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Conserved domains on  [gi|134133218|ref|NP_001077016|]
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dnaJ homolog subfamily C member 10 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 128-228 7.56e-69

PDIa family, N-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 comprised of the first TRX domain of ERdj5 located after the DnaJ domain at the N-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.


:

Pssm-ID: 239301 [Multi-domain]  Cd Length: 101  Bit Score: 221.63  E-value: 7.56e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 128 PEITTLDRGDFDAAVNSGEVWFVNFYFPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDNGMLCRSKGINSYPSLYVFR 207
Cdd:cd03003    1 PEIVTLDRGDFDAAVNSGEIWFVNFYSPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDDRMLCRSQGVNSYPSLYVFP 80

                         90       100
                 ....*....|....*....|.
gi 134133218 208 AGMNPEKYFNDRTKSSLTKFA 228
Cdd:cd03003   81 SGMNPEKYYGDRSKESLVKFA 101
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 552-660 2.71e-59

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: 195.97  E-value: 2.71e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 552 PVVVTLGPESFQELVKRRKssETWMVDFYAPWCGPCQALLPEWRRMARMLSGIVNVGTVDCQKHHSFCQSESVRAYPEIR 631
Cdd:cd03004    1 PSVITLTPEDFPELVLNRK--EPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIR 78

                         90       100
                 ....*....|....*....|....*....
gi 134133218 632 LFPQNsnrRDQYQTYNGWHRDAFSLKAWA 660
Cdd:cd03004   79 LYPGN---ASKYHSYNGWHRDADSILEFI 104
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 450-546 2.22e-48

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: 165.93  E-value: 2.22e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 450 HVTTLRPENFPNHE---KEPWLVDFFAPWCPPCRALLPELRKASIQLFGQLKFGTLDCTIHEGLCNTYNIHAYPTTVIFN 526
Cdd:cd03004    2 SVITLTPEDFPELVlnrKEPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLYP 81

                         90       100
                 ....*....|....*....|...
gi 134133218 527 --KSSIHEYEGHHS-ADGILEFI 546
Cdd:cd03004   82 gnASKYHSYNGWHRdADSILEFI 104
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 666-772 4.62e-44

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: 153.99  E-value: 4.62e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 666 RASVDLSPEDFKRKVLGGKDHWVLDFYAPWCGPCQQFAPEFEVLARMMKGTVRAGKVDCQAHYQTCQSAGIKAYPTVRFY 745
Cdd:cd03004    1 PSVITLTPEDFPELVLNRKEPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLY 80

                         90       100
                 ....*....|....*....|....*..
gi 134133218 746 PTLGTTRRDQGGEHinsRDATVIADIL 772
Cdd:cd03004   81 PGNASKYHSYNGWH---RDADSILEFI 104
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 33-120 6.34e-30

DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440252 [Multi-domain]  Cd Length: 139  Bit Score: 115.18  E-value: 6.34e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  33 DYYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGLQDEQQGGRYE 112
Cdd:COG0484    1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAES 80


                 ....*...
gi 134133218 113 SWNYYRYD 120
Cdd:COG0484   81 AAAEAAAA 88
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 276-318 6.17e-05

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is 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 the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member cd03004:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 104  Bit Score: 42.66  E-value: 6.17e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 134133218 276 RKLAGMLDGLVNVGWMDCTKQADLCESFEINT-STTALFPPGSS 318
Cdd:cd03004   42 RKAARALKGKVKVGSVDCQKYESLCQQANIRAyPTIRLYPGNAS 85
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 348-443 2.00e-04

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: 41.06  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 348 EILTKSSFEHKLAHHR-WLVSF-----SFGRNdLAsHEYKKL-NALLKNSHIQVGKVDCISDSELCSSLYIHK-PCVAVF 419
Cdd:cd02961    1 VELTDDNFDELVKDSKdVLVEFyapwcGHCKA-LA-PEYEKLaKELKGDGKVVVAKVDCTANNDLCSEYGVRGyPTIKLF 78

                         90       100
                 ....*....|....*....|....
gi 134133218 420 KGvGIHDFEIHHGKDALYNVVAFA 443
Cdd:cd02961   79 PN-GSKEPVKYEGPRTLESLVEFI 101
 
Name Accession Description Interval E-value
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 128-228 7.56e-69

PDIa family, N-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 comprised of the first TRX domain of ERdj5 located after the DnaJ domain at the N-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.


Pssm-ID: 239301 [Multi-domain]  Cd Length: 101  Bit Score: 221.63  E-value: 7.56e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 128 PEITTLDRGDFDAAVNSGEVWFVNFYFPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDNGMLCRSKGINSYPSLYVFR 207
Cdd:cd03003    1 PEIVTLDRGDFDAAVNSGEIWFVNFYSPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDDRMLCRSQGVNSYPSLYVFP 80

                         90       100
                 ....*....|....*....|.
gi 134133218 208 AGMNPEKYFNDRTKSSLTKFA 228
Cdd:cd03003   81 SGMNPEKYYGDRSKESLVKFA 101
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 552-660 2.71e-59

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: 195.97  E-value: 2.71e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 552 PVVVTLGPESFQELVKRRKssETWMVDFYAPWCGPCQALLPEWRRMARMLSGIVNVGTVDCQKHHSFCQSESVRAYPEIR 631
Cdd:cd03004    1 PSVITLTPEDFPELVLNRK--EPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIR 78

                         90       100
                 ....*....|....*....|....*....
gi 134133218 632 LFPQNsnrRDQYQTYNGWHRDAFSLKAWA 660
Cdd:cd03004   79 LYPGN---ASKYHSYNGWHRDADSILEFI 104
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 450-546 2.22e-48

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: 165.93  E-value: 2.22e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 450 HVTTLRPENFPNHE---KEPWLVDFFAPWCPPCRALLPELRKASIQLFGQLKFGTLDCTIHEGLCNTYNIHAYPTTVIFN 526
Cdd:cd03004    2 SVITLTPEDFPELVlnrKEPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLYP 81

                         90       100
                 ....*....|....*....|...
gi 134133218 527 --KSSIHEYEGHHS-ADGILEFI 546
Cdd:cd03004   82 gnASKYHSYNGWHRdADSILEFI 104
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 666-772 4.62e-44

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: 153.99  E-value: 4.62e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 666 RASVDLSPEDFKRKVLGGKDHWVLDFYAPWCGPCQQFAPEFEVLARMMKGTVRAGKVDCQAHYQTCQSAGIKAYPTVRFY 745
Cdd:cd03004    1 PSVITLTPEDFPELVLNRKEPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLY 80

                         90       100
                 ....*....|....*....|....*..
gi 134133218 746 PTLGTTRRDQGGEHinsRDATVIADIL 772
Cdd:cd03004   81 PGNASKYHSYNGWH---RDADSILEFI 104
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 33-120 6.34e-30

DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440252 [Multi-domain]  Cd Length: 139  Bit Score: 115.18  E-value: 6.34e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  33 DYYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGLQDEQQGGRYE 112
Cdd:COG0484    1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAES 80


                 ....*...
gi 134133218 113 SWNYYRYD 120
Cdd:COG0484   81 AAAEAAAA 88
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 33-95 6.51e-27

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 103.71  E-value: 6.51e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134133218   33 DYYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDETAHDKFLKINRAYEVLKDEDLRKKYD 95
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 33-109 7.61e-25

chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.


Pssm-ID: 274090 [Multi-domain]  Cd Length: 354  Bit Score: 106.92  E-value: 7.61e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134133218   33 DYYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDEtAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGLQDEQQGG 109
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKE-AEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFNGGGGGG 76
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 33-109 1.06e-24

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 106.77  E-value: 1.06e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134133218  33 DYYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGLQDEQQGG 109
Cdd:PRK10767   5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYDQYGHAAFEQGGGGG 81
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 33-87 2.62e-21

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 87.60  E-value: 2.62e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 134133218  33 DYYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDETAHDKFLKINRAYEVLKD 87
Cdd:cd06257    1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
DnaJ smart00271
DnaJ molecular chaperone homology domain;
32-89 5.88e-21

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 86.90  E-value: 5.88e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 134133218    32 EDYYKLLGISREASTRDIRQAFKKLALTMHPDKNPND-ETAHDKFLKINRAYEVLKDED 89
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDkEEAEEKFKEINEAYEVLSDPE 59
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 671-773 4.78e-20

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: 85.75  E-value: 4.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  671 LSPEDFKRKVLGGKDHWVLDFYAPWCGPCQQFAPEFEVLARMMKGTVRAGKVDCQAHYQTCQSAGIKAYPTVRFYPTlGT 750
Cdd:pfam00085   5 LTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKN-GQ 83

                          90       100
                  ....*....|....*....|...
gi 134133218  751 TRRDQGGehinSRDATVIADILR 773
Cdd:pfam00085  84 PVDDYVG----ARPKDALAAFLK 102
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
29-105 5.66e-20

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 93.35  E-value: 5.66e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134133218  29 SSDEDYYKLLGISREASTRDIRQAFKKLALTMHPDKNpNDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGLQDE 105
Cdd:NF037946   2 EEKRDYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRN-KAPDAAEIFAEINEAYEVLSNPEKRANYDKYGHDGVDGE 77
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 669-745 1.06e-19

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: 84.87  E-value: 1.06e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134133218 669 VDLSPEDFKRKVLGGKDHWVLDFYAPWCGPCQQFAPEFEVLARMMKGTVRAGKVDCQAHYQTCQSAGIKAYPTVRFY 745
Cdd:COG3118    3 VELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLF 79
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 451-548 4.69e-19

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: 83.05  E-value: 4.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  451 VTTLRPENFP---NHEKEPWLVDFFAPWCPPCRALLPELRKASIQLFGQLKFGTLDCTIHEGLCNTYNIHAYPTTVIF-N 526
Cdd:pfam00085   2 VVVLTDANFDevvQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFkN 81

                          90       100
                  ....*....|....*....|..
gi 134133218  527 KSSIHEYEGHHSADGILEFIED 548
Cdd:pfam00085  82 GQPVDDYVGARPKDALAAFLKA 103
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 436-572 9.86e-19

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 90.20  E-value: 9.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 436 LYNVVAFAKES---VNAHVTTLRPENFPN--HEKEPWLVDFFAPWCPPCRALLPELRKASIQL---FGQLKFGTLDCTIH 507
Cdd:PTZ00102  16 LLAFAVFGSAEehfISEHVTVLTDSTFDKfiTENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLkekKSEIVLASVDATEE 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 134133218 508 EGLCNTYNIHAYPTTVIFNKSSIHEYEGHHSADGILEFIEDLVNPVVVTLgpESFQELVKRRKSS 572
Cdd:PTZ00102  96 MELAQEFGVRGYPTIKFFNKGNPVNYSGGRTADGIVSWIKKLTGPAVTEV--ESASEIKLIAKKI 158
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 553-643 2.06e-18

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: 81.12  E-value: 2.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  553 VVVTLGPESFQELVKrrKSSETWMVDFYAPWCGPCQALLPEWRRMARMLSGIVNVGTVDCQKHHSFCQSESVRAYPEIRL 632
Cdd:pfam00085   1 VVVVLTDANFDEVVQ--KSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIF 78

                          90
                  ....*....|.
gi 134133218  633 FPqNSNRRDQY 643
Cdd:pfam00085  79 FK-NGQPVDDY 88
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 450-550 5.35e-18

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: 79.86  E-value: 5.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 450 HVTTLRPENFPNH---EKEPWLVDFFAPWCPPCRALLPELRKASIQLFGQLKFGTLDCTIHEGLCNTYNIHAYPTTVIF- 525
Cdd:COG3118    1 AVVELTDENFEEEvleSDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLFk 80

                         90       100
                 ....*....|....*....|....*
gi 134133218 526 NKSSIHEYEGHHSADGILEFIEDLV 550
Cdd:COG3118   81 DGQPVDRFVGALPKEQLREFLDKVL 105
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 450-570 3.26e-17

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: 85.11  E-value: 3.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  450 HVTTLRPENFPN--HEKEPWLVDFFAPWCPPCRALLPELRKASIQLFGQ---LKFGTLDCTIHEGLCNTYNIHAYPTTVI 524
Cdd:TIGR01130   2 DVLVLTKDNFDDfiKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKgppIKLAKVDATEEKDLAQKYGVSGYPTLKI 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 134133218  525 F--NKSSIHEYEGHHSADGILEFIEDLVNPVVVTLG-PESFQELVKRRK 570
Cdd:TIGR01130  82 FrnGEDSVSDYNGPRDADGIVKYMKKQSGPAVKEIEtVADLEAFLADDD 130
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 554-693 5.77e-17

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: 84.34  E-value: 5.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  554 VVTLGPESFQELVKrrkSSETWMVDFYAPWCGPCQALLPEWRRMARMLS---GIVNVGTVDCQKHHSFCQSESVRAYPEI 630
Cdd:TIGR01130   3 VLVLTKDNFDDFIK---SHEFVLVEFYAPWCGHCKSLAPEYEKAADELKkkgPPIKLAKVDATEEKDLAQKYGVSGYPTL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134133218  631 RLFpqnSNRRDQYQTYNGwHRDAFSLKAWALS-SLPRASVDLSPEDFKrKVLGGKDHWVLDFYA 693
Cdd:TIGR01130  80 KIF---RNGEDSVSDYNG-PRDADGIVKYMKKqSGPAVKEIETVADLE-AFLADDDVVVIGFFK 138
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 129-648 6.95e-17

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: 84.34  E-value: 6.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  129 EITTLDRGDFDAAVNSGEVWFVNFYFPRCSHCHDLAPTWREFA---KEMDGVIRIGAVNCGDNGMLCRSKGINSYPSLYV 205
Cdd:TIGR01130   2 DVLVLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAAdelKKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLKI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  206 FRAG-MNPEKYFNDRTKSSLTKfamqFVKSKVtelwqGNIYSEIERAfaerigwlitfcadtgdclesqtrrklagmldg 284
Cdd:TIGR01130  82 FRNGeDSVSDYNGPRDADGIVK----YMKKQS-----GPAVKEIETV--------------------------------- 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  285 lvnvgwmdctkqADLcESFEINTSTTALFppgssltqkgsvlFIQSLDtKEIYAQVLQ----HLPDLEILTKSSFEHKLA 360
Cdd:TIGR01130 120 ------------ADL-EAFLADDDVVVIG-------------FFKDLD-SELNDTFLSvaekLRDVYFFFAHSSDVAAFA 172

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  361 HhrwlvsFSFGRNDLASHEYKKLNallKNSHIQVGKVDCISDSelcsslyihkpcvavfkgvgIHDFeIHHGKDALynVV 440
Cdd:TIGR01130 173 K------LGAFPDSVVLFKPKDED---EKFSKVDGEMDTDVSD--------------------LEKF-IRAESLPL--VG 220

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  441 AFAKESvNAHVTTLRP--ENFPNHEKEpwlVDFFAPWcppcRALLPELRKASIQLFgqLKFGTLDCTIHEGLCNTYNIHA 518
Cdd:TIGR01130 221 EFTQET-AAKYFESGPlvVLYYNVDES---LDPFEEL----RNRFLEAAKKFRGKF--VNFAVADEEDFGRELEYFGLKA 290

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  519 --YPTTVIFNKSSIHEY---EGHHSADGILEFIEDLVN------------------PVVVTLGpESFQELVKRrkSSETW 575
Cdd:TIGR01130 291 ekFPAVAIQDLEGNKKYpmdQEEFSSENLEAFVKDFLDgklkpylksepipeddegPVKVLVG-KNFDEIVLD--ETKDV 367

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134133218  576 MVDFYAPWCGPCQALLPEWRRMARMLSGI---VNVGTVDCQK--HHSFcqseSVRAYPEIRLFPQNSNRrdQYQTYNG 648
Cdd:TIGR01130 368 LVEFYAPWCGHCKNLAPIYEELAEKYKDAesdVVIAKMDATAndVPPF----EVEGFPTIKFVPAGKKS--EPVPYDG 439
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 138-227 3.00e-15

