhibitors).


Pssm-ID: 206702 [Multi-domain]  Cd Length: 190  Bit Score: 52.53  E-value: 1.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   23 IVILGLDCAGKTTVLYRLQFNEFVNT-VPT--KGFNTEkIKVtlgNSKTVTFHFWDVGGQ---EKLRPLwkSYTRC-TDG 95
Cdd:cd04129   4 LVIVGDGACGKTSLLYVFTLGEFPEEyHPTvfENYVTD-CRV---DGKPVQLALWDTAGQeeyERLRPL--SYSKAhVIL 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 6680730   96 IVFVVDSVDveRMEEAKTE-LHKITRISENqgVPVLIVANKQDLR 139
Cdd:cd04129  78 IGFAIDTPD--SLENVRTKwIEEVRRYCPN--VPVILVGLKKDLR 118
Rab6 cd01861
Rab GTPase family 6 (Rab6); Rab6 is involved in microtubule-dependent transport pathways ...
21-138 6.33e-08

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: 49.93  E-value: 6.33e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLYRLQFNEFVNTV-PTKG--FNTEKIKVtlgNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIV 97
Cdd:cd01861   1 HKLVFLGDQSVGKTSIITRFMYDTFDNQYqATIGidFLSKTMYV---DDKTVRLQLWDTAGQERFRSLIPSYIRDSSVAV 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 6680730   98 FVVDSVDVERMEEAKTELHKITRISENQgVPVLIVANKQDL 138
Cdd:cd01861  78 VVYDITNRQSFDNTDKWIDDVRDERGND-VIIVLVGNKTDL 117
RSR1 cd04177
RSR1/Bud1p family GTPase; RSR1/Bud1p is a member of the Rap subfamily of the Ras family that ...
21-145 6.59e-08

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: 50.17  E-value: 6.59e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIKVTLGNsKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVV 100
Cdd:cd04177   2 YKIVVLGAGGVGKSALTVQFVQNVFIESYDPTIEDSYRKQVEIDG-RQCDLEILDTAGTEQFTAMRELYIKSGQGFLLVY 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 6680730  101 DSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLS 145
Cdd:cd04177  81 SVTSEASLNELGELREQVLRIKDSDNVPMVLVGNKADLEDDRQVS 125
Rab28 cd04109
Rab GTPase family 28 (Rab28); Rab28 subfamily. First identified in maize, Rab28 has been shown ...
21-138 8.95e-08

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: 50.57  E-value: 8.95e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLYRLQFNEFVNTVP-TKGFNTEKIKVTLGNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFV 99
Cdd:cd04109   1 IKIVVLGDGASGKTSLIRRFAQEGFGKSYKqTIGLDFFSRRITLPGSLNVTLQVWDIGGQQIGGKMLDKYIYGAQAVCLV 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 6680730  100 VD---SVDVERMEEAKTELHKITRISENQgVPVLIVANKQDL 138
Cdd:cd04109  81 YDitnSQSFENLEDWLSVVKKVNEESETK-PKMVLVGNKTDL 121
Rab14 cd04122
Rab GTPase family 14 (Rab14); Rab14 GTPases are localized to biosynthetic compartments, ...
21-141 9.53e-08

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


Pssm-ID: 133322 [Multi-domain]  Cd Length: 166  Bit Score: 49.83  E-value: 9.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLYRLQFNEFVNTVP-TKG--FNTEKIKVtlgNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIV 97
Cdd:cd04122   3 FKYIIIGDMGVGKSCLLHQFTEKKFMADCPhTIGveFGTRIIEV---NGQKIKLQIWDTAGQERFRAVTRSYYRGAAGAL 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 6680730   98 FVVDSVDVERMEEAKTELHKiTRISENQGVPVLIVANKQDLRNS 141
Cdd:cd04122  80 MVYDITRRSTYNHLSSWLTD-ARNLTNPNTVIFLIGNKADLEAQ 122
Rab4 cd04113
Rab GTPase family 4 (Rab4); Rab4 subfamily. Rab4 has been implicated in numerous functions ...
21-139 1.02e-07

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


Pssm-ID: 206696 [Multi-domain]  Cd Length: 161  Bit Score: 49.36  E-value: 1.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLYRLQFNEFV-NTVPTKG--FNTEKIKVtlgNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIV 97
Cdd:cd04113   1 FKFLIIGSAGTGKSCLLHQFIENKFKqDSNHTIGveFGSRVVNV---GGKSVKLQIWDTAGQERFRSVTRSYYRGAAGAL 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 6680730   98 FVVDSVDVERMEEAKTELHKiTRISENQGVPVLIVANKQDLR 139
Cdd:cd04113  78 LVYDITSRESFNALTNWLTD-ARTLASPDIVIILVGNKKDLE 118
Rab36_Rab34 cd04108
Rab GTPase families 34 (Rab34) and 36 (Rab36); Rab34/Rab36 subfamily. Rab34, found primarily ...
20-149 1.06e-07

Rab GTPase families 34 (Rab34) and 36 (Rab36); Rab34/Rab36 subfamily. Rab34, found primarily in the Golgi, interacts with its effector, Rab-interacting lysosomal protein (RILP). This enables its participation in microtubular dynenin-dynactin-mediated repositioning of lysosomes from the cell periphery to the Golgi. A Rab34 (Rah) isoform that lacks the consensus GTP-binding region has been identified in mice. This isoform is associated with membrane ruffles and promotes macropinosome formation. Rab36 has been mapped to human chromosome 22q11.2, a region that is homozygously deleted in malignant rhabdoid tumors (MRTs). However, experimental assessments do not implicate Rab36 as a tumor suppressor that would enable tumor formation through a loss-of-function mechanism. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins.


