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Conserved domains on  [gi|15235226|ref|NP_192117|]
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secretion-associated RAS super family 2 [Arabidopsis thaliana]

Protein Classification

GTP-binding protein Sar1( domain architecture ID 10096332)

GTP-binding protein Sar1 is a small GTPase component of COPII vesicle coats involved in export of cargo from the endoplasmic reticulum (ER), and functions as a molecular switch to control protein-protein and protein-lipid interactions that direct vesicle budding from the ER

CATH:  3.40.50.300
Gene Ontology:  GO:0003924|GO:0005525
PubMed:  1898771|12429613|11995995|2122258
SCOP:  4004043

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Sar1 cd00879
Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII ...
 2-192 2.39e-133

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: 371.23  E-value: 2.39e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226   2 FMIDWFYGVLASLGLWQKEAKILFLGLDNAGKTTLLHMLKDERLVQHQPTQHPTSEELSIGKIKFKAFDLGGHQIARRVW 81
Cdd:cd00879   1 FIFDWFYNVLSSLGLYKKEAKIVFLGLDNAGKTTLLHMLKDDRLAQHVPTLHPTSEELTIGNVKFTTFDLGGHEQARRVW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  82 KDYYAKVDAVVYLVDAYDKERFAESKKELDALLSDESLASVPFLILGNKIDIPYAASEDELRYHLGLSNFTTGKGKVNLT 161
Cdd:cd00879  81 KDYFPEVDGIVFLVDAADPERFQESKEELDSLLNDEELANVPILILGNKIDKPGAVSEEELREALGLYGTTTGKGGVSLK 160

                       170       180       190
                ....*....|....*....|....*....|.
gi 15235226 162 DSNVRPLEVFMCSIVRKMGYGEGFKWVSQYI 192
Cdd:cd00879 161 VSNIRPVEVFMCSVVKRQGYGEGFRWLSQYL 191
 
Name Accession Description Interval E-value
Sar1 cd00879
Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII ...
 2-192 2.39e-133

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: 371.23  E-value: 2.39e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226   2 FMIDWFYGVLASLGLWQKEAKILFLGLDNAGKTTLLHMLKDERLVQHQPTQHPTSEELSIGKIKFKAFDLGGHQIARRVW 81
Cdd:cd00879   1 FIFDWFYNVLSSLGLYKKEAKIVFLGLDNAGKTTLLHMLKDDRLAQHVPTLHPTSEELTIGNVKFTTFDLGGHEQARRVW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  82 KDYYAKVDAVVYLVDAYDKERFAESKKELDALLSDESLASVPFLILGNKIDIPYAASEDELRYHLGLSNFTTGKGKVNLT 161
Cdd:cd00879  81 KDYFPEVDGIVFLVDAADPERFQESKEELDSLLNDEELANVPILILGNKIDKPGAVSEEELREALGLYGTTTGKGGVSLK 160

                       170       180       190
                ....*....|....*....|....*....|.
gi 15235226 162 DSNVRPLEVFMCSIVRKMGYGEGFKWVSQYI 192
Cdd:cd00879 161 VSNIRPVEVFMCSVVKRQGYGEGFRWLSQYL 191
SAR smart00178
Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene ...
 4-192 2.72e-130

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: 363.10  E-value: 2.72e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226      4 IDWFYGVLASLGLWQKEAKILFLGLDNAGKTTLLHMLKDERLVQHQPTQHPTSEELSIGKIKFKAFDLGGHQIARRVWKD 83
Cdd:smart00178   1 FDWFYDILASLGLWNKHAKILFLGLDNAGKTTLLHMLKNDRLAQHQPTQHPTSEELAIGNIKFTTFDLGGHQQARRLWKD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226     84 YYAKVDAVVYLVDAYDKERFAESKKELDALLSDESLASVPFLILGNKIDIPYAASEDELRYHLGLSNFTTGKGKVnltds 163
Cdd:smart00178  81 YFPEVNGIVYLVDAYDKERFAESKRELDALLSDEELATVPFLILGNKIDAPYAASEDELRYALGLTNTTTGKGKV----- 155

                          170       180
                   ....*....|....*....|....*....
gi 15235226    164 NVRPLEVFMCSIVRKMGYGEGFKWVSQYI 192
Cdd:smart00178 156 GVRPVEVFMCSVVRRMGYGEGFKWLSQYI 184
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
 21-192 1.09e-85

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


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 249.45  E-value: 1.09e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226    21 AKILFLGLDNAGKTTLLHMLKDERLVQHQPTQHPTSEELSIGKIKFKAFDLGGHQIARRVWKDYYAKVDAVVYLVDAYDK 100
Cdd:pfam00025   1 MRILILGLDNAGKTTILYKLKLGEIVTTIPTIGFNVETVTYKNVKFTVWDVGGQESLRPLWRNYFPNTDAVIFVVDSADR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226   101 ERFAESKKELDALLSDESLASVPFLILGNKIDIPYAASEDELRYHLGLSNFTTgkgkvnltdsnvRPLEVFMCSIVRKMG 180
Cdd:pfam00025  81 DRIEEAKEELHALLNEEELADAPLLILANKQDLPGAMSEAEIRELLGLHELKD------------RPWEIQGCSAVTGEG 148

                         170
                  ....*....|..
gi 15235226   181 YGEGFKWVSQYI 192
Cdd:pfam00025 149 LDEGLDWLSNYI 160
PTZ00133 PTZ00133
ADP-ribosylation factor; Provisional
 3-193 4.40e-29