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: 71.88  E-value: 3.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  138 FDAAVNSGEVWF-VNFYFPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDNGMLCRSKGINSYPSLYVFRAGMNPEKYF 216
Cdd:pfam00085  10 FDEVVQKSSKPVlVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKNGQPVDDYV 89

                          90
                  ....*....|.
gi 134133218  217 NDRTKSSLTKF 227
Cdd:pfam00085  90 GARPKDALAAF 100
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 554-667 3.30e-15

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 75.43  E-value: 3.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 554 VVTLGPESFQELVKRRKSSET--WMVDFYAPWCGPCQALLPEWRRMARMLSGIVNVGTVDCQKHHSFCQSESVRAYPEIR 631
Cdd:PTZ00443  32 LVLLNDKNFEKLTQASTGATTgpWFVKFYAPWCSHCRKMAPAWERLAKALKGQVNVADLDATRALNLAKRFAIKGYPTLL 111

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 134133218 632 LFpqnsNRRDQYQtYNGWHRDAFSLKAWALSSLPRA 667
Cdd:PTZ00443 112 LF----DKGKMYQ-YEGGDRSTEKLAAFALGDFKKA 142
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 671-746 9.48e-15

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: 70.40  E-value: 9.48e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134133218  671 LSPEDFKRKVLGGKDHWVLDFYAPWCGPCQQFAPEFEVLARMMKGTVRAGKVDCQAHYQTCQSAGIKAYPTVRFYP 746
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFK 76
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 148-236 1.14e-13

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 71.19  E-value: 1.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 148 WFVNFYFPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDNGMLCRSKGINSYPSLYVFRAGMNPEKYFNDRTKSSLTKF 227
Cdd:PTZ00443  55 WFVKFYAPWCSHCRKMAPAWERLAKALKGQVNVADLDATRALNLAKRFAIKGYPTLLLFDKGKMYQYEGGDRSTEKLAAF 134


                 ....*....
gi 134133218 228 AMQFVKSKV 236
Cdd:PTZ00443 135 ALGDFKKAL 143
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 554-633 8.80e-13

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: 65.23  E-value: 8.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 554 VVTLGPESFQELVkrRKSSETWMVDFYAPWCGPCQALLPEWRRMARMLSGIVNVGTVDCQKHHSFCQSESVRAYPEIRLF 633
Cdd:COG3118    2 VVELTDENFEEEV--LESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLF 79
PRK10996 PRK10996
thioredoxin 2; Provisional
 688-745 1.47e-12

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 65.48  E-value: 1.47e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 134133218 688 VLDFYAPWCGPCQQFAPEFEVLARMMKGTVRAGKVDCQAHYQTCQSAGIKAYPTVRFY 745
Cdd:PRK10996  56 VIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIF 113
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 130-209 8.74e-12

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: 62.14  E-value: 8.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 130 ITTLDRGDFDAAV-NSGEVWFVNFYFPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDNGMLCRSKGINSYPSLYVFRA 208
Cdd:COG3118    2 VVELTDENFEEEVlESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLFKD 81


                 .
gi 134133218 209 G 209
Cdd:COG3118   82 G 82
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 276-318 6.17e-05

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: 42.66  E-value: 6.17e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 134133218 276 RKLAGMLDGLVNVGWMDCTKQADLCESFEINT-STTALFPPGSS 318
Cdd:cd03004   42 RKAARALKGKVKVGSVDCQKYESLCQQANIRAyPTIRLYPGNAS 85
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 348-443 2.00e-04

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: 41.06  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 348 EILTKSSFEHKLAHHR-WLVSF-----SFGRNdLAsHEYKKL-NALLKNSHIQVGKVDCISDSELCSSLYIHK-PCVAVF 419
Cdd:cd02961    1 VELTDDNFDELVKDSKdVLVEFyapwcGHCKA-LA-PEYEKLaKELKGDGKVVVAKVDCTANNDLCSEYGVRGyPTIKLF 78

                         90       100
                 ....*....|....*....|....
gi 134133218 420 KGvGIHDFEIHHGKDALYNVVAFA 443
Cdd:cd02961   79 PN-GSKEPVKYEGPRTLESLVEFI 101
 
Name Accession Description Interval E-value
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 128-228 7.56e-69

PDIa family, N-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 comprised of the first TRX domain of ERdj5 located after the DnaJ domain at the N-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.


Pssm-ID: 239301 [Multi-domain]  Cd Length: 101  Bit Score: 221.63  E-value: 7.56e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 128 PEITTLDRGDFDAAVNSGEVWFVNFYFPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDNGMLCRSKGINSYPSLYVFR 207
Cdd:cd03003    1 PEIVTLDRGDFDAAVNSGEIWFVNFYSPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDDRMLCRSQGVNSYPSLYVFP 80

                         90       100
                 ....*....|....*....|.
gi 134133218 208 AGMNPEKYFNDRTKSSLTKFA 228
Cdd:cd03003   81 SGMNPEKYYGDRSKESLVKFA 101
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 552-660 2.71e-59

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: 195.97  E-value: 2.71e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 552 PVVVTLGPESFQELVKRRKssETWMVDFYAPWCGPCQALLPEWRRMARMLSGIVNVGTVDCQKHHSFCQSESVRAYPEIR 631
Cdd:cd03004    1 PSVITLTPEDFPELVLNRK--EPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIR 78

                         90       100
                 ....*....|....*....|....*....
gi 134133218 632 LFPQNsnrRDQYQTYNGWHRDAFSLKAWA 660
Cdd:cd03004   79 LYPGN---ASKYHSYNGWHRDADSILEFI 104
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 450-546 2.22e-48

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: 165.93  E-value: 2.22e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 450 HVTTLRPENFPNHE---KEPWLVDFFAPWCPPCRALLPELRKASIQLFGQLKFGTLDCTIHEGLCNTYNIHAYPTTVIFN 526
Cdd:cd03004    2 SVITLTPEDFPELVlnrKEPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLYP 81

                         90       100
                 ....*....|....*....|...
gi 134133218 527 --KSSIHEYEGHHS-ADGILEFI 546
Cdd:cd03004   82 gnASKYHSYNGWHRdADSILEFI 104
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 666-772 4.62e-44

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: 153.99  E-value: 4.62e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 666 RASVDLSPEDFKRKVLGGKDHWVLDFYAPWCGPCQQFAPEFEVLARMMKGTVRAGKVDCQAHYQTCQSAGIKAYPTVRFY 745
Cdd:cd03004    1 PSVITLTPEDFPELVLNRKEPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLY 80

                         90       100
                 ....*....|....*....|....*..
gi 134133218 746 PTLGTTRRDQGGEHinsRDATVIADIL 772
Cdd:cd03004   81 PGNASKYHSYNGWH---RDADSILEFI 104
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 131-228 1.20e-30

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: 115.79  E-value: 1.20e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 131 TTLDRGDFDAAVNSGEVWFVNFYFPRCSHCHDLAPTWREFAKEM--DGVIRIGAVNCGDNGMLCRSKGINSYPSLYVFRA 208
Cdd:cd02961    1 VELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELkgDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPN 80

                         90       100
                 ....*....|....*....|.
gi 134133218 209 GM-NPEKYFNDRTKSSLTKFA 228
Cdd:cd02961   81 GSkEPVKYEGPRTLESLVEFI 101
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 555-660 1.83e-30

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: 115.40  E-value: 1.83e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 555 VTLGPESFQELVKrrkSSETWMVDFYAPWCGPCQALLPEWRRMARML--SGIVNVGTVDCQKHHSFCQSESVRAYPEIRL 632
Cdd:cd02961    1 VELTDDNFDELVK---DSKDVLVEFYAPWCGHCKALAPEYEKLAKELkgDGKVVVAKVDCTANNDLCSEYGVRGYPTIKL 77

                         90       100
                 ....*....|....*....|....*...
gi 134133218 633 FPQNSnrrDQYQTYNGwHRDAFSLKAWA 660
Cdd:cd02961   78 FPNGS---KEPVKYEG-PRTLESLVEFI 101
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 33-120 6.34e-30

DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440252 [Multi-domain]  Cd Length: 139  Bit Score: 115.18  E-value: 6.34e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  33 DYYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGLQDEQQGGRYE 112
Cdd:COG0484    1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAES 80


                 ....*...
gi 134133218 113 SWNYYRYD 120
Cdd:COG0484   81 AAAEAAAA 88
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 554-661 7.91e-28

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: 107.76  E-value: 7.91e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 554 VVTLGPESFQELVKrrKSSETWMVDFYAPWCGPCQALLPEWRRMARMLSGIVNVGTVDCQKHHSFCQSESVRAYPEIRLF 633
Cdd:cd03001    2 VVELTDSNFDKKVL--NSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVF 79

                         90       100
                 ....*....|....*....|....*...
gi 134133218 634 PQNSNRRdqyQTYNGwHRDAFSLKAWAL 661
Cdd:cd03001   80 GAGKNSP---QDYQG-GRTAKAIVSAAL 103
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 452-546 2.40e-27

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: 106.54  E-value: 2.40e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 452 TTLRPENFPNH--EKEPWLVDFFAPWCPPCRALLPELRKASIQLF--GQLKFGTLDCTIHEGLCNTYNIHAYPTTVIFNK 527
Cdd:cd02961    1 VELTDDNFDELvkDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKgdGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPN 80

                         90       100
                 ....*....|....*....|.
gi 134133218 528 SS--IHEYEGHHSADGILEFI 546
Cdd:cd02961   81 GSkePVKYEGPRTLESLVEFI 101
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 33-95 6.51e-27

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 103.71  E-value: 6.51e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134133218   33 DYYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDETAHDKFLKINRAYEVLKDEDLRKKYD 95
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 669-746 2.03e-26

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: 103.84  E-value: 2.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 669 VDLSPEDFKRKVLGGKDhWVLDFYAPWCGPCQQFAPEFEVLARMMK--GTVRAGKVDCQAHYQTCQSAGIKAYPTVRFYP 746
Cdd:cd02961    1 VELTDDNFDELVKDSKD-VLVEFYAPWCGHCKALAPEYEKLAKELKgdGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFP 79
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 33-109 7.61e-25

chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.


Pssm-ID: 274090 [Multi-domain]  Cd Length: 354  Bit Score: 106.92  E-value: 7.61e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134133218   33 DYYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDEtAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGLQDEQQGG 109
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKE-AEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFNGGGGGG 76
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 33-109 1.06e-24

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 106.77  E-value: 1.06e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134133218  33 DYYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGLQDEQQGG 109
Cdd:PRK10767   5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYDQYGHAAFEQGGGGG 81
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 667-770 1.58e-24

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: 98.51  E-value: 1.58e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 667 ASVDLSPEDFKRKVLGGKDHWVLDFYAPWCGPCQQFAPEFEVLARMMKGTVRAGKVDCQAHYQTCQSAGIKAYPTVRFYP 746
Cdd:cd03001    1 DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVFG 80

                         90       100
                 ....*....|....*....|....*
gi 134133218 747 TLGTTRRD-QGGehinsRDATVIAD 770
Cdd:cd03001   81 AGKNSPQDyQGG-----RTAKAIVS 100
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 33-102 4.12e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 99.50  E-value: 4.12e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  33 DYYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGL 102
Cdd:PRK14281   4 DYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNKEAEEHFKEVNEAYEVLSNDDKRRRYDQFGHAGV 73
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 33-87 2.62e-21

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 87.60  E-value: 2.62e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 134133218  33 DYYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDETAHDKFLKINRAYEVLKD 87
Cdd:cd06257    1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 28-126 3.24e-21

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 96.46  E-value: 3.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  28 ISSDEDYYKLLGISREASTRDIRQAFKKLALTMHPDKNpNDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGLQdeqq 107
Cdd:PRK14298   1 MATTRDYYEILGLSKDASVEDIKKAYRKLAMKYHPDKN-KEPDAEEKFKEISEAYAVLSDAEKRAQYDRFGHAGID---- 75

                         90       100
                 ....*....|....*....|
gi 134133218 108 gGRYESWNYYR-YDFGIYDD 126
Cdd:PRK14298  76 -NQYSAEDIFRgADFGGFGD 94
DnaJ smart00271
DnaJ molecular chaperone homology domain;
32-89 5.88e-21

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 86.90  E-value: 5.88e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 134133218    32 EDYYKLLGISREASTRDIRQAFKKLALTMHPDKNPND-ETAHDKFLKINRAYEVLKDED 89
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDkEEAEEKFKEINEAYEVLSDPE 59
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 30-113 6.39e-21

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 95.58  E-value: 6.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  30 SDEDYYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGLQDEQQGG 109
Cdd:PRK14301   2 SQRDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNPEAEQKFKEAAEAYEVLRDAEKRARYDRFGHAGVNGNGGFG 81


                 ....
gi 134133218 110 RYES 113
Cdd:PRK14301  82 GFSS 85
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 33-93 6.85e-21

Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 86.59  E-value: 6.85e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134133218  33 DYYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDETAHDKFLKINRAYEVLKDEDLRKK 93
Cdd:COG5407    1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDPKAEERFKEINEAYELLSDAEKRAR 61
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 138-229 1.66e-20

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: 86.96  E-value: 1.66e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 138 FDAAV-NSGEVWFVNFYFPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDNGMLCRSKGINSYPSLYVFRAGMN-PEKY 215
Cdd:cd03001   10 FDKKVlNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVFGAGKNsPQDY 89

                         90
                 ....*....|....
gi 134133218 216 FNDRTKSSLTKFAM 229
Cdd:cd03001   90 QGGRTAKAIVSAAL 103
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 554-661 2.43e-20

PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces cerevisiae MPD1 protein, which contains a single redox active TRX domain located at the N-terminus, and an ER retention signal at the C-terminus indicative of an ER-resident protein. MPD1 has been shown to suppress the maturation defect of carboxypeptidase Y caused by deletion of the yeast PDI1 gene. Other characterized members of this subfamily include the Aspergillus niger prpA protein and Giardia PDI-1. PrpA is non-essential to strain viability, however, its transcript level is induced by heterologous protein expression suggesting a possible role in oxidative protein folding during high protein production. Giardia PDI-1 has the ability to refold scrambled RNase and exhibits transglutaminase activity.


