NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|22331799|ref|NP_191056|]
View 

PDI-like 1-3 [Arabidopsis thaliana]

Protein Classification

protein disulfide isomerase family protein( domain architecture ID 1001536)

protein disulfide isomerase family protein may act as a protein-folding catalyst that interacts with nascent polypeptides to catalyze the formation, isomerization, and reduction or oxidation of disulfide bonds

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ER_PDI_fam super family cl36828
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 99-553 1.03e-163

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).


The actual alignment was detected with superfamily member TIGR01130:

Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 474.55  E-value: 1.03e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799    99 KDVAVLTKDNFTEFVGNNSFAMVEFYAPWCGACQALTPEYAAAATELKGLAA---LAKIDATEEGDLAQKYEIQGFPTVF 175
Cdd:TIGR01130   1 EDVLVLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPpikLAKVDATEEKDLAQKYGVSGYPTLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799   176 LFVDGE-MRKTYEGERTKDGIVTWLKKKASPSIHNITTKEEAERVLSAEPKLVFGFLNSLVGSESEELAAASRLEDDLSF 254
Cdd:TIGR01130  81 IFRNGEdSVSDYNGPRDADGIVKYMKKQSGPAVKEIETVADLEAFLADDDVVVIGFFKDLDSELNDTFLSVAEKLRDVYF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799   255 YQTASPDIAKLFEIETQVKRPALVLLKKEEEKLARFDGNFTKT--AIAEFVSANKVPLVINFTREGASLIFESSVKNQLI 332
Cdd:TIGR01130 161 FFAHSSDVAAFAKLGAFPDSVVLFKPKDEDEKFSKVDGEMDTDvsDLEKFIRAESLPLVGEFTQETAAKYFESGPLVVLY 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799   333 LFAKANES--EKHLPTLREVAKSFKGKFVFVYVqmDNEDYGEAVSGFFGVTG-AAPKVLVYTGNEDMRKFILDGELTVNN 409
Cdd:TIGR01130 241 YNVDESLDpfEELRNRFLEAAKKFRGKFVNFAV--ADEEDFGRELEYFGLKAeKFPAVAIQDLEGNKKYPMDQEEFSSEN 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799   410 IKTLAEDFLADKLKPFYKSDPLPENNDGDVKVIVGNNFDEIVLDESKDVLLEIYAPWCGHCQSFEPIYNKLGKYLKGIDS 489
Cdd:TIGR01130 319 LEAFVKDFLDGKLKPYLKSEPIPEDDEGPVKVLVGKNFDEIVLDETKDVLVEFYAPWCGHCKNLAPIYEELAEKYKDAES 398

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331799   490 -LVVAKMDGTSNEHPRAKADGFPTILFFPGGNKSfDPIAVDVDRTVVELYKFLKKHASIPFKLEK 553
Cdd:TIGR01130 399 dVVIAKMDATANDVPPFEVEGFPTIKFVPAGKKS-EPVPYDGDRTLEDFSKFIAKHATFPLEGKA 462
 
Name Accession Description Interval E-value
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 99-553 1.03e-163

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: 474.55  E-value: 1.03e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799    99 KDVAVLTKDNFTEFVGNNSFAMVEFYAPWCGACQALTPEYAAAATELKGLAA---LAKIDATEEGDLAQKYEIQGFPTVF 175
Cdd:TIGR01130   1 EDVLVLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPpikLAKVDATEEKDLAQKYGVSGYPTLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799   176 LFVDGE-MRKTYEGERTKDGIVTWLKKKASPSIHNITTKEEAERVLSAEPKLVFGFLNSLVGSESEELAAASRLEDDLSF 254
Cdd:TIGR01130  81 IFRNGEdSVSDYNGPRDADGIVKYMKKQSGPAVKEIETVADLEAFLADDDVVVIGFFKDLDSELNDTFLSVAEKLRDVYF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799   255 YQTASPDIAKLFEIETQVKRPALVLLKKEEEKLARFDGNFTKT--AIAEFVSANKVPLVINFTREGASLIFESSVKNQLI 332
Cdd:TIGR01130 161 FFAHSSDVAAFAKLGAFPDSVVLFKPKDEDEKFSKVDGEMDTDvsDLEKFIRAESLPLVGEFTQETAAKYFESGPLVVLY 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799   333 LFAKANES--EKHLPTLREVAKSFKGKFVFVYVqmDNEDYGEAVSGFFGVTG-AAPKVLVYTGNEDMRKFILDGELTVNN 409
Cdd:TIGR01130 241 YNVDESLDpfEELRNRFLEAAKKFRGKFVNFAV--ADEEDFGRELEYFGLKAeKFPAVAIQDLEGNKKYPMDQEEFSSEN 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799   410 IKTLAEDFLADKLKPFYKSDPLPENNDGDVKVIVGNNFDEIVLDESKDVLLEIYAPWCGHCQSFEPIYNKLGKYLKGIDS 489
Cdd:TIGR01130 319 LEAFVKDFLDGKLKPYLKSEPIPEDDEGPVKVLVGKNFDEIVLDETKDVLVEFYAPWCGHCKNLAPIYEELAEKYKDAES 398

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331799   490 -LVVAKMDGTSNEHPRAKADGFPTILFFPGGNKSfDPIAVDVDRTVVELYKFLKKHASIPFKLEK 553
Cdd:TIGR01130 399 dVVIAKMDATANDVPPFEVEGFPTIKFVPAGKKS-EPVPYDGDRTLEDFSKFIAKHATFPLEGKA 462
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 87-550 7.64e-91

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 287.80  E-value: 7.64e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799   87 GYEEEPLPpvdEKDVAVLTKDNFTEFVGNNSFAMVEFYAPWCGACQALTPEYAAAATELKGLAA---LAKIDATEEGDLA 163
Cdd:PTZ00102  23 GSAEEHFI---SEHVTVLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSeivLASVDATEEMELA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799  164 QKYEIQGFPTVFLFVDGEMRKtYEGERTKDGIVTWLKKKASPSIHNITTKEEaERVLSAEPKLVFGFLNSLVGSES---- 239
Cdd:PTZ00102 100 QEFGVRGYPTIKFFNKGNPVN-YSGGRTADGIVSWIKKLTGPAVTEVESASE-IKLIAKKIFVAFYGEYTSKDSELykkf 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799  240 EELAAASRleDDLSFYQTASPDIAKLFeietqvkrpalvLLKKEEEKLARFDGNfTKTAIAEFVSANKVPLVINFTREGA 319
Cdd:PTZ00102 178 EEVADKHR--EHAKFFVKKHEGKNKIY------------VLHKDEEGVELFMGK-TKEELEEFVSTESFPLFAEINAENY 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799  320 SLIFESSvkNQLILFAKANES-EKHLPTLREVAKSFKGKFVFVYVqmDNEDYGEAVSGFFGVTgAAPKvLVYTGNEDmrK 398
Cdd:PTZ00102 243 RRYISSG--KDLVWFCGTTEDyDKYKSVVRKVARKLREKYAFVWL--DTEQFGSHAKEHLLIE-EFPG-LAYQSPAG--R 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799  399 FILDGE----LTVNNIKTLAEDFLADKLKPFYKSDPLPENNDGDVKVIVGNNFDEIVLDESKDVLLEIYAPWCGHCQSFE 474
Cdd:PTZ00102 315 YLLPPAkesfDSVEALIEFFKDVEAGKVEKSIKSEPIPEEQDGPVKVVVGNTFEEIVFKSDKDVLLEIYAPWCGHCKNLE 394