ADP-ribosylation factor; Provisional


Pssm-ID: 173423  Cd Length: 182  Bit Score: 106.47  E-value: 4.40e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226    3 MIDWFYGVLASLgLWQKEAKILFLGLDNAGKTTLLHMLKDERLVQHQPTQHPTSEELSIGKIKFKAFDLGGHQIARRVWK 82
Cdd:PTZ00133   1 MGLWLSSAFKSL-FGKKEVRILMVGLDAAGKTTILYKLKLGEVVTTIPTIGFNVETVEYKNLKFTMWDVGGQDKLRPLWR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226   83 DYYAKVDAVVYLVDAYDKERFAESKKELDALLSDESLASVPFLILGNKIDIPYAASEDELRYHLGLsnfttgkgkvnltd 162
Cdd:PTZ00133  80 HYYQNTNGLIFVVDSNDRERIGDAREELERMLSEDELRDAVLLVFANKQDLPNAMSTTEVTEKLGL-------------- 145

                        170       180       190
                 ....*....|....*....|....*....|...
gi 15235226  163 SNVRPLEVFM--CSIVRKMGYGEGFKWVSQYIK 193
Cdd:PTZ00133 146 HSVRQRNWYIqgCCATTAQGLYEGLDWLSANIK 178
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 20-151 1.22e-12

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: 62.77  E-value: 1.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226    20 EAKILFLGLDNAGKTTLLHMLK--DERLVQHQP--TQH--PTSEELSIGKIKFKAFDLGGHQIARRVWKDYYAKVDAVVY 93
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLgnKGSITEYYPgtTRNyvTTVIEEDGKTYKFNLLDTAGQEDYDAIRRLYYPQVERSLR 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15235226    94 LVD-AYDKERFAESKKELDALLSDESLASVPFLILGNKIDIPYAASEDELRYHLGLSNF 151
Cdd:TIGR00231  81 VFDiVILVLDVEEILEKQTKEIIHHADSGVPIILVGNKIDLKDADLKTHVASEFAKLNG 139
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
18-182 2.17e-08

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 51.52  E-value: 2.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  18 QKEAKILFLGLDNAGKTTLLHMLKDER--LVQHQPTQHPTSEELSI----GKIKFKAFDLGGHQI---ARRVWKDYYAKV 88
Cdd:COG1100   1 MGEKKIVVVGTGGVGKTSLVNRLVGDIfsLEKYLSTNGVTIDKKELkldgLDVDLVIWDTPGQDEfreTRQFYARQLTGA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  89 DAVVYLVDAyDKERFAESKKELDALLSDESLASvPFLILGNKIDIpyaASEDELRYHLGLSNFTtgkgkvnltdSNVRPL 168
Cdd:COG1100  81 SLYLFVVDG-TREETLQSLYELLESLRRLGKKS-PIILVLNKIDL---YDEEEIEDEERLKEAL----------SEDNIV 145

                       170
                ....*....|....
gi 15235226 169 EVFMCSIvrKMGYG 182
Cdd:COG1100 146 EVVATSA--KTGEG 157
 
Name Accession Description Interval E-value
Sar1 cd00879
Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII ...
 2-192 2.39e-133

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: 371.23  E-value: 2.39e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226   2 FMIDWFYGVLASLGLWQKEAKILFLGLDNAGKTTLLHMLKDERLVQHQPTQHPTSEELSIGKIKFKAFDLGGHQIARRVW 81
Cdd:cd00879   1 FIFDWFYNVLSSLGLYKKEAKIVFLGLDNAGKTTLLHMLKDDRLAQHVPTLHPTSEELTIGNVKFTTFDLGGHEQARRVW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  82 KDYYAKVDAVVYLVDAYDKERFAESKKELDALLSDESLASVPFLILGNKIDIPYAASEDELRYHLGLSNFTTGKGKVNLT 161
Cdd:cd00879  81 KDYFPEVDGIVFLVDAADPERFQESKEELDSLLNDEELANVPILILGNKIDKPGAVSEEELREALGLYGTTTGKGGVSLK 160

                       170       180       190
                ....*....|....*....|....*....|.
gi 15235226 162 DSNVRPLEVFMCSIVRKMGYGEGFKWVSQYI 192
Cdd:cd00879 161 VSNIRPVEVFMCSVVKRQGYGEGFRWLSQYL 191
SAR smart00178
Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene ...
 4-192 2.72e-130

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: 363.10  E-value: 2.72e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226      4 IDWFYGVLASLGLWQKEAKILFLGLDNAGKTTLLHMLKDERLVQHQPTQHPTSEELSIGKIKFKAFDLGGHQIARRVWKD 83
Cdd:smart00178   1 FDWFYDILASLGLWNKHAKILFLGLDNAGKTTLLHMLKNDRLAQHQPTQHPTSEELAIGNIKFTTFDLGGHQQARRLWKD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226     84 YYAKVDAVVYLVDAYDKERFAESKKELDALLSDESLASVPFLILGNKIDIPYAASEDELRYHLGLSNFTTGKGKVnltds 163
Cdd:smart00178  81 YFPEVNGIVYLVDAYDKERFAESKRELDALLSDEELATVPFLILGNKIDAPYAASEDELRYALGLTNTTTGKGKV----- 155

