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Conserved domains on  [gi|24664720|ref|NP_648786|]
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uncharacterized protein Dmel_CG7650 [Drosophila melanogaster]

Protein Classification

phosducin family protein( domain architecture ID 10122234)

phosducin family protein similar to Drosophila melanogaster phosducin-like protein that functions as a co-chaperone for CCT in the assembly of heterotrimeric G protein complexes, facilitating the assembly of both Gbeta-Ggamma and RGS-Gbeta5 heterodimers

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Phd_like_Phd cd02987
Phosducin (Phd)-like family, Phd subfamily; Phd is a cytosolic regulator of G protein ...
 60-267 3.97e-82

Phosducin (Phd)-like family, Phd subfamily; Phd is a cytosolic regulator of G protein functions. It specifically binds G protein betagamma (Gbg)-subunits with high affinity, resulting in the solubilization of Gbg from the plasma membrane. This impedes the formation of a functional G protein trimer (G protein alphabetagamma), thereby inhibiting G protein-mediated signal transduction. Phd also inhibits the GTPase activity of G protein alpha. Phd can be phosphorylated by protein kinase A and G protein-coupled receptor kinase 2, leading to its inactivation. Phd was originally isolated from the retina, where it is highly expressed and has been implicated to play an important role in light adaptation. It is also found in the pineal gland, liver, spleen, striated muscle and the brain. The C-terminal domain of Phd adopts a thioredoxin fold, but it does not contain a CXXC motif. Phd interacts with G protein beta mostly through the N-terminal helical domain.


:

Pssm-ID: 239285  Cd Length: 175  Bit Score: 244.51  E-value: 3.97e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664720  60 QQSSTNTGPKGVVKDWQRFKQleaerrdeterqrlalakkltitattsaedeerkrQEELDAELDELMS--EDFLQQYQK 137
Cdd:cd02987   1 EGSGTNTGPKGVINDWRKFKQ-----------------------------------LKESEQEDDDDDEdkEEFLQQYRE 45

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664720 138 QRMAEMLRQTGHHQQFGQVQQLTSHEEFLACVEQENKHTTIIIHIYERQLAACATLNKCLDSLASDYPSIKFAKICSSVA 217
Cdd:cd02987  46 QRMQEMHAKLPFGRRFGKVYELDSGEQFLDAIDKEGKDTTVVVHIYEPGIPGCAALNSSLLCLAAEYPAVKFCKIRASAT 125

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 24664720 218 GMSRDFRTKGLPALLVYKAQAVIGNFVRLTDDLSDDFFASDVESFLIEHG 267
Cdd:cd02987 126 GASDEFDTDALPALLVYKGGELIGNFVRVTEDLGEDFDAEDLESFLVEYG 175
 
Name Accession Description Interval E-value
Phd_like_Phd cd02987
Phosducin (Phd)-like family, Phd subfamily; Phd is a cytosolic regulator of G protein ...
 60-267 3.97e-82

Phosducin (Phd)-like family, Phd subfamily; Phd is a cytosolic regulator of G protein functions. It specifically binds G protein betagamma (Gbg)-subunits with high affinity, resulting in the solubilization of Gbg from the plasma membrane. This impedes the formation of a functional G protein trimer (G protein alphabetagamma), thereby inhibiting G protein-mediated signal transduction. Phd also inhibits the GTPase activity of G protein alpha. Phd can be phosphorylated by protein kinase A and G protein-coupled receptor kinase 2, leading to its inactivation. Phd was originally isolated from the retina, where it is highly expressed and has been implicated to play an important role in light adaptation. It is also found in the pineal gland, liver, spleen, striated muscle and the brain. The C-terminal domain of Phd adopts a thioredoxin fold, but it does not contain a CXXC motif. Phd interacts with G protein beta mostly through the N-terminal helical domain.