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331799  475 PIYNKLGKYLKGIDSLVVAKMDGTSNEHP--RAKADGFPTILFFPGGNKsfDPIAVDVDRTVVELYKFLKKHASIPFK 550
Cdd:PTZ00102 395 PVYNELGEKYKDNDSIIVAKMNGTANETPleEFSWSAFPTILFVKAGER--TPIPYEGERTVEGFKEFVNKHATNPFE 470
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 439-541 2.30e-49

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: 166.19  E-value: 2.30e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 439 VKVIVGNNFDEIVLDESKDVLLEIYAPWCGHCQSFEPIYNKLGKYLKGIDSLVVAKMDGTSNEHPRAKA-DGFPTILFFP 517
Cdd:cd02995   2 VKVVVGKNFDEVVLDSDKDVLVEFYAPWCGHCKALAPIYEELAEKLKGDDNVVIAKMDATANDVPSEFVvDGFPTILFFP 81

                        90       100
                ....*....|....*....|....
gi 22331799 518 GGNKSfDPIAVDVDRTVVELYKFL 541
Cdd:cd02995  82 AGDKS-NPIKYEGDRTLEDLIKFI 104
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 101-201 1.34e-30

Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 115.02  E-value: 1.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799   101 VAVLTKDNFTEFVGNNS-FAMVEFYAPWCGACQALTPEYAAAATELKGLAALAKIDATEEGDLAQKYEIQGFPTVFLFVD 179
Cdd:pfam00085   2 VVVLTDANFDEVVQKSSkPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKN 81

                          90       100
                  ....*....|....*....|..
gi 22331799   180 GEMRKTYEGERTKDGIVTWLKK 201
Cdd:pfam00085  82 GQPVDDYVGARPKDALAAFLKA 103
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 104-201 9.79e-28

Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 107.21  E-value: 9.79e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 104 LTKDNF-TEFVGNNSFAMVEFYAPWCGACQALTPEYAAAATELKGLAALAKIDATEEGDLAQKYEIQGFPTVFLFVDGEM 182
Cdd:COG3118   5 LTDENFeEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQP 84

                        90
                ....*....|....*....
gi 22331799 183 RKTYEGERTKDGIVTWLKK 201
Cdd:COG3118  85 VDRFVGALPKEQLREFLDK 103
 
Name Accession Description Interval E-value
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 99-553 1.03e-163

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: 474.55  E-value: 1.03e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799    99 KDVAVLTKDNFTEFVGNNSFAMVEFYAPWCGACQALTPEYAAAATELKGLAA---LAKIDATEEGDLAQKYEIQGFPTVF 175
Cdd:TIGR01130   1 EDVLVLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPpikLAKVDATEEKDLAQKYGVSGYPTLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799   176 LFVDGE-MRKTYEGERTKDGIVTWLKKKASPSIHNITTKEEAERVLSAEPKLVFGFLNSLVGSESEELAAASRLEDDLSF 254
Cdd:TIGR01130  81 IFRNGEdSVSDYNGPRDADGIVKYMKKQSGPAVKEIETVADLEAFLADDDVVVIGFFKDLDSELNDTFLSVAEKLRDVYF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799   255 YQTASPDIAKLFEIETQVKRPALVLLKKEEEKLARFDGNFTKT--AIAEFVSANKVPLVINFTREGASLIFESSVKNQLI 332
Cdd:TIGR01130 161 FFAHSSDVAAFAKLGAFPDSVVLFKPKDEDEKFSKVDGEMDTDvsDLEKFIRAESLPLVGEFTQETAAKYFESGPLVVLY 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799   333 LFAKANES--EKHLPTLREVAKSFKGKFVFVYVqmDNEDYGEAVSGFFGVTG-AAPKVLVYTGNEDMRKFILDGELTVNN 409
Cdd:TIGR01130 241 YNVDESLDpfEELRNRFLEAAKKFRGKFVNFAV--ADEEDFGRELEYFGLKAeKFPAVAIQDLEGNKKYPMDQEEFSSEN 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799   410 IKTLAEDFLADKLKPFYKSDPLPENNDGDVKVIVGNNFDEIVLDESKDVLLEIYAPWCGHCQSFEPIYNKLGKYLKGIDS 489
Cdd:TIGR01130 319 LEAFVKDFLDGKLKPYLKSEPIPEDDEGPVKVLVGKNFDEIVLDETKDVLVEFYAPWCGHCKNLAPIYEELAEKYKDAES 398

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331799   490 -LVVAKMDGTSNEHPRAKADGFPTILFFPGGNKSfDPIAVDVDRTVVELYKFLKKHASIPFKLEK 553
Cdd:TIGR01130 399 dVVIAKMDATANDVPPFEVEGFPTIKFVPAGKKS-EPVPYDGDRTLEDFSKFIAKHATFPLEGKA 462
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 87-550 7.64e-91

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 287.80  E-value: 7.64e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799   87 GYEEEPLPpvdEKDVAVLTKDNFTEFVGNNSFAMVEFYAPWCGACQALTPEYAAAATELKGLAA---LAKIDATEEGDLA 163
Cdd:PTZ00102  23 GSAEEHFI---SEHVTVLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSeivLASVDATEEMELA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799  164 QKYEIQGFPTVFLFVDGEMRKtYEGERTKDGIVTWLKKKASPSIHNITTKEEaERVLSAEPKLVFGFLNSLVGSES---- 239
Cdd:PTZ00102 100 QEFGVRGYPTIKFFNKGNPVN-YSGGRTADGIVSWIKKLTGPAVTEVESASE-IKLIAKKIFVAFYGEYTSKDSELykkf 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799  240 EELAAASRleDDLSFYQTASPDIAKLFeietqvkrpalvLLKKEEEKLARFDGNfTKTAIAEFVSANKVPLVINFTREGA 319
Cdd:PTZ00102 178 EEVADKHR--EHAKFFVKKHEGKNKIY------------VLHKDEEGVELFMGK-TKEELEEFVSTESFPLFAEINAENY 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799  320 SLIFESSvkNQLILFAKANES-EKHLPTLREVAKSFKGKFVFVYVqmDNEDYGEAVSGFFGVTgAAPKvLVYTGNEDmrK 398
Cdd:PTZ00102 243 RRYISSG--KDLVWFCGTTEDyDKYKSVVRKVARKLREKYAFVWL--DTEQFGSHAKEHLLIE-EFPG-LAYQSPAG--R 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799  399 FILDGE----LTVNNIKTLAEDFLADKLKPFYKSDPLPENNDGDVKVIVGNNFDEIVLDESKDVLLEIYAPWCGHCQSFE 474
Cdd:PTZ00102 315 YLLPPAkesfDSVEALIEFFKDVEAGKVEKSIKSEPIPEEQDGPVKVVVGNTFEEIVFKSDKDVLLEIYAPWCGHCKNLE 394

