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Conserved domains on  [gi|575771915|ref|NP_001276528|]
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thioredoxin domain-containing protein 5 isoform 3 [Mus musculus]

Protein Classification

thioredoxin family protein( domain architecture ID 10221583)

thioredoxin family protein may function as a thiol disulfide reductase that catalyzes the reduction of protein disulfide bonds using an active site dithiol present in a CXXC motif

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 103-203 4.54e-64

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: 198.28  E-value: 4.54e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 103 GLYELSANNFELHVSQGNHFIKFFAPWCGHCKALAPTWEQLALGLEH-SETVKIGKVDCTQHYAVCSEHQVRGYPTLLWF 181
Cdd:cd03005    1 GVLELTEDNFDHHIAEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFNNeNPSVKIAKVDCTQHRELCSEFQVRGYPTLLLF 80

                         90       100
                 ....*....|....*....|..
gi 575771915 182 RDGKKVDQYKGKRDLESLRDYV 203
Cdd:cd03005   81 KDGEKVDKYKGTRDLDSLKEFV 102
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 235-336 1.42e-61

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: 191.73  E-value: 1.42e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 235 TVLALTEKSFEDTIAQGITFVKFYAPWCGHCKNLAPTWEELSKKEFPGLSDVTIAEVDCTAERNVCSKYSVRGYPTLLLF 314
Cdd:cd03005    1 GVLELTEDNFDHHIAEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFNNENPSVKIAKVDCTQHRELCSEFQVRGYPTLLLF 80

                         90       100
                 ....*....|....*....|..
gi 575771915 315 RGGEKVGEHNGGRDLDSLHSFV 336
Cdd:cd03005   81 KDGEKVDKYKGTRDLDSLKEFV 102
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 2-77 1.32e-43

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


The actual alignment was detected with superfamily member cd03005:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 102  Bit Score: 145.89  E-value: 1.32e-43
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575771915   2 CGHCQRLQPTWNDLGDKYNSmEDAKVYVAKVDCTADSDVCSAQGVRGYPTLKFFKPGQEAVKYQGPRDFETLENWM 77
Cdd:cd03005   28 CGHCKRLAPTWEQLAKKFNN-ENPSVKIAKVDCTQHRELCSEFQVRGYPTLLLFKDGEKVDKYKGTRDLDSLKEFV 102
 
Name Accession Description Interval E-value
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 103-203 4.54e-64

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: 198.28  E-value: 4.54e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 103 GLYELSANNFELHVSQGNHFIKFFAPWCGHCKALAPTWEQLALGLEH-SETVKIGKVDCTQHYAVCSEHQVRGYPTLLWF 181
Cdd:cd03005    1 GVLELTEDNFDHHIAEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFNNeNPSVKIAKVDCTQHRELCSEFQVRGYPTLLLF 80

                         90       100
                 ....*....|....*....|..
gi 575771915 182 RDGKKVDQYKGKRDLESLRDYV 203
Cdd:cd03005   81 KDGEKVDKYKGTRDLDSLKEFV 102
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 235-336 1.42e-61

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: 191.73  E-value: 1.42e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 235 TVLALTEKSFEDTIAQGITFVKFYAPWCGHCKNLAPTWEELSKKEFPGLSDVTIAEVDCTAERNVCSKYSVRGYPTLLLF 314
Cdd:cd03005    1 GVLELTEDNFDHHIAEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFNNENPSVKIAKVDCTQHRELCSEFQVRGYPTLLLF 80

                         90       100
                 ....*....|....*....|..
gi 575771915 315 RGGEKVGEHNGGRDLDSLHSFV 336
Cdd:cd03005   81 KDGEKVDKYKGTRDLDSLKEFV 102
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 2-77 1.32e-43

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: 145.89  E-value: 1.32e-43
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575771915   2 CGHCQRLQPTWNDLGDKYNSmEDAKVYVAKVDCTADSDVCSAQGVRGYPTLKFFKPGQEAVKYQGPRDFETLENWM 77
Cdd:cd03005   28 CGHCKRLAPTWEQLAKKFNN-ENPSVKIAKVDCTQHRELCSEFQVRGYPTLLLFKDGEKVDKYKGTRDLDSLKEFV 102
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 239-340 1.43e-40

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: 137.80  E-value: 1.43e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915  239 LTEKSFEDTIAQG-ITFVKFYAPWCGHCKNLAPTWEELSkKEFPGLSDVTIAEVDCTAERNVCSKYSVRGYPTLLLFRGG 317
Cdd:TIGR01126   1 LTASNFDEIVLSNkDVLVEFYAPWCGHCKNLAPEYEKLA-KELKKDPKIVLAKVDATAEKDLASRFGVSGFPTIKFFPKG 79

                          90       100
                  ....*....|....*....|...
gi 575771915  318 EKVGEHNGGRDLDSLHSFVLRQA 340
Cdd:TIGR01126  80 SKPVDYEGGRDLEAIVEFVNEKS 102
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 2-344 1.63e-40

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: 147.90  E-value: 1.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915    2 CGHCQRLQPTWNDLGDKYnSMEDAKVYVAKVDCTADSDVCSAQGVRGYPTLKFFKPGQEAVK-YQGPRDFETLENWML-Q 79
Cdd:TIGR01130  30 CGHCKSLAPEYEKAADEL-KKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLKIFRNGEDSVSdYNGPRDADGIVKYMKkQ 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915   80 TLneePATPEPEAePPRAPELKQG-------------------LYELSANNFELHVSQG--------------------- 119
Cdd:TIGR01130 109 SG---PAVKEIET-VADLEAFLADddvvvigffkdldselndtFLSVAEKLRDVYFFFAhssdvaafaklgafpdsvvlf 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915  120 ------NHFIKF------------------FAPWCGH----------------------CKALAPTWEQLALGLEHSET- 152
Cdd:TIGR01130 185 kpkdedEKFSKVdgemdtdvsdlekfiraeSLPLVGEftqetaakyfesgplvvlyynvDESLDPFEELRNRFLEAAKKf 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915  153 ----VKIGKVDCTQHYAVCSEHQV--RGYPTLLWFrDGKKVDQYK---GKRDLESLRDYVQSQLQGseaapeTVEPSeap 223
Cdd:TIGR01130 265 rgkfVNFAVADEEDFGRELEYFGLkaEKFPAVAIQ-DLEGNKKYPmdqEEFSSENLEAFVKDFLDG------KLKPY--- 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915  224 VMAAE-PTGDKGTVLALTEKSFEDTI--AQGITFVKFYAPWCGHCKNLAPTWEELSKKEFPGLSDVTIAEVDCTAerNVC 300
Cdd:TIGR01130 335 LKSEPiPEDDEGPVKVLVGKNFDEIVldETKDVLVEFYAPWCGHCKNLAPIYEELAEKYKDAESDVVIAKMDATA--NDV 412

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 575771915  301 SKYSVRGYPTLLLFRGGEKVG--EHNGGRDLDSLHSFVLRQAKDEL 344
Cdd:TIGR01130 413 PPFEVEGFPTIKFVPAGKKSEpvPYDGDRTLEDFSKFIAKHATFPL 458
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 236-336 1.44e-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: 116.95  E-value: 1.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915  236 VLALTEKSFEDTIAQGITF--VKFYAPWCGHCKNLAPTWEELSKkEFPGlsDVTIAEVDCTAERNVCSKYSVRGYPTLLL 313
Cdd:pfam00085   2 VVVLTDANFDEVVQKSSKPvlVDFYAPWCGPCKMLAPEYEELAQ-EYKG--NVVFAKVDVDENPDLASKYGVRGYPTLIF 78

                          90       100
                  ....*....|....*....|...
gi 575771915  314 FRGGEKVGEHNGGRDLDSLHSFV 336
Cdd:pfam00085  79 FKNGQPVDDYVGARPKDALAAFL 101
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 106-203 2.68e-29

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: 108.47  E-value: 2.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915  106 ELSANNFELHVSQGN--HFIKFFAPWCGHCKALAPTWEQLALglEHSETVKIGKVDCTQHYAVCSEHQVRGYPTLLWFRD 183
Cdd:pfam00085   4 VLTDANFDEVVQKSSkpVLVDFYAPWCGPCKMLAPEYEELAQ--EYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKN 81

                          90       100
                  ....*....|....*....|
gi 575771915  184 GKKVDQYKGKRDLESLRDYV 203
Cdd:pfam00085  82 GQPVDDYVGARPKDALAAFL 101
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 235-336 4.23e-26

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: 99.89  E-value: 4.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 235 TVLALTEKSFEDTI--AQGITFVKFYAPWCGHCKNLAPTWEELSKkEFPGlsDVTIAEVDCTAERNVCSKYSVRGYPTLL 312
Cdd:COG3118    1 AVVELTDENFEEEVleSDKPVLVDFWAPWCGPCKMLAPVLEELAA-EYGG--KVKFVKVDVDENPELAAQFGVRSIPTLL 77

                         90       100
                 ....*....|....*....|....
gi 575771915 313 LFRGGEKVGEHNGGRDLDSLHSFV 336
Cdd:COG3118   78 LFKDGQPVDRFVGALPKEQLREFL 101
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 236-336 1.04e-25

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 107.14  E-value: 1.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 236 VLALTEKSFEDTIAQG-ITFVKFYAPWCGHCKNLAPTWEELSKKEFPGLSDVTIAEVDCTAERNVCSKYSVRGYPTLLLF 314
Cdd:PTZ00102  34 VTVLTDSTFDKFITENeIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSEIVLASVDATEEMELAQEFGVRGYPTIKFF 113

                         90       100
                 ....*....|....*....|..
gi 575771915 315 RGGEKVgEHNGGRDLDSLHSFV 336
Cdd:PTZ00102 114 NKGNPV-NYSGGRTADGIVSWI 134
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 106-207 1.85e-24

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: 95.66  E-value: 1.85e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 106 ELSANNFELHVSQGNH--FIKFFAPWCGHCKALAPTWEQLALglEHSETVKIGKVDCTQHYAVCSEHQVRGYPTLLWFRD 183
Cdd:COG3118    4 ELTDENFEEEVLESDKpvLVDFWAPWCGPCKMLAPVLEELAA--EYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLFKD 81

