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Conserved domains on  [gi|16768382|gb|AAL28410|]
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GM03430p [Drosophila melanogaster]

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; ...
 60-171 3.87e-64

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: 194.33  E-value: 3.87e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16768382  60 GHGTYTELADEKEFFEMSKKSPNIVCHFYRDSTERCKIVDMHLKILAAKHVEAKFCKVNAEKTPFLTQRLRIKVIPTIAL 139
Cdd:cd02989   2 GHGKYREVSDEKEFFEIVKSSERVVCHFYHPEFFRCKIMDKHLEILAKKHLETKFIKVNAEKAPFLVEKLNIKVLPTVIL 81

                        90       100       110
                ....*....|....*....|....*....|..
gi 16768382 140 VKDSKTKDFIVGFTDLGNCDDFATEMLEWRIA 171
Cdd:cd02989  82 FKNGKTVDRIVGFEELGGKDDFSTETLEKRLA 113
 
Name Accession Description Interval E-value
Phd_like_TxnDC9 cd02989
Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; ...
 60-171 3.87e-64

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: 194.33  E-value: 3.87e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16768382  60 GHGTYTELADEKEFFEMSKKSPNIVCHFYRDSTERCKIVDMHLKILAAKHVEAKFCKVNAEKTPFLTQRLRIKVIPTIAL 139
Cdd:cd02989   2 GHGKYREVSDEKEFFEIVKSSERVVCHFYHPEFFRCKIMDKHLEILAKKHLETKFIKVNAEKAPFLVEKLNIKVLPTVIL 81

                        90       100       110
                ....*....|....*....|....*....|..
gi 16768382 140 VKDSKTKDFIVGFTDLGNCDDFATEMLEWRIA 171
Cdd:cd02989  82 FKNGKTVDRIVGFEELGGKDDFSTETLEKRLA 113
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 86-154 1.09e-08

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: 50.97  E-value: 1.09e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16768382  86 HFYRDSTERCKIVDMHLKILAAKHVE-AKFCKVNAEKTPFLTQRLRIKVIPTIALVKDSKTKDFIVGFTD 154
Cdd:COG3118  24 DFWAPWCGPCKMLAPVLEELAAEYGGkVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQPVDRFVGALP 93
Phosducin pfam02114
Phosducin;
31-167 5.32e-07

Phosducin;


Pssm-ID: 251094 [Multi-domain]  Cd Length: 265  Bit Score: 48.91  E-value: 5.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16768382    31 DSDDLKVLREQRLREMKDLNNKKQEWLRngHGTYTELADEKEFFEM---SKKSPNIVCHFYRDSTERCKIVDMHLKILAA 107
Cdd:pfam02114  96 DKDDEECLQKYRKQCMDDMHQKLHFGPQ--FGFVLEIESGEGFLDMidkEQKITLIMVHIYEDGIKGCDALNGCLICLAA 173

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16768382   108 KHVEAKFCKVNAEKTPfLTQRLRIKVIPTIALVKDSKTKDFIVGFTD-LGncDDFATEMLE 167
Cdd:pfam02114 174 EYPMVKFCKIKASNIG-AGDRFSRDALPALLIYKAGELIGNFIRVTDqLA--EDFFAGDLE 231
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 68-152 6.15e-05

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: 40.74  E-value: 6.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16768382    68 ADEKEFFEMSKKSP-NIVCHFYRDSTERCKIVDMHLKILAAK-HVEAKFCKVNAEKTPFLTQRLRIKVIPTIALVKDSKT 145
Cdd:TIGR01068   1 LTDANFDETIASSDkPVLVDFWAPWCGPCKMIAPILEELAKEyEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKE 80


                  ....*..
gi 16768382   146 KDFIVGF 152
Cdd:TIGR01068  81 VDRSVGA 87
PRK10996 PRK10996
thioredoxin 2; Provisional
 111-151 2.61e-04

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 39.67  E-value: 2.61e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 16768382  111 EAKFCKVNAEKTPFLTQRLRIKVIPTIALVKDSKTKDFIVG 151
Cdd:PRK10996  84 KVRFVKVNTEAERELSARFRIRSIPTIMIFKNGQVVDMLNG 124
 