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331799  475 PIYNKLGKYLKGIDSLVVAKMDGTSNEHP--RAKADGFPTILFFPGGNKsfDPIAVDVDRTVVELYKFLKKHASIPFK 550
Cdd:PTZ00102 395 PVYNELGEKYKDNDSIIVAKMNGTANETPleEFSWSAFPTILFVKAGER--TPIPYEGERTVEGFKEFVNKHATNPFE 470
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 439-541 2.30e-49

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: 166.19  E-value: 2.30e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 439 VKVIVGNNFDEIVLDESKDVLLEIYAPWCGHCQSFEPIYNKLGKYLKGIDSLVVAKMDGTSNEHPRAKA-DGFPTILFFP 517
Cdd:cd02995   2 VKVVVGKNFDEVVLDSDKDVLVEFYAPWCGHCKALAPIYEELAEKLKGDDNVVIAKMDATANDVPSEFVvDGFPTILFFP 81

                        90       100
                ....*....|....*....|....
gi 22331799 518 GGNKSfDPIAVDVDRTVVELYKFL 541
Cdd:cd02995  82 AGDKS-NPIKYEGDRTLEDLIKFI 104
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 103-199 1.33e-34

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: 126.19  E-value: 1.33e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 103 VLTKDNFTEFVGNNSFAMVEFYAPWCGACQALTPEYAAAATELK--GLAALAKIDATEEGDLAQKYEIQGFPTVFLFVDG 180
Cdd:cd02961   2 ELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKgdGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPNG 81

                        90       100
                ....*....|....*....|
gi 22331799 181 -EMRKTYEGERTKDGIVTWL 199
Cdd:cd02961  82 sKEPVKYEGPRTLESLVEFI 101
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 100-198 1.22e-32

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: 120.85  E-value: 1.22e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 100 DVAVLTKDNFTEFVGNN-SFAMVEFYAPWCGACQALTPEYAAAATELKGLAALAKIDATEEGDLAQKYEIQGFPTVFLFV 178
Cdd:cd03001   1 DVVELTDSNFDKKVLNSdDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVFG 80

                        90       100
                ....*....|....*....|.
gi 22331799 179 DGEMR-KTYEGERTKDGIVTW 198
Cdd:cd03001  81 AGKNSpQDYQGGRTAKAIVSA 101
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 101-201 1.34e-30

Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 115.02  E-value: 1.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799   101 VAVLTKDNFTEFVGNNS-FAMVEFYAPWCGACQALTPEYAAAATELKGLAALAKIDATEEGDLAQKYEIQGFPTVFLFVD 179
Cdd:pfam00085   2 VVVLTDANFDEVVQKSSkPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKN 81

                          90       100
                  ....*....|....*....|..
gi 22331799   180 GEMRKTYEGERTKDGIVTWLKK 201
Cdd:pfam00085  82 GQPVDDYVGARPKDALAAFLKA 103
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 442-545 7.20e-28

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: 107.37  E-value: 7.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799   442 IVGNNFDEIVLDeSKDVLLEIYAPWCGHCQSFEPIYNKLGKYLKGIDSLVVAKMDGTSNEHP--RAKADGFPTILFFPGG 519
Cdd:TIGR01126   1 LTASNFDEIVLS-NKDVLVEFYAPWCGHCKNLAPEYEKLAKELKKDPKIVLAKVDATAEKDLasRFGVSGFPTIKFFPKG 79

                          90       100
                  ....*....|....*....|....*.
gi 22331799   520 NKSFDpiaVDVDRTVVELYKFLKKHA 545
Cdd:TIGR01126  80 SKPVD---YEGGRDLEAIVEFVNEKS 102
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 104-201 9.79e-28

Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 107.21  E-value: 9.79e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 104 LTKDNF-TEFVGNNSFAMVEFYAPWCGACQALTPEYAAAATELKGLAALAKIDATEEGDLAQKYEIQGFPTVFLFVDGEM 182
Cdd:COG3118   5 LTDENFeEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQP 84

                        90
                ....*....|....*....
gi 22331799 183 RKTYEGERTKDGIVTWLKK 201
Cdd:COG3118  85 VDRFVGALPKEQLREFLDK 103
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 438-541 1.13e-27

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: 106.95  E-value: 1.13e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 438 DVKVIVGNNFDEIVLDESKDVLLEIYAPWCGHCQSFEPIYNKLGKYLKGIDSLVVAKMDGTSNEHP---RAKADGFPTIL 514
Cdd:cd02998   1 NVVELTDSNFDKVVGDDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFANEDDVVIAKVDADEANKDlakKYGVSGFPTLK 80

                        90       100
                ....*....|....*....|....*..
gi 22331799 515 FFPGGNKsfDPIAVDVDRTVVELYKFL 541
Cdd:cd02998  81 FFPKGST--EPVKYEGGRDLEDLVKFV 105
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 100-199 7.14e-27

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: 104.71  E-value: 7.14e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 100 DVAVLTKDNFTEFVGNNSFAMVEFYAPWCGACQALTPEYAAAATELK--GLAALAKIDAT--EEGDLAQKYEIQGFPTVF 175
Cdd:cd02997   1 DVVHLTDEDFRKFLKKEKHVLVMFYAPWCGHCKKMKPEFTKAATELKedGKGVLAAVDCTkpEHDALKEEYNVKGFPTFK 80

                        90       100
                ....*....|....*....|....
gi 22331799 176 LFVDGEMRKTYEGERTKDGIVTWL 199
Cdd:cd02997  81 YFENGKFVEKYEGERTAEDIIEFM 104
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 440-541 1.02e-26

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


Pssm-ID: 239259 [Multi-domain]  Cd Length: 101  Bit Score: 104.23  E-value: 1.02e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 440 KVIVGNNFDEIVLDeSKDVLLEIYAPWCGHCQSFEPIYNKLGKYLKGIDSLVVAKMDGTSN-EHP-RAKADGFPTILFFP 517
Cdd:cd02961   1 VELTDDNFDELVKD-SKDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGKVVVAKVDCTANnDLCsEYGVRGYPTIKLFP 79

                        90       100
                ....*....|....*....|....
gi 22331799 518 GGNKsfDPIAVDVDRTVVELYKFL 541
Cdd:cd02961  80 NGSK--EPVKYEGPRTLESLVEFI 101
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 104-196 1.29e-24

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: 98.59  E-value: 1.29e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 104 LTKDNFTEFV-GNNSFAMVEFYAPWCGACQALTPEYAAAATELKGLAALAKIDATEEG--DLAQKYEIQGFPTVFLF--- 177
Cdd:cd03002   5 LTPKNFDKVVhNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKELDGLVQVAAVDCDEDKnkPLCGKYGVQGFPTLKVFrpp 84