                         90       100
                 ....*....|....*....|....
gi 575771915 184 GKKVDQYKGKRDLESLRDYVQSQL 207
Cdd:COG3118   82 GQPVDRFVGALPKEQLREFLDKVL 105
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 2-77 4.12e-22

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: 89.21  E-value: 4.12e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575771915    2 CGHCQRLQPTWNDLGDKYnsmeDAKVYVAKVDCTADSDVCSAQGVRGYPTLKFFKPGQEAVKYQGPRDFETLENWM 77
Cdd:pfam00085  30 CGPCKMLAPEYEELAQEY----KGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKNGQPVDDYVGARPKDALAAFL 101
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 2-336 8.83e-22

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 95.59  E-value: 8.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915   2 CGHCQRLQPTWNDLGdKYNSMEDAKVYVAKVDCTADSDVCSAQGVRGYPTLKFFKPGQEaVKYQGPRDFETLENWMLQTL 81
Cdd:PTZ00102  61 CGHCKRLAPEYKKAA-KMLKEKKSEIVLASVDATEEMELAQEFGVRGYPTIKFFNKGNP-VNYSGGRTADGIVSWIKKLT 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915  82 NeePATPE---PEAEPPRAPELKQGLY-ELSANNFELH-----VSQGNHFI-KFFA-PWCGHCKALAPTWEQ----LALG 146
Cdd:PTZ00102 139 G--PAVTEvesASEIKLIAKKIFVAFYgEYTSKDSELYkkfeeVADKHREHaKFFVkKHEGKNKIYVLHKDEegveLFMG 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 147 LEHSETVKIGKVDCTQHYAVCSEHQVRGYPT----LLWFRDGKK-VDQYKG-----KRDLESLRDYV------------- 203
Cdd:PTZ00102 217 KTKEELEEFVSTESFPLFAEINAENYRRYISsgkdLVWFCGTTEdYDKYKSvvrkvARKLREKYAFVwldteqfgshake 296

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 204 ------------QSQ-----LQGSEAAPETVEP------------------SEapvmaAEPTGDKGTVLALTEKSFEDTI 248
Cdd:PTZ00102 297 hllieefpglayQSPagrylLPPAKESFDSVEAlieffkdveagkveksikSE-----PIPEEQDGPVKVVVGNTFEEIV 371

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 249 AQGITFV--KFYAPWCGHCKNLAPTWEELSKKefpgLSD---VTIAEVDCTAERNVCSKYSVRGYPTLLLFRGGEKVG-E 322
Cdd:PTZ00102 372 FKSDKDVllEIYAPWCGHCKNLEPVYNELGEK----YKDndsIIVAKMNGTANETPLEEFSWSAFPTILFVKAGERTPiP 447

                        410
                 ....*....|....
gi 575771915 323 HNGGRDLDSLHSFV 336
Cdd:PTZ00102 448 YEGERTVEGFKEFV 461
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 2-77 1.44e-11

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: 60.22  E-value: 1.44e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575771915   2 CGHCQRLQPTWNDLGDKYNSmedaKVYVAKVDCTADSDVCSAQGVRGYPTLKFFKPGQEAVKYQGPRDFETLENWM 77
Cdd:COG3118   30 CGPCKMLAPVLEELAAEYGG----KVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQPVDRFVGALPKEQLREFL 101
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 2-81 5.65e-09

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


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 53.06  E-value: 5.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915    2 CGHCQRLQPTWNDLGDKYNSmedaKVYVAKVDCTADSDVCSAQGVRGYPTLKFFKPGQEAVKYQGPRDFETLENWMLQTL 81
Cdd:TIGR01068  26 CGPCKMIAPILEELAKEYEG----KVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKEVDRSVGALPKAALKQLINKNL 101
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 2-91 3.92e-06

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 47.31  E-value: 3.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915   2 CGHCQRLQPTWNDLGDKYNsmedAKVYVAKVDCTADSDVCSAQGVRGYPTLKFFKPGQEAVKYQGPRDFETLENWMLQTL 81
Cdd:PTZ00443  64 CSHCRKMAPAWERLAKALK----GQVNVADLDATRALNLAKRFAIKGYPTLLLFDKGKMYQYEGGDRSTEKLAAFALGDF 139

                         90
                 ....*....|
gi 575771915  82 NEEPATPEPE 91
Cdd:PTZ00443 140 KKALGAPVPA 149
 
Name Accession Description Interval E-value
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 103-203 4.54e-64

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: 198.28  E-value: 4.54e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 103 GLYELSANNFELHVSQGNHFIKFFAPWCGHCKALAPTWEQLALGLEH-SETVKIGKVDCTQHYAVCSEHQVRGYPTLLWF 181
Cdd:cd03005    1 GVLELTEDNFDHHIAEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFNNeNPSVKIAKVDCTQHRELCSEFQVRGYPTLLLF 80

                         90       100
                 ....*....|....*....|..
gi 575771915 182 RDGKKVDQYKGKRDLESLRDYV 203
Cdd:cd03005   81 KDGEKVDKYKGTRDLDSLKEFV 102
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 235-336 1.42e-61

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: 191.73  E-value: 1.42e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 235 TVLALTEKSFEDTIAQGITFVKFYAPWCGHCKNLAPTWEELSKKEFPGLSDVTIAEVDCTAERNVCSKYSVRGYPTLLLF 314
Cdd:cd03005    1 GVLELTEDNFDHHIAEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFNNENPSVKIAKVDCTQHRELCSEFQVRGYPTLLLF 80

                         90       100
                 ....*....|....*....|..
gi 575771915 315 RGGEKVGEHNGGRDLDSLHSFV 336
Cdd:cd03005   81 KDGEKVDKYKGTRDLDSLKEFV 102
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 2-77 1.32e-43

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: 145.89  E-value: 1.32e-43
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575771915   2 CGHCQRLQPTWNDLGDKYNSmEDAKVYVAKVDCTADSDVCSAQGVRGYPTLKFFKPGQEAVKYQGPRDFETLENWM 77
Cdd:cd03005   28 CGHCKRLAPTWEQLAKKFNN-ENPSVKIAKVDCTQHRELCSEFQVRGYPTLLLFKDGEKVDKYKGTRDLDSLKEFV 102
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 106-203 1.59e-41

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: 140.44  E-value: 1.59e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 106 ELSANNFELHVSQGNH-FIKFFAPWCGHCKALAPTWEQLALGLEHSETVKIGKVDCTQHYAVCSEHQVRGYPTLLWFRDG 184
Cdd:cd02961    2 ELTDDNFDELVKDSKDvLVEFYAPWCGHCKALAPEYEKLAKELKGDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPNG 81

                         90       100
                 ....*....|....*....|
gi 575771915 185 -KKVDQYKGKRDLESLRDYV 203
Cdd:cd02961   82 sKEPVKYEGPRTLESLVEFI 101
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 239-340 1.43e-40

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: 137.80  E-value: 1.43e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915  239 LTEKSFEDTIAQG-ITFVKFYAPWCGHCKNLAPTWEELSkKEFPGLSDVTIAEVDCTAERNVCSKYSVRGYPTLLLFRGG 317
Cdd:TIGR01126   1 LTASNFDEIVLSNkDVLVEFYAPWCGHCKNLAPEYEKLA-KELKKDPKIVLAKVDATAEKDLASRFGVSGFPTIKFFPKG 79

                          90       100
                  ....*....|....*....|...
gi 575771915  318 EKVGEHNGGRDLDSLHSFVLRQA 340
Cdd:TIGR01126  80 SKPVDYEGGRDLEAIVEFVNEKS 102
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 2-344 1.63e-40

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: 147.90  E-value: 1.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915    2 CGHCQRLQPTWNDLGDKYnSMEDAKVYVAKVDCTADSDVCSAQGVRGYPTLKFFKPGQEAVK-YQGPRDFETLENWML-Q 79
Cdd:TIGR01130  30 CGHCKSLAPEYEKAADEL-KKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLKIFRNGEDSVSdYNGPRDADGIVKYMKkQ 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915   80 TLneePATPEPEAePPRAPELKQG-------------------LYELSANNFELHVSQG--------------------- 119
Cdd:TIGR01130 109 SG---PAVKEIET-VADLEAFLADddvvvigffkdldselndtFLSVAEKLRDVYFFFAhssdvaafaklgafpdsvvlf 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915  120 ------NHFIKF------------------FAPWCGH----------------------CKALAPTWEQLALGLEHSET- 152
Cdd:TIGR01130 185 kpkdedEKFSKVdgemdtdvsdlekfiraeSLPLVGEftqetaakyfesgplvvlyynvDESLDPFEELRNRFLEAAKKf 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915  153 ----VKIGKVDCTQHYAVCSEHQV--RGYPTLLWFrDGKKVDQYK---GKRDLESLRDYVQSQLQGseaapeTVEPSeap 223
Cdd:TIGR01130 265 rgkfVNFAVADEEDFGRELEYFGLkaEKFPAVAIQ-DLEGNKKYPmdqEEFSSENLEAFVKDFLDG------KLKPY--- 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915  224 VMAAE-PTGDKGTVLALTEKSFEDTI--AQGITFVKFYAPWCGHCKNLAPTWEELSKKEFPGLSDVTIAEVDCTAerNVC 300
Cdd:TIGR01130 335 LKSEPiPEDDEGPVKVLVGKNFDEIVldETKDVLVEFYAPWCGHCKNLAPIYEELAEKYKDAESDVVIAKMDATA--NDV 412

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 575771915  301 SKYSVRGYPTLLLFRGGEKVG--EHNGGRDLDSLHSFVLRQAKDEL 344
Cdd:TIGR01130 413 PPFEVEGFPTIKFVPAGKKSEpvPYDGDRTLEDFSKFIAKHATFPL 458
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 239-336 3.64e-40

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: 136.59  E-value: 3.64e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 239 LTEKSFEDTIAQG-ITFVKFYAPWCGHCKNLAPTWEELSKKeFPGLSDVTIAEVDCTAERNVCSKYSVRGYPTLLLFRGG 317
Cdd:cd02961    3 LTDDNFDELVKDSkDVLVEFYAPWCGHCKALAPEYEKLAKE-LKGDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPNG 81

                         90       100
                 ....*....|....*....|
gi 575771915 318 -EKVGEHNGGRDLDSLHSFV 336
Cdd:cd02961   82 sKEPVKYEGPRTLESLVEFI 101
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 107-206 1.31e-38

