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Conserved domains on  [gi|17561830|ref|NP_505157|]
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Guanine nucleotide-binding protein alpha-2 subunit [Caenorhabditis elegans]

Protein Classification

guanine nucleotide-binding protein subunit alpha( domain architecture ID 12199492)

guanine nucleotide-binding protein subunit alpha contains the guanine nucleotide binding site of heterotrimeric G protein, which functions as a modulator or transducer in various transmembrane signaling systems

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
G_alpha smart00275
G protein alpha subunit; Subunit of G proteins that contains the guanine nucleotide binding ...
13-354 6.78e-168

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: 471.68  E-value: 6.78e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830     13 TLKSRAIDKEIKQLQTSEERTVKLLLLGAGECGKSTVLKQMRLLTSKQYTDEELLTQAKLVYTNIVIEMDHLVKAMPAAG 92
Cdd:smart00275   1 IRRNKEIEKQLEEERKKKKREVKLLLLGAGESGKSTILKQMRILHGDGFSQEERREYRPLIYSNILESMKALVDAMEELN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830     93 LNFSDPMREHDVHMLTLYIK--DMQHKNFQQDAADHVEKLWKDPVVKRLYAERKELNIrdiGDNTEYFFENLPRISKEDY 170
Cdd:smart00275  81 IPFEDPESILDIRIITEQFNktDETENVLPKEIAKAIKALWKDEGIQECYRRRNEFQL---NDSASYFLDNIDRIGDPDY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830    171 HPNATDTLLLRTKTTGIVEVGFEIKKVKFRVFDVGGQRSERKKWIHCFEDVNAIIFIAALSEYNEVLFEDETTNRMIESM 250
Cdd:smart00275 158 VPTEQDILRSRVPTTGIQETAFIVKKLFFRMFDVGGQRSERKKWIHCFDNVTAIIFCVALSEYDQVLEEDESTNRMQESL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830    251 RLFESICNSRWFHNTNIILFLNKKDLFEEKIKKENIHKAFPEYRGEQNYAETVAFIKTKFEALSNN-PKKTFYVHETCAT 329
Cdd:smart00275 238 NLFESICNSRWFANTSIILFLNKIDLFEEKIKKVPLVDYFPDYKGPNDYEAAAKFIKQKFLRLNRNsSRKSIYHHFTCAT 317
                          330       340
                   ....*....|....*....|....*
gi 17561830    330 DTNQVQKILDSVISMIIQSNLHKSG 354
Cdd:smart00275 318 DTRNIRVVFDAVKDIILQRNLKDAG 342
 
Name Accession Description Interval E-value
G_alpha smart00275
G protein alpha subunit; Subunit of G proteins that contains the guanine nucleotide binding ...
13-354 6.78e-168

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: 471.68  E-value: 6.78e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830     13 TLKSRAIDKEIKQLQTSEERTVKLLLLGAGECGKSTVLKQMRLLTSKQYTDEELLTQAKLVYTNIVIEMDHLVKAMPAAG 92
Cdd:smart00275   1 IRRNKEIEKQLEEERKKKKREVKLLLLGAGESGKSTILKQMRILHGDGFSQEERREYRPLIYSNILESMKALVDAMEELN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830     93 LNFSDPMREHDVHMLTLYIK--DMQHKNFQQDAADHVEKLWKDPVVKRLYAERKELNIrdiGDNTEYFFENLPRISKEDY 170
Cdd:smart00275  81 IPFEDPESILDIRIITEQFNktDETENVLPKEIAKAIKALWKDEGIQECYRRRNEFQL---NDSASYFLDNIDRIGDPDY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830    171 HPNATDTLLLRTKTTGIVEVGFEIKKVKFRVFDVGGQRSERKKWIHCFEDVNAIIFIAALSEYNEVLFEDETTNRMIESM 250
Cdd:smart00275 158 VPTEQDILRSRVPTTGIQETAFIVKKLFFRMFDVGGQRSERKKWIHCFDNVTAIIFCVALSEYDQVLEEDESTNRMQESL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830    251 RLFESICNSRWFHNTNIILFLNKKDLFEEKIKKENIHKAFPEYRGEQNYAETVAFIKTKFEALSNN-PKKTFYVHETCAT 329
Cdd:smart00275 238 NLFESICNSRWFANTSIILFLNKIDLFEEKIKKVPLVDYFPDYKGPNDYEAAAKFIKQKFLRLNRNsSRKSIYHHFTCAT 317
                          330       340
                   ....*....|....*....|....*
gi 17561830    330 DTNQVQKILDSVISMIIQSNLHKSG 354
Cdd:smart00275 318 DTRNIRVVFDAVKDIILQRNLKDAG 342
G-alpha cd00066
Alpha subunit of G proteins (guanine nucleotide binding); The alpha subunit of G proteins ...
34-350 3.25e-158

