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Conserved domains on  [gi|79336174|ref|NP_171990|]
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PDI-like 2-2 [Arabidopsis thaliana]

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) ...
 279-408 9.89e-61

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: 193.72  E-value: 9.89e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 279 PAEVTELTGPDVMEDKCGSAAICFVSFLPDILDSKAEGRNKYLEMLLSVADKFKKDPYGFVWVAAGKQPDLEKRVGVGGY 358
Cdd:cd02983   1 APEIIELTSEDVFEETCEEKQLCIIAFLPHILDCQASCRNKYLEILKSVAEKFKKKPWGWLWTEAGAQLDLEEALNIGGF 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 79336174 359 GYPAMVALNAKKGAYAPLKSGFEVKHLKDFVKEAAKGGKGNLPIDGTMEI 408
Cdd:cd02983  81 GYPAMVAINFRKMKFATLKGSFSEDGINEFLRELSYGRGPTLPVNGLPKV 130
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 168-270 1.21e-57

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: 184.80  E-value: 1.21e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 168 ASVELNSSNFDELVTESKELWIVEFFAPWCGHCKKLAPEWKKAANNLKGKVKLGHVNCDAEQSIKSRFKVQGFPTILVFG 247
Cdd:cd03001   1 DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVFG 80

                        90       100
                ....*....|....*....|...
gi 79336174 248 SDKSSPVPYEGARSASAIESFAL 270
Cdd:cd03001  81 AGKNSPQDYQGGRTAKAIVSAAL 103
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 33-134 2.31e-54

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: 176.32  E-value: 2.31e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  33 PVLQLTPSNFKSKVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGIATVAAIDADAHKSVSQDYGVRGFPTIKVFV 112
Cdd:cd03001   1 DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVFG 80

                        90       100
                ....*....|....*....|...
gi 79336174 113 PGK-PPIDYQGARDAKSISQFAI 134
Cdd:cd03001  81 AGKnSPQDYQGGRTAKAIVSAAL 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) ...
 279-408 9.89e-61

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: 193.72  E-value: 9.89e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 279 PAEVTELTGPDVMEDKCGSAAICFVSFLPDILDSKAEGRNKYLEMLLSVADKFKKDPYGFVWVAAGKQPDLEKRVGVGGY 358
Cdd:cd02983   1 APEIIELTSEDVFEETCEEKQLCIIAFLPHILDCQASCRNKYLEILKSVAEKFKKKPWGWLWTEAGAQLDLEEALNIGGF 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 79336174 359 GYPAMVALNAKKGAYAPLKSGFEVKHLKDFVKEAAKGGKGNLPIDGTMEI 408
Cdd:cd02983  81 GYPAMVAINFRKMKFATLKGSFSEDGINEFLRELSYGRGPTLPVNGLPKV 130
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 168-270 1.21e-57

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: 184.80  E-value: 1.21e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 168 ASVELNSSNFDELVTESKELWIVEFFAPWCGHCKKLAPEWKKAANNLKGKVKLGHVNCDAEQSIKSRFKVQGFPTILVFG 247
Cdd:cd03001   1 DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVFG 80

                        90       100
                ....*....|....*....|...
gi 79336174 248 SDKSSPVPYEGARSASAIESFAL 270
Cdd:cd03001  81 AGKNSPQDYQGGRTAKAIVSAAL 103
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 33-134 2.31e-54

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: 176.32  E-value: 2.31e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  33 PVLQLTPSNFKSKVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGIATVAAIDADAHKSVSQDYGVRGFPTIKVFV 112
Cdd:cd03001   1 DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVFG 80

                        90       100
                ....*....|....*....|...
gi 79336174 113 PGK-PPIDYQGARDAKSISQFAI 134
Cdd:cd03001  81 AGKnSPQDYQGGRTAKAIVSAAL 103
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 172-272 6.64e-44