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: 132.80  E-value: 1.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915  107 LSANNFELHVSQGNH-FIKFFAPWCGHCKALAPTWEQLALGLEHSETVKIGKVDCTQHYAVCSEHQVRGYPTLLWFRDGK 185
Cdd:TIGR01126   1 LTASNFDEIVLSNKDvLVEFYAPWCGHCKNLAPEYEKLAKELKKDPKIVLAKVDATAEKDLASRFGVSGFPTIKFFPKGS 80

                          90       100
                  ....*....|....*....|.
gi 575771915  186 KVDQYKGKRDLESLRDYVQSQ 206
Cdd:TIGR01126  81 KPVDYEGGRDLEAIVEFVNEK 101
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 236-336 3.99e-36

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: 126.60  E-value: 3.99e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 236 VLALTEKSFEDTIAQGI--TFVKFYAPWCGHCKNLAPTWEELSkKEFPGLSDVTIAEVDCTAE-RNVCSKYSVRGYPTLL 312
Cdd:cd02998    2 VVELTDSNFDKVVGDDKkdVLVEFYAPWCGHCKNLAPEYEKLA-AVFANEDDVVIAKVDADEAnKDLAKKYGVSGFPTLK 80

                         90       100
                 ....*....|....*....|....*
gi 575771915 313 LFRGGEKVGE-HNGGRDLDSLHSFV 336
Cdd:cd02998   81 FFPKGSTEPVkYEGGRDLEDLVKFV 105
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 236-340 3.12e-34

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: 130.56  E-value: 3.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915  236 VLALTEKSFEDTIAQG-ITFVKFYAPWCGHCKNLAPTWE----ELSKKEfpglSDVTIAEVDCTAERNVCSKYSVRGYPT 310
Cdd:TIGR01130   3 VLVLTKDNFDDFIKSHeFVLVEFYAPWCGHCKSLAPEYEkaadELKKKG----PPIKLAKVDATEEKDLAQKYGVSGYPT 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 575771915  311 LLLFRGGEK-VGEHNGGRDLDSLHSFVLRQA 340
Cdd:TIGR01130  79 LKIFRNGEDsVSDYNGPRDADGIVKYMKKQS 109
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 236-336 1.44e-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: 116.95  E-value: 1.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915  236 VLALTEKSFEDTIAQGITF--VKFYAPWCGHCKNLAPTWEELSKkEFPGlsDVTIAEVDCTAERNVCSKYSVRGYPTLLL 313
Cdd:pfam00085   2 VVVLTDANFDEVVQKSSKPvlVDFYAPWCGPCKMLAPEYEELAQ-EYKG--NVVFAKVDVDENPDLASKYGVRGYPTLIF 78

                          90       100
                  ....*....|....*....|...
gi 575771915  314 FRGGEKVGEHNGGRDLDSLHSFV 336
Cdd:pfam00085  79 FKNGQPVDDYVGARPKDALAAFL 101
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 106-203 4.04e-32

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: 115.81  E-value: 4.04e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 106 ELSANNFELHV--SQGNHFIKFFAPWCGHCKALAPTWEQLALGLEHSETVKIGKVDCTQ-HYAVCSEHQVRGYPTLLWF- 181
Cdd:cd02998    4 ELTDSNFDKVVgdDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFANEDDVVIAKVDADEaNKDLAKKYGVSGFPTLKFFp 83

                         90       100
                 ....*....|....*....|..
gi 575771915 182 RDGKKVDQYKGKRDLESLRDYV 203
Cdd:cd02998   84 KGSTEPVKYEGGRDLEDLVKFV 105
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 106-222 1.13e-31

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: 123.63  E-value: 1.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915  106 ELSANNFELHVSQGNHFI-KFFAPWCGHCKALAPTWEQLALGL-EHSETVKIGKVDCTQHYAVCSEHQVRGYPTLLWFRD 183
Cdd:TIGR01130   5 VLTKDNFDDFIKSHEFVLvEFYAPWCGHCKSLAPEYEKAADELkKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLKIFRN 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 575771915  184 GKKVDQ-YKGKRDLESLRDYVQSQLQGSEAAPETVEPSEA 222
Cdd:TIGR01130  85 GEDSVSdYNGPRDADGIVKYMKKQSGPAVKEIETVADLEA 124
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 106-203 2.68e-29

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: 108.47  E-value: 2.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915  106 ELSANNFELHVSQGN--HFIKFFAPWCGHCKALAPTWEQLALglEHSETVKIGKVDCTQHYAVCSEHQVRGYPTLLWFRD 183
Cdd:pfam00085   4 VLTDANFDEVVQKSSkpVLVDFYAPWCGPCKMLAPEYEELAQ--EYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKN 81

                          90       100
                  ....*....|....*....|
gi 575771915  184 GKKVDQYKGKRDLESLRDYV 203
Cdd:pfam00085  82 GQPVDDYVGARPKDALAAFL 101
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 2-77 9.05e-29

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


Pssm-ID: 239259 [Multi-domain]  Cd Length: 101  Bit Score: 106.93  E-value: 9.05e-29
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575771915   2 CGHCQRLQPTWNDLGDKYNsmEDAKVYVAKVDCTADSDVCSAQGVRGYPTLKFFKPG-QEAVKYQGPRDFETLENWM 77
Cdd:cd02961   27 CGHCKALAPEYEKLAKELK--GDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPNGsKEPVKYEGPRTLESLVEFI 101
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 239-336 3.65e-27

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: 102.63  E-value: 3.65e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 239 LTEKSFEDTIAQGI--TFVKFYAPWCGHCKNLAPTWEELSKKeFPGLSDVTIAEVDCTAerN-VCSKYSVRGYPTLLLFR 315
Cdd:cd02995    5 VVGKNFDEVVLDSDkdVLVEFYAPWCGHCKALAPIYEELAEK-LKGDDNVVIAKMDATA--NdVPSEFVVDGFPTILFFP 81

                         90       100
                 ....*....|....*....|...
gi 575771915 316 GGEK--VGEHNGGRDLDSLHSFV 336
Cdd:cd02995   82 AGDKsnPIKYEGDRTLEDLIKFI 104
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 235-336 4.23e-26

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: 99.89  E-value: 4.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 235 TVLALTEKSFEDTI--AQGITFVKFYAPWCGHCKNLAPTWEELSKkEFPGlsDVTIAEVDCTAERNVCSKYSVRGYPTLL 312
Cdd:COG3118    1 AVVELTDENFEEEVleSDKPVLVDFWAPWCGPCKMLAPVLEELAA-EYGG--KVKFVKVDVDENPELAAQFGVRSIPTLL 77

                         90       100
                 ....*....|....*....|....
gi 575771915 313 LFRGGEKVGEHNGGRDLDSLHSFV 336
Cdd:COG3118   78 LFKDGQPVDRFVGALPKEQLREFL 101
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 105-203 4.29e-26

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: 99.94  E-value: 4.29e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 105 YELSANNFELHVSQG--NHFIKFFAPWCGHCKALAPTWEQLALGLEHSETVKIGKVDCTQHYaVCSEHQVRGYPTLLWFR 182
Cdd:cd02995    3 KVVVGKNFDEVVLDSdkDVLVEFYAPWCGHCKALAPIYEELAEKLKGDDNVVIAKMDATAND-VPSEFVVDGFPTILFFP 81

                         90       100
                 ....*....|....*....|...
gi 575771915 183 DGKKVD--QYKGKRDLESLRDYV 203
Cdd:cd02995   82 AGDKSNpiKYEGDRTLEDLIKFI 104
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 236-337 6.24e-26

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: 99.74  E-value: 6.24e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 236 VLALTEKSFEDTIAQG--ITFVKFYAPWCGHCKNLAPTWEELSkKEFPGLSDVtiAEVDCTAERN--VCSKYSVRGYPTL 311
Cdd:cd03002    2 VYELTPKNFDKVVHNTnyTTLVEFYAPWCGHCKNLKPEYAKAA-KELDGLVQV--AAVDCDEDKNkpLCGKYGVQGFPTL 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 575771915 312 LLFRGGEKVGEH-----NGGRDLDSLHSFVL 337
Cdd:cd03002   79 KVFRPPKKASKHavedyNGERSAKAIVDFVL 109
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 236-336 1.04e-25

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 107.14  E-value: 1.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 236 VLALTEKSFEDTIAQG-ITFVKFYAPWCGHCKNLAPTWEELSKKEFPGLSDVTIAEVDCTAERNVCSKYSVRGYPTLLLF 314
Cdd:PTZ00102  34 VTVLTDSTFDKFITENeIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSEIVLASVDATEEMELAQEFGVRGYPTIKFF 113

                         90       100
                 ....*....|....*....|..
gi 575771915 315 RGGEKVgEHNGGRDLDSLHSFV 336
Cdd:PTZ00102 114 NKGNPV-NYSGGRTADGIVSWI 134
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 106-201 3.58e-25

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: 97.36  E-value: 3.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 106 ELSANNFELHVSQGNH--FIKFFAPWCGHCKALAPTWEQLALGLEhsETVKIGKVDCTQHYAVCSEHQVRGYPTLLWFRD 183
Cdd:cd03001    4 ELTDSNFDKKVLNSDDvwLVEFYAPWCGHCKNLAPEWKKAAKALK--GIVKVGAVDADVHQSLAQQYGVRGFPTIKVFGA 81

                         90
                 ....*....|....*....
gi 575771915 184 GKKVDQ-YKGKRDLESLRD 201
Cdd:cd03001   82 GKNSPQdYQGGRTAKAIVS 100
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 236-337 5.48e-25

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: 96.97  E-value: 5.48e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 236 VLALTEKSFEDTIAQ--GITFVKFYAPWCGHCKNLAPTWEELSkKEFPGLsdVTIAEVDCTAERNVCSKYSVRGYPTLLL 313
Cdd:cd03001    2 VVELTDSNFDKKVLNsdDVWLVEFYAPWCGHCKNLAPEWKKAA-KALKGI--VKVGAVDADVHQSLAQQYGVRGFPTIKV 78

                         90       100
                 ....*....|....*....|....*
gi 575771915 314 FRGG-EKVGEHNGGRDLDSLHSFVL 337
Cdd:cd03001   79 FGAGkNSPQDYQGGRTAKAIVSAAL 103
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 232-344 1.54e-24