                        90       100
                ....*....|....*....|.
gi 22331799 178 --VDGEMRKTYEGERTKDGIV 196
Cdd:cd03002  85 kkASKHAVEDYNGERSAKAIV 105
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
242-416 6.89e-22

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 93.20  E-value: 6.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799   242 LAAASRLEDDLSFYQTASPDIAKLFeietQVKRPALVLLKKEEEKLARFDGN-FTKTAIAEFVSANKVPLVINFTREGAS 320
Cdd:pfam13848  13 RKAAKELKGDVRFGITFSKEVADKY----NIKEPAILLFRKFDEETVHYPGDsINFEDLKKFIQKNCLPLVREFTPENAE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799   321 LIFESSVKNQLILFAKAN--ESEKHLPTLREVAKSFKGKFVFVYVQMDNEDYgeaVSGFFGVTGA-APKVLVYTGNEDMR 397
Cdd:pfam13848  89 ELFEEGIPPLLLLFLKKDdeSTEEFKKALEKVAKKFRGKINFALVDAKSFGR---PLEYFGLSESdLPVIVIVDSFSHMY 165

                         170
                  ....*....|....*....
gi 22331799   398 KFILDGELTVNNIKTLAED 416
Cdd:pfam13848 166 KYFPSDEFSPESLKEFIND 184
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 100-199 7.19e-22

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: 90.39  E-value: 7.19e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 100 DVAVLTKDNFTEFVGNNSF-AMVEFYAPWCGACQALTPEYAAAATELKGLAAL--AKIDATEEG-DLAQKYEIQGFPTVF 175
Cdd:cd02998   1 NVVELTDSNFDKVVGDDKKdVLVEFYAPWCGHCKNLAPEYEKLAAVFANEDDVviAKVDADEANkDLAKKYGVSGFPTLK 80

                        90       100
                ....*....|....*....|....*
gi 22331799 176 LFVDGEMR-KTYEGERTKDGIVTWL 199
Cdd:cd02998  81 FFPKGSTEpVKYEGGRDLEDLVKFV 105
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 101-199 2.23e-21

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: 89.27  E-value: 2.23e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 101 VAVLTKDNFTEFVGNNS-FAMVEFYAPWCGACQALTPEYAAAATELKGLAALAKIDATEEGDLAQKYEIQGFPTVFLFVD 179
Cdd:cd03004   3 VITLTPEDFPELVLNRKePWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLYPG 82

                        90       100
                ....*....|....*....|..
gi 22331799 180 GEMR-KTYEGE-RTKDGIVTWL 199
Cdd:cd03004  83 NASKyHSYNGWhRDADSILEFI 104
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 107-200 7.89e-21

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: 87.23  E-value: 7.89e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 107 DNFTEFVGNNSFAMVEFYAPWCGACQALTPEYAAAATElKGLAALAKIDATEEGDLAQKYEIQGFPTVFLFVDGEMRKTY 186
Cdd:cd02947   1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEE-YPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRV 79

                        90
                ....*....|....
gi 22331799 187 EGERTKDGIVTWLK 200
Cdd:cd02947  80 VGADPKEELEEFLE 93
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 439-524 1.13e-20

Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 86.90  E-value: 1.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799   439 VKVIVGNNFDEIVLDESKDVLLEIYAPWCGHCQSFEPIYNKLGKYLKGIdsLVVAKMDGTSNEHPRAKAD--GFPTILFF 516
Cdd:pfam00085   2 VVVLTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGN--VVFAKVDVDENPDLASKYGvrGYPTLIFF 79


                  ....*...
gi 22331799   517 PGGNKSFD 524
Cdd:pfam00085  80 KNGQPVDD 87
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 104-201 1.36e-20

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


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 86.96  E-value: 1.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799   104 LTKDNFTEFV-GNNSFAMVEFYAPWCGACQALTPEYAAAATELKGLAALAKIDATEEGDLAQKYEIQGFPTVFLFVDGEM 182
Cdd:TIGR01068   1 LTDANFDETIaSSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKE 80

                          90
                  ....*....|....*....
gi 22331799   183 RKTYEGERTKDGIVTWLKK 201
Cdd:TIGR01068  81 VDRSVGALPKAALKQLINK 99
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 72-204 7.63e-20

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: 92.43  E-value: 7.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799    72 DDLEQGGGEFHHGDHG--YEEEPLPPVDEKDVAVLTKDNFTEFVGNNSF-AMVEFYAPWCGACQALTPEYAAAATELKGL 148
Cdd:TIGR01130 317 ENLEAFVKDFLDGKLKpyLKSEPIPEDDEGPVKVLVGKNFDEIVLDETKdVLVEFYAPWCGHCKNLAPIYEELAEKYKDA 396

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331799   149 ---AALAKIDATEEgDLAqKYEIQGFPTVFLFVDGEMRK--TYEGERTKDGIVTWLKKKAS 204
Cdd:TIGR01130 397 esdVVIAKMDATAN-DVP-PFEVEGFPTIKFVPAGKKSEpvPYDGDRTLEDFSKFIAKHAT 455
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 101-199 3.52e-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: 82.99  E-value: 3.52e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 101 VAVLTKDNFTEFVGNNSFAM-VEFYAPWCGACQALTPEYAAAATELKGLAAL--AKIDATEEgDLAQKYEIQGFPTVFLF 177
Cdd:cd02995   2 VKVVVGKNFDEVVLDSDKDVlVEFYAPWCGHCKALAPIYEELAEKLKGDDNVviAKMDATAN-DVPSEFVVDGFPTILFF 80

                        90       100
                ....*....|....*....|....
gi 22331799 178 VDGEMRK--TYEGERTKDGIVTWL 199
Cdd:cd02995  81 PAGDKSNpiKYEGDRTLEDLIKFI 104
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 107-203 3.39e-18

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: 80.19  E-value: 3.39e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 107 DNFTEfVGNNSFAMVEFYAPWCGACQALTPEYAAAATELKGLAA---LAKIDATEEGDLAQKYEIQGFPTVfLFVDGEMR 183
Cdd:cd03000   7 DSFKD-VRKEDIWLVDFYAPWCGHCKKLEPVWNEVGAELKSSGSpvrVGKLDATAYSSIASEFGVRGYPTI-KLLKGDLA 84

                        90       100
                ....*....|....*....|
gi 22331799 184 KTYEGERTKDGIVTWLKKKA 203
Cdd:cd03000  85 YNYRGPRTKDDIVEFANRVA 104
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 438-522 9.42e-18

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: 78.87  E-value: 9.42e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 438 DVKVIVGNNFDEIVLDESKDVLLEIYAPWCGHCQSFEPIYNKLGKYLKGIDSLVVAKMDGTSNEHPRAKADGFPTILFFP 517
Cdd:cd03001   1 DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVFG 80


                ....*
gi 22331799 518 GGNKS 522
Cdd:cd03001  81 AGKNS 85
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 100-201 3.78e-17

