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Conserved domains on  [gi|42571269|ref|NP_973708|]
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thioredoxin family protein [Arabidopsis thaliana]

Protein Classification

thioredoxin family protein( domain architecture ID 10122299)

thioredoxin family protein similar to conjugal transfer protein TraF

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 142-245 3.16e-59

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: 183.22  E-value: 3.16e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 142 NVVVLTPDNFDEIVLDQNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKQEEGVVIANLDAD-AHKALGEKYGVSGFPTLK 220
Cdd:cd02998   1 NVVELTDSNFDKVVGDDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFANEDDVVIAKVDADeANKDLAKKYGVSGFPTLK 80

                        90       100
                ....*....|....*....|....*
gi 42571269 221 FFPKDNKAGHDYDGGRDLDDFVSFI 245
Cdd:cd02998  81 FFPKGSTEPVKYEGGRDLEDLVKFV 105
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 28-126 6.69e-55

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: 172.43  E-value: 6.69e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  28 LTDDSFEKEVGKDK-GALVEFYAPWCGHCKKLAPEYEKLGASFKKAKSVLIAKVDCDE-QKSVCTKYGVSGYPTIQWFPK 105
Cdd:cd02998   5 LTDSNFDKVVGDDKkDVLVEFYAPWCGHCKNLAPEYEKLAAVFANEDDVVIAKVDADEaNKDLAKKYGVSGFPTLKFFPK 84

                        90       100
                ....*....|....*....|.
gi 42571269 106 GSLEPQKYEGPRNAEALAEYV 126
Cdd:cd02998  85 GSTEPVKYEGGRDLEDLVKFV 105
 
Name Accession Description Interval E-value
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 142-245 3.16e-59

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: 183.22  E-value: 3.16e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 142 NVVVLTPDNFDEIVLDQNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKQEEGVVIANLDAD-AHKALGEKYGVSGFPTLK 220
Cdd:cd02998   1 NVVELTDSNFDKVVGDDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFANEDDVVIAKVDADeANKDLAKKYGVSGFPTLK 80

                        90       100
                ....*....|....*....|....*
gi 42571269 221 FFPKDNKAGHDYDGGRDLDDFVSFI 245
Cdd:cd02998  81 FFPKGSTEPVKYEGGRDLEDLVKFV 105
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 28-126 6.69e-55

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: 172.43  E-value: 6.69e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  28 LTDDSFEKEVGKDK-GALVEFYAPWCGHCKKLAPEYEKLGASFKKAKSVLIAKVDCDE-QKSVCTKYGVSGYPTIQWFPK 105
Cdd:cd02998   5 LTDSNFDKVVGDDKkDVLVEFYAPWCGHCKNLAPEYEKLAAVFANEDDVVIAKVDADEaNKDLAKKYGVSGFPTLKFFPK 84

                        90       100
                ....*....|....*....|.
gi 42571269 106 GSLEPQKYEGPRNAEALAEYV 126
Cdd:cd02998  85 GSTEPVKYEGGRDLEDLVKFV 105
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 146-249 2.50e-53

protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein disulfide isomerases, generally found in two copies. The high cutoff for total score reflects the expectation of finding both copies. The domain is similar to thioredoxin but the redox-active disulfide region motif is APWCGHCK. [Protein fate, Protein folding and stabilization]


Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 168.24  E-value: 2.50e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269   146 LTPDNFDEIVLDqNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKQEEGVVIANLDADAHKALGEKYGVSGFPTLKFFPKD 225
Cdd:TIGR01126   1 LTASNFDEIVLS-NKDVLVEFYAPWCGHCKNLAPEYEKLAKELKKDPKIVLAKVDATAEKDLASRFGVSGFPTIKFFPKG 79

                          90       100
                  ....*....|....*....|....
gi 42571269   226 NKAgHDYDGGRDLDDFVSFINEKS 249
Cdd:TIGR01126  80 SKP-VDYEGGRDLEAIVEFVNEKS 102
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 28-129 2.83e-50

protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein disulfide isomerases, generally found in two copies. The high cutoff for total score reflects the expectation of finding both copies. The domain is similar to thioredoxin but the redox-active disulfide region motif is APWCGHCK. [Protein fate, Protein folding and stabilization]


Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 160.53  E-value: 2.83e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269    28 LTDDSFEKEVGKDKGALVEFYAPWCGHCKKLAPEYEKLGASFKKAKSVLIAKVDCDEQKSVCTKYGVSGYPTIQWFPKGS 107
Cdd:TIGR01126   1 LTASNFDEIVLSNKDVLVEFYAPWCGHCKNLAPEYEKLAKELKKDPKIVLAKVDATAEKDLASRFGVSGFPTIKFFPKGS 80

                          90       100
                  ....*....|....*....|..
gi 42571269   108 lEPQKYEGPRNAEALAEYVNKE 129
Cdd:TIGR01126  81 -KPVDYEGGRDLEAIVEFVNEK 101
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 142-247 1.25e-38

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: 130.82  E-value: 1.25e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269   142 NVVVLTPDNFDEIVLDQNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKqeEGVVIANLDADAHKALGEKYGVSGFPTLKF 221
Cdd:pfam00085   1 VVVVLTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYK--GNVVFAKVDVDENPDLASKYGVRGYPTLIF 78

                          90       100
                  ....*....|....*....|....*.
gi 42571269   222 FPKDNKAGhDYDGGRDLDDFVSFINE 247
Cdd:pfam00085  79 FKNGQPVD-DYVGARPKDALAAFLKA 103
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 28-250 1.27e-32

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 124.09  E-value: 1.27e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269   28 LTDDSFEKEVGKDKGALVEFYAPWCGHCKKLAPEYEKLGASFKKAKS-VLIAKVDCDEQKSVCTKYGVSGYPTIQWF--- 103
Cdd:PTZ00102  37 LTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSeIVLASVDATEEMELAQEFGVRGYPTIKFFnkg 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  104 ---------------------------------------------------PKGSLEPQKYE------------------ 114
Cdd:PTZ00102 117 npvnysggrtadgivswikkltgpavtevesaseikliakkifvafygeytSKDSELYKKFEevadkhrehakffvkkhe 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  115 --------------------------------------GPRNAEALAEYVNKEG------GTN----------------- 133
Cdd:PTZ00102 197 gknkiyvlhkdeegvelfmgktkeeleefvstesfplfAEINAENYRRYISSGKdlvwfcGTTedydkyksvvrkvarkl 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  134 ---------------------------------------------------------------------VKLAAVPQN-- 142
Cdd:PTZ00102 277 rekyafvwldteqfgshakehllieefpglayqspagryllppakesfdsvealieffkdveagkveksIKSEPIPEEqd 356

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  143 --VVVLTPDNFDEIVLDQNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKQEEGVVIANLDADAHKALGEKYGVSGFPTLK 220
Cdd:PTZ00102 357 gpVKVVVGNTFEEIVFKSDKDVLLEIYAPWCGHCKNLEPVYNELGEKYKDNDSIIVAKMNGTANETPLEEFSWSAFPTIL 436

                        410       420       430
                 ....*....|....*....|....*....|
gi 42571269  221 FFPKDNKAGHDYDGGRDLDDFVSFINEKSG 250
Cdd:PTZ00102 437 FVKAGERTPIPYEGERTVEGFKEFVNKHAT 466
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 28-128 1.61e-32

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: 115.02  E-value: 1.61e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269    28 LTDDSFEKEVGKDKG-ALVEFYAPWCGHCKKLAPEYEKLGAsfKKAKSVLIAKVDCDEQKSVCTKYGVSGYPTIQWFPKG 106
Cdd:pfam00085   5 LTDANFDEVVQKSSKpVLVDFYAPWCGPCKMLAPEYEELAQ--EYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKNG 82

                          90       100
                  ....*....|....*....|..
gi 42571269   107 SlEPQKYEGPRNAEALAEYVNK 128
Cdd:pfam00085  83 Q-PVDDYVGARPKDALAAFLKA 103
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 142-247 1.22e-28

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: 104.90  E-value: 1.22e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 142 NVVVLTPDNFDEIVLDQNKDVLVEFYAPWCGHCKSLAPTYEKVATvfKQEEGVVIANLDADAHKALGEKYGVSGFPTLKF 221
Cdd:COG3118   1 AVVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAA--EYGGKVKFVKVDVDENPELAAQFGVRSIPTLLL 78

                        90       100
                ....*....|....*....|....*.
gi 42571269 222 FpKDNKAGHDYDGGRDLDDFVSFINE 247
Cdd:COG3118  79 F-KDGQPVDRFVGALPKEQLREFLDK 103
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 28-128 2.24e-23

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: 91.03  E-value: 2.24e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  28 LTDDSFEKEVGKDKG-ALVEFYAPWCGHCKKLAPEYEKLGASFkkAKSVLIAKVDCDEQKSVCTKYGVSGYPTIQWFPKG 106
Cdd:COG3118   5 LTDENFEEEVLESDKpVLVDFWAPWCGPCKMLAPVLEELAAEY--GGKVKFVKVDVDENPELAAQFGVRSIPTLLLFKDG 82

                        90       100
                ....*....|....*....|..
gi 42571269 107 SLEPQKyEGPRNAEALAEYVNK 128
Cdd:COG3118  83 QPVDRF-VGALPKEQLREFLDK 103
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 28-151 2.97e-17

