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Conserved domains on  [gi|334182982|ref|NP_001185125|]
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extra-large GTP-binding protein 3 [Arabidopsis thaliana]

Protein Classification

guanine nucleotide-binding protein subunit alpha( domain architecture ID 10048024)

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 cd00066
Alpha subunit of G proteins (guanine nucleotide binding); The alpha subunit of G proteins ...
431-818 4.54e-89

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: 284.42  E-value: 4.54e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982 431 QKLLLLGIEGSGTSTIFKQAKFLYGNKFSVEELQDIKLMVQSNMYRYLSILLDGRERFEEEAlshtrglnavegdsgGEE 510
Cdd:cd00066    1 VKLLLLGAGESGKSTILKQMKILHGNGFSDEERREFRPVIYSNILQSMKALLRAMETLNIPY---------------GDP 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982 511 ANDEgtvttpqsvytlnprlkhFSDWLLDIiatgDLDAFFPAATREYAPLVEEVWKDPAIQATYRRKDELHfLPDVAEYF 590
Cdd:cd00066   66 ENEK------------------DAKKILSL----APRAEEGPLPPELAEAIKRLWKDPGIQACYDRRNEYQ-LNDSAKYF 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982 591 LSRAMEVSSNEYEPSERDIVYAEGVTqgNGLAFMEFSLSDHspmsesypenpdalsspqpKYQLIRVnaKGM-NDSCKWV 669
Cdd:cd00066  123 LDNLDRISDPDYIPTEQDILRSRVKT--TGIIETDFSIKNL-------------------KFRMFDV--GGQrSERKKWI 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982 670 EMFEDVRAVIFCISLSDYDQINITPESsgtvqyQNKMIQSKELFESMVKHPCFKDTPFILILNKYDQFEEKLNRAPLTSC 749
Cdd:cd00066  180 HCFEDVTAIIFVVALSEYDQVLVEDES------VNRMQESLKLFDSICNSRWFANTSIILFLNKKDLFEEKIKKSPLTDY 253
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334182982 750 dwFSDFCPVRtnNNVQslayQAYFYVAMKFKLLYFSiTGQKLFVWQARARDRANVDEGFKYVREVLKWD 818
Cdd:cd00066  254 --FPDYTGPP--NDYE----EAAKYIKKKFLDLNRN-PNKEIYPHFTCATDTENIRFVFDAVKDIILQN 313
 
Name Accession Description Interval E-value
G-alpha cd00066
Alpha subunit of G proteins (guanine nucleotide binding); The alpha subunit of G proteins ...
431-818 4.54e-89

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: 284.42  E-value: 4.54e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982 431 QKLLLLGIEGSGTSTIFKQAKFLYGNKFSVEELQDIKLMVQSNMYRYLSILLDGRERFEEEAlshtrglnavegdsgGEE 510
Cdd:cd00066    1 VKLLLLGAGESGKSTILKQMKILHGNGFSDEERREFRPVIYSNILQSMKALLRAMETLNIPY---------------GDP 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982 511 ANDEgtvttpqsvytlnprlkhFSDWLLDIiatgDLDAFFPAATREYAPLVEEVWKDPAIQATYRRKDELHfLPDVAEYF 590
Cdd:cd00066   66 ENEK------------------DAKKILSL----APRAEEGPLPPELAEAIKRLWKDPGIQACYDRRNEYQ-LNDSAKYF 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982 591 LSRAMEVSSNEYEPSERDIVYAEGVTqgNGLAFMEFSLSDHspmsesypenpdalsspqpKYQLIRVnaKGM-NDSCKWV 669
Cdd:cd00066  123 LDNLDRISDPDYIPTEQDILRSRVKT--TGIIETDFSIKNL-------------------KFRMFDV--GGQrSERKKWI 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982 670 EMFEDVRAVIFCISLSDYDQINITPESsgtvqyQNKMIQSKELFESMVKHPCFKDTPFILILNKYDQFEEKLNRAPLTSC 749
Cdd:cd00066  180 HCFEDVTAIIFVVALSEYDQVLVEDES------VNRMQESLKLFDSICNSRWFANTSIILFLNKKDLFEEKIKKSPLTDY 253
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334182982 750 dwFSDFCPVRtnNNVQslayQAYFYVAMKFKLLYFSiTGQKLFVWQARARDRANVDEGFKYVREVLKWD 818
Cdd:cd00066  254 --FPDYTGPP--NDYE----EAAKYIKKKFLDLNRN-PNKEIYPHFTCATDTENIRFVFDAVKDIILQN 313
G-alpha pfam00503
G-protein alpha subunit; G proteins couple receptors of extracellular signals to intracellular ...
428-815 6.48e-81