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: 445.82  E-value: 3.25e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830  34 VKLLLLGAGECGKSTVLKQMRLLTSKQYTDEELLTQAKLVYTNIVIEMDHLVKAMPAAGLNFSDPMREHDVHMLTLYIKD 113
Cdd:cd00066   1 VKLLLLGAGESGKSTILKQMKILHGNGFSDEERREFRPVIYSNILQSMKALLRAMETLNIPYGDPENEKDAKKILSLAPR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830 114 MQHKNFQQDAADHVEKLWKDPVVKRLYAERKELNIrdiGDNTEYFFENLPRISKEDYHPNATDTLLLRTKTTGIVEVGFE 193
Cdd:cd00066  81 AEEGPLPPELAEAIKRLWKDPGIQACYDRRNEYQL---NDSAKYFLDNLDRISDPDYIPTEQDILRSRVKTTGIIETDFS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830 194 IKKVKFRVFDVGGQRSERKKWIHCFEDVNAIIFIAALSEYNEVLFEDETTNRMIESMRLFESICNSRWFHNTNIILFLNK 273
Cdd:cd00066 158 IKNLKFRMFDVGGQRSERKKWIHCFEDVTAIIFVVALSEYDQVLVEDESVNRMQESLKLFDSICNSRWFANTSIILFLNK 237
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17561830 274 KDLFEEKIKKENIHKAFPEYRGEQN-YAETVAFIKTKFEALSNNPKKTFYVHETCATDTNQVQKILDSVISMIIQSNL 350
Cdd:cd00066 238 KDLFEEKIKKSPLTDYFPDYTGPPNdYEEAAKYIKKKFLDLNRNPNKEIYPHFTCATDTENIRFVFDAVKDIILQNNL 315
G-alpha pfam00503
G-protein alpha subunit; G proteins couple receptors of extracellular signals to intracellular ...
31-345 4.44e-138

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: 395.03  E-value: 4.44e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830    31 ERTVKLLLLGAGECGKSTVLKQMRLLTSKQYTDEELLTQAKLVYTNIVIEMDHLVKAMPAAGLNFSDPMREHDVHMLTLY 110
Cdd:pfam00503   3 KKEVKLLLLGAGESGKSTILKQMKIIHGGGFSEEERKQYRPVIYSNILRSLKTLIEAMERLGIELSNPENKERLDDLLSL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830   111 IKDMQH-KNFQQDAADHVEKLWKDPVVKRLYAERKELNIrdiGDNTEYFFENLPRISKEDYHPNATDTLLLRTKTTGIVE 189
Cdd:pfam00503  83 DSSLKNeTEFTPELAEDIKRLWNDPGIQECYERRNEFQL---PDSAEYFLDNLDRIASPDYVPTDQDILRARVKTTGIIE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830   190 VGFEIKKVKFRVFDVGGQRSERKKWIHCFEDVNAIIFIAALSEYNEVLFEDETTNRMIESMRLFESICNSRWFHNTNIIL 269
Cdd:pfam00503 160 TKFEFKGLKFRLFDVGGQRSERKKWIHCFEDVTAIIFVVSLSEYDQVLYEDDSTNRMEESLKLFEEICNSPWFKNTPIIL 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17561830   270 FLNKKDLFEEKIKKENIHKAFPEYRGEQN-YAETVAFIKTKFEALSNNPKKTFYVHETCATDTNQVQKILDSVISMI 345
Cdd:pfam00503 240 FLNKKDLFEEKLKKSPLSDYFPDYTGNPNdYEEALKYIRNKFLDLNKNPNRKIYTHFTCATDTENIRFVFDAVKDII 316
PLN00223 PLN00223
ADP-ribosylation factor; Provisional
177-349 7.29e-08