Name Accession Description Interval E-value
Phd_like_TxnDC9 cd02989
Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; ...
 60-171 3.87e-64

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: 194.33  E-value: 3.87e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16768382  60 GHGTYTELADEKEFFEMSKKSPNIVCHFYRDSTERCKIVDMHLKILAAKHVEAKFCKVNAEKTPFLTQRLRIKVIPTIAL 139
Cdd:cd02989   2 GHGKYREVSDEKEFFEIVKSSERVVCHFYHPEFFRCKIMDKHLEILAKKHLETKFIKVNAEKAPFLVEKLNIKVLPTVIL 81

                        90       100       110
                ....*....|....*....|....*....|..
gi 16768382 140 VKDSKTKDFIVGFTDLGNCDDFATEMLEWRIA 171
Cdd:cd02989  82 FKNGKTVDRIVGFEELGGKDDFSTETLEKRLA 113
Phd_like cd02957
Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as ...
 59-171 2.26e-43

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: 141.54  E-value: 2.26e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16768382  59 NGHGTYTELaDEKEFFEMSKKSP---NIVCHFYRDSTERCKIVDMHLKILAAKHVEAKFCKVNAEKTpFLTQRLRIKVIP 135
Cdd:cd02957   1 KGFGEVREI-SSKEFLEEVTKASkgtRVVVHFYEPGFPRCKILDSHLEELAAKYPETKFVKINAEKA-FLVNYLDIKVLP 78

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 16768382 136 TIALVKDSKTKDFIVGFTDLGNcDDFATEMLEWRIA 171
Cdd:cd02957  79 TLLVYKNGELIDNIVGFEELGG-DDFTTEDLEKFLA 113
Phd_like_VIAF cd02988
Phosducin (Phd)-like family, Viral inhibitor of apoptosis (IAP)-associated factor (VIAF) ...
 12-174 2.08e-12

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: 63.05  E-value: 2.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16768382  12 AAKTIEQQLDQQ-LDRLDNLDSDD-----LKVLREQRLREMKDLNNKKQewlrngHGTYTELADE---KEFFEMSKKSPn 82
Cdd:cd02988  32 IQEAHENALEKKlLDELDEELDEEeddrfLEEYRRKRLAEMKALAEKSK------FGEVYEISKPdyvREVTEASKDTW- 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16768382  83 IVCHFYRDSTERCKIVDMHLKILAAKHVEAKFCKVNA----EKTPfltqrlrIKVIPTIALVKDSKTKDFIVGFTDLG-- 156
Cdd:cd02988 105 VVVHLYKDGIPLCRLLNQHLSELARKFPDTKFVKIIStqciPNYP-------DKNLPTILVYRNGDIVKQFIGLLEFGgm 177

                       170       180
                ....*....|....*....|
gi 16768382 157 --NCDDfatemLEWRIAHSG 174
Cdd:cd02988 178 ntTMED-----LEWLLVQVG 192
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 71-152 2.05e-11

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: 58.34  E-value: 2.05e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16768382  71 KEFFEMSKKSPNIVCHFYRDSTERCKIVDMHLKILAAKHVEAKFCKVNAEKTPFLTQRLRIKVIPTIALVKDSKTKDFIV 150
Cdd:cd02947   1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVV 80


                ..
gi 16768382 151 GF 152
Cdd:cd02947  81 GA 82
Phd_like_Phd cd02987
Phosducin (Phd)-like family, Phd subfamily; Phd is a cytosolic regulator of G protein ...
 20-167 2.59e-11

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: 60.00  E-value: 2.59e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16768382  20 LDQQLDRLDNLDSDDLKVLREQRLREMKDLNNKKQEWlrnghGTYTELADEKEFFEMSKKSPN---IVCHFYRDSTERCK 96
Cdd:cd02987  25 SEQEDDDDDEDKEEFLQQYREQRMQEMHAKLPFGRRF-----GKVYELDSGEQFLDAIDKEGKdttVVVHIYEPGIPGCA 99

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16768382  97 IVDMHLKILAAKHVEAKFCKVNAEKTPfLTQRLRIKVIPTIALVKDSktkDFIVGFT----DLGncDDFATEMLE 167
Cdd:cd02987 100 ALNSSLLCLAAEYPAVKFCKIRASATG-ASDEFDTDALPALLVYKGG---ELIGNFVrvteDLG--EDFDAEDLE 168
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 86-154 1.09e-08