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 99.70  E-value: 1.54e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 232 DKGTVLALTEKSFEDTI------AQGITFVKFYAPWCGHCKNLAPTWEELSkKEFPGLsdVTIAEVDCTAERNVCSKYSV 305
Cdd:PTZ00443  28 DANALVLLNDKNFEKLTqastgaTTGPWFVKFYAPWCSHCRKMAPAWERLA-KALKGQ--VNVADLDATRALNLAKRFAI 104

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 575771915 306 RGYPTLLLFRGGEKVGEHNGGRDLDSLHSFVLRQAKDEL 344
Cdd:PTZ00443 105 KGYPTLLLFDKGKMYQYEGGDRSTEKLAAFALGDFKKAL 143
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 106-207 1.85e-24

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: 95.66  E-value: 1.85e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 106 ELSANNFELHVSQGNH--FIKFFAPWCGHCKALAPTWEQLALglEHSETVKIGKVDCTQHYAVCSEHQVRGYPTLLWFRD 183
Cdd:COG3118    4 ELTDENFEEEVLESDKpvLVDFWAPWCGPCKMLAPVLEELAA--EYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLFKD 81

                         90       100
                 ....*....|....*....|....
gi 575771915 184 GKKVDQYKGKRDLESLRDYVQSQL 207
Cdd:COG3118   82 GQPVDRFVGALPKEQLREFLDKVL 105
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 106-203 2.90e-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: 95.05  E-value: 2.90e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 106 ELSANNFELHVSQGNHF--IKFFAPWCGHCKALAPTWEQLALGLEHseTVKIGKVDCTQHYAVCSEHQVRGYPTL-LWFR 182
Cdd:cd03004    5 TLTPEDFPELVLNRKEPwlVDFYAPWCGPCQALLPELRKAARALKG--KVKVGSVDCQKYESLCQQANIRAYPTIrLYPG 82

                         90       100
                 ....*....|....*....|..
gi 575771915 183 DGKKVDQYKG-KRDLESLRDYV 203
Cdd:cd03004   83 NASKYHSYNGwHRDADSILEFI 104
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 236-340 1.20e-23

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: 93.67  E-value: 1.20e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 236 VLALTEKsFEDTIAQGITFVKFYAPWCGHCKNLAPTWEELSKKEFPGLSDVTIAEVDCTAERNVCSKYSVRGYPTLLLFR 315
Cdd:cd03000    2 VLDLDDS-FKDVRKEDIWLVDFYAPWCGHCKKLEPVWNEVGAELKSSGSPVRVGKLDATAYSSIASEFGVRGYPTIKLLK 80

                         90       100
                 ....*....|....*....|....*
gi 575771915 316 GGEKVgEHNGGRDLDSLHSFVLRQA 340
Cdd:cd03000   81 GDLAY-NYRGPRTKDDIVEFANRVA 104
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 242-336 5.61e-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: 91.47  E-value: 5.61e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 242 KSFEDTIAQ-GITFVKFYAPWCGHCKNLAPTWEELSKKEfpglSDVTIAEVDCTAERNVCSKYSVRGYPTLLLFRGGEKV 320
Cdd:cd02947    1 EEFEELIKSaKPVVVDFWAPWCGPCKAIAPVLEELAEEY----PKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEV 76

                         90
                 ....*....|....*.
gi 575771915 321 GEHNGGRDLDSLHSFV 336
Cdd:cd02947   77 DRVVGADPKEELEEFL 92
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 105-203 6.26e-23

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: 91.65  E-value: 6.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 105 YELSANNF--ELHVSQGNHFIKFFAPWCGHCKALAPTWEQLALGLehSETVKIGKVDCTQ--HYAVCSEHQVRGYPTLLW 180
Cdd:cd03002    3 YELTPKNFdkVVHNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKEL--DGLVQVAAVDCDEdkNKPLCGKYGVQGFPTLKV 80

                         90       100
                 ....*....|....*....|....*...
gi 575771915 181 FRDGKKVDQ-----YKGKRDLESLRDYV 203
Cdd:cd03002   81 FRPPKKASKhavedYNGERSAKAIVDFV 108
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 239-336 9.01e-23

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: 91.20  E-value: 9.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915  239 LTEKSFEDTIAQG--ITFVKFYAPWCGHCKNLAPTWEELSKKEFpglSDVTIAEVDCTAERNVCSKYSVRGYPTLLLFRG 316
Cdd:TIGR01068   1 LTDANFDETIASSdkPVLVDFWAPWCGPCKMIAPILEELAKEYE---GKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKN 77

                          90       100
                  ....*....|....*....|
gi 575771915  317 GEKVGEHNGGRDLDSLHSFV 336
Cdd:TIGR01068  78 GKEVDRSVGALPKAALKQLI 97
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 2-77 4.12e-22

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: 89.21  E-value: 4.12e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575771915    2 CGHCQRLQPTWNDLGDKYnsmeDAKVYVAKVDCTADSDVCSAQGVRGYPTLKFFKPGQEAVKYQGPRDFETLENWM 77
Cdd:pfam00085  30 CGPCKMLAPEYEELAQEY----KGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKNGQPVDDYVGARPKDALAAFL 101
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 122-202 6.59e-22

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: 88.67  E-value: 6.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 122 FIKFFAPWCGHCKALAPTWEQLALGLEHSET-VKIGKVDCTQHYAVCSEHQVRGYPTLLWFRDGKKVDqYKGKRDLESLR 200
Cdd:cd03000   19 LVDFYAPWCGHCKKLEPVWNEVGAELKSSGSpVRVGKLDATAYSSIASEFGVRGYPTIKLLKGDLAYN-YRGPRTKDDIV 97


                 ..
gi 575771915 201 DY 202
Cdd:cd03000   98 EF 99
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 2-336 8.83e-22

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 95.59  E-value: 8.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915   2 CGHCQRLQPTWNDLGdKYNSMEDAKVYVAKVDCTADSDVCSAQGVRGYPTLKFFKPGQEaVKYQGPRDFETLENWMLQTL 81
Cdd:PTZ00102  61 CGHCKRLAPEYKKAA-KMLKEKKSEIVLASVDATEEMELAQEFGVRGYPTIKFFNKGNP-VNYSGGRTADGIVSWIKKLT 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915  82 NeePATPE---PEAEPPRAPELKQGLY-ELSANNFELH-----VSQGNHFI-KFFA-PWCGHCKALAPTWEQ----LALG 146
Cdd:PTZ00102 139 G--PAVTEvesASEIKLIAKKIFVAFYgEYTSKDSELYkkfeeVADKHREHaKFFVkKHEGKNKIYVLHKDEegveLFMG 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 147 LEHSETVKIGKVDCTQHYAVCSEHQVRGYPT----LLWFRDGKK-VDQYKG-----KRDLESLRDYV------------- 203
Cdd:PTZ00102 217 KTKEELEEFVSTESFPLFAEINAENYRRYISsgkdLVWFCGTTEdYDKYKSvvrkvARKLREKYAFVwldteqfgshake 296

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 204 ------------QSQ-----LQGSEAAPETVEP------------------SEapvmaAEPTGDKGTVLALTEKSFEDTI 248
Cdd:PTZ00102 297 hllieefpglayQSPagrylLPPAKESFDSVEAlieffkdveagkveksikSE-----PIPEEQDGPVKVVVGNTFEEIV 371

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 249 AQGITFV--KFYAPWCGHCKNLAPTWEELSKKefpgLSD---VTIAEVDCTAERNVCSKYSVRGYPTLLLFRGGEKVG-E 322
Cdd:PTZ00102 372 FKSDKDVllEIYAPWCGHCKNLEPVYNELGEK----YKDndsIIVAKMNGTANETPLEEFSWSAFPTILFVKAGERTPiP 447

                        410
                 ....*....|....
gi 575771915 323 HNGGRDLDSLHSFV 336
Cdd:PTZ00102 448 YEGERTVEGFKEFV 461
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 106-228 2.33e-21

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 94.43  E-value: 2.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 106 ELSANNFELHVSQGNH-FIKFFAPWCGHCKALAPTWEQLALGL-EHSETVKIGKVDCTQHYAVCSEHQVRGYPTLLWFRD 183
Cdd:PTZ00102  36 VLTDSTFDKFITENEIvLVKFYAPWCGHCKRLAPEYKKAAKMLkEKKSEIVLASVDATEEMELAQEFGVRGYPTIKFFNK 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 575771915 184 GKKVDqYKGKRDLESLRDYVQsQLQGSeAAPETVEPSEAPVMAAE 228
Cdd:PTZ00102 116 GNPVN-YSGGRTADGIVSWIK-KLTGP-AVTEVESASEIKLIAKK 157
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 236-315 8.99e-21

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: 86.17  E-value: 8.99e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 236 VLALTEKSFEDTI--AQGITFVKFYAPWCGHCKNLAPTWEELSK--KEFPGLsdVTIAEVDCTAERN--VCSKYSVRGYP 309
Cdd:cd02992    3 VIVLDAASFNSALlgSPSAWLVEFYASWCGHCRAFAPTWKKLARdlRKWRPV--VRVAAVDCADEENvaLCRDFGVTGYP 80


                 ....*.
gi 575771915 310 TLLLFR 315
Cdd:cd02992   81 TLRYFP 86
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 106-202 3.20e-20

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: 84.63  E-value: 3.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 106 ELSANNFE--LHVSQGNHFIKFFAPWCGHCKALAPTWEQLA-LGLEHSETVKIGKVDCTQ--HYAVCSEHQVRGYPTLLW 180
Cdd:cd02992    5 VLDAASFNsaLLGSPSAWLVEFYASWCGHCRAFAPTWKKLArDLRKWRPVVRVAAVDCADeeNVALCRDFGVTGYPTLRY 84

                         90       100
                 ....*....|....*....|....*..
gi 575771915 181 F----RDGKKVDQYKG-KRDLESLRDY 202
Cdd:cd02992   85 FppfsKEATDGLKQEGpERDVNELREA 111
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 111-204 3.49e-20

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: 83.76  E-value: 3.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 111 NFELHVSQ-GNHFIKFFAPWCGHCKALAPTWEQLAlglEHSETVKIGKVDCTQHYAVCSEHQVRGYPTLLWFRDGKKVDQ 189
Cdd:cd02947    2 EFEELIKSaKPVVVDFWAPWCGPCKAIAPVLEELA---EEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDR 78