ADP-ribosylation factor; Provisional


Pssm-ID: 165788  Cd Length: 181  Bit Score: 51.89  E-value: 7.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830  177 TLLLRTK----TTGIVEVGF-----EIKKVKFRVFDVGGQRSERKKWIHCFEDVNAIIFIAALSEYNEVLFEDETTNRMI 247
Cdd:PLN00223  32 TILYKLKlgeiVTTIPTIGFnvetvEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRDRVVEARDELHRML 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830  248 ESMRLFESIcnsrwfhntnIILFLNKKDLfeekikkenihkafPEyrgeqnyAETVAFIKTKFeALSNNPKKTFYVHETC 327
Cdd:PLN00223 112 NEDELRDAV----------LLVFANKQDL--------------PN-------AMNAAEITDKL-GLHSLRQRHWYIQSTC 159
                        170       180
                 ....*....|....*....|..
gi 17561830  328 ATDTNQVQKILDSVISMIIQSN 349
Cdd:PLN00223 160 ATSGEGLYEGLDWLSNNIANKA 181
 
Name Accession Description Interval E-value
G_alpha smart00275
G protein alpha subunit; Subunit of G proteins that contains the guanine nucleotide binding ...
13-354 6.78e-168

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: 471.68  E-value: 6.78e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830     13 TLKSRAIDKEIKQLQTSEERTVKLLLLGAGECGKSTVLKQMRLLTSKQYTDEELLTQAKLVYTNIVIEMDHLVKAMPAAG 92
Cdd:smart00275   1 IRRNKEIEKQLEEERKKKKREVKLLLLGAGESGKSTILKQMRILHGDGFSQEERREYRPLIYSNILESMKALVDAMEELN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830     93 LNFSDPMREHDVHMLTLYIK--DMQHKNFQQDAADHVEKLWKDPVVKRLYAERKELNIrdiGDNTEYFFENLPRISKEDY 170
Cdd:smart00275  81 IPFEDPESILDIRIITEQFNktDETENVLPKEIAKAIKALWKDEGIQECYRRRNEFQL---NDSASYFLDNIDRIGDPDY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830    171 HPNATDTLLLRTKTTGIVEVGFEIKKVKFRVFDVGGQRSERKKWIHCFEDVNAIIFIAALSEYNEVLFEDETTNRMIESM 250
Cdd:smart00275 158 VPTEQDILRSRVPTTGIQETAFIVKKLFFRMFDVGGQRSERKKWIHCFDNVTAIIFCVALSEYDQVLEEDESTNRMQESL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830    251 RLFESICNSRWFHNTNIILFLNKKDLFEEKIKKENIHKAFPEYRGEQNYAETVAFIKTKFEALSNN-PKKTFYVHETCAT 329
Cdd:smart00275 238 NLFESICNSRWFANTSIILFLNKIDLFEEKIKKVPLVDYFPDYKGPNDYEAAAKFIKQKFLRLNRNsSRKSIYHHFTCAT 317
                          330       340
                   ....*....|....*....|....*
gi 17561830    330 DTNQVQKILDSVISMIIQSNLHKSG 354
Cdd:smart00275 318 DTRNIRVVFDAVKDIILQRNLKDAG 342
G-alpha cd00066
Alpha subunit of G proteins (guanine nucleotide binding); The alpha subunit of G proteins ...
34-350 3.25e-158

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: 445.82  E-value: 3.25e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830  34 VKLLLLGAGECGKSTVLKQMRLLTSKQYTDEELLTQAKLVYTNIVIEMDHLVKAMPAAGLNFSDPMREHDVHMLTLYIKD 113
Cdd:cd00066   1 VKLLLLGAGESGKSTILKQMKILHGNGFSDEERREFRPVIYSNILQSMKALLRAMETLNIPYGDPENEKDAKKILSLAPR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830 114 MQHKNFQQDAADHVEKLWKDPVVKRLYAERKELNIrdiGDNTEYFFENLPRISKEDYHPNATDTLLLRTKTTGIVEVGFE 193
Cdd:cd00066  81 AEEGPLPPELAEAIKRLWKDPGIQACYDRRNEYQL---NDSAKYFLDNLDRISDPDYIPTEQDILRSRVKTTGIIETDFS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830 194 IKKVKFRVFDVGGQRSERKKWIHCFEDVNAIIFIAALSEYNEVLFEDETTNRMIESMRLFESICNSRWFHNTNIILFLNK 273
Cdd:cd00066 158 IKNLKFRMFDVGGQRSERKKWIHCFEDVTAIIFVVALSEYDQVLVEDESVNRMQESLKLFDSICNSRWFANTSIILFLNK 237
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17561830 274 KDLFEEKIKKENIHKAFPEYRGEQN-YAETVAFIKTKFEALSNNPKKTFYVHETCATDTNQVQKILDSVISMIIQSNL 350
Cdd:cd00066 238 KDLFEEKIKKSPLTDYFPDYTGPPNdYEEAAKYIKKKFLDLNRNPNKEIYPHFTCATDTENIRFVFDAVKDIILQNNL 315
G-alpha pfam00503
G-protein alpha subunit; G proteins couple receptors of extracellular signals to intracellular ...
31-345 4.44e-138