Pssm-ID: 206693 [Multi-domain]  Cd Length: 170  Bit Score: 49.49  E-value: 1.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   20 SFHIVIlGLDCAGKTTVLYRLQFNEF-VNTVPTKG--FNTEKIKVtLGNSKTVtfHFWDVGGQEKLRPLWKSYTRCTDGI 96
Cdd:cd04108   1 SKVIVV-GDLSVGKTCLINRFCKDVFdKNYKATIGvdFEMERFEV-LGVPFSL--QLWDTAGQERFKCIASTYYRGAQAI 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 6680730   97 VFVVDSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIEK 149
Cdd:cd04108  77 IIVFDLTDVASLEHTRQWLEDALKENDPSSVLLFLVGTKKDLSSPAQYALMEQ 129
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
24-182 1.17e-07

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


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 49.17  E-value: 1.17e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   24 VILGLDCAGKTTVLYRLqFNEFVNTV-PTKGFNTEKIKVTLGNSKTVTFHFWDVGG--------QEKLRPLWKSYTRcTD 94
Cdd:cd00880   1 AIFGRPNVGKSSLLNAL-LGQNVGIVsPIPGTTRDPVRKEWELLPLGPVVLIDTPGldeegglgRERVEEARQVADR-AD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   95 GIVFVVDS-VDVERMEEAKTELHKitrisenQGVPVLIVANKQDLRNSlslSEIEKLLAMGELSSSTPWHLQPTCAIIGD 173
Cdd:cd00880  79 LVLLVVDSdLTPVEEEAKLGLLRE-------RGKPVLLVLNKIDLVPE---SEEEELLRERKLELLPDLPVIAVSALPGE 148

                ....*....
gi 6680730  174 GLKEGLEKL 182
Cdd:cd00880 149 GIDELRKKI 157
PLN03071 PLN03071
GTP-binding nuclear protein Ran; Provisional
16-140 1.35e-07

GTP-binding nuclear protein Ran; Provisional


Pssm-ID: 178620 [Multi-domain]  Cd Length: 219  Bit Score: 49.75  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730    16 PSFQSFHIVILGLDCAGKTTVLYRLQFNEF-VNTVPTKGFNTEKIKVTLgNSKTVTFHFWDVGGQEKLRPLWKSYTRCTD 94
Cdd:PLN03071   9 VDYPSFKLVIVGDGGTGKTTFVKRHLTGEFeKKYEPTIGVEVHPLDFFT-NCGKIRFYCWDTAGQEKFGGLRDGYYIHGQ 87
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 6680730    95 GIVFVVDSVDVERMEEAKTELHKITRISENqgVPVLIVANKQDLRN 140
Cdd:PLN03071  88 CAIIMFDVTARLTYKNVPTWHRDLCRVCEN--IPIVLCGNKVDVKN 131
Rho4_like cd04132
Ras homology family 4 (Rho4) of small guanosine triphosphatases (GTPases)-like; Rho4 is a ...
20-139 1.83e-07

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: 49.26  E-value: 1.83e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   20 SFHIVILGLDCAGKTTVLYRLQFNEFVNT-VPTKgFNTEKIKVTLGNSKTVTFHFWDVGGQE---KLRPLwkSYTRcTDg 95
Cdd:cd04132   3 KVKIVVVGDGGCGKTCLLMVYAQGSFPEEyVPTV-FENYVTTLQVPNGKIIELALWDTAGQEdydRLRPL--SYPD-VD- 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6680730   96 IVFVVDSVDvermeeAKTELHKITRI--SENQ----GVPVLIVANKQDLR 139
Cdd:cd04132  78 VILICYSVD------NPTSLDNVEDKwyPEVNhfcpGTPIVLVGLKTDLR 121
Rab39 cd04111
Rab GTPase family 39 (Rab39); Found in eukaryotes, Rab39 is mainly found in epithelial cell ...
21-192 4.55e-07

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


Pssm-ID: 133311 [Multi-domain]  Cd Length: 211  Bit Score: 48.22  E-value: 4.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLYRLQFNEFVNTV-PTKG--FNTEKIKVTLGnsKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIV 97
Cdd:cd04111   3 FRLIVIGDSTVGKSSLLKRFTEGRFAEVSdPTVGvdFFSRLIEIEPG--VRIKLQLWDTAGQERFRSITRSYYRNSVGVL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   98 FVVDSVDVERMEEAKtELHKITRISENQGVPV-LIVANKQDLRNSLSLSEIEKllamGELSSSTPWHLQPTCAIIGDGLK 176
Cdd:cd04111  81 LVFDITNRESFEHVH-DWLEEARSHIQPHRPVfILVGHKCDLESQRQVTREEA----EKLAKDLGMKYIETSARTGDNVE 155
                       170
                ....*....|....*.
gi 6680730  177 EGLEKLHDMIIKRRKM 192
Cdd:cd04111 156 EAFELLTQEIYERIKR 171
Rho3 cd04134
Ras homology family 3 (Rho3) of small guanosine triphosphatases (GTPases); Rho3 is a member of ...
23-140 6.63e-07

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: 47.55  E-value: 6.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   23 IVILGLDCAGKTTVLYRLQFNEFVNTV-PTKGFNTEKIKVTLGNSktVTFHFWDVGGQE---KLRPLWKSYTRCTdGIVF 98
Cdd:cd04134   3 VVVLGDGACGKTSLLNVFTRGYFPQVYePTVFENYIHDIFVDGLA--VELSLWDTAGQEefdRLRSLSYADTHVI-MLCF 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 6680730   99 VVDSVDVERMEEAKTelhkITRISEN-QGVPVLIVANKQDLRN 140
Cdd:cd04134  80 SVDNPDSLENVESKW----LAEIRHHcPGVKLVLVALKCDLRE 118
RhoA_like cd01870
Ras homology family A (RhoA)-like includes RhoA, RhoB and RhoC; The RhoA subfamily consists of ...
23-140 6.91e-07