                         90
                 ....*....|....*
gi 575771915 190 YKGKRDLESLRDYVQ 204
Cdd:cd02947   79 VVGADPKEELEEFLE 93
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 2-76 5.08e-20

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: 83.84  E-value: 5.08e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575771915   2 CGHCQRLQPTWNDLGDKYNSmeDAKVYVAKVDCTAD-SDVCSAQGVRGYPTLKFFKPG-QEAVKYQGPRDFETLENW 76
Cdd:cd02998   30 CGHCKNLAPEYEKLAAVFAN--EDDVVIAKVDADEAnKDLAKKYGVSGFPTLKFFPKGsTEPVKYEGGRDLEDLVKF 104
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 99-214 9.57e-20

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 86.60  E-value: 9.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915  99 ELKQGLYELSANNFE------LHVSQGNHFIKFFAPWCGHCKALAPTWEQLALGLEHseTVKIGKVDCTQHYAVCSEHQV 172
Cdd:PTZ00443  27 EDANALVLLNDKNFEkltqasTGATTGPWFVKFYAPWCSHCRKMAPAWERLAKALKG--QVNVADLDATRALNLAKRFAI 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 575771915 173 RGYPTLLWFRDGkKVDQYK-GKRDLESLRDYVQSQLQGSEAAP 214
Cdd:PTZ00443 105 KGYPTLLLFDKG-KMYQYEgGDRSTEKLAAFALGDFKKALGAP 146
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 236-336 1.62e-19

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


Pssm-ID: 239302 [Multi-domain]  Cd Length: 104  Bit Score: 82.34  E-value: 1.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 236 VLALTEKSFEDTIAQG--ITFVKFYAPWCGHCKNLAPTWEELSKKEFPglsDVTIAEVDCTAERNVCSKYSVRGYPTLLL 313
Cdd:cd03004    3 VITLTPEDFPELVLNRkePWLVDFYAPWCGPCQALLPELRKAARALKG---KVKVGSVDCQKYESLCQQANIRAYPTIRL 79

                         90       100
                 ....*....|....*....|....*
gi 575771915 314 FRGGE-KVGEHNG-GRDLDSLHSFV 336
Cdd:cd03004   80 YPGNAsKYHSYNGwHRDADSILEFI 104
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 107-207 3.71e-19

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: 81.18  E-value: 3.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915  107 LSANNFELHVSQGNH--FIKFFAPWCGHCKALAPTWEQLALGLEHSetVKIGKVDCTQHYAVCSEHQVRGYPTLLWFRDG 184
Cdd:TIGR01068   1 LTDANFDETIASSDKpvLVDFWAPWCGPCKMIAPILEELAKEYEGK--VKFVKLNVDENPDIAAKYGIRSIPTLLLFKNG 78

                          90       100
                  ....*....|....*....|...
gi 575771915  185 KKVDQYKGKRDLESLRDYVQSQL 207
Cdd:TIGR01068  79 KEVDRSVGALPKAALKQLINKNL 101
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 2-77 5.25e-19

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: 81.06  E-value: 5.25e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 575771915   2 CGHCQRLQPTWNDLGDKYNSMEDakVYVAKVDCTADsDVCSAQGVRGYPTLKFFKPG--QEAVKYQGPRDFETLENWM 77
Cdd:cd02995   30 CGHCKALAPIYEELAEKLKGDDN--VVIAKMDATAN-DVPSEFVVDGFPTILFFPAGdkSNPIKYEGDRTLEDLIKFI 104
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 234-336 1.58e-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: 79.74  E-value: 1.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 234 GTVLALTEKSFEDTI-AQGITFVKFYAPWCGHCKNLAPTWEELS---KKEFPGLSDVTIAEVDCTAERNVCSKYSVRGYP 309
Cdd:cd02996    1 SEIVSLTSGNIDDILqSAELVLVNFYADWCRFSQMLHPIFEEAAakiKEEFPDAGKVVWGKVDCDKESDIADRYRINKYP 80

                         90       100
                 ....*....|....*....|....*...
gi 575771915 310 TLLLFRGGEKVG-EHNGGRDLDSLHSFV 336
Cdd:cd02996   81 TLKLFRNGMMMKrEYRGQRSVEALAEFV 108
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 107-202 7.35e-18

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: 77.95  E-value: 7.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 107 LSANNFELHVSQGN-HFIKFFAPWCGHCKALAPTWEQLALGLEHseTVKIGKVDCTQHYAVCSEHQVRGYPTLLWFRDGK 185
Cdd:cd03003    6 LDRGDFDAAVNSGEiWFVNFYSPRCSHCHDLAPTWREFAKEMDG--VIRIGAVNCGDDRMLCRSQGVNSYPSLYVFPSGM 83

                         90
                 ....*....|....*..
gi 575771915 186 KVDQYKGKRDLESLRDY 202
Cdd:cd03003   84 NPEKYYGDRSKESLVKF 100
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 236-335 1.46e-17

PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a protein containing an N-terminal DnaJ domain and four redox active TRX domains. This subfamily is comprised of the first TRX domain of ERdj5 located after the DnaJ domain at the N-terminal half of the protein. ERdj5 is a ubiquitous protein localized in the endoplasmic reticulum (ER) and is abundant in secretory cells. It's transcription is induced during ER stress. It interacts with BiP through its DnaJ domain in an ATP-dependent manner. BiP, an ER-resident member of the Hsp70 chaperone family, functions in ER-associated degradation and protein translocation.


Pssm-ID: 239301 [Multi-domain]  Cd Length: 101  Bit Score: 76.79  E-value: 1.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 236 VLALTEKSFEDTIAQG-ITFVKFYAPWCGHCKNLAPTWEELSkKEFPGLsdVTIAEVDCTAERNVCSKYSVRGYPTLLLF 314
Cdd:cd03003    3 IVTLDRGDFDAAVNSGeIWFVNFYSPRCSHCHDLAPTWREFA-KEMDGV--IRIGAVNCGDDRMLCRSQGVNSYPSLYVF 79

                         90       100
                 ....*....|....*....|.
gi 575771915 315 RGGEKVGEHNGGRDLDSLHSF 335
Cdd:cd03003   80 PSGMNPEKYYGDRSKESLVKF 100
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 236-327 1.13e-16

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: 74.66  E-value: 1.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 236 VLALTEKSFEDTIAQGI-TFVKFYAPWCGHCKNLAPTWEELSkKEFPGLSDVTIAEVDCTAERN--VCSKYSVRGYPTLL 312
Cdd:cd02997    2 VVHLTDEDFRKFLKKEKhVLVMFYAPWCGHCKKMKPEFTKAA-TELKEDGKGVLAAVDCTKPEHdaLKEEYNVKGFPTFK 80

                         90
                 ....*....|....*
gi 575771915 313 LFRGGEKVGEHNGGR 327
Cdd:cd02997   81 YFENGKFVEKYEGER 95
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 2-78 2.08e-16

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: 73.86  E-value: 2.08e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 575771915   2 CGHCQRLQPTWndlgDKYNSMEDAKVYVAKVDCTADSDVCSAQGVRGYPTLKFFKPGQE-AVKYQGPRDFETLENWML 78
Cdd:cd03001   30 CGHCKNLAPEW----KKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVFGAGKNsPQDYQGGRTAKAIVSAAL 103
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 2-78 1.14e-15

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


Pssm-ID: 239300 [Multi-domain]  Cd Length: 109  Bit Score: 72.01  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915   2 CGHCQRLQPTWNDLGDKYNSMedakVYVAKVDCTADS--DVCSAQGVRGYPTLKFFKPGQEAVK-----YQGPRDFETLE 74
Cdd:cd03002   30 CGHCKNLKPEYAKAAKELDGL----VQVAAVDCDEDKnkPLCGKYGVQGFPTLKVFRPPKKASKhavedYNGERSAKAIV 105


                 ....
gi 575771915  75 NWML 78
Cdd:cd03002  106 DFVL 109
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 105-202 1.45e-15

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: 71.58  E-value: 1.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 105 YELSANNFELHVSQGNH-FIKFFAPWCGHCKALAPTWEQLALGLEHSETVKIGKVDCT--QHYAVCSEHQVRGYPTLLWF 181
Cdd:cd02997    3 VHLTDEDFRKFLKKEKHvLVMFYAPWCGHCKKMKPEFTKAATELKEDGKGVLAAVDCTkpEHDALKEEYNVKGFPTFKYF 82

                         90       100
                 ....*....|....*....|.
gi 575771915 182 RDGKKVDQYKGKRDLESLRDY 202
Cdd:cd02997   83 ENGKFVEKYEGERTAEDIIEF 103
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 2-73 1.68e-15

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: 71.33  E-value: 1.68e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 575771915   2 CGHCQRLQPTWNDLGDKYNSMeDAKVYVAKVDCTADSDVCSAQGVRGYPTLKFFKpGQEAVKYQGPRDFETL 73
Cdd:cd03000   27 CGHCKKLEPVWNEVGAELKSS-GSPVRVGKLDATAYSSIASEFGVRGYPTIKLLK-GDLAYNYRGPRTKDDI 96
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 106-203 2.52e-15

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: 70.87  E-value: 2.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 106 ELSANNFELhVSQGNHFIKFFAPWCGHCKALAPTWEQLAlglEHSET--VKIGKVDCTQHYAVCSEHQVRGYPTLLWFRD 183
Cdd:cd02994    5 ELTDSNWTL-VLEGEWMIEFYAPWCPACQQLQPEWEEFA---DWSDDlgINVAKVDVTQEPGLSGRFFVTALPTIYHAKD 80

                         90       100
                 ....*....|....*....|
gi 575771915 184 GkKVDQYKGKRDLESLRDYV 203
Cdd:cd02994   81 G-VFRRYQGPRDKEDLISFI 99
trxA PRK09381
thioredoxin TrxA;
236-336 1.41e-14

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 68.94  E-value: 1.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 236 VLALTEKSFEDTI--AQGITFVKFYAPWCGHCKNLAPTWEELSkKEFPGlsDVTIAEVDCTAERNVCSKYSVRGYPTLLL 313
Cdd:PRK09381   5 IIHLTDDSFDTDVlkADGAILVDFWAEWCGPCKMIAPILDEIA-DEYQG--KLTVAKLNIDQNPGTAPKYGIRGIPTLLL 81

