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Conserved domains on  [gi|1720359971|ref|XP_030100660|]
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ADP-ribosylation factor-like protein 1 isoform X1 [Mus musculus]

Protein Classification

ADP-ribosylation factor family protein( domain architecture ID 10134960)

ADP-ribosylation factor (Arf) family protein such as Homo sapiens ADP-ribosylation factor-like protein 1 (Arl1), which is a GTP-binding protein that recruits several effectors, such as golgins, arfaptins, and Arf-GEFs to the trans-Golgi network, and modulates their functions at the Golgi complex

CATH:  3.40.50.300
Gene Ontology:  GO:0005525|GO:0016192
SCOP:  4004043

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Arl1 cd04151
ADP ribosylation factor 1 (Arf1); Arl1 subfamily. Arl1 (Arf-like 1) localizes to the Golgi ...
19-176 2.18e-119

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: 333.99  E-value: 2.18e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSCDRD 98
Cdd:cd04151     1 RILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAIIYVVDSTDRD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720359971  99 RIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALGLPALKDRKWQIFKTSATKGTGLDEAMEWLVET 176
Cdd:cd04151    81 RLGISKSELHAMLEEEELKDAVLLVFANKQDMPGALSEAEVAEKLGLSELKDRTWQIFKTSATKGEGLDEGMDWLVNT 158
 
Name Accession Description Interval E-value
Arl1 cd04151
ADP ribosylation factor 1 (Arf1); Arl1 subfamily. Arl1 (Arf-like 1) localizes to the Golgi ...
19-176 2.18e-119

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: 333.99  E-value: 2.18e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSCDRD 98
Cdd:cd04151     1 RILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAIIYVVDSTDRD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720359971  99 RIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALGLPALKDRKWQIFKTSATKGTGLDEAMEWLVET 176
Cdd:cd04151    81 RLGISKSELHAMLEEEELKDAVLLVFANKQDMPGALSEAEVAEKLGLSELKDRTWQIFKTSATKGEGLDEGMDWLVNT 158
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
18-177 1.48e-103

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


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 294.13  E-value: 1.48e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  18 MRILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSCDR 97
Cdd:pfam00025   1 MRILILGLDNAGKTTILYKLKLGEIVTTIPTIGFNVETVTYKNVKFTVWDVGGQESLRPLWRNYFPNTDAVIFVVDSADR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  98 DRIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALGLPALKDRKWQIFKTSATKGTGLDEAMEWLVETL 177
Cdd:pfam00025  81 DRIEEAKEELHALLNEEELADAPLLILANKQDLPGAMSEAEIRELLGLHELKDRPWEIQGCSAVTGEGLDEGLDWLSNYI 160
ARF smart00177
ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular ...
16-179 6.53e-83

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: 242.52  E-value: 6.53e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971   16 REMRILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSC 95
Cdd:smart00177  12 KEMRILMVGLDAAGKTTILYKLKLGESVTTIPTIGFNVETVTYKNISFTVWDVGGQDKIRPLWRHYYTNTQGLIFVVDSN 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971   96 DRDRIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALGLPALKDRKWQIFKTSATKGTGLDEAMEWLVE 175
Cdd:smart00177  92 DRDRIDEAREELHRMLNEDELRDAVILVFANKQDLPDAMKAAEITEKLGLHSIRDRNWYIQPTCATSGDGLYEGLTWLSN 171

                   ....
gi 1720359971  176 TLKS 179
Cdd:smart00177 172 NLKN 175
PTZ00133 PTZ00133
ADP-ribosylation factor; Provisional
16-180 1.59e-80

ADP-ribosylation factor; Provisional


Pssm-ID: 173423  Cd Length: 182  Bit Score: 236.67  E-value: 1.59e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  16 REMRILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSC 95
Cdd:PTZ00133   16 KEVRILMVGLDAAGKTTILYKLKLGEVVTTIPTIGFNVETVEYKNLKFTMWDVGGQDKLRPLWRHYYQNTNGLIFVVDSN 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  96 DRDRIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALGLPALKDRKWQIFKTSATKGTGLDEAMEWLVE 175
Cdd:PTZ00133   96 DRERIGDAREELERMLSEDELRDAVLLVFANKQDLPNAMSTTEVTEKLGLHSVRQRNWYIQGCCATTAQGLYEGLDWLSA 175

                  ....*
gi 1720359971 176 TLKSR 180
Cdd:PTZ00133  176 NIKKS 180
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
16-177 9.28e-18

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 76.17  E-value: 9.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  16 REMRILILGLDGAGKTTILYRLqVGEVVTT---IPTIGFNVE----TVTYKNLKFQVWDLGGQT---SIRPYWRCYYSNT 85
Cdd:COG1100     2 GEKKIVVVGTGGVGKTSLVNRL-VGDIFSLekyLSTNGVTIDkkelKLDGLDVDLVIWDTPGQDefrETRQFYARQLTGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  86 DAVIYVVDScDRDRIGISKSELVAMLEEEELRKAILVVFaNKQDM---EQAMTPSEMANALGlpalKDRKWQIFKTSATK 162
Cdd:COG1100    81 SLYLFVVDG-TREETLQSLYELLESLRRLGKKSPIILVL-NKIDLydeEEIEDEERLKEALS----EDNIVEVVATSAKT 154
                         170
                  ....*....|....*
gi 1720359971 163 GTGLDEAMEWLVETL 177
Cdd:COG1100   155 GEGVEELFAALAEIL 169
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
17-169 1.99e-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: 67.01  E-value: 1.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  17 EMRILILGLDGAGKTTILYRL--QVGEVVTTIPTIGFNVET--VTYKNL--KFQVWDLGGQTSIRPYWRCYYSNTDAVIY 90
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLlgNKGSITEYYPGTTRNYVTtvIEEDGKtyKFNLLDTAGQEDYDAIRRLYYPQVERSLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  91 VVDScdrDRIGISKSELVaMLEEEELR-----KAILVVFANKQDMEQAMTPSEManALGLPALKdrKWQIFKTSATKGTG 165
Cdd:TIGR00231  81 VFDI---VILVLDVEEIL-EKQTKEIIhhadsGVPIILVGNKIDLKDADLKTHV--ASEFAKLN--GEPIIPLSAETGKN 152

                  ....
gi 1720359971 166 LDEA 169
Cdd:TIGR00231 153 IDSA 156
 
Name Accession Description Interval E-value
Arl1 cd04151
ADP ribosylation factor 1 (Arf1); Arl1 subfamily. Arl1 (Arf-like 1) localizes to the Golgi ...
19-176 2.18e-119

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: 333.99  E-value: 2.18e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSCDRD 98
Cdd:cd04151     1 RILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAIIYVVDSTDRD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720359971  99 RIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALGLPALKDRKWQIFKTSATKGTGLDEAMEWLVET 176
Cdd:cd04151    81 RLGISKSELHAMLEEEELKDAVLLVFANKQDMPGALSEAEVAEKLGLSELKDRTWQIFKTSATKGEGLDEGMDWLVNT 158
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
18-177 1.48e-103

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


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 294.13  E-value: 1.48e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  18 MRILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSCDR 97
Cdd:pfam00025   1 MRILILGLDNAGKTTILYKLKLGEIVTTIPTIGFNVETVTYKNVKFTVWDVGGQESLRPLWRNYFPNTDAVIFVVDSADR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  98 DRIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALGLPALKDRKWQIFKTSATKGTGLDEAMEWLVETL 177
Cdd:pfam00025  81 DRIEEAKEELHALLNEEELADAPLLILANKQDLPGAMSEAEIRELLGLHELKDRPWEIQGCSAVTGEGLDEGLDWLSNYI 160
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
19-175 2.89e-95

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: 273.30  E-value: 2.89e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSCDRD 98
Cdd:cd00878     1 RILMLGLDGAGKTTILYKLKLGEVVTTIPTIGFNVETVEYKNVKFTVWDVGGQDKIRPLWKHYYENTDGLIFVVDSSDRE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720359971  99 RIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALGLPALKDRKWQIFKTSATKGTGLDEAMEWLVE 175
Cdd:cd00878    81 RIEEAKNELHKLLNEEELKGAPLLILANKQDLPGALTESELIELLGLESIKGRRWHIQPCSAVTGDGLDEGLDWLIE 157
Arl5_Arl8 cd04153
Arf-like 5 (Arl5) and 8 (Arl8) GTPases; Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like ...
16-176 5.41e-84