Pssm-ID: 239300 [Multi-domain]  Cd Length: 109  Bit Score: 86.65  E-value: 2.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 554 VVTLGPESFQELVKRrkSSETWMVDFYAPWCGPCQALLPEWRRMARMLSGIVNVGTVDC--QKHHSFCQSESVRAYPEIR 631
Cdd:cd03002    2 VYELTPKNFDKVVHN--TNYTTLVEFYAPWCGHCKNLKPEYAKAAKELDGLVQVAAVDCdeDKNKPLCGKYGVQGFPTLK 79

                         90       100       110
                 ....*....|....*....|....*....|.
gi 134133218 632 LF-PQNSNRRDQYQTYNGwHRDAFSLKAWAL 661
Cdd:cd03002   80 VFrPPKKASKHAVEDYNG-ERSAKAIVDFVL 109
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 33-127 2.80e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 93.68  E-value: 2.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  33 DYYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDEtAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGLqdEQQGGRYE 112
Cdd:PRK14291   4 DYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPE-AEEKFKEINEAYQVLSDPEKRKLYDQFGHAAF--SGSGQQQQ 80

                         90
                 ....*....|....*
gi 134133218 113 SWNYYRYDFGIYDDD 127
Cdd:PRK14291  81 GQEGFSDFGGGNIED 95
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 451-545 3.00e-20

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: 86.19  E-value: 3.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 451 VTTLRPENFPN---HEKEPWLVDFFAPWCPPCRALLPELRKASIQLFGQLKFGTLDCTIHEGLCNTYNIHAYPTTVIF-- 525
Cdd:cd03001    2 VVELTDSNFDKkvlNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVFga 81

                         90       100
                 ....*....|....*....|
gi 134133218 526 NKSSIHEYEGHHSADGILEF 545
Cdd:cd03001   82 GKNSPQDYQGGRTAKAIVSA 101
PRK14297 PRK14297
molecular chaperone DnaJ;
32-122 3.91e-20

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 93.31  E-value: 3.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  32 EDYYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEKglqDEQQGGRY 111
Cdd:PRK14297   4 KDYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNKEAEEKFKEINEAYQVLSDPQKKAQYDQFGTA---DFNGAGGF 80

                         90
                 ....*....|.
gi 134133218 112 ESWNYYRYDFG 122
Cdd:PRK14297  81 GSGGFGGFDFS 91
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 671-773 4.78e-20

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: 85.75  E-value: 4.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  671 LSPEDFKRKVLGGKDHWVLDFYAPWCGPCQQFAPEFEVLARMMKGTVRAGKVDCQAHYQTCQSAGIKAYPTVRFYPTlGT 750
Cdd:pfam00085   5 LTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKN-GQ 83

                          90       100
                  ....*....|....*....|...
gi 134133218  751 TRRDQGGehinSRDATVIADILR 773
Cdd:pfam00085  84 PVDDYVG----ARPKDALAAFLK 102
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
29-105 5.66e-20

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 93.35  E-value: 5.66e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134133218  29 SSDEDYYKLLGISREASTRDIRQAFKKLALTMHPDKNpNDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGLQDE 105
Cdd:NF037946   2 EEKRDYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRN-KAPDAAEIFAEINEAYEVLSNPEKRANYDKYGHDGVDGE 77
PRK14293 PRK14293
molecular chaperone DnaJ;
33-102 6.29e-20

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 92.36  E-value: 6.29e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  33 DYYKLLGISREASTRDIRQAFKKLALTMHPDKNpNDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGL 102
Cdd:PRK14293   4 DYYEILGVSRDADKDELKRAYRRLARKYHPDVN-KEPGAEDRFKEINRAYEVLSDPETRARYDQFGEAGV 72
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 669-745 1.06e-19

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: 84.87  E-value: 1.06e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134133218 669 VDLSPEDFKRKVLGGKDHWVLDFYAPWCGPCQQFAPEFEVLARMMKGTVRAGKVDCQAHYQTCQSAGIKAYPTVRFY 745
Cdd:COG3118    3 VELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLF 79
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 33-109 1.68e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 90.98  E-value: 1.68e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134133218  33 DYYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGLQDEQQGG 109
Cdd:PRK14294   5 DYYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGDKEAEELFKEAAEAYEVLSDPKKRGIYDQYGHEGLSGTGFSG 81
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 33-126 2.11e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 91.02  E-value: 2.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  33 DYYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGL-QDEQQGGRY 111
Cdd:PRK14277   6 DYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDKEAEQKFKEINEAYEILSDPQKRAQYDQFGHAAFdPGGFGQGGF 85

                         90
                 ....*....|....*....
gi 134133218 112 ESWNY----YRYDFGIYDD 126
Cdd:PRK14277  86 GQGGFggggFDFDFGGFGD 104
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 128-206 2.13e-19

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: 83.88  E-value: 2.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 128 PEITTLDRGDFDAAV-NSGEVWFVNFYFPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDNGMLCRSKGINSYPSLYVF 206
Cdd:cd03004    1 PSVITLTPEDFPELVlNRKEPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLY 80
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 33-102 3.47e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 90.67  E-value: 3.47e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  33 DYYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGL 102
Cdd:PRK14284   2 DYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDAEAEKRFKEVSEAYEVLSDAQKRESYDRYGKDGP 71
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 451-548 4.69e-19

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: 83.05  E-value: 4.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  451 VTTLRPENFP---NHEKEPWLVDFFAPWCPPCRALLPELRKASIQLFGQLKFGTLDCTIHEGLCNTYNIHAYPTTVIF-N 526
Cdd:pfam00085   2 VVVLTDANFDevvQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFkN 81

                          90       100
                  ....*....|....*....|..
gi 134133218  527 KSSIHEYEGHHSADGILEFIED 548
Cdd:pfam00085  82 GQPVDDYVGARPKDALAAFLKA 103
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 31-109 5.00e-19

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 90.27  E-value: 5.00e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134133218  31 DEDYYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDEtahdKFLKINRAYEVLKDEDLRKKYDKYGEKGLQDEQQGG 109
Cdd:PTZ00037  27 NEKLYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGDPE----KFKEISRAYEVLSDPEKRKIYDEYGEEGLEGGEQPA 101
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 436-572 9.86e-19

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 90.20  E-value: 9.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 436 LYNVVAFAKES---VNAHVTTLRPENFPN--HEKEPWLVDFFAPWCPPCRALLPELRKASIQL---FGQLKFGTLDCTIH 507
Cdd:PTZ00102  16 LLAFAVFGSAEehfISEHVTVLTDSTFDKfiTENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLkekKSEIVLASVDATEE 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 134133218 508 EGLCNTYNIHAYPTTVIFNKSSIHEYEGHHSADGILEFIEDLVNPVVVTLgpESFQELVKRRKSS 572
Cdd:PTZ00102  96 MELAQEFGVRGYPTIKFFNKGNPVNYSGGRTADGIVSWIKKLTGPAVTEV--ESASEIKLIAKKI 158
PRK14289 PRK14289
molecular chaperone DnaJ;
33-111 1.61e-18

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 88.35  E-value: 1.61e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134133218  33 DYYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGLQDEQQGGRY 111
Cdd:PRK14289   6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGDKEAEEKFKEAAEAYDVLSDPDKRSRYDQFGHAGVGGAAGGGGF 84
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 553-643 2.06e-18

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: 81.12  E-value: 2.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  553 VVVTLGPESFQELVKrrKSSETWMVDFYAPWCGPCQALLPEWRRMARMLSGIVNVGTVDCQKHHSFCQSESVRAYPEIRL 632
Cdd:pfam00085   1 VVVVLTDANFDEVVQ--KSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIF 78

                          90
                  ....*....|.
gi 134133218  633 FPqNSNRRDQY 643
Cdd:pfam00085  79 FK-NGQPVDDY 88
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 33-98 2.12e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 88.02  E-value: 2.12e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134133218  33 DYYKLLGISREASTRDIRQAFKKLALTMHPDKNPnDETAHDKFLKINRAYEVLKDEDLRKKYDKYG 98
Cdd:PRK14292   3 DYYELLGVSRTASADEIKSAYRKLALKYHPDRNK-EKGAAEKFAQINEAYAVLSDAEKRAHYDRFG 67
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
32-107 2.32e-18

Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 80.53  E-value: 2.32e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134133218  32 EDYYKLLGISREASTRDIRQAFKKLALTMHPDKNPND-ETAHDKFLKINRAYEVLKDEDLRKKYD-KYGEKGLQDEQQ 107
Cdd:COG2214    5 KDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELkALAEELFQRLNEAYEVLSDPERRAEYDrELGQSGKGSASQ 82
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 450-550 5.35e-18

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: 79.86  E-value: 5.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 450 HVTTLRPENFPNH---EKEPWLVDFFAPWCPPCRALLPELRKASIQLFGQLKFGTLDCTIHEGLCNTYNIHAYPTTVIF- 525
Cdd:COG3118    1 AVVELTDENFEEEvleSDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLFk 80

                         90       100
                 ....*....|....*....|....*
gi 134133218 526 NKSSIHEYEGHHSADGILEFIEDLV 550
Cdd:COG3118   81 DGQPVDRFVGALPKEQLREFLDKVL 105
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 30-126 6.28e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 86.58  E-value: 6.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  30 SDEDYYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGLQDEQQG- 108
Cdd:PRK14286   2 SERSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNKESEEKFKEATEAYEILRDPKKRQAYDQFGKAGVNAGAGGf 81

                         90       100
                 ....*....|....*....|.
gi 134133218 109 --GRYESWNYYRYDFG-IYDD 126
Cdd:PRK14286  82 gqGAYTDFSDIFGDFGdIFGD 102
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 669-746 6.97e-18

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: 79.60  E-value: 6.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 669 VDLSPEDFKRKVLGGKDHWVLDFYAPWCGPCQQFAPEFEVLARMMKGT--VRAGKVDC-QAHYQTCQSAGIKAYPTVRFY 745
Cdd:cd02998    3 VELTDSNFDKVVGDDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFANEddVVIAKVDAdEANKDLAKKYGVSGFPTLKFF 82


                 .
gi 134133218 746 P 746
Cdd:cd02998   83 P 83
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 552-660 1.84e-17

PDIa family, N-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 comprised of the first TRX domain of ERdj5 located after the DnaJ domain at the N-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.


Pssm-ID: 239301 [Multi-domain]  Cd Length: 101  Bit Score: 78.34  E-value: 1.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 552 PVVVTLGPESFQELVKrrkSSETWMVDFYAPWCGPCQALLPEWRRMARMLSGIVNVGTVDCQKHHSFCQSESVRAYPEIR 631
Cdd:cd03003    1 PEIVTLDRGDFDAAVN---SGEIWFVNFYSPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDDRMLCRSQGVNSYPSLY 77

                         90       100
                 ....*....|....*....|....*....
gi 134133218 632 LFPQNSNrrdqYQTYNGwHRDAFSLKAWA 660
Cdd:cd03003   78 VFPSGMN----PEKYYG-DRSKESLVKFA 101
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 667-745 2.91e-17

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: 77.71  E-value: 2.91e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 667 ASVDLSPEDFKRKVLGGkDHWVLdFYAPWCGPCQQFAPEFEVLARMM---KGTVRAGKVDCQAHYQTCQSAGIKAYPTVR 743
Cdd:cd03005    1 GVLELTEDNFDHHIAEG-NHFVK-FFAPWCGHCKRLAPTWEQLAKKFnneNPSVKIAKVDCTQHRELCSEFQVRGYPTLL 78


                 ..
gi 134133218 744 FY 745
Cdd:cd03005   79 LF 80
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 450-570 3.26e-17

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: 85.11  E-value: 3.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  450 HVTTLRPENFPN--HEKEPWLVDFFAPWCPPCRALLPELRKASIQLFGQ---LKFGTLDCTIHEGLCNTYNIHAYPTTVI 524
Cdd:TIGR01130   2 DVLVLTKDNFDDfiKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKgppIKLAKVDATEEKDLAQKYGVSGYPTLKI 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 134133218  525 F--NKSSIHEYEGHHSADGILEFIEDLVNPVVVTLG-PESFQELVKRRK 570
Cdd:TIGR01130  82 FrnGEDSVSDYNGPRDADGIVKYMKKQSGPAVKEIEtVADLEAFLADDD 130
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 32-130 3.35e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 84.21  E-value: 3.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  32 EDYYKLLGISREASTRDIRQAFKKLALTMHPDKNP-NDETAHDKFLKINRAYEVLKDEDLRKKYDkygEKGLQDEQQGGR 110
Cdd:PRK14290   3 KDYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPgNKAEAEEKFKEISEAYEVLSDPQKRRQYD---QTGTVDFGAGGS 79

                         90       100
                 ....*....|....*....|
gi 134133218 111 YESWNyyryDFGIYDDDPEI 130
Cdd:PRK14290  80 NFNWD----NFTHFSDINDI 95
PRK14279 PRK14279
molecular chaperone DnaJ;
31-95 4.35e-17

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 84.01  E-value: 4.35e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 134133218  31 DEDYYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDETAHDKFLKINRAYEVLKDEDLRKKYD 95
Cdd:PRK14279   8 EKDFYKELGVSSDASAEEIKKAYRKLARELHPDANPGDPAAEERFKAVSEAHDVLSDPAKRKEYD 72
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 32-103 4.77e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 83.98  E-value: 4.77e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134133218  32 EDYYKLLGISREASTRDIRQAFKKLALTMHPDKNpNDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGLQ 103
Cdd:PRK14276   4 TEYYDRLGVSKDASQDEIKKAYRKLSKKYHPDIN-KEPGAEEKYKEVQEAYETLSDPQKRAAYDQYGAAGAN 74
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 554-693 5.77e-17

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: 84.34  E-value: 5.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  554 VVTLGPESFQELVKrrkSSETWMVDFYAPWCGPCQALLPEWRRMARMLS---GIVNVGTVDCQKHHSFCQSESVRAYPEI 630
Cdd:TIGR01130   3 VLVLTKDNFDDFIK---SHEFVLVEFYAPWCGHCKSLAPEYEKAADELKkkgPPIKLAKVDATEEKDLAQKYGVSGYPTL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134133218  631 RLFpqnSNRRDQYQTYNGwHRDAFSLKAWALS-SLPRASVDLSPEDFKrKVLGGKDHWVLDFYA 693
Cdd:TIGR01130  80 KIF---RNGEDSVSDYNG-PRDADGIVKYMKKqSGPAVKEIETVADLE-AFLADDDVVVIGFFK 138
PRK14295 PRK14295
molecular chaperone DnaJ;
31-116 5.99e-17

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 83.74  E-value: 5.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  31 DEDYYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDETAHDKFLKINRAYEVLKDEDLRKKYDK----YGEKGLQDEQ 106
Cdd:PRK14295   8 EKDYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDAKAEERFKEISEAYDVLSDEKKRKEYDEarslFGNGGFRPGP 87

                         90
                 ....*....|
gi 134133218 107 QGGRYESWNY 116
Cdd:PRK14295  88 GGGGGGGFNF 97
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 129-648 6.95e-17

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: 84.34  E-value: 6.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  129 EITTLDRGDFDAAVNSGEVWFVNFYFPRCSHCHDLAPTWREFA---KEMDGVIRIGAVNCGDNGMLCRSKGINSYPSLYV 205
Cdd:TIGR01130   2 DVLVLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAAdelKKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLKI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  206 FRAG-MNPEKYFNDRTKSSLTKfamqFVKSKVtelwqGNIYSEIERAfaerigwlitfcadtgdclesqtrrklagmldg 284
Cdd:TIGR01130  82 FRNGeDSVSDYNGPRDADGIVK----YMKKQS-----GPAVKEIETV--------------------------------- 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  285 lvnvgwmdctkqADLcESFEINTSTTALFppgssltqkgsvlFIQSLDtKEIYAQVLQ----HLPDLEILTKSSFEHKLA 360
Cdd:TIGR01130 120 ------------ADL-EAFLADDDVVVIG-------------FFKDLD-SELNDTFLSvaekLRDVYFFFAHSSDVAAFA 172

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  361 HhrwlvsFSFGRNDLASHEYKKLNallKNSHIQVGKVDCISDSelcsslyihkpcvavfkgvgIHDFeIHHGKDALynVV 440
Cdd:TIGR01130 173 K------LGAFPDSVVLFKPKDED---EKFSKVDGEMDTDVSD--------------------LEKF-IRAESLPL--VG 220

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  441 AFAKESvNAHVTTLRP--ENFPNHEKEpwlVDFFAPWcppcRALLPELRKASIQLFgqLKFGTLDCTIHEGLCNTYNIHA 518
Cdd:TIGR01130 221 EFTQET-AAKYFESGPlvVLYYNVDES---LDPFEEL----RNRFLEAAKKFRGKF--VNFAVADEEDFGRELEYFGLKA 290

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  519 --YPTTVIFNKSSIHEY---EGHHSADGILEFIEDLVN------------------PVVVTLGpESFQELVKRrkSSETW 575
Cdd:TIGR01130 291 ekFPAVAIQDLEGNKKYpmdQEEFSSENLEAFVKDFLDgklkpylksepipeddegPVKVLVG-KNFDEIVLD--ETKDV 367

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134133218  576 MVDFYAPWCGPCQALLPEWRRMARMLSGI---VNVGTVDCQK--HHSFcqseSVRAYPEIRLFPQNSNRrdQYQTYNG 648
Cdd:TIGR01130 368 LVEFYAPWCGHCKNLAPIYEELAEKYKDAesdVVIAKMDATAndVPPF----EVEGFPTIKFVPAGKKS--EPVPYDG 439
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 32-109 8.14e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 83.14  E-value: 8.14e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134133218  32 EDYYKLLGISREASTRDIRQAFKKLALTMHPDkNPNDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGLQDEQQGG 109
Cdd:PRK14300   3 QDYYQILGVSKTASQADLKKAYLKLAKQYHPD-TTDAKDAEKKFKEINAAYDVLKDEQKRAAYDRFGHDAFQNQQSRG 79
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 32-108 9.42e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 81.52  E-value: 9.42e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134133218  32 EDYYKLLGISREASTRDIRQAFKKLALTMHPDKNpNDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGLQDEQQG 108
Cdd:PRK14299   4 KDYYAILGVPKNASQDEIKKAFKKLARKYHPDVN-KSPGAEEKFKEINEAYTVLSDPEKRRIYDTYGTTAASAGWQG 79
termin_org_DnaJ TIGR03835
terminal organelle assembly protein TopJ; This model describes TopJ (MG_200, CbpA), a DnaJ ...
 33-105 9.96e-17

terminal organelle assembly protein TopJ; This model describes TopJ (MG_200, CbpA), a DnaJ homolog and probable assembly protein of the Mycoplasma terminal organelle. The terminal organelle is involved in both cytadherence and gliding motility. [Cellular processes, Chemotaxis and motility]


