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Conserved domains on  [gi|5031973|ref|NP_005733|]
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protein disulfide-isomerase A6 isoform d precursor [Homo sapiens]

Protein Classification

protein disulfide isomerase( domain architecture ID 10122318)

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

CATH:  3.40.30.10
Gene Ontology:  GO:0003756|GO:0006457
PubMed:  15158710|15558583|12766950|9694669|10085220
SCOP:  4000084

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P5_C cd02983
P5 family, C-terminal redox inactive TRX-like domain; P5 is a protein disulfide isomerase (PDI) ...
 275-404 1.21e-79

P5 family, C-terminal redox inactive TRX-like domain; P5 is a protein disulfide isomerase (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. The C-terminal domain is likely involved in substrate binding, similar to the b and b' domains of PDI.


:

Pssm-ID: 239281  Cd Length: 130  Bit Score: 242.26  E-value: 1.21e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  275 PPELLEIINEDIAKRTCEEHQLCVVAVLPHILDTGAAGRNSYLEVLLKLADKYKKKMWGWLWTEAGAQSELETALGIGGF 354
Cdd:cd02983   1 APEIIELTSEDVFEETCEEKQLCIIAFLPHILDCQASCRNKYLEILKSVAEKFKKKPWGWLWTEAGAQLDLEEALNIGGF 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 5031973  355 GYPAMAAINARKMKFALLKGSFSEQGINEFLRELSFGRGSTAPVGGGAFP 404
Cdd:cd02983  81 GYPAMVAINFRKMKFATLKGSFSEDGINEFLRELSYGRGPTLPVNGLPKV 130
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 26-128 1.85e-68

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: 212.53  E-value: 1.85e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   26 DVIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIFG 105
Cdd:cd03001   1 DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVFG 80

                        90       100
                ....*....|....*....|...
gi 5031973  106 SNKNRPEDYQGGRTGEAIVDAAL 128
Cdd:cd03001  81 AGKNSPQDYQGGRTAKAIVSAAL 103
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 161-266 4.57e-61

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: 193.66  E-value: 4.57e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  161 DVIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVkeqtKGKVKLAAVDATVNQVLASRYGIRGFPTI 240
Cdd:cd03001   1 DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKAL----KGIVKVGAVDADVHQSLAQQYGVRGFPTI 76

                        90       100
                ....*....|....*....|....*..
gi 5031973  241 KIFQKG-ESPVDYDGGRTRSDIVSRAL 266
Cdd:cd03001  77 KVFGAGkNSPQDYQGGRTAKAIVSAAL 103
 
Name Accession Description Interval E-value
P5_C cd02983
P5 family, C-terminal redox inactive TRX-like domain; P5 is a protein disulfide isomerase (PDI) ...
 275-404 1.21e-79

P5 family, C-terminal redox inactive TRX-like domain; P5 is a protein disulfide isomerase (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. The C-terminal domain is likely involved in substrate binding, similar to the b and b' domains of PDI.


Pssm-ID: 239281  Cd Length: 130  Bit Score: 242.26  E-value: 1.21e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  275 PPELLEIINEDIAKRTCEEHQLCVVAVLPHILDTGAAGRNSYLEVLLKLADKYKKKMWGWLWTEAGAQSELETALGIGGF 354
Cdd:cd02983   1 APEIIELTSEDVFEETCEEKQLCIIAFLPHILDCQASCRNKYLEILKSVAEKFKKKPWGWLWTEAGAQLDLEEALNIGGF 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 5031973  355 GYPAMAAINARKMKFALLKGSFSEQGINEFLRELSFGRGSTAPVGGGAFP 404
Cdd:cd02983  81 GYPAMVAINFRKMKFATLKGSFSEDGINEFLRELSYGRGPTLPVNGLPKV 130
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 26-128 1.85e-68

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: 212.53  E-value: 1.85e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   26 DVIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIFG 105
Cdd:cd03001   1 DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVFG 80

                        90       100
                ....*....|....*....|...
gi 5031973  106 SNKNRPEDYQGGRTGEAIVDAAL 128
Cdd:cd03001  81 AGKNSPQDYQGGRTAKAIVSAAL 103
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 161-266 4.57e-61

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: 193.66  E-value: 4.57e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  161 DVIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVkeqtKGKVKLAAVDATVNQVLASRYGIRGFPTI 240
Cdd:cd03001   1 DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKAL----KGIVKVGAVDADVHQSLAQQYGVRGFPTI 76

                        90       100
                ....*....|....*....|....*..
gi 5031973  241 KIFQKG-ESPVDYDGGRTRSDIVSRAL 266
Cdd:cd03001  77 KVFGAGkNSPQDYQGGRTAKAIVSAAL 103
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 165-263 6.62e-47

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: 156.68  E-value: 6.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973    165 LTDDSFDKNVLDSEDVwMVEFYAPWCGHCKNLEPEWAAAASEVKEQtkGKVKLAAVDATVNQVLASRYGIRGFPTIKIFQ 244
Cdd:TIGR01126   1 LTASNFDEIVLSNKDV-LVEFYAPWCGHCKNLAPEYEKLAKELKKD--PKIVLAKVDATAEKDLASRFGVSGFPTIKFFP 77

                          90
                  ....*....|....*....
gi 5031973    245 KGESPVDYDGGRTRSDIVS 263
Cdd:TIGR01126  78 KGSKPVDYEGGRDLEAIVE 96
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 25-262 2.41e-41

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


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 152.52  E-value: 2.41e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973     25 DDVIELTPSNFNrEVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKD---VVKVGAVDADKHHSLGGQYGVQGFPTI 101
Cdd:TIGR01130   1 EDVLVLTKDNFD-DFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKkgpPIKLAKVDATEEKDLAQKYGVSGYPTL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973    102 KIFGSNKNRPEDYQGGRTGEAIV--------------------------------------------------------- 124
Cdd:TIGR01130  80 KIFRNGEDSVSDYNGPRDADGIVkymkkqsgpavkeietvadleafladddvvvigffkdldselndtflsvaeklrdvy 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973    125 -------DAALSALRQLVKDRLGGRSGGYSSGKQGRSDSSSKKD---------------VIELTDDSFDK---------- 172
Cdd:TIGR01130 160 fffahssDVAAFAKLGAFPDSVVLFKPKDEDEKFSKVDGEMDTDvsdlekfiraeslplVGEFTQETAAKyfesgplvvl 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973    173 --NV---LDSEDVWMVEFY------------------------------------------------------------- 186
Cdd:TIGR01130 240 yyNVdesLDPFEELRNRFLeaakkfrgkfvnfavadeedfgreleyfglkaekfpavaiqdlegnkkypmdqeefssenl 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973    187 -----------------------------------------------------APWCGHCKNLEPEWAAAASEVKEQTKg 213
Cdd:TIGR01130 320 eafvkdfldgklkpylksepipeddegpvkvlvgknfdeivldetkdvlvefyAPWCGHCKNLAPIYEELAEKYKDAES- 398

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 5031973    214 KVKLAAVDATVNQVlaSRYGIRGFPTIKIFQKGE--SPVDYDGGRTRSDIV 262
Cdd:TIGR01130 399 DVVIAKMDATANDV--PPFEVEGFPTIKFVPAGKksEPVPYDGDRTLEDFS 447
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 30-125 1.24e-40

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


Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 140.50  E-value: 1.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973     30 LTPSNFNrEVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKD--VVKVGAVDADKHHSLGGQYGVQGFPTIKIFGSN 107
Cdd:TIGR01126   1 LTASNFD-EIVLSNKDVLVEFYAPWCGHCKNLAPEYEKLAKELKKdpKIVLAKVDATAEKDLASRFGVSGFPTIKFFPKG 79

                          90
                  ....*....|....*...
gi 5031973    108 KnRPEDYQGGRTGEAIVD 125
Cdd:TIGR01126  80 S-KPVDYEGGRDLEAIVE 96
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 27-130 1.81e-34

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: 123.88  E-value: 1.81e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973     27 VIELTPSNFNREVIQSDSLW-LVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIFg 105
Cdd:pfam00085   1 VVVVLTDANFDEVVQKSSKPvLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFF- 79