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: 245.34  E-value: 5.41e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  16 REMRILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSC 95
Cdd:cd04153    14 KEYKVIIVGLDNAGKTTILYQFLLGEVVHTSPTIGSNVEEIVYKNIRFLMWDIGGQESLRSSWNTYYTNTDAVILVIDST 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  96 DRDRIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALGLPALKDRKWQIFKTSATKGTGLDEAMEWLVE 175
Cdd:cd04153    94 DRERLPLTKEELYKMLAHEDLRKAVLLVLANKQDLKGAMTPAEISESLGLTSIRDHTWHIQGCCALTGEGLPEGLDWIAS 173

                  .
gi 1720359971 176 T 176
Cdd:cd04153   174 R 174
ARF smart00177
ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular ...
16-179 6.53e-83

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: 242.52  E-value: 6.53e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971   16 REMRILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSC 95
Cdd:smart00177  12 KEMRILMVGLDAAGKTTILYKLKLGESVTTIPTIGFNVETVTYKNISFTVWDVGGQDKIRPLWRHYYTNTQGLIFVVDSN 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971   96 DRDRIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALGLPALKDRKWQIFKTSATKGTGLDEAMEWLVE 175
Cdd:smart00177  92 DRDRIDEAREELHRMLNEDELRDAVILVFANKQDLPDAMKAAEITEKLGLHSIRDRNWYIQPTCATSGDGLYEGLTWLSN 171

                   ....
gi 1720359971  176 TLKS 179
Cdd:smart00177 172 NLKN 175
Arf1_5_like cd04150
ADP-ribosylation factor-1 (Arf1) and ADP-ribosylation factor-5 (Arf5); The Arf1-Arf5-like ...
18-173 3.02e-81

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: 237.69  E-value: 3.02e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  18 MRILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSCDR 97
Cdd:cd04150     1 MRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDR 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720359971  98 DRIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALGLPALKDRKWQIFKTSATKGTGLDEAMEWL 173
Cdd:cd04150    81 ERIGEAREELQRMLNEDELRDAVLLVFANKQDLPNAMSAAEVTDKLGLHSLRNRNWYIQATCATSGDGLYEGLDWL 156
PTZ00133 PTZ00133
ADP-ribosylation factor; Provisional
16-180 1.59e-80

ADP-ribosylation factor; Provisional


Pssm-ID: 173423  Cd Length: 182  Bit Score: 236.67  E-value: 1.59e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  16 REMRILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSC 95
Cdd:PTZ00133   16 KEVRILMVGLDAAGKTTILYKLKLGEVVTTIPTIGFNVETVEYKNLKFTMWDVGGQDKLRPLWRHYYQNTNGLIFVVDSN 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  96 DRDRIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALGLPALKDRKWQIFKTSATKGTGLDEAMEWLVE 175
Cdd:PTZ00133   96 DRERIGDAREELERMLSEDELRDAVLLVFANKQDLPNAMSTTEVTEKLGLHSVRQRNWYIQGCCATTAQGLYEGLDWLSA 175

                  ....*
gi 1720359971 176 TLKSR 180
Cdd:PTZ00133  176 NIKKS 180
PLN00223 PLN00223
ADP-ribosylation factor; Provisional
16-180 9.64e-80

ADP-ribosylation factor; Provisional


Pssm-ID: 165788  Cd Length: 181  Bit Score: 234.86  E-value: 9.64e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  16 REMRILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSC 95
Cdd:PLN00223   16 KEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSN 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  96 DRDRIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALGLPALKDRKWQIFKTSATKGTGLDEAMEWLVE 175
Cdd:PLN00223   96 DRDRVVEARDELHRMLNEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRQRHWYIQSTCATSGEGLYEGLDWLSN 175

                  ....*
gi 1720359971 176 TLKSR 180
Cdd:PLN00223  176 NIANK 180
Arf6 cd04149
ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins ...
15-173 2.30e-75

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: 223.11  E-value: 2.30e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  15 TREMRILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDS 94
Cdd:cd04149     7 NKEMRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVETVTYKNVKFNVWDVGGQDKIRPLWRHYYTGTQGLIFVVDS 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720359971  95 CDRDRIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALGLPALKDRKWQIFKTSATKGTGLDEAMEWL 173
Cdd:cd04149    87 ADRDRIDEARQELHRIINDREMRDALLLVFANKQDLPDAMKPHEIQEKLGLTRIRDRNWYVQPSCATSGDGLYEGLTWL 165
Arl3 cd04155
Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most ...
16-176 4.46e-70

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: 209.95  E-value: 4.46e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  16 REMRILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSC 95
Cdd:cd04155    14 QEVRILLLGLDNAGKTTILKQLASEDISHITPTQGFNIKNVQADGFKLNVWDIGGQRKIRPYWRNYFENTDVLIYVIDSA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  96 DRDRIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALGLPALKDRKWQIFKTSATKGTGLDEAMEWLVE 175
Cdd:cd04155    94 DRKRFEEAGQELVELLEEEKLAGVPVLVFANKQDLLTAAPAEEVAEALNLHDIRDRSWHIQACSAKTGEGLQEGMNWVCK 173

                  .
gi 1720359971 176 T 176
Cdd:cd04155   174 N 174
Arl2 cd04154
Arf-like 2 (Arl2) GTPase; Arl2 (Arf-like 2) GTPases are members of the Arf family that bind ...
16-174 4.38e-68

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: 204.87  E-value: 4.38e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  16 REMRILILGLDGAGKTTILYRLQvGEVVTTI-PTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDS 94
Cdd:cd04154    13 REMRILMLGLDNAGKTTILKKFN-GEDISTIsPTLGFNIKTLEYNGYKLNIWDVGGQKSLRSYWRNYFESTDALIWVVDS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  95 CDRDRIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALGLPALKDRKWQIFKTSATKGTGLDEAMEWLV 174
Cdd:cd04154    92 SDRARLEDCKRELQKLLVEERLAGATLLIFANKQDLPGALSPEEIREVLELDSIKSHHWRIFGCSAVTGENLLDGIDWLV 171
Arl6 cd04157
Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small ...
20-176 6.49e-55

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: 171.07  E-value: 6.49e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  20 ILILGLDGAGKTTILYRLQVGEVVTTI--PTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSCDR 97
Cdd:cd04157     2 ILVLGLDNSGKTTIINQLKPSNAQSQNivPTVGFNVESFKKGNLSFTAFDMSGQGKYRGLWEHYYKNIQGIIFVIDSSDR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  98 DRIGISKSELVAMLEEEEL--RKAILVVFANKQDMEQAMTPSEMANALGLPALKDRKWQIFKTSATKGTGLDEAMEWLVE 175
Cdd:cd04157    82 LRMVVAKDELELLLNHPDIkhRRIPILFYANKMDLPDALTAVKITQLLCLENIKDKPWHIFASSALTGEGLDEGVDWLQA 161

                  .
gi 1720359971 176 T 176
Cdd:cd04157   162 Q 162
ARD1 cd04158
(ADP-ribosylation factor domain protein 1 (ARD1); ARD1 (ADP-ribosylation factor domain protein ...
19-177 5.49e-54

(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: 169.05  E-value: 5.49e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSCDRD 98
Cdd:cd04158     1 RVVTLGLDGAGKTTILFKLKQDEFMQPIPTIGFNVETVEYKNLKFTIWDVGGKHKLRPLWKHYYLNTQAVVFVIDSSHRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  99 RIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALGLPAL-KDRKWQIFKTSATKGTGLDEAMEWLVETL 177
Cdd:cd04158    81 RVSEAHSELAKLLTEKELRDALLLIFANKQDVAGALSVEEMTELLSLHKLcCGRSWYIQGCDARSGMGLYEGLDWLSRQL 160
ARLTS1 cd04156
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ...
19-170 5.90e-53

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: 166.05  E-value: 5.90e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETV-TYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSCDR 97
Cdd:cd04156     1 QVLLLGLDSAGKSTLLYKLKHAELVTTIPTVGFNVEMLqLEKHLSLTVWDVGGQEKMRTVWKCYLENTDGLVYVVDSSDE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720359971  98 DRIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALGLPAL-KDRKWQIFKTSATKGTGLDEAM 170
Cdd:cd04156    81 ARLDESQKELKHILKNEHIKGVPVVLLANKQDLPGALTAEEITRRFKLKKYcSDRDWYVQPCSAVTGEGLAEAF 154
Sar1 cd00879
Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII ...
16-173 4.81e-49

