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Conserved domains on  [gi|19923979|ref|NP_612459|]
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ADP-ribosylation factor-like protein 11 [Homo sapiens]

Protein Classification

ARLTS1 domain-containing protein( domain architecture ID 10134976)

ARLTS1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ARLTS1 cd04156
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ...
 14-172 8.84e-96

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: 275.06  E-value: 8.84e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  14 QVVMMGLDSAGKTTLLYKLKGHQLVETLPTVGFNVEPLKAPGHVSLTLWDVGGQAPLRASWKDYLEGTDILVYVLDSTDE 93
Cdd:cd04156   1 QVLLLGLDSAGKSTLLYKLKHAELVTTIPTVGFNVEMLQLEKHLSLTVWDVGGQEKMRTVWKCYLENTDGLVYVVDSSDE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  94 ARLPESAAELTEVLNDPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERFQD-HCWELRGCSALTGEGLPEALQSLWSL 172
Cdd:cd04156  81 ARLDESQKELKHILKNEHIKGVPVVLLANKQDLPGALTAEEITRRFKLKKYCSdRDWYVQPCSAVTGEGLAEAFRKLASF 160
 
Name Accession Description Interval E-value
ARLTS1 cd04156
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ...
 14-172 8.84e-96

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: 275.06  E-value: 8.84e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  14 QVVMMGLDSAGKTTLLYKLKGHQLVETLPTVGFNVEPLKAPGHVSLTLWDVGGQAPLRASWKDYLEGTDILVYVLDSTDE 93
Cdd:cd04156   1 QVLLLGLDSAGKSTLLYKLKHAELVTTIPTVGFNVEMLQLEKHLSLTVWDVGGQEKMRTVWKCYLENTDGLVYVVDSSDE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  94 ARLPESAAELTEVLNDPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERFQD-HCWELRGCSALTGEGLPEALQSLWSL 172
Cdd:cd04156  81 ARLDESQKELKHILKNEHIKGVPVVLLANKQDLPGALTAEEITRRFKLKKYCSdRDWYVQPCSAVTGEGLAEAFRKLASF 160
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
 13-169 1.99e-64

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


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 195.91  E-value: 1.99e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979    13 AQVVMMGLDSAGKTTLLYKLKGHQLVETLPTVGFNVEPLKApGHVSLTLWDVGGQAPLRASWKDYLEGTDILVYVLDSTD 92
Cdd:pfam00025   1 MRILILGLDNAGKTTILYKLKLGEIVTTIPTIGFNVETVTY-KNVKFTVWDVGGQESLRPLWRNYFPNTDAVIFVVDSAD 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19923979    93 EARLPESAAELTEVLNDPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERFQDHCWELRGCSALTGEGLPEALQSL 169
Cdd:pfam00025  80 RDRIEEAKEELHALLNEEELADAPLLILANKQDLPGAMSEAEIRELLGLHELKDRPWEIQGCSAVTGEGLDEGLDWL 156
ARF smart00177
ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular ...
 10-175 1.58e-49

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: 158.55  E-value: 1.58e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979     10 KAEAQVVMMGLDSAGKTTLLYKLKGHQLVETLPTVGFNVEPLKAPgHVSLTLWDVGGQAPLRASWKDYLEGTDILVYVLD 89
Cdd:smart00177  11 NKEMRILMVGLDAAGKTTILYKLKLGESVTTIPTIGFNVETVTYK-NISFTVWDVGGQDKIRPLWRHYYTNTQGLIFVVD 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979     90 STDEARLPESAAELTEVLNDPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERFQDHCWELRGCSALTGEGLPEALQSL 169
Cdd:smart00177  90 SNDRDRIDEAREELHRMLNEDELRDAVILVFANKQDLPDAMKAAEITEKLGLHSIRDRNWYIQPTCATSGDGLYEGLTWL 169


                   ....*.
gi 19923979    170 WSLLKS 175
Cdd:smart00177 170 SNNLKN 175
PLN00223 PLN00223
ADP-ribosylation factor; Provisional
 10-177 2.96e-47

ADP-ribosylation factor; Provisional


Pssm-ID: 165788  Cd Length: 181  Bit Score: 152.81  E-value: 2.96e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979   10 KAEAQVVMMGLDSAGKTTLLYKLKGHQLVETLPTVGFNVEPLKAPgHVSLTLWDVGGQAPLRASWKDYLEGTDILVYVLD 89
Cdd:PLN00223  15 KKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYK-NISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979   90 STDEARLPESAAELTEVLNDPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERFQDHCWELRGCSALTGEGLPEALQSL 169
Cdd:PLN00223  94 SNDRDRVVEARDELHRMLNEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRQRHWYIQSTCATSGEGLYEGLDWL 173


                 ....*...
gi 19923979  170 WSLLKSRS 177
Cdd:PLN00223 174 SNNIANKA 181
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
12-169 4.98e-19

