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Conserved domains on  [gi|21706735|gb|AAH34431|]
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PDCL2 protein [Homo sapiens]

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) ...
 8-200 9.98e-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: 276.07  E-value: 9.98e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706735   8 TEWNDILRDFGILPPKEESKDEIEEMVLRL-----QKEAMVKPFEKMTLAQLKEAEDEfneedmQAVETYRKKRLQEWKA 82
Cdd:cd02988   1 TEWNDILRKKGILPPKPPSPKEEEEEALELaiqeaHENALEKKLLDELDEELDEEEDD------RFLEEYRRKRLAEMKA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706735  83 LKKKQKFGELREISGNQYVNEVTNAEEDVWVIIHLYRSSIPMCLLVNQHLSLLARKFPETKFVKAIVNSCIQHYHDNCLP 162
Cdd:cd02988  75 LAEKSKFGEVYEISKPDYVREVTEASKDTWVVVHLYKDGIPLCRLLNQHLSELARKFPDTKFVKIISTQCIPNYPDKNLP 154

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 21706735 163 TIFVYKNGQIEAKFIGIIECGGINLKLEELEWKLAEVG 200
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) ...
 8-200 9.98e-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: 276.07  E-value: 9.98e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706735   8 TEWNDILRDFGILPPKEESKDEIEEMVLRL-----QKEAMVKPFEKMTLAQLKEAEDEfneedmQAVETYRKKRLQEWKA 82
Cdd:cd02988   1 TEWNDILRKKGILPPKPPSPKEEEEEALELaiqeaHENALEKKLLDELDEELDEEEDD------RFLEEYRRKRLAEMKA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706735  83 LKKKQKFGELREISGNQYVNEVTNAEEDVWVIIHLYRSSIPMCLLVNQHLSLLARKFPETKFVKAIVNSCIQHYHDNCLP 162
Cdd:cd02988  75 LAEKSKFGEVYEISKPDYVREVTEASKDTWVVVHLYKDGIPLCRLLNQHLSELARKFPDTKFVKIISTQCIPNYPDKNLP 154

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 21706735 163 TIFVYKNGQIEAKFIGIIECGGINLKLEELEWKLAEVG 200
Cdd:cd02988 155 TILVYRNGDIVKQFIGLLEFGGMNTTMEDLEWLLVQVG 192
Phosducin pfam02114
Phosducin;
28-226 2.41e-15

Phosducin;


Pssm-ID: 251094 [Multi-domain]  Cd Length: 265  Bit Score: 73.18  E-value: 2.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706735    28 DEIEEMvlRLQKEAMVKPFEKMTLAQLKEAEDefNEEDMQAVETYRKKRLQEW-KALKKKQKFGELREI-SGNQYVNEVT 105
Cdd:pfam02114  66 DEEEEQ--QDDKDLKEKFSGKMSLKECELIDK--DKDDEECLQKYRKQCMDDMhQKLHFGPQFGFVLEIeSGEGFLDMID 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706735   106 NAEEDVWVIIHLYRSSIPMCLLVNQHLSLLARKFPETKF--VKAIVNSCIQHYHDNCLPTIFVYKNGQIEAKFIGIIECG 183
Cdd:pfam02114 142 KEQKITLIMVHIYEDGIKGCDALNGCLICLAAEYPMVKFckIKASNIGAGDRFSRDALPALLIYKAGELIGNFIRVTDQL 221

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 21706735   184 GINLKLEELEWKLAEVGAIqtdleenPRKDMvdMMVSSIRNTS 226
Cdd:pfam02114 222 AEDFFAGDLEAFLNEFGLL-------PEKEM--HVLEQTNMSA 255
PTZ00051 PTZ00051
thioredoxin; Provisional
 101-178 2.30e-03

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 36.39  E-value: 2.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706735  101 VNEVTNAEE-------DVWVIIHLYRSSIPMCLLVNQHLSLLARKFPETKFVKAIVNS---CIQHYHDNCLPTIFVYKNG 170
Cdd:PTZ00051   2 VHIVTSQAEfestlsqNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDVDElseVAEKENITSMPTFKVFKNG 81


                 ....*...
gi 21706735  171 QIEAKFIG 178
Cdd:PTZ00051  82 SVVDTLLG 89
 
Name Accession Description Interval E-value
Phd_like_VIAF cd02988
Phosducin (Phd)-like family, Viral inhibitor of apoptosis (IAP)-associated factor (VIAF) ...
 8-200 9.98e-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: 276.07  E-value: 9.98e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706735   8 TEWNDILRDFGILPPKEESKDEIEEMVLRL-----QKEAMVKPFEKMTLAQLKEAEDEfneedmQAVETYRKKRLQEWKA 82
Cdd:cd02988   1 TEWNDILRKKGILPPKPPSPKEEEEEALELaiqeaHENALEKKLLDELDEELDEEEDD------RFLEEYRRKRLAEMKA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706735  83 LKKKQKFGELREISGNQYVNEVTNAEEDVWVIIHLYRSSIPMCLLVNQHLSLLARKFPETKFVKAIVNSCIQHYHDNCLP 162
Cdd:cd02988  75 LAEKSKFGEVYEISKPDYVREVTEASKDTWVVVHLYKDGIPLCRLLNQHLSELARKFPDTKFVKIISTQCIPNYPDKNLP 154