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: 77.03  E-value: 3.78e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 100 DVAVLTKDNFTEFVGNNSfaMVEFYAPWCGACQALTPEYAAAATELKGLA-ALAKIDATEEGDLAQKYEIQGFPTVFLFV 178
Cdd:cd02994   2 NVVELTDSNWTLVLEGEW--MIEFYAPWCPACQQLQPEWEEFADWSDDLGiNVAKVDVTQEPGLSGRFFVTALPTIYHAK 79

                        90       100
                ....*....|....*....|...
gi 22331799 179 DGEMRKtYEGERTKDGIVTWLKK 201
Cdd:cd02994  80 DGVFRR-YQGPRDKEDLISFIEE 101
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 104-199 6.55e-17

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


Pssm-ID: 239303 [Multi-domain]  Cd Length: 102  Bit Score: 76.17  E-value: 6.55e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 104 LTKDNFTEFVGN-NSFamVEFYAPWCGACQALTPEYAAAATEL-KGLAA--LAKIDATEEGDLAQKYEIQGFPTVFLFVD 179
Cdd:cd03005   5 LTEDNFDHHIAEgNHF--VKFFAPWCGHCKRLAPTWEQLAKKFnNENPSvkIAKVDCTQHRELCSEFQVRGYPTLLLFKD 82

                        90       100
                ....*....|....*....|
gi 22331799 180 GEMRKTYEGERTKDGIVTWL 199
Cdd:cd03005  83 GEKVDKYKGTRDLDSLKEFV 102
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 97-191 1.21e-16

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 79.28  E-value: 1.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799   97 DEKDVAVLTKDNFTEFVGNNSFA-----MVEFYAPWCGACQALTPEYAAAATELKGLAALAKIDATEEGDLAQKYEIQGF 171
Cdd:PTZ00443  28 DANALVLLNDKNFEKLTQASTGAttgpwFVKFYAPWCSHCRKMAPAWERLAKALKGQVNVADLDATRALNLAKRFAIKGY 107

                         90       100
                 ....*....|....*....|
gi 22331799  172 PTVFLFVDGEMRKTYEGERT 191
Cdd:PTZ00443 108 PTLLLFDKGKMYQYEGGDRS 127
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 99-195 4.47e-15

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: 71.27  E-value: 4.47e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799  99 KDVAVLTKDNFTEFVGNNSFAMVEFYAPWCGACQALTPEYAAAATELK------GLAALAKIDATEEGDLAQKYEIQGFP 172
Cdd:cd02996   1 SEIVSLTSGNIDDILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKeefpdaGKVVWGKVDCDKESDIADRYRINKYP 80

                        90       100
                ....*....|....*....|....
gi 22331799 173 TVFLFVDGEM-RKTYEGERTKDGI 195
Cdd:cd02996  81 TLKLFRNGMMmKREYRGQRSVEAL 104
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 446-547 1.66e-14

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


Pssm-ID: 239300 [Multi-domain]  Cd Length: 109  Bit Score: 69.70  E-value: 1.66e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 446 NFDEIVLDESKDVLLEIYAPWCGHCQSFEPIYNKLGKYLKGIDSLVVAKMDGTSNEHPRAKAD--GFPTILFFPGGNKsf 523
Cdd:cd03002   9 NFDKVVHNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKELDGLVQVAAVDCDEDKNKPLCGKYGvqGFPTLKVFRPPKK-- 86

                        90       100
                ....*....|....*....|....
gi 22331799 524 dpiavdVDRTVVELYKFLKKHASI 547
Cdd:cd03002  87 ------ASKHAVEDYNGERSAKAI 104
PDI_b_family cd02981
Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of ...
 207-306 2.71e-14

Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; 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, calsequestrin and other PDI-related proteins like ERp72, ERp57, ERp44 and PDIR. PDI, ERp57 (or ERp60), ERp72 and PDIR 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 contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and one or more redox inactive TRX-like (b) domains. The molecular structure of PDI is abb'a'. Also included in this family is the PDI-related protein ERp27, which contains only redox-inactive TRX-like (b and b') domains. The redox inactive b domains are implicated in substrate recognition.


Pssm-ID: 239279  Cd Length: 97  Bit Score: 68.90  E-value: 2.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 207 IHNITTKEEAERVLSAEPKLVFGFLNSLVGSESEEL-AAASRLEDDLSFYQTASPDIAKLFEietqVKRPALVLLKKEEE 285
Cdd:cd02981   1 VKELTSKEELEKFLDKDDVVVVGFFKDEESEEYKTFeKVAESLRDDYGFGHTSDKEVAKKLK----VKPGSVVLFKPFEE 76

                        90       100
                ....*....|....*....|.
gi 22331799 286 KLARFDGNFTKTAIAEFVSAN 306
Cdd:cd02981  77 EPVEYDGEFTEESLVEFIKDN 97
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 446-544 2.42e-13

Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 66.38  E-value: 2.42e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 446 NFDEIVLDESKDVLLEIYAPWCGHCQSFEPIYNKLGKYLKGidSLVVAKMDgtSNEHP----RAKADGFPTILFFPGGNK 521
Cdd:COG3118   9 NFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGG--KVKFVKVD--VDENPelaaQFGVRSIPTLLLFKDGQP 84

                        90       100
                ....*....|....*....|....*...
gi 22331799 522 sfdpiavdVDRTV-----VELYKFLKKH 544
Cdd:COG3118  85 --------VDRFVgalpkEQLREFLDKV 104
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 439-522 3.77e-13

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: 65.77  E-value: 3.77e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 439 VKVIVGNNFDEIVldESKDVLLEIYAPWCGHCQSFEPIYNKLG-KYLKGIDSLVVAKMDGTS-----NEHpraKADGFPT 512
Cdd:cd03005   2 VLELTEDNFDHHI--AEGNHFVKFFAPWCGHCKRLAPTWEQLAkKFNNENPSVKIAKVDCTQhrelcSEF---QVRGYPT 76

                        90
                ....*....|
gi 22331799 513 ILFFPGGNKS 522
Cdd:cd03005  77 LLLFKDGEKV 86
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 452-519 4.74e-13

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: 65.55  E-value: 4.74e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 452 LDES-KDV------LLEIYAPWCGHCQSFEPIYNKLGKYLKGIDSLV-VAKMDGTSneHPRA----KADGFPTILFFPGG 519
Cdd:cd03000   5 LDDSfKDVrkediwLVDFYAPWCGHCKKLEPVWNEVGAELKSSGSPVrVGKLDATA--YSSIasefGVRGYPTIKLLKGD 82
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 456-523 1.13e-12

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: 64.40  E-value: 1.13e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331799 456 KDVLLEIYAPWCGHCQSFEPIYNKLGKYLKGiDSLVVAKMDGTSNEHPRAKADG----FPTILFFPGGNKSF 523
Cdd:cd02993  22 QSTLVVLYAPWCPFCQAMEASYEELAEKLAG-SNVKVAKFNADGEQREFAKEELqlksFPTILFFPKNSRQP 92
PRK10996 PRK10996
thioredoxin 2; Provisional
 105-199 1.25e-12