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 78.13  E-value: 2.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269   28 LTDDSFEKEVGKDKGA-----LVEFYAPWCGHCKKLAPEYEKLGASFKKAksVLIAKVDCDEQKSVCTKYGVSGYPTIQW 102
Cdd:PTZ00443  35 LNDKNFEKLTQASTGAttgpwFVKFYAPWCSHCRKMAPAWERLAKALKGQ--VNVADLDATRALNLAKRFAIKGYPTLLL 112

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 42571269  103 FPKGSLepQKYE-GPRNAEALAEYVNKEGGTNVKlAAVPQ--NVVVLTPDNF 151
Cdd:PTZ00443 113 FDKGKM--YQYEgGDRSTEKLAAFALGDFKKALG-APVPAplSFFALTIDFF 161
 
Name Accession Description Interval E-value
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 142-245 3.16e-59

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: 183.22  E-value: 3.16e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 142 NVVVLTPDNFDEIVLDQNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKQEEGVVIANLDAD-AHKALGEKYGVSGFPTLK 220
Cdd:cd02998   1 NVVELTDSNFDKVVGDDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFANEDDVVIAKVDADeANKDLAKKYGVSGFPTLK 80

                        90       100
                ....*....|....*....|....*
gi 42571269 221 FFPKDNKAGHDYDGGRDLDDFVSFI 245
Cdd:cd02998  81 FFPKGSTEPVKYEGGRDLEDLVKFV 105
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 28-126 6.69e-55

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: 172.43  E-value: 6.69e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  28 LTDDSFEKEVGKDK-GALVEFYAPWCGHCKKLAPEYEKLGASFKKAKSVLIAKVDCDE-QKSVCTKYGVSGYPTIQWFPK 105
Cdd:cd02998   5 LTDSNFDKVVGDDKkDVLVEFYAPWCGHCKNLAPEYEKLAAVFANEDDVVIAKVDADEaNKDLAKKYGVSGFPTLKFFPK 84

                        90       100
                ....*....|....*....|.
gi 42571269 106 GSLEPQKYEGPRNAEALAEYV 126
Cdd:cd02998  85 GSTEPVKYEGGRDLEDLVKFV 105
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 146-249 2.50e-53

protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein disulfide isomerases, generally found in two copies. The high cutoff for total score reflects the expectation of finding both copies. The domain is similar to thioredoxin but the redox-active disulfide region motif is APWCGHCK. [Protein fate, Protein folding and stabilization]


Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 168.24  E-value: 2.50e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269   146 LTPDNFDEIVLDqNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKQEEGVVIANLDADAHKALGEKYGVSGFPTLKFFPKD 225
Cdd:TIGR01126   1 LTASNFDEIVLS-NKDVLVEFYAPWCGHCKNLAPEYEKLAKELKKDPKIVLAKVDATAEKDLASRFGVSGFPTIKFFPKG 79

                          90       100
                  ....*....|....*....|....
gi 42571269   226 NKAgHDYDGGRDLDDFVSFINEKS 249
Cdd:TIGR01126  80 SKP-VDYEGGRDLEAIVEFVNEKS 102
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 28-129 2.83e-50

protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein disulfide isomerases, generally found in two copies. The high cutoff for total score reflects the expectation of finding both copies. The domain is similar to thioredoxin but the redox-active disulfide region motif is APWCGHCK. [Protein fate, Protein folding and stabilization]


Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 160.53  E-value: 2.83e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269    28 LTDDSFEKEVGKDKGALVEFYAPWCGHCKKLAPEYEKLGASFKKAKSVLIAKVDCDEQKSVCTKYGVSGYPTIQWFPKGS 107
Cdd:TIGR01126   1 LTASNFDEIVLSNKDVLVEFYAPWCGHCKNLAPEYEKLAKELKKDPKIVLAKVDATAEKDLASRFGVSGFPTIKFFPKGS 80

                          90       100
                  ....*....|....*....|..
gi 42571269   108 lEPQKYEGPRNAEALAEYVNKE 129
Cdd:TIGR01126  81 -KPVDYEGGRDLEAIVEFVNEK 101
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 28-126 3.22e-47

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: 152.38  E-value: 3.22e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  28 LTDDSFEKEVGKDKGALVEFYAPWCGHCKKLAPEYEKLGASFKKAKSVLIAKVDCDEQKSVCTKYGVSGYPTIQWFPKGS 107
Cdd:cd02961   3 LTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPNGS 82

                        90
                ....*....|....*....
gi 42571269 108 LEPQKYEGPRNAEALAEYV 126
Cdd:cd02961  83 KEPVKYEGPRTLESLVEFI 101
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 144-245 8.27e-47

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: 151.61  E-value: 8.27e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 144 VVLTPDNFDEIVLDqNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKQEEGVVIANLDADAHKALGEKYGVSGFPTLKFFP 223
Cdd:cd02961   1 VELTDDNFDELVKD-SKDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFP 79

                        90       100
                ....*....|....*....|..
gi 42571269 224 KDNKAGHDYDGGRDLDDFVSFI 245
Cdd:cd02961  80 NGSKEPVKYEGPRTLESLVEFI 101
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 28-249 5.27e-43

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: 152.14  E-value: 5.27e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269    28 LTDDSFEKEVGKDKGALVEFYAPWCGHCKKLAPEYEKLGASFKKAKS-VLIAKVDCDEQKSVCTKYGVSGYPTIQWFPKG 106
Cdd:TIGR01130   6 LTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPpIKLAKVDATEEKDLAQKYGVSGYPTLKIFRNG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269   107 SLEPQKYEGPRNAEALAEYVNKEGGTNVKlaavpqnvVVLTPDNFDEiVLDQNKDVLVEFYApwcGHCKSLAPTYEKVAT 186
Cdd:TIGR01130  86 EDSVSDYNGPRDADGIVKYMKKQSGPAVK--------EIETVADLEA-FLADDDVVVIGFFK---DLDSELNDTFLSVAE 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571269   187 VFKQEEGVVIANLDADAHKALGEKYGVSGFptLKFFPKDNKAGH-DYDGGRDLDDFVSFINEKS 249
Cdd:TIGR01130 154 KLRDVYFFFAHSSDVAAFAKLGAFPDSVVL--FKPKDEDEKFSKvDGEMDTDVSDLEKFIRAES 215
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 143-245 1.33e-41

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: 138.46  E-value: 1.33e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 143 VVVLTPDNFDEIVLDQNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKQEEGVVIANLDADAHKALGEkYGVSGFPTLKFF 222
Cdd:cd02995   2 VKVVVGKNFDEVVLDSDKDVLVEFYAPWCGHCKALAPIYEELAEKLKGDDNVVIAKMDATANDVPSE-FVVDGFPTILFF 80

                        90       100
                ....*....|....*....|....
gi 42571269 223 PKDNKA-GHDYDGGRDLDDFVSFI 245
Cdd:cd02995  81 PAGDKSnPIKYEGDRTLEDLIKFI 104
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 142-244 3.33e-41

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: 137.42  E-value: 3.33e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 142 NVVVLTPDNFDEIVLDQNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKqeeGVV-IANLDADAHKALGEKYGVSGFPTLK 220
Cdd:cd03001   1 DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALK---GIVkVGAVDADVHQSLAQQYGVRGFPTIK 77

                        90       100
                ....*....|....*....|....
gi 42571269 221 FFPKDNKAGHDYDGGRDLDDFVSF 244
Cdd:cd03001  78 VFGAGKNSPQDYQGGRTAKAIVSA 101
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 71-252 1.14e-39

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: 142.89  E-value: 1.14e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269    71 KAKSVLIAKVDCDEQKSVCTKYGV--SGYPTIQWFPKGslEPQKY---EGPRNAEALAEYVNK--EGGTN--VKLAAVPQ 141
Cdd:TIGR01130 265 RGKFVNFAVADEEDFGRELEYFGLkaEKFPAVAIQDLE--GNKKYpmdQEEFSSENLEAFVKDflDGKLKpyLKSEPIPE 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269   142 N----VVVLTPDNFDEIVLDQNKDVLVEFYAPWCGHCKSLAPTYEKVATVFK-QEEGVVIANLDADAHKAlgEKYGVSGF 216
Cdd:TIGR01130 343 DdegpVKVLVGKNFDEIVLDETKDVLVEFYAPWCGHCKNLAPIYEELAEKYKdAESDVVIAKMDATANDV--PPFEVEGF 420

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 42571269   217 PTLKFFPKDNKAGH-DYDGGRDLDDFVSFINEKSGTS 252
Cdd:TIGR01130 421 PTIKFVPAGKKSEPvPYDGDRTLEDFSKFIAKHATFP 457
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 142-247 1.25e-38

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: 130.82  E-value: 1.25e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269   142 NVVVLTPDNFDEIVLDQNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKqeEGVVIANLDADAHKALGEKYGVSGFPTLKF 221
Cdd:pfam00085   1 VVVVLTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYK--GNVVFAKVDVDENPDLASKYGVRGYPTLIF 78

                          90       100
                  ....*....|....*....|....*.
gi 42571269   222 FPKDNKAGhDYDGGRDLDDFVSFINE 247
Cdd:pfam00085  79 FKNGQPVD-DYVGARPKDALAAFLKA 103
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 142-250 5.56e-38

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: 138.65  E-value: 5.56e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269   142 NVVVLTPDNFDEiVLDQNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKQE-EGVVIANLDADAHKALGEKYGVSGFPTLK 220
Cdd:TIGR01130   2 DVLVLTKDNFDD-FIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKgPPIKLAKVDATEEKDLAQKYGVSGYPTLK 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 42571269   221 FFPKDNKAGHDYDGGRDLDDFVSFINEKSG 250
Cdd:TIGR01130  81 IFRNGEDSVSDYNGPRDADGIVKYMKKQSG 110
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 28-124 1.55e-33