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: 262.91  E-value: 6.48e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982  428 KKIQKLLLLGIEGSGTSTIFKQAKFLYGNKFSVEELQDIKLMVQSNMYRYLSILLDGRERFEEEALshtrglnavegdsg 507
Cdd:pfam00503   3 KKEVKLLLLGAGESGKSTILKQMKIIHGGGFSEEERKQYRPVIYSNILRSLKTLIEAMERLGIELS-------------- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982  508 geeandegtvttpqsvytlNPRLKHFSDWLLDIIATGDLDAFFPaatREYAPLVEEVWKDPAIQATYRRKDELHfLPDVA 587
Cdd:pfam00503  69 -------------------NPENKERLDDLLSLDSSLKNETEFT---PELAEDIKRLWNDPGIQECYERRNEFQ-LPDSA 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982  588 EYFLSRAMEVSSNEYEPSERDIVYAEgvTQGNGLAFMEFSLSDHspmsesypenpdalsspqpKYQLIRVNAKGmNDSCK 667
Cdd:pfam00503 126 EYFLDNLDRIASPDYVPTDQDILRAR--VKTTGIIETKFEFKGL-------------------KFRLFDVGGQR-SERKK 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982  668 WVEMFEDVRAVIFCISLSDYDQINItpESSGTvqyqNKMIQSKELFESMVKHPCFKDTPFILILNKYDQFEEKLNRAPLT 747
Cdd:pfam00503 184 WIHCFEDVTAIIFVVSLSEYDQVLY--EDDST----NRMEESLKLFEEICNSPWFKNTPIILFLNKKDLFEEKLKKSPLS 257
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334182982  748 scDWFSDFcpvrtnNNVQSLAYQAYFYVAMKFKLLYfSITGQKLFVWQARARDRANVDEGFKYVREVL 815
Cdd:pfam00503 258 --DYFPDY------TGNPNDYEEALKYIRNKFLDLN-KNPNRKIYTHFTCATDTENIRFVFDAVKDII 316
G_alpha smart00275
G protein alpha subunit; Subunit of G proteins that contains the guanine nucleotide binding ...
428-755 5.78e-47

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: 170.84  E-value: 5.78e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982   428 KKIQKLLLLGIEGSGTSTIFKQAKFLYGNKFSVEELQDIKLMVQSNMYRYLSILLDGRERFeeealshtrGLNavegdsg 507
Cdd:smart00275  19 KREVKLLLLGAGESGKSTILKQMRILHGDGFSQEERREYRPLIYSNILESMKALVDAMEEL---------NIP------- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982   508 geeandegtVTTPQSVYtlnpRLKHFsdwLLDIIATGDLDAFFPaatREYAPLVEEVWKDPAIQATYRRKDELHfLPDVA 587
Cdd:smart00275  83 ---------FEDPESIL----DIRII---TEQFNKTDETENVLP---KEIAKAIKALWKDEGIQECYRRRNEFQ-LNDSA 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982   588 EYFLSRAMEVSSNEYEPSERDIVYAE----GVTQgnglafMEFSLSDHspmsesypenpdalsspqpKYQLI-----RVN 658
Cdd:smart00275 143 SYFLDNIDRIGDPDYVPTEQDILRSRvpttGIQE------TAFIVKKL-------------------FFRMFdvggqRSE 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982   659 AKgmndscKWVEMFEDVRAVIFCISLSDYDQIniTPESSGTvqyqNKMIQSKELFESMVKHPCFKDTPFILILNKYDQFE 738
Cdd:smart00275 198 RK------KWIHCFDNVTAIIFCVALSEYDQV--LEEDEST----NRMQESLNLFESICNSRWFANTSIILFLNKIDLFE 265
                          330
                   ....*....|....*..
gi 334182982   739 EKLNRAPLTscDWFSDF 755
Cdd:smart00275 266 EKIKKVPLV--DYFPDY 280
 