Pssm-ID: 274808 [Multi-domain]  Cd Length: 871  Bit Score: 84.87  E-value: 9.96e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134133218   33 DYYKLLGISREASTRDIRQAFKKLALTMHPDKNpNDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGLQDE 105
Cdd:TIGR03835   3 DYYEVLGIDRDADEQEIKKAFRKLAKKYHPDRN-KAPDAASIFAEINEANDVLSNPKKRANYDKYGHDGVDRE 74
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 33-125 1.29e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 82.56  E-value: 1.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  33 DYYKLLGISREASTRDIRQAFKKLALTMHPDKNpNDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGLQDEQQGGRYE 112
Cdd:PRK14283   6 DYYEVLGVDRNADKKEIKKAYRKLARKYHPDVS-EEEGAEEKFKEISEAYAVLSDDEKRQRYDQFGHAGMDGFSQEDIFN 84

                         90       100
                 ....*....|....*....|
gi 134133218 113 SWNY------YRYDFG-IYD 125
Cdd:PRK14283  85 NINFedifqgFGFGIGnIFD 104
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 32-127 1.33e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 82.53  E-value: 1.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  32 EDYYKLLGISREASTRDIRQAFKKLALTMHPDKNP-NDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGLQDEQQ--- 107
Cdd:PRK14282   4 KDYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPeNRKEAEQKFKEIQEAYEVLSDPQKRAMYDRFGYVGEQPPYQete 83

                         90       100
                 ....*....|....*....|...
gi 134133218 108 --GGRYEswNYYRyDFG-IYDDD 127
Cdd:PRK14282  84 sgGGFFE--DIFK-DFEnIFNRD 103
PRK14280 PRK14280
molecular chaperone DnaJ;
30-108 1.39e-16

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 82.46  E-value: 1.39e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134133218  30 SDEDYYKLLGISREASTRDIRQAFKKLALTMHPDKNpNDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEkglQDEQQG 108
Cdd:PRK14280   2 AKRDYYEVLGVSKSASKDEIKKAYRKLSKKYHPDIN-KEEGADEKFKEISEAYEVLSDDQKRAQYDQFGH---AGPNQG 76
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 669-773 1.44e-16

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: 76.15  E-value: 1.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 669 VDLSPEDFKRKVLGGKDHWVLDFYAPWCGPCQQFAPEFEVLARMMK---GTVRAGKVDC--QAHYQTCQSAGIKAYPTVR 743
Cdd:cd02992    4 IVLDAASFNSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRkwrPVVRVAAVDCadEENVALCRDFGVTGYPTLR 83

                         90       100       110
                 ....*....|....*....|....*....|.
gi 134133218 744 FYPTlGTTRRDQG-GEHINSRDATVIADILR 773
Cdd:cd02992   84 YFPP-FSKEATDGlKQEGPERDVNELREALI 113
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 669-756 3.37e-16

PDIa family, N-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 comprised of the first TRX domain of ERdj5 located after the DnaJ domain at the N-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.


Pssm-ID: 239301 [Multi-domain]  Cd Length: 101  Bit Score: 74.87  E-value: 3.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 669 VDLSPEDFKRKVLGGkDHWVLDFYAPWCGPCQQFAPEFEVLARMMKGTVRAGKVDCQAHYQTCQSAGIKAYPTVRFYPTL 748
Cdd:cd03003    4 VTLDRGDFDAAVNSG-EIWFVNFYSPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDDRMLCRSQGVNSYPSLYVFPSG 82


                 ....*...
gi 134133218 749 GTTRRDQG 756
Cdd:cd03003   83 MNPEKYYG 90
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 33-95 5.13e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 80.48  E-value: 5.13e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134133218  33 DYYKLLGISREASTRDIRQAFKKLALTMHPDKNPnDETAHDKFLKINRAYEVLKDEDLRKKYD 95
Cdd:PRK14278   4 DYYGLLGVSRNASDAEIKRAYRKLARELHPDVNP-DEEAQEKFKEISVAYEVLSDPEKRRIVD 65
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 450-546 7.37e-16

PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces cerevisiae MPD1 protein, which contains a single redox active TRX domain located at the N-terminus, and an ER retention signal at the C-terminus indicative of an ER-resident protein. MPD1 has been shown to suppress the maturation defect of carboxypeptidase Y caused by deletion of the yeast PDI1 gene. Other characterized members of this subfamily include the Aspergillus niger prpA protein and Giardia PDI-1. PrpA is non-essential to strain viability, however, its transcript level is induced by heterologous protein expression suggesting a possible role in oxidative protein folding during high protein production. Giardia PDI-1 has the ability to refold scrambled RNase and exhibits transglutaminase activity.


Pssm-ID: 239300 [Multi-domain]  Cd Length: 109  Bit Score: 73.94  E-value: 7.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 450 HVTTLRPENFPN---HEKEPWLVDFFAPWCPPCRALLPELRKASIQLFGQLKFGTLDCT--IHEGLCNTYNIHAYPTTVI 524
Cdd:cd03002    1 PVYELTPKNFDKvvhNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKELDGLVQVAAVDCDedKNKPLCGKYGVQGFPTLKV 80

                         90       100
                 ....*....|....*....|....*...
gi 134133218 525 FNKSSIH------EYEGHHSADGILEFI 546
Cdd:cd03002   81 FRPPKKAskhaveDYNGERSAKAIVDFV 108
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 554-643 9.55e-16

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: 73.44  E-value: 9.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 554 VVTLGPESFQELVKrrKSSETWMVDFYAPWCGPCQALLPEWRRMARMLSG--IVNVGTVDC-QKHHSFCQSESVRAYPEI 630
Cdd:cd02998    2 VVELTDSNFDKVVG--DDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFANedDVVIAKVDAdEANKDLAKKYGVSGFPTL 79

                         90
                 ....*....|...
gi 134133218 631 RLFPQNSNRRDQY 643
Cdd:cd02998   80 KFFPKGSTEPVKY 92
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 32-98 1.07e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 79.61  E-value: 1.07e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134133218  32 EDYYKLLGISREASTRDIRQAFKKLALTMHPDKNpNDETAHDKFLKINRAYEVLKDEDLRKKYDKYG 98
Cdd:PRK14296   4 KDYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLN-KSPDAHDKMVEINEAADVLLDKDKRKQYDQFG 69
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 127-212 1.47e-15

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: 73.46  E-value: 1.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 127 DPeITTLDRGDFDAAV-NSGEVWFVNFYFPRCSHCHDLAPTWREFAKEMD---GVIRIGAVNCGD--NGMLCRSKGINSY 200
Cdd:cd02992    1 DP-VIVLDAASFNSALlGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRkwrPVVRVAAVDCADeeNVALCRDFGVTGY 79

                         90
                 ....*....|..
gi 134133218 201 PSLYVFRAGMNP 212
Cdd:cd02992   80 PTLRYFPPFSKE 91
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 133-227 1.76e-15

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: 72.70  E-value: 1.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 133 LDRGDFDAAVNSGeVWFVNFYFPRCSHCHDLAPTWREFAKEM---DGVIRIGAVNCGDNGMLCRSKGINSYPSLYVFRAG 209
Cdd:cd03005    5 LTEDNFDHHIAEG-NHFVKFFAPWCGHCKRLAPTWEQLAKKFnneNPSVKIAKVDCTQHRELCSEFQVRGYPTLLLFKDG 83

                         90
                 ....*....|....*...
gi 134133218 210 MNPEKYFNDRTKSSLTKF 227
Cdd:cd03005   84 EKVDKYKGTRDLDSLKEF 101
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 130-228 2.15e-15

PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces cerevisiae MPD1 protein, which contains a single redox active TRX domain located at the N-terminus, and an ER retention signal at the C-terminus indicative of an ER-resident protein. MPD1 has been shown to suppress the maturation defect of carboxypeptidase Y caused by deletion of the yeast PDI1 gene. Other characterized members of this subfamily include the Aspergillus niger prpA protein and Giardia PDI-1. PrpA is non-essential to strain viability, however, its transcript level is induced by heterologous protein expression suggesting a possible role in oxidative protein folding during high protein production. Giardia PDI-1 has the ability to refold scrambled RNase and exhibits transglutaminase activity.


Pssm-ID: 239300 [Multi-domain]  Cd Length: 109  Bit Score: 72.78  E-value: 2.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 130 ITTLDRGDFDAAV-NSGEVWFVNFYFPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGD--NGMLCRSKGINSYPSLYVF 206
Cdd:cd03002    2 VYELTPKNFDKVVhNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKELDGLVQVAAVDCDEdkNKPLCGKYGVQGFPTLKVF 81

                         90       100
                 ....*....|....*....|....*..
gi 134133218 207 RAGMN-----PEKYFNDRTKSSLTKFA 228
Cdd:cd03002   82 RPPKKaskhaVEDYNGERSAKAIVDFV 108
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 138-227 3.00e-15

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: 71.88  E-value: 3.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  138 FDAAVNSGEVWF-VNFYFPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDNGMLCRSKGINSYPSLYVFRAGMNPEKYF 216
Cdd:pfam00085  10 FDEVVQKSSKPVlVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKNGQPVDDYV 89

                          90
                  ....*....|.
gi 134133218  217 NDRTKSSLTKF 227
Cdd:pfam00085  90 GARPKDALAAF 100
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 32-115 3.18e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 78.11  E-value: 3.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  32 EDYYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGLQDeqqGGRY 111
Cdd:PRK14285   3 RDYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKEAESIFKEATEAYEVLIDDNKRAQYDRFGHTAFEG---GGGF 79


                 ....
gi 134133218 112 ESWN 115
Cdd:PRK14285  80 EGFS 83
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 554-667 3.30e-15

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 75.43  E-value: 3.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 554 VVTLGPESFQELVKRRKSSET--WMVDFYAPWCGPCQALLPEWRRMARMLSGIVNVGTVDCQKHHSFCQSESVRAYPEIR 631
Cdd:PTZ00443  32 LVLLNDKNFEKLTQASTGATTgpWFVKFYAPWCSHCRKMAPAWERLAKALKGQVNVADLDATRALNLAKRFAIKGYPTLL 111

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 134133218 632 LFpqnsNRRDQYQtYNGWHRDAFSLKAWALSSLPRA 667
Cdd:PTZ00443 112 LF----DKGKMYQ-YEGGDRSTEKLAAFALGDFKKA 142
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 554-659 6.25e-15

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: 71.16  E-value: 6.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 554 VVTLGPESFQELVKRRKSsetwMVDFYAPWCGPCQALLPEWRRMARML---SGIVNVGTVDCQKHHSFCQSESVRAYPEI 630
Cdd:cd03005    2 VLELTEDNFDHHIAEGNH----FVKFFAPWCGHCKRLAPTWEQLAKKFnneNPSVKIAKVDCTQHRELCSEFQVRGYPTL 77

                         90       100
                 ....*....|....*....|....*....
gi 134133218 631 RLFpQNSNRRDQYQTyngwHRDAFSLKAW 659
Cdd:cd03005   78 LLF-KDGEKVDKYKG----TRDLDSLKEF 101
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 674-745 6.91e-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: 70.66  E-value: 6.91e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134133218 674 EDFKRKVLGGKDHwVLDFYAPWCGPCQQFAPEFEVLARmMKGTVRAGKVDCQAHYQTCQSAGIKAYPTVRFY 745
Cdd:cd02947    1 EEFEELIKSAKPV-VVDFWAPWCGPCKAIAPVLEELAE-EYPKVKFVKVDVDENPELAEEYGVRSIPTFLFF 70
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 671-746 9.48e-15

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: 70.40  E-value: 9.48e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134133218  671 LSPEDFKRKVLGGKDHWVLDFYAPWCGPCQQFAPEFEVLARMMKGTVRAGKVDCQAHYQTCQSAGIKAYPTVRFYP 746
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFK 76
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 554-660 1.44e-14

PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS reductases containing a C-terminal redox active TRX domain and an N-terminal reductase domain which is part of a superfamily that includes N type ATP PPases. APS reductase catalyzes the reduction of activated sulfate to sulfite, a key step in the biosynthesis of sulfur-containing metabolites. Sulfate is first activated by ATP sulfurylase, forming APS, which can be phosphorylated to 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Depending on the organism, either APS or PAPS can be used for sulfate reduction. Prokaryotes and fungi use PAPS, whereas plants use both APS and PAPS. Since plant-type APS reductase uses glutathione (GSH) as its electron donor, the C-terminal domain may function like glutaredoxin, a GSH-dependent member of the TRX superfamily. The flow of reducing equivalents goes from GSH -> C-terminal TRX domain -> N-terminal reductase domain -> APS. Plant-type APS reductase shows no homology to that of dissimilatory sulfate-reducing bacteria, which is an iron-sulfur flavoenzyme. Also included in the alignment is EYE2 from Chlamydomonas reinhardtii, a protein required for eyespot assembly.


Pssm-ID: 239291 [Multi-domain]  Cd Length: 109  Bit Score: 70.17  E-value: 1.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 554 VVTLGPESFQELVKRRKSSETWMVDFYAPWCGPCQALLPEWRRMARMLSGI-VNVGTVDCQKHH-SFCQSE-SVRAYPEI 630
Cdd:cd02993    3 VVTLSRAEIEALAKGERRNQSTLVVLYAPWCPFCQAMEASYEELAEKLAGSnVKVAKFNADGEQrEFAKEElQLKSFPTI 82

                         90       100       110
                 ....*....|....*....|....*....|
gi 134133218 631 RLFPQNSnrrDQYQTYNGWHRDAFSLKAWA 660
Cdd:cd02993   83 LFFPKNS---RQPIKYPSEQRDVDSLLMFV 109
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 468-547 1.78e-14

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: 69.51  E-value: 1.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 468 LVDFFAPWCPPCRALLPELRKASiQLFGQLKFGTLDCTIHEGLCNTYNIHAYPTTVIF-NKSSIHEYEGHHSADGILEFI 546
Cdd:cd02947   14 VVDFWAPWCGPCKAIAPVLEELA-EEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFkNGKEVDRVVGADPKEELEEFL 92


                 .
gi 134133218 547 E 547
Cdd:cd02947   93 E 93
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 560-648 2.76e-14

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: 69.41  E-value: 2.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 560 ESFQELvkrrKSSETWMVDFYAPWCGPCQALLPEWRRMARMLSGI---VNVGTVDCQKHHSFCQSESVRAYPEIRLFpqn 636
Cdd:cd03000    7 DSFKDV----RKEDIWLVDFYAPWCGHCKKLEPVWNEVGAELKSSgspVRVGKLDATAYSSIASEFGVRGYPTIKLL--- 79

                         90
                 ....*....|..
gi 134133218 637 snRRDQYQTYNG 648
Cdd:cd03000   80 --KGDLAYNYRG 89
PRK14288 PRK14288
molecular chaperone DnaJ;
34-127 3.36e-14

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 75.11  E-value: 3.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  34 YYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEKGLQdeQQGGRYES 113
Cdd:PRK14288   5 YYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKEAEEKFKLINEAYGVLSDEKKRALYDRYGKKGLN--QAGASQSD 82

                         90
                 ....*....|....
gi 134133218 114 WNYYRYDFGIYDDD 127
Cdd:PRK14288  83 FSDFFEDLGSFFED 96
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 669-753 3.71e-14

PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces cerevisiae MPD1 protein, which contains a single redox active TRX domain located at the N-terminus, and an ER retention signal at the C-terminus indicative of an ER-resident protein. MPD1 has been shown to suppress the maturation defect of carboxypeptidase Y caused by deletion of the yeast PDI1 gene. Other characterized members of this subfamily include the Aspergillus niger prpA protein and Giardia PDI-1. PrpA is non-essential to strain viability, however, its transcript level is induced by heterologous protein expression suggesting a possible role in oxidative protein folding during high protein production. Giardia PDI-1 has the ability to refold scrambled RNase and exhibits transglutaminase activity.


