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Conserved domains on  [gi|589533613|gb|EXI13386|]
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thioredoxin [Acinetobacter sp. 694762]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10996 super family cl32621
thioredoxin 2; Provisional
1-126 2.05e-41

thioredoxin 2; Provisional


The actual alignment was detected with superfamily member PRK10996:

Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 134.43  E-value: 2.05e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613   1 MIIVCASCGAKNRVPEEKLSAQPSCGQCHQPLLPLAPIELNEQNFSNYItNSDLPILIDLWAEWCGPCKMMAPHFAQVA- 79
Cdd:PRK10996   1 MNTVCTSCQAINRLPDERIEDAAKCGRCGHDLFDGEVINATGETLDKLL-QDDLPVVIDFWAPWCGPCRNFAPIFEDVAa 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 589533613  80 KQNPRVIFAKINTEESPRLSQAFNVRSIPTLVLMNKTTEVARMSGAL 126
Cdd:PRK10996  80 ERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFKNGQVVDMLNGAV 126
 
Name Accession Description Interval E-value
PRK10996 PRK10996
thioredoxin 2; Provisional
1-126 2.05e-41

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 134.43  E-value: 2.05e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613   1 MIIVCASCGAKNRVPEEKLSAQPSCGQCHQPLLPLAPIELNEQNFSNYItNSDLPILIDLWAEWCGPCKMMAPHFAQVA- 79
Cdd:PRK10996   1 MNTVCTSCQAINRLPDERIEDAAKCGRCGHDLFDGEVINATGETLDKLL-QDDLPVVIDFWAPWCGPCRNFAPIFEDVAa 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 589533613  80 KQNPRVIFAKINTEESPRLSQAFNVRSIPTLVLMNKTTEVARMSGAL 126
Cdd:PRK10996  80 ERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFKNGQVVDMLNGAV 126
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
36-130 4.95e-41

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: 132.64  E-value: 4.95e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613  36 APIELNEQNFSNYITNSDLPILIDLWAEWCGPCKMMAPHFAQVAKQ-NPRVIFAKINTEESPRLSQAFNVRSIPTLVLMN 114
Cdd:COG3118    1 AVVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEyGGKVKFVKVDVDENPELAAQFGVRSIPTLLLFK 80
                         90
                 ....*....|....*.
gi 589533613 115 KTTEVARMSGALRAPE 130
Cdd:COG3118   81 DGQPVDRFVGALPKEQ 96
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
43-130 1.29e-34

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: 115.73  E-value: 1.29e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613  43 QNFSNYITNSDlPILIDLWAEWCGPCKMMAPHFAQVAKQNPRVIFAKINTEESPRLSQAFNVRSIPTLVLMNKTTEVARM 122
Cdd:cd02947    1 EEFEELIKSAK-PVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRV 79

                 ....*...
gi 589533613 123 SGALRAPE 130
Cdd:cd02947   80 VGADPKEE 87
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
40-126 2.15e-34

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: 115.46  E-value: 2.15e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613   40 LNEQNFSNYITNSDLPILIDLWAEWCGPCKMMAPHFAQVAKQ-NPRVIFAKINTEESPRLSQAFNVRSIPTLVLMNKTTE 118
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEyEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKE 80

                  ....*...
gi 589533613  119 VARMSGAL 126
Cdd:TIGR01068  81 VDRSVGAL 88
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
37-125 1.19e-25

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: 93.45  E-value: 1.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613   37 PIELNEQNFSNYITNSDLPILIDLWAEWCGPCKMMAPHFAQVAKQNP-RVIFAKINTEESPRLSQAFNVRSIPTLVLMNK 115
Cdd:pfam00085   2 VVVLTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKgNVVFAKVDVDENPDLASKYGVRGYPTLIFFKN 81
                          90
                  ....*....|
gi 589533613  116 TTEVARMSGA 125
Cdd:pfam00085  82 GQPVDDYVGA 91
 
Name Accession Description Interval E-value
PRK10996 PRK10996
thioredoxin 2; Provisional
1-126 2.05e-41

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 134.43  E-value: 2.05e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613   1 MIIVCASCGAKNRVPEEKLSAQPSCGQCHQPLLPLAPIELNEQNFSNYItNSDLPILIDLWAEWCGPCKMMAPHFAQVA- 79
Cdd:PRK10996   1 MNTVCTSCQAINRLPDERIEDAAKCGRCGHDLFDGEVINATGETLDKLL-QDDLPVVIDFWAPWCGPCRNFAPIFEDVAa 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 589533613  80 KQNPRVIFAKINTEESPRLSQAFNVRSIPTLVLMNKTTEVARMSGAL 126
Cdd:PRK10996  80 ERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFKNGQVVDMLNGAV 126
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
36-130 4.95e-41

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: 132.64  E-value: 4.95e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613  36 APIELNEQNFSNYITNSDLPILIDLWAEWCGPCKMMAPHFAQVAKQ-NPRVIFAKINTEESPRLSQAFNVRSIPTLVLMN 114
Cdd:COG3118    1 AVVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEyGGKVKFVKVDVDENPELAAQFGVRSIPTLLLFK 80
                         90
                 ....*....|....*.
gi 589533613 115 KTTEVARMSGALRAPE 130
Cdd:COG3118   81 DGQPVDRFVGALPKEQ 96
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
43-130 1.29e-34

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: 115.73  E-value: 1.29e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613  43 QNFSNYITNSDlPILIDLWAEWCGPCKMMAPHFAQVAKQNPRVIFAKINTEESPRLSQAFNVRSIPTLVLMNKTTEVARM 122
Cdd:cd02947    1 EEFEELIKSAK-PVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRV 79