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: 117.39  E-value: 1.55e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  28 LTDDSFEKEVGKDKGA-LVEFYAPWCGHCKKLAPEYEKLGASFK-KAKsvlIAKVDCDEQKSVCTKYGVSGYPTIQWFPK 105
Cdd:cd03001   5 LTDSNFDKKVLNSDDVwLVEFYAPWCGHCKNLAPEWKKAAKALKgIVK---VGAVDADVHQSLAQQYGVRGFPTIKVFGA 81

                        90
                ....*....|....*....
gi 42571269 106 GSLEPQKYEGPRNAEALAE 124
Cdd:cd03001  82 GKNSPQDYQGGRTAKAIVS 100
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 28-250 1.27e-32

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 124.09  E-value: 1.27e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269   28 LTDDSFEKEVGKDKGALVEFYAPWCGHCKKLAPEYEKLGASFKKAKS-VLIAKVDCDEQKSVCTKYGVSGYPTIQWF--- 103
Cdd:PTZ00102  37 LTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSeIVLASVDATEEMELAQEFGVRGYPTIKFFnkg 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  104 ---------------------------------------------------PKGSLEPQKYE------------------ 114
Cdd:PTZ00102 117 npvnysggrtadgivswikkltgpavtevesaseikliakkifvafygeytSKDSELYKKFEevadkhrehakffvkkhe 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  115 --------------------------------------GPRNAEALAEYVNKEG------GTN----------------- 133
Cdd:PTZ00102 197 gknkiyvlhkdeegvelfmgktkeeleefvstesfplfAEINAENYRRYISSGKdlvwfcGTTedydkyksvvrkvarkl 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  134 ---------------------------------------------------------------------VKLAAVPQN-- 142
Cdd:PTZ00102 277 rekyafvwldteqfgshakehllieefpglayqspagryllppakesfdsvealieffkdveagkveksIKSEPIPEEqd 356

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  143 --VVVLTPDNFDEIVLDQNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKQEEGVVIANLDADAHKALGEKYGVSGFPTLK 220
Cdd:PTZ00102 357 gpVKVVVGNTFEEIVFKSDKDVLLEIYAPWCGHCKNLEPVYNELGEKYKDNDSIIVAKMNGTANETPLEEFSWSAFPTIL 436

                        410       420       430
                 ....*....|....*....|....*....|
gi 42571269  221 FFPKDNKAGHDYDGGRDLDDFVSFINEKSG 250
Cdd:PTZ00102 437 FVKAGERTPIPYEGERTVEGFKEFVNKHAT 466
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 28-128 1.61e-32

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: 115.02  E-value: 1.61e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269    28 LTDDSFEKEVGKDKG-ALVEFYAPWCGHCKKLAPEYEKLGAsfKKAKSVLIAKVDCDEQKSVCTKYGVSGYPTIQWFPKG 106
Cdd:pfam00085   5 LTDANFDEVVQKSSKpVLVDFYAPWCGPCKMLAPEYEELAQ--EYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKNG 82

                          90       100
                  ....*....|....*....|..
gi 42571269   107 SlEPQKYEGPRNAEALAEYVNK 128
Cdd:pfam00085  83 Q-PVDDYVGARPKDALAAFLKA 103
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 28-126 3.59e-32

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: 113.92  E-value: 3.59e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  28 LTDDSFEKEVGKdKGALVEFYAPWCGHCKKLAPEYEKLGASFKKA-KSVLIAKVDCDEQKSVCTKYGVSGYPTIQWFpKG 106
Cdd:cd03005   5 LTEDNFDHHIAE-GNHFVKFFAPWCGHCKRLAPTWEQLAKKFNNEnPSVKIAKVDCTQHRELCSEFQVRGYPTLLLF-KD 82

                        90       100
                ....*....|....*....|
gi 42571269 107 SLEPQKYEGPRNAEALAEYV 126
Cdd:cd03005  83 GEKVDKYKGTRDLDSLKEFV 102
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 142-245 4.80e-32

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: 114.00  E-value: 4.80e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 142 NVVVLTPDNFDEIVLDQNKDVLVEFYAPWCGHCKSLAPTYEKVAtvfKQEEGVVI---ANLDADAHKALGEKYGVSGFPT 218
Cdd:cd03002   1 PVYELTPKNFDKVVHNTNYTTLVEFYAPWCGHCKNLKPEYAKAA---KELDGLVQvaaVDCDEDKNKPLCGKYGVQGFPT 77

                        90       100       110
                ....*....|....*....|....*....|.
gi 42571269 219 LKFFPKDNKAG----HDYDGGRDLDDFVSFI 245
Cdd:cd03002  78 LKVFRPPKKASkhavEDYNGERSAKAIVDFV 108
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 28-126 2.42e-30

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: 109.18  E-value: 2.42e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  28 LTDDSFEKEVG-KDKGALVEFYAPWCGHCKKLAPEYEKLGASFKKAKSVLIAKVDCDEQkSVCTKYGVSGYPTIQWFPKG 106
Cdd:cd02995   5 VVGKNFDEVVLdSDKDVLVEFYAPWCGHCKALAPIYEELAEKLKGDDNVVIAKMDATAN-DVPSEFVVDGFPTILFFPAG 83

                        90       100
                ....*....|....*....|.
gi 42571269 107 SL-EPQKYEGPRNAEALAEYV 126
Cdd:cd02995  84 DKsNPIKYEGDRTLEDLIKFI 104
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 28-125 2.68e-30

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: 109.33  E-value: 2.68e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  28 LTDDSFEKEVGKDKGALVEFYAPWCGHCKKLAPEYEKLGASFKKAKSVLIAKVDC--DEQKSVCTKYGVSGYPTIQWFPK 105
Cdd:cd02997   5 LTDEDFRKFLKKEKHVLVMFYAPWCGHCKKMKPEFTKAATELKEDGKGVLAAVDCtkPEHDALKEEYNVKGFPTFKYFEN 84

                        90       100
                ....*....|....*....|
gi 42571269 106 GSLEpQKYEGPRNAEALAEY 125
Cdd:cd02997  85 GKFV-EKYEGERTAEDIIEF 103
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 143-250 4.28e-30

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 117.16  E-value: 4.28e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  143 VVVLTPDNFDEIVLDqNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKQEEG-VVIANLDADAHKALGEKYGVSGFPTLKF 221
Cdd:PTZ00102  34 VTVLTDSTFDKFITE-NEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSeIVLASVDATEEMELAQEFGVRGYPTIKF 112

                         90       100
                 ....*....|....*....|....*....
gi 42571269  222 FPKDNKAghDYDGGRDLDDFVSFINEKSG 250
Cdd:PTZ00102 113 FNKGNPV--NYSGGRTADGIVSWIKKLTG 139
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 142-245 2.82e-29

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: 106.63  E-value: 2.82e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 142 NVVVLTPDNFDEIvLDQNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKQEEGVVIANLDA--DAHKALGEKYGVSGFPTL 219
Cdd:cd02997   1 DVVHLTDEDFRKF-LKKEKHVLVMFYAPWCGHCKKMKPEFTKAATELKEDGKGVLAAVDCtkPEHDALKEEYNVKGFPTF 79

                        90       100
                ....*....|....*....|....*.
gi 42571269 220 KFFPKDnKAGHDYDGGRDLDDFVSFI 245
Cdd:cd02997  80 KYFENG-KFVEKYEGERTAEDIIEFM 104
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 28-126 3.22e-29

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: 106.68  E-value: 3.22e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  28 LTDDSFEKEV-GKDKGALVEFYAPWCGHCKKLAPEYEKLGASFKKAksVLIAKVDCDEQ--KSVCTKYGVSGYPTIQWFP 104
Cdd:cd03002   5 LTPKNFDKVVhNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKELDGL--VQVAAVDCDEDknKPLCGKYGVQGFPTLKVFR 82

                        90       100
                ....*....|....*....|....*.
gi 42571269 105 KG----SLEPQKYEGPRNAEALAEYV 126
Cdd:cd03002  83 PPkkasKHAVEDYNGERSAKAIVDFV 108
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 142-245 9.10e-29

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: 105.06  E-value: 9.10e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 142 NVVVLTPDNFDEIVldQNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKQE-EGVVIANLDADAHKALGEKYGVSGFPTLK 220
Cdd:cd03005   1 GVLELTEDNFDHHI--AEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFNNEnPSVKIAKVDCTQHRELCSEFQVRGYPTLL 78

                        90       100
                ....*....|....*....|....*
gi 42571269 221 FFpKDNKAGHDYDGGRDLDDFVSFI 245
Cdd:cd03005  79 LF-KDGEKVDKYKGTRDLDSLKEFV 102
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 142-247 1.22e-28

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: 104.90  E-value: 1.22e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 142 NVVVLTPDNFDEIVLDQNKDVLVEFYAPWCGHCKSLAPTYEKVATvfKQEEGVVIANLDADAHKALGEKYGVSGFPTLKF 221
Cdd:COG3118   1 AVVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAA--EYGGKVKFVKVDVDENPELAAQFGVRSIPTLLL 78

                        90       100
                ....*....|....*....|....*.
gi 42571269 222 FpKDNKAGHDYDGGRDLDDFVSFINE 247
Cdd:COG3118  79 F-KDGQPVDRFVGALPKEQLREFLDK 103
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 40-138 2.93e-27