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 21706735 163 TIFVYKNGQIEAKFIGIIECGGINLKLEELEWKLAEVG 200
Cdd:cd02988 155 TILVYRNGDIVKQFIGLLEFGGMNTTMEDLEWLLVQVG 192
Phd_like cd02957
Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as ...
 87-197 2.30e-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: 147.70  E-value: 2.30e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706735  87 QKFGELREISGNQYVNEVTNAEEDVWVIIHLYRSSIPMCLLVNQHLSLLARKFPETKFVKAIV-NSCIQHYHDN-CLPTI 164
Cdd:cd02957   1 KGFGEVREISSKEFLEEVTKASKGTRVVVHFYEPGFPRCKILDSHLEELAAKYPETKFVKINAeKAFLVNYLDIkVLPTL 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 21706735 165 FVYKNGQIEAKFIGIIECGGINLKLEELEWKLA 197
Cdd:cd02957  81 LVYKNGELIDNIVGFEELGGDDFTTEDLEKFLA 113
Phd_like_Phd cd02987
Phosducin (Phd)-like family, Phd subfamily; Phd is a cytosolic regulator of G protein ...
 53-181 2.88e-26

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: 100.44  E-value: 2.88e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706735  53 QLKEAEDEF---NEEDMQAVETYRKKRLQEWKA-LKKKQKFGELREI-SGNQYVNEVTNAEEDVWVIIHLYRSSIPMCLL 127
Cdd:cd02987  21 QLKESEQEDdddDEDKEEFLQQYREQRMQEMHAkLPFGRRFGKVYELdSGEQFLDAIDKEGKDTTVVVHIYEPGIPGCAA 100

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21706735 128 VNQHLSLLARKFPETKFVKAIV-NSCIQHYHDN-CLPTIFVYKNGQIEAKFIGIIE 181
Cdd:cd02987 101 LNSSLLCLAAEYPAVKFCKIRAsATGASDEFDTdALPALLVYKGGELIGNFVRVTE 156
Phd_like_TxnDC9 cd02989
Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; ...
 87-197 1.16e-16

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: 73.38  E-value: 1.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706735  87 QKFGELREISGNQYVNEVTNAEEDVwvIIHLYRSSIPMCLLVNQHLSLLARKFPETKFVKAIVNSC---IQHYHDNCLPT 163
Cdd:cd02989   1 KGHGKYREVSDEKEFFEIVKSSERV--VCHFYHPEFFRCKIMDKHLEILAKKHLETKFIKVNAEKApflVEKLNIKVLPT 78

                        90       100       110
                ....*....|....*....|....*....|....*
gi 21706735 164 IFVYKNGQIEAKFIGIIECGGI-NLKLEELEWKLA 197
Cdd:cd02989  79 VILFKNGKTVDRIVGFEELGGKdDFSTETLEKRLA 113
Phosducin pfam02114
Phosducin;
28-226 2.41e-15

Phosducin;


Pssm-ID: 251094 [Multi-domain]  Cd Length: 265  Bit Score: 73.18  E-value: 2.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706735    28 DEIEEMvlRLQKEAMVKPFEKMTLAQLKEAEDefNEEDMQAVETYRKKRLQEW-KALKKKQKFGELREI-SGNQYVNEVT 105
Cdd:pfam02114  66 DEEEEQ--QDDKDLKEKFSGKMSLKECELIDK--DKDDEECLQKYRKQCMDDMhQKLHFGPQFGFVLEIeSGEGFLDMID 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706735   106 NAEEDVWVIIHLYRSSIPMCLLVNQHLSLLARKFPETKF--VKAIVNSCIQHYHDNCLPTIFVYKNGQIEAKFIGIIECG 183
Cdd:pfam02114 142 KEQKITLIMVHIYEDGIKGCDALNGCLICLAAEYPMVKFckIKASNIGAGDRFSRDALPALLIYKAGELIGNFIRVTDQL 221

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 21706735   184 GINLKLEELEWKLAEVGAIqtdleenPRKDMvdMMVSSIRNTS 226
Cdd:pfam02114 222 AEDFFAGDLEAFLNEFGLL-------PEKEM--HVLEQTNMSA 255
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 108-190 1.13e-04

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: 39.85  E-value: 1.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706735 108 EEDVWVIIHLYRSSIPMCLLVNQHLSLLARKFPETKFVKAIVNSC---IQHYHDNCLPTIFVYKNGQIEAKFIGIIECGG 184
Cdd:cd02947   8 KSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENpelAEEYGVRSIPTFLFFKNGKEVDRVVGADPKEE 87


                ....*.
gi 21706735 185 INLKLE 190
Cdd:cd02947  88 LEEFLE 93
PTZ00051 PTZ00051
thioredoxin; Provisional
 101-178 2.30e-03

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 36.39  E-value: 2.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21706735  101 VNEVTNAEE-------DVWVIIHLYRSSIPMCLLVNQHLSLLARKFPETKFVKAIVNS---CIQHYHDNCLPTIFVYKNG 170
Cdd:PTZ00051   2 VHIVTSQAEfestlsqNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDVDElseVAEKENITSMPTFKVFKNG 81


                 ....*...
gi 21706735  171 QIEAKFIG 178
Cdd:PTZ00051  82 SVVDTLLG 89
 
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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