                          170       180
                   ....*....|....*....|....*....
gi 15235226    164 NVRPLEVFMCSIVRKMGYGEGFKWVSQYI 192
Cdd:smart00178 156 GVRPVEVFMCSVVRRMGYGEGFKWLSQYI 184
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
 21-192 1.09e-85

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


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 249.45  E-value: 1.09e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226    21 AKILFLGLDNAGKTTLLHMLKDERLVQHQPTQHPTSEELSIGKIKFKAFDLGGHQIARRVWKDYYAKVDAVVYLVDAYDK 100
Cdd:pfam00025   1 MRILILGLDNAGKTTILYKLKLGEIVTTIPTIGFNVETVTYKNVKFTVWDVGGQESLRPLWRNYFPNTDAVIFVVDSADR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226   101 ERFAESKKELDALLSDESLASVPFLILGNKIDIPYAASEDELRYHLGLSNFTTgkgkvnltdsnvRPLEVFMCSIVRKMG 180
Cdd:pfam00025  81 DRIEEAKEELHALLNEEELADAPLLILANKQDLPGAMSEAEIRELLGLHELKD------------RPWEIQGCSAVTGEG 148

                         170
                  ....*....|..
gi 15235226   181 YGEGFKWVSQYI 192
Cdd:pfam00025 149 LDEGLDWLSNYI 160
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
 22-190 7.86e-55

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: 171.22  E-value: 7.86e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  22 KILFLGLDNAGKTTLLHMLKDERLVQHQPTQHPTSEELSIGKIKFKAFDLGGHQIARRVWKDYYAKVDAVVYLVDAYDKE 101
Cdd:cd00878   1 RILMLGLDGAGKTTILYKLKLGEVVTTIPTIGFNVETVEYKNVKFTVWDVGGQDKIRPLWKHYYENTDGLIFVVDSSDRE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226 102 RFAESKKELDALLSDESLASVPFLILGNKIDIPYAASEDELRYHLGLSnfttgkgkvNLTDSNVRpleVFMCSIVRKMGY 181
Cdd:cd00878  81 RIEEAKNELHKLLNEEELKGAPLLILANKQDLPGALTESELIELLGLE---------SIKGRRWH---IQPCSAVTGDGL 148


                ....*....
gi 15235226 182 GEGFKWVSQ 190
Cdd:cd00878 149 DEGLDWLIE 157
Arl3 cd04155
Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most ...
 19-188 6.58e-42

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: 139.07  E-value: 6.58e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  19 KEAKILFLGLDNAGKTTLLHMLKDERLVQHQPTQHPTSEELSIGKIKFKAFDLGGHQIARRVWKDYYAKVDAVVYLVDAY 98
Cdd:cd04155  14 QEVRILLLGLDNAGKTTILKQLASEDISHITPTQGFNIKNVQADGFKLNVWDIGGQRKIRPYWRNYFENTDVLIYVIDSA 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  99 DKERFAESKKELDALLSDESLASVPFLILGNKIDIPYAASEDELryhlglsnfttgKGKVNLTDSNVRPLEVFMCSIVRK 178
Cdd:cd04155  94 DRKRFEEAGQELVELLEEEKLAGVPVLVFANKQDLLTAAPAEEV------------AEALNLHDIRDRSWHIQACSAKTG 161

                       170
                ....*....|
gi 15235226 179 MGYGEGFKWV 188
Cdd:cd04155 162 EGLQEGMNWV 171
Arl1 cd04151
ADP ribosylation factor 1 (Arf1); Arl1 subfamily. Arl1 (Arf-like 1) localizes to the Golgi ...
 22-189 1.92e-39

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: 132.15  E-value: 1.92e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  22 KILFLGLDNAGKTTLLHMLKDERLVQHQPTQHPTSEELSIGKIKFKAFDLGGHQIARRVWKDYYAKVDAVVYLVDAYDKE 101
Cdd:cd04151   1 RILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAIIYVVDSTDRD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226 102 RFAESKKELDALLSDESLASVPFLILGNKIDIPYAASEDELRYHLGLSNFTTgkgkvnltdsnvRPLEVFMCSIVRKMGY 181
Cdd:cd04151  81 RLGISKSELHAMLEEEELKDAVLLVFANKQDMPGALSEAEVAEKLGLSELKD------------RTWQIFKTSATKGEGL 148


                ....*...
gi 15235226 182 GEGFKWVS 189
Cdd:cd04151 149 DEGMDWLV 156
Arl5_Arl8 cd04153
Arf-like 5 (Arl5) and 8 (Arl8) GTPases; Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like ...
 15-190 1.01e-37

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: 128.24  E-value: 1.01e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  15 GLW-----QKEAKILFLGLDNAGKTTLLHMLKDERLVQHQPTQHPTSEELSIGKIKFKAFDLGGHQIARRVWKDYYAKVD 89
Cdd:cd04153   5 SLWslffpRKEYKVIIVGLDNAGKTTILYQFLLGEVVHTSPTIGSNVEEIVYKNIRFLMWDIGGQESLRSSWNTYYTNTD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  90 AVVYLVDAYDKERFAESKKELDALLSDESLASVPFLILGNKIDIPYAASEDELRYHLGLSNFTTgkgkvnltdsnvRPLE 169
Cdd:cd04153  85 AVILVIDSTDRERLPLTKEELYKMLAHEDLRKAVLLVLANKQDLKGAMTPAEISESLGLTSIRD------------HTWH 152