Pssm-ID: 239300 [Multi-domain]  Cd Length: 109  Bit Score: 69.31  E-value: 3.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 669 VDLSPEDFKRKVLGGKDHWVLDFYAPWCGPCQQFAPEFEVLARMMKGTVRAGKVDC--QAHYQTCQSAGIKAYPTVR-FY 745
Cdd:cd03002    3 YELTPKNFDKVVHNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKELDGLVQVAAVDCdeDKNKPLCGKYGVQGFPTLKvFR 82


                 ....*...
gi 134133218 746 PTLGTTRR 753
Cdd:cd03002   83 PPKKASKH 90
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 130-227 5.68e-14

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: 68.43  E-value: 5.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 130 ITTLDRGDFDAAV-NSGEVWFVNFYFPRCSHCHDLAPTWREFA---KEMDGVIrIGAVNCGD-NGMLCRSKGINSYPSLY 204
Cdd:cd02998    2 VVELTDSNFDKVVgDDKKDVLVEFYAPWCGHCKNLAPEYEKLAavfANEDDVV-IAKVDADEaNKDLAKKYGVSGFPTLK 80

                         90       100
                 ....*....|....*....|....
gi 134133218 205 VFRAG-MNPEKYFNDRTKSSLTKF 227
Cdd:cd02998   81 FFPKGsTEPVKYEGGRDLEDLVKF 104
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 148-236 1.14e-13

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 71.19  E-value: 1.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 148 WFVNFYFPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDNGMLCRSKGINSYPSLYVFRAGMNPEKYFNDRTKSSLTKF 227
Cdd:PTZ00443  55 WFVKFYAPWCSHCRKMAPAWERLAKALKGQVNVADLDATRALNLAKRFAIKGYPTLLLFDKGKMYQYEGGDRSTEKLAAF 134


                 ....*....
gi 134133218 228 AMQFVKSKV 236
Cdd:PTZ00443 135 ALGDFKKAL 143
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 450-546 1.48e-13

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: 67.34  E-value: 1.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 450 HVTTlrpENFPNH--EKEPWLVDFFAPWCPPCRALLPELRKASIQLFGQLK--FGTLDCTI--HEGLCNTYNIHAYPTTV 523
Cdd:cd02997    4 HLTD---EDFRKFlkKEKHVLVMFYAPWCGHCKKMKPEFTKAATELKEDGKgvLAAVDCTKpeHDALKEEYNVKGFPTFK 80

                         90       100
                 ....*....|....*....|....
gi 134133218 524 IFNK-SSIHEYEGHHSADGILEFI 546
Cdd:cd02997   81 YFENgKFVEKYEGERTAEDIIEFM 104
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 450-546 2.42e-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: 66.50  E-value: 2.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 450 HVTTLRPENFPNH---EKEPWLVDFFAPWCPPCRALLPELRKASiQLFGQLK---FGTLDCT-IHEGLCNTYNIHAYPTT 522
Cdd:cd02998    1 NVVELTDSNFDKVvgdDKKDVLVEFYAPWCGHCKNLAPEYEKLA-AVFANEDdvvIAKVDADeANKDLAKKYGVSGFPTL 79

                         90       100
                 ....*....|....*....|....*.
gi 134133218 523 VIFNKSSI--HEYEGHHSADGILEFI 546
Cdd:cd02998   80 KFFPKGSTepVKYEGGRDLEDLVKFV 105
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 554-652 3.25e-13

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: 66.52  E-value: 3.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 554 VVTLGPESFQELVKrrKSSETWMVDFYAPWCGPCQALLPEWRRMARML---SGIVNVGTVDC--QKHHSFCQSESVRAYP 628
Cdd:cd02992    3 VIVLDAASFNSALL--GSPSAWLVEFYASWCGHCRAFAPTWKKLARDLrkwRPVVRVAAVDCadEENVALCRDFGVTGYP 80

                         90       100
                 ....*....|....*....|....
gi 134133218 629 EIRLFPQNSNRRDQYQTYNGWHRD 652
Cdd:cd02992   81 TLRYFPPFSKEATDGLKQEGPERD 104
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 464-550 4.02e-13

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: 65.77  E-value: 4.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  464 KEPWLVDFFAPWCPPCRALLPELRKASIQLFGQLKFGTLDCTIHEGLCNTYNIHAYPTTVIF-NKSSIHEYEGHHSADGI 542
Cdd:TIGR01068  14 DKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFkNGKEVDRSVGALPKAAL 93


                  ....*...
gi 134133218  543 LEFIEDLV 550
Cdd:TIGR01068  94 KQLINKNL 101
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 554-633 8.80e-13

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: 65.23  E-value: 8.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 554 VVTLGPESFQELVkrRKSSETWMVDFYAPWCGPCQALLPEWRRMARMLSGIVNVGTVDCQKHHSFCQSESVRAYPEIRLF 633
Cdd:COG3118    2 VVELTDENFEEEV--LESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLF 79
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 450-546 1.14e-12

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: 64.61  E-value: 1.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 450 HVTTLRPENFPNH-EKEPWLVDFFAPWCPPCRALLP---ELRKASIQLFGQLKFGTLDCTIHEGLCNTYNIHAYPTTVIF 525
Cdd:cd03005    1 GVLELTEDNFDHHiAEGNHFVKFFAPWCGHCKRLAPtweQLAKKFNNENPSVKIAKVDCTQHRELCSEFQVRGYPTLLLF 80

                         90       100
                 ....*....|....*....|..
gi 134133218 526 -NKSSIHEYEGHHSADGILEFI 546
Cdd:cd03005   81 kDGEKVDKYKGTRDLDSLKEFV 102
PRK10996 PRK10996
thioredoxin 2; Provisional
 688-745 1.47e-12

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 65.48  E-value: 1.47e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 134133218 688 VLDFYAPWCGPCQQFAPEFEVLARMMKGTVRAGKVDCQAHYQTCQSAGIKAYPTVRFY 745
Cdd:PRK10996  56 VIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIF 113
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 651-774 1.51e-12

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 70.55  E-value: 1.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 651 RDAFSLKAWALSSLPRASVDLSPEDFKR------------KVLGGKDHWVLDFYAPWCGPCQQFAPEFEVLARMMK---G 715
Cdd:PTZ00102   4 RSILSSLFLLLILLAFAVFGSAEEHFISehvtvltdstfdKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKekkS 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 134133218 716 TVRAGKVDCQAHYQTCQSAGIKAYPTVRFYPtlGTTRRDQGGehinSRDATVIADILRQ 774
Cdd:PTZ00102  84 EIVLASVDATEEMELAQEFGVRGYPTIKFFN--KGNPVNYSG----GRTADGIVSWIKK 136
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 461-545 2.91e-12

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: 63.63  E-value: 2.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 461 NHEKEPWLVDFFAPWCPPCRALLPELRKASIQLFGQ---LKFGTLDCTIHEGLCNTYNIHAYPTTVIFNKSSIHEYEGHH 537
Cdd:cd03000   12 VRKEDIWLVDFYAPWCGHCKKLEPVWNEVGAELKSSgspVRVGKLDATAYSSIASEFGVRGYPTIKLLKGDLAYNYRGPR 91


                 ....*...
gi 134133218 538 SADGILEF 545
Cdd:cd03000   92 TKDDIVEF 99
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 129-238 3.07e-12

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 69.78  E-value: 3.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 129 EITTLDRGDFDAAVNSGEVWFVNFYFPRCSHCHDLAPTWREFAKEMD---GVIRIGAVNCGDNGMLCRSKGINSYPSLYV 205
Cdd:PTZ00102  33 HVTVLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKekkSEIVLASVDATEEMELAQEFGVRGYPTIKF 112

                         90       100       110
                 ....*....|....*....|....*....|...
gi 134133218 206 FRAGmNPEKYFNDRTKSSLTKFAMQFVKSKVTE 238
Cdd:PTZ00102 113 FNKG-NPVNYSGGRTADGIVSWIKKLTGPAVTE 144
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 30-108 4.45e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 68.50  E-value: 4.45e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134133218  30 SDEDYYKLLGISREASTRDIRQAFKKLALTMHPDKNpNDETAHDKFLKINRAYEVLKDEDLRKKYDKYGEKglqDEQQG 108
Cdd:PRK14287   2 SKRDYYEVLGVDRNASVDEVKKAYRKLARKYHPDVN-KAPDAEDKFKEVKEAYDTLSDPQKKAHYDQFGHT---DPNQG 76
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 685-745 6.22e-12

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: 62.47  E-value: 6.22e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134133218 685 DHWVLDFYAPWCGPCQQFAPEFEVLARMMKGT---VRAGKVDCQAHYQTCQSAGIKAYPTVRFY 745
Cdd:cd03000   16 DIWLVDFYAPWCGHCKKLEPVWNEVGAELKSSgspVRVGKLDATAYSSIASEFGVRGYPTIKLL 79
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 680-777 6.72e-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: 68.55  E-value: 6.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  680 VLGGKDHWVLDFYAPWCGPCQQFAPEFEVLARMMK---GTVRAGKVDCQAHYQTCQSAGIKAYPTVRFYptlgttrRDqg 756
Cdd:TIGR01130  14 FIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKkkgPPIKLAKVDATEEKDLAQKYGVSGYPTLKIF-------RN-- 84

                          90       100
                  ....*....|....*....|....*.
gi 134133218  757 GEHINS-----RDATVIADILRQRLQ 777
Cdd:TIGR01130  85 GEDSVSdyngpRDADGIVKYMKKQSG 110
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 455-551 8.04e-12

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 63.56  E-value: 8.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 455 RPENFPNHEKEPWLVDFFAPWCPPCRALLPELRKASiQLFGQLKFGTLDC-------------------TIHEG---LCN 512
Cdd:COG0526   19 KPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELA-EEYGGVVFVGVDVdenpeavkaflkelglpypVLLDPdgeLAK 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 134133218 513 TYNIHAYPTTVIFNKSS--IHEYEGHHSADGILEFIEDLVN 551
Cdd:COG0526   98 AYGVRGIPTTVLIDKDGkiVARHVGPLSPEELEEALEKLLA 138
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 130-209 8.74e-12

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: 62.14  E-value: 8.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 130 ITTLDRGDFDAAV-NSGEVWFVNFYFPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDNGMLCRSKGINSYPSLYVFRA 208
Cdd:COG3118    2 VVELTDENFEEEVlESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLFKD 81


                 .
gi 134133218 209 G 209
Cdd:COG3118   82 G 82
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 466-545 1.41e-11

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 65.03  E-value: 1.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 466 PWLVDFFAPWCPPCRALLPELRKASIQLFGQLKFGTLDCTIHEGLCNTYNIHAYPTTVIFNKSSIHEYE-GHHSADGILE 544
Cdd:PTZ00443  54 PWFVKFYAPWCSHCRKMAPAWERLAKALKGQVNVADLDATRALNLAKRFAIKGYPTLLLFDKGKMYQYEgGDRSTEKLAA 133


                 .
gi 134133218 545 F 545
Cdd:PTZ00443 134 F 134
PLN02309 PLN02309
5'-adenylylsulfate reductase
 526-659 1.53e-11

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 67.51  E-value: 1.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 526 NKSSIHEYEGHHSADGILEFIEDLVN-PVVVTLGPESFQELVKRRKSSETWMVDFYAPWCGPCQALLPEWRRMARMLSGI 604
Cdd:PLN02309 318 HKGNIKEEDNGAANDNGNAAVADIFNsQNVVALSRAGIENLLKLENRKEPWLVVLYAPWCPFCQAMEASYEELAEKLAGS 397

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 134133218 605 -VNVGT--VDcQKHHSFCQSE-SVRAYPEIRLFPQNSNRrdqYQTYNGWHRDAFSLKAW 659
Cdd:PLN02309 398 gVKVAKfrAD-GDQKEFAKQElQLGSFPTILLFPKNSSR---PIKYPSEKRDVDSLLSF 452
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 547-659 2.52e-11

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 66.70  E-value: 2.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 547 EDLVNPVVVTLGPESFQELVKrrkSSETWMVDFYAPWCGPCQALLPEWRRMARMLSGI---VNVGTVDCQKHHSFCQSES 623
Cdd:PTZ00102  27 EHFISEHVTVLTDSTFDKFIT---ENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKkseIVLASVDATEEMELAQEFG 103

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 134133218 624 VRAYPEIRLFpQNSNRRDqyqtYNGwHRDAFSLKAW 659
Cdd:PTZ00102 104 VRGYPTIKFF-NKGNPVN----YSG-GRTADGIVSW 133
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 146-228 2.98e-11

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: 60.55  E-value: 2.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 146 EVWFVNFYFPRCSHCHDLAPTWREFAKEMDGV---IRIGAVNCGDNGMLCRSKGINSYPSLYVFRAGMNPEkYFNDRTKS 222
Cdd:cd03000   16 DIWLVDFYAPWCGHCKKLEPVWNEVGAELKSSgspVRVGKLDATAYSSIASEFGVRGYPTIKLLKGDLAYN-YRGPRTKD 94


                 ....*.
gi 134133218 223 SLTKFA 228
Cdd:cd03000   95 DIVEFA 100
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
30-88 7.93e-11

DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 58.65  E-value: 7.93e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 134133218  30 SDEDYYKLLGISREASTRDIRQAFKKLALTMHPDK----NPNDE--TAHDKFLKINRAYEVLKDE 88
Cdd:COG1076    2 QLDDAFELLGLPPDADDAELKRAYRKLQREHHPDRlaagLPEEEqrLALQKAAAINEAYETLKDP 66
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 669-745 1.48e-10

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: 1.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 669 VDLSPEDFkRKVLGGKDHWVLDFYAPWCGPCQQFAPEFEVLARMMK---GTVRAGkVDC--QAHYQTCQSAGIKAYPTVR 743
Cdd:cd02997    3 VHLTDEDF-RKFLKKEKHVLVMFYAPWCGHCKKMKPEFTKAATELKedgKGVLAA-VDCtkPEHDALKEEYNVKGFPTFK 80


                 ..
gi 134133218 744 FY 745
Cdd:cd02997   81 YF 82
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 554-659 3.38e-10

5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the assimilation of inorganic sulfate, is closely related to the thioredoxin-dependent PAPS reductase of Bacteria (CysH) and Saccharomyces cerevisiae. However, it has its own C-terminal thioredoxin-like domain and is not thioredoxin-dependent. Also, it has a substrate preference for 5'-adenylylsulfate (APS) over 3'-phosphoadenylylsulfate (PAPS) so the pathway does not require an APS kinase (CysC) to convert APS to PAPS. Arabidopsis thaliana appears to have three isozymes, all able to complement E. coli CysH mutants (even in backgrounds lacking thioredoxin or APS kinase) but likely localized to different compartments in Arabidopsis. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 273072 [Multi-domain]  Cd Length: 463  Bit Score: 63.11  E-value: 3.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  554 VVTLGPESFQELVKRRKSSETWMVDFYAPWCGPCQALLPEWRRMARMLSGI-VNVGTVDCQ-KHHSFCQSE-SVRAYPEI 630
Cdd:TIGR00424 353 VVSLSRPGIENLLKLEERKEAWLVVLYAPWCPFCQAMEASYLELAEKLAGSgVKVAKFRADgDQKEFAKQElQLGSFPTI 432

                          90       100
                  ....*....|....*....|....*....
gi 134133218  631 RLFPQNSNRRDQYQTYngwHRDAFSLKAW 659
Cdd:TIGR00424 433 LFFPKHSSRPIKYPSE---KRDVDSLMSF 458
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 465-545 5.46e-10

PDIa family, N-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 comprised of the first TRX domain of ERdj5 located after the DnaJ domain at the N-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.