                 ....*...
gi 589533613 123 SGALRAPE 130
Cdd:cd02947   80 VGADPKEE 87
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
40-126 2.15e-34

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: 115.46  E-value: 2.15e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613   40 LNEQNFSNYITNSDLPILIDLWAEWCGPCKMMAPHFAQVAKQ-NPRVIFAKINTEESPRLSQAFNVRSIPTLVLMNKTTE 118
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEyEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKE 80

                  ....*...
gi 589533613  119 VARMSGAL 126
Cdd:TIGR01068  81 VDRSVGAL 88
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
37-125 1.19e-25

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: 93.45  E-value: 1.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613   37 PIELNEQNFSNYITNSDLPILIDLWAEWCGPCKMMAPHFAQVAKQNP-RVIFAKINTEESPRLSQAFNVRSIPTLVLMNK 115
Cdd:pfam00085   2 VVVLTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKgNVVFAKVDVDENPDLASKYGVRGYPTLIFFKN 81
                          90
                  ....*....|
gi 589533613  116 TTEVARMSGA 125
Cdd:pfam00085  82 GQPVDDYVGA 91
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
31-130 1.30e-20

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 81.66  E-value: 1.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613  31 PLLPLAPIELNEQNFSNYitnSDLPILIDLWAEWCGPCKMMAPHFAQVAKQNPRVIFAKINTEESP-------------- 96
Cdd:COG0526    9 PDFTLTDLDGKPLSLADL---KGKPVLVNFWATWCPPCRAEMPVLKELAEEYGGVVFVGVDVDENPeavkaflkelglpy 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 589533613  97 --------RLSQAFNVRSIPTLVLMNKT-TEVARMSGALRAPE 130
Cdd:COG0526   86 pvlldpdgELAKAYGVRGIPTTVLIDKDgKIVARHVGPLSPEE 128
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
42-125 3.99e-20

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: 79.24  E-value: 3.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613  42 EQNFSNYI-TNSDLPILIDLWAEWCGPCKMMAPHFAQVAKQ-NPRVIFAKINTEESPRLSQAFNVRSIPTLVLMNKTTEV 119
Cdd:cd02984    2 EEEFEELLkSDASKLLVLHFWAPWAEPCKQMNQVFEELAKEaFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTIV 81

                 ....*.
gi 589533613 120 ARMSGA 125
Cdd:cd02984   82 DRVSGA 87
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
38-118 5.11e-19

Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI and PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5, PDIR, ERp46 and the transmembrane PDIs. PDI, ERp57, ERp72, P5, PDIR and ERp46 are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins usually contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and may also contain one or more redox inactive TRX-like (b) domains. Only one a domain is required for the oxidase function but multiple copies are necessary for the isomerase function. The different types of PDIs may show different substrate specificities and tissue-specific expression, or may be induced by stress. PDIs are in their reduced form at steady state and are oxidized to the active form by Ero1, which is localized in the ER through ERp44. Some members of this family also contain a DnaJ domain in addition to the redox active a domains; examples are ERdj5 and Pfj2. Also included in the family is the redox inactive N-terminal TRX-like domain of ERp29.


Pssm-ID: 239259 [Multi-domain]  Cd Length: 101  Bit Score: 76.50  E-value: 5.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613  38 IELNEQNFSNYITNSDlPILIDLWAEWCGPCKMMAPHFAQVA---KQNPRVIFAKINTEESPRLSQAFNVRSIPTLVLMN 114
Cdd:cd02961    1 VELTDDNFDELVKDSK-DVLVEFYAPWCGHCKALAPEYEKLAkelKGDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFP 79

                 ....
gi 589533613 115 KTTE 118
Cdd:cd02961   80 NGSK 83
PTZ00102 PTZ00102
disulphide isomerase; Provisional
29-129 9.78e-19

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 81.34  E-value: 9.78e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613  29 HQPLLPLAPIELNEQNFSNYITNSDLpILIDLWAEWCGPCKMMAPHFAQVAKQ----NPRVIFAKINTEESPRLSQAFNV 104
Cdd:PTZ00102  26 EEHFISEHVTVLTDSTFDKFITENEI-VLVKFYAPWCGHCKRLAPEYKKAAKMlkekKSEIVLASVDATEEMELAQEFGV 104
                         90       100
                 ....*....|....*....|....*
gi 589533613 105 RSIPTLVLMNKTTEVaRMSGALRAP 129
Cdd:PTZ00102 105 RGYPTIKFFNKGNPV-NYSGGRTAD 128
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
43-130 1.27e-18

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: 75.00  E-value: 1.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613  43 QNFSNYITNSDL-PILIDLWAEWCGPCKMMAPHFAQVAKQNP-RVIFAKINTEESPRLSQAFNVRSIPTLVLMNKTTEVA 120
Cdd:cd02956    1 QNFQQVLQESTQvPVVVDFWAPRSPPSKELLPLLERLAEEYQgQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVD 80
                         90
                 ....*....|
gi 589533613 121 RMSGALRAPE 130
Cdd:cd02956   81 GFQGAQPEEQ 90
trxA PRK09381
thioredoxin TrxA;
38-126 5.34e-18

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 73.95  E-value: 5.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613  38 IELNEQNFSNYITNSDLPILIDLWAEWCGPCKMMAPHFAQVAKQ-NPRVIFAKINTEESPRLSQAFNVRSIPTLVLMNKT 116
Cdd:PRK09381   6 IHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEyQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNG 85
                         90
                 ....*....|
gi 589533613 117 TEVARMSGAL 126
Cdd:PRK09381  86 EVAATKVGAL 95
PTZ00051 PTZ00051
thioredoxin; Provisional
42-125 1.68e-16