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: 50.97  E-value: 1.09e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16768382  86 HFYRDSTERCKIVDMHLKILAAKHVE-AKFCKVNAEKTPFLTQRLRIKVIPTIALVKDSKTKDFIVGFTD 154
Cdd:COG3118  24 DFWAPWCGPCKMLAPVLEELAAEYGGkVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQPVDRFVGALP 93
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 70-152 5.01e-07

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: 46.50  E-value: 5.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16768382  70 EKEFFEMSKKSPN--IVCHFYRDSTERCKIVDMHLKILAAK-HVEAKFCKVNAEKTPFLTQRLRIKVIPTIALVKDSKTK 146
Cdd:cd02984   2 EEEFEELLKSDASklLVLHFWAPWAEPCKQMNQVFEELAKEaFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTIV 81


                ....*.
gi 16768382 147 DFIVGF 152
Cdd:cd02984  82 DRVSGA 87
Phosducin pfam02114
Phosducin;
31-167 5.32e-07

Phosducin;


Pssm-ID: 251094 [Multi-domain]  Cd Length: 265  Bit Score: 48.91  E-value: 5.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16768382    31 DSDDLKVLREQRLREMKDLNNKKQEWLRngHGTYTELADEKEFFEM---SKKSPNIVCHFYRDSTERCKIVDMHLKILAA 107
Cdd:pfam02114  96 DKDDEECLQKYRKQCMDDMHQKLHFGPQ--FGFVLEIESGEGFLDMidkEQKITLIMVHIYEDGIKGCDALNGCLICLAA 173

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16768382   108 KHVEAKFCKVNAEKTPfLTQRLRIKVIPTIALVKDSKTKDFIVGFTD-LGncDDFATEMLE 167
Cdd:pfam02114 174 EYPMVKFCKIKASNIG-AGDRFSRDALPALLIYKAGELIGNFIRVTDqLA--EDFFAGDLE 231
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 68-152 6.15e-05

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: 40.74  E-value: 6.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16768382    68 ADEKEFFEMSKKSP-NIVCHFYRDSTERCKIVDMHLKILAAK-HVEAKFCKVNAEKTPFLTQRLRIKVIPTIALVKDSKT 145
Cdd:TIGR01068   1 LTDANFDETIASSDkPVLVDFWAPWCGPCKMIAPILEELAKEyEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKE 80


                  ....*..
gi 16768382   146 KDFIVGF 152
Cdd:TIGR01068  81 VDRSVGA 87
PRK10996 PRK10996
thioredoxin 2; Provisional
 111-151 2.61e-04

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 39.67  E-value: 2.61e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 16768382  111 EAKFCKVNAEKTPFLTQRLRIKVIPTIALVKDSKTKDFIVG 151
Cdd:PRK10996  84 KVRFVKVNTEAERELSARFRIRSIPTIMIFKNGQVVDMLNG 124
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 72-151 5.56e-04

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: 38.02  E-value: 5.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16768382  72 EFFEMSKKSPnIVCHFYRDSTERCKIVDMHLKILAAKHvEAKF--CKVNAEKTPFLTQRLRIKVIPTIALVKDSKTKDFI 149
Cdd:cd02956   5 QVLQESTQVP-VVVDFWAPRSPPSKELLPLLERLAEEY-QGQFvlAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVDGF 82


                ..
gi 16768382 150 VG 151
Cdd:cd02956  83 QG 84
PTZ00051 PTZ00051
thioredoxin; Provisional
 66-156 8.09e-04

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 37.55  E-value: 8.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16768382   66 ELADEKEFFEMSKKSPNIVCHFYRDSTERCKIVDMHLKILAAKHVEAKFCKVNAEKTPFLTQRLRIKVIPTIALVKDSKT 145
Cdd:PTZ00051   4 IVTSQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDVDELSEVAEKENITSMPTFKVFKNGSV 83

                         90
                 ....*....|.
gi 16768382  146 KDFIVGFTDLG 156
Cdd:PTZ00051  84 VDTLLGANDEA 94
 
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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