Pssm-ID: 239285  Cd Length: 175  Bit Score: 244.51  E-value: 3.97e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664720  60 QQSSTNTGPKGVVKDWQRFKQleaerrdeterqrlalakkltitattsaedeerkrQEELDAELDELMS--EDFLQQYQK 137
Cdd:cd02987   1 EGSGTNTGPKGVINDWRKFKQ-----------------------------------LKESEQEDDDDDEdkEEFLQQYRE 45

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664720 138 QRMAEMLRQTGHHQQFGQVQQLTSHEEFLACVEQENKHTTIIIHIYERQLAACATLNKCLDSLASDYPSIKFAKICSSVA 217
Cdd:cd02987  46 QRMQEMHAKLPFGRRFGKVYELDSGEQFLDAIDKEGKDTTVVVHIYEPGIPGCAALNSSLLCLAAEYPAVKFCKIRASAT 125

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 24664720 218 GMSRDFRTKGLPALLVYKAQAVIGNFVRLTDDLSDDFFASDVESFLIEHG 267
Cdd:cd02987 126 GASDEFDTDALPALLVYKGGELIGNFVRVTEDLGEDFDAEDLESFLVEYG 175
Phosducin pfam02114
Phosducin;
63-275 7.53e-64

Phosducin;


Pssm-ID: 251094 [Multi-domain]  Cd Length: 265  Bit Score: 201.07  E-value: 7.53e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664720    63 STNTGPKGVVKDWQRFKQLEAERRDETERQRLALAKKLTITATTSA-EDEERKRQEELDAELDELMS------------- 128
Cdd:pfam02114  20 ASHTGPKGVINDWRKFKQLESEDRDEQAHEKEEIIKKLSMSCRSHLdEEEEQQDDKDLKEKFSGKMSlkecelidkdkdd 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664720   129 EDFLQQYQKQRMAEMLRQTGHHQQFGQVQQLTSHEEFLACVEQENKHTTIIIHIYERQLAACATLNKCLDSLASDYPSIK 208
Cdd:pfam02114 100 EECLQKYRKQCMDDMHQKLHFGPQFGFVLEIESGEGFLDMIDKEQKITLIMVHIYEDGIKGCDALNGCLICLAAEYPMVK 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24664720   209 FAKICSSVAGMSRDFRTKGLPALLVYKAQAVIGNFVRLTDDLSDDFFASDVESFLIEHGIIVDRALY 275
Cdd:pfam02114 180 FCKIKASNIGAGDRFSRDALPALLIYKAGELIGNFIRVTDQLAEDFFAGDLEAFLNEFGLLPEKEMH 246
PTZ00051 PTZ00051
thioredoxin; Provisional
 156-249 1.07e-03

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 37.55  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664720  156 VQQLTSHEEFLACVEQEnkhTTIIIHIYERQLAACATLNKCLDSLASDYPSIKFAKI-CSSVAGMSRDFRTKGLPALLVY 234
Cdd:PTZ00051   2 VHIVTSQAEFESTLSQN---ELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVdVDELSEVAEKENITSMPTFKVF 78

                         90
                 ....*....|....*
gi 24664720  235 KAQAVIGNFVRLTDD 249
Cdd:PTZ00051  79 KNGSVVDTLLGANDE 93
 
Name Accession Description Interval E-value
Phd_like_Phd cd02987
Phosducin (Phd)-like family, Phd subfamily; Phd is a cytosolic regulator of G protein ...
 60-267 3.97e-82

Phosducin (Phd)-like family, Phd subfamily; Phd is a cytosolic regulator of G protein functions. It specifically binds G protein betagamma (Gbg)-subunits with high affinity, resulting in the solubilization of Gbg from the plasma membrane. This impedes the formation of a functional G protein trimer (G protein alphabetagamma), thereby inhibiting G protein-mediated signal transduction. Phd also inhibits the GTPase activity of G protein alpha. Phd can be phosphorylated by protein kinase A and G protein-coupled receptor kinase 2, leading to its inactivation. Phd was originally isolated from the retina, where it is highly expressed and has been implicated to play an important role in light adaptation. It is also found in the pineal gland, liver, spleen, striated muscle and the brain. The C-terminal domain of Phd adopts a thioredoxin fold, but it does not contain a CXXC motif. Phd interacts with G protein beta mostly through the N-terminal helical domain.