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 69.90  E-value: 1.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613  42 EQNFSNYITNSDLpILIDLWAEWCGPCKMMAPHFAQVAKQNPRVIFAKINTEESPRLSQAFNVRSIPTLVLMNKTTEVAR 121
Cdd:PTZ00051   8 QAEFESTLSQNEL-VIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDVDELSEVAEKENITSMPTFKVFKNGSVVDT 86

                 ....
gi 589533613 122 MSGA 125
Cdd:PTZ00051  87 LLGA 90
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
38-117 1.09e-14

PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a protein containing an N-terminal DnaJ domain and four redox active TRX domains. This subfamily is composed of the three TRX domains located at the C-terminal half of the protein. ERdj5 is a ubiquitous protein localized in the endoplasmic reticulum (ER) and is abundant in secretory cells. It's transcription is induced during ER stress. It interacts with BiP through its DnaJ domain in an ATP-dependent manner. BiP, an ER-resident member of the Hsp70 chaperone family, functions in ER-associated degradation and protein translocation. Also included in the alignment is the single complete TRX domain of an uncharacterized protein from Tetraodon nigroviridis, which also contains a DnaJ domain at its N-terminus.


Pssm-ID: 239302 [Multi-domain]  Cd Length: 104  Bit Score: 65.39  E-value: 1.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613  38 IELNEQNFSNYITNSDLPILIDLWAEWCGPCKMMAPHFAQVAKQ-NPRVIFAKINTEESPRLSQAFNVRSIPTLVLMNKT 116
Cdd:cd03004    4 ITLTPEDFPELVLNRKEPWLVDFYAPWCGPCQALLPELRKAARAlKGKVKVGSVDCQKYESLCQQANIRAYPTIRLYPGN 83

                 .
gi 589533613 117 T 117
Cdd:cd03004   84 A 84
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
38-110 1.17e-13

PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. Some members of this subfamily are P5-like proteins containing only one redox active TRX domain.


Pssm-ID: 239299 [Multi-domain]  Cd Length: 103  Bit Score: 62.69  E-value: 1.17e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 589533613  38 IELNEQNFSNYITNSDLPILIDLWAEWCGPCKMMAPHFAQVAKQNPRVI-FAKINTEESPRLSQAFNVRSIPTL 110
Cdd:cd03001    3 VELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVkVGAVDADVHQSLAQQYGVRGFPTI 76
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
38-110 1.63e-13

PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar to the P5-like protein first isolated from alfalfa, which contains two redox active TRX (a) domains at the N-terminus, like human P5, and a C-terminal domain with homology to the C-terminal domain of ERp29, unlike human P5. The cDNA clone of this protein (named G1) was isolated from an alfalfa cDNA library by screening with human protein disulfide isomerase (PDI) cDNA. The G1 protein is constitutively expressed in all major organs of the plant and its expression is induced by treatment with tunicamycin, indicating that it may be a glucose-regulated protein. The G1 homolog in the eukaryotic social amoeba Dictyostelium discoideum is also described as a P5-like protein, which is located in the endoplasmic reticulum (ER) despite the absence of an ER-retrieval signal. G1 homologs from Aspergillus niger and Neurospora crassa have also been characterized, and are named TIGA and ERp38, respectively. Also included in the alignment is an atypical PDI from Leishmania donovani containing a single a domain, and the C-terminal a domain of a P5-like protein from Entamoeba histolytica.


Pssm-ID: 239296 [Multi-domain]  Cd Length: 105  Bit Score: 62.27  E-value: 1.63e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 589533613  38 IELNEQNFSNYITNSDLPILIDLWAEWCGPCKMMAPHFAQVA---KQNPRVIFAKINTEESPR-LSQAFNVRSIPTL 110
Cdd:cd02998    3 VELTDSNFDKVVGDDKKDVLVEFYAPWCGHCKNLAPEYEKLAavfANEDDVVIAKVDADEANKdLAKKYGVSGFPTL 79
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
40-110 3.13e-12

PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide Isomerase Related). PDIR is composed of three redox active TRX (a) domains and an N-terminal redox inactive TRX-like (b) domain. Similar to PDI, it is involved in oxidative protein folding in the endoplasmic reticulum (ER) through its isomerase and chaperone activities. These activities are lower compared to PDI, probably due to PDIR acting only on a subset of proteins. PDIR is preferentially expressed in cells actively secreting proteins and its expression is induced by stress. Similar to PDI, the isomerase and chaperone activities of PDIR are independent; CXXC mutants lacking isomerase activity retain chaperone activity.


Pssm-ID: 239295 [Multi-domain]  Cd Length: 104  Bit Score: 58.87  E-value: 3.13e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 589533613  40 LNEQNFSNYITNSDlPILIDLWAEWCGPCKMMAPHFAQVA---KQNPRVIFAKINT--EESPRLSQAFNVRSIPTL 110
Cdd:cd02997    5 LTDEDFRKFLKKEK-HVLVMFYAPWCGHCKKMKPEFTKAAtelKEDGKGVLAAVDCtkPEHDALKEEYNVKGFPTF 79
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
39-110 3.53e-12

protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs).