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: 148.98  E-value: 6.64e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   172 LNSSNFDELVTESKeLWIVEFFAPWCGHCKKLAPEWKKAANNLKG--KVKLGHVNCDAEQSIKSRFKVQGFPTILVFGSD 249
Cdd:TIGR01126   1 LTASNFDEIVLSNK-DVLVEFYAPWCGHCKNLAPEYEKLAKELKKdpKIVLAKVDATAEKDLASRFGVSGFPTIKFFPKG 79

                          90       100
                  ....*....|....*....|...
gi 79336174   250 KsSPVPYEGARSASAIESFALEQ 272
Cdd:TIGR01126  80 S-KPVDYEGGRDLEAIVEFVNEK 101
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 37-137 2.79e-43

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: 147.43  E-value: 2.79e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174    37 LTPSNFKSKVLnSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGI--ATVAAIDADAHKSVSQDYGVRGFPTIKVFVPG 114
Cdd:TIGR01126   1 LTASNFDEIVL-SNKDVLVEFYAPWCGHCKNLAPEYEKLAKELKKDpkIVLAKVDATAEKDLASRFGVSGFPTIKFFPKG 79

                          90       100
                  ....*....|....*....|...
gi 79336174   115 KPPIDYQGARDAKSISQFAIKQI 137
Cdd:TIGR01126  80 SKPVDYEGGRDLEAIVEFVNEKS 102
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 34-395 4.88e-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: 140.97  E-value: 4.88e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174    34 VLQLTPSNFKSkVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLK---GIATVAAIDADAHKSVSQDYGVRGFPTIKV 110
Cdd:TIGR01130   3 VLVLTKDNFDD-FIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKkkgPPIKLAKVDATEEKDLAQKYGVSGYPTLKI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   111 FVPGKP-PIDYQGARDAKSISQFAIKQIKallkdrldgktsgtkngggssekkksePsASVELNSSNFDELVTESKELWI 189
Cdd:TIGR01130  82 FRNGEDsVSDYNGPRDADGIVKYMKKQSG---------------------------P-AVKEIETVADLEAFLADDDVVV 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   190 VEFFApwcGHCKKLAPEWKKAANNLKGKVKLGHVNCDAEQSIKSRFKVQGFPTILVFGSD-KSSPVPYEGARSASAIESF 268
Cdd:TIGR01130 134 IGFFK---DLDSELNDTFLSVAEKLRDVYFFFAHSSDVAAFAKLGAFPDSVVLFKPKDEDeKFSKVDGEMDTDVSDLEKF 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   269 AleqLESNAGPA-EVTELTGPDVMEDKCGSAAICFVSFlpdILDSKAEGRNKYLEmllsVADKFKKDPYGFVWVAAGK-Q 346
Cdd:TIGR01130 211 I---RAESLPLVgEFTQETAAKYFESGPLVVLYYNVDE---SLDPFEELRNRFLE----AAKKFRGKFVNFAVADEEDfG 280

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 79336174   347 PDLEKrVGVGGYGYPAMVALN-AKKGAYAPLKSGFEVKHLKDFVKEAAKG 395
Cdd:TIGR01130 281 RELEY-FGLKAEKFPAVAIQDlEGNKKYPMDQEEFSSENLEAFVKDFLDG 329
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 33-135 1.78e-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: 124.27  E-value: 1.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174    33 PVLQLTPSNFKSKVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGIATVAAIDADAHKSVSQDYGVRGFPTIKVFV 112
Cdd:pfam00085   1 VVVVLTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFK 80

                          90       100
                  ....*....|....*....|...
gi 79336174   113 PGKPPIDYQGARDAKSISQFAIK 135
Cdd:pfam00085  81 NGQPVDDYVGARPKDALAAFLKA 103
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 34-132 6.77e-30

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: 111.84  E-value: 6.77e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  34 VLQLTPSNFKSKVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGIATVAAIDADAHKSVSQDYGVRGFPTIKVFVP 113
Cdd:COG3118   2 VVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLFKD 81

                        90
                ....*....|....*....
gi 79336174 114 GKPPIDYQGARDAKSISQF 132
Cdd:COG3118  82 GQPVDRFVGALPKEQLREF 100
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 170-268 1.42e-29