Pssm-ID: 239285  Cd Length: 175  Bit Score: 244.51  E-value: 3.97e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664720  60 QQSSTNTGPKGVVKDWQRFKQleaerrdeterqrlalakkltitattsaedeerkrQEELDAELDELMS--EDFLQQYQK 137
Cdd:cd02987   1 EGSGTNTGPKGVINDWRKFKQ-----------------------------------LKESEQEDDDDDEdkEEFLQQYRE 45

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664720 138 QRMAEMLRQTGHHQQFGQVQQLTSHEEFLACVEQENKHTTIIIHIYERQLAACATLNKCLDSLASDYPSIKFAKICSSVA 217
Cdd:cd02987  46 QRMQEMHAKLPFGRRFGKVYELDSGEQFLDAIDKEGKDTTVVVHIYEPGIPGCAALNSSLLCLAAEYPAVKFCKIRASAT 125

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 24664720 218 GMSRDFRTKGLPALLVYKAQAVIGNFVRLTDDLSDDFFASDVESFLIEHG 267
Cdd:cd02987 126 GASDEFDTDALPALLVYKGGELIGNFVRVTEDLGEDFDAEDLESFLVEYG 175
Phosducin pfam02114
Phosducin;
63-275 7.53e-64

Phosducin;


Pssm-ID: 251094 [Multi-domain]  Cd Length: 265  Bit Score: 201.07  E-value: 7.53e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664720    63 STNTGPKGVVKDWQRFKQLEAERRDETERQRLALAKKLTITATTSA-EDEERKRQEELDAELDELMS------------- 128
Cdd:pfam02114  20 ASHTGPKGVINDWRKFKQLESEDRDEQAHEKEEIIKKLSMSCRSHLdEEEEQQDDKDLKEKFSGKMSlkecelidkdkdd 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664720   129 EDFLQQYQKQRMAEMLRQTGHHQQFGQVQQLTSHEEFLACVEQENKHTTIIIHIYERQLAACATLNKCLDSLASDYPSIK 208
Cdd:pfam02114 100 EECLQKYRKQCMDDMHQKLHFGPQFGFVLEIESGEGFLDMIDKEQKITLIMVHIYEDGIKGCDALNGCLICLAAEYPMVK 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24664720   209 FAKICSSVAGMSRDFRTKGLPALLVYKAQAVIGNFVRLTDDLSDDFFASDVESFLIEHGIIVDRALY 275
Cdd:pfam02114 180 FCKIKASNIGAGDRFSRDALPALLIYKAGELIGNFIRVTDQLAEDFFAGDLEAFLNEFGLLPEKEMH 246
Phd_like cd02957
Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as ...
 151-263 6.69e-40

Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as cytosolic regulators of G protein functions. Phd and PhLPs specifically bind G protein betagamma (Gbg)-subunits with high affinity, resulting in the solubilization of Gbg from the plasma membrane and impeding G protein-mediated signal transduction by inhibiting the formation of a functional G protein trimer (G protein alphabetagamma). Phd also inhibits the GTPase activity of G protein alpha. Phd can be phosphorylated by protein kinase A and G protein-coupled receptor kinase 2, leading to its inactivation. Phd was originally isolated from the retina, where it is highly expressed and has been implicated to play an important role in light adaptation. It is also found in the pineal gland, liver, spleen, striated muscle and the brain. The C-terminal domain of Phd adopts a thioredoxin fold, but it does not contain a CXXC motif. Phd interacts with G protein beta mostly through the N-terminal helical domain. Also included in this family is a PhLP characterized as a viral inhibitor of apoptosis (IAP)-associated factor, named VIAF, that functions in caspase activation during apoptosis.


Pssm-ID: 239255 [Multi-domain]  Cd Length: 113  Bit Score: 134.60  E-value: 6.69e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664720 151 QQFGQVQQLTShEEFLACVEQENKHTTIIIHIYERQLAACATLNKCLDSLASDYPSIKFAKICSSVAGMSRDFRTKGLPA 230
Cdd:cd02957   1 KGFGEVREISS-KEFLEEVTKASKGTRVVVHFYEPGFPRCKILDSHLEELAAKYPETKFVKINAEKAFLVNYLDIKVLPT 79