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: 109.38  E-value: 2.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269    40 DKGALVEFYAPWCGHCKKLAPEYEKLGASFKKAKS-VLIAKVDCDEQKsvCTKYGVSGYPTIQWFPKGS-LEPQKYEGPR 117
Cdd:TIGR01130 364 TKDVLVEFYAPWCGHCKNLAPIYEELAEKYKDAESdVVIAKMDATAND--VPPFEVEGFPTIKFVPAGKkSEPVPYDGDR 441

                          90       100
                  ....*....|....*....|.
gi 42571269   118 NAEALAEYVNKEGGTNVKLAA 138
Cdd:TIGR01130 442 TLEDFSKFIAKHATFPLEGKA 462
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 143-245 2.19e-24

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: 93.90  E-value: 2.19e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 143 VVVLTPDNFDEIVLDQNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKqeEGVVIANLDADAHKALGEKYGVSGFPTLKFF 222
Cdd:cd03004   3 VITLTPEDFPELVLNRKEPWLVDFYAPWCGPCQALLPELRKAARALK--GKVKVGSVDCQKYESLCQQANIRAYPTIRLY 80

                        90       100
                ....*....|....*....|....
gi 42571269 223 PKDNKAGHDYDG-GRDLDDFVSFI 245
Cdd:cd03004  81 PGNASKYHSYNGwHRDADSILEFI 104
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 30-128 4.21e-24

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: 93.29  E-value: 4.21e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  30 DDSFeKEVGKDKGALVEFYAPWCGHCKKLAPEYEKLGASFKKAKS-VLIAKVDCDEQKSVCTKYGVSGYPTIQWFpKGSL 108
Cdd:cd03000   6 DDSF-KDVRKEDIWLVDFYAPWCGHCKKLEPVWNEVGAELKSSGSpVRVGKLDATAYSSIASEFGVRGYPTIKLL-KGDL 83

                        90       100
                ....*....|....*....|
gi 42571269 109 EpQKYEGPRNAEALAEYVNK 128
Cdd:cd03000  84 A-YNYRGPRTKDDIVEFANR 102
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 28-126 1.46e-23

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: 91.58  E-value: 1.46e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  28 LTDDSF-EKEVGKDKGALVEFYAPWCGHCKKLAPEYEKLgASFKKAKsVLIAKVDCDEQKSVCTKYGVSGYPTIQWFPKG 106
Cdd:cd03004   6 LTPEDFpELVLNRKEPWLVDFYAPWCGPCQALLPELRKA-ARALKGK-VKVGSVDCQKYESLCQQANIRAYPTIRLYPGN 83

                        90       100
                ....*....|....*....|.
gi 42571269 107 SLEPQKYEG-PRNAEALAEYV 126
Cdd:cd03004  84 ASKYHSYNGwHRDADSILEFI 104
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 28-128 2.24e-23

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: 91.03  E-value: 2.24e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  28 LTDDSFEKEVGKDKG-ALVEFYAPWCGHCKKLAPEYEKLGASFkkAKSVLIAKVDCDEQKSVCTKYGVSGYPTIQWFPKG 106
Cdd:COG3118   5 LTDENFEEEVLESDKpVLVDFWAPWCGPCKMLAPVLEELAAEY--GGKVKFVKVDVDENPELAAQFGVRSIPTLLLFKDG 82

                        90       100
                ....*....|....*....|..
gi 42571269 107 SLEPQKyEGPRNAEALAEYVNK 128
Cdd:COG3118  83 QPVDRF-VGALPKEQLREFLDK 103
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 142-231 6.83e-23

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: 90.41  E-value: 6.83e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 142 NVVVLTPDNFDEIVLDQNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKQEEGVV-IANLD--ADAHKALGEKYGVSGFPT 218
Cdd:cd02992   2 PVIVLDAASFNSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRKWRPVVrVAAVDcaDEENVALCRDFGVTGYPT 81

                        90
                ....*....|...
gi 42571269 219 LKFFPKDNKAGHD 231
Cdd:cd02992  82 LRYFPPFSKEATD 94
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 149-246 9.30e-23

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: 89.15  E-value: 9.30e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 149 DNFDEIVlDQNKDVLVEFYAPWCGHCKSLAPTYEKVAtvfKQEEGVVIANLDADAHKALGEKYGVSGFPTLKFFpKDNKA 228
Cdd:cd02947   1 EEFEELI-KSAKPVVVDFWAPWCGPCKAIAPVLEELA---EEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFF-KNGKE 75

                        90
                ....*....|....*...
gi 42571269 229 GHDYDGGRDLDDFVSFIN 246
Cdd:cd02947  76 VDRVVGADPKEELEEFLE 93
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 28-125 1.37e-22

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: 89.25  E-value: 1.37e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  28 LTDDSFEKEV-GKDKGALVEFYAPWCGHCKKLAPEYEKLGASFKK-AKSVLIAKVDC--DEQKSVCTKYGVSGYPTIQWF 103
Cdd:cd02992   6 LDAASFNSALlGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRKwRPVVRVAAVDCadEENVALCRDFGVTGYPTLRYF 85

                        90       100
                ....*....|....*....|....*.
gi 42571269 104 PKGSLEPQ---KYEGP-RNAEALAEY 125
Cdd:cd02992  86 PPFSKEATdglKQEGPeRDVNELREA 111
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 146-247 5.77e-21

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: 84.65  E-value: 5.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269   146 LTPDNFDEIVLDQNKDVLVEFYAPWCGHCKSLAPTYEKVAtvfKQEEG-VVIANLDADAHKALGEKYGVSGFPTLKFFpK 224
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELA---KEYEGkVKFVKLNVDENPDIAAKYGIRSIPTLLLF-K 76

                          90       100
                  ....*....|....*....|...
gi 42571269   225 DNKAGHDYDGGRDLDDFVSFINE 247
Cdd:TIGR01068  77 NGKEVDRSVGALPKAALKQLINK 99
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 28-128 9.73e-20

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: 81.57  E-value: 9.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269    28 LTDDSFEKEV-GKDKGALVEFYAPWCGHCKKLAPEYEKLGAsfKKAKSVLIAKVDCDEQKSVCTKYGVSGYPTIQWFPKG 106
Cdd:TIGR01068   1 LTDANFDETIaSSDKPVLVDFWAPWCGPCKMIAPILEELAK--EYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNG 78

                          90       100
                  ....*....|....*....|..
gi 42571269   107 SlEPQKYEGPRNAEALAEYVNK 128
Cdd:TIGR01068  79 K-EVDRSVGALPKAALKQLINK 99
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 142-245 1.81e-19

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: 80.90  E-value: 1.81e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 142 NVVVLTPDNFDEIvLDQNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKQE----EGVVIANLDADAHKALGEKYGVSGFP 217
Cdd:cd02996   2 EIVSLTSGNIDDI-LQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEEfpdaGKVVWGKVDCDKESDIADRYRINKYP 80

                        90       100
                ....*....|....*....|....*...
gi 42571269 218 TLKFFPKDNKAGHDYDGGRDLDDFVSFI 245
Cdd:cd02996  81 TLKLFRNGMMMKREYRGQRSVEALAEFV 108
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 31-127 3.46e-19

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: 79.91  E-value: 3.46e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  31 DSFEKEVGKDKGALVEFYAPWCGHCKKLAPEYEKLGASFKKAKsvlIAKVDCDEQKSVCTKYGVSGYPTIQWFpKGSLEP 110
Cdd:cd02947   1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVK---FVKVDVDENPELAEEYGVRSIPTFLFF-KNGKEV 76

                        90
                ....*....|....*..
gi 42571269 111 QKYEGPRNAEALAEYVN 127
Cdd:cd02947  77 DRVVGADPKEELEEFLE 93
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 163-246 4.72e-19

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: 79.81  E-value: 4.72e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 163 LVEFYAPWCGHCKSLAPTYEKVATVFKQEEGVV-IANLDADAHKALGEKYGVSGFPTLKFFPKDnkAGHDYDGGRDLDDF 241
Cdd:cd03000  19 LVDFYAPWCGHCKKLEPVWNEVGAELKSSGSPVrVGKLDATAYSSIASEFGVRGYPTIKLLKGD--LAYNYRGPRTKDDI 96


                ....*
gi 42571269 242 VSFIN 246
Cdd:cd03000  97 VEFAN 101
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 28-126 1.73e-18

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: 78.59  E-value: 1.73e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  28 LTDDSFEKEVGKDKGALVEFYAPWCGHCKKLAPEYEKLGASFKK----AKSVLIAKVDCDEQKSVCTKYGVSGYPTIQWF 103
Cdd:cd02996   6 LTSGNIDDILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEefpdAGKVVWGKVDCDKESDIADRYRINKYPTLKLF 85

                        90       100
                ....*....|....*....|...
gi 42571269 104 PKGSLEPQKYEGPRNAEALAEYV 126
Cdd:cd02996  86 RNGMMMKREYRGQRSVEALAEFV 108
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 28-151 2.97e-17

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 78.13  E-value: 2.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269   28 LTDDSFEKEVGKDKGA-----LVEFYAPWCGHCKKLAPEYEKLGASFKKAksVLIAKVDCDEQKSVCTKYGVSGYPTIQW 102
Cdd:PTZ00443  35 LNDKNFEKLTQASTGAttgpwFVKFYAPWCSHCRKMAPAWERLAKALKGQ--VNVADLDATRALNLAKRFAIKGYPTLLL 112