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: 157.05  E-value: 4.81e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  16 REMRILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSC 95
Cdd:cd00879    18 KEAKIVFLGLDNAGKTTLLHMLKDDRLAQHVPTLHPTSEELTIGNVKFTTFDLGGHEQARRVWKDYFPEVDGIVFLVDAA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  96 DRDRIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALGLPAL------------KDRKWQIFKTSATKG 163
Cdd:cd00879    98 DPERFQESKEELDSLLNDEELANVPILILGNKIDKPGAVSEEELREALGLYGTttgkggvslkvsNIRPVEVFMCSVVKR 177
                         170
                  ....*....|
gi 1720359971 164 TGLDEAMEWL 173
Cdd:cd00879   178 QGYGEGFRWL 187
Arl4_Arl7 cd04152
Arf-like 4 (Arl4) and 7 (Arl7) GTPases; Arl4 (Arf-like 4) is highly expressed in testicular ...
18-181 5.53e-44

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: 144.17  E-value: 5.53e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  18 MRILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETV-----TYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVV 92
Cdd:cd04152     4 LHIVMLGLDSAGKTTVLYRLKFNEFVNTVPTKGFNTEKIkvslgNAKGVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  93 DSCDRDRIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALGLPALKD-RKWQIFKTSATKGTGLDEAME 171
Cdd:cd04152    84 DSVDVERMEEAKTELHKITKFSENQGVPVLVLANKQDLPNALPVSEVEKLLALHELSSsTPWHVQPACAIIGEGLQEGLE 163
                         170
                  ....*....|
gi 1720359971 172 WLVETLKSRQ 181
Cdd:cd04152   164 KLYEMILKRR 173
Arfrp1 cd04160
Arf-related protein 1 (Arfrp1); Arfrp1 (Arf-related protein 1), formerly known as ARP, is a ...
20-175 8.92e-43

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: 140.56  E-value: 8.92e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  20 ILILGLDGAGKTTILYRLQVGEVVTT--------IPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYV 91
Cdd:cd04160     2 VLILGLDNAGKTTFLEQTKTKFSKNYkglnpskiTPTVGLNIGTIEVGKARLMFWDLGGQEELRSLWDKYYAESHGVIYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  92 VDSCDRDRIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALG--LPALKDRKWQIFKTSATKGTGLDEA 169
Cdd:cd04160    82 IDSTDRERFNESKSAFEKVINNEALEGVPLLVLANKQDLPDALSVAEIKEVFDdcIALIGRRDCLVQPVSALEGEGVEEG 161

                  ....*.
gi 1720359971 170 MEWLVE 175
Cdd:cd04160   162 IEWLVD 167
Arl10_like cd04159
Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from ...
20-175 1.78e-40

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: 134.37  E-value: 1.78e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  20 ILILGLDGAGKTTILYRLQVGE-VVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSCDRD 98
Cdd:cd04159     2 ITLVGLQNSGKTTLVNVIASGQfSEDTIPTVGFNMRKVTKGNVTIKVWDLGGQPRFRSMWERYCRGVNAIVYVVDAADRE 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720359971  99 RIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALGLPALKDRKWQIFKTSATKGTGLDEAMEWLVE 175
Cdd:cd04159    82 KLEVAKNELHDLLEKPSLEGIPLLVLGNKNDLPGALSVDELIEQMNLKSITDREVSCYSISAKEKTNIDIVLDWLIK 158
Arl9_Arfrp2_like cd04162
Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first ...
20-162 2.29e-37

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: 126.41  E-value: 2.29e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  20 ILILGLDGAGKTTILYRLqVGEVV--TTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSCDR 97
Cdd:cd04162     2 ILVLGLDGAGKTSLLHSL-SSERSleSVVPTTGFNSVAIPTQDAIMELLEIGGSQNLRKYWKRYLSGSQGLIFVVDSADS 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720359971  98 DRIGISKSELVAMLEEEELRKaiLVVFANKQDMEQAMTPSEMANALGLPAL-KDRKWQIFKTSATK 162
Cdd:cd04162    81 ERLPLARQELHQLLQHPPDLP--LVVLANKQDLPAARSVQEIHKELELEPIaRGRRWILQGTSLDD 144
SAR smart00178
Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene ...
16-175 4.00e-33

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: 116.19  E-value: 4.00e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971   16 REMRILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSC 95
Cdd:smart00178  16 KHAKILFLGLDNAGKTTLLHMLKNDRLAQHQPTQHPTSEELAIGNIKFTTFDLGGHQQARRLWKDYFPEVNGIVYLVDAY 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971   96 DRDRIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALGL-------PALKDRKWQIFKTSATKGTGLDE 168
Cdd:smart00178  96 DKERFAESKRELDALLSDEELATVPFLILGNKIDAPYAASEDELRYALGLtntttgkGKVGVRPVEVFMCSVVRRMGYGE 175

                   ....*..
gi 1720359971  169 AMEWLVE 175
Cdd:smart00178 176 GFKWLSQ 182
Arl2l1_Arl13_like cd04161
Arl2-like protein 1 (Arl2l1) and Arl13; Arl2l1 (Arl2-like protein 1) and Arl13 form a ...
20-175 2.64e-23

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: 90.53  E-value: 2.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  20 ILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSCDRDR 99
Cdd:cd04161     2 LLTVGLDNAGKTTLVSALQGEIPKKVAPTVGFTPTKLRLDKYEVCIFDLGGGANFRGIWVNYYAEAHGLVFVVDSSDDDR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971 100 IGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALGLPALKDRK---WQIFKTSATKGTG------LDEAM 170
Cdd:cd04161    82 VQEVKEILRELLQHPRVSGKPILVLANKQDKKNALLGADVIEYLSLEKLVNENkslCHIEPCSAIEGLGkkidpsIVEGL 161

                  ....*
gi 1720359971 171 EWLVE 175
Cdd:cd04161   162 RWLLA 166
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
21-175 5.26e-21

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: 84.43  E-value: 5.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  21 LILGLDGAGKTTILYRL---QVGEV-VTTIPTIGFNVETVTY--KNLKFQVWDLGGQTSIRPYWRC-----YYSNTDAVI 89
Cdd:cd00882     1 VVVGRGGVGKSSLLNALlggEVGEVsDVPGTTRDPDVYVKELdkGKVKLVLVDTPGLDEFGGLGREelarlLLRGADLIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  90 YVVDSCDRDRIgisKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALGLpaLKDRKWQIFKTSATKGTGLDEA 169
Cdd:cd00882    81 LVVDSTDRESE---EDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEEL--AKILGVPVFEVSAKTGEGVDEL 155

                  ....*.
gi 1720359971 170 MEWLVE 175
Cdd:cd00882   156 FEKLIE 161
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
16-177 9.28e-18

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 76.17  E-value: 9.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  16 REMRILILGLDGAGKTTILYRLqVGEVVTT---IPTIGFNVE----TVTYKNLKFQVWDLGGQT---SIRPYWRCYYSNT 85
Cdd:COG1100     2 GEKKIVVVGTGGVGKTSLVNRL-VGDIFSLekyLSTNGVTIDkkelKLDGLDVDLVIWDTPGQDefrETRQFYARQLTGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  86 DAVIYVVDScDRDRIGISKSELVAMLEEEELRKAILVVFaNKQDM---EQAMTPSEMANALGlpalKDRKWQIFKTSATK 162
Cdd:COG1100    81 SLYLFVVDG-TREETLQSLYELLESLRRLGKKSPIILVL-NKIDLydeEEIEDEERLKEALS----EDNIVEVVATSAKT 154
                         170
                  ....*....|....*
gi 1720359971 163 GTGLDEAMEWLVETL 177
Cdd:COG1100   155 GEGVEELFAALAEIL 169
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
18-175 6.81e-15