Name Accession Description Interval E-value
G-alpha cd00066
Alpha subunit of G proteins (guanine nucleotide binding); The alpha subunit of G proteins ...
431-818 4.54e-89

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: 284.42  E-value: 4.54e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982 431 QKLLLLGIEGSGTSTIFKQAKFLYGNKFSVEELQDIKLMVQSNMYRYLSILLDGRERFEEEAlshtrglnavegdsgGEE 510
Cdd:cd00066    1 VKLLLLGAGESGKSTILKQMKILHGNGFSDEERREFRPVIYSNILQSMKALLRAMETLNIPY---------------GDP 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982 511 ANDEgtvttpqsvytlnprlkhFSDWLLDIiatgDLDAFFPAATREYAPLVEEVWKDPAIQATYRRKDELHfLPDVAEYF 590
Cdd:cd00066   66 ENEK------------------DAKKILSL----APRAEEGPLPPELAEAIKRLWKDPGIQACYDRRNEYQ-LNDSAKYF 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982 591 LSRAMEVSSNEYEPSERDIVYAEGVTqgNGLAFMEFSLSDHspmsesypenpdalsspqpKYQLIRVnaKGM-NDSCKWV 669
Cdd:cd00066  123 LDNLDRISDPDYIPTEQDILRSRVKT--TGIIETDFSIKNL-------------------KFRMFDV--GGQrSERKKWI 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982 670 EMFEDVRAVIFCISLSDYDQINITPESsgtvqyQNKMIQSKELFESMVKHPCFKDTPFILILNKYDQFEEKLNRAPLTSC 749
Cdd:cd00066  180 HCFEDVTAIIFVVALSEYDQVLVEDES------VNRMQESLKLFDSICNSRWFANTSIILFLNKKDLFEEKIKKSPLTDY 253
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334182982 750 dwFSDFCPVRtnNNVQslayQAYFYVAMKFKLLYFSiTGQKLFVWQARARDRANVDEGFKYVREVLKWD 818
Cdd:cd00066  254 --FPDYTGPP--NDYE----EAAKYIKKKFLDLNRN-PNKEIYPHFTCATDTENIRFVFDAVKDIILQN 313
G-alpha pfam00503
G-protein alpha subunit; G proteins couple receptors of extracellular signals to intracellular ...
428-815 6.48e-81

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: 262.91  E-value: 6.48e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982  428 KKIQKLLLLGIEGSGTSTIFKQAKFLYGNKFSVEELQDIKLMVQSNMYRYLSILLDGRERFEEEALshtrglnavegdsg 507
Cdd:pfam00503   3 KKEVKLLLLGAGESGKSTILKQMKIIHGGGFSEEERKQYRPVIYSNILRSLKTLIEAMERLGIELS-------------- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982  508 geeandegtvttpqsvytlNPRLKHFSDWLLDIIATGDLDAFFPaatREYAPLVEEVWKDPAIQATYRRKDELHfLPDVA 587
Cdd:pfam00503  69 -------------------NPENKERLDDLLSLDSSLKNETEFT---PELAEDIKRLWNDPGIQECYERRNEFQ-LPDSA 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982  588 EYFLSRAMEVSSNEYEPSERDIVYAEgvTQGNGLAFMEFSLSDHspmsesypenpdalsspqpKYQLIRVNAKGmNDSCK 667
Cdd:pfam00503 126 EYFLDNLDRIASPDYVPTDQDILRAR--VKTTGIIETKFEFKGL-------------------KFRLFDVGGQR-SERKK 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982  668 WVEMFEDVRAVIFCISLSDYDQINItpESSGTvqyqNKMIQSKELFESMVKHPCFKDTPFILILNKYDQFEEKLNRAPLT 747
Cdd:pfam00503 184 WIHCFEDVTAIIFVVSLSEYDQVLY--EDDST----NRMEESLKLFEEICNSPWFKNTPIILFLNKKDLFEEKLKKSPLS 257
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334182982  748 scDWFSDFcpvrtnNNVQSLAYQAYFYVAMKFKLLYfSITGQKLFVWQARARDRANVDEGFKYVREVL 815
Cdd:pfam00503 258 --DYFPDY------TGNPNDYEEALKYIRNKFLDLN-KNPNRKIYTHFTCATDTENIRFVFDAVKDII 316
G_alpha smart00275
G protein alpha subunit; Subunit of G proteins that contains the guanine nucleotide binding ...
428-755 5.78e-47

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: 170.84  E-value: 5.78e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982   428 KKIQKLLLLGIEGSGTSTIFKQAKFLYGNKFSVEELQDIKLMVQSNMYRYLSILLDGRERFeeealshtrGLNavegdsg 507
Cdd:smart00275  19 KREVKLLLLGAGESGKSTILKQMRILHGDGFSQEERREYRPLIYSNILESMKALVDAMEEL---------NIP------- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982   508 geeandegtVTTPQSVYtlnpRLKHFsdwLLDIIATGDLDAFFPaatREYAPLVEEVWKDPAIQATYRRKDELHfLPDVA 587
Cdd:smart00275  83 ---------FEDPESIL----DIRII---TEQFNKTDETENVLP---KEIAKAIKALWKDEGIQECYRRRNEFQ-LNDSA 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982   588 EYFLSRAMEVSSNEYEPSERDIVYAE----GVTQgnglafMEFSLSDHspmsesypenpdalsspqpKYQLI-----RVN 658
Cdd:smart00275 143 SYFLDNIDRIGDPDYVPTEQDILRSRvpttGIQE------TAFIVKKL-------------------FFRMFdvggqRSE 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982   659 AKgmndscKWVEMFEDVRAVIFCISLSDYDQIniTPESSGTvqyqNKMIQSKELFESMVKHPCFKDTPFILILNKYDQFE 738
Cdd:smart00275 198 RK------KWIHCFDNVTAIIFCVALSEYDQV--LEEDEST----NRMQESLNLFESICNSRWFANTSIILFLNKIDLFE 265
                          330
                   ....*....|....*..
gi 334182982   739 EKLNRAPLTscDWFSDF 755
Cdd:smart00275 266 EKIKKVPLV--DYFPDY 280
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
668-765 1.72e-05

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: 45.65  E-value: 1.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182982 668 WVEMFEDVRAVIFCISLSDYDQinitpessgtvqyqnkMIQSKELFESMVKHPCFKDTPFILILNKYD--------QFEE 739
Cdd:cd00878   60 WKHYYENTDGLIFVVDSSDRER----------------IEEAKNELHKLLNEEELKGAPLLILANKQDlpgaltesELIE 123
                         90       100
                 ....*....|....*....|....*.
gi 334182982 740 KLNRAPLTSCDWFSDFCPVRTNNNVQ 765
Cdd:cd00878  124 LLGLESIKGRRWHIQPCSAVTGDGLD 149
 
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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