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 62.38  E-value: 3.53e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 589533613   39 ELNEQNFSNYITNSDLpILIDLWAEWCGPCKMMAPHFAQVA----KQNPRVIFAKIN-TEESPrLSQAFNVRSIPTL 110
Cdd:TIGR01130   5 VLTKDNFDDFIKSHEF-VLVEFYAPWCGHCKSLAPEYEKAAdelkKKGPPIKLAKVDaTEEKD-LAQKYGVSGYPTL 79
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
49-124 2.89e-11

TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 56.86  E-value: 2.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613  49 ITNSDL---PILIDLWAEWCGPCKMMAPHFAQVAKQ--NPRVIFAKINTEESP-----------------------RLSQ 100
Cdd:cd02966   12 VSLSDLkgkVVLVNFWASWCPPCRAEMPELEALAKEykDDGVEVVGVNVDDDDpaavkaflkkygitfpvlldpdgELAK 91
                         90       100
                 ....*....|....*....|....*
gi 589533613 101 AFNVRSIPTLVLMNKT-TEVARMSG 124
Cdd:cd02966   92 AYGVRGLPTTFLIDRDgRIRARHVG 116
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
55-130 1.07e-10

Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 56.07  E-value: 1.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613  55 PILIDLWAEWCGPCKMM------APHFAQVAKQNprVIFAKINTEESPR-------------LSQAFNVRSIPTLVLMNK 115
Cdd:COG2143   42 PILLFFESDWCPYCKKLhkevfsDPEVAAYLKEN--FVVVQLDAEGDKEvtdfdgetltekeLARKYGVRGTPTLVFFDA 119
                         90
                 ....*....|....*.
gi 589533613 116 T-TEVARMSGALRAPE 130
Cdd:COG2143  120 EgKEIARIPGYLKPET 135
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
57-114 5.93e-10

Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include TRX, protein disulfide isomerase (PDI), tlpA-like, glutaredoxin, NrdH redoxin, and the bacterial Dsb (DsbA, DsbC, DsbG, DsbE, DsbDgamma) protein families. Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins and glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 52.32  E-value: 5.93e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 589533613  57 LIDLWAEWCGPCKMMAPHFAQVAKQNPRVIFAKINTEESP---RLSQAFNVRSIPTLVLMN 114
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELALLNKGVKFEAVDVDEDPaleKELKRYGVGGVPTLVVFG 61
PTZ00102 PTZ00102
disulphide isomerase; Provisional
44-112 3.87e-09

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 53.60  E-value: 3.87e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 589533613  44 NFSNYITNSDLPILIDLWAEWCGPCKMMAP---HFAQVAKQNPRVIFAKIN--TEESPrlSQAFNVRSIPTLVL 112
Cdd:PTZ00102 366 TFEEIVFKSDKDVLLEIYAPWCGHCKNLEPvynELGEKYKDNDSIIVAKMNgtANETP--LEEFSWSAFPTILF 437
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
55-130 3.18e-08

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 48.57  E-value: 3.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613   55 PILIDLWAEWCGPCKMMAPHFAQVA------KQNPRVIFAKINTEESP-----------RLSQAFNVRSIPTLVLMNKTT 117
Cdd:pfam13098   6 PVLVVFTDPDCPYCKKLKKELLEDPdvtvylGPNFVFIAVNIWCAKEVakaftdilenkELGRKYGVRGTPTIVFFDGKG 85
                          90
                  ....*....|...
gi 589533613  118 EVARMSGALRAPE 130
Cdd:pfam13098  86 ELLRLPGYVPAEE 98
DsbDgamma cd02953
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
55-130 3.24e-08

DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein DsbD. It contains a CXXC motif in a TRX fold and shuttles the reducing potential from the membrane domain (DsbD beta) to the N-terminal periplasmic domain (DsbD alpha). DsbD beta, a transmembrane domain comprising of eight helices, acquires its reducing potential from the cytoplasmic thioredoxin. DsbD alpha transfers the acquired reducing potential from DsbD gamma to target proteins such as the periplasmic protein disulphide isomerases, DsbC and DsbG. This flow of reducing potential from the cytoplasm through DsbD allows DsbC and DsbG to act as isomerases in the oxidizing environment of the bacterial periplasm. DsbD also transfers reducing potential from the cytoplasm to specific reductases in the periplasm which are involved in the maturation of cytochromes.


Pssm-ID: 239251 [Multi-domain]  Cd Length: 104  Bit Score: 48.37  E-value: 3.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613  55 PILIDLWAEWCGPCKMMAPHF---AQVAKQ-NPRVIFAKIN-TEESP---RLSQAFNVRSIPTLVLMNKTTEV--ARMSG 124
Cdd:cd02953   13 PVFVDFTADWCVTCKVNEKVVfsdPEVQAAlKKDVVLLRADwTKNDPeitALLKRFGVFGPPTYLFYGPGGEPepLRLPG 92

                 ....*.
gi 589533613 125 ALRAPE 130
Cdd:cd02953   93 FLTADE 98
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
36-125 3.62e-08

PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident protein containing three redox active TRX domains. Yeast complementation studies show that ERp46 can substitute for protein disulfide isomerase (PDI) function in vivo. It has been detected in many tissues, however, transcript and protein levels do not correlate in all tissues, suggesting regulation at a posttranscriptional level. An identical protein, named endoPDI, has been identified as an endothelial PDI that is highly expressed in the endothelium of tumors and hypoxic lesions. It has a protective effect on cells exposed to hypoxia.