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: 68.25  E-value: 6.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  18 MRILILGLDGAGKTTILYRLQVGE-VVTTIPTIG--FNVETVTY--KNLKFQVWDLGGQ---TSIRPYwrcYYSNTDAVI 89
Cdd:cd00154     1 FKIVLIGDSGVGKTSLLLRFVDNKfSENYKSTIGvdFKSKTIEVdgKKVKLQIWDTAGQerfRSITSS---YYRGAHGAI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  90 YVVDSCDRDrigiSKSEL---VAMLEEEELRKAILVVFANKQDMEQA-MTPSEMANALglpaLKDRKWQIFKTSATKGTG 165
Cdd:cd00154    78 LVYDVTNRE----SFENLdkwLNELKEYAPPNIPIILVGNKSDLEDErQVSTEEAQQF----AKENGLLFFETSAKTGEN 149
                         170
                  ....*....|
gi 1720359971 166 LDEAMEWLVE 175
Cdd:cd00154   150 VDEAFESLAR 159
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
17-169 1.99e-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: 67.01  E-value: 1.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  17 EMRILILGLDGAGKTTILYRL--QVGEVVTTIPTIGFNVET--VTYKNL--KFQVWDLGGQTSIRPYWRCYYSNTDAVIY 90
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLlgNKGSITEYYPGTTRNYVTtvIEEDGKtyKFNLLDTAGQEDYDAIRRLYYPQVERSLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  91 VVDScdrDRIGISKSELVaMLEEEELR-----KAILVVFANKQDMEQAMTPSEManALGLPALKdrKWQIFKTSATKGTG 165
Cdd:TIGR00231  81 VFDI---VILVLDVEEIL-EKQTKEIIhhadsGVPIILVGNKIDLKDADLKTHV--ASEFAKLN--GEPIIPLSAETGKN 152

                  ....
gi 1720359971 166 LDEA 169
Cdd:TIGR00231 153 IDSA 156
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
19-178 2.33e-14

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: 66.77  E-value: 2.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILYRLQVGEVVTT-IPTIG--FNVETVTY--KNLKFQVWDLGGQ---TSIRPYwrcYYSNTDAVIY 90
Cdd:pfam00071   1 KLVLVGDGGVGKSSLLIRFTQNKFPEEyIPTIGvdFYTKTIEVdgKTVKLQIWDTAGQerfRALRPL---YYRGADGFLL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  91 VVDSCDRDrigiskS-ELVAMLEEEELRKA----ILVVFANKQDMEQ--AMTPSE---MANALGLPalkdrkwqIFKTSA 160
Cdd:pfam00071  78 VYDITSRD------SfENVKKWVEEILRHAdenvPIVLVGNKCDLEDqrVVSTEEgeaLAKELGLP--------FMETSA 143
                         170
                  ....*....|....*...
gi 1720359971 161 TKGTGLDEAMEWLVETLK 178
Cdd:pfam00071 144 KTNENVEEAFEELAREIL 161
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
20-143 3.64e-12

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: 61.95  E-value: 3.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  20 ILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVT---YKNLKFQVWDLGGQTSIRPYWRCYYSNTD-AVIYVVDSC 95
Cdd:cd04105     3 VLLLGPSDSGKTALFTKLTTGKVRSTVTSIEPNVASFYsnsSKGKKLTLVDVPGHEKLRDKLLEYLKASLkAIVFVVDSA 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720359971  96 DRDRigiSKSELVAML-----EEEELRKAI-LVVFANKQDMEQAMTPSEMANAL 143
Cdd:cd04105    83 TFQK---NIRDVAEFLydiltDLEKIKNKIpILIACNKQDLFTAKPAKKIKELL 133
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
19-129 4.10e-12

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: 59.83  E-value: 4.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILYRLQVGE-VVTTIPTIGFNVETVTY-------KNLKFQVWDLGGQT---SIRPYwrcYYSNTDA 87
Cdd:pfam08477   1 KVVLLGDSGVGKTSLLKRFVDDTfDPKYKSTIGVDFKTKTVlenddngKKIKLNIWDTAGQErfrSLHPF---YYRGAAA 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1720359971  88 VIYVVDSCDRDRIGISKSELvamleEEELRKAILVVFANKQD 129
Cdd:pfam08477  78 ALLVYDSRTFSNLKYWLREL-----KKYAGNSPVILVGNKID 114
Rab18 cd01863
Rab GTPase family 18 (Rab18); Rab18 subfamily. Mammalian Rab18 is implicated in endocytic ...
19-177 4.23e-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: 58.09  E-value: 4.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILYRLQVGEVVTTI-PTIG--FNVETVTY--KNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVD 93
Cdd:cd01863     2 KILLIGDSGVGKSSLLLRFTDDTFDEDLsSTIGvdFKVKTVTVdgKKVKLAIWDTAGQERFRTLTSSYYRGAQGVILVYD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  94 SCDRDrigiSKSELVAMLEEEEL----RKAILVVFANKQDMEQAMTPSEMANALGlpalKDRKWQIFKTSATKGTGLDEA 169
Cdd:cd01863    82 VTRRD----TFDNLDTWLNELDTystnPDAVKMLVGNKIDKENREVTREEGQKFA----RKHNMLFIETSAKTRIGVQQA 153

                  ....*...
gi 1720359971 170 MEWLVETL 177
Cdd:cd01863   154 FEELVEKI 161
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
18-180 4.44e-11

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


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 58.29  E-value: 4.44e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971   18 MRILILGLDGAGKTTILYRLQVGEVV-TTIPTIG--FNVETVTY--KNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVV 92
Cdd:smart00175   1 FKIILIGDSGVGKSSLLSRFTDGKFSeQYKSTIGvdFKTKTIEVdgKRVKLQIWDTAGQERFRSITSSYYRGAVGALLVY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971   93 DSCDRDrigiSKSELVAMLeeEELRK-----AILVVFANKQDMEQAMTPS-----EMANALGLPAlkdrkwqiFKTSATK 162
Cdd:smart00175  81 DITNRE----SFENLENWL--KELREyaspnVVIMLVGNKSDLEEQRQVSreeaeAFAEEHGLPF--------FETSAKT 146
                          170
                   ....*....|....*...
gi 1720359971  163 GTGLDEAMEWLVETLKSR 180
Cdd:smart00175 147 NTNVEEAFEELAREILKR 164
Rab1_Ypt1 cd01869
Rab GTPase family 1 includes the yeast homolog Ypt1; Rab1/Ypt1 subfamily. Rab1 is found in ...
19-180 3.59e-10

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: 55.80  E-value: 3.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILYRLQVGEVVTT-IPTIG--FNVETVTY--KNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVD 93
Cdd:cd01869     4 KLLLIGDSGVGKSCLLLRFADDTYTESyISTIGvdFKIRTIELdgKTVKLQIWDTAGQERFRTITSSYYRGAHGIIIVYD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  94 SCDRDRIGISKSEL--VAMLEEEELRKaILVvfANKQDMEQA-----MTPSEMANALGLPALkdrkwqifKTSATKGTGL 166
Cdd:cd01869    84 VTDQESFNNVKQWLqeIDRYASENVNK-LLV--GNKCDLTDKkvvdyTEAKEFADELGIPFL--------ETSAKNATNV 152
                         170
                  ....*....|....
gi 1720359971 167 DEAMEWLVETLKSR 180
Cdd:cd01869   153 EEAFMTMAREIKKR 166
RJL cd04119
Rab GTPase family J-like (RabJ-like); RJLs are found in many protists and as chimeras with ...
19-177 2.18e-09

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


Pssm-ID: 133319 [Multi-domain]  Cd Length: 168  Bit Score: 53.90  E-value: 2.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILYRLQVGE-VVTTIPTIG--FNVETVTYKNLKFQV--WDLGGQTSIRPYWRCYYSNTDAVIYVVD 93
Cdd:cd04119     2 KVISMGNSGVGKSCIIKRYCEGRfVSKYLPTIGidYGVKKVSVRNKEVRVnfFDLSGHPEYLEVRNEFYKDTQGVLLVYD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  94 SCDRDRIGISKSELVAMLEE----EELRKAILVVFANKQDMEQAMTPSEmanALGLPALKDRKWQIFKTSATKGTGLDEA 169
Cdd:cd04119    82 VTDRQSFEALDSWLKEMKQEggphGNMENIVVVVCANKIDLTKHRAVSE---DEGRLWAESKGFKYFETSACTGEGVNEM 158

                  ....*...
gi 1720359971 170 MEWLVETL 177
Cdd:cd04119   159 FQTLFSSI 166
Rab21 cd04123
Rab GTPase family 21 (Rab21); The localization and function of Rab21 are not clearly defined, ...
18-177 2.58e-09