                        90       100       110
                ....*....|....*....|....*....|...
gi 24664720 231 LLVYKAQAVIGNFVRLTDDLSDDFFASDVESFL 263
Cdd:cd02957  80 LLVYKNGELIDNIVGFEELGGDDFTTEDLEKFL 112
Phd_like_VIAF cd02988
Phosducin (Phd)-like family, Viral inhibitor of apoptosis (IAP)-associated factor (VIAF) ...
 88-246 8.96e-25

Phosducin (Phd)-like family, Viral inhibitor of apoptosis (IAP)-associated factor (VIAF) subfamily; VIAF is a Phd-like protein that functions in caspase activation during apoptosis. It was identified as an IAP binding protein through a screen of a human B-cell library using a prototype IAP. VIAF lacks a consensus IAP binding motif and while it does not function as an IAP antagonist, it still plays a regulatory role in the complete activation of caspases. VIAF itself is a substrate for IAP-mediated ubiquitination, suggesting that it may be a target of IAPs in the prevention of cell death. The similarity of VIAF to Phd points to a potential role distinct from apoptosis regulation. Phd functions as a cytosolic regulator of G protein by specifically binding to G protein betagamma (Gbg)-subunits. The C-terminal domain of Phd adopts a thioredoxin fold, but it does not contain a CXXC motif. Phd interacts with G protein beta mostly through the N-terminal helical domain.


Pssm-ID: 239286 [Multi-domain]  Cd Length: 192  Bit Score: 97.72  E-value: 8.96e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664720  88 ETERQRLALAKKLTITATTSAEDEERKRQEELDAELDELMSEDFLQQYQKQRMAEMlRQTGHHQQFGQVQQLtSHEEFLA 167
Cdd:cd02988  17 PPSPKEEEEEALELAIQEAHENALEKKLLDELDEELDEEEDDRFLEEYRRKRLAEM-KALAEKSKFGEVYEI-SKPDYVR 94

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24664720 168 CVEQENKHTTIIIHIYERQLAACATLNKCLDSLASDYPSIKFAKICSSVAgmSRDFRTKGLPALLVYKAQAVIGNFVRL 246
Cdd:cd02988  95 EVTEASKDTWVVVHLYKDGIPLCRLLNQHLSELARKFPDTKFVKIISTQC--IPNYPDKNLPTILVYRNGDIVKQFIGL 171
Phd_like_TxnDC9 cd02989
Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; ...
 151-263 1.83e-04

Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; composed of predominantly uncharacterized eukaryotic proteins, containing a TRX-like domain without the redox active CXXC motif. The gene name for the human protein is TxnDC9. The two characterized members are described as Phd-like proteins, PLP1 of Saccharomyces cerevisiae and PhLP3 of Dictyostelium discoideum. Gene disruption experiments show that both PLP1 and PhLP3 are non-essential proteins. Unlike Phd and most Phd-like proteins, members of this group do not contain the Phd N-terminal helical domain which is implicated in binding to the G protein betagamma subunit.


Pssm-ID: 239287  Cd Length: 113  Bit Score: 40.25  E-value: 1.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664720 151 QQFGQVQQLTSHEEFLACVEQENKhttIIIHIYERQLAACATLNKCLDSLASDYPSIKFAKI----CSSVAgmsRDFRTK 226
Cdd:cd02989   1 KGHGKYREVSDEKEFFEIVKSSER---VVCHFYHPEFFRCKIMDKHLEILAKKHLETKFIKVnaekAPFLV---EKLNIK 74

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 24664720 227 GLPALLVYKAQAVIGNFVRLtDDL--SDDFFASDVESFL 263
Cdd:cd02989  75 VLPTVILFKNGKTVDRIVGF-EELggKDDFSTETLEKRL 112
PTZ00051 PTZ00051
thioredoxin; Provisional
 156-249 1.07e-03

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 37.55  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664720  156 VQQLTSHEEFLACVEQEnkhTTIIIHIYERQLAACATLNKCLDSLASDYPSIKFAKI-CSSVAGMSRDFRTKGLPALLVY 234
Cdd:PTZ00051   2 VHIVTSQAEFESTLSQN---ELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVdVDELSEVAEKENITSMPTFKVF 78

                         90
                 ....*....|....*
gi 24664720  235 KAQAVIGNFVRLTDD 249
Cdd:PTZ00051  79 KNGSVVDTLLGANDE 93
 
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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