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 80.03  E-value: 4.98e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  12 EAQVVMMGLDSAGKTTLLYKLKGHQ--LVETLPTVGFNVE--PLKAPGH-VSLTLWDVGGQ---APLRASWKDYLEGTDI 83
Cdd:COG1100   3 EKKIVVVGTGGVGKTSLVNRLVGDIfsLEKYLSTNGVTIDkkELKLDGLdVDLVIWDTPGQdefRETRQFYARQLTGASL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  84 LVYVLDSTDEARLpESAAELTEVLNDPNMAgVPFLVLANKQeapDALPLLKIRNRLSLERF--QDHCWELRGCSALTGEG 161
Cdd:COG1100  83 YLFVVDGTREETL-QSLYELLESLRRLGKK-SPIILVLNKI---DLYDEEEIEDEERLKEAlsEDNIVEVVATSAKTGEG 157


                ....*...
gi 19923979 162 LPEALQSL 169
Cdd:COG1100 158 VEELFAAL 165
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 12-129 1.18e-14

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: 68.17  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979    12 EAQVVMMGLDSAGKTTLLYKLKGHQL--VETLPTVGFNVEPLKA---PGHVSLTLWDVGGQAPLRASWKDYLEGTDILVY 86
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGsiTEYYPGTTRNYVTTVIeedGKTYKFNLLDTAGQEDYDAIRRLYYPQVERSLR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 19923979    87 VLD------STDEARLPEsaaelTEVLNDPNMAGVPFLVLANKQEAPDA 129
Cdd:TIGR00231  81 VFDivilvlDVEEILEKQ-----TKEIIHHADSGVPIILVGNKIDLKDA 124
 
Name Accession Description Interval E-value
ARLTS1 cd04156
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ...
 14-172 8.84e-96

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: 275.06  E-value: 8.84e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  14 QVVMMGLDSAGKTTLLYKLKGHQLVETLPTVGFNVEPLKAPGHVSLTLWDVGGQAPLRASWKDYLEGTDILVYVLDSTDE 93
Cdd:cd04156   1 QVLLLGLDSAGKSTLLYKLKHAELVTTIPTVGFNVEMLQLEKHLSLTVWDVGGQEKMRTVWKCYLENTDGLVYVVDSSDE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  94 ARLPESAAELTEVLNDPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERFQD-HCWELRGCSALTGEGLPEALQSLWSL 172
Cdd:cd04156  81 ARLDESQKELKHILKNEHIKGVPVVLLANKQDLPGALTAEEITRRFKLKKYCSdRDWYVQPCSAVTGEGLAEAFRKLASF 160
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
 14-167 1.06e-64

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: 196.26  E-value: 1.06e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  14 QVVMMGLDSAGKTTLLYKLKGHQLVETLPTVGFNVEPLKApGHVSLTLWDVGGQAPLRASWKDYLEGTDILVYVLDSTDE 93
Cdd:cd00878   1 RILMLGLDGAGKTTILYKLKLGEVVTTIPTIGFNVETVEY-KNVKFTVWDVGGQDKIRPLWKHYYENTDGLIFVVDSSDR 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19923979  94 ARLPESAAELTEVLNDPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERFQDHCWELRGCSALTGEGLPEALQ 167
Cdd:cd00878  80 ERIEEAKNELHKLLNEEELKGAPLLILANKQDLPGALTESELIELLGLESIKGRRWHIQPCSAVTGDGLDEGLD 153
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
 13-169 1.99e-64

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


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 195.91  E-value: 1.99e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979    13 AQVVMMGLDSAGKTTLLYKLKGHQLVETLPTVGFNVEPLKApGHVSLTLWDVGGQAPLRASWKDYLEGTDILVYVLDSTD 92
Cdd:pfam00025   1 MRILILGLDNAGKTTILYKLKLGEIVTTIPTIGFNVETVTY-KNVKFTVWDVGGQESLRPLWRNYFPNTDAVIFVVDSAD 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19923979    93 EARLPESAAELTEVLNDPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERFQDHCWELRGCSALTGEGLPEALQSL 169
Cdd:pfam00025  80 RDRIEEAKEELHALLNEEELADAPLLILANKQDLPGAMSEAEIRELLGLHELKDRPWEIQGCSAVTGEGLDEGLDWL 156
Arl5_Arl8 cd04153
Arf-like 5 (Arl5) and 8 (Arl8) GTPases; Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like ...
 8-166 7.77e-55

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: 171.76  E-value: 7.77e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979   8 GHKAEAQVVMMGLDSAGKTTLLYKLKGHQLVETLPTVGFNVEPLKAPGhVSLTLWDVGGQAPLRASWKDYLEGTDILVYV 87
Cdd:cd04153  11 FPRKEYKVIIVGLDNAGKTTILYQFLLGEVVHTSPTIGSNVEEIVYKN-IRFLMWDIGGQESLRSSWNTYYTNTDAVILV 89

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19923979  88 LDSTDEARLPESAAELTEVLNDPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERFQDHCWELRGCSALTGEGLPEAL 166
Cdd:cd04153  90 IDSTDRERLPLTKEELYKMLAHEDLRKAVLLVLANKQDLKGAMTPAEISESLGLTSIRDHTWHIQGCCALTGEGLPEGL 168
Arl3 cd04155
Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most ...
 10-166 4.07e-54

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: 170.27  E-value: 4.07e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  10 KAEAQVVMMGLDSAGKTTLLYKLKGHQLVETLPTVGFNVEPLKAPGhVSLTLWDVGGQAPLRASWKDYLEGTDILVYVLD 89
Cdd:cd04155  13 RQEVRILLLGLDNAGKTTILKQLASEDISHITPTQGFNIKNVQADG-FKLNVWDIGGQRKIRPYWRNYFENTDVLIYVID 91