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: 53.38  E-value: 2.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  18 MRILILGLDGAGKTTILYRLQVG-----EVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVV 92
Cdd:cd04123     1 FKVVLLGEGRVGKTSLVLRYVENkfnekHESTTQASFFQKTVNIGGKRIDLAIWDTAGQERYHALGPIYYRDADGAILVY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  93 DSCDRD---RIGISKSELVAMLEEeelrKAILVVFANKQDMEQAMTPS-----EMANALGLPalkdrkwqIFKTSATKGT 164
Cdd:cd04123    81 DITDADsfqKVKKWIKELKQMRGN----NISLVIVGNKIDLERQRVVSkseaeEYAKSVGAK--------HFETSAKTGK 148
                         170
                  ....*....|...
gi 1720359971 165 GLDEAMEWLVETL 177
Cdd:cd04123   149 GIEELFLSLAKRM 161
Rab8_Rab10_Rab13_like cd01867
Rab GTPase families 8, 10, 13 (Rab8, Rab10, Rab13); Rab8/Sec4/Ypt2 are known or suspected to ...
18-180 3.46e-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: 53.04  E-value: 3.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  18 MRILILGLDGAGKTTILYRLQVGEVVTT-IPTIG--FNVETVTY--KNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVV 92
Cdd:cd01867     4 FKLLLIGDSGVGKSCLLLRFSEDSFNPSfISTIGidFKIRTIELdgKKIKLQIWDTAGQERFRTITTSYYRGAMGIILVY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  93 DSCDRDRIGiSKSELVAMLEEEELRKAILVVFANKQDMEQAMTPS-----EMANALGLPalkdrkwqIFKTSATKGTGLD 167
Cdd:cd01867    84 DITDEKSFE-NIKNWMRNIDEHASEDVERMLVGNKCDMEEKRVVSkeegeALAREYGIK--------FLETSAKANINVE 154
                         170
                  ....*....|...
gi 1720359971 168 EAMEWLVETLKSR 180
Cdd:cd01867   155 EAFLTLAKDILKK 167
PLN03118 PLN03118
Rab family protein; Provisional
19-98 3.50e-09

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 53.91  E-value: 3.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVE----TVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDS 94
Cdd:PLN03118   16 KILLIGDSGVGKSSLLVSFISSSVEDLAPTIGVDFKikqlTVGGKRLKLTIWDTAGQERFRTLTSSYYRNAQGIILVYDV 95

                  ....
gi 1720359971  95 CDRD 98
Cdd:PLN03118   96 TRRE 99
Rab15 cd04117
Rab GTPase family 15 (Rab15); Rab15 colocalizes with the transferrin receptor in early ...
19-175 9.09e-09

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: 51.90  E-value: 9.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILYRLQVGEVVTT-IPTIG--FNVETVTYKNLK--FQVWDLGGQTSIRPYWRCYYSNTDAVIYVVD 93
Cdd:cd04117     2 RLLLIGDSGVGKTCLLCRFTDNEFHSShISTIGvdFKMKTIEVDGIKvrIQIWDTAGQERYQTITKQYYRRAQGIFLVYD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  94 -SCDRDRIGISKseLVAMLEEEELRKAILVVFANKQDMEQA-MTPSEMANALGLPALKDrkwqIFKTSATKGTGLDEAME 171
Cdd:cd04117    82 iSSERSYQHIMK--WVSDVDEYAPEGVQKILIGNKADEEQKrQVGDEQGNKLAKEYGMD----FFETSACTNKNIKESFT 155

                  ....
gi 1720359971 172 WLVE 175
Cdd:cd04117   156 RLTE 159
Rab5_related cd01860
Rab-related GTPase family includes Rab5 and Rab22; regulates early endosome fusion; The ...
19-177 2.24e-08

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: 51.01  E-value: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILYRLQVGEVVTTI-PTIG--FNVETVTY--KNLKFQVWDLGGQ---TSIRPYwrcYYSNTDAVIY 90
Cdd:cd01860     3 KLVLLGDSSVGKSSIVLRFVKNEFSENQeSTIGaaFLTQTVNLddTTVKFEIWDTAGQeryRSLAPM---YYRGAAAAIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  91 VVDSCDRDRIGISKSELvamleeEELRKA-----ILVVFANKQDMEQA-MTPSEMANALGlpalkDRKWQIFK-TSATKG 163
Cdd:cd01860    80 VYDITSEESFEKAKSWV------KELQEHgppniVIALAGNKADLESKrQVSTEEAQEYA-----DENGLLFMeTSAKTG 148
                         170
                  ....*....|....
gi 1720359971 164 TGLDEAMEWLVETL 177
Cdd:cd01860   149 ENVNELFTEIARKL 162
Rab33B_Rab33A cd04115
Rab GTPase family 33 includes Rab33A and Rab33B; Rab33B/Rab33A subfamily. Rab33B is ...
16-160 3.11e-08

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: 50.51  E-value: 3.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  16 REMRILILGLDGAGKTTILYRLQVGEVV-TTIPTIG--FNVETVTY--KNLKFQVWDLGGQTSIRPYW-RCYYSNTDAVI 89
Cdd:cd04115     1 RIFKIIVIGDSNVGKTCLTYRFCAGRFPeRTEATIGvdFRERTVEIdgERIKVQLWDTAGQERFRKSMvQHYYRNVHAVV 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720359971  90 YVVDSCDRDrigiSKSELVAMLEEEE------LRKAILVvfANKQDM-EQAMTPSEMANALGLPalkdRKWQIFKTSA 160
Cdd:cd04115    81 FVYDVTNMA----SFHSLPSWIEECEqhslpnEVPRILV--GNKCDLrEQIQVPTDLAQRFADA----HSMPLFETSA 148
Rab35 cd04110
Rab GTPase family 35 (Rab35); Rab35 is one of several Rab proteins to be found to participate ...
19-93 1.89e-07

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: 49.08  E-value: 1.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILYRLQ----VGEVVTTIpTIGFNVETVTY--KNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVV 92
Cdd:cd04110     8 KLLIIGDSGVGKSSLLLRFAdntfSGSYITTI-GVDFKIRTVEIngERVKLQIWDTAGQERFRTITSTYYRGTHGVIVVY 86

                  .
gi 1720359971  93 D 93
Cdd:cd04110    87 D 87
Rab26 cd04112
Rab GTPase family 26 (Rab26); Rab26 subfamily. First identified in rat pancreatic acinar cells, ...
19-180 2.27e-07

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: 48.71  E-value: 2.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILYRLQVGEVV--TTIPTIGFN----VETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVV 92
Cdd:cd04112     2 KVMLVGDSGVGKTCLLVRFKDGAFLagSFIATVGIQftnkVVTVDGVKVKLQIWDTAGQERFRSVTHAYYRDAHALLLLY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  93 DSCDRDRIGISKSELVAMLEEEElRKAILVVFANKQDM--EQAMTPSE---MANALGLPALkdrkwqifKTSATKGTGLD 167
Cdd:cd04112    82 DVTNKSSFDNIRAWLTEILEYAQ-SDVVIMLLGNKADMsgERVVKREDgerLAKEYGVPFM--------ETSAKTGLNVE 152
                         170
                  ....*....|...
gi 1720359971 168 EAMEWLVETLKSR 180
Cdd:cd04112   153 LAFTAVAKELKHR 165
Rab39 cd04111
Rab GTPase family 39 (Rab39); Found in eukaryotes, Rab39 is mainly found in epithelial cell ...
19-181 3.46e-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: 3.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILYRLQVGEVV-TTIPTIGFN-----VETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVV 92
Cdd:cd04111     4 RLIVIGDSTVGKSSLLKRFTEGRFAeVSDPTVGVDffsrlIEIEPGVRIKLQLWDTAGQERFRSITRSYYRNSVGVLLVF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  93 DSCDRDrigiSKSELVAMLEEEELR----KAILVVFANKQDM--EQAMTPSEmANALGlpalKDRKWQIFKTSATKGTGL 166
Cdd:cd04111    84 DITNRE----SFEHVHDWLEEARSHiqphRPVFILVGHKCDLesQRQVTREE-AEKLA----KDLGMKYIETSARTGDNV 154
                         170
                  ....*....|....*
gi 1720359971 167 DEAMEWLVETLKSRQ 181
Cdd:cd04111   155 EEAFELLTQEIYERI 169
Rab4 cd04113
Rab GTPase family 4 (Rab4); Rab4 subfamily. Rab4 has been implicated in numerous functions ...
19-169 3.96e-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: 47.43  E-value: 3.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILYRLQVGEVVTTIP-TIG--FNVETVTY--KNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVD 93
Cdd:cd04113     2 KFLIIGSAGTGKSCLLHQFIENKFKQDSNhTIGveFGSRVVNVggKSVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  94 SCDRDRIGISKSEL--VAMLEEEELrkaILVVFANKQDMEQA-----MTPSEMANALGLpalkdrkwQIFKTSATKGTGL 166
Cdd:cd04113    82 ITSRESFNALTNWLtdARTLASPDI---VIILVGNKKDLEDDrevtfLEASRFAQENGL--------LFLETSALTGENV 150