Pssm-ID: 239303 [Multi-domain]  Cd Length: 102  Bit Score: 48.44  E-value: 3.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613  36 APIELNEQNFSNYITNSdlPILIDLWAEWCGPCKMMAPHFAQVAK----QNPRVIFAKIN-TEESPrLSQAFNVRSIPTL 110
Cdd:cd03005    1 GVLELTEDNFDHHIAEG--NHFVKFFAPWCGHCKRLAPTWEQLAKkfnnENPSVKIAKVDcTQHRE-LCSEFQVRGYPTL 77
                         90
                 ....*....|....*
gi 589533613 111 VLMNKTTEVARMSGA 125
Cdd:cd03005   78 LLFKDGEKVDKYKGT 92
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
44-112 4.68e-08

PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' domains of PDI, ERp72, ERp57 (or ERp60) and EFP1. PDI, ERp72 and ERp57 are endoplasmic reticulum (ER)-resident eukaryotic proteins involved in oxidative protein folding. They are oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. PDI and ERp57 have the abb'a' domain structure (where a and a' are redox active TRX domains while b and b' are redox inactive TRX-like domains). PDI also contains an acidic region (c domain) after the a' domain that is absent in ERp57. ERp72 has an additional a domain at the N-terminus (a"abb'a' domain structure). ERp57 interacts with the lectin chaperones, calnexin and calreticulin, and specifically promotes the oxidative folding of glycoproteins, while PDI shows a wider substrate specificity. ERp72 associates with several ER chaperones and folding factors to form complexes in the ER that bind nascent proteins. EFP1 is a binding partner protein of thyroid oxidase, which is responsible for the generation of hydrogen peroxide, a crucial substrate of thyroperoxidase, which functions to iodinate thyroglobulin and synthesize thyroid hormones.


Pssm-ID: 239293 [Multi-domain]  Cd Length: 104  Bit Score: 47.94  E-value: 4.68e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 589533613  44 NFSNYITNSDLPILIDLWAEWCGPCKMMAPHFAQVA---KQNPRVIFAKIN-TE-ESPRLsqaFNVRSIPTLVL 112
Cdd:cd02995    9 NFDEVVLDSDKDVLVEFYAPWCGHCKALAPIYEELAeklKGDDNVVIAKMDaTAnDVPSE---FVVDGFPTILF 79
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
38-115 6.02e-08

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 49.62  E-value: 6.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613  38 IELNEQNFSNYITNSDL----PILIDLWAEWCGPCKMMAPHFAQVAKQ-NPRVIFAKINTEESPRLSQAFNVRSIPTLVL 112
Cdd:PTZ00443  33 VLLNDKNFEKLTQASTGattgPWFVKFYAPWCSHCRKMAPAWERLAKAlKGQVNVADLDATRALNLAKRFAIKGYPTLLL 112

                 ...
gi 589533613 113 MNK 115
Cdd:PTZ00443 113 FDK 115
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
29-112 1.75e-07

protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs).


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 48.90  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613   29 HQPLLPLAPI-ELNEQ--------NFSNYITNSDLPILIDLWAEWCGPCKMMAPHFAQVA----KQNPRVIFAKIN-TE- 93
Cdd:TIGR01130 331 LKPYLKSEPIpEDDEGpvkvlvgkNFDEIVLDETKDVLVEFYAPWCGHCKNLAPIYEELAekykDAESDVVIAKMDaTAn 410
                          90
                  ....*....|....*....
gi 589533613   94 ESPrlsqAFNVRSIPTLVL 112
Cdd:TIGR01130 411 DVP----PFEVEGFPTIKF 425
Phd_like_TxnDC9 cd02989
Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; ...
67-124 2.42e-07

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: 46.41  E-value: 2.42e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 589533613  67 PCKMMAPHFAQVAKQNPRVIFAKINTEESPRLSQAFNVRSIPTLVLMNKTTEVARMSG 124
Cdd:cd02989   36 RCKIMDKHLEILAKKHLETKFIKVNAEKAPFLVEKLNIKVLPTVILFKNGKTVDRIVG 93
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
38-110 3.03e-07

PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein containing an N-terminal redox active TRX domain, similar to that of PDI, and a small C-terminal flavin adenine dinucleotide (FAD)-binding domain homologous to the yeast ERV1p protein. QSOX oxidizes thiol groups to disulfides like PDI, however, unlike PDI, this oxidation is accompanied by the reduction of oxygen to hydrogen peroxide. QSOX is localized in high concentrations in cells with heavy secretory load and prefers peptides and proteins as substrates, not monothiols like glutathione. Inside the cell, QSOX is found in the endoplasmic reticulum and Golgi. The flow of reducing equivalents in a QSOX-catalyzed reaction goes from the dithiol substrate -> dithiol of the QSOX TRX domain -> dithiols of the QSOX ERV1p domain -> FAD -> oxygen.


Pssm-ID: 239290 [Multi-domain]  Cd Length: 114  Bit Score: 46.11  E-value: 3.03e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 589533613  38 IELNEQNFSNYITNSDLPILIDLWAEWCGPCKMMAPHFAQVAKQ----NPRVIFAKIN--TEESPRLSQAFNVRSIPTL 110
Cdd:cd02992    4 IVLDAASFNSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDlrkwRPVVRVAAVDcaDEENVALCRDFGVTGYPTL 82
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
38-119 2.55e-06

PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of uncharacterized PDI-like eukaryotic proteins containing only one redox active TRX (a) domain with a CXXS motif, similar to ERp44. CXXS is still a redox active motif; however, the mixed disulfide formed with the substrate is more stable than those formed by CXXC motif proteins. PDI-related proteins are usually involved in the oxidative protein folding in the ER by acting as catalysts and folding assistants. ERp44 is involved in thiol-mediated retention in the ER.


