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Conserved domains on  [gi|3916251|gb|AAC78849|]
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phosducin-like protein, partial [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Phosducin super family cl28441
Phosducin;
1-146 1.41e-94

Phosducin;


The actual alignment was detected with superfamily member pfam02114:

Pssm-ID: 251094 [Multi-domain]  Cd Length: 265  Bit Score: 273.87  E-value: 1.41e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3916251      1 MTLKEFAIMNEDQDDEEFLQQYRKQRMEEMRQQLHKGPQFKQVFEISSGEGFLDMIDKEQKSIVIMVHIYEDGIPGTEAM 80
Cdd:pfam02114  85 MSLKECELIDKDKDDEECLQKYRKQCMDDMHQKLHFGPQFGFVLEIESGEGFLDMIDKEQKITLIMVHIYEDGIKGCDAL 164

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3916251     81 NGCMICLAAEYPAVKFCKVKSSVIGASSQFTRNALPALLIYKGGELIGNFVRVTDQLGDDFFAVDL 146
Cdd:pfam02114 165 NGCLICLAAEYPMVKFCKIKASNIGAGDRFSRDALPALLIYKAGELIGNFIRVTDQLAEDFFAGDL 230
 
Name Accession Description Interval E-value
Phosducin pfam02114
Phosducin;
1-146 1.41e-94

Phosducin;


Pssm-ID: 251094 [Multi-domain]  Cd Length: 265  Bit Score: 273.87  E-value: 1.41e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3916251      1 MTLKEFAIMNEDQDDEEFLQQYRKQRMEEMRQQLHKGPQFKQVFEISSGEGFLDMIDKEQKSIVIMVHIYEDGIPGTEAM 80
Cdd:pfam02114  85 MSLKECELIDKDKDDEECLQKYRKQCMDDMHQKLHFGPQFGFVLEIESGEGFLDMIDKEQKITLIMVHIYEDGIKGCDAL 164

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3916251     81 NGCMICLAAEYPAVKFCKVKSSVIGASSQFTRNALPALLIYKGGELIGNFVRVTDQLGDDFFAVDL 146
Cdd:pfam02114 165 NGCLICLAAEYPMVKFCKIKASNIGAGDRFSRDALPALLIYKAGELIGNFIRVTDQLAEDFFAGDL 230
Phd_like_Phd cd02987
Phosducin (Phd)-like family, Phd subfamily; Phd is a cytosolic regulator of G protein ...
 4-146 1.52e-79

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: 232.57  E-value: 1.52e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3916251    4 KEFAIMNEDQDDEE----FLQQYRKQRMEEMRQQLHKGPQFKQVFEISSGEGFLDMIDKEQKSIVIMVHIYEDGIPGTEA 79
Cdd:cd02987  21 QLKESEQEDDDDDEdkeeFLQQYREQRMQEMHAKLPFGRRFGKVYELDSGEQFLDAIDKEGKDTTVVVHIYEPGIPGCAA 100

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3916251   80 MNGCMICLAAEYPAVKFCKVKSSVIGASSQFTRNALPALLIYKGGELIGNFVRVTDQLGDDFFAVDL 146
Cdd:cd02987 101 LNSSLLCLAAEYPAVKFCKIRASATGASDEFDTDALPALLVYKGGELIGNFVRVTEDLGEDFDAEDL 167
 
Name Accession Description Interval E-value
Phosducin pfam02114
Phosducin;
1-146 1.41e-94

Phosducin;


Pssm-ID: 251094 [Multi-domain]  Cd Length: 265  Bit Score: 273.87  E-value: 1.41e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3916251      1 MTLKEFAIMNEDQDDEEFLQQYRKQRMEEMRQQLHKGPQFKQVFEISSGEGFLDMIDKEQKSIVIMVHIYEDGIPGTEAM 80
Cdd:pfam02114  85 MSLKECELIDKDKDDEECLQKYRKQCMDDMHQKLHFGPQFGFVLEIESGEGFLDMIDKEQKITLIMVHIYEDGIKGCDAL 164

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3916251     81 NGCMICLAAEYPAVKFCKVKSSVIGASSQFTRNALPALLIYKGGELIGNFVRVTDQLGDDFFAVDL 146
Cdd:pfam02114 165 NGCLICLAAEYPMVKFCKIKASNIGAGDRFSRDALPALLIYKAGELIGNFIRVTDQLAEDFFAGDL 230
Phd_like_Phd cd02987
Phosducin (Phd)-like family, Phd subfamily; Phd is a cytosolic regulator of G protein ...
 4-146 1.52e-79

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: 232.57  E-value: 1.52e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3916251    4 KEFAIMNEDQDDEE----FLQQYRKQRMEEMRQQLHKGPQFKQVFEISSGEGFLDMIDKEQKSIVIMVHIYEDGIPGTEA 79
Cdd:cd02987  21 QLKESEQEDDDDDEdkeeFLQQYREQRMQEMHAKLPFGRRFGKVYELDSGEQFLDAIDKEGKDTTVVVHIYEPGIPGCAA 100

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3916251   80 MNGCMICLAAEYPAVKFCKVKSSVIGASSQFTRNALPALLIYKGGELIGNFVRVTDQLGDDFFAVDL 146
Cdd:cd02987 101 LNSSLLCLAAEYPAVKFCKIRASATGASDEFDTDALPALLVYKGGELIGNFVRVTEDLGEDFDAEDL 167
Phd_like cd02957
Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as ...
 38-146 1.45e-43

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: 139.23  E-value: 1.45e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3916251   38 PQFKQVFEISSGEgFLDMIDKEQKSIVIMVHIYEDGIPGTEAMNGCMICLAAEYPAVKFCKVKSSVIGASSQFTRNALPA 117
Cdd:cd02957   1 KGFGEVREISSKE-FLEEVTKASKGTRVVVHFYEPGFPRCKILDSHLEELAAKYPETKFVKINAEKAFLVNYLDIKVLPT 79

                        90       100
                ....*....|....*....|....*....
gi 3916251  118 LLIYKGGELIGNFVRVTDQLGDDFFAVDL 146
Cdd:cd02957  80 LLVYKNGELIDNIVGFEELGGDDFTTEDL 108
Phd_like_VIAF cd02988
Phosducin (Phd)-like family, Viral inhibitor of apoptosis (IAP)-associated factor (VIAF) ...
 2-131 2.84e-26

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: 2.84e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3916251    2 TLKEFAIMNEDQDDEEFLQQYRKQRMEEMRQQLHKGpQFKQVFEISsGEGFLDMIDKEQKSIVIMVHIYEDGIPGTEAMN 81
Cdd:cd02988  44 LLDELDEELDEEEDDRFLEEYRRKRLAEMKALAEKS-KFGEVYEIS-KPDYVREVTEASKDTWVVVHLYKDGIPLCRLLN 121

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 3916251   82 GCMICLAAEYPAVKFCKVKSSVigASSQFTRNALPALLIYKGGELIGNFV 131
Cdd:cd02988 122 QHLSELARKFPDTKFVKIISTQ--CIPNYPDKNLPTILVYRNGDIVKQFI 169
 
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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