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Conserved domains on  [gi|224009890|ref|XP_002293903|]
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heterotrimeric G protein alpha subunit 1, partial [Thalassiosira pseudonana CCMP1335]

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 ...
1-336 5.37e-121

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: 351.88  E-value: 5.37e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890     1 RSRQIEADLQRARHEEESKIKMLLLGAGESGKSTIFKQMRLLYGTERSEEDLRLYGVVARSNIVVAARKLCSHLRSLGL- 79
Cdd:smart00275   3 RNKEIEKQLEEERKKKKREVKLLLLGAGESGKSTILKQMRILHGDGFSQEERREYRPLIYSNILESMKALVDAMEELNIp 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890    80 ---EEELDREAKEMDELEGGDHGGVNCRQAYdelmaYLSIRILWQSNTMKQVWAKRSAVNIIDSHKDYLNDIPRIASPDY 156
Cdd:smart00275  83 fedPESILDIRIITEQFNKTDETENVLPKEI-----AKAIKALWKDEGIQECYRRRNEFQLNDSASYFLDNIDRIGDPDY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890   157 RPSTQDVIIARVRTTHVVMEKYRIDGIDFEMYDVGGQRSERRKWIDCFDQVTAVIFVAALSEYDQTLAEAKRTNRMVEAL 236
Cdd:smart00275 158 VPTEQDILRSRVPTTGIQETAFIVKKLFFRMFDVGGQRSERKKWIHCFDNVTAIIFCVALSEYDQVLEEDESTNRMQESL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890   237 ELFRSVCNNRAFSNTSIMLFLNKKDIFAEKIMHSDIAAQrpFCDYAGPtKDFDHGVLYFIQKFKDCLIDDEFNDSFIHVT 316
Cdd:smart00275 238 NLFESICNSRWFANTSIILFLNKIDLFEEKIKKVPLVDY--FPDYKGP-NDYEAAAKFIKQKFLRLNRNSSRKSIYHHFT 314
                          330       340
                   ....*....|....*....|
gi 224009890   317 CATDTNNMEFVLDSTRTIIM 336
Cdd:smart00275 315 CATDTRNIRVVFDAVKDIIL 334
 
Name Accession Description Interval E-value
G_alpha smart00275
G protein alpha subunit; Subunit of G proteins that contains the guanine nucleotide binding ...
1-336 5.37e-121

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: 351.88  E-value: 5.37e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890     1 RSRQIEADLQRARHEEESKIKMLLLGAGESGKSTIFKQMRLLYGTERSEEDLRLYGVVARSNIVVAARKLCSHLRSLGL- 79
Cdd:smart00275   3 RNKEIEKQLEEERKKKKREVKLLLLGAGESGKSTILKQMRILHGDGFSQEERREYRPLIYSNILESMKALVDAMEELNIp 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890    80 ---EEELDREAKEMDELEGGDHGGVNCRQAYdelmaYLSIRILWQSNTMKQVWAKRSAVNIIDSHKDYLNDIPRIASPDY 156
Cdd:smart00275  83 fedPESILDIRIITEQFNKTDETENVLPKEI-----AKAIKALWKDEGIQECYRRRNEFQLNDSASYFLDNIDRIGDPDY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890   157 RPSTQDVIIARVRTTHVVMEKYRIDGIDFEMYDVGGQRSERRKWIDCFDQVTAVIFVAALSEYDQTLAEAKRTNRMVEAL 236
Cdd:smart00275 158 VPTEQDILRSRVPTTGIQETAFIVKKLFFRMFDVGGQRSERKKWIHCFDNVTAIIFCVALSEYDQVLEEDESTNRMQESL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890   237 ELFRSVCNNRAFSNTSIMLFLNKKDIFAEKIMHSDIAAQrpFCDYAGPtKDFDHGVLYFIQKFKDCLIDDEFNDSFIHVT 316
Cdd:smart00275 238 NLFESICNSRWFANTSIILFLNKIDLFEEKIKKVPLVDY--FPDYKGP-NDYEAAAKFIKQKFLRLNRNSSRKSIYHHFT 314
                          330       340
                   ....*....|....*....|
gi 224009890   317 CATDTNNMEFVLDSTRTIIM 336
Cdd:smart00275 315 CATDTRNIRVVFDAVKDIIL 334
G-alpha cd00066
Alpha subunit of G proteins (guanine nucleotide binding); The alpha subunit of G proteins ...
20-335 1.18e-118