                       170       180
                ....*....|....*....|.
gi 15235226 170 VFMCSIVRKMGYGEGFKWVSQ 190
Cdd:cd04153 153 IQGCCALTGEGLPEGLDWIAS 173
Arl2 cd04154
Arf-like 2 (Arl2) GTPase; Arl2 (Arf-like 2) GTPases are members of the Arf family that bind ...
 7-190 1.50e-32

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: 114.73  E-value: 1.50e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226   7 FYGVLASLGLWQKEAKILFLGLDNAGKTTLLHMLKDERLVQHQPTQHPTSEELSIGKIKFKAFDLGGHQIARRVWKDYYA 86
Cdd:cd04154   1 LLTILRKTKQKEREMRILMLGLDNAGKTTILKKFNGEDISTISPTLGFNIKTLEYNGYKLNIWDVGGQKSLRSYWRNYFE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  87 KVDAVVYLVDAYDKERFAESKKELDALLSDESLASVPFLILGNKIDIPYAASEDELRYHLGLSNFTTgkgkvnltdsnvR 166
Cdd:cd04154  81 STDALIWVVDSSDRARLEDCKRELQKLLVEERLAGATLLIFANKQDLPGALSPEEIREVLELDSIKS------------H 148

                       170       180
                ....*....|....*....|....
gi 15235226 167 PLEVFMCSIVRKMGYGEGFKWVSQ 190
Cdd:cd04154 149 HWRIFGCSAVTGENLLDGIDWLVD 172
ARLTS1 cd04156
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ...
 22-191 4.60e-32

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: 113.28  E-value: 4.60e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  22 KILFLGLDNAGKTTLLHMLKDERLVQHQPTQHPTSEELSI-GKIKFKAFDLGGHQIARRVWKDYYAKVDAVVYLVDAYDK 100
Cdd:cd04156   1 QVLLLGLDSAGKSTLLYKLKHAELVTTIPTVGFNVEMLQLeKHLSLTVWDVGGQEKMRTVWKCYLENTDGLVYVVDSSDE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226 101 ERFAESKKELDALLSDESLASVPFLILGNKIDIPYAASEDELRYHLGLSNFTTGKgkvnltDSNVRPlevfmCSIVRKMG 180
Cdd:cd04156  81 ARLDESQKELKHILKNEHIKGVPVVLLANKQDLPGALTAEEITRRFKLKKYCSDR------DWYVQP-----CSAVTGEG 149

                       170
                ....*....|.
gi 15235226 181 YGEGFKWVSQY 191
Cdd:cd04156 150 LAEAFRKLASF 160
Arl6 cd04157
Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small ...
 23-190 6.22e-31

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: 110.60  E-value: 6.22e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  23 ILFLGLDNAGKTTLLHMLKDERLVQHQ--PTQHPTSEELSIGKIKFKAFDLGGHQIARRVWKDYYAKVDAVVYLVDAYDK 100
Cdd:cd04157   2 ILVLGLDNSGKTTIINQLKPSNAQSQNivPTVGFNVESFKKGNLSFTAFDMSGQGKYRGLWEHYYKNIQGIIFVIDSSDR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226 101 ERFAESKKELDALLS--DESLASVPFLILGNKIDIPYAASEDELRYHLGLSNFTTgkgkvnltdsnvRPLEVFMCSIVRK 178
Cdd:cd04157  82 LRMVVAKDELELLLNhpDIKHRRIPILFYANKMDLPDALTAVKITQLLCLENIKD------------KPWHIFASSALTG 149

                       170
                ....*....|..
gi 15235226 179 MGYGEGFKWVSQ 190
Cdd:cd04157 150 EGLDEGVDWLQA 161
Arfrp1 cd04160
Arf-related protein 1 (Arfrp1); Arfrp1 (Arf-related protein 1), formerly known as ARP, is a ...
 23-189 8.13e-31

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: 110.12  E-value: 8.13e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  23 ILFLGLDNAGKTTLLHMLKDERLVQHQ---PTQHPTSEELSIGKI-----KFKAFDLGGHQIARRVWKDYYAKVDAVVYL 94
Cdd:cd04160   2 VLILGLDNAGKTTFLEQTKTKFSKNYKglnPSKITPTVGLNIGTIevgkaRLMFWDLGGQEELRSLWDKYYAESHGVIYV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  95 VDAYDKERFAESKKELDALLSDESLASVPFLILGNKIDIPYAASEDELRyhlglSNFTTGKGKVNLTDSNVRPlevfmCS 174
Cdd:cd04160  82 IDSTDRERFNESKSAFEKVINNEALEGVPLLVLANKQDLPDALSVAEIK-----EVFDDCIALIGRRDCLVQP-----VS 151

                       170
                ....*....|....*
gi 15235226 175 IVRKMGYGEGFKWVS 189
Cdd:cd04160 152 ALEGEGVEEGIEWLV 166
PTZ00133 PTZ00133
ADP-ribosylation factor; Provisional
 3-193 4.40e-29