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


Pssm-ID: 206662 [Multi-domain]  Cd Length: 175  Bit Score: 47.42  E-value: 6.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   23 IVILGLDCAGKTTVLY---RLQFNE-FVNTVptkgFNT--EKIKVtlgNSKTVTFHFWDVGGQE---KLRPLwkSYTRcT 93
Cdd:cd01870   4 LVIVGDGACGKTCLLIvfsKDQFPEvYVPTV----FENyvADIEV---DGKQVELALWDTAGQEdydRLRPL--SYPD-T 73
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 6680730   94 DGIV--FVVDSVD-VERMEEAKT-ELHKITrisenQGVPVLIVANKQDLRN 140
Cdd:cd01870  74 DVILmcFSIDSPDsLENIPEKWTpEVKHFC-----PNVPIILVGNKKDLRN 119
Rab12 cd04120
Rab GTPase family 12 (Rab12); Rab12 was first identified in canine cells, where it was ...
23-137 9.70e-07

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: 47.31  E-value: 9.70e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   23 IVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIKVTLGNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVVDS 102
Cdd:cd04120   3 VIIIGSRGVGKTSLMERFTDDTFCEACKSTVGVDFKIKTVELRGKKIRLQIWDTAGQERFNSITSAYYRSAKGIILVYDI 82
                        90       100       110
                ....*....|....*....|....*....|....*
gi 6680730  103 VDVERMEEAKTELHKITRISeNQGVPVLIVANKQD 137
Cdd:cd04120  83 TKKETFDDLPKWMKMIDKYA-SEDAELLLVGNKLD 116
RhoG cd01875
Ras homolog family, member G (RhoG) of small guanosine triphosphatases (GTPases); RhoG is a ...
19-161 1.91e-06

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


Pssm-ID: 133277 [Multi-domain]  Cd Length: 191  Bit Score: 46.54  E-value: 1.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   19 QSFHIVILGLDCAGKTTVLYRLQFNEFVNT-VPTKgFNTEKIKVTLgNSKTVTFHFWDVGGQE---KLRPLwkSYTRcTD 94
Cdd:cd01875   2 QSIKCVVVGDGAVGKTCLLICYTTNAFPKEyIPTV-FDNYSAQTAV-DGRTVSLNLWDTAGQEeydRLRTL--SYPQ-TN 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6680730   95 GIVFVVDSVDVERMEEAKTELHKitRISEN-QGVPVLIVANKQDLRNSLSLseIEKLLAMGeLSSSTP 161
Cdd:cd01875  77 VFIICFSIASPSSYENVRHKWHP--EVCHHcPNVPILLVGTKKDLRNDADT--LKKLKEQG-QAPITP 139
Rab19 cd01864
Rab GTPase family 19 (Rab19); Rab19 subfamily. Rab19 proteins are associated with Golgi stacks. ...
21-158 1.97e-06

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


Pssm-ID: 133267 [Multi-domain]  Cd Length: 165  Bit Score: 45.89  E-value: 1.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLYRLQFNEFV----NTVPTKgFNTEKIKVtlgNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGI 96
Cdd:cd01864   4 FKIILIGDSNVGKTCVVQRFKSGTFSerqgNTIGVD-FTMKTLEI---QGKRVKLQIWDTAGQERFRTITQSYYRSANGA 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   97 VFVVDSVDVERMEEAKTELHKITRISENQGVPVLIvANKQDL--------RNSLSLSEIEKLLAMGELSS 158
Cdd:cd01864  80 IIAYDITRRSSFESVPHWIEEVEKYGASNVVLLLI-GNKCDLeeqrevlfEEACTLAEHYGILAVLETSA 148
RERG_RasL11_like cd04146
Ras-related and Estrogen-Regulated Growth inhibitor (RERG) and Ras-like 11 (RasL11)-like ...
22-159 4.09e-06

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: 44.96  E-value: 4.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   22 HIVILGLDCAGKTTVLYRlqfneFVntvpTKGF------NTEKI---KVTLgNSKTVTFHFWDVGGQE--KLRPLWKSYT 90
Cdd:cd04146   1 KIAVLGASGVGKSALTVR-----FL----TKRFigeyepNLESLysrQVTI-DGEQVSLEIQDTPGQQqnEDPESLERSL 70
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   91 RCTDGIVFVVDSVDVERMEEAKTELHKITRISENQG-VPVLIVANKQDLRNSLSLSEIEKLLAMGELSSS 159
Cdd:cd04146  71 RWADGFVLVYSITDRSSFDVVSQLLQLIREIKKRDGeIPVILVGNKADLLHSRQVSTEEGQKLALELGCL 140
Rab27A cd04127
Rab GTPase family 27a (Rab27a); The Rab27a subfamily consists of Rab27a and its highly ...
26-189 7.00e-06