                          90       100
                  ....*....|....*....|....*
gi 5031973    106 sNKNRPEDYQGGRTGEAIVDAALSA 130
Cdd:pfam00085  80 -KNGQPVDDYVGARPKDALAAFLKA 103
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 161-268 5.30e-34

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 132.57  E-value: 5.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   161 DVIELTDDSFDKNVLDSEDVwMVEFYAPWCGHCKNLEPEWAAAASEVKEQtKGKVKLAAVDATVNQVLASRYGIRGFPTI 240
Cdd:PTZ00102  33 HVTVLTDSTFDKFITENEIV-LVKFYAPWCGHCKRLAPEYKKAAKMLKEK-KSEIVLASVDATEEMELAQEFGVRGYPTI 110

                         90       100
                 ....*....|....*....|....*...
gi 5031973   241 KIFQKGEsPVDYDGGRTRSDIVSRALDL 268
Cdd:PTZ00102 111 KFFNKGN-PVNYSGGRTADGIVSWIKKL 137
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 162-263 6.37e-34

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: 122.73  E-value: 6.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973    162 VIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEvkeqTKGKVKLAAVDATVNQVLASRYGIRGFPTIK 241
Cdd:pfam00085   2 VVVLTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQE----YKGNVVFAKVDVDENPDLASKYGVRGYPTLI 77

                          90       100
                  ....*....|....*....|..
gi 5031973    242 IFQKGESPVDYDGGRTRSDIVS 263
Cdd:pfam00085  78 FFKNGQPVDDYVGARPKDALAA 99
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 2-125 2.11e-29

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 119.47  E-value: 2.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973     2 ALLVLGLVSCTFFLAVNGLYSSsDDVIELTPSNFNReVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDV---VKV 78
Cdd:PTZ00102  10 LFLLLILLAFAVFGSAEEHFIS-EHVTVLTDSTFDK-FITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKkseIVL 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 5031973    79 GAVDADKHHSLGGQYGVQGFPTIKIFgsNKNRPEDYQGGRTGEAIVD 125
Cdd:PTZ00102  88 ASVDATEEMELAQEFGVRGYPTIKFF--NKGNPVNYSGGRTADGIVS 132
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 162-251 3.62e-26

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


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 101.82  E-value: 3.62e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  162 VIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVkeqtKGKVKLAAVDATVNQVLASRYGIRGFPTIK 241
Cdd:COG3118   2 VVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEY----GGKVKFVKVDVDENPELAAQFGVRSIPTLL 77

                        90
                ....*....|
gi 5031973  242 IFQKGEsPVD 251
Cdd:COG3118  78 LFKDGQ-PVD 86
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 27-104 5.10e-25

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: 98.35  E-value: 5.10e-25
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031973   27 VIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIF 104
Cdd:COG3118   2 VVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLF 79
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
228-387 1.81e-03

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 39.27  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973    228 LASRYGIRgFPTIKIFQK-GESPVDYDGGRTRSDIVSRaldlFSDNAPPPeLLEIINEDIAKRTCEEHQLCVVAVlphIL 306
Cdd:pfam13848  33 VADKYNIK-EPAILLFRKfDEETVHYPGDSINFEDLKK----FIQKNCLP-LVREFTPENAEELFEEGIPPLLLL---FL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973    307 DTGAAGRNSYLEVLLKLADKYKKKMwGWLWTEAGA-QSELETaLGIGGFGYPAMAAIN-ARKMKFALLKGSFSEQGINEF 384
Cdd:pfam13848 104 KKDDESTEEFKKALEKVAKKFRGKI-NFALVDAKSfGRPLEY-FGLSESDLPVIVIVDsFSHMYKYFPSDEFSPESLKEF 181


                  ...
gi 5031973    385 LRE 387
Cdd:pfam13848 182 IND 184
 
Name Accession Description Interval E-value
P5_C cd02983
P5 family, C-terminal redox inactive TRX-like domain; P5 is a protein disulfide isomerase (PDI) ...
 275-404 1.21e-79

P5 family, C-terminal redox inactive TRX-like domain; P5 is a protein disulfide isomerase (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. The C-terminal domain is likely involved in substrate binding, similar to the b and b' domains of PDI.


Pssm-ID: 239281  Cd Length: 130  Bit Score: 242.26  E-value: 1.21e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  275 PPELLEIINEDIAKRTCEEHQLCVVAVLPHILDTGAAGRNSYLEVLLKLADKYKKKMWGWLWTEAGAQSELETALGIGGF 354
Cdd:cd02983   1 APEIIELTSEDVFEETCEEKQLCIIAFLPHILDCQASCRNKYLEILKSVAEKFKKKPWGWLWTEAGAQLDLEEALNIGGF 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 5031973  355 GYPAMAAINARKMKFALLKGSFSEQGINEFLRELSFGRGSTAPVGGGAFP 404
Cdd:cd02983  81 GYPAMVAINFRKMKFATLKGSFSEDGINEFLRELSYGRGPTLPVNGLPKV 130
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 26-128 1.85e-68

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: 212.53  E-value: 1.85e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   26 DVIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIFG 105
Cdd:cd03001   1 DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVFG 80

                        90       100
                ....*....|....*....|...
gi 5031973  106 SNKNRPEDYQGGRTGEAIVDAAL 128
Cdd:cd03001  81 AGKNSPQDYQGGRTAKAIVSAAL 103
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 161-266 4.57e-61

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: 193.66  E-value: 4.57e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  161 DVIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVkeqtKGKVKLAAVDATVNQVLASRYGIRGFPTI 240
Cdd:cd03001   1 DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKAL----KGIVKVGAVDADVHQSLAQQYGVRGFPTI 76

                        90       100
                ....*....|....*....|....*..
gi 5031973  241 KIFQKG-ESPVDYDGGRTRSDIVSRAL 266
Cdd:cd03001  77 KVFGAGkNSPQDYQGGRTAKAIVSAAL 103
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 165-263 6.62e-47

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: 156.68  E-value: 6.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973    165 LTDDSFDKNVLDSEDVwMVEFYAPWCGHCKNLEPEWAAAASEVKEQtkGKVKLAAVDATVNQVLASRYGIRGFPTIKIFQ 244
Cdd:TIGR01126   1 LTASNFDEIVLSNKDV-LVEFYAPWCGHCKNLAPEYEKLAKELKKD--PKIVLAKVDATAEKDLASRFGVSGFPTIKFFP 77

                          90
                  ....*....|....*....
gi 5031973    245 KGESPVDYDGGRTRSDIVS 263
Cdd:TIGR01126  78 KGSKPVDYEGGRDLEAIVE 96
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 28-125 3.84e-43

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: 146.99  E-value: 3.84e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   28 IELTPSNFNrEVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALK--DVVKVGAVDADKHHSLGGQYGVQGFPTIKIFG 105
Cdd:cd02961   1 VELTDDNFD-ELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKgdGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFP 79

                        90       100
                ....*....|....*....|
gi 5031973  106 SNKNRPEDYQGGRTGEAIVD 125
Cdd:cd02961  80 NGSKEPVKYEGPRTLESLVE 99
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 163-263 4.46e-43

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: 146.60  E-value: 4.46e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  163 IELTDDSFDKNVLDSEDvWMVEFYAPWCGHCKNLEPEWAAAASEVKEqtKGKVKLAAVDATVNQVLASRYGIRGFPTIKI 242
Cdd:cd02961   1 VELTDDNFDELVKDSKD-VLVEFYAPWCGHCKALAPEYEKLAKELKG--DGKVVVAKVDCTANNDLCSEYGVRGYPTIKL 77

                        90       100
                ....*....|....*....|..
gi 5031973  243 FQKGES-PVDYDGGRTRSDIVS 263
Cdd:cd02961  78 FPNGSKePVKYEGPRTLESLVE 99
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 25-262 2.41e-41