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 42571269  103 FPKGSLepQKYE-GPRNAEALAEYVNKEGGTNVKlAAVPQ--NVVVLTPDNF 151
Cdd:PTZ00443 113 FDKGKM--YQYEgGDRSTEKLAAFALGDFKKALG-APVPAplSFFALTIDFF 161
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 132-235 1.66e-16

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 76.20  E-value: 1.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  132 TNVKLAAVPQN-VVVLTPDNFDEIVLDQNKDV----LVEFYAPWCGHCKSLAPTYEKVAtvfKQEEGVV-IANLDADAHK 205
Cdd:PTZ00443  20 TNVKLDAEDANaLVLLNDKNFEKLTQASTGATtgpwFVKFYAPWCSHCRKMAPAWERLA---KALKGQVnVADLDATRAL 96

                         90       100       110
                 ....*....|....*....|....*....|
gi 42571269  206 ALGEKYGVSGFPTLKFFPKDNKagHDYDGG 235
Cdd:PTZ00443  97 NLAKRFAIKGYPTLLLFDKGKM--YQYEGG 124
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 142-247 4.03e-16

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: 72.03  E-value: 4.03e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 142 NVVVLTPDNFDEIVLDqnkDVLVEFYAPWCGHCKSLAPTYEKVATVfKQEEGVVIANLDADAHKALGEKYGVSGFPTLkF 221
Cdd:cd02994   2 NVVELTDSNWTLVLEG---EWMIEFYAPWCPACQQLQPEWEEFADW-SDDLGINVAKVDVTQEPGLSGRFFVTALPTI-Y 76

                        90       100
                ....*....|....*....|....*.
gi 42571269 222 FPKDNKAgHDYDGGRDLDDFVSFINE 247
Cdd:cd02994  77 HAKDGVF-RRYQGPRDKEDLISFIEE 101
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 44-128 1.83e-13

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: 64.71  E-value: 1.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  44 LVEFYAPWCGHCKKLAPEYEKLgASFKKAKSVLIAKVDCDEQKSVCTKYGVSGYPTIQWFPKGslEPQKYEGPRNAEALA 123
Cdd:cd02994  20 MIEFYAPWCPACQQLQPEWEEF-ADWSDDLGINVAKVDVTQEPGLSGRFFVTALPTIYHAKDG--VFRRYQGPRDKEDLI 96


                ....*
gi 42571269 124 EYVNK 128
Cdd:cd02994  97 SFIEE 101
PTZ00051 PTZ00051
thioredoxin; Provisional
 29-107 3.20e-13

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 64.13  E-value: 3.20e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42571269   29 TDDSFEKEVGKDKGALVEFYAPWCGHCKKLAPEYEKLGasfKKAKSVLIAKVDCDEQKSVCTKYGVSGYPTIQWFPKGS 107
Cdd:PTZ00051   7 SQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECS---KEYTKMVFVKVDVDELSEVAEKENITSMPTFKVFKNGS 82
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 33-125 4.58e-13

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: 63.70  E-value: 4.58e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  33 FEKEVGKDKGALVEFYAPWCGHCKKLAPEYEKLGasfKKAKSVL-IAKVDCDEQKSVCTKYGVSGYPTIQWFPKGsLEPQ 111
Cdd:cd03003  11 FDAAVNSGEIWFVNFYSPRCSHCHDLAPTWREFA---KEMDGVIrIGAVNCGDDRMLCRSQGVNSYPSLYVFPSG-MNPE 86

                        90
                ....*....|....
gi 42571269 112 KYEGPRNAEALAEY 125
Cdd:cd03003  87 KYYGDRSKESLVKF 100
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 28-126 9.10e-13

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: 63.24  E-value: 9.10e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  28 LTDDSFEKEVG---KDKGALVEFYAPWCGHCKKLAPEYEKLGASFKKAKsVLIAKVDCD-EQKSVCTK-YGVSGYPTIQW 102
Cdd:cd02993   6 LSRAEIEALAKgerRNQSTLVVLYAPWCPFCQAMEASYEELAEKLAGSN-VKVAKFNADgEQREFAKEeLQLKSFPTILF 84

                        90       100
                ....*....|....*....|....*
gi 42571269 103 FPKGSLEPQKYEGP-RNAEALAEYV 126
Cdd:cd02993  85 FPKNSRQPIKYPSEqRDVDSLLMFV 109
trxA PRK09381
thioredoxin TrxA;
28-112 9.70e-13

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 63.16  E-value: 9.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269   28 LTDDSFEKEVGKDKG-ALVEFYAPWCGHCKKLAPEYEKLGASFKKAKSVliAKVDCDEQKSVCTKYGVSGYPTIQWFPKG 106
Cdd:PRK09381   8 LTDDSFDTDVLKADGaILVDFWAEWCGPCKMIAPILDEIADEYQGKLTV--AKLNIDQNPGTAPKYGIRGIPTLLLFKNG 85


                 ....*.
gi 42571269  107 SLEPQK 112
Cdd:PRK09381  86 EVAATK 91
trxA PRK09381
thioredoxin TrxA;
143-222 2.17e-12

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 62.00  E-value: 2.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  143 VVVLTPDNFDEIVLDQNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKQEegVVIANLDADAHKALGEKYGVSGFPTLKFF 222
Cdd:PRK09381   5 IIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGK--LTVAKLNIDQNPGTAPKYGIRGIPTLLLF 82
PTZ00051 PTZ00051
thioredoxin; Provisional
 145-222 7.44e-12

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 60.27  E-value: 7.44e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42571269  145 VLTPDNFDEIvLDQNKDVLVEFYAPWCGHCKSLAPTYEKVAtvfKQEEGVVIANLDADAHKALGEKYGVSGFPTLKFF 222
Cdd:PTZ00051   5 VTSQAEFEST-LSQNELVIVDFYAEWCGPCKRIAPFYEECS---KEYTKMVFVKVDVDELSEVAEKENITSMPTFKVF 78
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 153-228 3.12e-11

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


Pssm-ID: 239248 [Multi-domain]  Cd Length: 142  Bit Score: 59.66  E-value: 3.12e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571269 153 EIVLDQNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKQEEGVVIANLDADAHKALGEKYGVSGFPTLKFFPKDNKA 228
Cdd:cd02950  14 EVALSNGKPTLVEFYADWCTVCQEMAPDVAKLKQKYGDQVNFVMLNVDNPKWLPEIDRYRVDGIPHFVFLDREGNE 89
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 156-245 3.88e-11

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: 58.52  E-value: 3.88e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 156 LDQNKD--VLVEFYAPWCGHCKSLAPTYEKVATVFKQeegvvIANLDADA---HKALGEKYGVSGFPTLKFFPKDNKAgh 230
Cdd:cd02999  13 MAFNREdyTAVLFYASWCPFSASFRPHFNALSSMFPQ-----IRHLAIEEssiKPSLLSRYGVVGFPTILLFNSTPRV-- 85

                        90
                ....*....|....*
gi 42571269 231 DYDGGRDLDDFVSFI 245
Cdd:cd02999  86 RYNGTRTLDSLAAFY 100
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 141-244 1.05e-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: 1.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 141 QNVVVLTPDNFDEIVLDQnkDV-LVEFYAPWCGHCKSLAPTYEKVAtvfKQEEGVV-IANLDADAHKALGEKYGVSGFPT 218
Cdd:cd03003   1 PEIVTLDRGDFDAAVNSG--EIwFVNFYSPRCSHCHDLAPTWREFA---KEMDGVIrIGAVNCGDDRMLCRSQGVNSYPS 75

                        90       100
                ....*....|....*....|....*.
gi 42571269 219 LKFFPKDNKaGHDYDGGRDLDDFVSF 244
Cdd:cd03003  76 LYVFPSGMN-PEKYYGDRSKESLVKF 100
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 159-245 1.06e-10

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: 57.46  E-value: 1.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 159 NKDVLVEFYAPWCGHCKSLAPTYEKVATVFKqEEGVVIANLDADAH-KALG-EKYGVSGFPTLKFFPKDNKAGHDYDG-G 235
Cdd:cd02993  21 NQSTLVVLYAPWCPFCQAMEASYEELAEKLA-GSNVKVAKFNADGEqREFAkEELQLKSFPTILFFPKNSRQPIKYPSeQ 99

                        90
                ....*....|
gi 42571269 236 RDLDDFVSFI 245
Cdd:cd02993 100 RDVDSLLMFV 109
PRK10996 PRK10996
thioredoxin 2; Provisional
 143-222 1.31e-10

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 58.16  E-value: 1.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  143 VVVLTPDNFDEIvLDQNKDVLVEFYAPWCGHCKSLAPTYEKVAtvfkQEEG--VVIANLDADAHKALGEKYGVSGFPTLK 220
Cdd:PRK10996  37 VINATGETLDKL-LQDDLPVVIDFWAPWCGPCRNFAPIFEDVA----AERSgkVRFVKVNTEAERELSARFRIRSIPTIM 111


                 ..
gi 42571269  221 FF 222
Cdd:PRK10996 112 IF 113
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 44-127 1.65e-10

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: 56.51  E-value: 1.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  44 LVEFYAPWCGHCKKLAPEYEKLGASFkkAKSVLIAKVDCDEQKSVCTKYGVSGYPTIQWFPKGSLEPQkYEGPRNAEALA 123
Cdd:cd02956  16 VVDFWAPRSPPSKELLPLLERLAEEY--QGQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVDG-FQGAQPEEQLR 92