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 65.48  E-value: 1.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799  105 TKDNFTEFVGNNSFAMVEFYAPWCGACQALTPEYAAAATELKGLAALAKIDATEEGDLAQKYEIQGFPTVFLFVDGEMRK 184
Cdd:PRK10996  41 TGETLDKLLQDDLPVVIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFKNGQVVD 120

                         90
                 ....*....|....*
gi 22331799  185 TYEGERTKDGIVTWL 199
Cdd:PRK10996 121 MLNGAVPKAPFDSWL 135
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 438-524 1.83e-12

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


Pssm-ID: 239295 [Multi-domain]  Cd Length: 104  Bit Score: 63.88  E-value: 1.83e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 438 DVKVIVGNNFDEIvLDESKDVLLEIYAPWCGHCQSFEPIYNKLGKYLKGIDSLVVAKMDGTSNEHPRAKAD----GFPTI 513
Cdd:cd02997   1 DVVHLTDEDFRKF-LKKEKHVLVMFYAPWCGHCKKMKPEFTKAATELKEDGKGVLAAVDCTKPEHDALKEEynvkGFPTF 79

                        90
                ....*....|.
gi 22331799 514 LFFPGGNKSFD 524
Cdd:cd02997  80 KYFENGKFVEK 90
PTZ00051 PTZ00051
thioredoxin; Provisional
 103-188 5.93e-12

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 62.20  E-value: 5.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799  103 VLTKDNFTEFVGNNSFAMVEFYAPWCGACQALTPEYAAAATELKGLaALAKIDATEEGDLAQKYEIQGFPTVFLFVDGEM 182
Cdd:PTZ00051   5 VTSQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKM-VFVKVDVDELSEVAEKENITSMPTFKVFKNGSV 83


                 ....*.
gi 22331799  183 RKTYEG 188
Cdd:PTZ00051  84 VDTLLG 89
trxA PRK09381
thioredoxin TrxA;
104-199 9.00e-12

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 62.00  E-value: 9.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799  104 LTKDNF-TEFVGNNSFAMVEFYAPWCGACQALTPEYAAAATELKGLAALAKIDATEEGDLAQKYEIQGFPTVFLFVDGEM 182
Cdd:PRK09381   8 LTDDSFdTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEV 87

                         90
                 ....*....|....*..
gi 22331799  183 RKTYEGERTKDGIVTWL 199
Cdd:PRK09381  88 AATKVGALSKGQLKEFL 104
PDI_b'_family cd02982
Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of ...
 318-418 1.10e-11

Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; 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, calsequestrin and other PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5 and PDIR. PDI, ERp57, ERp72, P5 and PDIR 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 contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and one or more redox inactive TRX-like (b) domains. The molecular structure of PDI is abb'a'. Also included in this family is the PDI-related protein ERp27, which contains only redox-inactive TRX-like (b and b') domains. The redox inactive domains are implicated in substrate recognition with the b' domain serving as the primary substrate binding site. Only the b' domain is necessary for the binding of small peptide substrates. In addition to the b' domain, other domains are required for the binding of larger polypeptide substrates. The b' domain is also implicated in chaperone activity.


Pssm-ID: 239280 [Multi-domain]  Cd Length: 103  Bit Score: 61.52  E-value: 1.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 318 GASLIFESSV--KNQLILFAKANE--SEKHLPTLREVAKSFKGKFVFVYVqmDNEDYGeAVSGFFGVTGAAPKVLVYTGN 393
Cdd:cd02982   1 NAETFFNYEEsgKPLLVLFYNKDDseSEELRERFKEVAKKFKGKLLFVVV--DADDFG-RHLEYFGLKEEDLPVIAIINL 77

                        90       100
                ....*....|....*....|....*.
gi 22331799 394 EDMRKFILDGE-LTVNNIKTLAEDFL 418
Cdd:cd02982  78 SDGKKYLMPEEeLTAESLEEFVEDFL 103
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 101-177 1.31e-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: 61.52  E-value: 1.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 101 VAVLTKDNFTEFV-GNNSFAMVEFYAPWCGACQALTPEYAAAATELK---GLAALAKIDATEE--GDLAQKYEIQGFPTV 174
Cdd:cd02992   3 VIVLDAASFNSALlGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRkwrPVVRVAAVDCADEenVALCRDFGVTGYPTL 82


                ...
gi 22331799 175 FLF 177
Cdd:cd02992  83 RYF 85
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 446-523 1.94e-11

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: 60.77  E-value: 1.94e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 446 NFDEIVLDESKDVLLEIYAPWCGHCQSFEPIYNKLGKYLKGIdsLVVAKMDGTSNEHPRAKAD--GFPTILFFPGGNKSF 523
Cdd:cd03004  10 DFPELVLNRKEPWLVDFYAPWCGPCQALLPELRKAARALKGK--VKVGSVDCQKYESLCQQANirAYPTIRLYPGNASKY 87
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 121-180 2.14e-11

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: 60.36  E-value: 2.14e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 121 VEFYAPWCGACQALTPEYAAAATELKGLAALAKIDATEEGDLAQKYEIQGFPTVFLFVDG 180
Cdd:cd02956  17 VDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAG 76
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 446-521 5.95e-11

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: 59.23  E-value: 5.95e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331799   446 NFDEIVLDESKDVLLEIYAPWCGHCQSFEPIYNKLGKYLKGidSLVVAKMDGTSNEHPRAKAD--GFPTILFFPGGNK 521
Cdd:TIGR01068   5 NFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEG--KVKFVKLNVDENPDIAAKYGirSIPTLLLFKNGKE 80
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 120-201 1.10e-10

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 59.70  E-value: 1.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 120 MVEFYAPWCGACQALTPEYAAAATELKGL---------------AALAKIDAT------EEGDLAQKYEIQGFPTVFLF- 177
Cdd:COG0526  32 LVNFWATWCPPCRAEMPVLKELAEEYGGVvfvgvdvdenpeavkAFLKELGLPypvlldPDGELAKAYGVRGIPTTVLId 111

                        90       100
                ....*....|....*....|....
gi 22331799 178 VDGEMRKTYEGERTKDGIVTWLKK 201
Cdd:COG0526 112 KDGKIVARHVGPLSPEELEEALEK 135
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 439-537 5.37e-10

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: 56.89  E-value: 5.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 439 VKVIVGNNFDEIVLDESKDVLLEIYAPWCGHCQSFEPIYNKLGKYLKGIDSLV-VAKMD-------GTSNEHpraKADGF 510
Cdd:cd02992   3 VIVLDAASFNSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRKWRPVVrVAAVDcadeenvALCRDF---GVTGY 79

                        90       100
                ....*....|....*....|....*....
gi 22331799 511 PTILFFPGGNKSFD--PIAVDVDRTVVEL 537
Cdd:cd02992  80 PTLRYFPPFSKEATdgLKQEGPERDVNEL 108
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 100-196 2.71e-09