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: 44.80  E-value: 7.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   26 LGLDCAGKTTVLYRL---QFN-EFVNTVPTKG------FNTEKIKVTLGNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDG 95
Cdd:cd04127  10 LGDSGVGKTTFLYRYtdnKFNpKFITTVGIDFrekrvvYNSQGPDGTSGKAFRVHLQLWDTAGQERFRSLTTAFFRDAMG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   96 IVFVVDSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEiEKLLAMGElSSSTPWHlqPTCAIIGDGL 175
Cdd:cd04127  90 FLLMFDLTSEQSFLNVRNWMSQLQAHAYCENPDIVLIGNKADLPDQREVSE-RQARELAD-KYGIPYF--ETSAATGQNV 165
                       170
                ....*....|....
gi 6680730  176 KEGLEKLHDMIIKR 189
Cdd:cd04127 166 EKAVETLLDLIMKR 179
Rab15 cd04117
Rab GTPase family 15 (Rab15); Rab15 colocalizes with the transferrin receptor in early ...
21-107 1.16e-05

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: 43.81  E-value: 1.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLYRLQFNEFVNT-VPTKGFNTeKIKVTLGNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFV 99
Cdd:cd04117   1 FRLLLIGDSGVGKTCLLCRFTDNEFHSShISTIGVDF-KMKTIEVDGIKVRIQIWDTAGQERYQTITKQYYRRAQGIFLV 79

                ....*...
gi 6680730  100 VDsVDVER 107
Cdd:cd04117  80 YD-ISSER 86
PTZ00132 PTZ00132
GTP-binding nuclear protein Ran; Provisional
20-140 1.19e-05

GTP-binding nuclear protein Ran; Provisional


Pssm-ID: 240284 [Multi-domain]  Cd Length: 215  Bit Score: 44.30  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730    20 SFHIVILGLDCAGKTTVLYRLQFNEFVNT-VPTKGFNTEKIKVTLgNSKTVTFHFWDVGGQEKLRPLWKSY---TRCTDg 95
Cdd:PTZ00132   9 EFKLILVGDGGVGKTTFVKRHLTGEFEKKyIPTLGVEVHPLKFYT-NCGPICFNVWDTAGQEKFGGLRDGYyikGQCAI- 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 6680730    96 IVFVVDSVDVERMEEaktELHK-ITRISENqgVPVLIVANKQDLRN 140
Cdd:PTZ00132  87 IMFDVTSRITYKNVP---NWHRdIVRVCEN--IPIVLVGNKVDVKD 127
G-alpha pfam00503
G-protein alpha subunit; G proteins couple receptors of extracellular signals to intracellular ...
49-138 1.22e-05

G-protein alpha subunit; G proteins couple receptors of extracellular signals to intracellular signaling pathways. The G protein alpha subunit binds guanyl nucleotide and is a weak GTPase. A set of residues that are unique to G-alpha as compared to its ancestor the Arf-like family form a ring of residues centered on the nucleotide binding site. A Ggamma is found fused to an inactive Galpha in the Dictyostelium protein gbqA.


Pssm-ID: 459835 [Multi-domain]  Cd Length: 316  Bit Score: 44.89  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730     49 VPTKGFNTEKIKVtlgnsKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVV-----DSVDVE-----RMEEAKTELHKI 118
Cdd:pfam00503 152 VKTTGIIETKFEF-----KGLKFRLFDVGGQRSERKKWIHCFEDVTAIIFVVslseyDQVLYEddstnRMEESLKLFEEI 226
                          90       100
                  ....*....|....*....|
gi 6680730    119 TRISENQGVPVLIVANKQDL 138
Cdd:pfam00503 227 CNSPWFKNTPIILFLNKKDL 246
RAS smart00173
Ras subfamily of RAS small GTPases; Similar in fold and function to the bacterial EF-Tu GTPase. ...
23-150 1.42e-05

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: 43.31  E-value: 1.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730      23 IVILGLDCAGKTTVLYRLQFNEFVNTV-PT-KGFNTEKIKVtlgNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVV 100
Cdd:smart00173   3 LVVLGSGGVGKSALTIQFIQGHFVDDYdPTiEDSYRKQIEI---DGEVCLLDILDTAGQEEFSAMRDQYMRTGEGFLLVY 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 6680730     101 DSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNS--LSLSEIEKL 150
Cdd:smart00173  80 SITDRQSFEEIKKFREQILRVKDRDDVPIVLVGNKCDLESErvVSTEEGKEL 131
Rab7 cd01862
Rab GTPase family 7 (Rab7); Rab7 subfamily. Rab7 is a small Rab GTPase that regulates ...
21-146 1.53e-05

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: 43.42  E-value: 1.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLyrlqfNEFVNtvptKGFnTEKIKVTLG----------NSKTVTFHFWDVGGQEKLRPLWKSYT 90
Cdd:cd01862   1 LKVIILGDSGVGKTSLM-----NQYVN----KKF-SNQYKATIGadfltkevtvDDRLVTLQIWDTAGQERFQSLGVAFY 70
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6680730   91 RCTDGIVFVVD---SVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSE 146
Cdd:cd01862  71 RGADCCVLVYDvtnPKSFESLDSWRDEFLIQASPRDPENFPFVVLGNKIDLEEKRQVST 129
PTZ00369 PTZ00369
Ras-like protein; Provisional
21-148 1.84e-05

Ras-like protein; Provisional


Pssm-ID: 240385 [Multi-domain]  Cd Length: 189  Bit Score: 43.70  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730    21 FHIVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIKVTLgNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVV 100
Cdd:PTZ00369   6 YKLVVVGGGGVGKSALTIQFIQNHFIDEYDPTIEDSYRKQCVI-DEETCLLDILDTAGQEEYSAMRDQYMRTGQGFLCVY 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 6680730   101 DSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIE 148
Cdd:PTZ00369  85 SITSRSSFEEIASFREQILRVKDKDRVPMILVGNKCDLDSERQVSTGE 132
Rnd cd04131
Rho family GTPase subfamily Rnd includes Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8; The Rnd ...
23-143 2.52e-05