ADP-ribosylation factor; Provisional


Pssm-ID: 173423  Cd Length: 182  Bit Score: 106.47  E-value: 4.40e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226    3 MIDWFYGVLASLgLWQKEAKILFLGLDNAGKTTLLHMLKDERLVQHQPTQHPTSEELSIGKIKFKAFDLGGHQIARRVWK 82
Cdd:PTZ00133   1 MGLWLSSAFKSL-FGKKEVRILMVGLDAAGKTTILYKLKLGEVVTTIPTIGFNVETVEYKNLKFTMWDVGGQDKLRPLWR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226   83 DYYAKVDAVVYLVDAYDKERFAESKKELDALLSDESLASVPFLILGNKIDIPYAASEDELRYHLGLsnfttgkgkvnltd 162
Cdd:PTZ00133  80 HYYQNTNGLIFVVDSNDRERIGDAREELERMLSEDELRDAVLLVFANKQDLPNAMSTTEVTEKLGL-------------- 145

                        170       180       190
                 ....*....|....*....|....*....|...
gi 15235226  163 SNVRPLEVFM--CSIVRKMGYGEGFKWVSQYIK 193
Cdd:PTZ00133 146 HSVRQRNWYIqgCCATTAQGLYEGLDWLSANIK 178
Arf6 cd04149
ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins ...
 19-190 2.64e-28

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: 103.70  E-value: 2.64e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  19 KEAKILFLGLDNAGKTTLLHMLKDERLVQHQPTQHPTSEELSIGKIKFKAFDLGGHQIARRVWKDYYAKVDAVVYLVDAY 98
Cdd:cd04149   8 KEMRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVETVTYKNVKFNVWDVGGQDKIRPLWRHYYTGTQGLIFVVDSA 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  99 DKERFAESKKELDALLSDESLASVPFLILGNKIDIPYAASEDELRYHLGLSnfttgkgkvNLTDsnvRPLEVFMCSIVRK 178
Cdd:cd04149  88 DRDRIDEARQELHRIINDREMRDALLLVFANKQDLPDAMKPHEIQEKLGLT---------RIRD---RNWYVQPSCATSG 155

                       170
                ....*....|..
gi 15235226 179 MGYGEGFKWVSQ 190
Cdd:cd04149 156 DGLYEGLTWLSS 167
Arl10_like cd04159
Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from ...
 26-152 5.80e-28

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: 102.78  E-value: 5.80e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  26 LGLDNAGKTTLLHMLK-DERLVQHQPTQHPTSEELSIGKIKFKAFDLGGHQIARRVWKDYYAKVDAVVYLVDAYDKERFA 104
Cdd:cd04159   5 VGLQNSGKTTLVNVIAsGQFSEDTIPTVGFNMRKVTKGNVTIKVWDLGGQPRFRSMWERYCRGVNAIVYVVDAADREKLE 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15235226 105 ESKKELDALLSDESLASVPFLILGNKIDIPYAASEDELRYHLGLSNFT 152
Cdd:cd04159  85 VAKNELHDLLEKPSLEGIPLLVLGNKNDLPGALSVDELIEQMNLKSIT 132
PLN00223 PLN00223
ADP-ribosylation factor; Provisional
 18-192 6.65e-28

ADP-ribosylation factor; Provisional


Pssm-ID: 165788  Cd Length: 181  Bit Score: 103.12  E-value: 6.65e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226   18 QKEAKILFLGLDNAGKTTLLHMLKDERLVQHQPTQHPTSEELSIGKIKFKAFDLGGHQIARRVWKDYYAKVDAVVYLVDA 97
Cdd:PLN00223  15 KKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226   98 YDKERFAESKKELDALLSDESLASVPFLILGNKIDIPYAASEDELRYHLGLsnfttgkgkvnltdSNVRPLEVFMCSIVR 177
Cdd:PLN00223  95 NDRDRVVEARDELHRMLNEDELRDAVLLVFANKQDLPNAMNAAEITDKLGL--------------HSLRQRHWYIQSTCA 160

                        170
                 ....*....|....*..
gi 15235226  178 KMGYG--EGFKWVSQYI 192
Cdd:PLN00223 161 TSGEGlyEGLDWLSNNI 177
ARF smart00177
ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular ...
 18-193 1.11e-27

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: 102.31  E-value: 1.11e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226     18 QKEAKILFLGLDNAGKTTLLHMLKDERLVQHQPTQHPTSEELSIGKIKFKAFDLGGHQIARRVWKDYYAKVDAVVYLVDA 97
Cdd:smart00177  11 NKEMRILMVGLDAAGKTTILYKLKLGESVTTIPTIGFNVETVTYKNISFTVWDVGGQDKIRPLWRHYYTNTQGLIFVVDS 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226     98 YDKERFAESKKELDALLSDESLASVPFLILGNKIDIPYAASEDELRYHLGLsnfttgkgkvnltdSNVRPLEVFMCSIVR 177
Cdd:smart00177  91 NDRDRIDEAREELHRMLNEDELRDAVILVFANKQDLPDAMKAAEITEKLGL--------------HSIRDRNWYIQPTCA 156

                          170
                   ....*....|....*...
gi 15235226    178 KMGYG--EGFKWVSQYIK 193
Cdd:smart00177 157 TSGDGlyEGLTWLSNNLK 174
Arf1_5_like cd04150
ADP-ribosylation factor-1 (Arf1) and ADP-ribosylation factor-5 (Arf5); The Arf1-Arf5-like ...
 22-150 3.87e-25