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: 395.03  E-value: 4.44e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830    31 ERTVKLLLLGAGECGKSTVLKQMRLLTSKQYTDEELLTQAKLVYTNIVIEMDHLVKAMPAAGLNFSDPMREHDVHMLTLY 110
Cdd:pfam00503   3 KKEVKLLLLGAGESGKSTILKQMKIIHGGGFSEEERKQYRPVIYSNILRSLKTLIEAMERLGIELSNPENKERLDDLLSL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830   111 IKDMQH-KNFQQDAADHVEKLWKDPVVKRLYAERKELNIrdiGDNTEYFFENLPRISKEDYHPNATDTLLLRTKTTGIVE 189
Cdd:pfam00503  83 DSSLKNeTEFTPELAEDIKRLWNDPGIQECYERRNEFQL---PDSAEYFLDNLDRIASPDYVPTDQDILRARVKTTGIIE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830   190 VGFEIKKVKFRVFDVGGQRSERKKWIHCFEDVNAIIFIAALSEYNEVLFEDETTNRMIESMRLFESICNSRWFHNTNIIL 269
Cdd:pfam00503 160 TKFEFKGLKFRLFDVGGQRSERKKWIHCFEDVTAIIFVVSLSEYDQVLYEDDSTNRMEESLKLFEEICNSPWFKNTPIIL 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17561830   270 FLNKKDLFEEKIKKENIHKAFPEYRGEQN-YAETVAFIKTKFEALSNNPKKTFYVHETCATDTNQVQKILDSVISMI 345
Cdd:pfam00503 240 FLNKKDLFEEKLKKSPLSDYFPDYTGNPNdYEEALKYIRNKFLDLNKNPNRKIYTHFTCATDTENIRFVFDAVKDII 316
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
177-344 2.79e-10

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: 58.36  E-value: 2.79e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830 177 TLLLRTKTTGIVE----VGF-----EIKKVKFRVFDVGGQRSERKKWIHCFEDVNAIIFI--AALSEynevlfedettnR 245
Cdd:cd00878  14 TILYKLKLGEVVTtiptIGFnvetvEYKNVKFTVWDVGGQDKIRPLWKHYYENTDGLIFVvdSSDRE------------R 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830 246 MIESMRLFESICNSRWFHNTNIILFLNKKDLfeekikkenihkafPEYRGEQNyaetvafIKTKFEaLSNNPKKTFYVHE 325
Cdd:cd00878  82 IEEAKNELHKLLNEEELKGAPLLILANKQDL--------------PGALTESE-------LIELLG-LESIKGRRWHIQP 139
                       170
                ....*....|....*....
gi 17561830 326 TCATDTNQVQKILDSVISM 344
Cdd:cd00878 140 CSAVTGDGLDEGLDWLIEQ 158
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
177-276 1.09e-09

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


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 56.46  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830   177 TLLLRTKTTGIVE----VGF-----EIKKVKFRVFDVGGQRSERKKWIHCFEDVNAIIFIAALSEynevlfedetTNRMI 247
Cdd:pfam00025  15 TILYKLKLGEIVTtiptIGFnvetvTYKNVKFTVWDVGGQESLRPLWRNYFPNTDAVIFVVDSAD----------RDRIE 84
                          90       100
                  ....*....|....*....|....*....
gi 17561830   248 ESMRLFESICNSRWFHNTNIILFLNKKDL 276
Cdd:pfam00025  85 EAKEELHALLNEEELADAPLLILANKQDL 113
Arf6 cd04149
ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins ...
178-330 5.30e-09