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


Pssm-ID: 206703 [Multi-domain]  Cd Length: 176  Bit Score: 42.81  E-value: 2.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   23 IVILGLDCAGKTT---VLYRLQFNE-FVNTV---PTKGFNTEKIKVTLGnsktvtfhFWDVGGQE---KLRPLwkSYTRc 92
Cdd:cd04131   4 IVLVGDSQCGKTAllqVFAKDSFPEnYVPTVfenYTASFEVDKQRIELS--------LWDTSGSPyydNVRPL--SYPD- 72
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 6680730   93 TDGIVFVVDsvdVERMEEAKTELHK-ITRISE-NQGVPVLIVANKQDLRNSLS 143
Cdd:cd04131  73 SDAVLICFD---ISRPETLDSVLKKwKGEVREfCPNTPVLLVGCKSDLRTDLS 122
PLN03108 PLN03108
Rab family protein; Provisional
21-150 3.23e-05

Rab family protein; Provisional


Pssm-ID: 178655 [Multi-domain]  Cd Length: 210  Bit Score: 43.01  E-value: 3.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730    21 FHIVILGLDCAGKTTVLyrLQFNEfvntvptKGF---NTEKIKVTLG------NSKTVTFHFWDVGGQEKLRPLWKSYTR 91
Cdd:PLN03108   7 FKYIIIGDTGVGKSCLL--LQFTD-------KRFqpvHDLTIGVEFGarmitiDNKPIKLQIWDTAGQESFRSITRSYYR 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6680730    92 CTDGIVFVVDSVDVERMEEAKTELHKiTRISENQGVPVLIVANKQDL--RNSLSLSEIEKL 150
Cdd:PLN03108  78 GAAGALLVYDITRRETFNHLASWLED-ARQHANANMTIMLIGNKCDLahRRAVSTEEGEQF 137
Rab30 cd04114
Rab GTPase family 30 (Rab30); Rab30 subfamily. Rab30 appears to be associated with the Golgi ...
21-138 3.80e-05

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: 42.58  E-value: 3.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLYRLQFNEFV-NTVPTKGFNTEKIKVTLGNSKtVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFV 99
Cdd:cd04114   8 FKIVLIGNAGVGKTCLVRRFTQGLFPpGQGATIGVDFMIKTVEIKGEK-IKLQIWDTAGQERFRSITQSYYRSANALILT 86
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 6680730  100 VDSVDVERMEEAKTELHKITRISENQGVPVLiVANKQDL 138
Cdd:cd04114  87 YDITCEESFRCLPEWLREIEQYANNKVITIL-VGNKIDL 124
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
22-135 4.73e-05

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 41.07  E-value: 4.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730     22 HIVILGLDCAGKTTVLYRLqFNEFVNTVPTKGFNTEKIKVTLgNSKTVTFHFWDVGG-------QEKLRPLWKSYTRCtD 94
Cdd:pfam01926   1 RVALVGRPNVGKSTLINAL-TGAKAIVSDYPGTTRDPNEGRL-ELKGKQIILVDTPGliegaseGEGLGRAFLAIIEA-D 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 6680730     95 GIVFVVDSVdvermEEAKTELHKITRISENQGVPVLIVANK 135
Cdd:pfam01926  78 LILFVVDSE-----EGITPLDEELLELLRENKKPIILVLNK 113
small_GTPase smart00010
Small GTPase of the Ras superfamily; ill-defined subfamily; SMART predicts Ras-like small ...
23-150 4.76e-05

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: 42.16  E-value: 4.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730      23 IVILGLDCAGKTTVLYRLQFNEFVNTV-PT-KGFNTEKIKVtlgNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVV 100
Cdd:smart00010   5 LVVLGGGGVGKSALTIQFVQGHFVDEYdPTiEDSYRKQIEI---DGEVCLLDILDTAGQEEFSAMRDQYMRTGEGFLLVY 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 6680730     101 DSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNS--LSLSEIEKL 150
Cdd:smart00010  82 SITDRQSFEEIAKFREQILRVKDRDDVPIVLVGNKCDLENErvVSTEEGKEL 133
Rab9 cd04116
Rab GTPase family 9 (Rab9); Rab9 is found in late endosomes, together with mannose 6-phosphate ...
21-138 5.37e-05

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: 41.78  E-value: 5.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLYRLQFNEF-VNTVPTKG--FNTEKIKVtlgNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDG-- 95
Cdd:cd04116   6 LKVILLGDGGVGKSSLMNRYVTNKFdTQLFHTIGveFLNKDLEV---DGHFVTLQIWDTAGQERFRSLRTPFYRGSDCcl 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 6680730   96 IVFVVDSVD-VERMEEAKTELHKITRISENQGVPVLIVANKQDL 138
Cdd:cd04116  83 LTFSVDDSQsFQNLSNWKKEFIYYADVKEPESFPFVILGNKIDI 126
Ras2 cd04144
Rat sarcoma (Ras) family 2 of small guanosine triphosphatases (GTPases); The Ras2 subfamily, ...
23-148 6.37e-05

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: 42.14  E-value: 6.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   23 IVILGLDCAGKTTVLYRLQFNEFVNTV-PTkgFNTEKIKVTLGNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVVD 101
Cdd:cd04144   2 LVVLGDGGVGKTALTIQLCLNHFVETYdPT--IEDSYRKQVVVDGQPCMLEVLDTAGQEEYTALRDQWIREGEGFILVYS 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 6680730  102 SVDVERMEEAKTELHKITRISENQ--GVPVLIVANKQDLRNSLSLSEIE 148
Cdd:cd04144  80 ITSRSTFERVERFREQIQRVKDESaaDVPIMIVGNKCDKVYEREVSTEE 128
Cdc42 cd01874
cell division cycle 42 (Cdc42) is a small GTPase of the Rho family; Cdc42 is an essential ...
24-150 1.04e-04