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: 95.55  E-value: 3.87e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  22 KILFLGLDNAGKTTLLHMLKDERLVQHQPTQHPTSEELSIGKIKFKAFDLGGHQIARRVWKDYYAKVDAVVYLVDAYDKE 101
Cdd:cd04150   2 RILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRE 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15235226 102 RFAESKKELDALLSDESLASVPFLILGNKIDIPYAASEDELRYHLGLSN 150
Cdd:cd04150  82 RIGEAREELQRMLNEDELRDAVLLVFANKQDLPNAMSAAEVTDKLGLHS 130
Arl9_Arfrp2_like cd04162
Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first ...
 23-156 5.02e-25

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: 95.21  E-value: 5.02e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  23 ILFLGLDNAGKTTLLHMLKDER-LVQHQPTQHPTSEELSIGKIKFKAFDLGGHQIARRVWKDYYAKVDAVVYLVDAYDKE 101
Cdd:cd04162   2 ILVLGLDGAGKTSLLHSLSSERsLESVVPTTGFNSVAIPTQDAIMELLEIGGSQNLRKYWKRYLSGSQGLIFVVDSADSE 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15235226 102 RFAESKKELDALLSDESlaSVPFLILGNKIDIPYAASEDELRYHLGLSNFTTGKG 156
Cdd:cd04162  82 RLPLARQELHQLLQHPP--DLPLVVLANKQDLPAARSVQEIHKELELEPIARGRR 134
ARD1 cd04158
(ADP-ribosylation factor domain protein 1 (ARD1); ARD1 (ADP-ribosylation factor domain protein ...
 22-190 1.63e-22

(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: 88.93  E-value: 1.63e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  22 KILFLGLDNAGKTTLLHMLKDERLVQHQPTQHPTSEELSIGKIKFKAFDLGGHQIARRVWKDYYAKVDAVVYLVDAYDKE 101
Cdd:cd04158   1 RVVTLGLDGAGKTTILFKLKQDEFMQPIPTIGFNVETVEYKNLKFTIWDVGGKHKLRPLWKHYYLNTQAVVFVIDSSHRD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226 102 RFAESKKELDALLSDESLASVPFLILGNKIDIPYAASEDELRYHLGLSNFTTGkgkvnltdsnvRPLEVFMCSIVRKMGY 181
Cdd:cd04158  81 RVSEAHSELAKLLTEKELRDALLLIFANKQDVAGALSVEEMTELLSLHKLCCG-----------RSWYIQGCDARSGMGL 149


                ....*....
gi 15235226 182 GEGFKWVSQ 190
Cdd:cd04158 150 YEGLDWLSR 158
Arl4_Arl7 cd04152
Arf-like 4 (Arl4) and 7 (Arl7) GTPases; Arl4 (Arf-like 4) is highly expressed in testicular ...
 23-153 2.47e-22

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: 88.70  E-value: 2.47e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  23 ILFLGLDNAGKTTLLHMLKDERLVQHQPTQHPTSE--ELSIGK---IKFKAFDLGGHQIARRVWKDYYAKVDAVVYLVDA 97
Cdd:cd04152   6 IVMLGLDSAGKTTVLYRLKFNEFVNTVPTKGFNTEkiKVSLGNakgVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVVDS 85

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15235226  98 YDKERFAESKKELDALLSDESLASVPFLILGNKIDIPYAASEDELRYHLG---LSNFTT 153
Cdd:cd04152  86 VDVERMEEAKTELHKITKFSENQGVPVLVLANKQDLPNALPVSEVEKLLAlheLSSSTP 144
Arl2l1_Arl13_like cd04161
Arl2-like protein 1 (Arl2l1) and Arl13; Arl2l1 (Arl2-like protein 1) and Arl13 form a ...
 23-193 3.69e-22

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: 87.83  E-value: 3.69e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  23 ILFLGLDNAGKTTLLHMLKDERLVQHQPTQHPTSEELSIGKIKFKAFDLGGHQIARRVWKDYYAKVDAVVYLVDAYDKER 102
Cdd:cd04161   2 LLTVGLDNAGKTTLVSALQGEIPKKVAPTVGFTPTKLRLDKYEVCIFDLGGGANFRGIWVNYYAEAHGLVFVVDSSDDDR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226 103 FAESKKELDALLSDESLASVPFLILGNKIDIPYAASEDELRYHLGLSnfttgkgkvNLTDSNVRPLEVFMCSIVRKMGyg 182
Cdd:cd04161  82 VQEVKEILRELLQHPRVSGKPILVLANKQDKKNALLGADVIEYLSLE---------KLVNENKSLCHIEPCSAIEGLG-- 150

                       170
                ....*....|.
gi 15235226 183 egfKWVSQYIK 193
Cdd:cd04161 151 ---KKIDPSIV 158
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 24-190 1.11e-12

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: 62.86  E-value: 1.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  24 LFLGLDNAGKTTLLHMLKDERLVQ----HQPTQHPTSEELSI--GKIKFKAFDLGGHQIARRVW-----KDYYAKVDAVV 92
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVGEvsdvPGTTRDPDVYVKELdkGKVKLVLVDTPGLDEFGGLGreelaRLLLRGADLIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  93 YLVDAYDKERFAESKKELDALLSDEslaSVPFLILGNKIDIPYAASEDELRYHLGLSNFTtgkgkvnltdsnvrPLEVFM 172
Cdd:cd00882  81 LVVDSTDRESEEDAKLLILRRLRKE---GIPIILVGNKIDLLEEREVEELLRLEELAKIL--------------GVPVFE 143

                       170
                ....*....|....*...
gi 15235226 173 CSIVRKMGYGEGFKWVSQ 190
Cdd:cd00882 144 VSAKTGEGVDELFEKLIE 161
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 20-151 1.22e-12

