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Conserved domains on  [gi|18104959|ref|NP_005774|]
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thioredoxin domain-containing protein 9 [Homo sapiens]

Protein Classification

thioredoxin domain-containing protein( domain architecture ID 10122241)

thioredoxin (TRX) domain-containing protein belonging to the phosducin family contains a TRX fold domain without the redox active CXXC motif, similar to human thioredoxin domain-containing protein 9 (TXND9), which forms ternary complexes with the chaperonin TCP1 complex and significantly reducing its ATPase activity, and thus negatively impacting protein folding, including that of actin or tubulin

CATH:  3.40.30.10
PubMed:  12074972|10049365|15558583
SCOP:  4000237

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Phd_like_TxnDC9 cd02989
Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; ...
 68-180 1.65e-68

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: 205.50  E-value: 1.65e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104959  68 KGHGEYREIPSERDFFQEVKESENVVCHFYRDSTFRCKILDRHLAILSKKHLETKFLKLNVEKAPFLCERLHIKVIPTLA 147
Cdd:cd02989   1 KGHGKYREVSDEKEFFEIVKSSERVVCHFYHPEFFRCKIMDKHLEILAKKHLETKFIKVNAEKAPFLVEKLNIKVLPTVI 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 18104959 148 LLKDGKTQDYVVGFTDLGNTDDFTTETLEWRLG 180
Cdd:cd02989  81 LFKNGKTVDRIVGFEELGGKDDFSTETLEKRLA 113
 
Name Accession Description Interval E-value
Phd_like_TxnDC9 cd02989
Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; ...
 68-180 1.65e-68

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: 205.50  E-value: 1.65e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104959  68 KGHGEYREIPSERDFFQEVKESENVVCHFYRDSTFRCKILDRHLAILSKKHLETKFLKLNVEKAPFLCERLHIKVIPTLA 147
Cdd:cd02989   1 KGHGKYREVSDEKEFFEIVKSSERVVCHFYHPEFFRCKIMDKHLEILAKKHLETKFIKVNAEKAPFLVEKLNIKVLPTVI 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 18104959 148 LLKDGKTQDYVVGFTDLGNTDDFTTETLEWRLG 180
Cdd:cd02989  81 LFKNGKTVDRIVGFEELGGKDDFSTETLEKRLA 113
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 78-163 1.58e-10

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: 56.37  E-value: 1.58e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104959  78 SERDFFQEVKESEN-VVCHFYRDSTFRCKILDRHLAILSKKHLET-KFLKLNVEKAPFLCERLHIKVIPTLALLKDGKTQ 155
Cdd:COG3118   6 TDENFEEEVLESDKpVLVDFWAPWCGPCKMLAPVLEELAAEYGGKvKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQPV 85


                ....*...
gi 18104959 156 DYVVGFTD 163
Cdd:COG3118  86 DRFVGALP 93
PTZ00051 PTZ00051
thioredoxin; Provisional
 74-165 3.00e-08

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 49.87  E-value: 3.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104959   74 REIPSERDFFQEVKESENVVCHFYRDSTFRCKILDRHLAILSKKHLETKFLKLNVEKAPFLCERLHIKVIPTLALLKDGK 153
Cdd:PTZ00051   3 HIVTSQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDVDELSEVAEKENITSMPTFKVFKNGS 82

                         90
                 ....*....|..
gi 18104959  154 TQDYVVGFTDLG 165
Cdd:PTZ00051  83 VVDTLLGANDEA 94
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 78-161 2.67e-06

thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport]


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 44.59  E-value: 2.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104959    78 SERDFFQEVKESE-NVVCHFYRDSTFRCKILDRHLAILSKK-HLETKFLKLNVEKAPFLCERLHIKVIPTLALLKDGKTQ 155
Cdd:TIGR01068   2 TDANFDETIASSDkPVLVDFWAPWCGPCKMIAPILEELAKEyEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKEV 81


                  ....*.
gi 18104959   156 DYVVGF 161
Cdd:TIGR01068  82 DRSVGA 87
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 81-160 1.06e-05

Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 42.99  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104959    81 DFFQEV--KESENVVCHFYRDSTFRCKILDRHLAILSKKHLET-KFLKLNVEKAPFLCERLHIKVIPTLALLKDGKTQDY 157
Cdd:pfam00085   8 ANFDEVvqKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNvVFAKVDVDENPDLASKYGVRGYPTLIFFKNGQPVDD 87