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19923979  90 STDEARLPESAAELTEVLNDPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERFQDHCWELRGCSALTGEGLPEAL 166
Cdd:cd04155  92 SADRKRFEEAGQELVELLEEEKLAGVPVLVFANKQDLLTAAPAEEVAEALNLHDIRDRSWHIQACSAKTGEGLQEGM 168
Arl4_Arl7 cd04152
Arf-like 4 (Arl4) and 7 (Arl7) GTPases; Arl4 (Arf-like 4) is highly expressed in testicular ...
 15-184 3.45e-52

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: 165.36  E-value: 3.45e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  15 VVMMGLDSAGKTTLLYKLKGHQLVETLPTVGFNVEPLKAP----GHVSLTLWDVGGQAPLRASWKDYLEGTDILVYVLDS 90
Cdd:cd04152   6 IVMLGLDSAGKTTVLYRLKFNEFVNTVPTKGFNTEKIKVSlgnaKGVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVVDS 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  91 TDEARLPESAAELTEVLNDPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERFQDHC-WELRGCSALTGEGLPEALQSL 169
Cdd:cd04152  86 VDVERMEEAKTELHKITKFSENQGVPVLVLANKQDLPNALPVSEVEKLLALHELSSSTpWHVQPACAIIGEGLQEGLEKL 165

                       170
                ....*....|....*.
gi 19923979 170 WSL-LKSRSCMCLQAR 184
Cdd:cd04152 166 YEMiLKRRKMLRQQKK 181
Arf6 cd04149
ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins ...
 12-166 7.49e-52

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: 164.18  E-value: 7.49e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  12 EAQVVMMGLDSAGKTTLLYKLKGHQLVETLPTVGFNVEPLKAPgHVSLTLWDVGGQAPLRASWKDYLEGTDILVYVLDST 91
Cdd:cd04149   9 EMRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVETVTYK-NVKFNVWDVGGQDKIRPLWRHYYTGTQGLIFVVDSA 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19923979  92 DEARLPESAAELTEVLNDPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERFQDHCWELRGCSALTGEGLPEAL 166
Cdd:cd04149  88 DRDRIDEARQELHRIINDREMRDALLLVFANKQDLPDAMKPHEIQEKLGLTRIRDRNWYVQPSCATSGDGLYEGL 162
Arl2 cd04154
Arf-like 2 (Arl2) GTPase; Arl2 (Arf-like 2) GTPases are members of the Arf family that bind ...
 12-166 1.48e-51

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: 163.65  E-value: 1.48e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  12 EAQVVMMGLDSAGKTTLLYKLKGHQLVETLPTVGFNVEPLKAPGHvSLTLWDVGGQAPLRASWKDYLEGTDILVYVLDST 91
Cdd:cd04154  14 EMRILMLGLDNAGKTTILKKFNGEDISTISPTLGFNIKTLEYNGY-KLNIWDVGGQKSLRSYWRNYFESTDALIWVVDSS 92

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19923979  92 DEARLPESAAELTEVLNDPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERFQDHCWELRGCSALTGEGLPEAL 166
Cdd:cd04154  93 DRARLEDCKRELQKLLVEERLAGATLLIFANKQDLPGALSPEEIREVLELDSIKSHHWRIFGCSAVTGENLLDGI 167
Arl1 cd04151
ADP ribosylation factor 1 (Arf1); Arl1 subfamily. Arl1 (Arf-like 1) localizes to the Golgi ...
 14-169 1.50e-49

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: 157.96  E-value: 1.50e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  14 QVVMMGLDSAGKTTLLYKLKGHQLVETLPTVGFNVEPLKAPgHVSLTLWDVGGQAPLRASWKDYLEGTDILVYVLDSTDE 93
Cdd:cd04151   1 RILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYK-NLKFQVWDLGGQTSIRPYWRCYYSNTDAIIYVVDSTDR 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19923979  94 ARLPESAAELTEVLNDPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERFQDHCWELRGCSALTGEGLPEALQSL 169
Cdd:cd04151  80 DRLGISKSELHAMLEEEELKDAVLLVFANKQDMPGALSEAEVAEKLGLSELKDRTWQIFKTSATKGEGLDEGMDWL 155
ARF smart00177
ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular ...
 10-175 1.58e-49

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: 158.55  E-value: 1.58e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979     10 KAEAQVVMMGLDSAGKTTLLYKLKGHQLVETLPTVGFNVEPLKAPgHVSLTLWDVGGQAPLRASWKDYLEGTDILVYVLD 89
Cdd:smart00177  11 NKEMRILMVGLDAAGKTTILYKLKLGESVTTIPTIGFNVETVTYK-NISFTVWDVGGQDKIRPLWRHYYTNTQGLIFVVD 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979     90 STDEARLPESAAELTEVLNDPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERFQDHCWELRGCSALTGEGLPEALQSL 169
Cdd:smart00177  90 SNDRDRIDEAREELHRMLNEDELRDAVILVFANKQDLPDAMKAAEITEKLGLHSIRDRNWYIQPTCATSGDGLYEGLTWL 169