                         90       100
                 ....*....|....*....|...
gi 575771915 314 FRGGEKVGEHNGGRDLDSLHSFV 336
Cdd:PRK09381  82 FKNGEVAATKVGALSKGQLKEFL 104
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 234-336 8.89e-14

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: 66.63  E-value: 8.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 234 GTVLALTEKSFEDTIaQGITFVKFYAPWCGHCKNLAPTWEELSKKefpglSD---VTIAEVDCTAERNVCSKYSVRGYPT 310
Cdd:cd02994    1 SNVVELTDSNWTLVL-EGEWMIEFYAPWCPACQQLQPEWEEFADW-----SDdlgINVAKVDVTQEPGLSGRFFVTALPT 74

                         90       100
                 ....*....|....*....|....*.
gi 575771915 311 LLLFRGGEkVGEHNGGRDLDSLHSFV 336
Cdd:cd02994   75 IYHAKDGV-FRRYQGPRDKEDLISFI 99
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 2-76 2.26e-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: 65.24  E-value: 2.26e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575771915   2 CGHCQRLQPTWNDLGDKYnsmeDAKVYVAKVDCTADSDVCSAQGVRGYPTLKFFKPGQEAVKYQGPRDFETLENW 76
Cdd:cd03003   30 CSHCHDLAPTWREFAKEM----DGVIRIGAVNCGDDRMLCRSQGVNSYPSLYVFPSGMNPEKYYGDRSKESLVKF 100
PTZ00051 PTZ00051
thioredoxin; Provisional
 240-328 1.89e-12

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 62.59  E-value: 1.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 240 TEKSFEDTIAQG-ITFVKFYAPWCGHCKNLAPTWEELSkKEFPGLSDVTIaEVDCTAErnVCSKYSVRGYPTLLLFRGGE 318
Cdd:PTZ00051   7 SQAEFESTLSQNeLVIVDFYAEWCGPCKRIAPFYEECS-KEYTKMVFVKV-DVDELSE--VAEKENITSMPTFKVFKNGS 82

                         90
                 ....*....|
gi 575771915 319 KVGEHNGGRD 328
Cdd:PTZ00051  83 VVDTLLGAND 92
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 253-336 2.80e-12

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: 62.38  E-value: 2.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 253 TFVKFYAPWCGHCKNLAPTWEELSKKeFPGLSDVTIAEvdCTAERNVCSKYSVRGYPTLLLFRGGEKVgEHNGGRDLDSL 332
Cdd:cd02999   21 TAVLFYASWCPFSASFRPHFNALSSM-FPQIRHLAIEE--SSIKPSLLSRYGVVGFPTILLFNSTPRV-RYNGTRTLDSL 96


                 ....
gi 575771915 333 HSFV 336
Cdd:cd02999   97 AAFY 100
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 2-76 5.26e-12

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: 61.54  E-value: 5.26e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575771915   2 CGHCQRLQPTWndlgDKYNSMEDAKVYVAKVDCTADSDVCSAQGVRGYPTLKFFKPGQEAV-KYQG-PRDFETLENW 76
Cdd:cd03004   31 CGPCQALLPEL----RKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLYPGNASKYhSYNGwHRDADSILEF 103
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 2-77 1.44e-11

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: 60.22  E-value: 1.44e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575771915   2 CGHCQRLQPTWNDLGDKYNSmedaKVYVAKVDCTADSDVCSAQGVRGYPTLKFFKPGQEAVKYQGPRDFETLENWM 77
Cdd:COG3118   30 CGPCKMLAPVLEELAAEYGG----KVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQPVDRFVGALPKEQLREFL 101
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 2-57 2.43e-11

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: 59.97  E-value: 2.43e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 575771915   2 CGHCQRLQPTW----NDLgDKYNSMedakVYVAKVDCTADS--DVCSAQGVRGYPTLKFFKP 57
Cdd:cd02992   31 CGHCRAFAPTWkklaRDL-RKWRPV----VRVAAVDCADEEnvALCRDFGVTGYPTLRYFPP 87
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 2-76 2.97e-11

TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins.


Pssm-ID: 239245 [Multi-domain]  Cd Length: 93  Bit Score: 59.11  E-value: 2.97e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575771915   2 CGHCQRLQPTWNDLGDKYNsmedaKVYVAKVDCTADSDVCSAQGVRGYPTLKFFKPGQEAVKYQGPRDFETLENW 76
Cdd:cd02947   22 CGPCKAIAPVLEELAEEYP-----KVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVVGADPKEELEEF 91
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 106-203 6.35e-11

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: 58.56  E-value: 6.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 106 ELSANNFElHVSQGNH--FIKFFAPWCGHCKALAPTWEQLALGLEH----SETVKIGKVDCTQHYAVCSEHQVRGYPTLL 179
Cdd:cd02996    5 SLTSGNID-DILQSAElvLVNFYADWCRFSQMLHPIFEEAAAKIKEefpdAGKVVWGKVDCDKESDIADRYRINKYPTLK 83

                         90       100
                 ....*....|....*....|....*
gi 575771915 180 WFRDGKKVDQ-YKGKRDLESLRDYV 203
Cdd:cd02996   84 LFRNGMMMKReYRGQRSVEALAEFV 108
PRK10996 PRK10996
thioredoxin 2; Provisional
 255-325 1.69e-10

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 58.54  E-value: 1.69e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 575771915 255 VKFYAPWCGHCKNLAPTWEELSKKEfpgLSDVTIAEVDCTAERNVCSKYSVRGYPTLLLFRGGEKVGEHNG 325
Cdd:PRK10996  57 IDFWAPWCGPCRNFAPIFEDVAAER---SGKVRFVKVNTEAERELSARFRIRSIPTIMIFKNGQVVDMLNG 124
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 2-77 2.17e-10

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


Pssm-ID: 239295 [Multi-domain]  Cd Length: 104  Bit Score: 56.94  E-value: 2.17e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 575771915   2 CGHCQRLQPTWNDLGDKYNsmEDAKVYVAKVDCT-ADSDVCSAQG-VRGYPTLKFFKPGQEAVKYQGPRDFETLENWM 77
Cdd:cd02997   29 CGHCKKMKPEFTKAATELK--EDGKGVLAAVDCTkPEHDALKEEYnVKGFPTFKYFENGKFVEKYEGERTAEDIIEFM 104
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 254-320 4.18e-10

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


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 55.40  E-value: 4.18e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 254 FVKFYAPWCGHCKNLAPTWEELSKKEfpglSDVTIAEVDCTAERNVC---SKYSVRGYPTLLLFRGGEKV 320
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELALLN----KGVKFEAVDVDEDPALEkelKRYGVGGVPTLVVFGPGIGV 66
PRK10996 PRK10996
thioredoxin 2; Provisional
 123-192 6.15e-10

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 56.62  E-value: 6.15e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 123 IKFFAPWCGHCKALAPTWEQLAlgLEHSETVKIGKVDCTQHYAVCSEHQVRGYPTLLWFRDGKKVDQYKG 192
Cdd:PRK10996  57 IDFWAPWCGPCRNFAPIFEDVA--AERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFKNGQVVDMLNG 124
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 92-209 1.68e-09

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 55.47  E-value: 1.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915  92 AEPPRAPELKqgLYELSANNFELHVSQGN-HFIKFFAPWCGHCKALAPTWEQLA--------LGL---EHSETVK--IGK 157
Cdd:COG0526    3 AVGKPAPDFT--LTDLDGKPLSLADLKGKpVLVNFWATWCPPCRAEMPVLKELAeeyggvvfVGVdvdENPEAVKafLKE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 575771915 158 VDCT------QHYAVCSEHQVRGYPTLLWF-RDGKKVDQYKGKRDLESLRDYVQSQLQG 209
Cdd:COG0526   81 LGLPypvlldPDGELAKAYGVRGIPTTVLIdKDGKIVARHVGPLSPEELEEALEKLLAK 139
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 252-338 2.02e-09

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 55.47  E-value: 2.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 252 ITFVKFYAPWCGHCKNLAPTWEELsKKEFPGLSDVTIAeVDCTAE--------------------RNVCSKYSVRGYPTL 311
Cdd:COG0526   30 PVLVNFWATWCPPCRAEMPVLKEL-AEEYGGVVFVGVD-VDENPEavkaflkelglpypvlldpdGELAKAYGVRGIPTT 107

                         90       100
                 ....*....|....*....|....*...
gi 575771915 312 LLF-RGGEKVGEHNGGRDLDSLHSFVLR 338
Cdd:COG0526  108 VLIdKDGKIVARHVGPLSPEELEEALEK 135
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 122-190 5.28e-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: 52.32  E-value: 5.28e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 575771915 122 FIKFFAPWCGHCKALAPTWEQLAlglEHSETVKIGKVDCTQHYAVCSEHQ---VRGYPTLLWFRDGKKVDQY 190
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELA---LLNKGVKFEAVDVDEDPALEKELKrygVGGVPTLVVFGPGIGVKYG 69
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 2-81 5.65e-09

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


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 53.06  E-value: 5.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915    2 CGHCQRLQPTWNDLGDKYNSmedaKVYVAKVDCTADSDVCSAQGVRGYPTLKFFKPGQEAVKYQGPRDFETLENWMLQTL 81
Cdd:TIGR01068  26 CGPCKMIAPILEELAKEYEG----KVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKEVDRSVGALPKAALKQLINKNL 101
trxA PRK09381
thioredoxin TrxA;
104-207 7.28e-09

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 52.76  E-value: 7.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 104 LYELSANNFELHV--SQGNHFIKFFAPWCGHCKALAPTWEQLAlgLEHSETVKIGKVDCTQHYAVCSEHQVRGYPTLLWF 181
Cdd:PRK09381   5 IIHLTDDSFDTDVlkADGAILVDFWAEWCGPCKMIAPILDEIA--DEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLF 82

                         90       100
                 ....*....|....*....|....*.
gi 575771915 182 RDGKKVDQYKGKRDLESLRDYVQSQL 207
Cdd:PRK09381  83 KNGEVAATKVGALSKGQLKEFLDANL 108
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 123-203 1.07e-08