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: 54.45  E-value: 2.71e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 100 DVAVLTKDNFTEFVGNNSFAMVEFYAPWCGACQALTPEYAAAATELKGLAALAKIDATEEGDLAQKYEIQGFPTVFLFVD 179
Cdd:cd03003   2 EIVTLDRGDFDAAVNSGEIWFVNFYSPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDDRMLCRSQGVNSYPSLYVFPS 81

                        90
                ....*....|....*..
gi 22331799 180 GEMRKTYEGERTKDGIV 196
Cdd:cd03003  82 GMNPEKYYGDRSKESLV 98
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 446-521 3.00e-09

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


Pssm-ID: 239245 [Multi-domain]  Cd Length: 93  Bit Score: 54.10  E-value: 3.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 446 NFDEIVlDESKDVLLEIYAPWCGHCQSFEPIYNKLGKYLkgiDSLVVAKMDgtSNEHP----RAKADGFPTILFFPGGNK 521
Cdd:cd02947   2 EFEELI-KSAKPVVVDFWAPWCGPCKAIAPVLEELAEEY---PKVKFVKVD--VDENPelaeEYGVRSIPTFLFFKNGKE 75
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 120-184 3.49e-08

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: 50.39  E-value: 3.49e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331799 120 MVEFYAPWCGACQALTPEYAAAATELKGLaALAKIDATEEGDL---AQKYEIQGFPTVFLFVDGEMRK 184
Cdd:cd01659   1 LVLFYAPWCPFCQALRPVLAELALLNKGV-KFEAVDVDEDPALekeLKRYGVGGVPTLVVFGPGIGVK 67
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 459-519 1.82e-07

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 52.32  E-value: 1.82e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331799  459 LLEIYAPWCGHCQSFEPIYNKLGKYLKGIdsLVVAKMDGTSNEH--PRAKADGFPTILFFPGG 519
Cdd:PTZ00443  56 FVKFYAPWCSHCRKMAPAWERLAKALKGQ--VNVADLDATRALNlaKRFAIKGYPTLLLFDKG 116
PLN02309 PLN02309
5'-adenylylsulfate reductase
 455-523 2.37e-07

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 53.25  E-value: 2.37e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331799  455 SKDVLLEIYAPWCGHCQSFEPIYNKLGKYLKGiDSLVVAKMDGTSNEHPRAKAD----GFPTILFFPGGNKSF 523
Cdd:PLN02309 365 KEPWLVVLYAPWCPFCQAMEASYEELAEKLAG-SGVKVAKFRADGDQKEFAKQElqlgSFPTILLFPKNSSRP 436
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 120-192 6.64e-07

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: 47.88  E-value: 6.64e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331799 120 MVEFYAPWCGACQALTPEYAAAATELKGLAALAKIDATEEGDLAQKYEIQGFPTVFLFVDGEMRKTYEGERTK 192
Cdd:cd02949  17 LVLYTSPTCGPCRTLKPILNKVIDEFDGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDKELVKEISGVKMK 89
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 452-541 1.09e-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: 51.17  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799   452 LDESKDV-LLEIYAPWCGHCQSFEPIYNKLGKYLKGiDSLVVAKMDGTSNEHPRAKAD----GFPTILFFPggNKSFDPI 526
Cdd:TIGR00424 367 LEERKEAwLVVLYAPWCPFCQAMEASYLELAEKLAG-SGVKVAKFRADGDQKEFAKQElqlgSFPTILFFP--KHSSRPI 443

                          90
                  ....*....|....*.
gi 22331799   527 AVDVD-RTVVELYKFL 541
Cdd:TIGR00424 444 KYPSEkRDVDSLMSFV 459
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 99-199 1.15e-06

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


Pssm-ID: 239291 [Multi-domain]  Cd Length: 109  Bit Score: 47.45  E-value: 1.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799  99 KDVAVLTKDNFTEFVG---NNSFAMVEFYAPWCGACQALTPEYAAAATELKGLAA-LAKIDATEEGDLAQKYEIQ--GFP 172
Cdd:cd02993   1 EAVVTLSRAEIEALAKgerRNQSTLVVLYAPWCPFCQAMEASYEELAEKLAGSNVkVAKFNADGEQREFAKEELQlkSFP 80

                        90       100
                ....*....|....*....|....*....
gi 22331799 173 TVFLFVDGEMRK-TYEGE-RTKDGIVTWL 199
Cdd:cd02993  81 TILFFPKNSRQPiKYPSEqRDVDSLLMFV 109
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 105-188 2.66e-06

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


Pssm-ID: 239282 [Multi-domain]  Cd Length: 97  Bit Score: 46.11  E-value: 2.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 105 TKDNFTEFVGNN--SFAMVEFYAPWCGACQALTPEYAAAATELKGLAALAKIDATEEGDLAQKYEIQGFPTVFLFVDGEM 182
Cdd:cd02984   1 SEEEFEELLKSDasKLLVLHFWAPWAEPCKQMNQVFEELAKEAFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTI 80


                ....*.
gi 22331799 183 RKTYEG 188
Cdd:cd02984  81 VDRVSG 86
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 120-188 2.83e-06

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: 46.46  E-value: 2.83e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 120 MVEFYAPWCGACQALTPEYAAAATELKG------------------LAALAKIDAT------EEGDLAQKYEIQGFPTVF 175
Cdd:cd02966  23 LVNFWASWCPPCRAEMPELEALAKEYKDdgvevvgvnvddddpaavKAFLKKYGITfpvlldPDGELAKAYGVRGLPTTF 102

                        90
                ....*....|....
gi 22331799 176 LF-VDGEMRKTYEG 188
Cdd:cd02966 103 LIdRDGRIRARHVG 116
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 437-500 4.21e-06

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


Pssm-ID: 239292 [Multi-domain]  Cd Length: 101  Bit Score: 45.45  E-value: 4.21e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22331799 437 GDVKVIVGNNFDEIVLDESkdvLLEIYAPWCGHCQSFEPIYNKLGKYLKGIDsLVVAKMDGTSN 500
Cdd:cd02994   1 SNVVELTDSNWTLVLEGEW---MIEFYAPWCPACQQLQPEWEEFADWSDDLG-INVAKVDVTQE 60
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
114-199 8.12e-06

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 44.72  E-value: 8.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799   114 GNNSFAMVEFYAPWCGACQAL--------------TPEYAAAATELKGLA--ALAKIDATEEGDLAQKYEIQGFPTVFLF 177
Cdd:pfam13098   2 GNGKPVLVVFTDPDCPYCKKLkkelledpdvtvylGPNFVFIAVNIWCAKevAKAFTDILENKELGRKYGVRGTPTIVFF 81

                          90       100
                  ....*....|....*....|...
gi 22331799   178 vDGEMRKT-YEGERTKDGIVTWL 199
Cdd:pfam13098  82 -DGKGELLrLPGYVPAEEFLALL 103
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 115-196 1.24e-05