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: 54.78  E-value: 5.30e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830 178 LLLRTKTTGIVEVGFEI-----KKVKFRVFDVGGQRSERKKWIHCFEDVNAIIFIAALSEYnevlfedettNRMIESMRL 252
Cdd:cd04149  29 LKLGQSVTTIPTVGFNVetvtyKNVKFNVWDVGGQDKIRPLWRHYYTGTQGLIFVVDSADR----------DRIDEARQE 98
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17561830 253 FESICNSRWFHNTNIILFLNKKDLFEEKIKKEnihkafpeyrgeqnyaetvafIKTKFEaLSNNPKKTFYVHETCATD 330
Cdd:cd04149  99 LHRIINDREMRDALLLVFANKQDLPDAMKPHE---------------------IQEKLG-LTRIRDRNWYVQPSCATS 154
ARF smart00177
ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular ...
177-329 4.57e-08

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: 52.23  E-value: 4.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830    177 TLLLRTK----TTGIVEVGFEI-----KKVKFRVFDVGGQRSERKKWIHCFEDVNAIIFIAALSEYNEVLFEDETTNRMI 247
Cdd:smart00177  28 TILYKLKlgesVTTIPTIGFNVetvtyKNISFTVWDVGGQDKIRPLWRHYYTNTQGLIFVVDSNDRDRIDEAREELHRML 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830    248 esmrlfesicNSRWFHNTNIILFLNKKDLfeekikkenihkafPEyrgeqnyAETVAFIKTKFeALSNNPKKTFYVHETC 327
Cdd:smart00177 108 ----------NEDELRDAVILVFANKQDL--------------PD-------AMKAAEITEKL-GLHSIRDRNWYIQPTC 155

                   ..
gi 17561830    328 AT 329
Cdd:smart00177 156 AT 157
PLN00223 PLN00223
ADP-ribosylation factor; Provisional
177-349 7.29e-08

ADP-ribosylation factor; Provisional


Pssm-ID: 165788  Cd Length: 181  Bit Score: 51.89  E-value: 7.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830  177 TLLLRTK----TTGIVEVGF-----EIKKVKFRVFDVGGQRSERKKWIHCFEDVNAIIFIAALSEYNEVLFEDETTNRMI 247
Cdd:PLN00223  32 TILYKLKlgeiVTTIPTIGFnvetvEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRDRVVEARDELHRML 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830  248 ESMRLFESIcnsrwfhntnIILFLNKKDLfeekikkenihkafPEyrgeqnyAETVAFIKTKFeALSNNPKKTFYVHETC 327
Cdd:PLN00223 112 NEDELRDAV----------LLVFANKQDL--------------PN-------AMNAAEITDKL-GLHSLRQRHWYIQSTC 159
                        170       180
                 ....*....|....*....|..
gi 17561830  328 ATDTNQVQKILDSVISMIIQSN 349
Cdd:PLN00223 160 ATSGEGLYEGLDWLSNNIANKA 181
ARLTS1 cd04156
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ...
177-276 1.40e-07

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: 50.49  E-value: 1.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830 177 TLLLRTKTTGIVE----VGFEI------KKVKFRVFDVGGQRSERKKWIHCFEDVNAIIFIAALSEYnevlfedettNRM 246
Cdd:cd04156  14 TLLYKLKHAELVTtiptVGFNVemlqleKHLSLTVWDVGGQEKMRTVWKCYLENTDGLVYVVDSSDE----------ARL 83
                        90       100       110
                ....*....|....*....|....*....|
gi 17561830 247 IESMRLFESICNSRWFHNTNIILFLNKKDL 276
Cdd:cd04156  84 DESQKELKHILKNEHIKGVPVVLLANKQDL 113
Sar1 cd00879
Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII ...
192-299 5.05e-07

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: 49.58  E-value: 5.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830 192 FEIKKVKFRVFDVGGQRSERKKWIHCFEDVNAIIFIAALSEYnevlfedettNRMIESMRLFESICNSRWFHNTNIILFL 271
Cdd:cd00879  58 LTIGNVKFTTFDLGGHEQARRVWKDYFPEVDGIVFLVDAADP----------ERFQESKEELDSLLNDEELANVPILILG 127
                        90       100
                ....*....|....*....|....*...
gi 17561830 272 NKKDLfEEKIKKENIHKAFPEYRGEQNY 299
Cdd:cd00879 128 NKIDK-PGAVSEEELREALGLYGTTTGK 154
Arl3 cd04155
Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most ...
191-276 8.89e-07