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


Pssm-ID: 206664 [Multi-domain]  Cd Length: 175  Bit Score: 41.40  E-value: 1.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   24 VILGLDCAGKTTVLYRLQFNEF-VNTVPTKgFNTEKIKVTLGNsKTVTFHFWDVGGQE---KLRPLwkSYTRcTDGIVFV 99
Cdd:cd01874   5 VVVGDGAVGKTCLLISYTTNKFpSEYVPTV-FDNYAVTVMIGG-EPYTLGLFDTAGQEdydRLRPL--SYPQ-TDVFLVC 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 6680730  100 VDSVDVERMEEAKTELHKITRiSENQGVPVLIVANKQDLRNSLSLseIEKL 150
Cdd:cd01874  80 FSVVSPSSFENVKEKWVPEIT-HHCPKTPFLLVGTQIDLRDDPST--IEKL 127
Spg1 cd04128
Septum-promoting GTPase (Spg1); Spg1p. Spg1p (septum-promoting GTPase) was first identified in ...
23-131 1.22e-04

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


Pssm-ID: 206701 [Multi-domain]  Cd Length: 182  Bit Score: 41.23  E-value: 1.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   23 IVILGlDC-AGKTTVLYRLQFNEF-VNTVPTKGFNTEKIKVTLGNsKTVTFHFWDVGGQEKLR---PLwksytRCTDG-- 95
Cdd:cd04128   3 IGLLG-DAqIGKTSLMVKYVEGEFdEEYIQTLGVNFMEKTISIRG-TEITFSIWDLGGQREFInmlPL-----VCKDAva 75
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 6680730   96 IVFVVDSVDVERMEEAKtELHKITRISENQGVPVLI 131
Cdd:cd04128  76 ILFMFDLTRKSTLNSIK-EWYRQARGFNKTAIPILV 110
RRP22 cd04142
Ras-related protein on chromosome 22 (RRP22) family; RRP22 (Ras-related protein on chromosome ...
21-139 1.23e-04

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: 41.39  E-value: 1.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLYRLQFNEFVNT-VPTKGFNTEKIKVTLgNSKTVTFHFWDV---------GGQEKLRPLWKSYt 90
Cdd:cd04142   1 VRVAVLGAPGVGKTAIVRQFLAQEFPEEyIPTEHRRLYRPAVVL-SGRVYDLHILDVpnmqrypgtAGQEWMDPRFRGL- 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 6680730   91 RCTDGIVFVVDSVDVERMEEAKTELHKI--TRISENQGVPVLIVANKQDLR 139
Cdd:cd04142  79 RNSRAFILVYDICSPDSFHYVKLLRQQIleTRPAGNKEPPIVVVGNKRDQQ 129
Rit_Rin_Ric cd04141
Ras-like protein in all tissues (Rit), Ras-like protein in neurons (Rin) and Ras-related ...
21-138 1.30e-04

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: 40.99  E-value: 1.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIKVTLGNsKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVV 100
Cdd:cd04141   3 YKIVMLGAGGVGKSAVTMQFISHSFPDYHDPTIEDAYKTQARIDN-EPALLDILDTAGQAEFTAMRDQYMRCGEGFIICY 81
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 6680730  101 DSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDL 138
Cdd:cd04141  82 SVTDRHSFQEASEFKELITRVRLTEDIPLVLVGNKVDL 119
Rab23_like cd04106
Rab GTPase family 23 (Rab23)-like; Rab23-like subfamily. Rab23 is a member of the Rab family ...
23-138 1.38e-04

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: 40.50  E-value: 1.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   23 IVILGLDCAGKTTVLYRLQFNEFVNTV-PTKGFNTEKIKVTLGNSKT-VTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVV 100
Cdd:cd04106   3 VIVVGNGNVGKSSMIQRFVKGIFTKDYkKTIGVDFLEKQIFLRQSDEdVRLMLWDTAGQEEFDAITKAYYRGAQACILVF 82
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 6680730  101 DSVDVERMEEAKTELHKITRISENqgVPVLIVANKQDL 138
Cdd:cd04106  83 STTDRESFEAIESWKEKVEAECGD--IPMVLVQTKIDL 118
Rap2 cd04176
Rap2 family GTPase consists of Rap2a, Rap2b, and Rap2c; The Rap2 subgroup is part of the Rap ...
21-138 3.07e-04

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: 39.82  E-value: 3.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLYRLQFNEFVNTV-PT-KGFNTEKIKVtlgNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVF 98
Cdd:cd04176   2 YKVVVLGSGGVGKSALTVQFVSGTFIEKYdPTiEDFYRKEIEV---DSSPSVLEILDTAGTEQFASMRDLYIKNGQGFIV 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 6680730   99 VVDSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDL 138
Cdd:cd04176  79 VYSLVNQQTFQDIKPMRDQIVRVKGYEKVPIILVGNKVDL 118
RAN smart00176
Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases; Ran is involved in the ...
32-140 3.38e-04