                  ...
gi 1720359971 167 DEA 169
Cdd:cd04113   151 EEA 153
Rab3 cd01865
Rab GTPase family 3 contains Rab3A, Rab3B, Rab3C and Rab3D; The Rab3 subfamily contains Rab3A, ...
19-177 8.25e-07

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


Pssm-ID: 206657 [Multi-domain]  Cd Length: 165  Bit Score: 46.83  E-value: 8.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILYRLQ----VGEVVTTIpTIGFNVETVTY--KNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVV 92
Cdd:cd01865     3 KLLIIGNSSVGKTSFLFRYAddsfTSAFVSTV-GIDFKVKTVYRndKRIKLQIWDTAGQERYRTITTAYYRGAMGFILMY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  93 DSCDRDRIGiSKSELVAMLEEEELRKAILVVFANKQDMEQAMTPS-----EMANALGLpalkdrkwQIFKTSATKGTGLD 167
Cdd:cd01865    82 DITNEESFN-AVQDWSTQIKTYSWDNAQVILVGNKCDMEDERVVSaergrQLADQLGF--------EFFEASAKENINVK 152
                         170
                  ....*....|
gi 1720359971 168 EAMEWLVETL 177
Cdd:cd01865   153 QVFERLVDII 162
G-alpha pfam00503
G-protein alpha subunit; G proteins couple receptors of extracellular signals to intracellular ...
46-130 8.69e-07

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: 47.58  E-value: 8.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  46 IPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSCDRD----------RIGISKSELVAMLEEEE 115
Cdd:pfam00503 152 VKTTGIIETKFEFKGLKFRLFDVGGQRSERKKWIHCFEDVTAIIFVVSLSEYDqvlyeddstnRMEESLKLFEEICNSPW 231
                          90
                  ....*....|....*
gi 1720359971 116 LRKAILVVFANKQDM 130
Cdd:pfam00503 232 FKNTPIILFLNKKDL 246
Rab19 cd01864
Rab GTPase family 19 (Rab19); Rab19 subfamily. Rab19 proteins are associated with Golgi stacks. ...
19-177 1.43e-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: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILYRLQVGEVVTTI-PTIG--FNVETVTY--KNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVD 93
Cdd:cd01864     5 KIILIGDSNVGKTCVVQRFKSGTFSERQgNTIGvdFTMKTLEIqgKRVKLQIWDTAGQERFRTITQSYYRSANGAIIAYD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  94 SCDRDrigiSKSELVAMLEEEELRKA---ILVVFANKQDMEQ-----AMTPSEMANALGLPAlkdrkwqIFKTSATKGTG 165
Cdd:cd01864    85 ITRRS----SFESVPHWIEEVEKYGAsnvVLLLIGNKCDLEEqrevlFEEACTLAEHYGILA-------VLETSAKESSN 153
                         170
                  ....*....|..
gi 1720359971 166 LDEAMEWLVETL 177
Cdd:cd01864   154 VEEAFLLMATEL 165
RocCOR cd09914
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ...
17-71 4.43e-06

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: 44.63  E-value: 4.43e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720359971  17 EMRILILGLDGAGKTTILYRLqVGEVV--TTIPTIGFNVETVTYKN-----LKFQVWDLGGQ 71
Cdd:cd09914     1 EAKLMLVGQGGVGKTSLCKQL-IGEKFdgDESSTHGINVQDWKIPAperkkIRLNVWDFGGQ 61
Rab27A cd04127
Rab GTPase family 27a (Rab27a); The Rab27a subfamily consists of Rab27a and its highly ...
18-180 6.23e-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: 44.41  E-value: 6.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  18 MRILILGLDGAGKTTILYRLQVGEVVTT-IPTIG--FNVETVTYKN------------LKFQVWDLGGQTSIRPYWRCYY 82
Cdd:cd04127     5 IKLLALGDSGVGKTTFLYRYTDNKFNPKfITTVGidFREKRVVYNSqgpdgtsgkafrVHLQLWDTAGQERFRSLTTAFF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  83 SNTDAVIYVVD-----SCDRDRIGISKSELVAMLEEEElrkaiLVVFANKQDMEQAMTPS-----EMANALGLPalkdrk 152
Cdd:cd04127    85 RDAMGFLLMFDltseqSFLNVRNWMSQLQAHAYCENPD-----IVLIGNKADLPDQREVSerqarELADKYGIP------ 153
                         170       180
                  ....*....|....*....|....*...
gi 1720359971 153 wqIFKTSATKGTGLDEAMEWLVETLKSR 180
Cdd:cd04127   154 --YFETSAATGQNVEKAVETLLDLIMKR 179
Rab32_Rab38 cd04107
Rab GTPase families 18 (Rab18) and 32 (Rab32); Rab38/Rab32 subfamily. Rab32 and Rab38 are ...
19-177 7.72e-06

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


Pssm-ID: 206692 [Multi-domain]  Cd Length: 201  Bit Score: 44.22  E-value: 7.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILYRLqvgevVTTI------PTIG--FNVETVT---YKNLKFQVWDLGGQTSIRPYWRCYYSNTDA 87
Cdd:cd04107     2 KVLVIGDLGVGKTSIIKRY-----VHGVfsqhykATIGvdFALKVIEwdpNTVVRLQLWDIAGQERFGGMTRVYYKGAVG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  88 VIYVVDSCDRDRIGIS---KSEL---VAMLEEEELRkAILVvfANKQDMEQA--MTPSEMANAL----GLPAlkdrkWqi 155
Cdd:cd04107    77 AIIVFDVTRPSTFEAVlkwKADLdskVTLPNGEPIP-ALLL--ANKCDLKKErlAKDPEQMDQFckenGFIG-----W-- 146
                         170       180
                  ....*....|....*....|..
gi 1720359971 156 FKTSATKGTGLDEAMEWLVETL 177
Cdd:cd04107   147 FETSAKENINIEEAMRFLVKNI 168
Rab30 cd04114
Rab GTPase family 30 (Rab30); Rab30 subfamily. Rab30 appears to be associated with the Golgi ...
19-130 9.08e-06

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


Pssm-ID: 133314 [Multi-domain]  Cd Length: 169  Bit Score: 43.73  E-value: 9.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILYRLQVGevvtTIP-----TIG--FNVETVTYKN--LKFQVWDLGGQTSIRPYWRCYYSNTDAVI 89
Cdd:cd04114     9 KIVLIGNAGVGKTCLVRRFTQG----LFPpgqgaTIGvdFMIKTVEIKGekIKLQIWDTAGQERFRSITQSYYRSANALI 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1720359971  90 YVVD-SCDRDRIGIskSELVAMLEEEELRKAILVVFANKQDM 130
Cdd:cd04114    85 LTYDiTCEESFRCL--PEWLREIEQYANNKVITILVGNKIDL 124
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
19-127 9.74e-06

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: 42.61  E-value: 9.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILYRLqVGEVVTT--IP--TIGFNVETVTYKNLKFQVWDLGG--QTSIRPYW--RCYYSN--TDAV 88
Cdd:pfam01926   1 RVALVGRPNVGKSTLINAL-TGAKAIVsdYPgtTRDPNEGRLELKGKQIILVDTPGliEGASEGEGlgRAFLAIieADLI 79
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1720359971  89 IYVVDScdRDRIGISKSELVAMLEEEElrKAILVVFaNK 127
Cdd:pfam01926  80 LFVVDS--EEGITPLDEELLELLRENK--KPIILVL-NK 113
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
22-177 1.13e-05

