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Conserved domains on  [gi|1851984901|gb|EAN33373|]
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Protein disulfide-isomerase A4 [Theileria parva strain Muguga]

Protein Classification

protein disulfide isomerase family protein( domain architecture ID 13519640)

protein disulfide isomerase (PDI) family protein belongs to the thioredoxin superfamily, and 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

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List of domain hits

 Name Accession Description Interval E-value
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 386-488 4.19e-37

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: 132.29  E-value: 4.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 386 PVKTIVGEDFHRRVIESKDDILVLFLSSWCGHCHKAKRVFRDMGRRLKGSNGPILATFDAYNNEVEDMEISQ-FPTIALF 464
Cdd:cd02995     1 PVKVVVGKNFDEVVLDSDKDVLVEFYAPWCGHCKALAPIYEELAEKLKGDDNVVIAKMDATANDVPSEFVVDgFPTILFF 80

                          90       100
                  ....*....|....*....|....
gi 1851984901 465 QSGNKSDPVFYNGPDNLEDISLFL 488
Cdd:cd02995    81 PAGDKSNPIKYEGDRTLEDLIKFI 104
ER_PDI_fam super family cl36828
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 101-491 5.79e-34

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


The actual alignment was detected with superfamily member TIGR01130:

Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 133.65  E-value: 5.79e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 101 PVLTYVKDGE--TKKYDGPINPGYIMSWLSNQNvcEMRVKDLSNFKSFQKSLPSGHVQVLVLFAEHDPKLVETVRSFiAE 178
Cdd:TIGR01130  77 PTLKIFRNGEdsVSDYNGPRDADGIVKYMKKQS--GPAVKEIETVADLEAFLADDDVVVIGFFKDLDSELNDTFLSV-AE 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 179 KDLAVPVLFSPEqtlSDqivKSLSQEGIKYPTLLIMRNMSLL--PKITFYTNDVRNKKELYEFLKEELIPPI----HSTN 252
Cdd:TIGR01130 154 KLRDVYFFFAHS---SD---VAAFAKLGAFPDSVVLFKPKDEdeKFSKVDGEMDTDVSDLEKFIRAESLPLVgeftQETA 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 253 SymlpmFLVMKKTIVYIYTRDKELKKYlSESWINT---VPRKHSEKLVFLHSKGSDLVENKMNTILAIDSDYEEIVVRaf 329
Cdd:TIGR01130 228 A-----KYFESGPLVVLYYNVDESLDP-FEELRNRfleAAKKFRGKFVNFAVADEEDFGRELEYFGLKAEKFPAVAIQ-- 299

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 330 viNLDTLEFYKFKPLTIEDGTISEqgmnrFIDDLENDRLSHYVKSElPIPENiDRGPVKTIVGEDFHRRVIESKDDILVL 409
Cdd:TIGR01130 300 --DLEGNKKYPMDQEEFSSENLEA-----FVKDFLDGKLKPYLKSE-PIPED-DEGPVKVLVGKNFDEIVLDETKDVLVE 370

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 410 FLSSWCGHCHKAKRVFRDMGRRLKGSN-GPILATFDAYNNEVEDMEISQFPTIALFQSGNKSDPVFYNGPDNLEDISLFL 488
Cdd:TIGR01130 371 FYAPWCGHCKNLAPIYEELAEKYKDAEsDVVIAKMDATANDVPPFEVEGFPTIKFVPAGKKSEPVPYDGDRTLEDFSKFI 450


                  ...
gi 1851984901 489 EKN 491
Cdd:TIGR01130 451 AKH 453
 
Name Accession Description Interval E-value
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 386-488 4.19e-37

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: 132.29  E-value: 4.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 386 PVKTIVGEDFHRRVIESKDDILVLFLSSWCGHCHKAKRVFRDMGRRLKGSNGPILATFDAYNNEVEDMEISQ-FPTIALF 464
Cdd:cd02995     1 PVKVVVGKNFDEVVLDSDKDVLVEFYAPWCGHCKALAPIYEELAEKLKGDDNVVIAKMDATANDVPSEFVVDgFPTILFF 80