                   ....*.
gi 19923979    170 WSLLKS 175
Cdd:smart00177 170 SNNLKN 175
PLN00223 PLN00223
ADP-ribosylation factor; Provisional
 10-177 2.96e-47

ADP-ribosylation factor; Provisional


Pssm-ID: 165788  Cd Length: 181  Bit Score: 152.81  E-value: 2.96e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979   10 KAEAQVVMMGLDSAGKTTLLYKLKGHQLVETLPTVGFNVEPLKAPgHVSLTLWDVGGQAPLRASWKDYLEGTDILVYVLD 89
Cdd:PLN00223  15 KKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYK-NISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979   90 STDEARLPESAAELTEVLNDPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERFQDHCWELRGCSALTGEGLPEALQSL 169
Cdd:PLN00223  94 SNDRDRVVEARDELHRMLNEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRQRHWYIQSTCATSGEGLYEGLDWL 173


                 ....*...
gi 19923979  170 WSLLKSRS 177
Cdd:PLN00223 174 SNNIANKA 181
PTZ00133 PTZ00133
ADP-ribosylation factor; Provisional
 10-177 5.70e-47

ADP-ribosylation factor; Provisional


Pssm-ID: 173423  Cd Length: 182  Bit Score: 152.31  E-value: 5.70e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979   10 KAEAQVVMMGLDSAGKTTLLYKLKGHQLVETLPTVGFNVEPLKAPgHVSLTLWDVGGQAPLRASWKDYLEGTDILVYVLD 89
Cdd:PTZ00133  15 KKEVRILMVGLDAAGKTTILYKLKLGEVVTTIPTIGFNVETVEYK-NLKFTMWDVGGQDKLRPLWRHYYQNTNGLIFVVD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979   90 STDEARLPESAAELTEVLNDPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERFQDHCWELRGCSALTGEGLPEALQSL 169
Cdd:PTZ00133  94 SNDRERIGDAREELERMLSEDELRDAVLLVFANKQDLPNAMSTTEVTEKLGLHSVRQRNWYIQGCCATTAQGLYEGLDWL 173


                 ....*...
gi 19923979  170 WSLLKSRS 177
Cdd:PTZ00133 174 SANIKKSM 181
Arf1_5_like cd04150
ADP-ribosylation factor-1 (Arf1) and ADP-ribosylation factor-5 (Arf5); The Arf1-Arf5-like ...
 14-169 1.88e-45

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: 147.55  E-value: 1.88e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  14 QVVMMGLDSAGKTTLLYKLKGHQLVETLPTVGFNVEPLKAPgHVSLTLWDVGGQAPLRASWKDYLEGTDILVYVLDSTDE 93
Cdd:cd04150   2 RILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYK-NISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDR 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19923979  94 ARLPESAAELTEVLNDPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERFQDHCWELRGCSALTGEGLPEALQSL 169
Cdd:cd04150  81 ERIGEAREELQRMLNEDELRDAVLLVFANKQDLPNAMSAAEVTDKLGLHSLRNRNWYIQATCATSGDGLYEGLDWL 156
Sar1 cd00879
Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII ...
 10-169 7.38e-42

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: 139.34  E-value: 7.38e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  10 KAEAQVVMMGLDSAGKTTLLYKLKGHQLVETLPTVGFNVEPLkAPGHVSLTLWDVGGQAPLRASWKDYLEGTDILVYVLD 89
Cdd:cd00879  17 KKEAKIVFLGLDNAGKTTLLHMLKDDRLAQHVPTLHPTSEEL-TIGNVKFTTFDLGGHEQARRVWKDYFPEVDGIVFLVD 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  90 STDEARLPESAAELTEVLNDPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERFQDHCWELRG------------CSAL 157
Cdd:cd00879  96 AADPERFQESKEELDSLLNDEELANVPILILGNKIDKPGAVSEEELREALGLYGTTTGKGGVSLkvsnirpvevfmCSVV 175

                       170
                ....*....|..
gi 19923979 158 TGEGLPEALQSL 169
Cdd:cd00879 176 KRQGYGEGFRWL 187
Arfrp1 cd04160
Arf-related protein 1 (Arfrp1); Arfrp1 (Arf-related protein 1), formerly known as ARP, is a ...
 15-165 5.58e-39

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: 131.31  E-value: 5.58e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  15 VVMMGLDSAGKTTLLYKLK--------GHQLVETLPTVGFNVEPLKAPGhVSLTLWDVGGQAPLRASWKDYLEGTDILVY 86
Cdd:cd04160   2 VLILGLDNAGKTTFLEQTKtkfsknykGLNPSKITPTVGLNIGTIEVGK-ARLMFWDLGGQEELRSLWDKYYAESHGVIY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  87 VLDSTDEARLPESAAELTEVLNDPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERFQDHCWELR--GCSALTGEGLPE 164
Cdd:cd04160  81 VIDSTDRERFNESKSAFEKVINNEALEGVPLLVLANKQDLPDALSVAEIKEVFDDCIALIGRRDCLvqPVSALEGEGVEE 160


                .
gi 19923979 165 A 165
Cdd:cd04160 161 G 161
Arl6 cd04157
Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small ...
 14-169 1.13e-37