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


Pssm-ID: 239254 [Multi-domain]  Cd Length: 96  Bit Score: 51.89  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 123 IKFFAPWCGHCKALAPTWEQLALglEHSETVKIGKVDCTQHYAVCSEHQVRGYPTLLWFRDGKKVDQYKGKRDLESLRDY 202
Cdd:cd02956   17 VDFWAPRSPPSKELLPLLERLAE--EYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVDGFQGAQPEEQLRQM 94


                 .
gi 575771915 203 V 203
Cdd:cd02956   95 L 95
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 125-203 1.28e-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: 51.98  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 125 FFAPWCGHCKALAPTWEQLA--------LGLEHSetvkigkvdcTQHYAVCSEHQVRGYPTLLWFRDGKKVdQYKGKRDL 196
Cdd:cd02999   25 FYASWCPFSASFRPHFNALSsmfpqirhLAIEES----------SIKPSLLSRYGVVGFPTILLFNSTPRV-RYNGTRTL 93


                 ....*..
gi 575771915 197 ESLRDYV 203
Cdd:cd02999   94 DSLAAFY 100
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 126-203 1.51e-08

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: 52.07  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 126 FAPWCGHCKALAPTWEQLALGLEHSeTVKIGKV--DCTQHYAVCSEHQVRGYPTLLWF-RDGKKVDQYKG-KRDLESLRD 201
Cdd:cd02993   29 YAPWCPFCQAMEASYEELAEKLAGS-NVKVAKFnaDGEQREFAKEELQLKSFPTILFFpKNSRQPIKYPSeQRDVDSLLM 107


                 ..
gi 575771915 202 YV 203
Cdd:cd02993  108 FV 109
PLN02309 PLN02309
5'-adenylylsulfate reductase
 126-205 1.01e-07

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 53.25  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 126 FAPWCGHCKALAPTWEQLALGLEHSEtVKIGK--VDCTQHYAVCSEHQVRGYPTLLWF-RDGKKVDQYKG-KRDLESLRD 201
Cdd:PLN02309 373 YAPWCPFCQAMEASYEELAEKLAGSG-VKVAKfrADGDQKEFAKQELQLGSFPTILLFpKNSSRPIKYPSeKRDVDSLLS 451


                 ....
gi 575771915 202 YVQS 205
Cdd:PLN02309 452 FVNS 455
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 2-79 1.19e-07

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


Pssm-ID: 239292 [Multi-domain]  Cd Length: 101  Bit Score: 49.30  E-value: 1.19e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 575771915   2 CGHCQRLQPTWNDLGDKynsMEDAKVYVAKVDCTADSDVCSAQGVRGYPTLKFFKPGqEAVKYQGPRDFETLENWMLQ 79
Cdd:cd02994   28 CPACQQLQPEWEEFADW---SDDLGINVAKVDVTQEPGLSGRFFVTALPTIYHAKDG-VFRRYQGPRDKEDLISFIEE 101
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 230-336 1.56e-07

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


Pssm-ID: 239291 [Multi-domain]  Cd Length: 109  Bit Score: 48.99  E-value: 1.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 230 TGDKGTVLALT--EKSFEDTIaqgitfVKFYAPWCGHCKNLAPTWEELSKKefPGLSDVTIAEVDCTAERNVCSK--YSV 305
Cdd:cd02993    5 TLSRAEIEALAkgERRNQSTL------VVLYAPWCPFCQAMEASYEELAEK--LAGSNVKVAKFNADGEQREFAKeeLQL 76

                         90       100       110
                 ....*....|....*....|....*....|...
gi 575771915 306 RGYPTLLLFRGGEK--VGEHNGGRDLDSLHSFV 336
Cdd:cd02993   77 KSFPTILFFPKNSRqpIKYPSEQRDVDSLLMFV 109
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 252-325 2.20e-07

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


Pssm-ID: 239282 [Multi-domain]  Cd Length: 97  Bit Score: 48.42  E-value: 2.20e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 575771915 252 ITFVKFYAPWCGHCKNLAPTWEELSKKEFPglsDVTIAEVDCTAERNVCSKYSVRGYPTLLLFRGGEKVGEHNG 325
Cdd:cd02984   16 LLVLHFWAPWAEPCKQMNQVFEELAKEAFP---SVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTIVDRVSG 86
PTZ00051 PTZ00051
thioredoxin; Provisional
 123-195 5.30e-07

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 47.18  E-value: 5.30e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 575771915 123 IKFFAPWCGHCKALAPTWEQLAlgLEHSETVKIgKVDCTQHYAVCSEHQVRGYPTLLWFRDGKKVDQYKGKRD 195
Cdd:PTZ00051  23 VDFYAEWCGPCKRIAPFYEECS--KEYTKMVFV-KVDVDELSEVAEKENITSMPTFKVFKNGSVVDTLLGAND 92
PLN02309 PLN02309
5'-adenylylsulfate reductase
 253-336 1.02e-06

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 50.17  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 253 TFVKFYAPWCGHCKNLAPTWEELSKKeFPGlSDVTIAE--VDCTAERNVCSKYSVRGYPTLLLFRGGE----KVGEHNgg 326
Cdd:PLN02309 368 WLVVLYAPWCPFCQAMEASYEELAEK-LAG-SGVKVAKfrADGDQKEFAKQELQLGSFPTILLFPKNSsrpiKYPSEK-- 443

                         90
                 ....*....|
gi 575771915 327 RDLDSLHSFV 336
Cdd:PLN02309 444 RDVDSLLSFV 453
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 2-73 1.75e-06

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: 46.23  E-value: 1.75e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575771915   2 CGHCQRLQPTWNDLGDKYNSM--EDAKVYVAKVDCTADSDVCSAQGVRGYPTLKFFKPGQEA-VKYQGPRDFETL 73
Cdd:cd02996   30 CRFSQMLHPIFEEAAAKIKEEfpDAGKVVWGKVDCDKESDIADRYRINKYPTLKLFRNGMMMkREYRGQRSVEAL 104
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 125-203 2.43e-06

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: 48.86  E-value: 2.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915  125 FFAPWCGHCKALAPTWEQLALGLEHSeTVKIGK--VDCTQHYAVCSEHQVRGYPTLLWF--RDGKKVDQYKGKRDLESLR 200
Cdd:TIGR00424 378 LYAPWCPFCQAMEASYLELAEKLAGS-GVKVAKfrADGDQKEFAKQELQLGSFPTILFFpkHSSRPIKYPSEKRDVDSLM 456


                  ...
gi 575771915  201 DYV 203
Cdd:TIGR00424 457 SFV 459
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 255-333 2.54e-06

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: 45.34  E-value: 2.54e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575771915 255 VKFYAPWCGHCKNLAPTWEELSKkEFPGlsDVTIAEVDCTAERNVCSKYSVRGYPTLLLFRGGEKVGEHNGGRDLDSLH 333
Cdd:cd02956   17 VDFWAPRSPPSKELLPLLERLAE-EYQG--QFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVDGFQGAQPEEQLR 92
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 2-91 3.92e-06

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 47.31  E-value: 3.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915   2 CGHCQRLQPTWNDLGDKYNsmedAKVYVAKVDCTADSDVCSAQGVRGYPTLKFFKPGQEAVKYQGPRDFETLENWMLQTL 81
Cdd:PTZ00443  64 CSHCRKMAPAWERLAKALK----GQVNVADLDATRALNLAKRFAIKGYPTLLLFDKGKMYQYEGGDRSTEKLAAFALGDF 139

                         90
                 ....*....|
gi 575771915  82 NEEPATPEPE 91
Cdd:PTZ00443 140 KKALGAPVPA 149
TMX2 cd02962
TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related ...
 224-320 6.77e-06

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: 45.45  E-value: 6.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 224 VMAAEPTGDK-GTVLALTEKSFEDTIAQGIT---FVKFYAPWCGHCKNLAPTWEELSKK-EFPGLSdvtIAEVDCTAERN 298
Cdd:cd02962   17 LLAPQPLYMGpEHIKYFTPKTLEEELERDKRvtwLVEFFTTWSPECVNFAPVFAELSLKyNNNNLK---FGKIDIGRFPN 93

                         90       100
                 ....*....|....*....|....*...
gi 575771915 299 VCSKYSV------RGYPTLLLFRGGEKV 320
Cdd:cd02962   94 VAEKFRVstsplsKQLPTIILFQGGKEV 121
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 2-56 7.50e-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: 44.03  E-value: 7.50e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 575771915   2 CGHCQRLQPTWNDLGDKYNSmedaKVYVAKVDCTADSDVCSAQGVRGYPTLKFFK 56
Cdd:cd02949   25 CGPCRTLKPILNKVIDEFDG----AVHFVEIDIDEDQEIAEAAGIMGTPTVQFFK 75
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 2-83 2.87e-05

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 43.53  E-value: 2.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915   2 CGHCQRLQPTWNDLGDKYN-----------SMEDAKVYVAKVDCT------ADSDVCSAQGVRGYPTLKFFKP-GQEAVK 63
Cdd:COG0526   40 CPPCRAEMPVLKELAEEYGgvvfvgvdvdeNPEAVKAFLKELGLPypvlldPDGELAKAYGVRGIPTTVLIDKdGKIVAR 119

                         90       100
                 ....*....|....*....|
gi 575771915  64 YQGPRDFETLENWMLQTLNE 83
Cdd:COG0526  120 HVGPLSPEELEEALEKLLAK 139
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 255-336 3.38e-05

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: 45.39  E-value: 3.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915  255 VKFYAPWCGHCKNLAPTWEELSKKeFPGlSDVTIAEVDCTAERNVCSKYSVR--GYPTLLLF--RGGEKVGEHNGGRDLD 330
Cdd:TIGR00424 376 VVLYAPWCPFCQAMEASYLELAEK-LAG-SGVKVAKFRADGDQKEFAKQELQlgSFPTILFFpkHSSRPIKYPSEKRDVD 453


                  ....*.
gi 575771915  331 SLHSFV 336
Cdd:TIGR00424 454 SLMSFV 459
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 125-192 5.19e-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: 41.49  E-value: 5.19e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 575771915 125 FFAPWCGHCKALAPTWEQLAlgLEHSETVKIGKVDCTQHYAVCSEHQVRGYPTLLWFRDGKKVDQYKG 192
Cdd:cd02984   21 FWAPWAEPCKQMNQVFEELA--KEAFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTIVDRVSG 86
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 253-332 6.82e-05