Pssm-ID: 239297 [Multi-domain]  Cd Length: 100  Bit Score: 43.50  E-value: 2.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613  38 IELNEQNFSNYItnsdlpiLIDLWAEWCGPCKMMAPHFAQVAKQNPRVIFAKIntEES---PRLSQAFNVRSIPTLVLMN 114
Cdd:cd02999   10 LDLMAFNREDYT-------AVLFYASWCPFSASFRPHFNALSSMFPQIRHLAI--EESsikPSLLSRYGVVGFPTILLFN 80

                 ....*
gi 589533613 115 KTTEV 119
Cdd:cd02999   81 STPRV 85
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
57-113 6.30e-06

PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX related transmembrane protein containing one redox active TRX domain at the N-terminus and a classical ER retrieval sequence for type I transmembrane proteins at the C-terminus. The TMX3 transcript is found in a variety of tissues with the highest levels detected in skeletal muscle and the heart. In vitro, TMX3 showed oxidase activity albeit slightly lower than that of protein disulfide isomerase.


Pssm-ID: 239298 [Multi-domain]  Cd Length: 104  Bit Score: 42.44  E-value: 6.30e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 589533613  57 LIDLWAEWCGPCKMMAPHFAQVAKQ----NPRVIFAKINTEESPRLSQAFNVRSIPTLVLM 113
Cdd:cd03000   19 LVDFYAPWCGHCKKLEPVWNEVGAElkssGSPVRVGKLDATAYSSIASEFGVRGYPTIKLL 79
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
52-124 9.45e-06

TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found only in oxygenic photosynthetic organisms containing both TRX and NTR domains. The TRX domain functions as a protein disulfide reductase via the reversible oxidation of an active center dithiol present in a CXXC motif, while the NTR domain functions as a reductant to oxidized TRX. The fusion protein is bifunctional, showing both TRX and NTR activities, but it is not an independent NTR/TRX system. In plants, the protein is found exclusively in shoots and mature leaves and is localized in the chloroplast. It is involved in plant protection against oxidative stress.


Pssm-ID: 239247 [Multi-domain]  Cd Length: 97  Bit Score: 41.72  E-value: 9.45e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 589533613  52 SDLPILIDLWAEWCGPCKMMAPHFAQVAKQ-NPRVIFAKINTEESPRLSQAFNVRSIPTLVLMNKTTEVARMSG 124
Cdd:cd02949   12 SDRLILVLYTSPTCGPCRTLKPILNKVIDEfDGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDKELVKEISG 85
OST3_OST6 pfam04756
OST3 / OST6 family, transporter family; The proteins in this family are part of a complex of ...
37-112 9.53e-06

OST3 / OST6 family, transporter family; The proteins in this family are part of a complex of eight ER proteins that transfers core oligosaccharide from dolichol carrier to Asn-X-Ser/Thr motifs. This family includes both OST3 and OST6, each of which contains four predicted transmembrane helices. Disruption of OST3 and OST6 leads to a defect in the assembly of the complex. Hence, the function of these genes seems to be essential for recruiting a fully active complex necessary for efficient N-glycosylation. These proteins are also thought to be novel Mg2+ transporters.


Pssm-ID: 461420  Cd Length: 294  Bit Score: 43.77  E-value: 9.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613   37 PIELNEQNFSNYIT---NSDLPILIDlwAEW----CGPCKMMAPHFAQVAK--------QNPRVIFAKINTEESPRLSQA 101
Cdd:pfam04756  13 VIKLNDSNYKRLLSgprDYSVVVLLT--ALDprfgCQLCREFQPEFELVAKswfkdhkaGSSKLFFATLDFDDGKDVFQS 90
                          90
                  ....*....|.
gi 589533613  102 FNVRSIPTLVL 112
Cdd:pfam04756  91 LGLQTAPHLLL 101
TMX2 cd02962
TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related ...
57-122 1.14e-05

TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related transmembrane protein, identified and characterized through the cloning of its cDNA from a human fetal library. It contains a TRX domain but the redox active CXXC motif is replaced with SXXC. Sequence analysis predicts that TMX2 may be a Type I membrane protein, with its C-terminal half protruding on the luminal side of the endoplasmic reticulum (ER). In addition to the TRX domain, transmembrane region and ER-retention signal, TMX2 also contains a Myb DNA-binding domain repeat signature and a dileucine motif in the tail.


Pssm-ID: 239260 [Multi-domain]  Cd Length: 152  Bit Score: 42.37  E-value: 1.14e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 589533613  57 LIDLWAEWCGPCKMMAPHFAQVAK--QNPRVIFAKINTEESPRLSQAFNV------RSIPTLVLMNKTTEVARM 122
Cdd:cd02962   51 LVEFFTTWSPECVNFAPVFAELSLkyNNNNLKFGKIDIGRFPNVAEKFRVstsplsKQLPTIILFQGGKEVARR 124
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
49-129 2.54e-05

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 41.39  E-value: 2.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613  49 ITNSDL---PILIDLWAEWCGPCKMMAPHFAQVAKQNPR---VIFAkINTEESPRLSQAFNVRSIPTLVLMNKTTEVARM 122
Cdd:COG1225   14 VSLSDLrgkPVVLYFYATWCPGCTAELPELRDLYEEFKDkgvEVLG-VSSDSDEAHKKFAEKYGLPFPLLSDPDGEVAKA 92

                 ....*..
gi 589533613 123 SGALRAP 129
Cdd:COG1225   93 YGVRGTP 99
DsbD COG4232
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ...
55-119 5.80e-05

Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443376 [Multi-domain]  Cd Length: 416  Bit Score: 41.71  E-value: 5.80e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 589533613  55 PILIDLWAEWCGPCKMM------APHFAQVAKQNprVIFAKI----NTEESPRLSQAFNVRSIPTLVLMNKTTEV 119
Cdd:COG4232  322 PVFVDFTADWCVTCKENertvfsDPEVQAALADD--VVLLKAdvtdNDPEITALLKRFGRFGVPTYVFYDPDGEE 394
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
31-86 6.11e-05

periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the biogenesis of c-type cytochromes as well as in disulfide bond formation in some periplasmic proteins. [Protein fate, Protein folding and stabilization]


Pssm-ID: 129481 [Multi-domain]  Cd Length: 173  Bit Score: 40.92  E-value: 6.11e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 589533613   31 PLLPLAPIELNEQNFSNYITNSDLPILIDLWAEWCGPCKMMAPHFAQVAKQNPRVI 86
Cdd:TIGR00385  41 PAFRLASLDEPGQFYTADVLTQGKPVLLNVWASWCPPCRAEHPYLNELAKQGLPIV 96
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
49-112 6.44e-05

TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE homolog subfamily; composed of ScsD, the DsbE homolog of Mycobacterium tuberculosis (MtbDsbE) and similar proteins, all containing a redox-active CXXC motif. The Salmonella typhimurium ScsD is a thioredoxin-like protein which confers copper tolerance to copper-sensitive mutants of E. coli. MtbDsbE has been characterized as an oxidase in vitro, catalyzing the disulfide bond formation of substrates like hirudin. The reduced form of MtbDsbE is more stable than its oxidized form, consistent with an oxidase function. This is in contrast to the function of DsbE from gram-negative bacteria which is a specific reductase of apocytochrome c.


Pssm-ID: 239309 [Multi-domain]  Cd Length: 123  Bit Score: 39.97  E-value: 6.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613  49 ITNSDLPILIDLWAEWCGPCKMMAPHFAQVAK------------QNPRVI---------FAKINTEESpRLSQAFNVRSI 107
Cdd:cd03011   16 ESLSGKPVLVYFWATWCPVCRFTSPTVNQLAAdypvvsvalrsgDDGAVArfmqkkgygFPVINDPDG-VISARWGVSVT 94

                 ....*
gi 589533613 108 PTLVL 112
Cdd:cd03011   95 PAIVI 99
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
55-127 6.77e-05

TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium Synechococcus. It is found only in oxygenic photosynthetic organisms. TRX is a small enzyme that participate in redox reactions, via the reversible oxidation of an active site dithiol present in a CXXC motif. Disruption of the txlA gene suggests that the protein is involved in the redox regulation of the structure and function of photosynthetic apparatus. The plant homolog (designated as HCF164) is localized in the chloroplast and is involved in the assembly of the cytochrome b6f complex, which takes a central position in photosynthetic electron transport.


Pssm-ID: 239248 [Multi-domain]  Cd Length: 142  Bit Score: 40.40  E-value: 6.77e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 589533613  55 PILIDLWAEWCGPCKMMAPHFAQVAKQ-NPRVIFAKINTEES---PRLSQaFNVRSIPTLVLMNKT-TEVARMSGALR 127
Cdd:cd02950   22 PTLVEFYADWCTVCQEMAPDVAKLKQKyGDQVNFVMLNVDNPkwlPEIDR-YRVDGIPHFVFLDREgNEEGQSIGLQP 98
PHA02125 PHA02125
thioredoxin-like protein
62-127 9.19e-05

thioredoxin-like protein


Pssm-ID: 133998 [Multi-domain]  Cd Length: 75  Bit Score: 38.81  E-value: 9.19e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 589533613  62 AEWCGPCKMMAPHFAQVAKQnprviFAKINTEESPRLSQAFNVRSIPTLVlmnKTTEVARMSGALR 127
Cdd:PHA02125   7 AEWCANCKMVKPMLANVEYT-----YVDVDTDEGVELTAKHHIRSLPTLV---NTSTLDRFTGVPR 64
Phd_like cd02957
Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as ...
38-124 1.05e-04

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: 39.07  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613  38 IELNEQNFSNYITNS--DLPILIDLWAEWCGPCKMMAPHFAQVAKQNPRVIFAKINTEESpRLSQAFNVRSIPTLVLMNK 115
Cdd:cd02957    7 REISSKEFLEEVTKAskGTRVVVHFYEPGFPRCKILDSHLEELAAKYPETKFVKINAEKA-FLVNYLDIKVLPTLLVYKN 85

                 ....*....
gi 589533613 116 TTEVARMSG 124
Cdd:cd02957   86 GELIDNIVG 94
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
38-110 1.24e-04

PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human transmembrane protein, TMX. TMX is a type I integral membrane protein; the N-terminal redox active TRX domain is present in the endoplasmic reticulum (ER) lumen while the C-terminus is oriented towards the cytoplasm. It is expressed in many cell types and its active site motif (CPAC) is unique. In vitro, TMX reduces interchain disulfides of insulin and renatures inactive RNase containing incorrect disulfide bonds. The C. elegans homolog, DPY-11, is expressed only in the hypodermis and resides in the cytoplasm. It is required for body and sensory organ morphogeneis. Another uncharacterized TRX-related transmembrane protein, human TMX4, is included in the alignment. The active site sequence of TMX4 is CPSC.