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: 127.93  E-value: 1.13e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  14 QVVMMGLDSAGKTTLLYKLK--GHQLVETLPTVGFNVEPLKApGHVSLTLWDVGGQAPLRASWKDYLEGTDILVYVLDST 91
Cdd:cd04157   1 NILVLGLDNSGKTTIINQLKpsNAQSQNIVPTVGFNVESFKK-GNLSFTAFDMSGQGKYRGLWEHYYKNIQGIIFVIDSS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  92 DEARLPESAAELTEVLNDPNMAG--VPFLVLANKQEAPDALPLLKIRNRLSLERFQDHCWELRGCSALTGEGLPEALQSL 169
Cdd:cd04157  80 DRLRMVVAKDELELLLNHPDIKHrrIPILFYANKMDLPDALTAVKITQLLCLENIKDKPWHIFASSALTGEGLDEGVDWL 159
Arl10_like cd04159
Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from ...
 15-169 2.30e-36

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: 124.35  E-value: 2.30e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  15 VVMMGLDSAGKTTLLYKLKGHQLVE-TLPTVGFNVEPLKApGHVSLTLWDVGGQAPLRASWKDYLEGTDILVYVLDSTDE 93
Cdd:cd04159   2 ITLVGLQNSGKTTLVNVIASGQFSEdTIPTVGFNMRKVTK-GNVTIKVWDLGGQPRFRSMWERYCRGVNAIVYVVDAADR 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19923979  94 ARLPESAAELTEVLNDPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERFQDHCWELRGCSALTGEGLPEALQSL 169
Cdd:cd04159  81 EKLEVAKNELHDLLEKPSLEGIPLLVLGNKNDLPGALSVDELIEQMNLKSITDREVSCYSISAKEKTNIDIVLDWL 156
ARD1 cd04158
(ADP-ribosylation factor domain protein 1 (ARD1); ARD1 (ADP-ribosylation factor domain protein ...
 14-169 9.63e-33

(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: 115.51  E-value: 9.63e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  14 QVVMMGLDSAGKTTLLYKLKGHQLVETLPTVGFNVEPLKAPgHVSLTLWDVGGQAPLRASWKDYLEGTDILVYVLDSTDE 93
Cdd:cd04158   1 RVVTLGLDGAGKTTILFKLKQDEFMQPIPTIGFNVETVEYK-NLKFTIWDVGGKHKLRPLWKHYYLNTQAVVFVIDSSHR 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19923979  94 ARLPESAAELTEVLNDPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERF-QDHCWELRGCSALTGEGLPEALQSL 169
Cdd:cd04158  80 DRVSEAHSELAKLLTEKELRDALLLIFANKQDVAGALSVEEMTELLSLHKLcCGRSWYIQGCDARSGMGLYEGLDWL 156
SAR smart00178
Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene ...
 12-169 2.86e-30

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: 109.64  E-value: 2.86e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979     12 EAQVVMMGLDSAGKTTLLYKLKGHQLVETLPTVGFNVEPLkAPGHVSLTLWDVGGQAPLRASWKDYLEGTDILVYVLDST 91
Cdd:smart00178  17 HAKILFLGLDNAGKTTLLHMLKNDRLAQHQPTQHPTSEEL-AIGNIKFTTFDLGGHQQARRLWKDYFPEVNGIVYLVDAY 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979     92 DEARLPESAAELTEVLNDPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERFQDHCWELRG-------CSALTGEGLPE 164
Cdd:smart00178  96 DKERFAESKRELDALLSDEELATVPFLILGNKIDAPYAASEDELRYALGLTNTTTGKGKVGVrpvevfmCSVVRRMGYGE 175


                   ....*
gi 19923979    165 ALQSL 169
Cdd:smart00178 176 GFKWL 180
Arl2l1_Arl13_like cd04161
Arl2-like protein 1 (Arl2l1) and Arl13; Arl2l1 (Arl2-like protein 1) and Arl13 form a ...
 15-161 2.52e-29

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: 106.71  E-value: 2.52e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  15 VVMMGLDSAGKTTLLYKLKGHQLVETLPTVGFnvEPLKAP-GHVSLTLWDVGGQAPLRASWKDYLEGTDILVYVLDSTDE 93
Cdd:cd04161   2 LLTVGLDNAGKTTLVSALQGEIPKKVAPTVGF--TPTKLRlDKYEVCIFDLGGGANFRGIWVNYYAEAHGLVFVVDSSDD 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19923979  94 ARLPESAAELTEVLNDPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERFQD----HCwELRGCSALTGEG 161
Cdd:cd04161  80 DRVQEVKEILRELLQHPRVSGKPILVLANKQDKKNALLGADVIEYLSLEKLVNenksLC-HIEPCSAIEGLG 150
Arl9_Arfrp2_like cd04162
Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first ...
 14-173 3.23e-29

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: 106.38  E-value: 3.23e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  14 QVVMMGLDSAGKTTLLYKLKGHQLVE-TLPTVGFNVEPLKApGHVSLTLWDVGGQAPLRASWKDYLEGTDILVYVLDSTD 92
Cdd:cd04162   1 QILVLGLDGAGKTSLLHSLSSERSLEsVVPTTGFNSVAIPT-QDAIMELLEIGGSQNLRKYWKRYLSGSQGLIFVVDSAD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  93 EARLPESAAELTEVLNDPnmAGVPFLVLANKQEAPDALPLLKIRNRLSLERF-QDHCWELRGCSaLTGEGLPEALQSLWS 171
Cdd:cd04162  80 SERLPLARQELHQLLQHP--PDLPLVVLANKQDLPAARSVQEIHKELELEPIaRGRRWILQGTS-LDDDGSPSRMEAVKD 156