                          90       100
                  ....*....|....*....|....
gi 1851984901 465 QSGNKSDPVFYNGPDNLEDISLFL 488
Cdd:cd02995    81 PAGDKSNPIKYEGDRTLEDLIKFI 104
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 101-491 5.79e-34

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


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 133.65  E-value: 5.79e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 101 PVLTYVKDGE--TKKYDGPINPGYIMSWLSNQNvcEMRVKDLSNFKSFQKSLPSGHVQVLVLFAEHDPKLVETVRSFiAE 178
Cdd:TIGR01130  77 PTLKIFRNGEdsVSDYNGPRDADGIVKYMKKQS--GPAVKEIETVADLEAFLADDDVVVIGFFKDLDSELNDTFLSV-AE 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 179 KDLAVPVLFSPEqtlSDqivKSLSQEGIKYPTLLIMRNMSLL--PKITFYTNDVRNKKELYEFLKEELIPPI----HSTN 252
Cdd:TIGR01130 154 KLRDVYFFFAHS---SD---VAAFAKLGAFPDSVVLFKPKDEdeKFSKVDGEMDTDVSDLEKFIRAESLPLVgeftQETA 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 253 SymlpmFLVMKKTIVYIYTRDKELKKYlSESWINT---VPRKHSEKLVFLHSKGSDLVENKMNTILAIDSDYEEIVVRaf 329
Cdd:TIGR01130 228 A-----KYFESGPLVVLYYNVDESLDP-FEELRNRfleAAKKFRGKFVNFAVADEEDFGRELEYFGLKAEKFPAVAIQ-- 299

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 330 viNLDTLEFYKFKPLTIEDGTISEqgmnrFIDDLENDRLSHYVKSElPIPENiDRGPVKTIVGEDFHRRVIESKDDILVL 409
Cdd:TIGR01130 300 --DLEGNKKYPMDQEEFSSENLEA-----FVKDFLDGKLKPYLKSE-PIPED-DEGPVKVLVGKNFDEIVLDETKDVLVE 370

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 410 FLSSWCGHCHKAKRVFRDMGRRLKGSN-GPILATFDAYNNEVEDMEISQFPTIALFQSGNKSDPVFYNGPDNLEDISLFL 488
Cdd:TIGR01130 371 FYAPWCGHCKNLAPIYEELAEKYKDAEsDVVIAKMDATANDVPPFEVEGFPTIKFVPAGKKSEPVPYDGDRTLEDFSKFI 450


                  ...
gi 1851984901 489 EKN 491
Cdd:TIGR01130 451 AKH 453
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 358-519 2.24e-21

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 97.13  E-value: 2.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 358 RFIDDLENDRLSHYVKSElPIPENIDrGPVKTIVGEDFHRRVIESKDDILVLFLSSWCGHCHKAKRVFRDMGRRLKGSNG 437
Cdd:PTZ00102  332 EFFKDVEAGKVEKSIKSE-PIPEEQD-GPVKVVVGNTFEEIVFKSDKDVLLEIYAPWCGHCKNLEPVYNELGEKYKDNDS 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 438 PILATFDAYNNE--VEDMEISQFPTIALFQSGNKsDPVFYNGPDNLEDISLFLEknckrnkvnaenilqKHVSQEQIFEF 515
Cdd:PTZ00102  410 IIVAKMNGTANEtpLEEFSWSAFPTILFVKAGER-TPIPYEGERTVEGFKEFVN---------------KHATNPFEDDT 473


                  ....
gi 1851984901 516 HTEL 519
Cdd:PTZ00102  474 HEEL 477
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 386-490 5.16e-08

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: 50.69  E-value: 5.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 386 PVKTIVGEDFHRRVIESKDDILVLFLSSWCGHCHKAKRVFRDMGRRLKGSngpilATF-----DAYNNEVEDMEISQFPT 460
Cdd:pfam00085   1 VVVVLTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGN-----VVFakvdvDENPDLASKYGVRGYPT 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 1851984901 461 IALFQSGNKSDpvFYNGPDNLEDISLFLEK 490
Cdd:pfam00085  76 LIFFKNGQPVD--DYVGARPKDALAAFLKA 103
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 387-491 2.61e-06