Pssm-ID: 239301 [Multi-domain]  Cd Length: 101  Bit Score: 57.15  E-value: 5.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 465 EPWLVDFFAPWCPPCRALLPELRKASIQLFGQLKFGTLDCTIHEGLCNTYNIHAYPTTVIFNKSSIHE-YEGHHSADGIL 543
Cdd:cd03003   19 EIWFVNFYSPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDDRMLCRSQGVNSYPSLYVFPSGMNPEkYYGDRSKESLV 98


                 ..
gi 134133218 544 EF 545
Cdd:cd03003   99 KF 100
PRK10266 PRK10266
curved DNA-binding protein;
32-96 6.51e-10

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 61.38  E-value: 6.51e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134133218  32 EDYYKLLGISREASTRDIRQAFKKLALTMHPD--KNPNDETahdKFLKINRAYEVLKDEDLRKKYDK 96
Cdd:PRK10266   4 KDYYAIMGVKPTDDLKTIKTAYRRLARKYHPDvsKEPDAEA---RFKEVAEAWEVLSDEQRRAEYDQ 67
PTZ00051 PTZ00051
thioredoxin; Provisional
 672-745 7.10e-10

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 56.81  E-value: 7.10e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134133218 672 SPEDFKrKVLGGKDHWVLDFYAPWCGPCQQFAPEFEVLARMMKGTVRAgKVDCQAHYQTCQSAGIKAYPTVRFY 745
Cdd:PTZ00051   7 SQAEFE-STLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFV-KVDVDELSEVAEKENITSMPTFKVF 78
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 31-139 8.38e-10

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 62.50  E-value: 8.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218   31 DEDYYKLLGISREASTRDIRQAFKKLALTMHPDKNPNDETAHdKFLKINRAYEVLKDEDLRKKYDKYGEKGLqdeQQGGR 110
Cdd:PTZ00341  572 DTLFYDILGVGVNADMKEISERYFKLAENYYPPKRSGNEGFH-KFKKINEAYQILGDIDKKKMYNKFGYDGI---KGVNF 647

                          90       100       110
                  ....*....|....*....|....*....|...
gi 134133218  111 YESWNYYRY----DFGIYDDDPEITTLDRGDFD 139
Cdd:PTZ00341  648 IHPSIFYLLasleKFADFTGSPQIVTLLKFFFE 680
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 687-742 1.40e-09

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 58.87  E-value: 1.40e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 134133218 687 WVLDFYAPWCGPCQQFAPEFEVLARMMKGTVRAGKVDCQAHYQTCQSAGIKAYPTV 742
Cdd:PTZ00443  55 WFVKFYAPWCSHCRKMAPAWERLAKALKGQVNVADLDATRALNLAKRFAIKGYPTL 110
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 554-633 2.51e-09

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: 55.40  E-value: 2.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 554 VVTLGPESFQELVKRRKSSetwMVDFYAPWCGPCQALLPEWRRMARML---SGIVNVGtVDCQK-HHSFCQSE-SVRAYP 628
Cdd:cd02997    2 VVHLTDEDFRKFLKKEKHV---LVMFYAPWCGHCKKMKPEFTKAATELkedGKGVLAA-VDCTKpEHDALKEEyNVKGFP 77


                 ....*
gi 134133218 629 EIRLF 633
Cdd:cd02997   78 TFKYF 82
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 468-546 2.88e-09

PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain, similar to that of PDIa, with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. The CXFS motif in the N-terminal domain allows ERp44 to form stable reversible mixed disulfides with its substrates. Through this activity, ERp44 mediates the ER localization of Ero1alpha, a protein that oxidizes protein disulfide isomerases into their active form. ERp44 also prevents the secretion of unassembled cargo protein with unpaired cysteines. It also modulates the activity of inositol 1,4,5-triphosphate type I receptor (IP3R1), an intracellular channel protein that mediates calcium release from the ER to the cytosol.


Pssm-ID: 239294 [Multi-domain]  Cd Length: 108  Bit Score: 55.09  E-value: 2.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 468 LVDFFAPWCPPCRALLPELRKAS---IQLF---GQLKFGTLDCTIHEGLCNTYNIHAYPTTVIFNKSSI--HEYEGHHSA 539
Cdd:cd02996   22 LVNFYADWCRFSQMLHPIFEEAAakiKEEFpdaGKVVWGKVDCDKESDIADRYRINKYPTLKLFRNGMMmkREYRGQRSV 101


                 ....*..
gi 134133218 540 DGILEFI 546
Cdd:cd02996  102 EALAEFV 108
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 560-635 3.40e-09

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: 54.60  E-value: 3.40e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134133218  560 ESFQELVKrrKSSETWMVDFYAPWCGPCQALLPEWRRMARMLSGIVNVGTVDCQKHHSFCQSESVRAYPEIRLFPQ 635
Cdd:TIGR01068   4 ANFDETIA--SSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKN 77
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 468-533 3.43e-09

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: 53.86  E-value: 3.43e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134133218 468 LVDFFAPWCPPCRALLPELRKASiQLFGQLKFGTLDCTIHEGLCNT---YNIHAYPTTVIFNKSSIHEY 533
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELA-LLNKGVKFEAVDVDEDPALEKElkrYGVGGVPTLVVFGPGIGVKY 68
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 129-232 4.17e-09

PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain, similar to that of PDIa, with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. The CXFS motif in the N-terminal domain allows ERp44 to form stable reversible mixed disulfides with its substrates. Through this activity, ERp44 mediates the ER localization of Ero1alpha, a protein that oxidizes protein disulfide isomerases into their active form. ERp44 also prevents the secretion of unassembled cargo protein with unpaired cysteines. It also modulates the activity of inositol 1,4,5-triphosphate type I receptor (IP3R1), an intracellular channel protein that mediates calcium release from the ER to the cytosol.


Pssm-ID: 239294 [Multi-domain]  Cd Length: 108  Bit Score: 54.70  E-value: 4.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 129 EITTLDRGDFDAAVNSGEVWFVNFYFPRCSHCHDLAPTWREFAKEM------DGVIRIGAVNCGDNGMLCRSKGINSYPS 202
Cdd:cd02996    2 EIVSLTSGNIDDILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIkeefpdAGKVVWGKVDCDKESDIADRYRINKYPT 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 134133218 203 LYVFRAGMNPEKYFndRTKSSLTKFAmQFV 232
Cdd:cd02996   82 LKLFRNGMMMKREY--RGQRSVEALA-EFV 108
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 560-633 4.60e-09

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: 54.10  E-value: 4.60e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134133218 560 ESFQELVKRRKSSetwMVDFYAPWCGPCQALLPEWRRMARMLSGIVnVGTVDCQKHHSFCQSESVRAYPEIRLF 633
Cdd:cd02947    1 EEFEELIKSAKPV---VVDFWAPWCGPCKAIAPVLEELAEEYPKVK-FVKVDVDENPELAEEYGVRSIPTFLFF 70
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 552-648 7.01e-09

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: 54.10  E-value: 7.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 552 PVVVTLGpESFQELVKrrKSSETWMVDFYAPWCGPCQALLPEWRRMARMLSGIVNV--GTVDCQK--HHSfcqSESVRAY 627
Cdd:cd02995    1 PVKVVVG-KNFDEVVL--DSDKDVLVEFYAPWCGHCKALAPIYEELAEKLKGDDNVviAKMDATAndVPS---EFVVDGF 74

                         90       100
                 ....*....|....*....|.
gi 134133218 628 PEIRLFPqnSNRRDQYQTYNG 648
Cdd:cd02995   75 PTILFFP--AGDKSNPIKYEG 93
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 149-227 1.22e-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: 53.33  E-value: 1.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 149 FVNFYFPRCSHCHDLAPTWREFAKEMDGV--IRIGAVNcGDNGMLCRSKGINSYPSLYVFRAGM--NPEKYFNDRTKSSL 224
Cdd:cd02995   22 LVEFYAPWCGHCKALAPIYEELAEKLKGDdnVVIAKMD-ATANDVPSEFVVDGFPTILFFPAGDksNPIKYEGDRTLEDL 100


                 ...
gi 134133218 225 TKF 227
Cdd:cd02995  101 IKF 103
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 575-611 1.36e-08

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: 53.15  E-value: 1.36e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 134133218 575 WMVDFYAPWCGPCQALLPEWRRMARMLSGI-VNVGTVD 611
Cdd:cd02994   19 WMIEFYAPWCPACQQLQPEWEEFADWSDDLgINVAKVD 56
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 137-209 1.75e-08

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: 52.56  E-value: 1.75e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134133218 137 DFDAAVNSGEVWFVNFYFPRCSHCHDLAPTWREFAKEMDGViRIGAVNCGDNGMLCRSKGINSYPSLYVFRAG 209
Cdd:cd02947    2 EFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKV-KFVKVDVDENPELAEEYGVRSIPTFLFFKNG 73
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 679-746 2.10e-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: 52.56  E-value: 2.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 679 KVLGGKDHW--VLD--------FYAPWCGPCQQFAPEFEVLARMMKGT--VRAGKVDCQA-----HYQTcqsagiKAYPT 741
Cdd:cd02995    3 KVVVGKNFDevVLDsdkdvlveFYAPWCGHCKALAPIYEELAEKLKGDdnVVIAKMDATAndvpsEFVV------DGFPT 76


                 ....*
gi 134133218 742 VRFYP 746
Cdd:cd02995   77 ILFFP 81
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 467-548 2.26e-08

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: 52.38  E-value: 2.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 467 WLVDFFAPWCPPCRALLP---ELRKASIQLfgQLKFGTLDCTIHEGLCNTYNIHAYPTtvIFN-KSSI-HEYEGHHSADG 541
Cdd:cd02994   19 WMIEFYAPWCPACQQLQPeweEFADWSDDL--GINVAKVDVTQEPGLSGRFFVTALPT--IYHaKDGVfRRYQGPRDKED 94


                 ....*..
gi 134133218 542 ILEFIED 548
Cdd:cd02994   95 LISFIEE 101
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 688-742 2.99e-08

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: 51.89  E-value: 2.99e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 134133218 688 VLDFYAPWCGPCQQFAPEFEVLARMMKGTVRAGKVDCQAHYQTCQSAGIKAYPTV 742
Cdd:cd02956   16 VVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTV 70
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 655-715 6.28e-08

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 52.38  E-value: 6.28e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134133218 655 SLKAWALSSLPRASVDLSpeDFKRKVLggkdhwVLDFYAPWCGPCQQFAPEFEVLARMMKG 715
Cdd:COG0526    7 PAPDFTLTDLDGKPLSLA--DLKGKPV------LVNFWATWCPPCRAEMPVLKELAEEYGG 59
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 466-527 1.03e-07

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: 50.35  E-value: 1.03e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134133218 466 PWLVDFFAPWCPPCRALLPELRKASIQLFGQLKFGTLDCTIHEGLCNTYNIHAYPTTVIFNK 527
Cdd:cd02956   14 PVVVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAA 75
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 467-537 1.11e-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: 50.73  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 467 WLVDFFAPWCPPCRALLPELRKASIQLF---GQLKFGTLDCTIHE--GLCNTYNIHAYPTTVIF----NKSSIHE-YEGH 536
Cdd:cd02992   22 WLVEFYASWCGHCRAFAPTWKKLARDLRkwrPVVRVAAVDCADEEnvALCRDFGVTGYPTLRYFppfsKEATDGLkQEGP 101


                 .
gi 134133218 537 H 537
Cdd:cd02992  102 E 102
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 133-227 1.54e-07

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: 50.01  E-value: 1.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 133 LDRGDFDAAVNSGEVWFVNFYFPRCSHCHDLAPTWREFAKEM--DGVIRIGAVNC--GDNGMLCRSKGINSYPSLYVFRA 208
Cdd:cd02997    5 LTDEDFRKFLKKEKHVLVMFYAPWCGHCKKMKPEFTKAATELkeDGKGVLAAVDCtkPEHDALKEEYNVKGFPTFKYFEN 84

                         90
                 ....*....|....*....
gi 134133218 209 GMNPEKYFNDRTKSSLTKF 227
Cdd:cd02997   85 GKFVEKYEGERTAEDIIEF 103
trxA PRK09381
thioredoxin TrxA;
669-745 1.73e-07

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 50.06  E-value: 1.73e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134133218 669 VDLSPEDFKRKVLGGKDHWVLDFYAPWCGPCQQFAPEFEVLARMMKGTVRAGKVDCQAHYQTCQSAGIKAYPTVRFY 745
Cdd:PRK09381   6 IHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLF 82
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 684-723 4.41e-07

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: 48.91  E-value: 4.41e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 134133218 684 KDHWVLDFYAPWCGPCQQFAPEFEVLARMMKG-TVRAGKVD 723
Cdd:cd02994   16 EGEWMIEFYAPWCPACQQLQPEWEEFADWSDDlGINVAKVD 56
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 687-746 4.94e-07

PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS reductases containing a C-terminal redox active TRX domain and an N-terminal reductase domain which is part of a superfamily that includes N type ATP PPases. APS reductase catalyzes the reduction of activated sulfate to sulfite, a key step in the biosynthesis of sulfur-containing metabolites. Sulfate is first activated by ATP sulfurylase, forming APS, which can be phosphorylated to 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Depending on the organism, either APS or PAPS can be used for sulfate reduction. Prokaryotes and fungi use PAPS, whereas plants use both APS and PAPS. Since plant-type APS reductase uses glutathione (GSH) as its electron donor, the C-terminal domain may function like glutaredoxin, a GSH-dependent member of the TRX superfamily. The flow of reducing equivalents goes from GSH -> C-terminal TRX domain -> N-terminal reductase domain -> APS. Plant-type APS reductase shows no homology to that of dissimilatory sulfate-reducing bacteria, which is an iron-sulfur flavoenzyme. Also included in the alignment is EYE2 from Chlamydomonas reinhardtii, a protein required for eyespot assembly.


Pssm-ID: 239291 [Multi-domain]  Cd Length: 109  Bit Score: 48.99  E-value: 4.94e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134133218 687 WVLDFYAPWCGPCQQFAPEFEVLARMMKGT-VRAGKV--DCQAHYQTCQSAGIKAYPTVRFYP 746
Cdd:cd02993   24 TLVVLYAPWCPFCQAMEASYEELAEKLAGSnVKVAKFnaDGEQREFAKEELQLKSFPTILFFP 86
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 149-210 5.11e-07

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: 47.69  E-value: 5.11e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 134133218 149 FVNFYFPRCSHCHDLAPTWREFAKEMDGViRIGAVNCGDNGMLCRSK---GINSYPSLYVFRAGM 210
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELALLNKGV-KFEAVDVDEDPALEKELkryGVGGVPTLVVFGPGI 64
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 149-227 8.22e-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: 52.37  E-value: 8.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  149 FVNFYFPRCSHCHDLAPTWREFAKEM----DGVIrIGAVNCGDNGMlcRSKGINSYPSLYVFRAG--MNPEKYFNDRTKS 222
Cdd:TIGR01130 368 LVEFYAPWCGHCKNLAPIYEELAEKYkdaeSDVV-IAKMDATANDV--PPFEVEGFPTIKFVPAGkkSEPVPYDGDRTLE 444


                  ....*
gi 134133218  223 SLTKF 227
Cdd:TIGR01130 445 DFSKF 449
PTZ00051 PTZ00051
thioredoxin; Provisional
 573-637 1.48e-06

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 47.18  E-value: 1.48e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 134133218 573 ETWMVDFYAPWCGPCQALLPEWRRMARMLSGIVNVgTVDCQKHHSFCQSESVRAYPEIRLFPQNS 637
Cdd:PTZ00051  19 ELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFV-KVDVDELSEVAEKENITSMPTFKVFKNGS 82
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 145-227 2.04e-06

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: 46.99  E-value: 2.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 145 GEvWFVNFYFPRCSHCHDLAPTWREFAKEMDGV-IRIGAVNCGDNGMLCRSKGINSYPSLY-----VFRagmnpeKYFND 218
Cdd:cd02994   17 GE-WMIEFYAPWCPACQQLQPEWEEFADWSDDLgINVAKVDVTQEPGLSGRFFVTALPTIYhakdgVFR------RYQGP 89


                 ....*....
gi 134133218 219 RTKSSLTKF 227
Cdd:cd02994   90 RDKEDLISF 98
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 128-228 2.73e-06

PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS reductases containing a C-terminal redox active TRX domain and an N-terminal reductase domain which is part of a superfamily that includes N type ATP PPases. APS reductase catalyzes the reduction of activated sulfate to sulfite, a key step in the biosynthesis of sulfur-containing metabolites. Sulfate is first activated by ATP sulfurylase, forming APS, which can be phosphorylated to 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Depending on the organism, either APS or PAPS can be used for sulfate reduction. Prokaryotes and fungi use PAPS, whereas plants use both APS and PAPS. Since plant-type APS reductase uses glutathione (GSH) as its electron donor, the C-terminal domain may function like glutaredoxin, a GSH-dependent member of the TRX superfamily. The flow of reducing equivalents goes from GSH -> C-terminal TRX domain -> N-terminal reductase domain -> APS. Plant-type APS reductase shows no homology to that of dissimilatory sulfate-reducing bacteria, which is an iron-sulfur flavoenzyme. Also included in the alignment is EYE2 from Chlamydomonas reinhardtii, a protein required for eyespot assembly.