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


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 110.79  E-value: 1.42e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   170 VELNSSNFDELVTESKELWIVEFFAPWCGHCKKLAPEWKKAANNLKGKVKLGHVNCDAEQSIKSRFKVQGFPTILvFGSD 249
Cdd:pfam00085   3 VVLTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLI-FFKN 81

                          90
                  ....*....|....*....
gi 79336174   250 KSSPVPYEGARSASAIESF 268
Cdd:pfam00085  82 GQPVDDYVGARPKDALAAF 100
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 167-346 5.72e-28

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 115.62  E-value: 5.72e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  167 SASVELNSSNFDELVTEsKELWIVEFFAPWCGHCKKLAPEWKKAANNLK---GKVKLGHVNCDAEQSIKSRFKVQGFPTI 243
Cdd:PTZ00102  32 EHVTVLTDSTFDKFITE-NEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKekkSEIVLASVDATEEMELAQEFGVRGYPTI 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  244 LVFgsDKSSPVPYEGARSASAIESFaLEQLesnAGPAeVTELTGPDVMEDKcgsAAICFVSFLPDILDSKAEGRNKYLEm 323
Cdd:PTZ00102 111 KFF--NKGNPVNYSGGRTADGIVSW-IKKL---TGPA-VTEVESASEIKLI---AKKIFVAFYGEYTSKDSELYKKFEE- 179

                        170       180
                 ....*....|....*....|...
gi 79336174  324 llsVADKFKKDPYGFVWVAAGKQ 346
Cdd:PTZ00102 180 ---VADKHREHAKFFVKKHEGKN 199
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 170-273 6.24e-27

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: 103.75  E-value: 6.24e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 170 VELNSSNFDELVTESKELWIVEFFAPWCGHCKKLAPEWKKAANNLKGKVKLGHVNCDAEQSIKSRFKVQGFPTILVFgsD 249
Cdd:COG3118   3 VELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLF--K 80

                        90       100
                ....*....|....*....|....*
gi 79336174 250 KSSPVP-YEGARSASAIESFaLEQL 273
Cdd:COG3118  81 DGQPVDrFVGALPKEQLREF-LDKV 104
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 1-137 2.51e-24

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 104.83  E-value: 2.51e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174    1 MERKMYKSTVFPICCLLFALFDRGNALYGSSSpVLQLTPSNFKsKVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLK 80
Cdd:PTZ00102   2 GFRSILSSLFLLLILLAFAVFGSAEEHFISEH-VTVLTDSTFD-KFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLK 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   81 GIAT---VAAIDADAHKSVSQDYGVRGFPTIKVFvPGKPPIDYQGARDAKSISQFaIKQI 137
Cdd:PTZ00102  80 EKKSeivLASVDATEEMELAQEFGVRGYPTIKFF-NKGNPVNYSGGRTADGIVSW-IKKL 137
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
201-391 2.07e-08

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 53.90  E-value: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   201 KKLAPEWKKAANNLKGKVKLGHVNcDAEQSIKSRFKvqgFPTILVFGSDKSSPVPYEG-ARSASAIESFALEQLESNAGp 279
Cdd:pfam13848   6 SPLYEIFRKAAKELKGDVRFGITF-SKEVADKYNIK---EPAILLFRKFDEETVHYPGdSINFEDLKKFIQKNCLPLVR- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   280 aEVTELTGPDVMEDKCGSAAICFvsflpdiLDSKAEGRNKYLEMLLSVADKFkKDPYGFVWVAAGKQPDLEKRVGVGGYG 359
Cdd:pfam13848  81 -EFTPENAEELFEEGIPPLLLLF-------LKKDDESTEEFKKALEKVAKKF-RGKINFALVDAKSFGRPLEYFGLSESD 151

                         170       180       190
                  ....*....|....*....|....*....|...
gi 79336174   360 YPAMVALNAKKGAYAPLKSG-FEVKHLKDFVKE 391
Cdd:pfam13848 152 LPVIVIVDSFSHMYKYFPSDeFSPESLKEFIND 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) ...
 279-408 9.89e-61