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: 45.97  E-value: 2.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 387 VKTIVGEDFHRRVIESKDDILVLFLSSWCGHCHKAKRVFRDMGRRLKGSNgpILATFDAYNNE--VEDMEISQFPTIALF 464
Cdd:COG3118     2 VVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKV--KFVKVDVDENPelAAQFGVRSIPTLLLF 79

                          90       100
                  ....*....|....*....|....*...
gi 1851984901 465 QSGNksdPVF-YNGPDNLEDISLFLEKN 491
Cdd:COG3118    80 KDGQ---PVDrFVGALPKEQLREFLDKV 104
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 399-490 2.77e-06

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: 49.67  E-value: 2.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 399 VIESKDDILVLFLSSWCGHCHKAKRVFRDMGRRLKGSNGPI-LATFDAYNNE--VEDMEISQFPTIALFQSGNKSdPVFY 475
Cdd:TIGR01130  14 FIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPPIkLAKVDATEEKdlAQKYGVSGYPTLKIFRNGEDS-VSDY 92

                          90
                  ....*....|....*
gi 1851984901 476 NGPDNLEDISLFLEK 490
Cdd:TIGR01130  93 NGPRDADGIVKYMKK 107
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
201-362 5.49e-03

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 38.11  E-value: 5.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 201 LSQEGIKYPTLLIMRNMSLlpKITFYTNDVRNKKELYEFLKEELIPPIHSTNSYMLPMFLVMKKTIVYIYTRDK---ELK 277
Cdd:pfam13848  34 ADKYNIKEPAILLFRKFDE--ETVHYPGDSINFEDLKKFIQKNCLPLVREFTPENAEELFEEGIPPLLLLFLKKddeSTE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 278 KYLSEswINTVPRKHSEKLVFLHSKGsDLVENKMNTILAIDSDYEEIVvrafVINLDTLEfYKFKPltieDGTISEQGMN 357
Cdd:pfam13848 112 EFKKA--LEKVAKKFRGKINFALVDA-KSFGRPLEYFGLSESDLPVIV----IVDSFSHM-YKYFP----SDEFSPESLK 179


                  ....*
gi 1851984901 358 RFIDD 362
Cdd:pfam13848 180 EFIND 184
 
Name Accession Description Interval E-value
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 386-488 4.19e-37

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: 132.29  E-value: 4.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 386 PVKTIVGEDFHRRVIESKDDILVLFLSSWCGHCHKAKRVFRDMGRRLKGSNGPILATFDAYNNEVEDMEISQ-FPTIALF 464
Cdd:cd02995     1 PVKVVVGKNFDEVVLDSDKDVLVEFYAPWCGHCKALAPIYEELAEKLKGDDNVVIAKMDATANDVPSEFVVDgFPTILFF 80

                          90       100
                  ....*....|....*....|....
gi 1851984901 465 QSGNKSDPVFYNGPDNLEDISLFL 488
Cdd:cd02995    81 PAGDKSNPIKYEGDRTLEDLIKFI 104
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 101-491 5.79e-34

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


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 133.65  E-value: 5.79e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 101 PVLTYVKDGE--TKKYDGPINPGYIMSWLSNQNvcEMRVKDLSNFKSFQKSLPSGHVQVLVLFAEHDPKLVETVRSFiAE 178
Cdd:TIGR01130  77 PTLKIFRNGEdsVSDYNGPRDADGIVKYMKKQS--GPAVKEIETVADLEAFLADDDVVVIGFFKDLDSELNDTFLSV-AE 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 179 KDLAVPVLFSPEqtlSDqivKSLSQEGIKYPTLLIMRNMSLL--PKITFYTNDVRNKKELYEFLKEELIPPI----HSTN 252
Cdd:TIGR01130 154 KLRDVYFFFAHS---SD---VAAFAKLGAFPDSVVLFKPKDEdeKFSKVDGEMDTDVSDLEKFIRAESLPLVgeftQETA 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 253 SymlpmFLVMKKTIVYIYTRDKELKKYlSESWINT---VPRKHSEKLVFLHSKGSDLVENKMNTILAIDSDYEEIVVRaf 329
Cdd:TIGR01130 228 A-----KYFESGPLVVLYYNVDESLDP-FEELRNRfleAAKKFRGKFVNFAVADEEDFGRELEYFGLKAEKFPAVAIQ-- 299