                ..
gi 19923979 172 LL 173
Cdd:cd04162 157 LL 158
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
12-169 4.98e-19

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 80.03  E-value: 4.98e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  12 EAQVVMMGLDSAGKTTLLYKLKGHQ--LVETLPTVGFNVE--PLKAPGH-VSLTLWDVGGQ---APLRASWKDYLEGTDI 83
Cdd:COG1100   3 EKKIVVVGTGGVGKTSLVNRLVGDIfsLEKYLSTNGVTIDkkELKLDGLdVDLVIWDTPGQdefRETRQFYARQLTGASL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  84 LVYVLDSTDEARLpESAAELTEVLNDPNMAgVPFLVLANKQeapDALPLLKIRNRLSLERF--QDHCWELRGCSALTGEG 161
Cdd:COG1100  83 YLFVVDGTREETL-QSLYELLESLRRLGKK-SPIILVLNKI---DLYDEEEIEDEERLKEAlsEDNIVEVVATSAKTGEG 157


                ....*...
gi 19923979 162 LPEALQSL 169
Cdd:COG1100 158 VEELFAAL 165
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 16-169 1.08e-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: 76.34  E-value: 1.08e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  16 VMMGLDSAGKTTLLYKLKGHQLVETL----PTVGFNVEPLKAPGH-VSLTLWDVGGQAPLRASW-----KDYLEGTDILV 85
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVGEVSdvpgTTRDPDVYVKELDKGkVKLVLVDTPGLDEFGGLGreelaRLLLRGADLIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  86 YVLDSTDEARLPEsaaELTEVLNDPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERFQDH-CWElrgCSALTGEGLPE 164
Cdd:cd00882  81 LVVDSTDRESEED---AKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELAKILGVpVFE---VSAKTGEGVDE 154


                ....*
gi 19923979 165 ALQSL 169
Cdd:cd00882 155 LFEKL 159
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 12-129 1.18e-14

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: 68.17  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979    12 EAQVVMMGLDSAGKTTLLYKLKGHQL--VETLPTVGFNVEPLKA---PGHVSLTLWDVGGQAPLRASWKDYLEGTDILVY 86
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGsiTEYYPGTTRNYVTTVIeedGKTYKFNLLDTAGQEDYDAIRRLYYPQVERSLR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 19923979    87 VLD------STDEARLPEsaaelTEVLNDPNMAGVPFLVLANKQEAPDA 129
Cdd:TIGR00231  81 VFDivilvlDVEEILEKQ-----TKEIIHHADSGVPIILVGNKIDLKDA 124
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
 15-142 4.43e-14

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: 67.35  E-value: 4.43e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  15 VVMMGLDSAGKTTLLYKLKGHQLVETLPTVGFNVEPLKAPGH--VSLTLWDVGGQAPLRASWKDYLEGTDI-LVYVLDST 91
Cdd:cd04105   3 VLLLGPSDSGKTALFTKLTTGKVRSTVTSIEPNVASFYSNSSkgKKLTLVDVPGHEKLRDKLLEYLKASLKaIVFVVDSA 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 19923979  92 DEARLPESAAE-LTEVLND----PNmaGVPFLVLANKQEAPDALPLLKIRNRLSLE 142
Cdd:cd04105  83 TFQKNIRDVAEfLYDILTDlekiKN--KIPILIACNKQDLFTAKPAKKIKELLEKE 136
SRPRB pfam09439
Signal recognition particle receptor beta subunit; The beta subunit of the signal recognition ...
 15-142 1.77e-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: 54.76  E-value: 1.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979    15 VVMMGLDSAGKTTLLYKLkghQLVETLPTVgFNVEPLKAPGHV-----SLTLWDVGGQAPLRASWKDYLEGTDI---LVY 86
Cdd:pfam09439   6 VIIAGLCDSGKTSLFTLL---TTDSVRPTV-TSQEPSAAYRYMlnkgnSFTLIDFPGHVKLRYKLLETLKDSSSlkgIVF 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 19923979    87 VLDST-DEARLPESAAELTEVLNDPNMA--GVPFLVLANKQEAPDALPLLKIRNRLSLE 142
Cdd:pfam09439  82 VVDSTiFPKEVTDTAEFLYDILSITELLknGIDILIACNKQESFTARPPKKIKQALEKE 140
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
 15-123 7.19e-08

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: 48.66  E-value: 7.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979    15 VVMMGLDSAGKTTLLYKLKGHQLVE-TLPTVGFNVEPLKAP------GHVSLTLWDVGGQAPLRASWKDYLEGTDILVYV 87
Cdd:pfam08477   2 VVLLGDSGVGKTSLLKRFVDDTFDPkYKSTIGVDFKTKTVLenddngKKIKLNIWDTAGQERFRSLHPFYYRGAAAALLV 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 19923979    88 LDSTDEARLPESAAELTEVLNDpnmagVPFLVLANK 123
Cdd:pfam08477  82 YDSRTFSNLKYWLRELKKYAGN-----SPVILVGNK 112
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 19-173 7.39e-08

