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Conserved domains on  [gi|115497192|ref|NP_001069113|]
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phosducin-like protein 3 [Bos taurus]

Protein Classification

phosducin family protein( domain architecture ID 10122238)

phosducin family protein belonging to the thioredoxin (TRX) superfamily that contains a TRX fold without the redox active CXXC motif, similar to human phosducin-like protein 3, also called viral IAP-associated factor 1, that acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination and degradation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Phd_like_VIAF cd02988
Phosducin (Phd)-like family, Viral inhibitor of apoptosis (IAP)-associated factor (VIAF) ...
 8-203 1.91e-95

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: 277.22  E-value: 1.91e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497192   8 TEWNDILRKKGILPSKEDLKD--LEKEAEEEEQRILQQSIVKTYEDMTLEELEDNEDEfneedeRAIEMYRQQRLAEWKA 85
Cdd:cd02988    1 TEWNDILRKKGILPPKPPSPKeeEEEALELAIQEAHENALEKKLLDELDEELDEEEDD------RFLEEYRRKRLAEMKA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497192  86 TQLKNKFGEVLEISGKDYVQEVTKAGEGLWVILHLYKQGIPLCALINQHLSALARKFPDVKFIKAISTTCIPSYPDRNLP 165
Cdd:cd02988   75 LAEKSKFGEVYEISKPDYVREVTEASKDTWVVVHLYKDGIPLCRLLNQHLSELARKFPDTKFVKIISTQCIPNYPDKNLP 154

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 115497192 166 TVFVYLEGDIKAQFIGPLVFGGMNLTLDELEWKLSESG 203
Cdd:cd02988  155 TILVYRNGDIVKQFIGLLEFGGMNTTMEDLEWLLVQVG 192
 
Name Accession Description Interval E-value
Phd_like_VIAF cd02988
Phosducin (Phd)-like family, Viral inhibitor of apoptosis (IAP)-associated factor (VIAF) ...
 8-203 1.91e-95

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: 277.22  E-value: 1.91e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497192   8 TEWNDILRKKGILPSKEDLKD--LEKEAEEEEQRILQQSIVKTYEDMTLEELEDNEDEfneedeRAIEMYRQQRLAEWKA 85
Cdd:cd02988    1 TEWNDILRKKGILPPKPPSPKeeEEEALELAIQEAHENALEKKLLDELDEELDEEEDD------RFLEEYRRKRLAEMKA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497192  86 TQLKNKFGEVLEISGKDYVQEVTKAGEGLWVILHLYKQGIPLCALINQHLSALARKFPDVKFIKAISTTCIPSYPDRNLP 165
Cdd:cd02988   75 LAEKSKFGEVYEISKPDYVREVTEASKDTWVVVHLYKDGIPLCRLLNQHLSELARKFPDTKFVKIISTQCIPNYPDKNLP 154

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 115497192 166 TVFVYLEGDIKAQFIGPLVFGGMNLTLDELEWKLSESG 203
Cdd:cd02988  155 TILVYRNGDIVKQFIGLLEFGGMNTTMEDLEWLLVQVG 192
Phosducin pfam02114
Phosducin;
72-238 9.50e-12

Phosducin;


Pssm-ID: 251094 [Multi-domain]  Cd Length: 265  Bit Score: 63.16  E-value: 9.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497192   72 IEMYRQQRLAEWKATQLKN-KFGEVLEI-SGKDYVQEVTKAGEGLWVILHLYKQGIPLCALINQHLSALARKFPDVKF-- 147
Cdd:pfam02114 103 LQKYRKQCMDDMHQKLHFGpQFGFVLEIeSGEGFLDMIDKEQKITLIMVHIYEDGIKGCDALNGCLICLAAEYPMVKFck 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497192  148 IKAISTTCIPSYPDRNLPTVFVYLEGDIKAQFIGPLVFGGMNLTLDELEWKLSESGAIktsleenPKKPVEdVLLSAVRC 227
Cdd:pfam02114 183 IKASNIGAGDRFSRDALPALLIYKAGELIGNFIRVTDQLAEDFFAGDLEAFLNEFGLL-------PEKEMH-VLEQTNMS 254

                         170
                  ....*....|.
gi 115497192  228 SVPAKRDSDSE 238
Cdd:pfam02114 255 ATCHSEDEDLE 265
phd_fam TIGR01552
prevent-host-death family protein; This model recognizes a region of about 55 amino acids ...
 82-118 3.17e-03

prevent-host-death family protein; This model recognizes a region of about 55 amino acids toward the N-terminal end of bacterial proteins of about 85 amino acids in length. The best-characterized member is prevent-host-death (phd) of bacteriophage P1, the antidote partner of death-on-curing (doc) (TIGR01550) in an addiction module. Addiction modules prevent plasmid curing by killing the host cell as the longer-lived killing protein persists while the gene for the shorter-lived antidote is lost. Note, however, that relatively few members of this family appear to be plasmid or phage-encoded. Also, there is little overlap, except for phage P1 itself, of species with this family and with the doc family. [Cellular processes, Toxin production and resistance, Mobile and extrachromosomal element functions, Other]


Pssm-ID: 273688  Cd Length: 52  Bit Score: 34.95  E-value: 3.17e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 115497192   82 EWKATQLKNKFGEVLEISGKDYVQEVTKAGEGLWVIL 118
Cdd:TIGR01552   1 SVSLSEAKNKLGELLKRVRDGEPVTITKRGRPVAVLV 37
 
Name Accession Description Interval E-value
Phd_like_VIAF cd02988
Phosducin (Phd)-like family, Viral inhibitor of apoptosis (IAP)-associated factor (VIAF) ...
 8-203 1.91e-95

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: 277.22  E-value: 1.91e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497192   8 TEWNDILRKKGILPSKEDLKD--LEKEAEEEEQRILQQSIVKTYEDMTLEELEDNEDEfneedeRAIEMYRQQRLAEWKA 85
Cdd:cd02988    1 TEWNDILRKKGILPPKPPSPKeeEEEALELAIQEAHENALEKKLLDELDEELDEEEDD------RFLEEYRRKRLAEMKA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497192  86 TQLKNKFGEVLEISGKDYVQEVTKAGEGLWVILHLYKQGIPLCALINQHLSALARKFPDVKFIKAISTTCIPSYPDRNLP 165
Cdd:cd02988   75 LAEKSKFGEVYEISKPDYVREVTEASKDTWVVVHLYKDGIPLCRLLNQHLSELARKFPDTKFVKIISTQCIPNYPDKNLP 154

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 115497192 166 TVFVYLEGDIKAQFIGPLVFGGMNLTLDELEWKLSESG 203
Cdd:cd02988  155 TILVYRNGDIVKQFIGLLEFGGMNTTMEDLEWLLVQVG 192
Phd_like cd02957
Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as ...
 90-200 8.15e-49

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: 156.18  E-value: 8.15e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497192  90 NKFGEVLEISGKDYVQEVTKAGEGLWVILHLYKQGIPLCALINQHLSALARKFPDVKFIKAIST-TCIPSYPDR-NLPTV 167
Cdd:cd02957    1 KGFGEVREISSKEFLEEVTKASKGTRVVVHFYEPGFPRCKILDSHLEELAAKYPETKFVKINAEkAFLVNYLDIkVLPTL 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 115497192 168 FVYLEGDIKAQFIGPLVFGGMNLTLDELEWKLS 200
Cdd:cd02957   81 LVYKNGELIDNIVGFEELGGDDFTTEDLEKFLA 113
Phd_like_Phd cd02987
Phosducin (Phd)-like family, Phd subfamily; Phd is a cytosolic regulator of G protein ...
 70-182 1.56e-18

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: 80.03  E-value: 1.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497192  70 RAIEMYRQQRLAEWKA-TQLKNKFGEVLEI-SGKDYVQEVTKAGEGLWVILHLYKQGIPLCALINQHLSALARKFPDVKF 147
Cdd:cd02987   38 EFLQQYREQRMQEMHAkLPFGRRFGKVYELdSGEQFLDAIDKEGKDTTVVVHIYEPGIPGCAALNSSLLCLAAEYPAVKF 117

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 115497192 148 IKAISTTCIPSYPDRN--LPTVFVYLEGDIKAQFIGP 182
Cdd:cd02987  118 CKIRASATGASDEFDTdaLPALLVYKGGELIGNFVRV 154
Phosducin pfam02114
Phosducin;
72-238 9.50e-12

Phosducin;


Pssm-ID: 251094 [Multi-domain]  Cd Length: 265  Bit Score: 63.16  E-value: 9.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497192   72 IEMYRQQRLAEWKATQLKN-KFGEVLEI-SGKDYVQEVTKAGEGLWVILHLYKQGIPLCALINQHLSALARKFPDVKF-- 147
Cdd:pfam02114 103 LQKYRKQCMDDMHQKLHFGpQFGFVLEIeSGEGFLDMIDKEQKITLIMVHIYEDGIKGCDALNGCLICLAAEYPMVKFck 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497192  148 IKAISTTCIPSYPDRNLPTVFVYLEGDIKAQFIGPLVFGGMNLTLDELEWKLSESGAIktsleenPKKPVEdVLLSAVRC 227
Cdd:pfam02114 183 IKASNIGAGDRFSRDALPALLIYKAGELIGNFIRVTDQLAEDFFAGDLEAFLNEFGLL-------PEKEMH-VLEQTNMS 254

                         170
                  ....*....|.
gi 115497192  228 SVPAKRDSDSE 238
Cdd:pfam02114 255 ATCHSEDEDLE 265
Phd_like_TxnDC9 cd02989
Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; ...
 92-200 4.96e-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: 52.58  E-value: 4.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497192  92 FGEVLEISG-KDYVQEVTKAGEglwVILHLYKQGIPLCALINQHLSALARKFPDVKFIKAISTTCiPSYPDR----NLPT 166
Cdd:cd02989    3 HGKYREVSDeKEFFEIVKSSER---VVCHFYHPEFFRCKIMDKHLEILAKKHLETKFIKVNAEKA-PFLVEKlnikVLPT 78

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 115497192 167 VFVYLEGDIKAQFIGPLVFGGM-NLTLDELEWKLS 200
Cdd:cd02989   79 VILFKNGKTVDRIVGFEELGGKdDFSTETLEKRLA 113
phd_fam TIGR01552
prevent-host-death family protein; This model recognizes a region of about 55 amino acids ...
 82-118 3.17e-03

prevent-host-death family protein; This model recognizes a region of about 55 amino acids toward the N-terminal end of bacterial proteins of about 85 amino acids in length. The best-characterized member is prevent-host-death (phd) of bacteriophage P1, the antidote partner of death-on-curing (doc) (TIGR01550) in an addiction module. Addiction modules prevent plasmid curing by killing the host cell as the longer-lived killing protein persists while the gene for the shorter-lived antidote is lost. Note, however, that relatively few members of this family appear to be plasmid or phage-encoded. Also, there is little overlap, except for phage P1 itself, of species with this family and with the doc family. [Cellular processes, Toxin production and resistance, Mobile and extrachromosomal element functions, Other]


Pssm-ID: 273688  Cd Length: 52  Bit Score: 34.95  E-value: 3.17e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 115497192   82 EWKATQLKNKFGEVLEISGKDYVQEVTKAGEGLWVIL 118
Cdd:TIGR01552   1 SVSLSEAKNKLGELLKRVRDGEPVTITKRGRPVAVLV 37
 
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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