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: 62.77  E-value: 1.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226    20 EAKILFLGLDNAGKTTLLHMLK--DERLVQHQP--TQH--PTSEELSIGKIKFKAFDLGGHQIARRVWKDYYAKVDAVVY 93
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLgnKGSITEYYPgtTRNyvTTVIEEDGKTYKFNLLDTAGQEDYDAIRRLYYPQVERSLR 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15235226    94 LVD-AYDKERFAESKKELDALLSDESLASVPFLILGNKIDIPYAASEDELRYHLGLSNF 151
Cdd:TIGR00231  81 VFDiVILVLDVEEILEKQTKEIIHHADSGVPIILVGNKIDLKDADLKTHVASEFAKLNG 139
G-alpha pfam00503
G-protein alpha subunit; G proteins couple receptors of extracellular signals to intracellular ...
 49-133 5.22e-10

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: 57.21  E-value: 5.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226    49 QPTQHPTSEELSIGKIKFKAFDLGGHQIARRVWKDYYAKVDAVVYLV--DAYDK---E-----RFAESKKELDALLSDES 118
Cdd:pfam00503 152 VKTTGIIETKFEFKGLKFRLFDVGGQRSERKKWIHCFEDVTAIIFVVslSEYDQvlyEddstnRMEESLKLFEEICNSPW 231

                          90
                  ....*....|....*
gi 15235226   119 LASVPFLILGNKIDI 133
Cdd:pfam00503 232 FKNTPIILFLNKKDL 246
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
18-182 2.17e-08

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 51.52  E-value: 2.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  18 QKEAKILFLGLDNAGKTTLLHMLKDER--LVQHQPTQHPTSEELSI----GKIKFKAFDLGGHQI---ARRVWKDYYAKV 88
Cdd:COG1100   1 MGEKKIVVVGTGGVGKTSLVNRLVGDIfsLEKYLSTNGVTIDKKELkldgLDVDLVIWDTPGQDEfreTRQFYARQLTGA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  89 DAVVYLVDAyDKERFAESKKELDALLSDESLASvPFLILGNKIDIpyaASEDELRYHLGLSNFTtgkgkvnltdSNVRPL 168
Cdd:COG1100  81 SLYLFVVDG-TREETLQSLYELLESLRRLGKKS-PIILVLNKIDL---YDEEEIEDEERLKEAL----------SEDNIV 145

                       170
                ....*....|....
gi 15235226 169 EVFMCSIvrKMGYG 182
Cdd:COG1100 146 EVVATSA--KTGEG 157
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
 23-133 2.41e-08

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: 51.55  E-value: 2.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  23 ILFLGLDNAGKTTLLHMLKDERLVQHQPTQHP---TSEELSIGKIKFKAFDLGGHQIAR-RVWKDYYAKVDAVVYLVDAY 98
Cdd:cd04105   3 VLLLGPSDSGKTALFTKLTTGKVRSTVTSIEPnvaSFYSNSSKGKKLTLVDVPGHEKLRdKLLEYLKASLKAIVFVVDSA 82

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15235226  99 DKERFAESKKE-LDALLSDESL--ASVPFLILGNKIDI 133
Cdd:cd04105  83 TFQKNIRDVAEfLYDILTDLEKikNKIPILIACNKQDL 120
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 22-130 1.88e-07

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: 47.61  E-value: 1.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226    22 KILFLGLDNAGKTTLLHMLKDER-LVQHQP--TQHPTSEELSIGKIKFKAFDLGG-------HQIARRVWKDyYAKVDAV 91
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKaIVSDYPgtTRDPNEGRLELKGKQIILVDTPGliegaseGEGLGRAFLA-IIEADLI 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 15235226    92 VYLVDAydKERFAESKKELDALLSDeslASVPFLILGNK 130
Cdd:pfam01926  80 LFVVDS--EEGITPLDEELLELLRE---NKKPIILVLNK 113
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 25-144 4.49e-06

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: 44.93  E-value: 4.49e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  25 FLGLDNAGKTTLLHML--KDERLVQHQP--TQHPTSEEL-SIGKIKFKAFDLGG-----HQIARRVWKDY--YAKVDAVV 92
Cdd:cd00880   2 IFGRPNVGKSSLLNALlgQNVGIVSPIPgtTRDPVRKEWeLLPLGPVVLIDTPGldeegGLGRERVEEARqvADRADLVL 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15235226  93 YLVDAydkerfAESKKELDALLSDESLASVPFLILGNKIDIpYAASEDELRY 144
Cdd:cd00880  82 LVVDS------DLTPVEEEAKLGLLRERGKPVLLVLNKIDL-VPESEEEELL 126
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
 22-132 2.15e-05

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: 42.11  E-value: 2.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226    22 KILFLGLDNAGKTTLLHmlkdeRLVQHQ--PTQHPT-----------SEELSIGKIKFKAFDLGGHQIARRVWKDYYAkv 88
Cdd:pfam08477   1 KVVLLGDSGVGKTSLLK-----RFVDDTfdPKYKSTigvdfktktvlENDDNGKKIKLNIWDTAGQERFRSLHPFYYR-- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 15235226    89 DAVVYLVDaYDKERFAESKKELDALlsDESLASVPFLILGNKID 132
Cdd:pfam08477  74 GAAAALLV-YDSRTFSNLKYWLREL--KKYAGNSPVILVGNKID 114
RJL cd04119
Rab GTPase family J-like (RabJ-like); RJLs are found in many protists and as chimeras with ...
 63-143 3.65e-05