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


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 152.52  E-value: 2.41e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973     25 DDVIELTPSNFNrEVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKD---VVKVGAVDADKHHSLGGQYGVQGFPTI 101
Cdd:TIGR01130   1 EDVLVLTKDNFD-DFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKkgpPIKLAKVDATEEKDLAQKYGVSGYPTL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973    102 KIFGSNKNRPEDYQGGRTGEAIV--------------------------------------------------------- 124
Cdd:TIGR01130  80 KIFRNGEDSVSDYNGPRDADGIVkymkkqsgpavkeietvadleafladddvvvigffkdldselndtflsvaeklrdvy 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973    125 -------DAALSALRQLVKDRLGGRSGGYSSGKQGRSDSSSKKD---------------VIELTDDSFDK---------- 172
Cdd:TIGR01130 160 fffahssDVAAFAKLGAFPDSVVLFKPKDEDEKFSKVDGEMDTDvsdlekfiraeslplVGEFTQETAAKyfesgplvvl 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973    173 --NV---LDSEDVWMVEFY------------------------------------------------------------- 186
Cdd:TIGR01130 240 yyNVdesLDPFEELRNRFLeaakkfrgkfvnfavadeedfgreleyfglkaekfpavaiqdlegnkkypmdqeefssenl 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973    187 -----------------------------------------------------APWCGHCKNLEPEWAAAASEVKEQTKg 213
Cdd:TIGR01130 320 eafvkdfldgklkpylksepipeddegpvkvlvgknfdeivldetkdvlvefyAPWCGHCKNLAPIYEELAEKYKDAES- 398

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 5031973    214 KVKLAAVDATVNQVlaSRYGIRGFPTIKIFQKGE--SPVDYDGGRTRSDIV 262
Cdd:TIGR01130 399 DVVIAKMDATANDV--PPFEVEGFPTIKFVPAGKksEPVPYDGDRTLEDFS 447
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 30-125 1.24e-40

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


Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 140.50  E-value: 1.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973     30 LTPSNFNrEVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKD--VVKVGAVDADKHHSLGGQYGVQGFPTIKIFGSN 107
Cdd:TIGR01126   1 LTASNFD-EIVLSNKDVLVEFYAPWCGHCKNLAPEYEKLAKELKKdpKIVLAKVDATAEKDLASRFGVSGFPTIKFFPKG 79

                          90
                  ....*....|....*...
gi 5031973    108 KnRPEDYQGGRTGEAIVD 125
Cdd:TIGR01126  80 S-KPVDYEGGRDLEAIVE 96
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 27-128 1.39e-38

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: 135.18  E-value: 1.39e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   27 VIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAV--DADKHHSLGGQYGVQGFPTIKIF 104
Cdd:cd03002   2 VYELTPKNFDKVVHNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKELDGLVQVAAVdcDEDKNKPLCGKYGVQGFPTLKVF 81

                        90       100
                ....*....|....*....|....*...
gi 5031973  105 ----GSNKNRPEDYQGGRTGEAIVDAAL 128
Cdd:cd03002  82 rppkKASKHAVEDYNGERSAKAIVDFVL 109
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 160-263 1.07e-37

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


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 142.51  E-value: 1.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973    160 KDVIELTDDSFDkNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVKEQTKgKVKLAAVDATVNQVLASRYGIRGFPT 239
Cdd:TIGR01130   1 EDVLVLTKDNFD-DFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGP-PIKLAKVDATEEKDLAQKYGVSGYPT 78

                          90       100
                  ....*....|....*....|....*
gi 5031973    240 IKIFQKGE-SPVDYDGGRTRSDIVS 263
Cdd:TIGR01130  79 LKIFRNGEdSVSDYNGPRDADGIVK 103
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 27-116 3.16e-35

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: 126.25  E-value: 3.16e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   27 VIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIFGS 106
Cdd:cd03004   3 VITLTPEDFPELVLNRKEPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLYPG 82

                        90
                ....*....|
gi 5031973  107 NKNRPEDYQG 116
Cdd:cd03004  83 NASKYHSYNG 92
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 26-124 9.68e-35

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: 124.67  E-value: 9.68e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   26 DVIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALK--DVVKVGAVDADK-HHSLGGQYGVQGFPTIK 102
Cdd:cd02998   1 NVVELTDSNFDKVVGDDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFAneDDVVIAKVDADEaNKDLAKKYGVSGFPTLK 80

                        90       100
                ....*....|....*....|..
gi 5031973  103 IFGSNKNRPEDYQGGRTGEAIV 124
Cdd:cd02998  81 FFPKGSTEPVKYEGGRDLEDLV 102
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 27-130 1.81e-34

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: 123.88  E-value: 1.81e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973     27 VIELTPSNFNREVIQSDSLW-LVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIFg 105
Cdd:pfam00085   1 VVVVLTDANFDEVVQKSSKPvLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFF- 79

                          90       100
                  ....*....|....*....|....*
gi 5031973    106 sNKNRPEDYQGGRTGEAIVDAALSA 130
Cdd:pfam00085  80 -KNGQPVDDYVGARPKDALAAFLKA 103
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 161-268 5.30e-34

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 132.57  E-value: 5.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   161 DVIELTDDSFDKNVLDSEDVwMVEFYAPWCGHCKNLEPEWAAAASEVKEQtKGKVKLAAVDATVNQVLASRYGIRGFPTI 240
Cdd:PTZ00102  33 HVTVLTDSTFDKFITENEIV-LVKFYAPWCGHCKRLAPEYKKAAKMLKEK-KSEIVLASVDATEEMELAQEFGVRGYPTI 110

                         90       100
                 ....*....|....*....|....*...
gi 5031973   241 KIFQKGEsPVDYDGGRTRSDIVSRALDL 268
Cdd:PTZ00102 111 KFFNKGN-PVNYSGGRTADGIVSWIKKL 137
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 162-263 6.37e-34

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: 122.73  E-value: 6.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973    162 VIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEvkeqTKGKVKLAAVDATVNQVLASRYGIRGFPTIK 241
Cdd:pfam00085   2 VVVLTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQE----YKGNVVFAKVDVDENPDLASKYGVRGYPTLI 77

                          90       100
                  ....*....|....*....|..
gi 5031973    242 IFQKGESPVDYDGGRTRSDIVS 263
Cdd:pfam00085  78 FFKNGQPVDDYVGARPKDALAA 99
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 161-263 7.72e-34

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: 122.36  E-value: 7.72e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  161 DVIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVKEqtKGKVKLAAVDAT-VNQVLASRYGIRGFPT 239
Cdd:cd02998   1 NVVELTDSNFDKVVGDDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFAN--EDDVVIAKVDADeANKDLAKKYGVSGFPT 78

                        90       100
                ....*....|....*....|....*
gi 5031973  240 IKIFQKGES-PVDYDGGRTRSDIVS 263
Cdd:cd02998  79 LKFFPKGSTePVKYEGGRDLEDLVK 103
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 161-263 1.27e-32

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: 118.96  E-value: 1.27e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  161 DVIELTDDSFDKNVLDSEDVwMVEFYAPWCGHCKNLEPEWAAAASEVKEqtKGKVKLAAVDATV--NQVLASRYGIRGFP 238
Cdd:cd02997   1 DVVHLTDEDFRKFLKKEKHV-LVMFYAPWCGHCKKMKPEFTKAATELKE--DGKGVLAAVDCTKpeHDALKEEYNVKGFP 77

                        90       100
                ....*....|....*....|....*
gi 5031973  239 TIKIFQKGESPVDYDGGRTRSDIVS 263
Cdd:cd02997  78 TFKYFENGKFVEKYEGERTAEDIIE 102
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 162-266 8.21e-32

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


Pssm-ID: 239300 [Multi-domain]  Cd Length: 109  Bit Score: 117.08  E-value: 8.21e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  162 VIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVkeqtKGKVKLAAV--DATVNQVLASRYGIRGFPT 239
Cdd:cd03002   2 VYELTPKNFDKVVHNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKEL----DGLVQVAAVdcDEDKNKPLCGKYGVQGFPT 77

                        90       100       110
                ....*....|....*....|....*....|..
gi 5031973  240 IKIFQKGE-----SPVDYDGGRTRSDIVSRAL 266
Cdd:cd03002  78 LKVFRPPKkaskhAVEDYNGERSAKAIVDFVL 109
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 2-125 2.11e-29

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 119.47  E-value: 2.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973     2 ALLVLGLVSCTFFLAVNGLYSSsDDVIELTPSNFNReVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDV---VKV 78
Cdd:PTZ00102  10 LFLLLILLAFAVFGSAEEHFIS-EHVTVLTDSTFDK-FITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKkseIVL 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 5031973    79 GAVDADKHHSLGGQYGVQGFPTIKIFgsNKNRPEDYQGGRTGEAIVD 125
Cdd:PTZ00102  88 ASVDATEEMELAQEFGVRGYPTIKFF--NKGNPVNYSGGRTADGIVS 132
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 162-266 7.97e-28

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: 106.38  E-value: 7.97e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  162 VIELtDDSFDKNvlDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVKEqTKGKVKLAAVDATVNQVLASRYGIRGFPTIK 241
Cdd:cd03000   2 VLDL-DDSFKDV--RKEDIWLVDFYAPWCGHCKKLEPVWNEVGAELKS-SGSPVRVGKLDATAYSSIASEFGVRGYPTIK 77

                        90       100
                ....*....|....*....|....*
gi 5031973  242 IFqKGESPVDYDGGRTRSDIVSRAL 266
Cdd:cd03000  78 LL-KGDLAYNYRGPRTKDDIVEFAN 101
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 162-262 2.48e-27

PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' domains of PDI, ERp72, ERp57 (or ERp60) and EFP1. PDI, ERp72 and ERp57 are endoplasmic reticulum (ER)-resident eukaryotic proteins involved in oxidative protein folding. They are oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. PDI and ERp57 have the abb'a' domain structure (where a and a' are redox active TRX domains while b and b' are redox inactive TRX-like domains). PDI also contains an acidic region (c domain) after the a' domain that is absent in ERp57. ERp72 has an additional a domain at the N-terminus (a"abb'a' domain structure). ERp57 interacts with the lectin chaperones, calnexin and calreticulin, and specifically promotes the oxidative folding of glycoproteins, while PDI shows a wider substrate specificity. ERp72 associates with several ER chaperones and folding factors to form complexes in the ER that bind nascent proteins. EFP1 is a binding partner protein of thyroid oxidase, which is responsible for the generation of hydrogen peroxide, a crucial substrate of thyroperoxidase, which functions to iodinate thyroglobulin and synthesize thyroid hormones.


Pssm-ID: 239293 [Multi-domain]  Cd Length: 104  Bit Score: 104.95  E-value: 2.48e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  162 VIELTDDSFDKNVLDSE-DVwMVEFYAPWCGHCKNLEPEWAAAASEVKeqTKGKVKLAAVDATVNQVLASrYGIRGFPTI 240
Cdd:cd02995   2 VKVVVGKNFDEVVLDSDkDV-LVEFYAPWCGHCKALAPIYEELAEKLK--GDDNVVIAKMDATANDVPSE-FVVDGFPTI 77

                        90       100
                ....*....|....*....|....
gi 5031973  241 KIFQKG--ESPVDYDGGRTRSDIV 262
Cdd:cd02995  78 LFFPAGdkSNPIKYEGDRTLEDLI 101
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 162-251 3.62e-26

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


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 101.82  E-value: 3.62e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  162 VIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVkeqtKGKVKLAAVDATVNQVLASRYGIRGFPTIK 241
Cdd:COG3118   2 VVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEY----GGKVKFVKVDVDENPELAAQFGVRSIPTLL 77

                        90
                ....*....|
gi 5031973  242 IFQKGEsPVD 251
Cdd:COG3118  78 LFKDGQ-PVD 86
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 162-254 1.50e-25

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: 100.06  E-value: 1.50e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  162 VIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASevkeQTKGKVKLAAVDATVNQVLASRYGIRGFPTIK 241
Cdd:cd03004   3 VITLTPEDFPELVLNRKEPWLVDFYAPWCGPCQALLPELRKAAR----ALKGKVKVGSVDCQKYESLCQQANIRAYPTIR 78

                        90
                ....*....|....
gi 5031973  242 IFQKGESPV-DYDG 254
Cdd:cd03004  79 LYPGNASKYhSYNG 92
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 26-125 4.04e-25

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: 98.93  E-value: 4.04e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   26 DVIELTPSNFnREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKV--GAVDADK--HHSLGGQYGVQGFPTI 101
Cdd:cd02997   1 DVVHLTDEDF-RKFLKKEKHVLVMFYAPWCGHCKKMKPEFTKAATELKEDGKGvlAAVDCTKpeHDALKEEYNVKGFPTF 79

                        90       100
                ....*....|....*....|....
gi 5031973  102 KIFgSNKNRPEDYQGGRTGEAIVD 125
Cdd:cd02997  80 KYF-ENGKFVEKYEGERTAEDIIE 102
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 27-104 5.10e-25

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: 98.35  E-value: 5.10e-25
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031973   27 VIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIF 104
Cdd:COG3118   2 VVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLF 79
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 162-257 5.62e-25

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: 98.51  E-value: 5.62e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  162 VIELTDDSFDKNVldSEDVWMVEFYAPWCGHCKNLEPEWAA-AASEVKEQTKgkVKLAAVDATVNQVLASRYGIRGFPTI 240
Cdd:cd03005   2 VLELTEDNFDHHI--AEGNHFVKFFAPWCGHCKRLAPTWEQlAKKFNNENPS--VKIAKVDCTQHRELCSEFQVRGYPTL 77

                        90
                ....*....|....*..
gi 5031973  241 KIFQKGESPVDYDGGRT 257
Cdd:cd03005  78 LLFKDGEKVDKYKGTRD 94
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 43-128 1.83e-24

PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX related transmembrane protein containing one redox active TRX domain at the N-terminus and a classical ER retrieval sequence for type I transmembrane proteins at the C-terminus. The TMX3 transcript is found in a variety of tissues with the highest levels detected in skeletal muscle and the heart. In vitro, TMX3 showed oxidase activity albeit slightly lower than that of protein disulfide isomerase.


Pssm-ID: 239298 [Multi-domain]  Cd Length: 104  Bit Score: 97.14  E-value: 1.83e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   43 DSLWLVEFYAPWCGHCQRLTPEWKKAATALKDV---VKVGAVDADKHHSLGGQYGVQGFPTIKIFgsNKNRPEDYQGGRT 119
Cdd:cd03000  15 EDIWLVDFYAPWCGHCKKLEPVWNEVGAELKSSgspVRVGKLDATAYSSIASEFGVRGYPTIKLL--KGDLAYNYRGPRT 92


                ....*....
gi 5031973  120 GEAIVDAAL 128
Cdd:cd03000  93 KDDIVEFAN 101
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 27-125 8.68e-23

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: 92.23  E-value: 8.68e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   27 VIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDV--VKVGAVDADK--HHSLggqYGVQGFPTIK 102
Cdd:cd02995   2 VKVVVGKNFDEVVLDSDKDVLVEFYAPWCGHCKALAPIYEELAEKLKGDdnVVIAKMDATAndVPSE---FVVDGFPTIL 78

                        90       100
                ....*....|....*....|....
gi 5031973  103 IF-GSNKNRPEDYQGGRTGEAIVD 125
Cdd:cd02995  79 FFpAGDKSNPIKYEGDRTLEDLIK 102
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 27-123 2.88e-22

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: 90.81  E-value: 2.88e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   27 VIELTPSNFNREVIQSDSLwlVEFYAPWCGHCQRLTPEWKKAATALKDV---VKVGAVDADKHHSLGGQYGVQGFPTIKI 103
Cdd:cd03005   2 VLELTEDNFDHHIAEGNHF--VKFFAPWCGHCKRLAPTWEQLAKKFNNEnpsVKIAKVDCTQHRELCSEFQVRGYPTLLL 79

                        90       100
                ....*....|....*....|
gi 5031973  104 FGSNKnRPEDYQGGRTGEAI 123
Cdd:cd03005  80 FKDGE-KVDKYKGTRDLDSL 98
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 25-132 1.09e-21