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: 44.27  E-value: 1.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 115 NNSFAMVeFYAPWCGACQALTPEYAAAATELKGLAALAkIDATEE-GDLAQKYEIQGFPTVFLFvDGEMRKTYEGERTKD 193
Cdd:cd02999  18 EDYTAVL-FYASWCPFSASFRPHFNALSSMFPQIRHLA-IEESSIkPSLLSRYGVVGFPTILLF-NSTPRVRYNGTRTLD 94


                ...
gi 22331799 194 GIV 196
Cdd:cd02999  95 SLA 97
trxA PRK09381
thioredoxin TrxA;
442-519 1.26e-05

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 44.28  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799  442 IVGNNFDEIVLDESKDVLLEIYAPWCGHCQSFEPIYNKLGKYLKGidSLVVAKM--DGTSNEHPRAKADGFPTILFFPGG 519
Cdd:PRK09381   8 LTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQG--KLTVAKLniDQNPGTAPKYGIRGIPTLLLFKNG 85
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 459-521 1.30e-05

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


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 43.07  E-value: 1.30e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331799 459 LLEIYAPWCGHCQSFEPIYNKLGKYLKGIdslVVAKMDGTSNEHPRAKA-----DGFPTILFFPGGNK 521
Cdd:cd01659   1 LVLFYAPWCPFCQALRPVLAELALLNKGV---KFEAVDVDEDPALEKELkrygvGGVPTLVVFGPGIG 65
DsbD COG4232
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ...
 120-201 2.16e-05

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


Pssm-ID: 443376 [Multi-domain]  Cd Length: 416  Bit Score: 47.11  E-value: 2.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 120 MVEFYAPWCGACQAL------TPEYAAAateLKGLAALAKIDAT----EEGDLAQKYEIQGFPTVFLFV-DGEMRKTYEG 188
Cdd:COG4232 324 FVDFTADWCVTCKENertvfsDPEVQAA---LADDVVLLKADVTdndpEITALLKRFGRFGVPTYVFYDpDGEELPRLGF 400

                        90
                ....*....|...
gi 22331799 189 ERTKDGIVTWLKK 201
Cdd:COG4232 401 MLTADEFLAALEK 413
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 115-193 2.82e-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: 44.25  E-value: 2.82e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 115 NNSFAMVEFYAPWCGACQALTPEYAAAATELKGLA--ALAKIDATEEGDLAQKYEIQGFPT-VFLFVDGEMRKTYEGERT 191
Cdd:cd02950  19 NGKPTLVEFYADWCTVCQEMAPDVAKLKQKYGDQVnfVMLNVDNPKWLPEIDRYRVDGIPHfVFLDREGNEEGQSIGLQP 98


                ..
gi 22331799 192 KD 193
Cdd:cd02950  99 KQ 100
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 119-195 3.74e-05

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


Pssm-ID: 239309 [Multi-domain]  Cd Length: 123  Bit Score: 43.44  E-value: 3.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 119 AMVEFYAPWCGACQALTPE--YAAAATELKGLAALAKID-----------------ATEEGDLAQKYEIQGFPTVFLFVD 179
Cdd:cd03011  23 VLVYFWATWCPVCRFTSPTvnQLAADYPVVSVALRSGDDgavarfmqkkgygfpviNDPDGVISARWGVSVTPAIVIVDP 102

                        90
                ....*....|....*.
gi 22331799 180 GEMRKTYEGERTKDGI 195
Cdd:cd03011 103 GGIVFVTTGVTSEWGL 118
PRK10996 PRK10996
thioredoxin 2; Provisional
 436-477 4.37e-05

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 43.52  E-value: 4.37e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 22331799  436 DGDVKVIVGNNFDEIvLDESKDVLLEIYAPWCGHCQSFEPIY 477
Cdd:PRK10996  34 DGEVINATGETLDKL-LQDDLPVVIDFWAPWCGPCRNFAPIF 74
PLN02309 PLN02309
5'-adenylylsulfate reductase
 120-177 7.02e-05

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 45.55  E-value: 7.02e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331799  120 MVEFYAPWCGACQALTPEYAAAATELKGLAA-LAKIDA-TEEGDLA-QKYEIQGFPTVFLF 177
Cdd:PLN02309 369 LVVLYAPWCPFCQAMEASYEELAEKLAGSGVkVAKFRAdGDQKEFAkQELQLGSFPTILLF 429
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 120-177 8.86e-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: 8.86e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331799   120 MVEFYAPWCGACQALTPEYAAAATELKGLAA-LAKIDATEEGDLAQKYEIQ--GFPTVFLF 177
Cdd:TIGR00424 375 LVVLYAPWCPFCQAMEASYLELAEKLAGSGVkVAKFRADGDQKEFAKQELQlgSFPTILFF 435
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
120-194 1.33e-04

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 42.16  E-value: 1.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 120 MVEFYAPWCGACQALTPEYAAAATELKGL----------------AALAKIDAT------EEGDLAQKYEIQGFPTVFLF 177
Cdd:COG1225  25 VLYFYATWCPGCTAELPELRDLYEEFKDKgvevlgvssdsdeahkKFAEKYGLPfpllsdPDGEVAKAYGVRGTPTTFLI 104

                        90
                ....*....|....*...
gi 22331799 178 -VDGEMRKTYEGERTKDG 194
Cdd:COG1225 105 dPDGKIRYVWVGPVDPRP 122
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 120-201 2.78e-04

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 41.43  E-value: 2.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 120 MVEFYAPWCGACQAL------TPEYAAAateLKGLAALAKIDA-------------TEEGDLAQKYEIQGFPT-VFLFVD 179
Cdd:COG2143  44 LLFFESDWCPYCKKLhkevfsDPEVAAY---LKENFVVVQLDAegdkevtdfdgetLTEKELARKYGVRGTPTlVFFDAE 120

                        90       100
                ....*....|....*....|..
gi 22331799 180 GEMRKTYEGERTKDGIVTWLKK 201
Cdd:COG2143 121 GKEIARIPGYLKPETFLALLKY 142
DsbDgamma cd02953
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
 120-177 3.68e-04

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


Pssm-ID: 239251 [Multi-domain]  Cd Length: 104  Bit Score: 39.89  E-value: 3.68e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331799 120 MVEFYAPWCGACQAL------TPEYAAAateLKGLAALAKIDATEEGD----LAQKYEIQGFPTVFLF 177
Cdd:cd02953  15 FVDFTADWCVTCKVNekvvfsDPEVQAA---LKKDVVLLRADWTKNDPeitaLLKRFGVFGPPTYLFY 79
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 447-519 7.00e-04

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: 39.26  E-value: 7.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331799 447 FDEIVLDESKD---------VLLEIYAPWCGHCQSFEPIYNKLGKYLKGIDSLVVAKmdgtSNEHPRAKAD----GFPTI 513
Cdd:cd02999   1 PPEEVLNIALDlmafnredyTAVLFYASWCPFSASFRPHFNALSSMFPQIRHLAIEE----SSIKPSLLSRygvvGFPTI 76


                ....*.
gi 22331799 514 LFFPGG 519
Cdd:cd02999  77 LLFNST 82
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH