NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|28574924|ref|NP_524032|]
View 

viral IAP-associated factor [Drosophila melanogaster]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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) ...
 8-210 2.13e-98

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: 284.93  E-value: 2.13e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574924   8 TEWNDVLRAKGIIGPKAKEaeitedqiQKLMDDAIQRRTDLPLNEGQRDKKIDDMSLDELDELEDsedEAVLEQYRQRRI 87
Cdd:cd02988   1 TEWNDILRKKGILPPKPPS--------PKEEEEEALELAIQEAHENALEKKLLDELDEELDEEED---DRFLEEYRRKRL 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574924  88 AEMRATAEKARFGSVREISGQDYVNEVTKAGEGIWVVLHLYANGVPLCALIHHHMQQLAVRFPQTKFVRSVATTCIPNFP 167
Cdd:cd02988  70 AEMKALAEKSKFGEVYEISKPDYVREVTEASKDTWVVVHLYKDGIPLCRLLNQHLSELARKFPDTKFVKIISTQCIPNYP 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 28574924 168 EKNLPTIFIYHEGALRKQYIGPLELRGDKLTAEELEFMLGQAG 210
Cdd:cd02988 150 DKNLPTILVYRNGDIVKQFIGLLEFGGMNTTMEDLEWLLVQVG 192
 
Name Accession Description Interval E-value
Phd_like_VIAF cd02988
Phosducin (Phd)-like family, Viral inhibitor of apoptosis (IAP)-associated factor (VIAF) ...
 8-210 2.13e-98

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: 284.93  E-value: 2.13e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574924   8 TEWNDVLRAKGIIGPKAKEaeitedqiQKLMDDAIQRRTDLPLNEGQRDKKIDDMSLDELDELEDsedEAVLEQYRQRRI 87
Cdd:cd02988   1 TEWNDILRKKGILPPKPPS--------PKEEEEEALELAIQEAHENALEKKLLDELDEELDEEED---DRFLEEYRRKRL 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574924  88 AEMRATAEKARFGSVREISGQDYVNEVTKAGEGIWVVLHLYANGVPLCALIHHHMQQLAVRFPQTKFVRSVATTCIPNFP 167
Cdd:cd02988  70 AEMKALAEKSKFGEVYEISKPDYVREVTEASKDTWVVVHLYKDGIPLCRLLNQHLSELARKFPDTKFVKIISTQCIPNYP 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 28574924 168 EKNLPTIFIYHEGALRKQYIGPLELRGDKLTAEELEFMLGQAG 210
Cdd:cd02988 150 DKNLPTILVYRNGDIVKQFIGLLEFGGMNTTMEDLEWLLVQVG 192
Phosducin pfam02114
Phosducin;
17-213 1.22e-18

Phosducin;


Pssm-ID: 251094 [Multi-domain]  Cd Length: 265  Bit Score: 82.04  E-value: 1.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574924    17 KGIIGP----KAKEAEITEDQIQKlMDDAIQR-----RTDLPLNEGQRDKK------IDDMSLDELDELE-DSEDEAVLE 80
Cdd:pfam02114  26 KGVINDwrkfKQLESEDRDEQAHE-KEEIIKKlsmscRSHLDEEEEQQDDKdlkekfSGKMSLKECELIDkDKDDEECLQ 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574924    81 QYRQRRIAEMRATAEKA-RFGSVREI-SGQDYVNEVTKAGEGIWVVLHLYANGVPLCALIHHHMQQLAVRFPQTKF--VR 156
Cdd:pfam02114 105 KYRKQCMDDMHQKLHFGpQFGFVLEIeSGEGFLDMIDKEQKITLIMVHIYEDGIKGCDALNGCLICLAAEYPMVKFckIK 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 28574924   157 SVATTCIPNFPEKNLPTIFIYHEGALRKQYIGPLELRGDKLTAEELEFMLGQAGAVP 213
Cdd:pfam02114 185 ASNIGAGDRFSRDALPALLIYKAGELIGNFIRVTDQLAEDFFAGDLEAFLNEFGLLP 241
 
Name Accession Description Interval E-value
Phd_like_VIAF cd02988
Phosducin (Phd)-like family, Viral inhibitor of apoptosis (IAP)-associated factor (VIAF) ...
 8-210 2.13e-98

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: 284.93  E-value: 2.13e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574924   8 TEWNDVLRAKGIIGPKAKEaeitedqiQKLMDDAIQRRTDLPLNEGQRDKKIDDMSLDELDELEDsedEAVLEQYRQRRI 87
Cdd:cd02988   1 TEWNDILRKKGILPPKPPS--------PKEEEEEALELAIQEAHENALEKKLLDELDEELDEEED---DRFLEEYRRKRL 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574924  88 AEMRATAEKARFGSVREISGQDYVNEVTKAGEGIWVVLHLYANGVPLCALIHHHMQQLAVRFPQTKFVRSVATTCIPNFP 167
Cdd:cd02988  70 AEMKALAEKSKFGEVYEISKPDYVREVTEASKDTWVVVHLYKDGIPLCRLLNQHLSELARKFPDTKFVKIISTQCIPNYP 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 28574924 168 EKNLPTIFIYHEGALRKQYIGPLELRGDKLTAEELEFMLGQAG 210
Cdd:cd02988 150 DKNLPTILVYRNGDIVKQFIGLLEFGGMNTTMEDLEWLLVQVG 192
Phd_like cd02957
Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as ...
 98-206 1.20e-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: 145.39  E-value: 1.20e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574924  98 RFGSVREISGQDYVNEVTKAGEGIWVVLHLYANGVPLCALIHHHMQQLAVRFPQTKFVR-SVATTCIPNFPE-KNLPTIF 175
Cdd:cd02957   2 GFGEVREISSKEFLEEVTKASKGTRVVVHFYEPGFPRCKILDSHLEELAAKYPETKFVKiNAEKAFLVNYLDiKVLPTLL 81

                        90       100       110
                ....*....|....*....|....*....|.
gi 28574924 176 IYHEGALRKQYIGPLELRGDKLTAEELEFML 206
Cdd:cd02957  82 VYKNGELIDNIVGFEELGGDDFTTEDLEKFL 112
Phd_like_Phd cd02987
Phosducin (Phd)-like family, Phd subfamily; Phd is a cytosolic regulator of G protein ...
 61-203 3.58e-24

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: 94.67  E-value: 3.58e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574924  61 DMSLDELDELEDsEDEAVLEQYRQRRIAEMRA-TAEKARFGSVREI-SGQDYVNEVTKAGEGIWVVLHLYANGVPLCALI 138
Cdd:cd02987  23 KESEQEDDDDDE-DKEEFLQQYREQRMQEMHAkLPFGRRFGKVYELdSGEQFLDAIDKEGKDTTVVVHIYEPGIPGCAAL 101

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574924 139 HHHMQQLAVRFPQTKF--VRSVATTCIPNFPEKNLPTIFIYHEGALRKQYIGPLELRGDKLTAEELE 203
Cdd:cd02987 102 NSSLLCLAAEYPAVKFckIRASATGASDEFDTDALPALLVYKGGELIGNFVRVTEDLGEDFDAEDLE 168
Phosducin pfam02114
Phosducin;
17-213 1.22e-18

Phosducin;


Pssm-ID: 251094 [Multi-domain]  Cd Length: 265  Bit Score: 82.04  E-value: 1.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574924    17 KGIIGP----KAKEAEITEDQIQKlMDDAIQR-----RTDLPLNEGQRDKK------IDDMSLDELDELE-DSEDEAVLE 80
Cdd:pfam02114  26 KGVINDwrkfKQLESEDRDEQAHE-KEEIIKKlsmscRSHLDEEEEQQDDKdlkekfSGKMSLKECELIDkDKDDEECLQ 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574924    81 QYRQRRIAEMRATAEKA-RFGSVREI-SGQDYVNEVTKAGEGIWVVLHLYANGVPLCALIHHHMQQLAVRFPQTKF--VR 156
Cdd:pfam02114 105 KYRKQCMDDMHQKLHFGpQFGFVLEIeSGEGFLDMIDKEQKITLIMVHIYEDGIKGCDALNGCLICLAAEYPMVKFckIK 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 28574924   157 SVATTCIPNFPEKNLPTIFIYHEGALRKQYIGPLELRGDKLTAEELEFMLGQAGAVP 213
Cdd:pfam02114 185 ASNIGAGDRFSRDALPALLIYKAGELIGNFIRVTDQLAEDFFAGDLEAFLNEFGLLP 241
Phd_like_TxnDC9 cd02989
Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; ...
 99-207 2.22e-10

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: 56.43  E-value: 2.22e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574924  99 FGSVREISGQDYVNEVTKAGEGiwVVLHLYANGVPLCALIHHHMQQLAVRFPQTKFVRSVATTCiPNFPEK----NLPTI 174
Cdd:cd02989   3 HGKYREVSDEKEFFEIVKSSER--VVCHFYHPEFFRCKIMDKHLEILAKKHLETKFIKVNAEKA-PFLVEKlnikVLPTV 79

                        90       100       110
                ....*....|....*....|....*....|....
gi 28574924 175 FIYHEGALRKQYIGPLELRG-DKLTAEELEFMLG 207
Cdd:cd02989  80 ILFKNGKTVDRIVGFEELGGkDDFSTETLEKRLA 113
 
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