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


Pssm-ID: 239290 [Multi-domain]  Cd Length: 114  Bit Score: 89.64  E-value: 1.09e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   25 DDVIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKD---VVKVGAVD--ADKHHSLGGQYGVQGFP 99
Cdd:cd02992   1 DPVIVLDAASFNSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRKwrpVVRVAAVDcaDEENVALCRDFGVTGYP 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 5031973  100 TIKIFGSNKNRPEDYQGGRTGEAIVDAALSALR 132
Cdd:cd02992  81 TLRYFPPFSKEATDGLKQEGPERDVNELREALI 113
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 22-125 2.08e-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: 93.20  E-value: 2.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973     22 SSSDDVIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDV---VKVGAVDADKHHSLGgqYGVQGF 98
Cdd:TIGR01130 343 DDEGPVKVLVGKNFDEIVLDETKDVLVEFYAPWCGHCKNLAPIYEELAEKYKDAesdVVIAKMDATANDVPP--FEVEGF 420

                          90       100
                  ....*....|....*....|....*...
gi 5031973     99 PTIKIF-GSNKNRPEDYQGGRTGEAIVD 125
Cdd:TIGR01130 421 PTIKFVpAGKKSEPVPYDGDRTLEDFSK 448
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 155-282 2.28e-20

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 89.30  E-value: 2.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   155 DSSSKKDVIELTDDSFDKNVLDSEDV----WMVEFYAPWCGHCKNLEPEWAAAASEVkeqtKGKVKLAAVDATVNQVLAS 230
Cdd:PTZ00443  25 DAEDANALVLLNDKNFEKLTQASTGAttgpWFVKFYAPWCSHCRKMAPAWERLAKAL----KGQVNVADLDATRALNLAK 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 5031973   231 RYGIRGFPTIKIFQKGESpVDYDGG-RTRSDIVSRALDLFSD--NAPPPELLEII 282
Cdd:PTZ00443 101 RFAIKGYPTLLLFDKGKM-YQYEGGdRSTEKLAAFALGDFKKalGAPVPAPLSFF 154
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 162-243 5.20e-20

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


Pssm-ID: 239290 [Multi-domain]  Cd Length: 114  Bit Score: 85.01  E-value: 5.20e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  162 VIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVKEQtKGKVKLAAVD--ATVNQVLASRYGIRGFPT 239
Cdd:cd02992   3 VIVLDAASFNSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRKW-RPVVRVAAVDcaDEENVALCRDFGVTGYPT 81


                ....
gi 5031973  240 IKIF 243
Cdd:cd02992  82 LRYF 85
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 27-135 2.31e-19

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 86.60  E-value: 2.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973    27 VIELTPSNFNREVIQSDSL----WLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIK 102
Cdd:PTZ00443  32 LVLLNDKNFEKLTQASTGAttgpWFVKFYAPWCSHCRKMAPAWERLAKALKGQVNVADLDATRALNLAKRFAIKGYPTLL 111

                         90       100       110
                 ....*....|....*....|....*....|....
gi 5031973   103 IFgsNKNRPEDYQGG-RTGEAIVDAALSALRQLV 135
Cdd:PTZ00443 112 LF--DKGKMYQYEGGdRSTEKLAAFALGDFKKAL 143
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 165-251 1.33e-18

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: 80.80  E-value: 1.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973    165 LTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVkeqtKGKVKLAAVDATVNQVLASRYGIRGFPTIKIFQ 244
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEY----EGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFK 76


                  ....*..
gi 5031973    245 KGEsPVD 251
Cdd:TIGR01068  77 NGK-EVD 82
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 26-127 4.73e-18

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


Pssm-ID: 239301 [Multi-domain]  Cd Length: 101  Bit Score: 79.11  E-value: 4.73e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   26 DVIELTPSNFNREVIQSDsLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIFG 105
Cdd:cd03003   2 EIVTLDRGDFDAAVNSGE-IWFVNFYSPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDDRMLCRSQGVNSYPSLYVFP 80

                        90       100
                ....*....|....*....|..
gi 5031973  106 SNKNrPEDYQGGRTGEAIVDAA 127
Cdd:cd03003  81 SGMN-PEKYYGDRSKESLVKFA 101
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 168-247 2.95e-17

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: 76.44  E-value: 2.95e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  168 DSFDKNVLDSEDVwMVEFYAPWCGHCKNLEPEWAAAASEvkeqtKGKVKLAAVDATVNQVLASRYGIRGFPTIKIFQKGE 247
Cdd:cd02947   1 EEFEELIKSAKPV-VVDFWAPWCGPCKAIAPVLEELAEE-----YPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGK 74
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 161-265 3.04e-17

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


Pssm-ID: 239301 [Multi-domain]  Cd Length: 101  Bit Score: 76.79  E-value: 3.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  161 DVIELTDDSFDKNVlDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVkeqtKGKVKLAAVDATVNQVLASRYGIRGFPTI 240
Cdd:cd03003   2 EIVTLDRGDFDAAV-NSGEIWFVNFYSPRCSHCHDLAPTWREFAKEM----DGVIRIGAVNCGDDRMLCRSQGVNSYPSL 76

                        90       100
                ....*....|....*....|....*
gi 5031973  241 KIFQKGESPVDYDGGRTRSDIVSRA 265
Cdd:cd03003  77 YVFPSGMNPEKYYGDRSKESLVKFA 101
trxA PRK09381
thioredoxin TrxA;
162-247 7.33e-17

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 75.87  E-value: 7.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   162 VIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPewaaAASEVKEQTKGKVKLAAVDATVNQVLASRYGIRGFPTIK 241
Cdd:PRK09381   5 IIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAP----ILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLL 80


                 ....*.
gi 5031973   242 IFQKGE 247
Cdd:PRK09381  81 LFKNGE 86
PRK10996 PRK10996
thioredoxin 2; Provisional
 161-247 9.30e-17

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 76.65  E-value: 9.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   161 DVIELTDDSFDKnVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEvkeqTKGKVKLAAVDATVNQVLASRYGIRGFPTI 240
Cdd:PRK10996  36 EVINATGETLDK-LLQDDLPVVIDFWAPWCGPCRNFAPIFEDVAAE----RSGKVRFVKVNTEAERELSARFRIRSIPTI 110


                 ....*..
gi 5031973   241 KIFQKGE 247
Cdd:PRK10996 111 MIFKNGQ 117
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 30-104 1.22e-16

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: 75.02  E-value: 1.22e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5031973     30 LTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIF 104
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLF 75
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 161-263 1.24e-16

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


Pssm-ID: 239292 [Multi-domain]  Cd Length: 101  Bit Score: 75.11  E-value: 1.24e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  161 DVIELTDDSFDKnVLDSEdvWMVEFYAPWCGHCKNLEPEWAAAASEVKEQtkgKVKLAAVDATVNQVLASRYGIRGFPTI 240
Cdd:cd02994   2 NVVELTDSNWTL-VLEGE--WMIEFYAPWCPACQQLQPEWEEFADWSDDL---GINVAKVDVTQEPGLSGRFFVTALPTI 75

                        90       100
                ....*....|....*....|....*...
gi 5031973  241 -----KIFQKgespvdYDGGRTRSDIVS 263
Cdd:cd02994  76 yhakdGVFRR------YQGPRDKEDLIS 97
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 26-124 4.16e-16

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


Pssm-ID: 239292 [Multi-domain]  Cd Length: 101  Bit Score: 73.57  E-value: 4.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   26 DVIELTPSNFNReVIQSDslWLVEFYAPWCGHCQRLTPEWKKAATALKDV-VKVGAVDADKHHSLGGQYGVQGFPTikIF 104
Cdd:cd02994   2 NVVELTDSNWTL-VLEGE--WMIEFYAPWCPACQQLQPEWEEFADWSDDLgINVAKVDVTQEPGLSGRFFVTALPT--IY 76

                        90       100
                ....*....|....*....|
gi 5031973  105 GSNKNRPEDYQGGRTGEAIV 124
Cdd:cd02994  77 HAKDGVFRRYQGPRDKEDLI 96
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 160-257 2.96e-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: 2.96e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  160 KDVIELTDDSFDkNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVKEQ--TKGKVKLAAVDATVNQVLASRYGIRGF 237
Cdd:cd02996   1 SEIVSLTSGNID-DILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEEfpDAGKVVWGKVDCDKESDIADRYRINKY 79