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: 48.55  E-value: 8.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830 191 GFEIKKV-----KFRVFDVGGQRSERKKWIHCFEDVNAIIFIAalseynevlfeDETTNRMIESMRL-FESICNSRWFHN 264
Cdd:cd04155  48 GFNIKNVqadgfKLNVWDIGGQRKIRPYWRNYFENTDVLIYVI-----------DSADRKRFEEAGQeLVELLEEEKLAG 116
                        90
                ....*....|..
gi 17561830 265 TNIILFLNKKDL 276
Cdd:cd04155 117 VPVLVFANKQDL 128
PTZ00133 PTZ00133
ADP-ribosylation factor; Provisional
177-276 5.30e-06

ADP-ribosylation factor; Provisional


Pssm-ID: 173423  Cd Length: 182  Bit Score: 46.38  E-value: 5.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830  177 TLLLRTK----TTGIVEVGF-----EIKKVKFRVFDVGGQRSERKKWIHCFEDVNAIIFIAALSEYNEVLFEDETTNRMI 247
Cdd:PTZ00133  32 TILYKLKlgevVTTIPTIGFnvetvEYKNLKFTMWDVGGQDKLRPLWRHYYQNTNGLIFVVDSNDRERIGDAREELERML 111
                         90       100
                 ....*....|....*....|....*....
gi 17561830  248 ESMRLfesicnsrwfHNTNIILFLNKKDL 276
Cdd:PTZ00133 112 SEDEL----------RDAVLLVFANKQDL 130
Arf1_5_like cd04150
ADP-ribosylation factor-1 (Arf1) and ADP-ribosylation factor-5 (Arf5); The Arf1-Arf5-like ...
185-329 8.06e-06

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: 45.48  E-value: 8.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830 185 TGIVEVGF-----EIKKVKFRVFDVGGQRSERKKWIHCFEDVNAIIFIAALSEYNEVLFEDETTNRMIESMRLFESIcns 259
Cdd:cd04150  27 TTIPTIGFnvetvEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERIGEAREELQRMLNEDELRDAV--- 103
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830 260 rwfhntnIILFLNKKDLfeekikkenihkafPEyrgeqnyAETVAFIKTKFeALSNNPKKTFYVHETCAT 329
Cdd:cd04150 104 -------LLVFANKQDL--------------PN-------AMSAAEVTDKL-GLHSLRNRNWYIQATCAT 144
Arfrp1 cd04160
Arf-related protein 1 (Arfrp1); Arfrp1 (Arf-related protein 1), formerly known as ARP, is a ...
185-276 3.35e-05

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: 43.87  E-value: 3.35e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830 185 TGIVEVGfeikKVKFRVFDVGGQRSERKKWIHCFEDVNAIIFIAALSeynevlfeDETtnRMIESMRLFESICNSRWFHN 264
Cdd:cd04160  43 IGTIEVG----KARLMFWDLGGQEELRSLWDKYYAESHGVIYVIDST--------DRE--RFNESKSAFEKVINNEALEG 108
                        90
                ....*....|..
gi 17561830 265 TNIILFLNKKDL 276
Cdd:cd04160 109 VPLLVLANKQDL 120
Arl10_like cd04159
Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from ...
173-227 7.49e-05

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: 42.69  E-value: 7.49e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17561830 173 NATDTLLLRTKTTG------IVEVGFEIKKVK-----FRVFDVGGQRSERKKWIHCFEDVNAIIFI 227
Cdd:cd04159   9 NSGKTTLVNVIASGqfsedtIPTVGFNMRKVTkgnvtIKVWDLGGQPRFRSMWERYCRGVNAIVYV 74
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
184-304 8.54e-05

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: 42.44  E-value: 8.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830 184 TTGIV--EVGFEIKKVKFRVFDVGGQRSERKKWI-----HCFEDVNAIIFIAALSEYNEvlfEDETTNRMIESMRLfesi 256
Cdd:cd00882  32 TRDPDvyVKELDKGKVKLVLVDTPGLDEFGGLGReelarLLLRGADLILLVVDSTDRES---EEDAKLLILRRLRK---- 104
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 17561830 257 cnsrwfHNTNIILFLNKKDLFEEKIKKENIHKAFPEYRGEQNYAETVA 304
Cdd:cd00882 105 ------EGIPIILVGNKIDLLEEREVEELLRLEELAKILGVPVFEVSA 146
Arl2 cd04154
Arf-like 2 (Arl2) GTPase; Arl2 (Arf-like 2) GTPases are members of the Arf family that bind ...
190-276 9.04e-05