                ....
gi 42571269 124 EYVN 127
Cdd:cd02956  93 QMLD 96
PLN02309 PLN02309
5'-adenylylsulfate reductase
 35-127 2.65e-10

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 60.19  E-value: 2.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269   35 KEVGKDKGALVEFYAPWCGHCKKLAPEYEKLGASFKKAKsVLIAKVDCD-EQKSVCT-KYGVSGYPTIQWFPKGSLEPQK 112
Cdd:PLN02309 360 KLENRKEPWLVVLYAPWCPFCQAMEASYEELAEKLAGSG-VKVAKFRADgDQKEFAKqELQLGSFPTILLFPKNSSRPIK 438

                         90
                 ....*....|....*.
gi 42571269  113 YEGP-RNAEALAEYVN 127
Cdd:PLN02309 439 YPSEkRDVDSLLSFVN 454
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 149-247 3.34e-10

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: 55.74  E-value: 3.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 149 DNFDEIVLDQ-NKDVLVEFYAPWCGHCKSLAPTYEKVATVFKQEegVVIANLDADAHKALGEKYGVSGFPTLKFFpkdnk 227
Cdd:cd02956   1 QNFQQVLQEStQVPVVVDFWAPRSPPSKELLPLLERLAEEYQGQ--FVLAKVNCDAQPQIAQQFGVQALPTVYLF----- 73

                        90       100
                ....*....|....*....|
gi 42571269 228 aghdyDGGRDLDDFVSFINE 247
Cdd:cd02956  74 -----AAGQPVDGFQGAQPE 88
PLN02309 PLN02309
5'-adenylylsulfate reductase
 141-246 8.54e-10

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 58.65  E-value: 8.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  141 QNVVVLTPDNFDEIVLDQNKD--VLVEFYAPWCGHCKSLAPTYEKVATVFKQeEGVVIANLDAD-AHKALG-EKYGVSGF 216
Cdd:PLN02309 345 QNVVALSRAGIENLLKLENRKepWLVVLYAPWCPFCQAMEASYEELAEKLAG-SGVKVAKFRADgDQKEFAkQELQLGSF 423

                         90       100       110
                 ....*....|....*....|....*....|.
gi 42571269  217 PTLKFFPKDNKAGHDYDG-GRDLDDFVSFIN 246
Cdd:PLN02309 424 PTILLFPKNSSRPIKYPSeKRDVDSLLSFVN 454
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 113-246 1.02e-09

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: 58.49  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269   113 YEGPRNAEALAEYVNKEGGTNVKLAAVPQNVVVLTPDNFDEIV-LDQNKDV-LVEFYAPWCGHCKSLAPTYEKVATVFKQ 190
Cdd:TIGR00424 323 HKGNIKEETLDGAVNGNGSDAVADIFDSNNVVSLSRPGIENLLkLEERKEAwLVVLYAPWCPFCQAMEASYLELAEKLAG 402

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 42571269   191 eEGVVIANLDADA-HKALG-EKYGVSGFPTLKFFPKDNKAGHDYDG-GRDLDDFVSFIN 246
Cdd:TIGR00424 403 -SGVKVAKFRADGdQKEFAkQELQLGSFPTILFFPKHSSRPIKYPSeKRDVDSLMSFVN 460
PRK10996 PRK10996
thioredoxin 2; Provisional
 29-108 4.04e-09

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 53.92  E-value: 4.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269   29 TDDSFEKEVGKDKGALVEFYAPWCGHCKKLAPEYEKLGAsfKKAKSVLIAKVDCDEQKSVCTKYGVSGYPTIQWFPKGSL 108
Cdd:PRK10996  41 TGETLDKLLQDDLPVVIDFWAPWCGPCRNFAPIFEDVAA--ERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFKNGQV 118
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 44-106 6.34e-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: 51.55  E-value: 6.34e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571269  44 LVEFYAPWCGHCKKLAPEYEKLgasFKKAKSVLIAKVDCDEQKSVC---TKYGVSGYPTIQWFPKG 106
Cdd:cd01659   1 LVLFYAPWCPFCQALRPVLAEL---ALLNKGVKFEAVDVDEDPALEkelKRYGVGGVPTLVVFGPG 63
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 146-247 7.35e-09

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 53.16  E-value: 7.35e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 146 LTPDNFDEIVLDQNKD--VLVEFYAPWCGHCKSLAPTYEKVAtvfKQEEGVVIANLD----------------------A 201
Cdd:COG0526  13 LTDLDGKPLSLADLKGkpVLVNFWATWCPPCRAEMPVLKELA---EEYGGVVFVGVDvdenpeavkaflkelglpypvlL 89

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 42571269 202 DAHKALGEKYGVSGFPTLKFFPKDNKAGHDYDGGRDLDDFVSFINE 247
Cdd:COG0526  90 DPDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEK 135
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 28-128 8.44e-09

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 52.77  E-value: 8.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  28 LTDDSFEKEVGKDKGALVEFYAPWCGHCKKLAPEYEKLgasFKKAKSVLIAKVDCDEQK--------------------- 86
Cdd:COG0526  16 LDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKEL---AEEYGGVVFVGVDVDENPeavkaflkelglpypvlldpd 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 42571269  87 -SVCTKYGVSGYPTIQWFPKGSLEPQKYEGPRNAEALAEYVNK 128
Cdd:COG0526  93 gELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEK 135
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 44-127 8.47e-09

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: 55.79  E-value: 8.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269    44 LVEFYAPWCGHCKKLAPEYEKLGASFkKAKSVLIAKVDCD-EQKSVCTK-YGVSGYPTIQWFPKGSLEPQKYEGP-RNAE 120
Cdd:TIGR00424 375 LVVLYAPWCPFCQAMEASYLELAEKL-AGSGVKVAKFRADgDQKEFAKQeLQLGSFPTILFFPKHSSRPIKYPSEkRDVD 453


                  ....*..
gi 42571269   121 ALAEYVN 127
Cdd:TIGR00424 454 SLMSFVN 460
DsbDgamma cd02953
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
 158-226 1.17e-08

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


Pssm-ID: 239251 [Multi-domain]  Cd Length: 104  Bit Score: 51.45  E-value: 1.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 158 QNKDVLVEFYAPWCGHCKslapTYEKVatVFKQEE-------GVVIANLDA----DAHKALGEKYGVSGFPTLKFFPKDN 226
Cdd:cd02953  10 QGKPVFVDFTADWCVTCK----VNEKV--VFSDPEvqaalkkDVVLLRADWtkndPEITALLKRFGVFGPPTYLFYGPGG 83
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 39-126 2.78e-08

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: 50.43  E-value: 2.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  39 KDKGALVEFYAPWCGHCKKLAPEYEKLGASFkkaKSVLIAKVDCDEQK-SVCTKYGVSGYPTIQWFPKGSLepQKYEGPR 117
Cdd:cd02999  17 REDYTAVLFYASWCPFSASFRPHFNALSSMF---PQIRHLAIEESSIKpSLLSRYGVVGFPTILLFNSTPR--VRYNGTR 91


                ....*....
gi 42571269 118 NAEALAEYV 126
Cdd:cd02999  92 TLDSLAAFY 100
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 157-246 4.16e-08

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 51.06  E-value: 4.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 157 DQNKDVLVEFYAPWCGHCKSLaptyekVATVFKQEE-------GVVIANLDADA-------------HKALGEKYGVSGF 216
Cdd:COG2143  38 AEGKPILLFFESDWCPYCKKL------HKEVFSDPEvaaylkeNFVVVQLDAEGdkevtdfdgetltEKELARKYGVRGT 111

                        90       100       110
                ....*....|....*....|....*....|
gi 42571269 217 PTLKFFPKDNKAGHDYDGGRDLDDFVSFIN 246
Cdd:COG2143 112 PTLVFFDAEGKEIARIPGYLKPETFLALLK 141
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
158-225 7.82e-08

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 49.35  E-value: 7.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269   158 QNKDVLVEFYAPWCGHCKSLA--------------PTYEKVATVFKQEEGVVIANLDADAHKALGEKYGVSGFPTLKFFP 223
Cdd:pfam13098   3 NGKPVLVVFTDPDCPYCKKLKkelledpdvtvylgPNFVFIAVNIWCAKEVAKAFTDILENKELGRKYGVRGTPTIVFFD 82


                  ..
gi 42571269   224 KD 225
Cdd:pfam13098  83 GK 84
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 163-227 4.29e-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: 46.54  E-value: 4.29e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42571269 163 LVEFYAPWCGHCKSLAPTYEKVAtvfKQEEGVVIANLDAD---AHKALGEKYGVSGFPTLKFFPKDNK 227
Cdd:cd01659   1 LVLFYAPWCPFCQALRPVLAELA---LLNKGVKFEAVDVDedpALEKELKRYGVGGVPTLVVFGPGIG 65
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 40-124 8.69e-07

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


Pssm-ID: 239248 [Multi-domain]  Cd Length: 142  Bit Score: 47.33  E-value: 8.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  40 DKGALVEFYAPWCGHCKKLAPEYEKLGASFKKAKSVLIAKVDCDEQKSVCTKYGVSGYPTIQWF-----PKGS---LEPQ 111
Cdd:cd02950  20 GKPTLVEFYADWCTVCQEMAPDVAKLKQKYGDQVNFVMLNVDNPKWLPEIDRYRVDGIPHFVFLdregnEEGQsigLQPK 99

                        90
                ....*....|...
gi 42571269 112 KYEGpRNAEALAE 124
Cdd:cd02950 100 QVLA-QNLDALVA 111
OST3_OST6 pfam04756
OST3 / OST6 family, transporter family; The proteins in this family are part of a complex of ...
 52-128 9.55e-07

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


Pssm-ID: 461420  Cd Length: 294  Bit Score: 48.78  E-value: 9.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269    52 CGHCKKLAPEYEKLGASFKKA-----KSVLIAKVDCDEQKSVCTKYGVSGYPTIQWFP------KGSLEPQKY---EGPR 117
Cdd:pfam04756  46 CQLCREFQPEFELVAKSWFKDhkagsSKLFFATLDFDDGKDVFQSLGLQTAPHLLLFPptggpkISDSEPDQYdftRGGF 125

                          90
                  ....*....|.
gi 42571269   118 NAEALAEYVNK 128
Cdd:pfam04756 126 SAEQLAAFLSR 136
DsbD COG4232
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ...
 156-227 1.64e-06

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


Pssm-ID: 443376 [Multi-domain]  Cd Length: 416  Bit Score: 48.65  E-value: 1.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 156 LDQNKDVLVEFYAPWCGHCKSLaptyEKvaTVFKQEE-------GVVIANLDAD----AHKALGEKYGVSGFPTLKFFPK 224
Cdd:COG4232 317 RAEGKPVFVDFTADWCVTCKEN----ER--TVFSDPEvqaaladDVVLLKADVTdndpEITALLKRFGRFGVPTYVFYDP 390


                ...
gi 42571269 225 DNK 227
Cdd:COG4232 391 DGE 393
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 147-222 1.78e-06

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


Pssm-ID: 239282 [Multi-domain]  Cd Length: 97  Bit Score: 45.34  E-value: 1.78e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42571269 147 TPDNFDEIV-LDQNKDVLVEFYAPWCGHCKSLAPTYEKVAT-VFKQeegVVIANLDADAHKALGEKYGVSGFPTLKFF 222
Cdd:cd02984   1 SEEEFEELLkSDASKLLVLHFWAPWAEPCKQMNQVFEELAKeAFPS---VLFLSIEAEELPEISEKFEITAVPTFVFF 75
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 157-245 2.04e-06

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


Pssm-ID: 239247 [Multi-domain]  Cd Length: 97  Bit Score: 45.18  E-value: 2.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 157 DQNKDVLVEFYAPWCGHCKSLAPTYEKVATVFkqEEGVVIANLDADAHKALGEKYGVSGFPTLKFFpKDNKAGHDYDGGR 236
Cdd:cd02949  11 ESDRLILVLYTSPTCGPCRTLKPILNKVIDEF--DGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFF-KDKELVKEISGVK 87


                ....*....
gi 42571269 237 DLDDFVSFI 245
Cdd:cd02949  88 MKSEYREFI 96
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
158-218 2.13e-06

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 46.01  E-value: 2.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 158 QNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKQEEGVVIA-NLD-------------------ADAHKALGEKYGVSGFP 217
Cdd:COG1225  20 RGKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGvSSDsdeahkkfaekyglpfpllSDPDGEVAKAYGVRGTP 99


                .
gi 42571269 218 T 218
Cdd:COG1225 100 T 100
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 151-227 2.35e-06

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


Pssm-ID: 239309 [Multi-domain]  Cd Length: 123  Bit Score: 45.75  E-value: 2.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 151 FDEIVLDQnKDVLVEFYAPWCGHCKSLAPTYEKVA---TV---------------FKQEEGVVIANLdADAHKALGEKYG 212
Cdd:cd03011  13 FDLESLSG-KPVLVYFWATWCPVCRFTSPTVNQLAadyPVvsvalrsgddgavarFMQKKGYGFPVI-NDPDGVISARWG 90

                        90
                ....*....|....*
gi 42571269 213 VSGFPTLKFFPKDNK 227
Cdd:cd03011  91 VSVTPAIVIVDPGGI 105
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
39-99 2.64e-06

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 45.63  E-value: 2.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  39 KDKGALVEFYAPWCGHCKKLAPEYEKLGASFKKAKSVLIA----KVD----------------CDEQKSVCTKYGVSGYP 98
Cdd:COG1225  20 RGKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGvssdSDEahkkfaekyglpfpllSDPDGEVAKAYGVRGTP 99


                .
gi 42571269  99 T 99
Cdd:COG1225 100 T 100
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
41-125 1.45e-05

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 42.80  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269    41 KGALVEFYAPWCGHCKKLA--------------PEYEKLGASFKKAKSVLIAKVDCDEQKSVCTKYGVSGYPTIqWFPKG 106
Cdd:pfam13098   5 KPVLVVFTDPDCPYCKKLKkelledpdvtvylgPNFVFIAVNIWCAKEVAKAFTDILENKELGRKYGVRGTPTI-VFFDG 83

                          90
                  ....*....|....*....
gi 42571269   107 SLEPQKYEGPRNAEALAEY 125
Cdd:pfam13098  84 KGELLRLPGYVPAEEFLAL 102
TMX2 cd02962
TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related ...
 140-223 1.83e-05

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


Pssm-ID: 239260 [Multi-domain]  Cd Length: 152  Bit Score: 43.52  E-value: 1.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 140 PQNVVVLTPDNFDEIvLDQNKDV--LVEFYAPWCGHCKSLAPTYEKVATVFkQEEGVVIANLDADAHKALGEKYGVSGFP 217
Cdd:cd02962  27 PEHIKYFTPKTLEEE-LERDKRVtwLVEFFTTWSPECVNFAPVFAELSLKY-NNNNLKFGKIDIGRFPNVAEKFRVSTSP 104


                ....*.
gi 42571269 218 TLKFFP 223
Cdd:cd02962 105 LSKQLP 110
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 158-218 3.75e-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: 42.22  E-value: 3.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 158 QNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKQEEGVVIA-NLD---------------------ADAHKALGEKYGVSG 215
Cdd:cd02966  18 KGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGvNVDdddpaavkaflkkygitfpvlLDPDGELAKAYGVRG 97


                ...
gi 42571269 216 FPT 218
Cdd:cd02966  98 LPT 100
OST3_OST6 pfam04756
OST3 / OST6 family, transporter family; The proteins in this family are part of a complex of ...
 142-252 6.22e-05

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


Pssm-ID: 461420  Cd Length: 294  Bit Score: 43.39  E-value: 6.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269   142 NVVVLTPDNFDEIVLD-QNKDVLVEFYAPW----CGHCKSLAPTYEKVA-----TVFKQEEGVVIANLDADAHKALGEKY 211
Cdd:pfam04756  12 GVIKLNDSNYKRLLSGpRDYSVVVLLTALDprfgCQLCREFQPEFELVAkswfkDHKAGSSKLFFATLDFDDGKDVFQSL 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 42571269   212 GVSGFPTLKFFP------KDNKAGHDYD---GGRDLDDFVSFINEKSGTS 252
Cdd:pfam04756  92 GLQTAPHLLLFPptggpkISDSEPDQYDftrGGFSAEQLAAFLSRHTGVP 141
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 158-219 6.54e-05

Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX.


Pssm-ID: 239262 [Multi-domain]  Cd Length: 132  Bit Score: 41.83  E-value: 6.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269 158 QNKDVLVEFYAPWCGHCKSLAPT----YEKVATVFKQEEgVVIANLDADA-----------------------HKALGEK 210
Cdd:cd02964  16 EGKTVGLYFSASWCPPCRAFTPKlvefYEKLKEEGKNFE-IVFVSRDRSEesfneyfsemppwlavpfedeelRELLEKQ 94


                ....*....
gi 42571269 211 YGVSGFPTL 219
Cdd:cd02964  95 FKVEGIPTL 103
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 29-108 9.61e-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: 40.33  E-value: 9.61e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  29 TDDSFEKEVGKDKGAL--VEFYAPWCGHCKKLAPEYEKLGAsfKKAKSVLIAKVDCDEQKSVCTKYGVSGYPTIQWFPKG 106
Cdd:cd02984   1 SEEEFEELLKSDASKLlvLHFWAPWAEPCKQMNQVFEELAK--EAFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNG 78


                ..
gi 42571269 107 SL 108
Cdd:cd02984  79 TI 80
dipZ PRK00293
thiol:disulfide interchange protein precursor; Provisional
 158-236 9.85e-05

thiol:disulfide interchange protein precursor; Provisional


Pssm-ID: 234717 [Multi-domain]  Cd Length: 571  Bit Score: 43.28  E-value: 9.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  158 QNKDVLVEFYAPWCGHCKSlaptYEKVatVFKQEEgvVIANLD------AD------AHKALGEKYGVSGFPTLKFFpkd 225
Cdd:PRK00293 473 KGKPVMLDLYADWCVACKE----FEKY--TFSDPQ--VQQALAdtvllqADvtannaEDVALLKHYNVLGLPTILFF--- 541

                         90
                 ....*....|.
gi 42571269  226 NKAGHDYDGGR 236
Cdd:PRK00293 542 DAQGQEIPDAR 552
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 40-103 1.38e-04