                  ...
gi 18104959   158 VVG 160
Cdd:pfam00085  88 YVG 90
 
Name Accession Description Interval E-value
Phd_like_TxnDC9 cd02989
Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; ...
 68-180 1.65e-68

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: 205.50  E-value: 1.65e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104959  68 KGHGEYREIPSERDFFQEVKESENVVCHFYRDSTFRCKILDRHLAILSKKHLETKFLKLNVEKAPFLCERLHIKVIPTLA 147
Cdd:cd02989   1 KGHGKYREVSDEKEFFEIVKSSERVVCHFYHPEFFRCKIMDKHLEILAKKHLETKFIKVNAEKAPFLVEKLNIKVLPTVI 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 18104959 148 LLKDGKTQDYVVGFTDLGNTDDFTTETLEWRLG 180
Cdd:cd02989  81 LFKNGKTVDRIVGFEELGGKDDFSTETLEKRLA 113
Phd_like cd02957
Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as ...
 68-179 6.44e-48

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: 153.48  E-value: 6.44e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104959  68 KGHGEYREIpSERDFFQEVKES---ENVVCHFYRDSTFRCKILDRHLAILSKKHLETKFLKLNVEKApFLCERLHIKVIP 144
Cdd:cd02957   1 KGFGEVREI-SSKEFLEEVTKAskgTRVVVHFYEPGFPRCKILDSHLEELAAKYPETKFVKINAEKA-FLVNYLDIKVLP 78

                        90       100       110
                ....*....|....*....|....*....|....*
gi 18104959 145 TLALLKDGKTQDYVVGFTDLGNtDDFTTETLEWRL 179
Cdd:cd02957  79 TLLVYKNGELIDNIVGFEELGG-DDFTTEDLEKFL 112
Phd_like_VIAF cd02988
Phosducin (Phd)-like family, Viral inhibitor of apoptosis (IAP)-associated factor (VIAF) ...
 15-180 2.76e-17

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: 76.54  E-value: 2.76e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104959  15 EHQLLQTTKLVEEHLDSEIQKLDQMDEDE--LERLKEKRLQALRKAQQQKQewlskgHGEYREIpSERDFFQEVKE-SEN 91
Cdd:cd02988  30 LAIQEAHENALEKKLLDELDEELDEEEDDrfLEEYRRKRLAEMKALAEKSK------FGEVYEI-SKPDYVREVTEaSKD 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104959  92 --VVCHFYRDSTFRCKILDRHLAILSKKHLETKFLKLNVEKApflCERLHIKVIPTLALLKDGKTQDYVVGFTDLGNtDD 169
Cdd:cd02988 103 twVVVHLYKDGIPLCRLLNQHLSELARKFPDTKFVKIISTQC---IPNYPDKNLPTILVYRNGDIVKQFIGLLEFGG-MN 178

                       170
                ....*....|.
gi 18104959 170 FTTETLEWRLG 180
Cdd:cd02988 179 TTMEDLEWLLV 189
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 81-161 4.42e-15

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: 67.97  E-value: 4.42e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104959  81 DFFQEVKESENVVCHFYRDSTFRCKILDRHLAILSKKHLETKFLKLNVEKAPFLCERLHIKVIPTLALLKDGKTQDYVVG 160
Cdd:cd02947   2 EFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVVG 81


                .
gi 18104959 161 F 161
Cdd:cd02947  82 A 82
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 78-163 1.58e-10

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: 56.37  E-value: 1.58e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104959  78 SERDFFQEVKESEN-VVCHFYRDSTFRCKILDRHLAILSKKHLET-KFLKLNVEKAPFLCERLHIKVIPTLALLKDGKTQ 155
Cdd:COG3118   6 TDENFEEEVLESDKpVLVDFWAPWCGPCKMLAPVLEELAAEYGGKvKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQPV 85


                ....*...
gi 18104959 156 DYVVGFTD 163
Cdd:COG3118  86 DRFVGALP 93
Phd_like_Phd cd02987
Phosducin (Phd)-like family, Phd subfamily; Phd is a cytosolic regulator of G protein ...
 27-176 5.98e-10

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: 56.53  E-value: 5.98e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104959  27 EHLDSEIQKLDQMDEDE---LERLKEKRLQALRKAQQQKQEWlskghGEYREIPSERDFFQEV-KESEN--VVCHFYRDS 100
Cdd:cd02987  20 KQLKESEQEDDDDDEDKeefLQQYREQRMQEMHAKLPFGRRF-----GKVYELDSGEQFLDAIdKEGKDttVVVHIYEPG 94