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


Pssm-ID: 128473 [Multi-domain]  Cd Length: 200  Bit Score: 39.99  E-value: 3.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730      32 GKTTVLYRLQFNEFVNT-VPTKGFNTEKIkVTLGNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVVDSVDVERMEE 110
Cdd:smart00176   7 GKTTFVKRHLTGEFEKKyVATLGVEVHPL-VFHTNRGPIRFNVWDTAGQEKFGGLRDGYYIQGQCAIIMFDVTARVTYKN 85
                           90       100       110
                   ....*....|....*....|....*....|
gi 6680730     111 AKTELHKITRISENqgVPVLIVANKQDLRN 140
Cdd:smart00176  86 VPNWHRDLVRVCEN--IPIVLCGNKVDVKD 113
Ran cd00877
Ras-related nuclear proteins (Ran)/TC4 family of small GTPases; Ran GTPase is involved in ...
21-139 4.62e-04

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


Pssm-ID: 206643 [Multi-domain]  Cd Length: 166  Bit Score: 39.21  E-value: 4.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLYRLQFNEFV-NTVPTKGFNTEKIKVTLgNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFV 99
Cdd:cd00877   1 FKLVLVGDGGTGKTTFVKRHLTGEFEkKYVATLGVEVHPLDFHT-NRGKIRFNVWDTAGQEKFGGLRDGYYIQGQCAIIM 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 6680730  100 VDSVD-VERMEEAKTelHK-ITRISENqgVPVLIVANKQDLR 139
Cdd:cd00877  80 FDVTSrVTYKNVPNW--HRdLVRVCEN--IPIVLCGNKVDIK 117
Rab24 cd04118
Rab GTPase family 24 (Rab24); Rab24 is distinct from other Rabs in several ways. It exists ...
23-138 6.15e-04

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: 39.08  E-value: 6.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   23 IVILGLDCAGKTTVLYRLQFNEFV-----NTVpTKGFNTEKIKVtlgNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIV 97
Cdd:cd04118   3 VVMLGKESVGKTSLVERYVHHRFLvgpyqNTI-GAAFVAKRMVV---GERVVTLGIWDTAGSERYEAMSRIYYRGAKAAI 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 6680730   98 FVVDSVDVERMEEAKTELHKITRISEnqGVPVLIVANKQDL 138
Cdd:cd04118  79 VCYDLTDSSSFERAKFWVKELQNLEE--HCKIYLCGTKSDL 117
Rap_like cd04136
Rap-like family consists of Rap1, Rap2 and RSR1; The Rap subfamily consists of the Rap1, Rap2, ...
21-148 7.80e-04

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: 38.69  E-value: 7.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLYRLQFNEFVNTV-PT-KGFNTEKIKVtlgNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVF 98
Cdd:cd04136   2 YKLVVLGSGGVGKSALTVQFVQGIFVDKYdPTiEDSYRKQIEV---DCQQCMLEILDTAGTEQFTAMRDLYIKNGQGFAL 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6680730   99 VVDSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIE 148
Cdd:cd04136  79 VYSITAQQSFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVSKEE 128
Rac1_like cd01871
Ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1)-like ...
24-150 8.68e-04

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


Pssm-ID: 206663 [Multi-domain]  Cd Length: 174  Bit Score: 38.64  E-value: 8.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   24 VILGLDCAGKTTVLYRLQFNEFVNT-VPTKgFNTEKIKVTLgNSKTVTFHFWDVGGQE---KLRPLwkSYTRcTDGIVFV 99
Cdd:cd01871   5 VVVGDGAVGKTCLLISYTTNAFPGEyIPTV-FDNYSANVMV-DGKPVNLGLWDTAGQEdydRLRPL--SYPQ-TDVFLIC 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 6680730  100 VDSVDVERMEEAKTELH-KITRISENqgVPVLIVANKQDLRNslSLSEIEKL 150
Cdd:cd01871  80 FSLVSPASFENVRAKWYpEVRHHCPN--TPIILVGTKLDLRD--DKDTIEKL 127
Rab26 cd04112
Rab GTPase family 26 (Rab26); Rab26 subfamily. First identified in rat pancreatic acinar cells, ...
21-138 9.93e-04

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


Pssm-ID: 206695 [Multi-domain]  Cd Length: 191  Bit Score: 38.69  E-value: 9.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLYRLQFNEFV--NTVPTKGFNTEKIKVTLGNSKtVTFHFWDVGGQEKLRPLWKSYTRCTDGIVF 98
Cdd:cd04112   1 FKVMLVGDSGVGKTCLLVRFKDGAFLagSFIATVGIQFTNKVVTVDGVK-VKLQIWDTAGQERFRSVTHAYYRDAHALLL 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 6680730   99 VVDSVDVERMEEAKTELHKITRISENQGVPVLIvANKQDL 138
Cdd:cd04112  80 LYDVTNKSSFDNIRAWLTEILEYAQSDVVIMLL-GNKADM 118
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, ...
75-140 1.07e-03

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: 38.17  E-value: 1.07e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6680730   75 DVGGQEKLRPLWKSYTRCTDGIVFVVDSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRN 140
Cdd:cd04138  55 DTAGQEEYSAMRDQYMRTGEGFLCVFAINSRKSFEDIHTYREQIKRVKDSDDVPMVLVGNKCDLAA 120
Rab2 cd01866
Rab GTPase family 2 (Rab2); Rab2 is localized on cis-Golgi membranes and interacts with Golgi ...
21-138 1.23e-03

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: 38.17  E-value: 1.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   21 FHIVILGLDCAGKTTVLyrLQFNE--FVN----TVPTKgFNTEKIKVtlgNSKTVTFHFWDVGGQEKLRPLWKSYTRCTD 94
Cdd:cd01866   5 FKYIIIGDTGVGKSCLL--LQFTDkrFQPvhdlTIGVE-FGARMITI---DGKQIKLQIWDTAGQESFRSITRSYYRGAA 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 6680730   95 GIVFVVDSVDVERMEEAKTELHKITRISeNQGVPVLIVANKQDL 138
Cdd:cd01866  79 GALLVYDITRRETFNHLTSWLEDARQHS-NSNMTIMLIGNKCDL 121
G-alpha cd00066
Alpha subunit of G proteins (guanine nucleotide binding); The alpha subunit of G proteins ...
49-138 1.32e-03