Pssm-ID: 239291 [Multi-domain]  Cd Length: 109  Bit Score: 46.68  E-value: 2.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 128 PEITTLDRGDFDAAV---NSGEVWFVNFYFPRCSHCHDLAPTWREFAKEMDGV-IRIGAVNC-GDNGMLCRSK-GINSYP 201
Cdd:cd02993    1 EAVVTLSRAEIEALAkgeRRNQSTLVVLYAPWCPFCQAMEASYEELAEKLAGSnVKVAKFNAdGEQREFAKEElQLKSFP 80

                         90       100
                 ....*....|....*....|....*....
gi 134133218 202 SLYVFRAGM-NPEKYFND-RTKSSLTKFA 228
Cdd:cd02993   81 TILFFPKNSrQPIKYPSEqRDVDSLLMFV 109
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 468-546 2.78e-06

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: 46.40  E-value: 2.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 468 LVDFFAPWCPPCRALLPELRKASIQLFGQ--LKFGTLDCTIHEgLCNTYNIHAYPTTVIFNKSSIHE---YEGHHSADGI 542
Cdd:cd02995   22 LVEFYAPWCGHCKALAPIYEELAEKLKGDdnVVIAKMDATAND-VPSEFVVDGFPTILFFPAGDKSNpikYEGDRTLEDL 100


                 ....
gi 134133218 543 LEFI 546
Cdd:cd02995  101 IKFI 104
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 127-206 3.24e-06

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 47.38  E-value: 3.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 127 DPEITTLDRGDFDAAVNSGEVWFVNFYFPRCSHCHDLAPTWREFAKEMDGVIRIGaVNCGDN------------------ 188
Cdd:COG0526   10 DFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYGGVVFVG-VDVDENpeavkaflkelglpypvl 88

                         90       100
                 ....*....|....*....|..
gi 134133218 189 ----GMLCRSKGINSYPSLYVF 206
Cdd:COG0526   89 ldpdGELAKAYGVRGIPTTVLI 110
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 462-546 3.91e-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: 46.20  E-value: 3.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 462 HEKEPWLVDFFAPWCPPCRALLPELRKASiQLFGQLKFGTLD-CTIHEGLCNTYNIHAYPTTVIFNKSSIHEYEGHHSAD 540
Cdd:cd02999   16 NREDYTAVLFYASWCPFSASFRPHFNALS-SMFPQIRHLAIEeSSIKPSLLSRYGVVGFPTILLFNSTPRVRYNGTRTLD 94


                 ....*.
gi 134133218 541 GILEFI 546
Cdd:cd02999   95 SLAAFY 100
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 441-495 6.08e-06

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: 46.03  E-value: 6.08e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 134133218 441 AFAKESVNAHVTTLRPENFPNHekePWLVDFFAPWCPPCRALLPEL----RKASIQLFG 495
Cdd:cd03010    5 AFSLPALPGPDKTLTSADLKGK---PYLLNVWASWCAPCREEHPVLmalaRQGRVPIYG 60
trxA PRK09381
thioredoxin TrxA;
468-530 9.59e-06

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 45.06  E-value: 9.59e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134133218 468 LVDFFAPWCPPCRALLPELRKASIQLFGQLKFGTLDCTIHEGLCNTYNIHAYPTTVIFNKSSI 530
Cdd:PRK09381  25 LVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEV 87
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 576-630 1.06e-05

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: 43.84  E-value: 1.06e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 134133218 576 MVDFYAPWCGPCQALLPEWRRMARMLSGIVnVGTVDC---QKHHSFCQSESVRAYPEI 630
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELALLNKGVK-FEAVDVdedPALEKELKRYGVGGVPTL 57
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
374-548 1.07e-05

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 46.59  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  374 DLASHEYKKLNALLKN--SHIQVGkvdCISDSELCSSLYIHKPCVAVFKGVGIHDFEIHHGKDALYNVVAFAKESVNAHV 451
Cdd:pfam13848   3 DKDSPLYEIFRKAAKElkGDVRFG---ITFSKEVADKYNIKEPAILLFRKFDEETVHYPGDSINFEDLKKFIQKNCLPLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  452 TTLRPENFPN--HEKEPWLVDFFAPWCP-PCRALLPELRKASIQLFGQLKFGTLDCTIHEGLCNTYNI--HAYPTTVIFN 526
Cdd:pfam13848  80 REFTPENAEElfEEGIPPLLLLFLKKDDeSTEEFKKALEKVAKKFRGKINFALVDAKSFGRPLEYFGLseSDLPVIVIVD 159

                         170       180
                  ....*....|....*....|....*.
gi 134133218  527 KSSiHEY----EGHHSADGILEFIED 548
Cdd:pfam13848 160 SFS-HMYkyfpSDEFSPESLKEFIND 184
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 660-715 1.16e-05

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: 44.92  E-value: 1.16e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 134133218 660 ALSSLPRASVDLSpeDFKRKVLggkdhwVLDFYAPWCGPCQQFAPEFEVLARMMKG 715
Cdd:cd02966    3 SLPDLDGKPVSLS--DLKGKVV------LVNFWASWCPPCRAEMPELEALAKEYKD 50
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 575-605 1.16e-05

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 45.84  E-value: 1.16e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 134133218 575 WMVDFYAPWCGPCQALLPEWRRMARMLSGIV 605
Cdd:COG0526   31 VLVNFWATWCPPCRAEMPVLKELAEEYGGVV 61
PRK10996 PRK10996
thioredoxin 2; Provisional
 466-527 1.67e-05

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 45.45  E-value: 1.67e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134133218 466 PWLVDFFAPWCPPCRALLPELRKASIQLFGQLKFGTLDCTIHEGLCNTYNIHAYPTTVIFNK 527
Cdd:PRK10996  54 PVVIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFKN 115
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 554-633 1.78e-05

PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain, similar to that of PDIa, with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. The CXFS motif in the N-terminal domain allows ERp44 to form stable reversible mixed disulfides with its substrates. Through this activity, ERp44 mediates the ER localization of Ero1alpha, a protein that oxidizes protein disulfide isomerases into their active form. ERp44 also prevents the secretion of unassembled cargo protein with unpaired cysteines. It also modulates the activity of inositol 1,4,5-triphosphate type I receptor (IP3R1), an intracellular channel protein that mediates calcium release from the ER to the cytosol.


Pssm-ID: 239294 [Multi-domain]  Cd Length: 108  Bit Score: 44.30  E-value: 1.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 554 VVTLGPESFQELVKrrkSSETWMVDFYAPWCGPCQALLPEWRRMARML------SGIVNVGTVDCQKHHSFCQSESVRAY 627
Cdd:cd02996    3 IVSLTSGNIDDILQ---SAELVLVNFYADWCRFSQMLHPIFEEAAAKIkeefpdAGKVVWGKVDCDKESDIADRYRINKY 79


                 ....*.
gi 134133218 628 PEIRLF 633
Cdd:cd02996   80 PTLKLF 85
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 688-744 2.51e-05

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: 43.80  E-value: 2.51e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 134133218 688 VLDFYAPWCGPCQQFAPEFEVLARMMKGTVRAGKVDCQAHYQTCQSAGIKAYPTVRF 744
Cdd:cd02984   18 VLHFWAPWAEPCKQMNQVFEELAKEAFPSVLFLSIEAEELPEISEKFEITAVPTFVF 74
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 466-490 3.11e-05

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: 43.76  E-value: 3.11e-05
                         10        20
                 ....*....|....*....|....*
gi 134133218 466 PWLVDFFAPWCPPCRALLPELRKAS 490
Cdd:cd02966   21 VVLVNFWASWCPPCRAEMPELEALA 45
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 680-770 3.32e-05

PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain, similar to that of PDIa, with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. The CXFS motif in the N-terminal domain allows ERp44 to form stable reversible mixed disulfides with its substrates. Through this activity, ERp44 mediates the ER localization of Ero1alpha, a protein that oxidizes protein disulfide isomerases into their active form. ERp44 also prevents the secretion of unassembled cargo protein with unpaired cysteines. It also modulates the activity of inositol 1,4,5-triphosphate type I receptor (IP3R1), an intracellular channel protein that mediates calcium release from the ER to the cytosol.


Pssm-ID: 239294 [Multi-domain]  Cd Length: 108  Bit Score: 43.53  E-value: 3.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 680 VLGGKDHWVLDFYAPWCGPCQQFAPEFEVLARMMK------GTVRAGKVDCQAHYQTCQSAGIKAYPTVR-FYPTLGTTR 752
Cdd:cd02996   14 ILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKeefpdaGKVVWGKVDCDKESDIADRYRINKYPTLKlFRNGMMMKR 93

                         90
                 ....*....|....*...
gi 134133218 753 rdqggEHINSRDATVIAD 770
Cdd:cd02996   94 -----EYRGQRSVEALAE 106
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 439-495 5.02e-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: 44.77  E-value: 5.02e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  439 VVAFAKESVNAHVTTLRPENFPnhEKEPWLVDFFAPWCPPCRA---LLPELRKASIQLFG 495
Cdd:TIGR00385  40 VPAFRLASLDEPGQFYTADVLT--QGKPVLLNVWASWCPPCRAehpYLNELAKQGLPIVG 97
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 276-318 6.17e-05

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: 42.66  E-value: 6.17e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 134133218 276 RKLAGMLDGLVNVGWMDCTKQADLCESFEINT-STTALFPPGSS 318
Cdd:cd03004   42 RKAARALKGKVKVGSVDCQKYESLCQQANIRAyPTIRLYPGNAS 85
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 33-95 6.26e-05

Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 46.18  E-value: 6.26e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134133218  33 DYYKLLGISR---EASTRDIRQAFKKLALTMHPDKNPNDETAHDK--FLKINRAYEVLKDEDLRKKYD 95
Cdd:COG5269   44 DLYALLGLSKyrtKAIPPQILKAHKKKVYKYHPDKTAAGGNKGCDefFKLIQKAREVLGDRKLRLQYD 111
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 560-633 7.98e-05

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: 42.26  E-value: 7.98e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134133218 560 ESFQELVKRRKSSETwMVDFYAPWCGPCQALLPEWRRMARMLSGIVNVGTVDCQKHHSFCQSESVRAYPEIRLF 633
Cdd:cd02956    1 QNFQQVLQESTQVPV-VVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLF 73
PTZ00051 PTZ00051
thioredoxin; Provisional
 468-535 8.11e-05

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 42.17  E-value: 8.11e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134133218 468 LVDFFAPWCPPCRALLPELRKASIQlFGQLKFGTLDCTIHEGLCNTYNIHAYPTTVIF-NKSSIHEYEG 535
Cdd:PTZ00051  22 IVDFYAEWCGPCKRIAPFYEECSKE-YTKMVFVKVDVDELSEVAEKENITSMPTFKVFkNGSVVDTLLG 89
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 688-742 1.01e-04

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: 41.14  E-value: 1.01e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 134133218 688 VLDFYAPWCGPCQQFAPEFEVLARMMKGtVRAGKVDCQAHYQTCQSA---GIKAYPTV 742
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELALLNKG-VKFEAVDVDEDPALEKELkryGVGGVPTL 57
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 658-718 1.40e-04

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: 42.18  E-value: 1.40e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134133218 658 AWALSSLPRASVDLSPEDFKRKVlggkdhWVLDFYAPWCGPCQQFAPEFEVLARmmKGTVR 718
Cdd:cd03010    5 AFSLPALPGPDKTLTSADLKGKP------YLLNVWASWCAPCREEHPVLMALAR--QGRVP 57
trxA PRK09381
thioredoxin TrxA;
554-633 1.65e-04

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 41.59  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 554 VVTLGPESFQELVkrRKSSETWMVDFYAPWCGPCQALLPEWRRMARMLSGIVNVGTVDCQKHHSFCQSESVRAYPEIRLF 633
Cdd:PRK09381   5 IIHLTDDSFDTDV--LKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLF 82
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 438-496 1.69e-04

PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS reductases containing a C-terminal redox active TRX domain and an N-terminal reductase domain which is part of a superfamily that includes N type ATP PPases. APS reductase catalyzes the reduction of activated sulfate to sulfite, a key step in the biosynthesis of sulfur-containing metabolites. Sulfate is first activated by ATP sulfurylase, forming APS, which can be phosphorylated to 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Depending on the organism, either APS or PAPS can be used for sulfate reduction. Prokaryotes and fungi use PAPS, whereas plants use both APS and PAPS. Since plant-type APS reductase uses glutathione (GSH) as its electron donor, the C-terminal domain may function like glutaredoxin, a GSH-dependent member of the TRX superfamily. The flow of reducing equivalents goes from GSH -> C-terminal TRX domain -> N-terminal reductase domain -> APS. Plant-type APS reductase shows no homology to that of dissimilatory sulfate-reducing bacteria, which is an iron-sulfur flavoenzyme. Also included in the alignment is EYE2 from Chlamydomonas reinhardtii, a protein required for eyespot assembly.


Pssm-ID: 239291 [Multi-domain]  Cd Length: 109  Bit Score: 41.67  E-value: 1.69e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134133218 438 NVVAFAKESVnahvttlrpENFPNHEK--EPWLVDFFAPWCPPCRALLPELRKASIQLFGQ 496
Cdd:cd02993    2 AVVTLSRAEI---------EALAKGERrnQSTLVVLYAPWCPFCQAMEASYEELAEKLAGS 53
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 348-443 2.00e-04

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: 41.06  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 348 EILTKSSFEHKLAHHR-WLVSF-----SFGRNdLAsHEYKKL-NALLKNSHIQVGKVDCISDSELCSSLYIHK-PCVAVF 419
Cdd:cd02961    1 VELTDDNFDELVKDSKdVLVEFyapwcGHCKA-LA-PEYEKLaKELKGDGKVVVAKVDCTANNDLCSEYGVRGyPTIKLF 78

                         90       100
                 ....*....|....*....|....
gi 134133218 420 KGvGIHDFEIHHGKDALYNVVAFA 443
Cdd:cd02961   79 PN-GSKEPVKYEGPRTLESLVEFI 101
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 438-546 2.17e-04

5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the assimilation of inorganic sulfate, is closely related to the thioredoxin-dependent PAPS reductase of Bacteria (CysH) and Saccharomyces cerevisiae. However, it has its own C-terminal thioredoxin-like domain and is not thioredoxin-dependent. Also, it has a substrate preference for 5'-adenylylsulfate (APS) over 3'-phosphoadenylylsulfate (PAPS) so the pathway does not require an APS kinase (CysC) to convert APS to PAPS. Arabidopsis thaliana appears to have three isozymes, all able to complement E. coli CysH mutants (even in backgrounds lacking thioredoxin or APS kinase) but likely localized to different compartments in Arabidopsis. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 273072 [Multi-domain]  Cd Length: 463  Bit Score: 44.62  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  438 NVVAFAKESVNahvTTLRPENfpnhEKEPWLVDFFAPWCPPCRALLPELRKASIQLFGQ-LKFGTL--DCTIHEGLCNTY 514
Cdd:TIGR00424 352 NVVSLSRPGIE---NLLKLEE----RKEAWLVVLYAPWCPFCQAMEASYLELAEKLAGSgVKVAKFraDGDQKEFAKQEL 424

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 134133218  515 NIHAYPTTVIFNKSS---IHEYEGHHSADGILEFI 546
Cdd:TIGR00424 425 QLGSFPTILFFPKHSsrpIKYPSEKRDVDSLMSFV 459
PRK10996 PRK10996
thioredoxin 2; Provisional
 577-635 2.26e-04

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 41.98  E-value: 2.26e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 134133218 577 VDFYAPWCGPCQALLPEWRRMARMLSGIVNVGTVDCQKHHSFCQSESVRAYPEIRLFPQ 635
Cdd:PRK10996  57 IDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFKN 115
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
466-551 2.35e-04

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 41.77  E-value: 2.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 466 PWLVDFFAPWCPPCRALLPELRKAsiqlfgQLKFGTLDCTI----------------------------HEGLCNTYNIH 517
Cdd:COG1225   23 PVVLYFYATWCPGCTAELPELRDL------YEEFKDKGVEVlgvssdsdeahkkfaekyglpfpllsdpDGEVAKAYGVR 96

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 134133218 518 AYPTTVIFNKSS--IHEYEGHHSADGIL-EFIEDLVN 551
Cdd:COG1225   97 GTPTTFLIDPDGkiRYVWVGPVDPRPHLeEVLEALLA 133
PDI_a_EFP1_N cd03006
PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase ...
 566-633 4.36e-04

PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase (ThOX), also called Duox. ThOX proteins are responsible for the generation of hydrogen peroxide, a crucial substrate of thyroperoxidase, which functions to iodinate thyroglobulin and synthesize thyroid hormones. EFP1 was isolated through a yeast two-hybrid method using the EF-hand fragment of dog Duox1 as a bait. It could be one of the partners in the assembly of a multiprotein complex constituting the thyroid hydrogen peroxide generating system. EFP1 contains two TRX domains related to the redox active TRX domains of protein disulfide isomerase (PDI). This subfamily is composed of the N-terminal TRX domain of EFP1, which contains a CXXS sequence in place of the typical CXXC motif, similar to ERp44. The CXXS motif allows the formation of stable mixed disulfides, crucial for the ER-retention function of ERp44.