                        90       100
                ....*....|....*....|.
gi 5031973  238 PTIKIFQKGESP-VDYDGGRT 257
Cdd:cd02996  80 PTLKLFRNGMMMkREYRGQRS 100
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 26-125 6.72e-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: 70.50  E-value: 6.72e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   26 DVIELTPSNFNrEVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDV------VKVGAVDADKHHSLGGQYGVQGFP 99
Cdd:cd02996   2 EIVSLTSGNID-DILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEEfpdagkVVWGKVDCDKESDIADRYRINKYP 80

                        90       100
                ....*....|....*....|....*...
gi 5031973  100 TIKIF--GSNKNRpeDYQGGRTGEAIVD 125
Cdd:cd02996  81 TLKLFrnGMMMKR--EYRGQRSVEALAE 106
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 33-104 1.62e-14

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


Pssm-ID: 239245 [Multi-domain]  Cd Length: 93  Bit Score: 68.74  E-value: 1.62e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031973   33 SNFNREVIQSDSLwLVEFYAPWCGHCQRLTPEWKKAATALKDvVKVGAVDADKHHSLGGQYGVQGFPTIKIF 104
Cdd:cd02947   1 EEFEELIKSAKPV-VVDFWAPWCGPCKAIAPVLEELAEEYPK-VKFVKVDVDENPELAEEYGVRSIPTFLFF 70
trxA PRK09381
thioredoxin TrxA;
24-104 5.07e-12

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 62.39  E-value: 5.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973    24 SDDVIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKI 103
Cdd:PRK09381   2 SDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLL 81


                 .
gi 5031973   104 F 104
Cdd:PRK09381  82 F 82
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 34-125 1.33e-10

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 63.23  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973    34 NFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDV--VKVGAVDADKHHSLGGQYGVQGFPTIKIFGSNKNRP 111
Cdd:PTZ00102 366 TFEEIVFKSDKDVLLEIYAPWCGHCKNLEPVYNELGEKYKDNdsIIVAKMNGTANETPLEEFSWSAFPTILFVKAGERTP 445

                         90
                 ....*....|....
gi 5031973   112 EDYQGGRTGEAIVD 125
Cdd:PTZ00102 446 IPYEGERTVEGFKE 459
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 47-110 2.47e-10

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


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 56.17  E-value: 2.47e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031973   47 LVEFYAPWCGHCQRLTPEWKKAATALKDV--VKVGAVDADKHHSLGGQYGVQGFPTIKIFGSNKNR 110
Cdd:cd01659   1 LVLFYAPWCPFCQALRPVLAELALLNKGVkfEAVDVDEDPALEKELKRYGVGGVPTLVVFGPGIGV 66
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 183-251 3.51e-10

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


Pssm-ID: 239254 [Multi-domain]  Cd Length: 96  Bit Score: 56.51  E-value: 3.51e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5031973  183 VEFYAPWCGHCKNLEPewaaAASEVKEQTKGKVKLAAVDATVNQVLASRYGIRGFPTIKIFQKGEsPVD 251
Cdd:cd02956  17 VDFWAPRSPPSKELLP----LLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQ-PVD 80
PTZ00051 PTZ00051
thioredoxin; Provisional
 166-248 1.05e-09

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 55.27  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   166 TDDSFDKnVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEvkeqtKGKVKLAAVDATVNQVLASRYGIRGFPTIKIFQK 245
Cdd:PTZ00051   7 SQAEFES-TLSQNELVIVDFYAEWCGPCKRIAPFYEECSKE-----YTKMVFVKVDVDELSEVAEKENITSMPTFKVFKN 80


                 ...
gi 5031973   246 GES 248
Cdd:PTZ00051  81 GSV 83
PTZ00051 PTZ00051
thioredoxin; Provisional
 39-108 1.35e-09

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 54.88  E-value: 1.35e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973    39 VIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVgAVDADKHHSLGGQYGVQGFPTIKIFGSNK 108
Cdd:PTZ00051  14 TLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFV-KVDVDELSEVAEKENITSMPTFKVFKNGS 82
PRK10996 PRK10996
thioredoxin 2; Provisional
 26-104 4.07e-09

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 54.69  E-value: 4.07e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5031973    26 DVIELTPSNFNrEVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIF 104
Cdd:PRK10996  36 EVINATGETLD-KLLQDDLPVVIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIF 113
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 46-118 7.89e-09

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: 53.23  E-value: 7.89e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031973   46 WLVEFYAPWCGHCQRLTPEWKKAATALKDV-VKVGAVDADKHHSLGGQ--YGVQGFPTIKIFGSNKNRPEDYQGGR 118
Cdd:cd02993  24 TLVVLYAPWCPFCQAMEASYEELAEKLAGSnVKVAKFNADGEQREFAKeeLQLKSFPTILFFPKNSRQPIKYPSEQ 99
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 46-133 9.85e-09

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 53.54  E-value: 9.85e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   46 WLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVG-AVD--------------------ADKHHSLGGQYGVQGFPTIKIF 104
Cdd:COG0526  31 VLVNFWATWCPPCRAEMPVLKELAEEYGGVVFVGvDVDenpeavkaflkelglpypvlLDPDGELAKAYGVRGIPTTVLI 110

                        90       100
                ....*....|....*....|....*....
gi 5031973  105 GSNKNRPEDYQGGRTGEAIVDAALSALRQ 133
Cdd:COG0526 111 DKDGKIVARHVGPLSPEELEEALEKLLAK 139
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 47-125 1.76e-08

PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of uncharacterized PDI-like eukaryotic proteins containing only one redox active TRX (a) domain with a CXXS motif, similar to ERp44. CXXS is still a redox active motif; however, the mixed disulfide formed with the substrate is more stable than those formed by CXXC motif proteins. PDI-related proteins are usually involved in the oxidative protein folding in the ER by acting as catalysts and folding assistants. ERp44 is involved in thiol-mediated retention in the ER.


Pssm-ID: 239297 [Multi-domain]  Cd Length: 100  Bit Score: 51.98  E-value: 1.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   47 LVEFYAPWCGHCQRLTPEWKKAATALKDVvKVGAVDADK-HHSLGGQYGVQGFPTIKIFGSNKN-RpedYQGGRTGEAIV 124
Cdd:cd02999  22 AVLFYASWCPFSASFRPHFNALSSMFPQI-RHLAIEESSiKPSLLSRYGVVGFPTILLFNSTPRvR---YNGTRTLDSLA 97


                .
gi 5031973  125 D 125
Cdd:cd02999  98 A 98
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 33-123 5.26e-08

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


Pssm-ID: 239254 [Multi-domain]  Cd Length: 96  Bit Score: 50.35  E-value: 5.26e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   33 SNFNREVIQSD-SLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIFgsNKNRP 111
Cdd:cd02956   1 QNFQQVLQESTqVPVVVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLF--AAGQP 78

                        90
                ....*....|...
gi 5031973  112 ED-YQGGRTGEAI 123
Cdd:cd02956  79 VDgFQGAQPEEQL 91
PLN02309 PLN02309
5'-adenylylsulfate reductase
 46-114 6.59e-08

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 54.41  E-value: 6.59e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031973    46 WLVEFYAPWCGHCQRLTPEWKKAATALKDV-VKVGAVDADKHHSLGGQYGVQ--GFPTIKIFGSNKNRPEDY 114
Cdd:PLN02309 368 WLVVLYAPWCPFCQAMEASYEELAEKLAGSgVKVAKFRADGDQKEFAKQELQlgSFPTILLFPKNSSRPIKY 439
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 182-247 8.49e-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: 49.23  E-value: 8.49e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5031973  182 MVEFYAPWCGHCKNLEPEWAAAASEvkeqtKGKVKLAAVDATVNQVL---ASRYGIRGFPTIKIFQKGE 247
Cdd:cd01659   1 LVLFYAPWCPFCQALRPVLAELALL-----NKGVKFEAVDVDEDPALekeLKRYGVGGVPTLVVFGPGI 64
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 178-257 9.24e-08

PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of uncharacterized PDI-like eukaryotic proteins containing only one redox active TRX (a) domain with a CXXS motif, similar to ERp44. CXXS is still a redox active motif; however, the mixed disulfide formed with the substrate is more stable than those formed by CXXC motif proteins. PDI-related proteins are usually involved in the oxidative protein folding in the ER by acting as catalysts and folding assistants. ERp44 is involved in thiol-mediated retention in the ER.