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: 42.34  E-value: 3.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  63 KIKFKAFDLGGHQIARRVWKDYYAKVDAVVYLVDAYDKERF-------AESKKEldaLLSDESLASVPFLILGNKIDIPY 135
Cdd:cd04119  48 EVRVNFFDLSGHPEYLEVRNEFYKDTQGVLLVYDVTDRQSFealdswlKEMKQE---GGPHGNMENIVVVVCANKIDLTK 124

                        90
                ....*....|
gi 15235226 136 --AASEDELR 143
Cdd:cd04119 125 hrAVSEDEGR 134
SRPRB pfam09439
Signal recognition particle receptor beta subunit; The beta subunit of the signal recognition ...
 23-187 4.05e-05

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


Pssm-ID: 462797 [Multi-domain]  Cd Length: 181  Bit Score: 42.43  E-value: 4.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226    23 ILFLGLDNAGKTTLLHMLKDERLVQHQPTQHPTSEE--LSIGKIKFKAFDLGGHQIARRVWKDYY---AKVDAVVYLVD- 96
Cdd:pfam09439   6 VIIAGLCDSGKTSLFTLLTTDSVRPTVTSQEPSAAYryMLNKGNSFTLIDFPGHVKLRYKLLETLkdsSSLKGIVFVVDs 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226    97 AYDKERFAESKKELDALLSDESLA--SVPFLILGNKIDIPYAASE----DELRYHLGLSNFTTGKGkVNLTDSNVRPLEV 170
Cdd:pfam09439  86 TIFPKEVTDTAEFLYDILSITELLknGIDILIACNKQESFTARPPkkikQALEKEINTIRERRSKA-LSGLDGSEDLSAV 164

                         170
                  ....*....|....*..
gi 15235226   171 FMCSivrkmgyGEGFKW 187
Cdd:pfam09439 165 LGKK-------GKGFKF 174
RocCOR cd09914
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ...
 20-132 7.87e-05

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


Pssm-ID: 206741 [Multi-domain]  Cd Length: 161  Bit Score: 41.17  E-value: 7.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  20 EAKILFLGLDNAGKTTLLHMLKDERLVQHQPTQH--------PTSEELSigKIKFKAFDLGGHQIarrvwkdYYAK---- 87
Cdd:cd09914   1 EAKLMLVGQGGVGKTSLCKQLIGEKFDGDESSTHginvqdwkIPAPERK--KIRLNVWDFGGQEI-------YHAThqff 71

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15235226  88 -VDAVVYLVdAYDKERFAESKKELDALLSDESLASVPFLIL-GNKID 132
Cdd:cd09914  72 lTSRSLYLL-VFDLRTGDEVSRVPYWLRQIKAFGGVSPVILvGTHID 117
RalA_RalB cd04139
Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily ...
 22-133 3.30e-04

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


Pssm-ID: 206710 [Multi-domain]  Cd Length: 163  Bit Score: 39.33  E-value: 3.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  22 KILFLGLDNAGKTTL-LHMLKDERLVQHQPTQHPTSEELSI---GKIKFKAFDLGGHQIARRVWKDYYAKVDAVVYLVDA 97
Cdd:cd04139   2 KVIMVGSGGVGKSALtLQFMYDEFVEDYEPTKADSYRKKVVldgEEVQLNILDTAGQEDYAAIRDNYFRSGEGFLLVFSI 81

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15235226  98 YDKERFAESKKELDALLSDESLASVPFLILGNKIDI 133
Cdd:cd04139  82 TDMESFTALAEFREQILRVKEDDNVPLLLVGNKCDL 117
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 30-140 3.21e-03

tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440253 [Multi-domain]  Cd Length: 448  Bit Score: 37.35  E-value: 3.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  30 NAGKTTLL-HMLKDER-LVQHQP-TqhpT----SEELSIGKIKFKAFD-------------LGghqIARRvwKDYYAKVD 89
Cdd:COG0486 223 NVGKSSLLnALLGEERaIVTDIAgT---TrdviEERINIGGIPVRLIDtaglretedevekIG---IERA--REAIEEAD 294

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15235226  90 AVVYLVDAYDkerfaESKKELDALLsdESLASVPFLILGNKIDIPYAASED 140
Cdd:COG0486 295 LVLLLLDASE-----PLTEEDEEIL--EKLKDKPVIVVLNKIDLPSEADGE 338
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 22-149 3.47e-03

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


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 36.32  E-value: 3.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235226  22 KILFLGLDNAGKTTLL-HMLKDER-LVQHQP-TqhpT----SEELSIGKIKFKAFDLGG--------HQIA-RRVWKdYY 85
Cdd:cd04164   5 KVVIAGKPNVGKSSLLnALAGRDRaIVSDIAgT---TrdviEEEIDLGGIPVRLIDTAGlretedeiEKIGiERARE-AI 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15235226  86 AKVDAVVYLVDAydkerfAESKKELDALLsDESLASVPFLILGNKIDI---PYAASEDELRYHLGLS 149
Cdd:cd04164  81 EEADLVLLVVDA------SEGLDEEDLEI-LELPAKKPVIVVLNKSDLlsdAEGISELNGKPIIAIS 140
 
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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