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: 43.39  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  22 ILGLDGAGKTTILYRL---QVGEV-----VTTIPtIGFNVETVTYKNLKFQvwDLGGQTSIRPY--------WRcYYSNT 85
Cdd:cd00880     2 IFGRPNVGKSSLLNALlgqNVGIVspipgTTRDP-VRKEWELLPLGPVVLI--DTPGLDEEGGLgrerveeaRQ-VADRA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  86 DAVIYVVDScdrdriGISKSELVAMLEEEELR-KAILVVFaNKQDMEQAMTPSEMANALGLPALKDRKwqIFKTSATKGT 164
Cdd:cd00880    78 DLVLLVVDS------DLTPVEEEAKLGLLRERgKPVLLVL-NKIDLVPESEEEELLRERKLELLPDLP--VIAVSALPGE 148
                         170
                  ....*....|...
gi 1720359971 165 GLDEAMEWLVETL 177
Cdd:cd00880   149 GIDELRKKIAELL 161
PLN03108 PLN03108
Rab family protein; Provisional
19-98 5.42e-05

Rab family protein; Provisional


Pssm-ID: 178655 [Multi-domain]  Cd Length: 210  Bit Score: 42.24  E-value: 5.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILY-----RLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVD 93
Cdd:PLN03108    8 KYIIIGDTGVGKSCLLLqftdkRFQPVHDLTIGVEFGARMITIDNKPIKLQIWDTAGQESFRSITRSYYRGAAGALLVYD 87

                  ....*
gi 1720359971  94 SCDRD 98
Cdd:PLN03108   88 ITRRE 92
Rab9 cd04116
Rab GTPase family 9 (Rab9); Rab9 is found in late endosomes, together with mannose 6-phosphate ...
18-171 6.50e-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: 41.40  E-value: 6.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  18 MRILILGLDGAGKTTILYRLqvgeVVTTIPTIGFNVETVTYKN---------LKFQVWDLGGQTSIRPYWRCYYSNTDAV 88
Cdd:cd04116     6 LKVILLGDGGVGKSSLMNRY----VTNKFDTQLFHTIGVEFLNkdlevdghfVTLQIWDTAGQERFRSLRTPFYRGSDCC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  89 IYVVDSCDRDR---IGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPSEMANALglpALKDRKWQIFKTSATKGTG 165
Cdd:cd04116    82 LLTFSVDDSQSfqnLSNWKKEFIYYADVKEPESFPFVILGNKIDIPERQVSTEEAQAW---CRDNGDYPYFETSAKDATN 158

                  ....*.
gi 1720359971 166 LDEAME 171
Cdd:cd04116   159 VAAAFE 164
PLN03110 PLN03110
Rab GTPase; Provisional
19-171 6.84e-05

Rab GTPase; Provisional


Pssm-ID: 178657 [Multi-domain]  Cd Length: 216  Bit Score: 41.84  E-value: 6.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILYRLQVGE-VVTTIPTIGFNVETVTY----KNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVD 93
Cdd:PLN03110   14 KIVLIGDSGVGKSNILSRFTRNEfCLESKSTIGVEFATRTLqvegKTVKAQIWDTAGQERYRAITSAYYRGAVGALLVYD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  94 SCDRDRIGISKSELVAMLEEEELRKAILVVfANKQDMEQAMTPSE-----MANALGLPALkdrkwqifKTSATKGTGLDE 168
Cdd:PLN03110   94 ITKRQTFDNVQRWLRELRDHADSNIVIMMA-GNKSDLNHLRSVAEedgqaLAEKEGLSFL--------ETSALEATNVEK 164

                  ...
gi 1720359971 169 AME 171
Cdd:PLN03110  165 AFQ 167
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
86-177 7.15e-05

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: 41.29  E-value: 7.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  86 DAVIYVVDSCDRDRIGISKseLVAMLEEEElRKAILVVfaNKQDmeQAMTPSEMANALGLPALKDRKWQIFKTSATKGTG 165
Cdd:cd04163    84 DLVLFVVDASEWIGEGDEF--ILELLKKSK-TPVILVL--NKID--LVKDKEDLLPLLEKLKELHPFAEIFPISALKGEN 156
                          90
                  ....*....|..
gi 1720359971 166 LDEAMEWLVETL 177
Cdd:cd04163   157 VDELLEYIVEYL 168
Gtr1_RagA pfam04670
Gtr1/RagA G protein conserved region; GTR1 was first identified in S. cerevisiae as a ...
19-100 8.21e-05

Gtr1/RagA G protein conserved region; GTR1 was first identified in S. cerevisiae as a suppressor of a mutation in RCC1. Biochemical analysis revealed that Gtr1 is in fact a G protein of the Ras family. The RagA/B proteins are the human homologs of Gtr1. Included in this family is the human Rag C, a novel protein that has been shown to interact with RagA/B.


Pssm-ID: 398377 [Multi-domain]  Cd Length: 231  Bit Score: 41.41  E-value: 8.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTT----ILYRLQVGEVVTTIPTIGFNVETV-TYKNLKFQVWDLGGQTSI-RPYWR----CYYSNTDAV 88
Cdd:pfam04670   1 KVLLMGLSGSGKSSmrsvIFSNYSPRDTLRLGATIDVEHSHVrFLGNLVLNLWDCGGQDDFfDNYLTfqkeHIFSNVGVL 80
                          90
                  ....*....|..
gi 1720359971  89 IYVVDSCDRDRI 100
Cdd:pfam04670  81 IYVFDVQSREYE 92
Rab2 cd01866
Rab GTPase family 2 (Rab2); Rab2 is localized on cis-Golgi membranes and interacts with Golgi ...
21-131 1.30e-04

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: 40.48  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  21 LILGLDGAGKTTILY-----RLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSC 95
Cdd:cd01866     8 IIIGDTGVGKSCLLLqftdkRFQPVHDLTIGVEFGARMITIDGKQIKLQIWDTAGQESFRSITRSYYRGAAGALLVYDIT 87
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1720359971  96 DRDrigiSKSELVAMLEEEELR---KAILVVFANKQDME 131
Cdd:cd01866    88 RRE----TFNHLTSWLEDARQHsnsNMTIMLIGNKCDLE 122
Rab12 cd04120
Rab GTPase family 12 (Rab12); Rab12 was first identified in canine cells, where it was ...
18-131 1.83e-04

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: 40.38  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  18 MRILILGLDGAGKTTILYRL---QVGEVVTTIPTIGFNVETVTY--KNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVV 92
Cdd:cd04120     1 LQVIIIGSRGVGKTSLMERFtddTFCEACKSTVGVDFKIKTVELrgKKIRLQIWDTAGQERFNSITSAYYRSAKGIILVY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720359971  93 DscdrdrigISKSEL-------VAMLEEEELRKAILVVFANKQDME 131
Cdd:cd04120    81 D--------ITKKETfddlpkwMKMIDKYASEDAELLLVGNKLDCE 118
Rab6 cd01861
Rab GTPase family 6 (Rab6); Rab6 is involved in microtubule-dependent transport pathways ...
19-177 1.95e-04

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: 39.91  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILYRLQVGEVV-TTIPTIG--FNVETVTY--KNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVD 93
Cdd:cd01861     2 KLVFLGDQSVGKTSIITRFMYDTFDnQYQATIGidFLSKTMYVddKTVRLQLWDTAGQERFRSLIPSYIRDSSVAVVVYD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  94 SCDRDRIgISKSELVAMLEEEELRKAILVVFANKQDMEQAMTPS--EMANALGLPALKDRkwqifKTSATKGTGLDEAME 171
Cdd:cd01861    82 ITNRQSF-DNTDKWIDDVRDERGNDVIIVLVGNKTDLSDKRQVSteEGEKKAKENNAMFI-----ETSAKAGHNVKQLFK 155

                  ....*.
gi 1720359971 172 WLVETL 177
Cdd:cd01861   156 KIAQAL 161
Rab14 cd04122
Rab GTPase family 14 (Rab14); Rab14 GTPases are localized to biosynthetic compartments, ...
21-93 3.64e-04

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: 39.43  E-value: 3.64e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720359971  21 LILGLDGAGKTTILYRLQVGEVVTTIP-TIGFNVET----VTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVD 93
Cdd:cd04122     6 IIIGDMGVGKSCLLHQFTEKKFMADCPhTIGVEFGTriieVNGQKIKLQIWDTAGQERFRAVTRSYYRGAAGALMVYD 83
PTZ00132 PTZ00132
GTP-binding nuclear protein Ran; Provisional
17-98 3.97e-04

GTP-binding nuclear protein Ran; Provisional


Pssm-ID: 240284 [Multi-domain]  Cd Length: 215  Bit Score: 39.68  E-value: 3.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  17 EMRILILGLDGAGKTTILYRLQVGEVVTT-IPTIGFNVETVT-YKN---LKFQVWDLGGQTSIRPYWRCYYSNTDAVIYV 91
Cdd:PTZ00132    9 EFKLILVGDGGVGKTTFVKRHLTGEFEKKyIPTLGVEVHPLKfYTNcgpICFNVWDTAGQEKFGGLRDGYYIKGQCAIIM 88

                  ....*..
gi 1720359971  92 VDSCDRD 98
Cdd:PTZ00132   89 FDVTSRI 95
RabL3 cd04102
Rab GTPase-like family 3 (Rab-like3); RabL3 (Rab-like3) subfamily. RabL3s are novel proteins ...
18-97 4.42e-04

Rab GTPase-like family 3 (Rab-like3); RabL3 (Rab-like3) subfamily. RabL3s are novel proteins that have high sequence similarity with Rab family members, but display features that are distinct from Rabs, and have been termed Rab-like. As in other Rab-like proteins, RabL3 lacks a prenylation site at the C-terminus. The specific function of RabL3 remains unknown.


