NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|12408668|ref|NP_072098|]
View 

phosducin isoform b [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Phosducin super family cl28441
Phosducin;
4-194 1.04e-117

Phosducin;


The actual alignment was detected with superfamily member pfam02114:

Pssm-ID: 251094 [Multi-domain]  Cd Length: 265  Bit Score: 334.73  E-value: 1.04e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408668     4 PQSRNGKDSKERVSRKMSIQEYELIHKEKEDENCLRKYRRQCMQDMHQKLSFGPRYGFVYELETGKQFLETIEKELKITT 83
Cdd:pfam02114  69 EEQQDDKDLKEKFSGKMSLKECELIDKDKDDEECLQKYRKQCMDDMHQKLHFGPQFGFVLEIESGEGFLDMIDKEQKITL 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408668    84 IVVHIYEDGIKGCDALNSSLTCLAAEYPIVKFCKIKASNTGAGDRFSLDVLPTLLIYKGGELISNFISVAEQFAEEFFAG 163
Cdd:pfam02114 149 IMVHIYEDGIKGCDALNGCLICLAAEYPMVKFCKIKASNIGAGDRFSRDALPALLIYKAGELIGNFIRVTDQLAEDFFAG 228

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 12408668   164 DVESFLNEYGLLPEREVHVLEHTKI------EEEDVE 194
Cdd:pfam02114 229 DLEAFLNEFGLLPEKEMHVLEQTNMsatchsEDEDLE 265
 
Name Accession Description Interval E-value
Phosducin pfam02114
Phosducin;
4-194 1.04e-117

Phosducin;


Pssm-ID: 251094 [Multi-domain]  Cd Length: 265  Bit Score: 334.73  E-value: 1.04e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408668     4 PQSRNGKDSKERVSRKMSIQEYELIHKEKEDENCLRKYRRQCMQDMHQKLSFGPRYGFVYELETGKQFLETIEKELKITT 83
Cdd:pfam02114  69 EEQQDDKDLKEKFSGKMSLKECELIDKDKDDEECLQKYRKQCMDDMHQKLHFGPQFGFVLEIESGEGFLDMIDKEQKITL 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408668    84 IVVHIYEDGIKGCDALNSSLTCLAAEYPIVKFCKIKASNTGAGDRFSLDVLPTLLIYKGGELISNFISVAEQFAEEFFAG 163
Cdd:pfam02114 149 IMVHIYEDGIKGCDALNGCLICLAAEYPMVKFCKIKASNIGAGDRFSRDALPALLIYKAGELIGNFIRVTDQLAEDFFAG 228

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 12408668   164 DVESFLNEYGLLPEREVHVLEHTKI------EEEDVE 194
Cdd:pfam02114 229 DLEAFLNEFGLLPEKEMHVLEQTNMsatchsEDEDLE 265
Phd_like_Phd cd02987
Phosducin (Phd)-like family, Phd subfamily; Phd is a cytosolic regulator of G protein ...
 10-173 9.84e-83

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: 242.58  E-value: 9.84e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408668  10 KDSKERVSRKMSIQEYELIHKEKEDenCLRKYRRQCMQDMHQKLSFGPRYGFVYELETGKQFLETIEKELKITTIVVHIY 89
Cdd:cd02987  14 NDWRKFKQLKESEQEDDDDDEDKEE--FLQQYREQRMQEMHAKLPFGRRFGKVYELDSGEQFLDAIDKEGKDTTVVVHIY 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408668  90 EDGIKGCDALNSSLTCLAAEYPIVKFCKIKASNTGAGDRFSLDVLPTLLIYKGGELISNFISVAEQFAEEFFAGDVESFL 169
Cdd:cd02987  92 EPGIPGCAALNSSLLCLAAEYPAVKFCKIRASATGASDEFDTDALPALLVYKGGELIGNFVRVTEDLGEDFDAEDLESFL 171


                ....
gi 12408668 170 NEYG 173
Cdd:cd02987 172 VEYG 175
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 106-172 2.98e-03

Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 35.95  E-value: 2.98e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12408668 106 LAAEY-PIVKFCKIKA-SNTGAGDRFSLDVLPTLLIYKGGELISNFISVAEqfaeeffAGDVESFLNEY 172
Cdd:COG3118  43 LAAEYgGKVKFVKVDVdENPELAAQFGVRSIPTLLLFKDGQPVDRFVGALP-------KEQLREFLDKV 104
 
Name Accession Description Interval E-value
Phosducin pfam02114
Phosducin;
4-194 1.04e-117

Phosducin;


Pssm-ID: 251094 [Multi-domain]  Cd Length: 265  Bit Score: 334.73  E-value: 1.04e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408668     4 PQSRNGKDSKERVSRKMSIQEYELIHKEKEDENCLRKYRRQCMQDMHQKLSFGPRYGFVYELETGKQFLETIEKELKITT 83
Cdd:pfam02114  69 EEQQDDKDLKEKFSGKMSLKECELIDKDKDDEECLQKYRKQCMDDMHQKLHFGPQFGFVLEIESGEGFLDMIDKEQKITL 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408668    84 IVVHIYEDGIKGCDALNSSLTCLAAEYPIVKFCKIKASNTGAGDRFSLDVLPTLLIYKGGELISNFISVAEQFAEEFFAG 163
Cdd:pfam02114 149 IMVHIYEDGIKGCDALNGCLICLAAEYPMVKFCKIKASNIGAGDRFSRDALPALLIYKAGELIGNFIRVTDQLAEDFFAG 228