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: 40.18  E-value: 1.38e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571269  40 DKGALVEFYAPWCGHCKKLAPEYEKLGASFKKAksVLIAKVDCDEQKSVCTKYGVSGYPTIQWF 103
Cdd:cd02949  13 DRLILVLYTSPTCGPCRTLKPILNKVIDEFDGA--VHFVEIDIDEDQEIAEAAGIMGTPTVQFF 74
PDI_a_EFP1_N cd03006
PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase ...
 44-119 1.86e-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: 40.15  E-value: 1.86e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42571269  44 LVEFYAPWCGHCKKLAPEYEKlgASFKKAKSVLIAKVDCDEQKSVC-TKYGVSGYPTIQWFPKgSLEPQKYEGPRNA 119
Cdd:cd03006  33 LVMYYAPWDAQSQAARQEFEQ--VAQKLSDQVLFVAINCWWPQGKCrKQKHFFYFPVIHLYYR-SRGPIEYKGPMRA 106
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 39-129 2.10e-04

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 40.66  E-value: 2.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  39 KDKGALVEFYAPWCGHCKKL------APEyeklgasFKKA--KSVLIAKVDCDEQKSVCT-------------KYGVSGY 97
Cdd:COG2143  39 EGKPILLFFESDWCPYCKKLhkevfsDPE-------VAAYlkENFVVVQLDAEGDKEVTDfdgetltekelarKYGVRGT 111

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 42571269  98 PTIQWFPK---------GSLEPQKYegprnaEALAEYVNKE 129
Cdd:COG2143 112 PTLVFFDAegkeiaripGYLKPETF------LALLKYVAEG 146
GlrX_arch TIGR02187
Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal ...
 51-248 3.63e-04

Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal domain with homology to bacterial and eukaryotic glutaredoxins, including a CPYC motif. There is an N-terminal domain which has even more distant homology to glutaredoxins. The name "glutaredoxin" may be inappropriate in the sense of working in tandem with glutathione and glutathione reductase which may not be present in the archaea. The overall domain structure appears to be related to bacterial alkylhydroperoxide reductases, but the homology may be distant enough that the function of this family is wholly different.


Pssm-ID: 274021 [Multi-domain]  Cd Length: 215  Bit Score: 40.89  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269    51 WCGHCKKLAPEYEKLGASFKkaksVLIAKVDCDEQKSVCTKYGVSGYPTIQWFPKGSLEPQKYEGPRNAEALAEYVN--- 127
Cdd:TIGR02187  36 YCKETEQLLEELSEVSPKLK----LEIYDFDTPEDKEEAEKYGVERVPTTIILEEGKDGGIRYTGIPAGYEFAALIEdiv 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269   128 --KEGGTNvklaaVPQNVVvltpdnfdEIVLDQNKDVLVE-FYAPWCGHCKSLAPTYEKVATVFKQEEGVVIanlDADAH 204
Cdd:TIGR02187 112 rvSQGEPG-----LSEKTV--------ELLQSLDEPVRIEvFVTPTCPYCPYAVLMAHKFALANDKILGEMI---EANEN 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 42571269   205 KALGEKYGVSGFPTLKFfpkdNKAGHDYDGGRDLDDFVSFINEK 248
Cdd:TIGR02187 176 PDLAEKYGVMSVPKIVI----NKGVEEFVGAYPEEQFLEYILSA 215
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 39-99 3.98e-04

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: 39.14  E-value: 3.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  39 KDKGALVEFYAPWCGHCKKLAPEYEKLGASFKKAKSVLIA----------------------KVDCDEQKSVCTKYGVSG 96
Cdd:cd02966  18 KGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGvnvddddpaavkaflkkygitfPVLLDPDGELAKAYGVRG 97


                ...
gi 42571269  97 YPT 99
Cdd:cd02966  98 LPT 100
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 141-219 1.84e-03

TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of about 500-800 amino acids, containing an N-terminal DnaJ domain followed by one redox active TRX domain. DnaJ is a member of the 40 kDa heat-shock protein (Hsp40) family of molecular chaperones, which regulate the activity of Hsp70s. TRX is involved in the redox regulation of many protein substrates through the reduction of disulfide bonds. TRX has been implicated to catalyse the reduction of Hsp33, a chaperone holdase that binds to unfolded protein intermediates. The presence of DnaJ and TRX domains in members of this family suggests that they could be involved in a redox-regulated chaperone network.


Pssm-ID: 239261 [Multi-domain]  Cd Length: 111  Bit Score: 36.97  E-value: 1.84e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42571269 141 QNVVVltPDNFDeivldqnKDVLVEFYAPWCGHCKSLAPTYEKVATVFkQEEGVVIANLDADAHKALGEKYGVSGFPTL 219
Cdd:cd02963  15 ENEIV--PKSFK-------KPYLIKITSDWCFSCIHIEPVWKEVIQEL-EPLGVGIATVNAGHERRLARKLGAHSVPAI 83
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 44-77 3.17e-03

DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer membrane-associated immunoreactive protein originally found in both acute and chronic disease strains of the pathogenic bacteria Coxiella burnetti. It contains a CXXC motif, assumed to be imbedded in a DsbA-like structure. Its homology to DsbA suggests that the protein is a protein disulfide oxidoreductase. The role of such a protein in pathogenesis is unknown.


Pssm-ID: 239321 [Multi-domain]  Cd Length: 154  Bit Score: 37.19  E-value: 3.17e-03
                        10        20        30
                ....*....|....*....|....*....|....
gi 42571269  44 LVEFYAPWCGHCKKLAPEYEKLGASFKKAKSVLI 77
Cdd:cd03023   9 IVEFFDYNCGYCKKLAPELEKLLKEDPDVRVVFK 42
DsbDgamma cd02953
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
 30-110 4.19e-03

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


Pssm-ID: 239251 [Multi-domain]  Cd Length: 104  Bit Score: 36.04  E-value: 4.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  30 DDSFEKEVGKDKGALVEFYAPWCGHCK---KLAPEYEKLGASFKKAKSVLIAKV--DCDEQKSVCTKYGVSGYPTIQWFP 104
Cdd:cd02953   1 EAALAQALAQGKPVFVDFTADWCVTCKvneKVVFSDPEVQAALKKDVVLLRADWtkNDPEITALLKRFGVFGPPTYLFYG 80


                ....*.
gi 42571269 105 KGSLEP 110
Cdd:cd02953  81 PGGEPE 86
mauD cd02967
Methylamine utilization (mau) D family; mauD protein is the translation product of the mauD ...
 163-218 4.27e-03

Methylamine utilization (mau) D family; mauD protein is the translation product of the mauD gene found in methylotrophic bacteria, which are able to use methylamine as a sole carbon source and a nitrogen source. mauD is an essential accessory protein for the biosynthesis of methylamine dehydrogenase (MADH), the enzyme that catalyzes the oxidation of methylamine and other primary amines. MADH possesses an alpha2beta2 subunit structure; the alpha subunit is also referred to as the large subunit. Each beta (small) subunit contains a tryptophan tryptophylquinone (TTQ) prosthetic group. Accessory proteins are essential for the proper transport of MADH to the periplasm, TTQ synthesis and the formation of several structural disulfide bonds. Bacterial mutants containing an insertion on the mauD gene were unable to grow on methylamine as a sole carbon source, were found to lack the MADH small subunit and had decreased amounts of the MADH large subunit.


Pssm-ID: 239265  Cd Length: 114  Bit Score: 36.22  E-value: 4.27e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571269 163 LVEFYAPWCGHCKSLAPTYEKVATVFKQEEGVVIA-NLDADAHKALGEKYGVSGFPT 218
Cdd:cd02967  25 LLFFLSPTCPVCKKLLPVIRSIARAEADWLDVVLAsDGEKAEHQRFLKKHGLEAFPY 81
TMX2 cd02962
TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related ...
 28-106 5.98e-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: 36.59  E-value: 5.98e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269  28 LTDDSFEKEV--GKDKGALVEFYAPWCGHCKKLAPEYEKLgaSFKKAKSVL-IAKVDCDEQKSVCTKYGVSGY------P 98
Cdd:cd02962  33 FTPKTLEEELerDKRVTWLVEFFTTWSPECVNFAPVFAEL--SLKYNNNNLkFGKIDIGRFPNVAEKFRVSTSplskqlP 110


                ....*...
gi 42571269  99 TIQWFPKG 106
Cdd:cd02962 111 TIILFQGG 118
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
56-247 7.44e-03

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 36.57  E-value: 7.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269    56 KKLAPEYEKLGASFKKAKSVLIAKvdcdeQKSVCTKYGVSgYPTIQWFPKGSLEPQKYEGP-RNAEALAEYVNKEggtnv 134
Cdd:pfam13848   6 SPLYEIFRKAAKELKGDVRFGITF-----SKEVADKYNIK-EPAILLFRKFDEETVHYPGDsINFEDLKKFIQKN----- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269   135 klaAVPqNVVVLTPDNFDEIVLDQNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKQEegVVIANLDADAHKALGEKYGVS 214
Cdd:pfam13848  75 ---CLP-LVREFTPENAEELFEEGIPPLLLLFLKKDDESTEEFKKALEKVAKKFRGK--INFALVDAKSFGRPLEYFGLS 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 42571269   215 G--FPTL----------KFFPKDNKaghdydggrDLDDFVSFINE 247
Cdd:pfam13848 149 EsdLPVIvivdsfshmyKYFPSDEF---------SPESLKEFIND 184
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 159-219 7.61e-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: 34.98  E-value: 7.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571269   159 NKDVLVEFYAPWCGHCKSLAPTYEKVATVFKQEEGVVIA--NLDADAH-----------------------KALGEKYGV 213
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLKKKKNVEIVfvSLDRDLEefkdylkkmpkdwlsvpfddderNELKRKYGV 80


                  ....*.
gi 42571269   214 SGFPTL 219
Cdd:pfam13905  81 NAIPTL 86
 
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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