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: 49.94  E-value: 7.39e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  19 GLDSAGKTTLLYKLKGHQLVETLPT-------VGFNVEPLKA--------PGhvsltLWDVGGQAPLR-ASWKDYLEGTD 82
Cdd:cd00880   4 GRPNVGKSSLLNALLGQNVGIVSPIpgttrdpVRKEWELLPLgpvvlidtPG-----LDEEGGLGRERvEEARQVADRAD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  83 ILVYVLDSTdeaRLPEsaaELTEVLNDPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERFQDHcwELRGCSALTGEGL 162
Cdd:cd00880  79 LVLLVVDSD---LTPV---EEEAKLGLLRERGKPVLLVLNKIDLVPESEEEELLRERKLELLPDL--PVIAVSALPGEGI 150

                       170
                ....*....|.
gi 19923979 163 PEALQSLWSLL 173
Cdd:cd00880 151 DELRKKIAELL 161
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 78-173 1.66e-07

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


Pssm-ID: 206685 [Multi-domain]  Cd Length: 170  Bit Score: 48.96  E-value: 1.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  78 LEGTDILVYVLDSTDEARLPESAAELTEVLN--DPNMAGVPFLVLANKQEAPDALPLLKIrnrlsLERFQDHCWELR--G 153
Cdd:cd01898  76 IERTRVLLHVIDLSGEDDPVEDYETIRNELEayNPGLAEKPRIVVLNKIDLLDAEERFEK-----LKELLKELKGKKvfP 150

                        90       100
                ....*....|....*....|
gi 19923979 154 CSALTGEGLPEALQSLWSLL 173
Cdd:cd01898 151 ISALTGEGLDELLKKLAKLL 170
obgE PRK12299
GTPase CgtA; Reviewed
 78-175 2.48e-07

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 49.68  E-value: 2.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979   78 LEGTDILVYVLDSTDEArlPESAAELteVLN-----DPNMAGVPFLVLANKQEAPDALPLLKIRNRLSLERFQDHCWELr 152
Cdd:PRK12299 234 IERTRLLLHLVDIEAVD--PVEDYKT--IRNelekySPELADKPRILVLNKIDLLDEEEEREKRAALELAALGGPVFLI- 308

                         90       100
                 ....*....|....*....|...
gi 19923979  153 gcSALTGEGLPEALQSLWSLLKS 175
Cdd:PRK12299 309 --SAVTGEGLDELLRALWELLEE 329
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
 15-169 7.49e-06

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: 43.98  E-value: 7.49e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  15 VVMMGlDSA-GKTTLLYKL-KGHQLVETLPTVG--FNVEPLKAPGH-VSLTLWDVGGQ---APLRASwkdYLEGTD--IL 84
Cdd:cd00154   3 IVLIG-DSGvGKTSLLLRFvDNKFSENYKSTIGvdFKSKTIEVDGKkVKLQIWDTAGQerfRSITSS---YYRGAHgaIL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  85 VYvlDSTDEarlpESAAELTEVLNDPNMAG---VPFLVLANKQEapdalplLKIRNRLSLERFQ----DHCWELRGCSAL 157
Cdd:cd00154  79 VY--DVTNR----ESFENLDKWLNELKEYAppnIPIILVGNKSD-------LEDERQVSTEEAQqfakENGLLFFETSAK 145

                       170
                ....*....|..
gi 19923979 158 TGEGLPEALQSL 169
Cdd:cd00154 146 TGENVDEAFESL 157
RocCOR cd09914
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ...
 12-164 1.90e-05

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: 43.09  E-value: 1.90e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  12 EAQVVMMGLDSAGKTTLLYKLKGHQLVE-TLPTVGFNVEPLKAPGH----VSLTLWDVGGQAPLRASWKDYLEGTDILVY 86
Cdd:cd09914   1 EAKLMLVGQGGVGKTSLCKQLIGEKFDGdESSTHGINVQDWKIPAPerkkIRLNVWDFGGQEIYHATHQFFLTSRSLYLL 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19923979  87 VLDSTDEARlpESAAELTeVLNDPNMAGV-PFLVLANKQeapDALPLLKIRNRLSLERFQDHCWELRGCSALTGEGLPE 164
Cdd:cd09914  81 VFDLRTGDE--VSRVPYW-LRQIKAFGGVsPVILVGTHI---DESCDEDILKKALNKKFPAIINDIHFVSCKNGKGIAE 153
PLN03118 PLN03118
Rab family protein; Provisional
 1-91 2.31e-05

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 43.51  E-value: 2.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979    1 MGSVN--SRGHKAEAQVVMMGLDSAGKTTLLYKLKGHQLVETLPTVG--FNVEPLKAPG-HVSLTLWDVGGQAPLRASWK 75
Cdd:PLN03118   1 MGSSSgqSSGYDLSFKILLIGDSGVGKSSLLVSFISSSVEDLAPTIGvdFKIKQLTVGGkRLKLTIWDTAGQERFRTLTS 80

                         90
                 ....*....|....*.
gi 19923979   76 DYLEGTDILVYVLDST 91
Cdd:PLN03118  81 SYYRNAQGIILVYDVT 96
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 23-169 4.79e-05

