phosducin [Mus musculus]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| Phosducin super family | cl28441 | Phosducin; |
1-244 | 2.65e-139 | |||||
Phosducin; The actual alignment was detected with superfamily member pfam02114: Pssm-ID: 251094 [Multi-domain] Cd Length: 265 Bit Score: 391.35 E-value: 2.65e-139
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| Name | Accession | Description | Interval | E-value | |||||
| Phosducin | pfam02114 | Phosducin; |
1-244 | 2.65e-139 | |||||
Phosducin; Pssm-ID: 251094 [Multi-domain] Cd Length: 265 Bit Score: 391.35 E-value: 2.65e-139
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| Phd_like_Phd | cd02987 | Phosducin (Phd)-like family, Phd subfamily; Phd is a cytosolic regulator of G protein ... |
14-223 | 3.10e-91 | |||||
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: 266.08 E-value: 3.10e-91
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| CnoX | COG3118 | Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ... |
117-208 | 1.72e-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: 37.11 E-value: 1.72e-03
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| PTZ00051 | PTZ00051 | thioredoxin; Provisional |
112-200 | 3.46e-03 | |||||
thioredoxin; Provisional Pssm-ID: 173347 [Multi-domain] Cd Length: 98 Bit Score: 36.01 E-value: 3.46e-03
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| Name | Accession | Description | Interval | E-value | |||||
| Phosducin | pfam02114 | Phosducin; |
1-244 | 2.65e-139 | |||||
Phosducin; Pssm-ID: 251094 [Multi-domain] Cd Length: 265 Bit Score: 391.35 E-value: 2.65e-139
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| Phd_like_Phd | cd02987 | Phosducin (Phd)-like family, Phd subfamily; Phd is a cytosolic regulator of G protein ... |
14-223 | 3.10e-91 | |||||
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: 266.08 E-value: 3.10e-91
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| Phd_like | cd02957 | Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as ... |
107-220 | 4.58e-44 | |||||
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: 144.23 E-value: 4.58e-44
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| Phd_like_VIAF | cd02988 | Phosducin (Phd)-like family, Viral inhibitor of apoptosis (IAP)-associated factor (VIAF) ... |
43-223 | 5.79e-20 | |||||
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: 84.24 E-value: 5.79e-20
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| Phd_like_TxnDC9 | cd02989 | Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; ... |
109-196 | 5.87e-06 | |||||
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: 44.10 E-value: 5.87e-06
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| TRX_family | cd02947 | TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ... |
119-200 | 9.97e-06 | |||||
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: 42.93 E-value: 9.97e-06
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| CnoX | COG3118 | Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ... |
117-208 | 1.72e-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: 37.11 E-value: 1.72e-03
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| PTZ00051 | PTZ00051 | thioredoxin; Provisional |
112-200 | 3.46e-03 | |||||
thioredoxin; Provisional Pssm-ID: 173347 [Multi-domain] Cd Length: 98 Bit Score: 36.01 E-value: 3.46e-03
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