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: 193.72  E-value: 9.89e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 279 PAEVTELTGPDVMEDKCGSAAICFVSFLPDILDSKAEGRNKYLEMLLSVADKFKKDPYGFVWVAAGKQPDLEKRVGVGGY 358
Cdd:cd02983   1 APEIIELTSEDVFEETCEEKQLCIIAFLPHILDCQASCRNKYLEILKSVAEKFKKKPWGWLWTEAGAQLDLEEALNIGGF 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 79336174 359 GYPAMVALNAKKGAYAPLKSGFEVKHLKDFVKEAAKGGKGNLPIDGTMEI 408
Cdd:cd02983  81 GYPAMVAINFRKMKFATLKGSFSEDGINEFLRELSYGRGPTLPVNGLPKV 130
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 168-270 1.21e-57

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: 184.80  E-value: 1.21e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 168 ASVELNSSNFDELVTESKELWIVEFFAPWCGHCKKLAPEWKKAANNLKGKVKLGHVNCDAEQSIKSRFKVQGFPTILVFG 247
Cdd:cd03001   1 DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVFG 80

                        90       100
                ....*....|....*....|...
gi 79336174 248 SDKSSPVPYEGARSASAIESFAL 270
Cdd:cd03001  81 AGKNSPQDYQGGRTAKAIVSAAL 103
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 33-134 2.31e-54

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: 176.32  E-value: 2.31e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  33 PVLQLTPSNFKSKVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGIATVAAIDADAHKSVSQDYGVRGFPTIKVFV 112
Cdd:cd03001   1 DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVFG 80

                        90       100
                ....*....|....*....|...
gi 79336174 113 PGK-PPIDYQGARDAKSISQFAI 134
Cdd:cd03001  81 AGKnSPQDYQGGRTAKAIVSAAL 103
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 172-272 6.64e-44

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: 148.98  E-value: 6.64e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   172 LNSSNFDELVTESKeLWIVEFFAPWCGHCKKLAPEWKKAANNLKG--KVKLGHVNCDAEQSIKSRFKVQGFPTILVFGSD 249
Cdd:TIGR01126   1 LTASNFDEIVLSNK-DVLVEFYAPWCGHCKNLAPEYEKLAKELKKdpKIVLAKVDATAEKDLASRFGVSGFPTIKFFPKG 79

                          90       100
                  ....*....|....*....|...
gi 79336174   250 KsSPVPYEGARSASAIESFALEQ 272
Cdd:TIGR01126  80 S-KPVDYEGGRDLEAIVEFVNEK 101
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 37-137 2.79e-43

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: 147.43  E-value: 2.79e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174    37 LTPSNFKSKVLnSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGI--ATVAAIDADAHKSVSQDYGVRGFPTIKVFVPG 114
Cdd:TIGR01126   1 LTASNFDEIVL-SNKDVLVEFYAPWCGHCKNLAPEYEKLAKELKKDpkIVLAKVDATAEKDLASRFGVSGFPTIKFFPKG 79

                          90       100
                  ....*....|....*....|...
gi 79336174   115 KPPIDYQGARDAKSISQFAIKQI 137
Cdd:TIGR01126  80 SKPVDYEGGRDLEAIVEFVNEKS 102
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 170-269 4.68e-40

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


Pssm-ID: 239259 [Multi-domain]  Cd Length: 101  Bit Score: 138.90  E-value: 4.68e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 170 VELNSSNFDELVTESKeLWIVEFFAPWCGHCKKLAPEWKKAANNLK--GKVKLGHVNCDAEQSIKSRFKVQGFPTILVFG 247
Cdd:cd02961   1 VELTDDNFDELVKDSK-DVLVEFYAPWCGHCKALAPEYEKLAKELKgdGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFP 79

                        90       100
                ....*....|....*....|..
gi 79336174 248 SDKSSPVPYEGARSASAIESFA 269
Cdd:cd02961  80 NGSKEPVKYEGPRTLESLVEFI 101
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 33-133 1.21e-37