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 330 viNLDTLEFYKFKPLTIEDGTISEqgmnrFIDDLENDRLSHYVKSElPIPENiDRGPVKTIVGEDFHRRVIESKDDILVL 409
Cdd:TIGR01130 300 --DLEGNKKYPMDQEEFSSENLEA-----FVKDFLDGKLKPYLKSE-PIPED-DEGPVKVLVGKNFDEIVLDETKDVLVE 370

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 410 FLSSWCGHCHKAKRVFRDMGRRLKGSN-GPILATFDAYNNEVEDMEISQFPTIALFQSGNKSDPVFYNGPDNLEDISLFL 488
Cdd:TIGR01130 371 FYAPWCGHCKNLAPIYEELAEKYKDAEsDVVIAKMDATANDVPPFEVEGFPTIKFVPAGKKSEPVPYDGDRTLEDFSKFI 450


                  ...
gi 1851984901 489 EKN 491
Cdd:TIGR01130 451 AKH 453
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 358-519 2.24e-21

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 97.13  E-value: 2.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 358 RFIDDLENDRLSHYVKSElPIPENIDrGPVKTIVGEDFHRRVIESKDDILVLFLSSWCGHCHKAKRVFRDMGRRLKGSNG 437
Cdd:PTZ00102  332 EFFKDVEAGKVEKSIKSE-PIPEEQD-GPVKVVVGNTFEEIVFKSDKDVLLEIYAPWCGHCKNLEPVYNELGEKYKDNDS 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 438 PILATFDAYNNE--VEDMEISQFPTIALFQSGNKsDPVFYNGPDNLEDISLFLEknckrnkvnaenilqKHVSQEQIFEF 515
Cdd:PTZ00102  410 IIVAKMNGTANEtpLEEFSWSAFPTILFVKAGER-TPIPYEGERTVEGFKEFVN---------------KHATNPFEDDT 473


                  ....
gi 1851984901 516 HTEL 519
Cdd:PTZ00102  474 HEEL 477
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 388-488 7.70e-18

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: 78.81  E-value: 7.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 388 KTIVGEDFHRRVIESKDdILVLFLSSWCGHCHKAKRVFRDMGRRLKGSNGPILATFDAY-NNEV-EDMEISQFPTIALFQ 465
Cdd:cd02961     1 VELTDDNFDELVKDSKD-VLVEFYAPWCGHCKALAPEYEKLAKELKGDGKVVVAKVDCTaNNDLcSEYGVRGYPTIKLFP 79

                          90       100
                  ....*....|....*....|...
gi 1851984901 466 SGNKsDPVFYNGPDNLEDISLFL 488
Cdd:cd02961    80 NGSK-EPVKYEGPRTLESLVEFI 101
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 387-488 5.28e-12

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


Pssm-ID: 239296 [Multi-domain]  Cd Length: 105  Bit Score: 62.27  E-value: 5.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 387 VKTIVGEDFHRRVIESKDDILVLFLSSWCGHCHKAKRVFRDMGRRLKGSNGPILATFDA--YNNEV-EDMEISQFPTIAL 463
Cdd:cd02998     2 VVELTDSNFDKVVGDDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFANEDDVVIAKVDAdeANKDLaKKYGVSGFPTLKF 81

                          90       100
                  ....*....|....*....|....*
gi 1851984901 464 FQSGNKsDPVFYNGPDNLEDISLFL 488
Cdd:cd02998    82 FPKGST-EPVKYEGGRDLEDLVKFV 105
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 386-484 2.82e-11

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: 59.99  E-value: 2.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 386 PVKTIVGEDFHRRVIESKDDILVLFLSSWCGHCHKAKRVFRDMGRRLKGSNGpiLATFDAYNNEV--EDMEISQFPTIAL 463
Cdd:cd03001     1 DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVK--VGAVDADVHQSlaQQYGVRGFPTIKV 78

                          90       100
                  ....*....|....*....|.
gi 1851984901 464 FQSGnKSDPVFYNGPDNLEDI 484
Cdd:cd03001    79 FGAG-KNSPQDYQGGRTAKAI 98
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 390-488 3.07e-10