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: 344.90  E-value: 1.18e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890  20 IKMLLLGAGESGKSTIFKQMRLLYGTERSEEDLRLYGVVARSNIVVAARKLCSHLRSLGLE---EELDREAKEMDELEGG 96
Cdd:cd00066    1 VKLLLLGAGESGKSTILKQMKILHGNGFSDEERREFRPVIYSNILQSMKALLRAMETLNIPygdPENEKDAKKILSLAPR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890  97 DHGGVNCRQAYDElmaylsIRILWQSNTMKQVWAKRSAVNIIDSHKDYLNDIPRIASPDYRPSTQDVIIARVRTTHVVME 176
Cdd:cd00066   81 AEEGPLPPELAEA------IKRLWKDPGIQACYDRRNEYQLNDSAKYFLDNLDRISDPDYIPTEQDILRSRVKTTGIIET 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890 177 KYRIDGIDFEMYDVGGQRSERRKWIDCFDQVTAVIFVAALSEYDQTLAEAKRTNRMVEALELFRSVCNNRAFSNTSIMLF 256
Cdd:cd00066  155 DFSIKNLKFRMFDVGGQRSERKKWIHCFEDVTAIIFVVALSEYDQVLVEDESVNRMQESLKLFDSICNSRWFANTSIILF 234
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224009890 257 LNKKDIFAEKIMHSDIaaQRPFCDYAGPTKDFDHGVLYFIQKFKDcLIDDEFNDSFIHVTCATDTNNMEFVLDSTRTII 335
Cdd:cd00066  235 LNKKDLFEEKIKKSPL--TDYFPDYTGPPNDYEEAAKYIKKKFLD-LNRNPNKEIYPHFTCATDTENIRFVFDAVKDII 310
G-alpha pfam00503
G-protein alpha subunit; G proteins couple receptors of extracellular signals to intracellular ...
17-335 5.32e-113

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: 330.32  E-value: 5.32e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890   17 ESKIKMLLLGAGESGKSTIFKQMRLLYGTERSEEDLRLYGVVARSNIVVAARKLCSHLRSLGLEEELDREAKEMDELEGG 96
Cdd:pfam00503   3 KKEVKLLLLGAGESGKSTILKQMKIIHGGGFSEEERKQYRPVIYSNILRSLKTLIEAMERLGIELSNPENKERLDDLLSL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890   97 DHGGVNCRQAYDELMAYlsIRILWQSNTMKQVWAKRSAVNIIDSHKDYLNDIPRIASPDYRPSTQDVIIARVRTTHVVME 176
Cdd:pfam00503  83 DSSLKNETEFTPELAED--IKRLWNDPGIQECYERRNEFQLPDSAEYFLDNLDRIASPDYVPTDQDILRARVKTTGIIET 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890  177 KYRIDGIDFEMYDVGGQRSERRKWIDCFDQVTAVIFVAALSEYDQTLAEAKRTNRMVEALELFRSVCNNRAFSNTSIMLF 256
Cdd:pfam00503 161 KFEFKGLKFRLFDVGGQRSERKKWIHCFEDVTAIIFVVSLSEYDQVLYEDDSTNRMEESLKLFEEICNSPWFKNTPIILF 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224009890  257 LNKKDIFAEKIMHSDIaaQRPFCDYAGPTKDFDHGVLYFIQKFKDCLIDDEFNDsFIHVTCATDTNNMEFVLDSTRTII 335
Cdd:pfam00503 241 LNKKDLFEEKLKKSPL--SDYFPDYTGNPNDYEEALKYIRNKFLDLNKNPNRKI-YTHFTCATDTENIRFVFDAVKDII 316
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
170-262 2.50e-04

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: 40.82  E-value: 2.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890  170 TTHVVMEKYRIDGID--FEMYDVGGQRSERRKWIDCFDQVTAVIFVAALseydqtlaeAKRTNRMVEALELFRSVCNNRA 247
Cdd:TIGR00231  36 TRNYVTTVIEEDGKTykFNLLDTAGQEDYDAIRRLYYPQVERSLRVFDI---------VILVLDVEEILEKQTKEIIHHA 106
                          90
                  ....*....|....*
gi 224009890  248 FSNTSIMLFLNKKDI 262
Cdd:TIGR00231 107 DSGVPIILVGNKIDL 121
PLN00223 PLN00223
ADP-ribosylation factor; Provisional
164-262 6.75e-04

ADP-ribosylation factor; Provisional


Pssm-ID: 165788  Cd Length: 181  Bit Score: 39.95  E-value: 6.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890 164 IIARVRTTHVVMEKYRIDGIDFEMYDVGGQRSERRKWIDCFDQVTAVIFVAALSEYDQTLAEAKRTNRMVEALELFRSVc 243
Cdd:PLN00223  42 IVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRDRVVEARDELHRMLNEDELRDAV- 120
                         90
                 ....*....|....*....
gi 224009890 244 nnrafsntsIMLFLNKKDI 262
Cdd:PLN00223 121 ---------LLVFANKQDL 130
 
Name Accession Description Interval E-value
G_alpha smart00275
G protein alpha subunit; Subunit of G proteins that contains the guanine nucleotide binding ...
1-336 5.37e-121

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: 351.88  E-value: 5.37e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890     1 RSRQIEADLQRARHEEESKIKMLLLGAGESGKSTIFKQMRLLYGTERSEEDLRLYGVVARSNIVVAARKLCSHLRSLGL- 79
Cdd:smart00275   3 RNKEIEKQLEEERKKKKREVKLLLLGAGESGKSTILKQMRILHGDGFSQEERREYRPLIYSNILESMKALVDAMEELNIp 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890    80 ---EEELDREAKEMDELEGGDHGGVNCRQAYdelmaYLSIRILWQSNTMKQVWAKRSAVNIIDSHKDYLNDIPRIASPDY 156
Cdd:smart00275  83 fedPESILDIRIITEQFNKTDETENVLPKEI-----AKAIKALWKDEGIQECYRRRNEFQLNDSASYFLDNIDRIGDPDY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890   157 RPSTQDVIIARVRTTHVVMEKYRIDGIDFEMYDVGGQRSERRKWIDCFDQVTAVIFVAALSEYDQTLAEAKRTNRMVEAL 236
Cdd:smart00275 158 VPTEQDILRSRVPTTGIQETAFIVKKLFFRMFDVGGQRSERKKWIHCFDNVTAIIFCVALSEYDQVLEEDESTNRMQESL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890   237 ELFRSVCNNRAFSNTSIMLFLNKKDIFAEKIMHSDIAAQrpFCDYAGPtKDFDHGVLYFIQKFKDCLIDDEFNDSFIHVT 316
Cdd:smart00275 238 NLFESICNSRWFANTSIILFLNKIDLFEEKIKKVPLVDY--FPDYKGP-NDYEAAAKFIKQKFLRLNRNSSRKSIYHHFT 314
                          330       340
                   ....*....|....*....|
gi 224009890   317 CATDTNNMEFVLDSTRTIIM 336
Cdd:smart00275 315 CATDTRNIRVVFDAVKDIIL 334
G-alpha cd00066
Alpha subunit of G proteins (guanine nucleotide binding); The alpha subunit of G proteins ...
20-335 1.18e-118