Pssm-ID: 206689  Cd Length: 204  Bit Score: 39.50  E-value: 4.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  18 MRILILGLDGAGKTTILYRLQVGEVVTTIP-TIG--FNVETVTY-------KNLKFQVWDLGGQ----TSIRPYWRCYYS 83
Cdd:cd04102     1 VKVLVLGDSGVGKSSLVHLLCKNQVLGNPSwTVGcsVDVRHHTYgegtpeeKTFYVELWDVGGSvgsaESVKSTRAVFYN 80
                          90
                  ....*....|....
gi 1720359971  84 NTDAVIYVVDSCDR 97
Cdd:cd04102    81 QINGIIFVHDLTNK 94
Rhes_like cd04143
Ras homolog enriched in striatum (Rhes) and activator of G-protein signaling 1 (Dexras1/AGS1); ...
19-173 4.54e-04

Ras homolog enriched in striatum (Rhes) and activator of G-protein signaling 1 (Dexras1/AGS1); This subfamily includes Rhes (Ras homolog enriched in striatum) and Dexras1/AGS1 (activator of G-protein signaling 1). These proteins are homologous, but exhibit significant differences in tissue distribution and subcellular localization. Rhes is found primarily in the striatum of the brain, but is also expressed in other areas of the brain, such as the cerebral cortex, hippocampus, inferior colliculus, and cerebellum. Rhes expression is controlled by thyroid hormones. In rat PC12 cells, Rhes is farnesylated and localizes to the plasma membrane. Rhes binds and activates PI3K, and plays a role in coupling serpentine membrane receptors with heterotrimeric G-protein signaling. Rhes has recently been shown to be reduced under conditions of dopamine supersensitivity and may play a role in determining dopamine receptor sensitivity. Dexras1/AGS1 is a dexamethasone-induced Ras protein that is expressed primarily in the brain, with low expression levels in other tissues. Dexras1 localizes primarily to the cytoplasm, and is a critical regulator of the circadian master clock to photic and nonphotic input. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins.


Pssm-ID: 133343 [Multi-domain]  Cd Length: 247  Bit Score: 39.35  E-value: 4.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  19 RILILGLDGAGKTTILYRLQVGEVVTT-IPTI-GFNVETVTYKNLKFQVwDLGGQTSIRPY---WRCYYSNTDAVIYVVD 93
Cdd:cd04143     2 RMVVLGASKVGKTAIVSRFLGGRFEEQyTPTIeDFHRKLYSIRGEVYQL-DILDTSGNHPFpamRRLSILTGDVFILVFS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  94 SCDRDrigiSKSELVAMLEE------------EELRKAILVVFANKQDMEQAMTP--SEMANALGlpalKDRKWQIFKTS 159
Cdd:cd04143    81 LDNRE----SFEEVCRLREQiletksclknktKENVKIPMVICGNKADRDFPREVqrDEVEQLVG----GDENCAYFEVS 152
                         170
                  ....*....|....
gi 1720359971 160 ATKGTGLDEAMEWL 173
Cdd:cd04143   153 AKKNSNLDEMFRAL 166
G_alpha smart00275
G protein alpha subunit; Subunit of G proteins that contains the guanine nucleotide binding ...
46-129 6.57e-04

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: 39.10  E-value: 6.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971   46 IPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSCDRDRIgiskselvamLEEEE---------- 115
Cdd:smart00275 169 VPTTGIQETAFIVKKLFFRMFDVGGQRSERKKWIHCFDNVTAIIFCVALSEYDQV----------LEEDEstnrmqesln 238
                           90       100
                   ....*....|....*....|....
gi 1720359971  116 ----------LRKAILVVFANKQD 129
Cdd:smart00275 239 lfesicnsrwFANTSIILFLNKID 262
RERG_RasL11_like cd04146
Ras-related and Estrogen-Regulated Growth inhibitor (RERG) and Ras-like 11 (RasL11)-like ...
20-133 1.40e-03

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: 37.64  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  20 ILILGLDGAGKTTILYRLQ----VGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQT----------SIRpyWrcyysnT 85
Cdd:cd04146     2 IAVLGASGVGKSALTVRFLtkrfIGEYEPNLESLYSRQVTIDGEQVSLEIQDTPGQQqnedpeslerSLR--W------A 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720359971  86 DAVIYVVDSCDRDRIGISKS--ELVAMLEEEELRKAILVVfANKQDMEQA 133
Cdd:cd04146    74 DGFVLVYSITDRSSFDVVSQllQLIREIKKRDGEIPVILV-GNKADLLHS 122
G-alpha cd00066
Alpha subunit of G proteins (guanine nucleotide binding); The alpha subunit of G proteins ...
46-129 1.55e-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: 37.89  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  46 IPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSCDRDRIGISKSELVAMLEEEELRKAI----- 120
Cdd:cd00066   146 VKTTGIIETDFSIKNLKFRMFDVGGQRSERKKWIHCFEDVTAIIFVVALSEYDQVLVEDESVNRMQESLKLFDSIcnsrw 225
                          90
                  ....*....|....
gi 1720359971 121 -----LVVFANKQD 129
Cdd:cd00066   226 fantsIILFLNKKD 239
Rab28 cd04109
Rab GTPase family 28 (Rab28); Rab28 subfamily. First identified in maize, Rab28 has been shown ...
18-132 2.05e-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: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  18 MRILILGlDGA-GKTTILYRL-QVGEVVTTIPTIG--FNVETVTY---KNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIY 90
Cdd:cd04109     1 IKIVVLG-DGAsGKTSLIRRFaQEGFGKSYKQTIGldFFSRRITLpgsLNVTLQVWDIGGQQIGGKMLDKYIYGAQAVCL 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720359971  91 VVDSCDrdrigiSKS--------ELVAMLEEEELRKAILVVFANKQDMEQ 132
Cdd:cd04109    80 VYDITN------SQSfenledwlSVVKKVNEESETKPKMVLVGNKTDLEH 123
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
86-178 2.14e-03

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


Pssm-ID: 206684 [Multi-domain]  Cd Length: 167  Bit Score: 37.15  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  86 DAVIYVVD---SCdrdriGISKSELVAMLEE-EELRKAILVVFANKQDMeqaMTPSEMANALGLPALKDRKWqiFKTSAT 161
Cdd:cd01897    81 AAVLFFIDpseTC-----GYSIEEQLSLFKEiKPLFNKPVIVVLNKIDL---LTEEDLSEIEKELEKEGEEV--IKISTL 150
                          90
                  ....*....|....*..
gi 1720359971 162 KGTGLDEAMEWLVETLK 178
Cdd:cd01897   151 TEEGVDELKNKACELLL 167
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
86-177 2.97e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 37.34  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720359971  86 DAVIYVVDScdrdRIGISKS-ELVAmleeEELRKA----ILVVfaNKQDMEQAMTPSEMANALGLPalkdrkwQIFKTSA 160
Cdd:PRK00093   82 DVILFVVDG----RAGLTPAdEEIA----KILRKSnkpvILVV--NKVDGPDEEADAYEFYSLGLG-------EPYPISA 144
                          90
                  ....*....|....*..
gi 1720359971 161 TKGTGLDEAMEWLVETL 177
Cdd:PRK00093  145 EHGRGIGDLLDAILEEL 161
 
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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