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


Pssm-ID: 239295 [Multi-domain]  Cd Length: 104  Bit Score: 57.33  E-value: 3.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 390 IVGEDFhRRVIESKDDILVLFLSSWCGHCHKAKRVFRDMGRRLKGSNGPILATFDAY--NNEV--EDMEISQFPTIALFQ 465
Cdd:cd02997     5 LTDEDF-RKFLKKEKHVLVMFYAPWCGHCKKMKPEFTKAATELKEDGKGVLAAVDCTkpEHDAlkEEYNVKGFPTFKYFE 83

                          90       100
                  ....*....|....*....|....
gi 1851984901 466 SGNKsdpVF-YNGPDNLEDISLFL 488
Cdd:cd02997    84 NGKF---VEkYEGERTAEDIIEFM 104
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 393-487 6.45e-10

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: 56.31  E-value: 6.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 393 EDFHRRVIESKDD--ILVLFLSSWCGHCHKAKRVFRDMGRRLKGSNGPI-LATFDA--YNNEVEDMEISQFPTIALFqsg 467
Cdd:cd03000     3 LDLDDSFKDVRKEdiWLVDFYAPWCGHCKKLEPVWNEVGAELKSSGSPVrVGKLDAtaYSSIASEFGVRGYPTIKLL--- 79

                          90       100
                  ....*....|....*....|.
gi 1851984901 468 nKSDPVF-YNGPDNLEDISLF 487
Cdd:cd03000    80 -KGDLAYnYRGPRTKDDIVEF 99
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 386-490 5.16e-08

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: 50.69  E-value: 5.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 386 PVKTIVGEDFHRRVIESKDDILVLFLSSWCGHCHKAKRVFRDMGRRLKGSngpilATF-----DAYNNEVEDMEISQFPT 460
Cdd:pfam00085   1 VVVVLTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGN-----VVFakvdvDENPDLASKYGVRGYPT 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 1851984901 461 IALFQSGNKSDpvFYNGPDNLEDISLFLEK 490
Cdd:pfam00085  76 LIFFKNGQPVD--DYVGARPKDALAAFLKA 103
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 386-487 4.48e-07

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: 48.51  E-value: 4.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 386 PVKTIVGEDFHRRVIESKDDILVLFLSSWCGHCHKAKRVFRDMGRRLKGsngpiLATFDAYNNEVED-------MEISQF 458
Cdd:cd03002     1 PVYELTPKNFDKVVHNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKELDG-----LVQVAAVDCDEDKnkplcgkYGVQGF 75

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1851984901 459 PTIALFQSGNKSD---PVFYNGPDNLEDISLF 487
Cdd:cd03002    76 PTLKVFRPPKKASkhaVEDYNGERSAKAIVDF 107
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 386-470 7.60e-07

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


Pssm-ID: 239290 [Multi-domain]  Cd Length: 114  Bit Score: 48.03  E-value: 7.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 386 PVKTIVGEDFHRRVIESKDDILVLFLSSWCGHCHKAKRVFRDMGRRLKGSNGPILATF----DAYNNEV-EDMEISQFPT 460
Cdd:cd02992     2 PVIVLDAASFNSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRKWRPVVRVAAvdcaDEENVALcRDFGVTGYPT 81

                          90
                  ....*....|
gi 1851984901 461 IALFQSGNKS 470
Cdd:cd02992    82 LRYFPPFSKE 91
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 387-491 2.61e-06

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: 45.97  E-value: 2.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 387 VKTIVGEDFHRRVIESKDDILVLFLSSWCGHCHKAKRVFRDMGRRLKGSNgpILATFDAYNNE--VEDMEISQFPTIALF 464
Cdd:COG3118     2 VVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKV--KFVKVDVDENPelAAQFGVRSIPTLLLF 79

                          90       100
                  ....*....|....*....|....*...
gi 1851984901 465 QSGNksdPVF-YNGPDNLEDISLFLEKN 491
Cdd:COG3118    80 KDGQ---PVDrFVGALPKEQLREFLDKV 104
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 399-490 2.77e-06