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: 344.90  E-value: 1.18e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890  20 IKMLLLGAGESGKSTIFKQMRLLYGTERSEEDLRLYGVVARSNIVVAARKLCSHLRSLGLE---EELDREAKEMDELEGG 96
Cdd:cd00066    1 VKLLLLGAGESGKSTILKQMKILHGNGFSDEERREFRPVIYSNILQSMKALLRAMETLNIPygdPENEKDAKKILSLAPR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890  97 DHGGVNCRQAYDElmaylsIRILWQSNTMKQVWAKRSAVNIIDSHKDYLNDIPRIASPDYRPSTQDVIIARVRTTHVVME 176
Cdd:cd00066   81 AEEGPLPPELAEA------IKRLWKDPGIQACYDRRNEYQLNDSAKYFLDNLDRISDPDYIPTEQDILRSRVKTTGIIET 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890 177 KYRIDGIDFEMYDVGGQRSERRKWIDCFDQVTAVIFVAALSEYDQTLAEAKRTNRMVEALELFRSVCNNRAFSNTSIMLF 256
Cdd:cd00066  155 DFSIKNLKFRMFDVGGQRSERKKWIHCFEDVTAIIFVVALSEYDQVLVEDESVNRMQESLKLFDSICNSRWFANTSIILF 234
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224009890 257 LNKKDIFAEKIMHSDIaaQRPFCDYAGPTKDFDHGVLYFIQKFKDcLIDDEFNDSFIHVTCATDTNNMEFVLDSTRTII 335
Cdd:cd00066  235 LNKKDLFEEKIKKSPL--TDYFPDYTGPPNDYEEAAKYIKKKFLD-LNRNPNKEIYPHFTCATDTENIRFVFDAVKDII 310
G-alpha pfam00503
G-protein alpha subunit; G proteins couple receptors of extracellular signals to intracellular ...
17-335 5.32e-113

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: 330.32  E-value: 5.32e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890   17 ESKIKMLLLGAGESGKSTIFKQMRLLYGTERSEEDLRLYGVVARSNIVVAARKLCSHLRSLGLEEELDREAKEMDELEGG 96
Cdd:pfam00503   3 KKEVKLLLLGAGESGKSTILKQMKIIHGGGFSEEERKQYRPVIYSNILRSLKTLIEAMERLGIELSNPENKERLDDLLSL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890   97 DHGGVNCRQAYDELMAYlsIRILWQSNTMKQVWAKRSAVNIIDSHKDYLNDIPRIASPDYRPSTQDVIIARVRTTHVVME 176
Cdd:pfam00503  83 DSSLKNETEFTPELAED--IKRLWNDPGIQECYERRNEFQLPDSAEYFLDNLDRIASPDYVPTDQDILRARVKTTGIIET 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890  177 KYRIDGIDFEMYDVGGQRSERRKWIDCFDQVTAVIFVAALSEYDQTLAEAKRTNRMVEALELFRSVCNNRAFSNTSIMLF 256
Cdd:pfam00503 161 KFEFKGLKFRLFDVGGQRSERKKWIHCFEDVTAIIFVVSLSEYDQVLYEDDSTNRMEESLKLFEEICNSPWFKNTPIILF 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224009890  257 LNKKDIFAEKIMHSDIaaQRPFCDYAGPTKDFDHGVLYFIQKFKDCLIDDEFNDsFIHVTCATDTNNMEFVLDSTRTII 335
Cdd:pfam00503 241 LNKKDLFEEKLKKSPL--SDYFPDYTGNPNDYEEALKYIRNKFLDLNKNPNRKI-YTHFTCATDTENIRFVFDAVKDII 316
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
170-262 2.48e-08

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


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 52.61  E-value: 2.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890  170 TTHVVMEKYRIDGIDFEMYDVGGQRSERRKWIDCFDQVTAVIFVAALSEydqtlaeakrTNRMVEALELFRSVCNNRAFS 249
Cdd:pfam00025  31 TIGFNVETVTYKNVKFTVWDVGGQESLRPLWRNYFPNTDAVIFVVDSAD----------RDRIEEAKEELHALLNEEELA 100
                          90
                  ....*....|...
gi 224009890  250 NTSIMLFLNKKDI 262
Cdd:pfam00025 101 DAPLLILANKQDL 113
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
170-261 9.25e-08