Pssm-ID: 239297 [Multi-domain]  Cd Length: 100  Bit Score: 49.66  E-value: 9.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  178 EDVWMVEFYAPWCGHCKNLEPEWAAAASEVKEqtkgkVKLAAVDATVNQ-VLASRYGIRGFPTIKIFQkgESP-VDYDGG 255
Cdd:cd02999  18 EDYTAVLFYASWCPFSASFRPHFNALSSMFPQ-----IRHLAIEESSIKpSLLSRYGVVGFPTILLFN--STPrVRYNGT 90


                ..
gi 5031973  256 RT 257
Cdd:cd02999  91 RT 92
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 181-256 1.07e-07

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


Pssm-ID: 239291 [Multi-domain]  Cd Length: 109  Bit Score: 49.76  E-value: 1.07e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5031973  181 WMVEFYAPWCGHCKNLEPEWAAAASEVKEQtkgKVKLAAVDATVNQVLASR--YGIRGFPTIKIFQKGES-PVDYDGGR 256
Cdd:cd02993  24 TLVVLYAPWCPFCQAMEASYEELAEKLAGS---NVKVAKFNADGEQREFAKeeLQLKSFPTILFFPKNSRqPIKYPSEQ 99
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 46-114 1.33e-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: 50.40  E-value: 1.33e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031973     46 WLVEFYAPWCGHCQRLTPEWKKAATALKDV-VKVGAVDADKHHSLGGQYGVQ--GFPTIKIFGSNKNRPEDY 114
Cdd:TIGR00424 374 WLVVLYAPWCPFCQAMEASYLELAEKLAGSgVKVAKFRADGDQKEFAKQELQlgSFPTILFFPKHSSRPIKY 445
DsbDgamma cd02953
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
 182-251 2.42e-06

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: 46.06  E-value: 2.42e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5031973  182 MVEFYAPWCGHCKNLEPEwAAAASEVKEQTKGKVKLAAVDAT----VNQVLASRYGIRGFPTIKIFQKGESPVD 251
Cdd:cd02953  15 FVDFTADWCVTCKVNEKV-VFSDPEVQAALKKDVVLLRADWTkndpEITALLKRFGVFGPPTYLFYGPGGEPEP 87
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 41-116 2.66e-06

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


Pssm-ID: 239247 [Multi-domain]  Cd Length: 97  Bit Score: 45.57  E-value: 2.66e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031973   41 QSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIFgSNKNRPEDYQG 116
Cdd:cd02949  11 ESDRLILVLYTSPTCGPCRTLKPILNKVIDEFDGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFF-KDKELVKEISG 85
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 163-267 2.80e-06

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 46.61  E-value: 2.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  163 IELTDdsFDKNVLDSED----VWMVEFYAPWCGHCKNLEPEWAAAASEVK---------EQTKGKVKLAAVDATV----- 224
Cdd:COG0526  11 FTLTD--LDGKPLSLADlkgkPVLVNFWATWCPPCRAEMPVLKELAEEYGgvvfvgvdvDENPEAVKAFLKELGLpypvl 88

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 5031973  225 ---NQVLASRYGIRGFPTIKIFQKGESPVDYDGGRTRSDIVSRALD 267
Cdd:COG0526  89 ldpDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALE 134
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 182-276 6.78e-06

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: 45.79  E-value: 6.78e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  182 MVEFYAPWCGHCKNLEPEWAaaasEVKEQTKGKVKLAA--VDATVNQVLASRYGIRGFPTIKIFQKGESPVDYDGGRTRS 259
Cdd:cd02950  24 LVEFYADWCTVCQEMAPDVA----KLKQKYGDQVNFVMlnVDNPKWLPEIDRYRVDGIPHFVFLDREGNEEGQSIGLQPK 99

                        90
                ....*....|....*..
gi 5031973  260 DIVSRALDLFSDNAPPP 276
Cdd:cd02950 100 QVLAQNLDALVAGEPLP 116
PDI_a_EFP1_N cd03006
PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase ...
 162-255 2.40e-05

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


Pssm-ID: 239304  Cd Length: 113  Bit Score: 43.23  E-value: 2.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  162 VIELTDDSFDKNVLDSE--DVWMVEFYAPWCGHCKNLEPEWAAAASEVKEQtkgkVKLAAVDATVNQVLASR-YGIRGFP 238
Cdd:cd03006  11 VLDFYKGQLDYAEELRTdaEVSLVMYYAPWDAQSQAARQEFEQVAQKLSDQ----VLFVAINCWWPQGKCRKqKHFFYFP 86

                        90
                ....*....|....*..
gi 5031973  239 TIKIFQKGESPVDYDGG 255
Cdd:cd03006  87 VIHLYYRSRGPIEYKGP 103
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 172-252 6.90e-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: 45.01  E-value: 6.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973    172 KNVLDSE---DVWMVEFYAPWCGHCKNLEpewaAAASEVKEQTKGK-VKLAAVDATVNQVLASRYGIR--GFPTIKIFQK 245
Cdd:TIGR00424 362 ENLLKLEerkEAWLVVLYAPWCPFCQAME----ASYLELAEKLAGSgVKVAKFRADGDQKEFAKQELQlgSFPTILFFPK 437


                  ....*...
gi 5031973    246 GES-PVDY 252
Cdd:TIGR00424 438 HSSrPIKY 445
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 182-243 8.42e-05

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 42.58  E-value: 8.42e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5031973  182 MVEFYAPWCGHCKNLEPEwAAAASEVKEQTKGKVKLAAVDA-------------TVNQVLASRYGIRGFPTIKIF 243
Cdd:COG2143  44 LLFFESDWCPYCKKLHKE-VFSDPEVAAYLKENFVVVQLDAegdkevtdfdgetLTEKELARKYGVRGTPTLVFF 117
PDI_a_EFP1_N cd03006
PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase ...
 21-119 8.56e-05

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


Pssm-ID: 239304  Cd Length: 113  Bit Score: 41.69  E-value: 8.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   21 YSSSDDVIELTPSNFNR--EVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDAdkHHSLG---GQYGV 95
Cdd:cd03006   5 FSQRSPVLDFYKGQLDYaeELRTDAEVSLVMYYAPWDAQSQAARQEFEQVAQKLSDQVLFVAINC--WWPQGkcrKQKHF 82

                        90       100
                ....*....|....*....|....
gi 5031973   96 QGFPTIKIFGSNKNRPEDYQGGRT 119
Cdd:cd03006  83 FYFPVIHLYYRSRGPIEYKGPMRA 106
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 47-104 1.00e-04

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 42.20  E-value: 1.00e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031973   47 LVEFYAPWCGHCQRL------TPEWKKAATALKDVVKvgaVDAD-------------KHHSLGGQYGVQGFPTIKIF 104
Cdd:COG2143  44 LLFFESDWCPYCKKLhkevfsDPEVAAYLKENFVVVQ---LDAEgdkevtdfdgetlTEKELARKYGVRGTPTLVFF 117
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 176-260 1.07e-04

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


Pssm-ID: 239247 [Multi-domain]  Cd Length: 97  Bit Score: 40.95  E-value: 1.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  176 DSEDVWMVEFYAPWCGHCKNLEPEwaaaASEVKEQTKGKVKLAAVDATVNQVLASRYGIRGFPTIKIFQKGESPVDYDGG 255
Cdd:cd02949  11 ESDRLILVLYTSPTCGPCRTLKPI----LNKVIDEFDGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDKELVKEISGV 86


                ....*
gi 5031973  256 RTRSD 260
Cdd:cd02949  87 KMKSE 91
Thioredoxin_7 pfam13899
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 182-243 1.11e-04

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


Pssm-ID: 433567 [Multi-domain]  Cd Length: 84  Bit Score: 40.81  E-value: 1.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031973    182 MVEFYAPWCGHCKNLEpEWAAAASEVKEQTKGK-VKLAAVDATVNQVLASRYGIRGFPTIKIF 243
Cdd:pfam13899  21 LVDFGADWCFTCQVLE-RDFLSHEEVKAALAKNfVLLRLDWTSRDANITRAFDGQGVPHIAFL 82
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 47-131 1.81e-04