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: 49.67  E-value: 2.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 399 VIESKDDILVLFLSSWCGHCHKAKRVFRDMGRRLKGSNGPI-LATFDAYNNE--VEDMEISQFPTIALFQSGNKSdPVFY 475
Cdd:TIGR01130  14 FIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPPIkLAKVDATEEKdlAQKYGVSGYPTLKIFRNGEDS-VSDY 92

                          90
                  ....*....|....*
gi 1851984901 476 NGPDNLEDISLFLEK 490
Cdd:TIGR01130  93 NGPRDADGIVKYMKK 107
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 387-477 1.30e-05

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 47.82  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 387 VKTIVGEDFHRrVIESKDDILVLFLSSWCGHCHKAKRVFRDMGRRLKGSNGPI-LATFDAY--NNEVEDMEISQFPTIAL 463
Cdd:PTZ00102   34 VTVLTDSTFDK-FITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSEIvLASVDATeeMELAQEFGVRGYPTIKF 112

                          90
                  ....*....|....
gi 1851984901 464 FqsgNKSDPVFYNG 477
Cdd:PTZ00102  113 F---NKGNPVNYSG 123
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 387-477 2.57e-05

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


Pssm-ID: 239302 [Multi-domain]  Cd Length: 104  Bit Score: 43.05  E-value: 2.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 387 VKTIVGEDFHRRVIESKDDILVLFLSSWCGHCHKAKRVFRDMGRRLKGsngpiLATF-----DAYNNEVEDMEISQFPTI 461
Cdd:cd03004     3 VITLTPEDFPELVLNRKEPWLVDFYAPWCGPCQALLPELRKAARALKG-----KVKVgsvdcQKYESLCQQANIRAYPTI 77

                          90
                  ....*....|....*.
gi 1851984901 462 ALFqSGNKSDPVFYNG 477
Cdd:cd03004    78 RLY-PGNASKYHSYNG 92
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 387-488 3.10e-04

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: 39.96  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 387 VKTIVGEDFHRRVieSKDDILVLFLSSWCGHCHKAKRVFRDMGRRL-KGSNGPILATFD--AYNNEVEDMEISQFPTIAL 463
Cdd:cd03005     2 VLELTEDNFDHHI--AEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFnNENPSVKIAKVDctQHRELCSEFQVRGYPTLLL 79

                          90       100
                  ....*....|....*....|....*
gi 1851984901 464 FQSGNKSDPvfYNGPDNLEDISLFL 488
Cdd:cd03005    80 FKDGEKVDK--YKGTRDLDSLKEFV 102
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 393-471 4.48e-03

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: 36.38  E-value: 4.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 393 EDFHRRVIESKDdILVLFLSSWCGHCHKAKRVFRDmgrrLKGSNGPI-LATFDAYNNE--VEDMEISQFPTIALFQSGNK 469
Cdd:cd02947     1 EEFEELIKSAKP-VVVDFWAPWCGPCKAIAPVLEE----LAEEYPKVkFVKVDVDENPelAEEYGVRSIPTFLFFKNGKE 75


                  ..
gi 1851984901 470 SD 471
Cdd:cd02947    76 VD 77
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
201-362 5.49e-03

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 38.11  E-value: 5.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 201 LSQEGIKYPTLLIMRNMSLlpKITFYTNDVRNKKELYEFLKEELIPPIHSTNSYMLPMFLVMKKTIVYIYTRDK---ELK 277
Cdd:pfam13848  34 ADKYNIKEPAILLFRKFDE--ETVHYPGDSINFEDLKKFIQKNCLPLVREFTPENAEELFEEGIPPLLLLFLKKddeSTE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851984901 278 KYLSEswINTVPRKHSEKLVFLHSKGsDLVENKMNTILAIDSDYEEIVvrafVINLDTLEfYKFKPltieDGTISEQGMN 357
Cdd:pfam13848 112 EFKKA--LEKVAKKFRGKINFALVDA-KSFGRPLEYFGLSESDLPVIV----IVDSFSHM-YKYFP----SDEFSPESLK 179


                  ....*
gi 1851984901 358 RFIDD 362
Cdd:pfam13848 180 EFIND 184
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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