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: 51.04  E-value: 9.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890 170 TTHVVMEKYRIDGIDFEMYDVGGQRSERRKWIDCFDQVTAVIFVaalseYDQTLAEakrtnRMVEALELFRSVCNNRAFS 249
Cdd:cd00878   30 TIGFNVETVEYKNVKFTVWDVGGQDKIRPLWKHYYENTDGLIFV-----VDSSDRE-----RIEEAKNELHKLLNEEELK 99
                         90
                 ....*....|..
gi 224009890 250 NTSIMLFLNKKD 261
Cdd:cd00878  100 GAPLLILANKQD 111
Arl5_Arl8 cd04153
Arf-like 5 (Arl5) and 8 (Arl8) GTPases; Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like ...
175-262 3.80e-07

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: 49.27  E-value: 3.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890 175 MEKYRIDGIDFEMYDVGGQRSERRKWIDCFDQVTAVIFVAalseyDQTLAEakRTNRMVEalELFRSVcNNRAFSNTSIM 254
Cdd:cd04153   51 VEEIVYKNIRFLMWDIGGQESLRSSWNTYYTNTDAVILVI-----DSTDRE--RLPLTKE--ELYKML-AHEDLRKAVLL 120

                 ....*...
gi 224009890 255 LFLNKKDI 262
Cdd:cd04153  121 VLANKQDL 128
Sar1 cd00879
Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII ...
168-262 1.33e-05

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: 45.35  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890 168 VRTTHVVMEKYRIDGIDFEMYDVGGQRSERRKWIDCFDQVTAVIFVAALSEYdqtlaeakrtNRMVEALELFRSVCNNRA 247
Cdd:cd00879   48 VPTLHPTSEELTIGNVKFTTFDLGGHEQARRVWKDYFPEVDGIVFLVDAADP----------ERFQESKEELDSLLNDEE 117
                         90
                 ....*....|....*
gi 224009890 248 FSNTSIMLFLNKKDI 262
Cdd:cd00879  118 LANVPILILGNKIDK 132
Arf6 cd04149
ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins ...
183-262 1.67e-05

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: 44.38  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890 183 IDFEMYDVGGQRSERRKWIDCFDQVTAVIFVAALSEYdqtlaeakrtNRMVEALELFRSVCNNRAFSNTSIMLFLNKKDI 262
Cdd:cd04149   53 VKFNVWDVGGQDKIRPLWRHYYTGTQGLIFVVDSADR----------DRIDEARQELHRIINDREMRDALLLVFANKQDL 122
Arl3 cd04155
Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most ...
181-270 4.61e-05

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: 43.54  E-value: 4.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890 181 DGIDFEMYDVGGQRSERRKWIDCFDQVTAVIFVAALSeyDQTlaeakrtnRMVEALELFRSVCNNRAFSNTSIMLFLNKK 260
Cdd:cd04155   57 DGFKLNVWDIGGQRKIRPYWRNYFENTDVLIYVIDSA--DRK--------RFEEAGQELVELLEEEKLAGVPVLVFANKQ 126
                         90
                 ....*....|....
gi 224009890 261 DIF----AEKIMHS 270
Cdd:cd04155  127 DLLtaapAEEVAEA 140
Arfrp1 cd04160
Arf-related protein 1 (Arfrp1); Arfrp1 (Arf-related protein 1), formerly known as ARP, is a ...
180-261 4.92e-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: 43.10  E-value: 4.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890 180 IDGIDFEMYDVGGQRSERRKWIDCFDQVTAVIFVaalseydqtlAEAKRTNRMVEALELFRSVCNNRAFSNTSIMLFLNK 259
Cdd:cd04160   48 VGKARLMFWDLGGQEELRSLWDKYYAESHGVIYV----------IDSTDRERFNESKSAFEKVINNEALEGVPLLVLANK 117

                 ..
gi 224009890 260 KD 261
Cdd:cd04160  118 QD 119
ARF smart00177
ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular ...
164-262 7.76e-05

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: 42.60  E-value: 7.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890   164 IIARVRTTHVVMEKYRIDGIDFEMYDVGGQRSERRKWIDCFDQVTAVIFVAALSEYDqtlaeakrtnRMVEALELFRSVC 243
Cdd:smart00177  38 SVTTIPTIGFNVETVTYKNISFTVWDVGGQDKIRPLWRHYYTNTQGLIFVVDSNDRD----------RIDEAREELHRML 107
                           90
                   ....*....|....*....
gi 224009890   244 NNRAFSNTSIMLFLNKKDI 262
Cdd:smart00177 108 NEDELRDAVILVFANKQDL 126
SAR smart00178
Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene ...
170-228 9.52e-05