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 12408668   164 DVESFLNEYGLLPEREVHVLEHTKI------EEEDVE 194
Cdd:pfam02114 229 DLEAFLNEFGLLPEKEMHVLEQTNMsatchsEDEDLE 265
Phd_like_Phd cd02987
Phosducin (Phd)-like family, Phd subfamily; Phd is a cytosolic regulator of G protein ...
 10-173 9.84e-83

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: 242.58  E-value: 9.84e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408668  10 KDSKERVSRKMSIQEYELIHKEKEDenCLRKYRRQCMQDMHQKLSFGPRYGFVYELETGKQFLETIEKELKITTIVVHIY 89
Cdd:cd02987  14 NDWRKFKQLKESEQEDDDDDEDKEE--FLQQYREQRMQEMHAKLPFGRRFGKVYELDSGEQFLDAIDKEGKDTTVVVHIY 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408668  90 EDGIKGCDALNSSLTCLAAEYPIVKFCKIKASNTGAGDRFSLDVLPTLLIYKGGELISNFISVAEQFAEEFFAGDVESFL 169
Cdd:cd02987  92 EPGIPGCAALNSSLLCLAAEYPAVKFCKIRASATGASDEFDTDALPALLVYKGGELIGNFVRVTEDLGEDFDAEDLESFL 171


                ....
gi 12408668 170 NEYG 173
Cdd:cd02987 172 VEYG 175
Phd_like cd02957
Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as ...
 57-170 3.32e-45

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: 145.39  E-value: 3.32e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408668  57 PRYGFVYELeTGKQFLETIEKELKITTIVVHIYEDGIKGCDALNSSLTCLAAEYPIVKFCKIKASNTGAGDRFSLDVLPT 136
Cdd:cd02957   1 KGFGEVREI-SSKEFLEEVTKASKGTRVVVHFYEPGFPRCKILDSHLEELAAKYPETKFVKINAEKAFLVNYLDIKVLPT 79

                        90       100       110
                ....*....|....*....|....*....|....
gi 12408668 137 LLIYKGGELISNFISVAEQFAEEFFAGDVESFLN 170
Cdd:cd02957  80 LLVYKNGELIDNIVGFEELGGDDFTTEDLEKFLA 113
Phd_like_VIAF cd02988
Phosducin (Phd)-like family, Viral inhibitor of apoptosis (IAP)-associated factor (VIAF) ...
 30-173 5.35e-22

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: 88.09  E-value: 5.35e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408668  30 KEKEDENCLRKYRRQCMQDMhQKLSFGPRYGFVYELeTGKQFLETIEKELKITTIVVHIYEDGIKGCDALNSSLTCLAAE 109
Cdd:cd02988  53 DEEEDDRFLEEYRRKRLAEM-KALAEKSKFGEVYEI-SKPDYVREVTEASKDTWVVVHLYKDGIPLCRLLNQHLSELARK 130

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408668 110 YPIVKFCKIKASNtgAGDRFSLDVLPTLLIYKGGELISNFISVAEqfaeefFAG------DVESFLNEYG 173
Cdd:cd02988 131 FPDTKFVKIISTQ--CIPNYPDKNLPTILVYRNGDIVKQFIGLLE------FGGmnttmeDLEWLLVQVG 192
Phd_like_TxnDC9 cd02989
Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; ...
 59-146 9.03e-09

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: 51.04  E-value: 9.03e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408668  59 YGFVYELETGKQFLETIEKELKIttiVVHIYEDGIKGCDALNSSLTCLAAEYPIVKFCKIKASNTG-AGDRFSLDVLPTL 137
Cdd:cd02989   3 HGKYREVSDEKEFFEIVKSSERV---VCHFYHPEFFRCKIMDKHLEILAKKHLETKFIKVNAEKAPfLVEKLNIKVLPTV 79


                ....*....
gi 12408668 138 LIYKGGELI 146
Cdd:cd02989  80 ILFKNGKTV 88
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 69-150 5.24e-05

TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins.


Pssm-ID: 239245 [Multi-domain]  Cd Length: 93  Bit Score: 40.62  E-value: 5.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12408668  69 KQFLETIEKELKIttiVVHIYEDGIKGCDALNSSLTCLAAEYPIVKFCKIKA-SNTGAGDRFSLDVLPTLLIYKGGELIS 147
Cdd:cd02947   1 EEFEELIKSAKPV---VVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVdENPELAEEYGVRSIPTFLFFKNGKEVD 77


                ...
gi 12408668 148 NFI 150
Cdd:cd02947  78 RVV 80
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 106-172 2.98e-03

Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 35.95  E-value: 2.98e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12408668 106 LAAEY-PIVKFCKIKA-SNTGAGDRFSLDVLPTLLIYKGGELISNFISVAEqfaeeffAGDVESFLNEY 172
Cdd:COG3118  43 LAAEYgGKVKFVKVDVdENPELAAQFGVRSIPTLLLFKDGQPVDRFVGALP-------KEQLREFLDKV 104
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH