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Conserved domains on  [gi|578832131|ref|XP_006722387|]
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guanine nucleotide-binding protein G(olf) subunit alpha isoform X1 [Homo sapiens]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 120-240 6.76e-56

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd00066:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 315  Bit Score: 180.80  E-value: 6.76e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832131 120 HRLLLLGAGESGKSTIVKQMRILHVNGFNPEEKKQKILDIRKNVKDAIVTIVSAMSTIIPpvPLANPENQFRSDYIKSIA 199
Cdd:cd00066    1 VKLLLLGAGESGKSTILKQMKILHGNGFSDEERREFRPVIYSNILQSMKALLRAMETLNI--PYGDPENEKDAKKILSLA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 578832131 200 P-ITDFEYSQEFFDHVKKLWDDEGVKACFERSNEYQLIDCAQ 240
Cdd:cd00066   79 PrAEEGPLPPELAEAIKRLWKDPGIQACYDRRNEYQLNDSAK 120
 
Name Accession Description Interval E-value
G-alpha cd00066
Alpha subunit of G proteins (guanine nucleotide binding); The alpha subunit of G proteins ...
 120-240 6.76e-56

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: 180.80  E-value: 6.76e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832131 120 HRLLLLGAGESGKSTIVKQMRILHVNGFNPEEKKQKILDIRKNVKDAIVTIVSAMSTIIPpvPLANPENQFRSDYIKSIA 199
Cdd:cd00066    1 VKLLLLGAGESGKSTILKQMKILHGNGFSDEERREFRPVIYSNILQSMKALLRAMETLNI--PYGDPENEKDAKKILSLA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 578832131 200 P-ITDFEYSQEFFDHVKKLWDDEGVKACFERSNEYQLIDCAQ 240
Cdd:cd00066   79 PrAEEGPLPPELAEAIKRLWKDPGIQACYDRRNEYQLNDSAK 120
G_alpha smart00275
G protein alpha subunit; Subunit of G proteins that contains the guanine nucleotide binding ...
 99-240 1.95e-48

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: 162.36  E-value: 1.95e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832131    99 RKVSRGIDRMLRDQKRDLQQTHRLLLLGAGESGKSTIVKQMRILHVNGFNPEEKKQKILDIRKNVKDAIVTIVSAMSTII 178
Cdd:smart00275   1 IRRNKEIEKQLEEERKKKKREVKLLLLGAGESGKSTILKQMRILHGDGFSQEERREYRPLIYSNILESMKALVDAMEELN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578832131   179 ppVPLANPENQFRSDYIKSI---APITDFEYSQEFFDHVKKLWDDEGVKACFERSNEYQLIDCAQ 240
Cdd:smart00275  81 --IPFEDPESILDIRIITEQfnkTDETENVLPKEIAKAIKALWKDEGIQECYRRRNEFQLNDSAS 143
G-alpha pfam00503
G-protein alpha subunit; G proteins couple receptors of extracellular signals to intracellular ...
 115-239 2.66e-40

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: 140.80  E-value: 2.66e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832131  115 DLQQTHRLLLLGAGESGKSTIVKQMRILHVNGFNPEEKKQKILDIRKNVKDAIVTIVSAMSTIipPVPLANPENQFRSDY 194
Cdd:pfam00503   1 KLKKEVKLLLLGAGESGKSTILKQMKIIHGGGFSEEERKQYRPVIYSNILRSLKTLIEAMERL--GIELSNPENKERLDD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 578832131  195 IKSI--APITDFEYSQEFFDHVKKLWDDEGVKACFERSNEYQLIDCA 239
Cdd:pfam00503  79 LLSLdsSLKNETEFTPELAEDIKRLWNDPGIQECYERRNEFQLPDSA 125
 
Name Accession Description Interval E-value
G-alpha cd00066
Alpha subunit of G proteins (guanine nucleotide binding); The alpha subunit of G proteins ...
 120-240 6.76e-56

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: 180.80  E-value: 6.76e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832131 120 HRLLLLGAGESGKSTIVKQMRILHVNGFNPEEKKQKILDIRKNVKDAIVTIVSAMSTIIPpvPLANPENQFRSDYIKSIA 199
Cdd:cd00066    1 VKLLLLGAGESGKSTILKQMKILHGNGFSDEERREFRPVIYSNILQSMKALLRAMETLNI--PYGDPENEKDAKKILSLA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 578832131 200 P-ITDFEYSQEFFDHVKKLWDDEGVKACFERSNEYQLIDCAQ 240
Cdd:cd00066   79 PrAEEGPLPPELAEAIKRLWKDPGIQACYDRRNEYQLNDSAK 120
G_alpha smart00275
G protein alpha subunit; Subunit of G proteins that contains the guanine nucleotide binding ...
 99-240 1.95e-48

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: 162.36  E-value: 1.95e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832131    99 RKVSRGIDRMLRDQKRDLQQTHRLLLLGAGESGKSTIVKQMRILHVNGFNPEEKKQKILDIRKNVKDAIVTIVSAMSTII 178
Cdd:smart00275   1 IRRNKEIEKQLEEERKKKKREVKLLLLGAGESGKSTILKQMRILHGDGFSQEERREYRPLIYSNILESMKALVDAMEELN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578832131   179 ppVPLANPENQFRSDYIKSI---APITDFEYSQEFFDHVKKLWDDEGVKACFERSNEYQLIDCAQ 240
Cdd:smart00275  81 --IPFEDPESILDIRIITEQfnkTDETENVLPKEIAKAIKALWKDEGIQECYRRRNEFQLNDSAS 143
G-alpha pfam00503
G-protein alpha subunit; G proteins couple receptors of extracellular signals to intracellular ...
 115-239 2.66e-40

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: 140.80  E-value: 2.66e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578832131  115 DLQQTHRLLLLGAGESGKSTIVKQMRILHVNGFNPEEKKQKILDIRKNVKDAIVTIVSAMSTIipPVPLANPENQFRSDY 194
Cdd:pfam00503   1 KLKKEVKLLLLGAGESGKSTILKQMKIIHGGGFSEEERKQYRPVIYSNILRSLKTLIEAMERL--GIELSNPENKERLDD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 578832131  195 IKSI--APITDFEYSQEFFDHVKKLWDDEGVKACFERSNEYQLIDCA 239
Cdd:pfam00503  79 LLSLdsSLKNETEFTPELAEDIKRLWNDPGIQECYERRNEFQLPDSA 125
 
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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