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


Pssm-ID: 206666 [Multi-domain]  Cd Length: 204  Bit Score: 42.45  E-value: 4.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  23 AGKTTLLYKLKG-HQLVE-----TL-PTVgfnvEPLKAPGHVSLTLWD-VG--GQAP--LRASWKDYLEGT---DILVYV 87
Cdd:cd01878  52 AGKSTLFNALTGaDVLAEdqlfaTLdPTT----RRIKLPGGREVLLTDtVGfiRDLPhqLVEAFRSTLEEVaeaDLLLHV 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  88 LDSTDEARLPESAAELtEVLNDPNMAGVPFLVLANKQeapDALPLLKIRNRLSLERFQDHCwelrgCSALTGEGLPEALQ 167
Cdd:cd01878 128 VDASDPDREEQIETVE-EVLKELGADDIPIILVLNKI---DLLDDEELEERLRAGRPDAVF-----ISAKTGEGLDLLKE 198


                ..
gi 19923979 168 SL 169
Cdd:cd01878 199 AI 200
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 14-123 2.67e-04

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: 39.14  E-value: 2.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979    14 QVVMMGLDSAGKTTLLYKLKG-HQLVETLP--TVGFNVEPLKAPGHvSLTLWDVGG-------QAPLRASWKDYLEgTDI 83
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGaKAIVSDYPgtTRDPNEGRLELKGK-QIILVDTPGliegaseGEGLGRAFLAIIE-ADL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 19923979    84 LVYVLDSTDEARlpesaAELTEVLNDPNMAGVPFLVLANK 123
Cdd:pfam01926  79 ILFVVDSEEGIT-----PLDEELLELLRENKKPIILVLNK 113
G-alpha pfam00503
G-protein alpha subunit; G proteins couple receptors of extracellular signals to intracellular ...
 41-123 5.44e-04

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: 39.88  E-value: 5.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979    41 LPTVG-----FNVEPLKapghvsLTLWDVGGQAPLRASWKDYLEGTDILVYV--LDSTDEA--------RLPESAAELTE 105
Cdd:pfam00503 152 VKTTGiietkFEFKGLK------FRLFDVGGQRSERKKWIHCFEDVTAIIFVvsLSEYDQVlyeddstnRMEESLKLFEE 225

                          90
                  ....*....|....*...
gi 19923979   106 VLNDPNMAGVPFLVLANK 123
Cdd:pfam00503 226 ICNSPWFKNTPIILFLNK 243
Rab4 cd04113
Rab GTPase family 4 (Rab4); Rab4 subfamily. Rab4 has been implicated in numerous functions ...
 16-165 6.42e-04

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: 38.57  E-value: 6.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  16 VMMGLDSAGKTTLLYKLKGHQLVETLP-TVG--FNVEPLKAPG-HVSLTLWDVGGQAPLRASWKDYLEGT--DILVYvlD 89
Cdd:cd04113   4 LIIGSAGTGKSCLLHQFIENKFKQDSNhTIGveFGSRVVNVGGkSVKLQIWDTAGQERFRSVTRSYYRGAagALLVY--D 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  90 STDEarlpESAAELTEVLNDPNMAGVPFLVL---ANKQEAPDAlpllkiRNRLSLE--RF-QDHCWELRGCSALTGEGLP 163
Cdd:cd04113  82 ITSR----ESFNALTNWLTDARTLASPDIVIilvGNKKDLEDD------REVTFLEasRFaQENGLLFLETSALTGENVE 151


                ..
gi 19923979 164 EA 165
Cdd:cd04113 152 EA 153
Rab9 cd04116
Rab GTPase family 9 (Rab9); Rab9 is found in late endosomes, together with mannose 6-phosphate ...
 14-128 9.89e-04

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: 38.32  E-value: 9.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  14 QVVMMGLDSAGKTTLLYKLKGHQLVETL-PTVG--FNVEPLKAPGH-VSLTLWDVGGQAPLRASWKDYLEGTDI--LVYV 87
Cdd:cd04116   7 KVILLGDGGVGKSSLMNRYVTNKFDTQLfHTIGveFLNKDLEVDGHfVTLQIWDTAGQERFRSLRTPFYRGSDCclLTFS 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 19923979  88 LDSTDEAR-LPESAAELTEVLNDPNMAGVPFLVLANKQEAPD 128
Cdd:cd04116  87 VDDSQSFQnLSNWKKEFIYYADVKEPESFPFVILGNKIDIPE 128
Rab28 cd04109
Rab GTPase family 28 (Rab28); Rab28 subfamily. First identified in maize, Rab28 has been shown ...
 14-127 2.17e-03

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: 37.47  E-value: 2.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19923979  14 QVVMMGLDSAGKTTLLYKLK----GHQLVETLpTVGFNVEPLKAPGH--VSLTLWDVGGQAPLRASWKDYLEGTDILVYV 87
Cdd:cd04109   2 KIVVLGDGASGKTSLIRRFAqegfGKSYKQTI-GLDFFSRRITLPGSlnVTLQVWDIGGQQIGGKMLDKYIYGAQAVCLV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 19923979  88 LDSTDEARLPESAAELTEVLNDPNMAGV-PFLVL-ANKQEAP 127
Cdd:cd04109  81 YDITNSQSFENLEDWLSVVKKVNEESETkPKMVLvGNKTDLE 122
 
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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