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: 42.70  E-value: 9.04e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830 190 VGFEIKKVKFR-----VFDVGGQRSERKKWIHCFEDVNAIIFIAALSEynevlfedetTNRMIESMRLFESICNSRWFHN 264
Cdd:cd04154  46 LGFNIKTLEYNgyklnIWDVGGQKSLRSYWRNYFESTDALIWVVDSSD----------RARLEDCKRELQKLLVEERLAG 115
                        90
                ....*....|..
gi 17561830 265 TNIILFLNKKDL 276
Cdd:cd04154 116 ATLLIFANKQDL 127
Arl6 cd04157
Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small ...
184-276 2.23e-04

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: 41.26  E-value: 2.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830 184 TTGIVEVGFEIKKVKFRVFDVGGQRSERKKWIHCFEDVNAIIFIAALS-EYNEVLFEDEttnrmIESMRLFESICNSRwf 262
Cdd:cd04157  32 TVGFNVESFKKGNLSFTAFDMSGQGKYRGLWEHYYKNIQGIIFVIDSSdRLRMVVAKDE-----LELLLNHPDIKHRR-- 104
                        90
                ....*....|....
gi 17561830 263 hnTNIILFLNKKDL 276
Cdd:cd04157 105 --IPILFYANKMDL 116
Arl1 cd04151
ADP ribosylation factor 1 (Arf1); Arl1 subfamily. Arl1 (Arf-like 1) localizes to the Golgi ...
185-276 3.08e-04

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: 40.85  E-value: 3.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830 185 TGIVEVGFEI-----KKVKFRVFDVGGQRSERKKWIHCFEDVNAIIFIAALSEYNEVLFEDETTNRMIESMRLFESIcns 259
Cdd:cd04151  26 TTIPTIGFNVetvtyKNLKFQVWDLGGQTSIRPYWRCYYSNTDAIIYVVDSTDRDRLGISKSELHAMLEEEELKDAV--- 102
                        90
                ....*....|....*..
gi 17561830 260 rwfhntnIILFLNKKDL 276
Cdd:cd04151 103 -------LLVFANKQDM 112
SAR smart00178
Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene ...
194-227 1.87e-03

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


Pssm-ID: 197556 [Multi-domain]  Cd Length: 184  Bit Score: 38.76  E-value: 1.87e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 17561830    194 IKKVKFRVFDVGGQRSERKKWIHCFEDVNAIIFI 227
Cdd:smart00178  58 IGNIKFTTFDLGGHQQARRLWKDYFPEVNGIVYL 91
Arl5_Arl8 cd04153
Arf-like 5 (Arl5) and 8 (Arl8) GTPases; Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like ...
192-276 2.52e-03

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: 38.48  E-value: 2.52e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830 192 FEIKKVKFRVFDVGGQRSERKKWIHCFEDVNAIIFI------AALSEYNEVLFedettnRMI--ESMRlfesicnsrwfh 263
Cdd:cd04153  54 IVYKNIRFLMWDIGGQESLRSSWNTYYTNTDAVILVidstdrERLPLTKEELY------KMLahEDLR------------ 115
                        90
                ....*....|...
gi 17561830 264 NTNIILFLNKKDL 276
Cdd:cd04153 116 KAVLLVLANKQDL 128
ARD1 cd04158
(ADP-ribosylation factor domain protein 1 (ARD1); ARD1 (ADP-ribosylation factor domain protein ...
193-288 5.80e-03

(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: 37.32  E-value: 5.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561830 193 EIKKVKFRVFDVGGQRSERKKWIHCFEDVNAIIFIaalseynevlFEDETTNRMIESMRLFESICNSRWFHNTNIILFLN 272
Cdd:cd04158  39 EYKNLKFTIWDVGGKHKLRPLWKHYYLNTQAVVFV----------IDSSHRDRVSEAHSELAKLLTEKELRDALLLIFAN 108
                        90       100
                ....*....|....*....|.
gi 17561830 273 KKDL-----FEEKIKKENIHK 288
Cdd:cd04158 109 KQDVagalsVEEMTELLSLHK 129
 
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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