Pssm-ID: 239292 [Multi-domain]  Cd Length: 101  Bit Score: 38.90  E-value: 1.24e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 589533613  38 IELNEQNFSNYITNSdlpILIDLWAEWCGPCKMMAP---HFAQVAKqNPRVIFAKINTEESPRLSQAFNVRSIPTL 110
Cdd:cd02994    4 VELTDSNWTLVLEGE---WMIEFYAPWCPACQQLQPeweEFADWSD-DLGINVAKVDVTQEPGLSGRFFVTALPTI 75
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
62-119 1.44e-04

Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are thioredoxin (TRX)-like protein disulfide oxidoreductases that alter the redox state of target proteins via the reversible oxidation of an active center CXXC motif. TryX is involved in the regulation of oxidative stress in parasitic trypanosomatids by reducing TryX peroxidase, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. TryX derives reducing equivalents from reduced trypanothione, a polyamine peptide conjugate unique to trypanosomatids, which is regenerated by the NADPH-dependent flavoprotein trypanothione reductase. Vertebrate NRX is a 400-amino acid nuclear protein with one redox active TRX domain containing a CPPC active site motif followed by one redox inactive TRX-like domain. Mouse NRX transcripts are expressed in all adult tissues but is restricted to the nervous system and limb buds in embryos. Plant NRX, longer than the vertebrate NRX by about 100-200 amino acids, is a nuclear protein containing a redox inactive TRX-like domain between two redox active TRX domains. Both vertebrate and plant NRXs show thiol oxidoreductase activity in vitro. Their localization in the nucleus suggests a role in the redox regulation of nuclear proteins such as transcription factors.


Pssm-ID: 239307 [Multi-domain]  Cd Length: 131  Bit Score: 39.19  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613  62 AEWCGPCKMMAPHFAQV------AKQNPRVIFAKINTEES--------------P--------RLSQAFNVRSIPTLVLM 113
Cdd:cd03009   27 ASWCPPCRAFTPKLVEFyeklkeSGKNFEIVFISWDRDEEsfndyfskmpwlavPfsdrerrsRLNRTFKIEGIPTLIIL 106

                 ....*.
gi 589533613 114 NKTTEV 119
Cdd:cd03009  107 DADGEV 112
zinc_ribbon_4 pfam13717
zinc-ribbon domain; This family consists of a single zinc ribbon domain, ie half of a pair as ...
1-30 1.15e-03

zinc-ribbon domain; This family consists of a single zinc ribbon domain, ie half of a pair as in family DZR, pfam12773.


Pssm-ID: 433426 [Multi-domain]  Cd Length: 36  Bit Score: 34.87  E-value: 1.15e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 589533613    1 MIIVCASCGAKNRVPEEKLSAQPS---CGQCHQ 30
Cdd:pfam13717   1 MIITCPSCKAKYRIDDEKIPASGVkvrCSKCGH 33
PRK15412 PRK15412
thiol:disulfide interchange protein DsbE; Provisional
31-86 1.32e-03

thiol:disulfide interchange protein DsbE; Provisional


Pssm-ID: 185310 [Multi-domain]  Cd Length: 185  Bit Score: 37.28  E-value: 1.32e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 589533613  31 PLLPLAPIELNEQNFSNYITNSDLPILIDLWAEWCGPCKMMAPHFAQVAKQNPRVI 86
Cdd:PRK15412  46 PKFRLESLENPGQFYQADVLTQGKPVLLNVWATWCPTCRAEHQYLNQLSAQGIRVV 101
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
36-130 1.33e-03

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 36.43  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589533613   36 AP-IELNEQNFSNyITNSDL---PILIDLWAE-WCGPCKMMAPHFAQVAKQnprviFAKINTE------ESPRLSQAF-N 103
Cdd:pfam00578   5 APdFELPDGDGGT-VSLSDYrgkWVVLFFYPAdWTPVCTTELPALADLYEE-----FKKLGVEvlgvsvDSPESHKAFaE 78
                          90       100
                  ....*....|....*....|....*..
gi 589533613  104 VRSIPTLVLMNKTTEVARMSGALRAPE 130
Cdd:pfam00578  79 KYGLPFPLLSDPDGEVARAYGVLNEEE 105
Thioredoxin_7 pfam13899
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
55-115 1.56e-03

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.


Pssm-ID: 433567 [Multi-domain]  Cd Length: 84  Bit Score: 35.41  E-value: 1.56e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 589533613   55 PILIDLWAEWCGPCKMMA------PHFAQVAKQNprVIFAKIN-TEESPRLSQAFNVRSIPTLVLMNK 115
Cdd:pfam13899  19 PVLVDFGADWCFTCQVLErdflshEEVKAALAKN--FVLLRLDwTSRDANITRAFDGQGVPHIAFLDP 84
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
43-81 4.51e-03

TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, periplasmic TRX-like reductase containing a CXXC motif that specifically donates reducing equivalents to apocytochrome c via CcmH, another cytochrome c maturation (Ccm) factor with a redox active CXXC motif. Assembly of cytochrome c requires the ligation of heme to reduced thiols of the apocytochrome. In bacteria, this assembly occurs in the periplasm. The reductase activity of DsbE in the oxidizing environment of the periplasm is crucial in the maturation of cytochrome c.


Pssm-ID: 239308 [Multi-domain]  Cd Length: 127  Bit Score: 34.86  E-value: 4.51e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 589533613  43 QNFSNYITNSDL---PILIDLWAEWCGPCKMMAPHFAQVAKQ 81
Cdd:cd03010   12 PGPDKTLTSADLkgkPYLLNVWASWCAPCREEHPVLMALARQ 53
 
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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