Pssm-ID: 239304  Cd Length: 113  Bit Score: 40.53  E-value: 4.36e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134133218 566 VKRRKSSETWMVDFYAPWCGPCQALLPEWRRMARMLSGIVNVGTVDCQKHHSFCQSESVRAY-PEIRLF 633
Cdd:cd03006   23 EELRTDAEVSLVMYYAPWDAQSQAARQEFEQVAQKLSDQVLFVAINCWWPQGKCRKQKHFFYfPVIHLY 91
PTZ00051 PTZ00051
thioredoxin; Provisional
 129-209 4.64e-04

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 40.24  E-value: 4.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 129 EITTldRGDFDAAVNSGEVWFVNFYFPRCSHCHDLAPTWREFAKEMDGVIRIgAVNCGDNGMLCRSKGINSYPSLYVFRA 208
Cdd:PTZ00051   4 IVTS--QAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFV-KVDVDELSEVAEKENITSMPTFKVFKN 80


                 .
gi 134133218 209 G 209
Cdd:PTZ00051  81 G 81
PLN02309 PLN02309
5'-adenylylsulfate reductase
 438-529 8.43e-04

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 42.47  E-value: 8.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 438 NVVAFAKESVNAHVTTlrpenfPNHeKEPWLVDFFAPWCPPCRALLPELRKASIQLFGQ-LKFGTLDC-TIHEGLCN-TY 514
Cdd:PLN02309 346 NVVALSRAGIENLLKL------ENR-KEPWLVVLYAPWCPFCQAMEASYEELAEKLAGSgVKVAKFRAdGDQKEFAKqEL 418

                         90
                 ....*....|....*
gi 134133218 515 NIHAYPTTVIFNKSS 529
Cdd:PLN02309 419 QLGSFPTILLFPKNS 433
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 153-239 8.85e-04

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 42.43  E-value: 8.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 153 YFPRCSHCHDLAPTWREFAKEMDGVIRIgaVNCGDNGMLCRS--KGIN--SYPSLYVFRAGMN-PEKYFNDRTKSSLTKF 227
Cdd:PTZ00102 383 YAPWCGHCKNLEPVYNELGEKYKDNDSI--IVAKMNGTANETplEEFSwsAFPTILFVKAGERtPIPYEGERTVEGFKEF 460

                         90
                 ....*....|....*..
gi 134133218 228 -----AMQFVKSKVTEL 239
Cdd:PTZ00102 461 vnkhaTNPFEDDTHEEL 477
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 468-530 9.35e-04

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: 39.18  E-value: 9.35e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134133218 468 LVDFFAPWCPPCRALLPELRKASIQLFGQLKFGTLDCTIHEGLCNTYNIHAYPTTVIFNKSSI 530
Cdd:cd02984   18 VLHFWAPWAEPCKQMNQVFEELAKEAFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTI 80
djlA PRK09430
co-chaperone DjlA;
32-86 1.09e-03

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 41.72  E-value: 1.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 134133218  32 EDYYKLLGISREASTRDIRQAFKKLaltM---HPDK-----NPND--ETAHDKFLKINRAYEVLK 86
Cdd:PRK09430 200 EDAYKVLGVSESDDDQEIKRAYRKL---MsehHPDKlvakgLPPEmmEMAKEKAQEIQAAYELIK 261
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
669-707 1.34e-03

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 39.46  E-value: 1.34e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 134133218 669 VDLSpeDFKRKVLggkdhwVLDFYAPWCGPCQQFAPEFE 707
Cdd:COG1225   14 VSLS--DLRGKPV------VLYFYATWCPGCTAELPELR 44
PLN02309 PLN02309
5'-adenylylsulfate reductase
 684-754 1.39e-03

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 42.08  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 684 KDHWVLDFYAPWCGPCQQFAPEFEVLARMMKGT-VRAGK--VD------CQAHYQtcqsagIKAYPTVRFYPT------- 747
Cdd:PLN02309 365 KEPWLVVLYAPWCPFCQAMEASYEELAEKLAGSgVKVAKfrADgdqkefAKQELQ------LGSFPTILLFPKnssrpik 438


                 ....*..
gi 134133218 748 LGTTRRD 754
Cdd:PLN02309 439 YPSEKRD 445
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
463-546 1.55e-03

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 38.56  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  463 EKEPWLVDFFAPWCPPCRALLPELRK--------------ASIQLFG--QLKFGTLDCTIHEGLCNTYNIHAYPTTVIFN 526
Cdd:pfam13098   3 NGKPVLVVFTDPDCPYCKKLKKELLEdpdvtvylgpnfvfIAVNIWCakEVAKAFTDILENKELGRKYGVRGTPTIVFFD 82

                          90       100
                  ....*....|....*....|.
gi 134133218  527 -KSSIHEYEGHHSADGILEFI 546
Cdd:pfam13098  83 gKGELLRLPGYVPAEEFLALL 103
PDI_a_EFP1_N cd03006
PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase ...
 683-749 1.72e-03

PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase (ThOX), also called Duox. ThOX proteins are responsible for the generation of hydrogen peroxide, a crucial substrate of thyroperoxidase, which functions to iodinate thyroglobulin and synthesize thyroid hormones. EFP1 was isolated through a yeast two-hybrid method using the EF-hand fragment of dog Duox1 as a bait. It could be one of the partners in the assembly of a multiprotein complex constituting the thyroid hydrogen peroxide generating system. EFP1 contains two TRX domains related to the redox active TRX domains of protein disulfide isomerase (PDI). This subfamily is composed of the N-terminal TRX domain of EFP1, which contains a CXXS sequence in place of the typical CXXC motif, similar to ERp44. The CXXS motif allows the formation of stable mixed disulfides, crucial for the ER-retention function of ERp44.


Pssm-ID: 239304  Cd Length: 113  Bit Score: 38.99  E-value: 1.72e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134133218 683 GKDHWVLDFYAPWCGPCQQFAPEFEVLARMMKGTVRAGKVDCQAHYQTC--QSAGIKAYPTVRFYPTLG 749
Cdd:cd03006   28 DAEVSLVMYYAPWDAQSQAARQEFEQVAQKLSDQVLFVAINCWWPQGKCrkQKHFFYFPVIHLYYRSRG 96
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 678-745 1.86e-03

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: 38.25  E-value: 1.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134133218 678 RKVLGGKDHWVLDFY-APWCGPCQQFAPEFEVLARMMKGTVRAGKVDCQAHYQTCQSAGIKAYPTVRFY 745
Cdd:cd02949    6 RKLYHESDRLILVLYtSPTCGPCRTLKPILNKVIDEFDGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFF 74
TMX2 cd02962
TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related ...
 450-503 1.91e-03

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: 39.67  E-value: 1.91e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 134133218 450 HVTTLRPENFPNH-EKEP---WLVDFFAPWCPPCRALLPELRKASIQLFG-QLKFGTLD 503
Cdd:cd02962   29 HIKYFTPKTLEEElERDKrvtWLVEFFTTWSPECVNFAPVFAELSLKYNNnNLKFGKID 87
PLN02309 PLN02309
5'-adenylylsulfate reductase
 128-232 2.23e-03

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 41.31  E-value: 2.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 128 PEITTLDRGDFDAAV---NSGEVWFVNFYFPRCSHCHDLAPTWREFAKEMDGV-IRIGAVNC-GDNGMLCRSK-GINSYP 201
Cdd:PLN02309 345 QNVVALSRAGIENLLkleNRKEPWLVVLYAPWCPFCQAMEASYEELAEKLAGSgVKVAKFRAdGDQKEFAKQElQLGSFP 424

                         90       100       110
                 ....*....|....*....|....*....|...
gi 134133218 202 SLYVF-RAGMNPEKYFND-RTKSSLTKFAMQFV 232
Cdd:PLN02309 425 TILLFpKNSSRPIKYPSEkRDVDSLLSFVNSLR 457
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 468-528 2.52e-03

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


Pssm-ID: 464033 [Multi-domain]  Cd Length: 95  Bit Score: 38.06  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218  468 LVDFFAPWCPPCRALLPELRKASIQL-----------------------FGQLKFGTLDCTIHEGLCNT----YNIHAYP 520
Cdd:pfam13905   5 LLYFGASWCKPCRRFTPLLKELYEKLkkkknveivfvsldrdleefkdyLKKMPKDWLSVPFDDDERNElkrkYGVNAIP 84


                  ....*...
gi 134133218  521 TTVIFNKS 528
Cdd:pfam13905  85 TLVLLDPN 92
PRK10996 PRK10996
thioredoxin 2; Provisional
 138-209 2.66e-03

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 38.90  E-value: 2.66e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134133218 138 FDAAVNSGEVWFVNFYFPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDNGMLCRSKGINSYPSLYVFRAG 209
Cdd:PRK10996  45 LDKLLQDDLPVVIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFKNG 116
PDI_a_EFP1_N cd03006
PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase ...
 123-215 3.36e-03

PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase (ThOX), also called Duox. ThOX proteins are responsible for the generation of hydrogen peroxide, a crucial substrate of thyroperoxidase, which functions to iodinate thyroglobulin and synthesize thyroid hormones. EFP1 was isolated through a yeast two-hybrid method using the EF-hand fragment of dog Duox1 as a bait. It could be one of the partners in the assembly of a multiprotein complex constituting the thyroid hydrogen peroxide generating system. EFP1 contains two TRX domains related to the redox active TRX domains of protein disulfide isomerase (PDI). This subfamily is composed of the N-terminal TRX domain of EFP1, which contains a CXXS sequence in place of the typical CXXC motif, similar to ERp44. The CXXS motif allows the formation of stable mixed disulfides, crucial for the ER-retention function of ERp44.


Pssm-ID: 239304  Cd Length: 113  Bit Score: 37.83  E-value: 3.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 123 IYDDDPEITTLDRGDFDAAV---NSGEVWFVNFYFPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDNGMLCRSKGINS 199
Cdd:cd03006    4 FFSQRSPVLDFYKGQLDYAEelrTDAEVSLVMYYAPWDAQSQAARQEFEQVAQKLSDQVLFVAINCWWPQGKCRKQKHFF 83

                         90
                 ....*....|....*..
gi 134133218 200 Y-PSLYVFRAGMNPEKY 215
Cdd:cd03006   84 YfPVIHLYYRSRGPIEY 100
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 150-209 4.44e-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: 37.25  E-value: 4.44e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 150 VNFYFPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDNGMLCRSKGINSYPSLYVFRAG 209
Cdd:cd02956   17 VDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAG 76
trxA PRK09381
thioredoxin TrxA;
129-227 4.91e-03

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 37.35  E-value: 4.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 129 EITTLDRGDFDAAVNSGE-VWFVNFYFPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDNGMLCRSKGINSYPSLYVFR 207
Cdd:PRK09381   4 KIIHLTDDSFDTDVLKADgAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFK 83

                         90       100
                 ....*....|....*....|
gi 134133218 208 AGMNPEKYFNDRTKSSLTKF 227
Cdd:PRK09381  84 NGEVAATKVGALSKGQLKEF 103
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 576-599 7.85e-03

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: 36.83  E-value: 7.85e-03
                         10        20
                 ....*....|....*....|....
gi 134133218 576 MVDFYAPWCGPCQALLPEWRRMAR 599
Cdd:cd02966   23 LVNFWASWCPPCRAEMPELEALAK 46
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 691-742 8.09e-03

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: 36.57  E-value: 8.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 134133218 691 FYAPWCGPCQQFAPEFEVLARMMKgTVRAGKVD-CQAHYQTCQSAGIKAYPTV 742
Cdd:cd02999   25 FYASWCPFSASFRPHFNALSSMFP-QIRHLAIEeSSIKPSLLSRYGVVGFPTI 76
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 569-658 8.33e-03

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: 36.57  E-value: 8.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134133218 569 RKSSETWMVDFYAPWCGPCQALLPEWRRMARMLSGIVNVGTVDCQKHHSFCQSESVRAYPEIRLFPQNSNRRdqyqtYNG 648
Cdd:cd02999   15 FNREDYTAVLFYASWCPFSASFRPHFNALSSMFPQIRHLAIEESSIKPSLLSRYGVVGFPTILLFNSTPRVR-----YNG 89

                         90
                 ....*....|
gi 134133218 649 wHRDAFSLKA 658
Cdd:cd02999   90 -TRTLDSLAA 98
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 471-489 8.34e-03

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: 37.26  E-value: 8.34e-03
                         10
                 ....*....|....*....
gi 134133218 471 FFAPWCPPCRALLPELRKA 489
Cdd:cd03009   25 FSASWCPPCRAFTPKLVEF 43
TRX_NDPK cd02948
TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are ...
 563-597 9.09e-03

TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are fusion proteins which contain one redox active TRX domain containing a CXXC motif and three NDPK domains, and are characterized as intermediate chains (ICs) of axonemal outer arm dynein. Dyneins are molecular motors that generate force against microtubules to produce cellular movement, and are divided into two classes: axonemal and cytoplasmic. They are supramolecular complexes consisting of three protein groups classified according to size: dynein heavy, intermediate and light chains. Axonemal dyneins form two structures, the inner and outer arms, which are attached to doublet microtubules throughout the cilia and flagella. The human homolog is the sperm-specific Sptrx-2, presumed to be a component of the human sperm axoneme architecture. Included in this group is another human protein, TRX-like protein 2, a smaller fusion protein containing one TRX and one NDPK domain, which is also associated with microtubular structures. The other members of this group are hypothetical insect proteins containing a TRX domain and outer arm dynein light chains (14 and 16kDa) of Chlamydomonas reinhardtii. Using standard assays, the fusion proteins have shown no TRX enzymatic activity.


Pssm-ID: 239246 [Multi-domain]  Cd Length: 102  Bit Score: 36.54  E-value: 9.09e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 134133218 563 QELVKRRKSSET-WMVDFYAPWCGPCQALLPEWRRM 597
Cdd:cd02948    7 QEEWEELLSNKGlTVVDVYQEWCGPCKAVVSLFKKI 42
 
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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