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18104959 101 TFRCKILDRHLAILSKKHLETKFLKLNvEKAPFLCERLHIKVIPTLALLKDGKTQDYVVGFT-DLGntDDFTTETLE 176
Cdd:cd02987  95 IPGCAALNSSLLCLAAEYPAVKFCKIR-ASATGASDEFDTDALPALLVYKGGELIGNFVRVTeDLG--EDFDAEDLE 168
PTZ00051 PTZ00051
thioredoxin; Provisional
 74-165 3.00e-08

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 49.87  E-value: 3.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104959   74 REIPSERDFFQEVKESENVVCHFYRDSTFRCKILDRHLAILSKKHLETKFLKLNVEKAPFLCERLHIKVIPTLALLKDGK 153
Cdd:PTZ00051   3 HIVTSQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDVDELSEVAEKENITSMPTFKVFKNGS 82

                         90
                 ....*....|..
gi 18104959  154 TQDYVVGFTDLG 165
Cdd:PTZ00051  83 VVDTLLGANDEA 94
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 78-161 2.67e-06

thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport]


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 44.59  E-value: 2.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104959    78 SERDFFQEVKESE-NVVCHFYRDSTFRCKILDRHLAILSKK-HLETKFLKLNVEKAPFLCERLHIKVIPTLALLKDGKTQ 155
Cdd:TIGR01068   2 TDANFDETIASSDkPVLVDFWAPWCGPCKMIAPILEELAKEyEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKEV 81


                  ....*.
gi 18104959   156 DYVVGF 161
Cdd:TIGR01068  82 DRSVGA 87
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 78-161 3.32e-06

TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT contains an N-terminal TRX-like domain, which does not contain the catalytic CXXC motif, followed by one to three glutaredoxin domains. The TRX-like domain is required for interaction with PKC theta. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli.


Pssm-ID: 239282 [Multi-domain]  Cd Length: 97  Bit Score: 44.18  E-value: 3.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104959  78 SERDFFQEVKESEN--VVCHFYRDSTFRCKILDRHLAILSKK-HLETKFLKLNVEKAPFLCERLHIKVIPTLALLKDGKT 154
Cdd:cd02984   1 SEEEFEELLKSDASklLVLHFWAPWAEPCKQMNQVFEELAKEaFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTI 80


                ....*..
gi 18104959 155 QDYVVGF 161
Cdd:cd02984  81 VDRVSGA 87
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 81-160 1.06e-05

Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 42.99  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104959    81 DFFQEV--KESENVVCHFYRDSTFRCKILDRHLAILSKKHLET-KFLKLNVEKAPFLCERLHIKVIPTLALLKDGKTQDY 157
Cdd:pfam00085   8 ANFDEVvqKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNvVFAKVDVDENPDLASKYGVRGYPTLIFFKNGQPVDD 87


                  ...
gi 18104959   158 VVG 160
Cdd:pfam00085  88 YVG 90
Phosducin pfam02114
Phosducin;
32-173 3.69e-03

Phosducin;


Pssm-ID: 251094 [Multi-domain]  Cd Length: 265  Bit Score: 37.74  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104959    32 EIQKLDQMDEDElERLKEKRLQALRKAQQQkqewLSKG--HGEYREIPSERDFFQEV---KESENVVCHFYRDSTFRCKI 106
Cdd:pfam02114  89 ECELIDKDKDDE-ECLQKYRKQCMDDMHQK----LHFGpqFGFVLEIESGEGFLDMIdkeQKITLIMVHIYEDGIKGCDA 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18104959   107 LDRHLAILSKKHLETKFLKLNVEKAPfLCERLHIKVIPTLALLKDGKTQDYVVGFTDLGNTDDFTTE 173
Cdd:pfam02114 164 LNGCLICLAAEYPMVKFCKIKASNIG-AGDRFSRDALPALLIYKAGELIGNFIRVTDQLAEDFFAGD 229
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 81-156 7.22e-03

ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like domain. Its gene has been sequenced from several gammaproteobacteria and actinobacteria.


Pssm-ID: 239254 [Multi-domain]  Cd Length: 96  Bit Score: 34.94  E-value: 7.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104959  81 DFFQEVKESEN--VVCHFYRDSTFRCKILDRHLAILSKKHlETKFL--KLNVEKAPFLCERLHIKVIPTLALLKDGKTQD 156
Cdd:cd02956   2 NFQQVLQESTQvpVVVDFWAPRSPPSKELLPLLERLAEEY-QGQFVlaKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVD 80
 
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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