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: 42.61  E-value: 9.52e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 224009890   170 TTHVVMEKYRIDGIDFEMYDVGGQRSERRKWIDCFDQVTAVIFVAALSEYDQtLAEAKR 228
Cdd:smart00178  48 TQHPTSEELAIGNIKFTTFDLGGHQQARRLWKDYFPEVNGIVYLVDAYDKER-FAESKR 105
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
170-262 2.50e-04

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: 40.82  E-value: 2.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890  170 TTHVVMEKYRIDGID--FEMYDVGGQRSERRKWIDCFDQVTAVIFVAALseydqtlaeAKRTNRMVEALELFRSVCNNRA 247
Cdd:TIGR00231  36 TRNYVTTVIEEDGKTykFNLLDTAGQEDYDAIRRLYYPQVERSLRVFDI---------VILVLDVEEILEKQTKEIIHHA 106
                          90
                  ....*....|....*
gi 224009890  248 FSNTSIMLFLNKKDI 262
Cdd:TIGR00231 107 DSGVPIILVGNKIDL 121
ARLTS1 cd04156
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ...
187-262 3.72e-04

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: 40.48  E-value: 3.72e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224009890 187 MYDVGGQRSERRKWIDCFDQVTAVIFVAALSEYdQTLAEAKRTnrmvealelFRSVCNNRAFSNTSIMLFLNKKDI 262
Cdd:cd04156   48 VWDVGGQEKMRTVWKCYLENTDGLVYVVDSSDE-ARLDESQKE---------LKHILKNEHIKGVPVVLLANKQDL 113
PLN00223 PLN00223
ADP-ribosylation factor; Provisional
164-262 6.75e-04

ADP-ribosylation factor; Provisional


Pssm-ID: 165788  Cd Length: 181  Bit Score: 39.95  E-value: 6.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890 164 IIARVRTTHVVMEKYRIDGIDFEMYDVGGQRSERRKWIDCFDQVTAVIFVAALSEYDQTLAEAKRTNRMVEALELFRSVc 243
Cdd:PLN00223  42 IVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRDRVVEARDELHRMLNEDELRDAV- 120
                         90
                 ....*....|....*....
gi 224009890 244 nnrafsntsIMLFLNKKDI 262
Cdd:PLN00223 121 ---------LLVFANKQDL 130
Arf1_5_like cd04150
ADP-ribosylation factor-1 (Arf1) and ADP-ribosylation factor-5 (Arf5); The Arf1-Arf5-like ...
164-262 1.86e-03

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: 38.54  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890 164 IIARVRTTHVVMEKYRIDGIDFEMYDVGGQRSERRKWIDCFDQVTAVIFVAALSEYDqtlaeakrtnRMVEALELFRSVC 243
Cdd:cd04150   25 IVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRE----------RIGEAREELQRML 94
                         90
                 ....*....|....*....
gi 224009890 244 NNRAFSNTSIMLFLNKKDI 262
Cdd:cd04150   95 NEDELRDAVLLVFANKQDL 113
Arl2 cd04154
Arf-like 2 (Arl2) GTPase; Arl2 (Arf-like 2) GTPases are members of the Arf family that bind ...
181-262 2.99e-03

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: 38.07  E-value: 2.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224009890 181 DGIDFEMYDVGGQRSERRKWIDCFDQVTAVIFVAALSEyDQTLAEAKRtnrmvealELFRSVCNNRaFSNTSIMLFLNKK 260
Cdd:cd04154   56 NGYKLNIWDVGGQKSLRSYWRNYFESTDALIWVVDSSD-RARLEDCKR--------ELQKLLVEER-LAGATLLIFANKQ 125

                 ..
gi 224009890 261 DI 262
Cdd:cd04154  126 DL 127
 
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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