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


Pssm-ID: 239248 [Multi-domain]  Cd Length: 142  Bit Score: 42.32  E-value: 6.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 253 TFVKFYAPWCGHCKNLAPTWEELsKKEFPGLSDVTIAEVDCTAERNVCSKYSVRGYPTLLLF-RGGEKVGEHNGGRDLDS 331
Cdd:cd02950   23 TLVEFYADWCTVCQEMAPDVAKL-KQKYGDQVNFVMLNVDNPKWLPEIDRYRVDGIPHFVFLdREGNEEGQSIGLQPKQV 101


                 .
gi 575771915 332 L 332
Cdd:cd02950  102 L 102
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 237-336 7.78e-05

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: 41.59  E-value: 7.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 237 LALTEKSFEDTI----AQGITFVKFYAPWCGHCKNLAPTWEELSkKEFPGLSdVTIAEVDCTAERNVCSKYSVRGYPTLL 312
Cdd:cd02963    7 YSLTFSQYENEIvpksFKKPYLIKITSDWCFSCIHIEPVWKEVI-QELEPLG-VGIATVNAGHERRLARKLGAHSVPAIV 84

                         90       100
                 ....*....|....*....|....
gi 575771915 313 LFRGGEKVGEHNGGRDLDSLHSFV 336
Cdd:cd02963   85 GIINGQVTFYHDSSFTKQHVVDFV 108
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 2-58 1.99e-04

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


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 39.22  E-value: 1.99e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915   2 CGHCQRLQPTWNDLGDkynsmEDAKVYVAKVDCTADSDVCSAQ---GVRGYPTLKFFKPG 58
Cdd:cd01659    9 CPFCQALRPVLAELAL-----LNKGVKFEAVDVDEDPALEKELkryGVGGVPTLVVFGPG 63
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 2-76 2.72e-04

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


Pssm-ID: 239254 [Multi-domain]  Cd Length: 96  Bit Score: 39.56  E-value: 2.72e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575771915   2 CGHCQRLQPTWNDLGDKYNsmedAKVYVAKVDCTADSDVCSAQGVRGYPTLKFFKPGQEAVKYQGPRDFETLENW 76
Cdd:cd02956   24 SPPSKELLPLLERLAEEYQ----GQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVDGFQGAQPEEQLRQM 94
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 255-325 3.36e-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: 39.41  E-value: 3.36e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 575771915 255 VKFYAPWCGHCKNLAPTweeLSK--KEFPGlsDVTIAEVDCTAERNVCSKYSVRGYPTLLLFRGGEKVGEHNG 325
Cdd:cd02949   18 VLYTSPTCGPCRTLKPI---LNKviDEFDG--AVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDKELVKEISG 85
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 2-77 3.48e-04

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


Pssm-ID: 239291 [Multi-domain]  Cd Length: 109  Bit Score: 39.74  E-value: 3.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915   2 CGHCQRLQPTWNDLGDKynsMEDAKVYVAKVDCTADSDVCSAQ--GVRGYPTLKFFKPG-QEAVKYQGP-RDFETLENWM 77
Cdd:cd02993   33 CPFCQAMEASYEELAEK---LAGSNVKVAKFNADGEQREFAKEelQLKSFPTILFFPKNsRQPIKYPSEqRDVDSLLMFV 109
trxA PRK09381
thioredoxin TrxA;
2-66 3.73e-04

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 39.66  E-value: 3.73e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575771915   2 CGHCQRLQPTWNDLGDKYNsmedAKVYVAKVDCTADSDVCSAQGVRGYPTLKFFKPGQEAVKYQG 66
Cdd:PRK09381  33 CGPCKMIAPILDEIADEYQ----GKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVG 93
PTZ00051 PTZ00051
thioredoxin; Provisional
 2-59 3.76e-04

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 39.09  E-value: 3.76e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 575771915   2 CGHCQRLQPTWNDLGDKYNSMEDAKVYVAKVdctadSDVCSAQGVRGYPTLKFFKPGQ 59
Cdd:PTZ00051  30 CGPCKRIAPFYEECSKEYTKMVFVKVDVDEL-----SEVAEKENITSMPTFKVFKNGS 82
TMX2 cd02962
TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related ...
 123-195 1.23e-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: 38.90  E-value: 1.23e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575771915 123 IKFFAPWCGHCKALAPTWEQLALGLEHSeTVKIGKVD------CTQHYAVCSEHQVRGYPTLLWFRDGKKVDQYKGKRD 195
Cdd:cd02962   52 VEFFTTWSPECVNFAPVFAELSLKYNNN-NLKFGKIDigrfpnVAEKFRVSTSPLSKQLPTIILFQGGKEVARRPYYND 129
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 123-204 1.95e-03

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


Pssm-ID: 239247 [Multi-domain]  Cd Length: 97  Bit Score: 37.10  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 123 IKFFAPWCGHCKALAPTWEQLALglEHSETVKIGKVDCTQHYAVCSEHQVRGYPTLLWFRDGKKVDQYKGKRDLESLRDY 202
Cdd:cd02949   18 VLYTSPTCGPCRTLKPILNKVID--EFDGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDKELVKEISGVKMKSEYREF 95


                 ..
gi 575771915 203 VQ 204
Cdd:cd02949   96 IE 97
TRX_CDSP32 cd02985
TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed ...
 255-329 2.20e-03

TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed of two TRX domains, a C-terminal TRX domain which contains a redox active CXXC motif and an N-terminal TRX-like domain which contains an SXXS sequence instead of the redox active motif. CDSP32 is a stress-inducible TRX, i.e., it acts as a TRX by reducing protein disulfides and is induced by environmental and oxidative stress conditions. It plays a critical role in plastid defense against oxidative damage, a role related to its function as a physiological electron donor to BAS1, a plastidic 2-cys peroxiredoxin. Plants lacking CDSP32 exhibit decreased photosystem II photochemical efficiencies and chlorophyll retention compared to WT controls, as well as an increased proportion of BAS1 in its overoxidized monomeric form.


Pssm-ID: 239283  Cd Length: 103  Bit Score: 37.08  E-value: 2.20e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575771915 255 VKFYAPWCGHCKNLAPTWEELSKKefpgLSDVTIAEV---DCTAERNVCSKYSVRGYPTLLLFRGGEKVGEHNG-GRDL 329
Cdd:cd02985   20 LEFALKHSGPSVKIYPTMVKLSRT----CNDVVFLLVngdENDSTMELCRREKIIEVPHFLFYKDGEKIHEEEGiGPDE 94
PDI_a_EFP1_N cd03006
PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase ...
 252-326 2.75e-03

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


Pssm-ID: 239304  Cd Length: 113  Bit Score: 37.06  E-value: 2.75e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575771915 252 ITFVKFYAPWCGHCKNLAPTWEELSKKefpgLSD-VTIAEVDCTAERNVC-SKYSVRGYPTLLLFRGGEKVGEHNGG 326
Cdd:cd03006   31 VSLVMYYAPWDAQSQAARQEFEQVAQK----LSDqVLFVAINCWWPQGKCrKQKHFFYFPVIHLYYRSRGPIEYKGP 103
PDI_a_EFP1_N cd03006
PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase ...
 122-192 2.84e-03

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


Pssm-ID: 239304  Cd Length: 113  Bit Score: 37.06  E-value: 2.84e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 575771915 122 FIKFFAPWCGHCKALAPTWEQLALGLehSETVKIGKVDCTQHYAVCsEHQVR--GYPTLLWFRDGKKVDQYKG 192
Cdd:cd03006   33 LVMYYAPWDAQSQAARQEFEQVAQKL--SDQVLFVAINCWWPQGKC-RKQKHffYFPVIHLYYRSRGPIEYKG 102
HyaE cd02965
HyaE family; HyaE is also called HupG and HoxO. They are proteins serving a critical role in ...
 278-332 2.97e-03

HyaE family; HyaE is also called HupG and HoxO. They are proteins serving a critical role in the assembly of multimeric [NiFe] hydrogenases, the enzymes that catalyze the oxidation of molecular hydrogen to enable microorganisms to utilize hydrogen as the sole energy source. The E. coli HyaE protein is a chaperone that specifically interacts with the twin-arginine translocation (Tat) signal peptide of the [NiFe] hydrogenase-1 beta subunit precursor. Tat signal peptides target precursor proteins to the Tat protein export system, which facilitates the transport of fully folded proteins across the inner membrane. HyaE may be involved in regulating the traffic of [NiFe] hydrogenase-1 on the Tat transport pathway.


Pssm-ID: 239263  Cd Length: 111  Bit Score: 36.90  E-value: 2.97e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 575771915 278 KEFPGLSDvtIAEVDCTAERNVCSKYSVRGYPTLLLFRGGEKVGEHNGGRDLDSL 332
Cdd:cd02965   56 KAFPGRFR--AAVVGRADEQALAARFGVLRTPALLFFRDGRYVGVLAGIRDWDEY 108
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 252-325 8.23e-03

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


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 35.67  E-value: 8.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 252 ITFVKFYAPWCGHCKNLAPTWEELSKK-EFPGLSDVTIAEVDCTAER--------------------NVCSKYSVRGYPT 310
Cdd:cd02966   21 VVLVNFWASWCPPCRAEMPELEALAKEyKDDGVEVVGVNVDDDDPAAvkaflkkygitfpvlldpdgELAKAYGVRGLPT 100

                         90
                 ....*....|....*.
gi 575771915 311 LLLF-RGGEKVGEHNG 325
Cdd:cd02966  101 TFLIdRDGRIRARHVG 116
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 125-144 8.94e-03

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: 35.74  E-value: 8.94e-03
                         10        20
                 ....*....|....*....|
gi 575771915 125 FFAPWCGHCKALAPTWEQLA 144
Cdd:cd03011   27 FWATWCPVCRFTSPTVNQLA 46
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 121-205 9.43e-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: 35.43  E-value: 9.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771915 121 HFIKFFAPWCGHCKALAPTWEQLALGLEhSETVKIGKVDCTQHYAVCSEHQVRGYPTLLWFRDGKKVDQYKGKRDLESLR 200
Cdd:cd02963   27 YLIKITSDWCFSCIHIEPVWKEVIQELE-PLGVGIATVNAGHERRLARKLGAHSVPAIVGIINGQVTFYHDSSFTKQHVV 105


                 ....*
gi 575771915 201 DYVQS 205
Cdd:cd02963  106 DFVRK 110
 
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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