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: 41.55  E-value: 1.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   47 LVEFYAPWCGHCQRLTPEWKKAATALKD---VVKVGaVDADKHHSLGGQYGVQGFPTIKIFgSNKNRPEDYQGGRTGEAI 123
Cdd:cd02950  24 LVEFYADWCTVCQEMAPDVAKLKQKYGDqvnFVMLN-VDNPKWLPEIDRYRVDGIPHFVFL-DREGNEEGQSIGLQPKQV 101


                ....*...
gi 5031973  124 VDAALSAL 131
Cdd:cd02950 102 LAQNLDAL 109
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
182-266 2.67e-04

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 40.10  E-value: 2.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973    182 MVEFYAPWCGHCKNLEPE---WAAAASEVKEQTKGK---------VKLAAVDATVNQVLASRYGIRGFPTIkIFQKGESP 249
Cdd:pfam13098   8 LVVFTDPDCPYCKKLKKElleDPDVTVYLGPNFVFIavniwcakeVAKAFTDILENKELGRKYGVRGTPTI-VFFDGKGE 86

                          90
                  ....*....|....*..
gi 5031973    250 VDYDGGRTRSDIVSRAL 266
Cdd:pfam13098  87 LLRLPGYVPAEEFLALL 103
TRX_GRX_like cd02973
Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins ...
 185-242 3.32e-04

Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins that show similarity to both TRX and GRX, including the C-terminal TRX-fold subdomain of Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO). All members contain a redox-active CXXC motif and may function as PDOs. The archaeal proteins Mj0307 and Mt807 show structures more similar to GRX, but activities more similar to TRX. Some members of the family are similar to PfPDO in that they contain a second CXXC motif located in a second TRX-fold subdomain at the N-terminus; the superimposable N- and C-terminal TRX subdomains form a compact structure. PfPDO is postulated to be the archaeal counterpart of bacterial DsbA and eukaryotic protein disulfide isomerase (PDI). The C-terminal CXXC motif of PfPDO is required for its oxidase, reductase and isomerase activities. Also included in the family is the C-terminal TRX-fold subdomain of the N-terminal domain (NTD) of bacterial AhpF, which has a similar fold as PfPDO with two TRX-fold subdomains but without the second CXXC motif.


Pssm-ID: 239271 [Multi-domain]  Cd Length: 67  Bit Score: 38.70  E-value: 3.32e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5031973  185 FYAPWCGHCknlePEWAAAASEVKEqTKGKVKLAAVDATVNQVLASRYGIRGFPTIKI 242
Cdd:cd02973   6 FVSPTCPYC----PDAVQAANRIAA-LNPNISAEMIDAAEFPDLADEYGVMSVPAIVI 58
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 164-262 5.82e-04

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


Pssm-ID: 239261 [Multi-domain]  Cd Length: 111  Bit Score: 39.28  E-value: 5.82e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  164 ELTDDSFDKnvldsedVWMVEFYAPWCGHCKNLEPEWAAAASEVKEQTKGkvkLAAVDATVNQVLASRYGIRGFPTIKIF 243
Cdd:cd02963  17 EIVPKSFKK-------PYLIKITSDWCFSCIHIEPVWKEVIQELEPLGVG---IATVNAGHERRLARKLGAHSVPAIVGI 86

                        90
                ....*....|....*....
gi 5031973  244 QKGESPVDYDGGRTRSDIV 262
Cdd:cd02963  87 INGQVTFYHDSSFTKQHVV 105
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 22-101 9.36e-04

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


Pssm-ID: 239261 [Multi-domain]  Cd Length: 111  Bit Score: 38.89  E-value: 9.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   22 SSSDDVIELTPSNFNREVIqSDSL---WLVEFYAPWCGHCQRLTPEWKKAATALKDV-VKVGAVDADKHHSLGGQYGVQG 97
Cdd:cd02963   1 DSFDYKYSLTFSQYENEIV-PKSFkkpYLIKITSDWCFSCIHIEPVWKEVIQELEPLgVGIATVNAGHERRLARKLGAHS 79


                ....
gi 5031973   98 FPTI 101
Cdd:cd02963  80 VPAI 83
PLN02309 PLN02309
5'-adenylylsulfate reductase
 178-263 1.05e-03

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 41.31  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973   178 EDVWMVEFYAPWCGHCKNLEpewaAAASEVKEQTKGK-VKLAAVDATVNQVLASRYGI--RGFPTIKIFQKGES-PVDYd 253
Cdd:PLN02309 365 KEPWLVVLYAPWCPFCQAME----ASYEELAEKLAGSgVKVAKFRADGDQKEFAKQELqlGSFPTILLFPKNSSrPIKY- 439

                         90
                 ....*....|
gi 5031973   254 gGRTRSDIVS 263
Cdd:PLN02309 440 -PSEKRDVDS 448
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
228-387 1.81e-03

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 39.27  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973    228 LASRYGIRgFPTIKIFQK-GESPVDYDGGRTRSDIVSRaldlFSDNAPPPeLLEIINEDIAKRTCEEHQLCVVAVlphIL 306
Cdd:pfam13848  33 VADKYNIK-EPAILLFRKfDEETVHYPGDSINFEDLKK----FIQKNCLP-LVREFTPENAEELFEEGIPPLLLL---FL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973    307 DTGAAGRNSYLEVLLKLADKYKKKMwGWLWTEAGA-QSELETaLGIGGFGYPAMAAIN-ARKMKFALLKGSFSEQGINEF 384
Cdd:pfam13848 104 KKDDESTEEFKKALEKVAKKFRGKI-NFALVDAKSfGRPLEY-FGLSESDLPVIVIVDsFSHMYKYFPSDEFSPESLKEF 181


                  ...
gi 5031973    385 LRE 387
Cdd:pfam13848 182 IND 184
DsbDgamma cd02953
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
 47-111 1.86e-03

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


Pssm-ID: 239251 [Multi-domain]  Cd Length: 104  Bit Score: 37.58  E-value: 1.86e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031973   47 LVEFYAPWCGHCQ---RLT---PEWKKAATalKDVVkvgAVDAD------KHHSLGGQYGVQGFPTIKIFGSNKNRP 111
Cdd:cd02953  15 FVDFTADWCVTCKvneKVVfsdPEVQAALK--KDVV---LLRADwtkndpEITALLKRFGVFGPPTYLFYGPGGEPE 86
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
47-104 1.90e-03

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 37.79  E-value: 1.90e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5031973     47 LVEFYAPWCGHCQRL--------------TPEWKKAATALK--DVVKVGAVDADKHHSLGGQYGVQGFPTIKIF 104
Cdd:pfam13098   8 LVVFTDPDCPYCKKLkkelledpdvtvylGPNFVFIAVNIWcaKEVAKAFTDILENKELGRKYGVRGTPTIVFF 81
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 183-257 3.96e-03

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


Pssm-ID: 239309 [Multi-domain]  Cd Length: 123  Bit Score: 37.28  E-value: 3.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031973  183 VEFYAPWCGHCKNLEPEWAAAASEV-------KEQTKGKVK--LAAVD---ATVNQ---VLASRYGIRGFPTIKIFQKGE 247
Cdd:cd03011  25 VYFWATWCPVCRFTSPTVNQLAADYpvvsvalRSGDDGAVArfMQKKGygfPVINDpdgVISARWGVSVTPAIVIVDPGG 104

                        90
                ....*....|
gi 5031973  248 SpVDYDGGRT 257
Cdd:cd03011 105 I-VFVTTGVT 113
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 47-100 6.84e-03

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


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 36.45  E-value: 6.84e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031973   47 LVEFYAPWCGHCQRLTPEWKKAA--TALKDVVKVG-AVD---------------------ADKHHSLGGQYGVQGFPT 100
Cdd:cd02966  23 LVNFWASWCPPCRAEMPELEALAkeYKDDGVEVVGvNVDdddpaavkaflkkygitfpvlLDPDGELAKAYGVRGLPT 100
 
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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