Alpha subunit of G proteins (guanine nucleotide binding); The alpha subunit of G proteins contains the guanine nucleotide binding site. The heterotrimeric GNP-binding proteins are signal transducers that communicate signals from many hormones, neurotransmitters, chemokines, and autocrine and paracrine factors. Extracellular signals are received by receptors, which activate the G proteins, which in turn route the signals to several distinct intracellular signaling pathways. The alpha subunit of G proteins is a weak GTPase. In the resting state, heterotrimeric G proteins are associated at the cytosolic face of the plasma membrane and the alpha subunit binds to GDP. Upon activation by a receptor GDP is replaced with GTP, and the G-alpha/GTP complex dissociates from the beta and gamma subunits. This results in activation of downstream signaling pathways, such as cAMP synthesis by adenylyl cyclase, which is terminated when GTP is hydrolized and the heterotrimers reconstitute.


Pssm-ID: 206639 [Multi-domain]  Cd Length: 315  Bit Score: 38.66  E-value: 1.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   49 VPTKGFNTEKIKVtlgnsKTVTFHFWDVGGQEKLRPLWksyTRCTDG---IVFVV-----DSVDVE-----RMEEAKTEL 115
Cdd:cd00066 146 VKTTGIIETDFSI-----KNLKFRMFDVGGQRSERKKW---IHCFEDvtaIIFVValseyDQVLVEdesvnRMQESLKLF 217
                        90       100
                ....*....|....*....|...
gi 6680730  116 HKITRISENQGVPVLIVANKQDL 138
Cdd:cd00066 218 DSICNSRWFANTSIILFLNKKDL 240
Rab32_Rab38 cd04107
Rab GTPase families 18 (Rab18) and 32 (Rab32); Rab38/Rab32 subfamily. Rab32 and Rab38 are ...
32-139 1.35e-03

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: 38.06  E-value: 1.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   32 GKTTVLYRlqfneFVNtvptkGFNTEKIKVTLG-----------NSKTVTFHFWDVGGQEKLRPLWKSYTRCTDG--IVF 98
Cdd:cd04107  12 GKTSIIKR-----YVH-----GVFSQHYKATIGvdfalkviewdPNTVVRLQLWDIAGQERFGGMTRVYYKGAVGaiIVF 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 6680730   99 vvdsvDVERME--EA----KTELHKITRISENQGVPVLIVANKQDLR 139
Cdd:cd04107  82 -----DVTRPStfEAvlkwKADLDSKVTLPNGEPIPALLLANKCDLK 123
PTZ00099 PTZ00099
rab6; Provisional
69-138 1.77e-03

rab6; Provisional


Pssm-ID: 185444 [Multi-domain]  Cd Length: 176  Bit Score: 37.80  E-value: 1.77e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730    69 VTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVVDSVDVERMEEAKTELHKITRiSENQGVPVLIVANKQDL 138
Cdd:PTZ00099  29 VRLQLWDTAGQERFRSLIPSYIRDSAAAIVVYDITNRQSFENTTKWIQDILN-ERGKDVIIALVGNKTDL 97
G_alpha smart00275
G protein alpha subunit; Subunit of G proteins that contains the guanine nucleotide binding ...
49-150 3.07e-03

G protein alpha subunit; Subunit of G proteins that contains the guanine nucleotide binding site


Pssm-ID: 214595 [Multi-domain]  Cd Length: 342  Bit Score: 37.56  E-value: 3.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730      49 VPTKGFNTEKIKVTLgnsktVTFHFWDVGGQEKLRPLWksyTRCTDG---IVFVV-----DSVDVE-----RMEEAKtEL 115
Cdd:smart00275 169 VPTTGIQETAFIVKK-----LFFRMFDVGGQRSERKKW---IHCFDNvtaIIFCValseyDQVLEEdestnRMQESL-NL 239
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 6680730     116 HKItrISENQ---GVPVLIVANKQDLrnslslsEIEKL 150
Cdd:smart00275 240 FES--ICNSRwfaNTSIILFLNKIDL-------FEEKI 268
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
86-182 3.59e-03

E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 36.67  E-value: 3.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   86 WKSYTRCtDGIVFVVDSVdvermEEAKTELHKITRISENQGVPVLIVANKQDL--RNSLSLSEIEKLLAMGElssstPWH 163
Cdd:cd04163  77 WSALKDV-DLVLFVVDAS-----EWIGEGDEFILELLKKSKTPVILVLNKIDLvkDKEDLLPLLEKLKELHP-----FAE 145
                        90
                ....*....|....*....
gi 6680730  164 LQPTCAIIGDGLKEGLEKL 182
Cdd:cd04163 146 IFPISALKGENVDELLEYI 164
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
96-186 4.49e-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: 36.32  E-value: 4.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680730   96 IVFVVDSVDVERMEEAKtelhkitRISENQGVPVLIVANKQDLRNSLSLSEIEKLLAMGELSSSTpwhlqptcaiiGDGL 175
Cdd:cd04164  86 VLLVVDASEGLDEEDLE-------ILELPAKKPVIVVLNKSDLLSDAEGISELNGKPIIAISAKT-----------GEGI 147
                        90
                ....*....|.
gi 6680730  176 KEGLEKLHDMI 186
Cdd:cd04164 148 DELKEALLELA 158
 
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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