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: 132.87  E-value: 1.21e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  33 PVLQLTPSNFKSKVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGIATVAAI--DADAHKSVSQDYGVRGFPTIKV 110
Cdd:cd03002   1 PVYELTPKNFDKVVHNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKELDGLVQVAAVdcDEDKNKPLCGKYGVQGFPTLKV 80

                        90       100
                ....*....|....*....|....*...
gi 79336174 111 FVPGKP-----PIDYQGARDAKSISQFA 133
Cdd:cd03002  81 FRPPKKaskhaVEDYNGERSAKAIVDFV 108
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 35-133 1.40e-37

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: 132.35  E-value: 1.40e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  35 LQLTPSNFKsKVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLK--GIATVAAIDADAHKSVSQDYGVRGFPTIKVFV 112
Cdd:cd02961   1 VELTDDNFD-ELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKgdGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFP 79

                        90       100
                ....*....|....*....|..
gi 79336174 113 PG-KPPIDYQGARDAKSISQFA 133
Cdd:cd02961  80 NGsKEPVKYEGPRTLESLVEFI 101
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 34-395 4.88e-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: 140.97  E-value: 4.88e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174    34 VLQLTPSNFKSkVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLK---GIATVAAIDADAHKSVSQDYGVRGFPTIKV 110
Cdd:TIGR01130   3 VLVLTKDNFDD-FIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKkkgPPIKLAKVDATEEKDLAQKYGVSGYPTLKI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   111 FVPGKP-PIDYQGARDAKSISQFAIKQIKallkdrldgktsgtkngggssekkksePsASVELNSSNFDELVTESKELWI 189
Cdd:TIGR01130  82 FRNGEDsVSDYNGPRDADGIVKYMKKQSG---------------------------P-AVKEIETVADLEAFLADDDVVV 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   190 VEFFApwcGHCKKLAPEWKKAANNLKGKVKLGHVNCDAEQSIKSRFKVQGFPTILVFGSD-KSSPVPYEGARSASAIESF 268
Cdd:TIGR01130 134 IGFFK---DLDSELNDTFLSVAEKLRDVYFFFAHSSDVAAFAKLGAFPDSVVLFKPKDEDeKFSKVDGEMDTDVSDLEKF 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   269 AleqLESNAGPA-EVTELTGPDVMEDKCGSAAICFVSFlpdILDSKAEGRNKYLEmllsVADKFKKDPYGFVWVAAGK-Q 346
Cdd:TIGR01130 211 I---RAESLPLVgEFTQETAAKYFESGPLVVLYYNVDE---SLDPFEELRNRFLE----AAKKFRGKFVNFAVADEEDfG 280

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 79336174   347 PDLEKrVGVGGYGYPAMVALN-AKKGAYAPLKSGFEVKHLKDFVKEAAKG 395
Cdd:TIGR01130 281 RELEY-FGLKAEKFPAVAIQDlEGNKKYPMDQEEFSSENLEAFVKDFLDG 329
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 33-135 1.78e-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: 124.27  E-value: 1.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174    33 PVLQLTPSNFKSKVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGIATVAAIDADAHKSVSQDYGVRGFPTIKVFV 112
Cdd:pfam00085   1 VVVVLTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFK 80

                          90       100
                  ....*....|....*....|...
gi 79336174   113 PGKPPIDYQGARDAKSISQFAIK 135
Cdd:pfam00085  81 NGQPVDDYVGARPKDALAAFLKA 103
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 167-338 9.55e-34

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


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 131.72  E-value: 9.55e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   167 SASVELNSSNFDELVtESKELWIVEFFAPWCGHCKKLAPEWKKAANNLKGK---VKLGHVNCDAEQSIKSRFKVQGFPTI 243
Cdd:TIGR01130   1 EDVLVLTKDNFDDFI-KSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKgppIKLAKVDATEEKDLAQKYGVSGYPTL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   244 LVFGSDKSSPVPYEGARSASAIESFALEQlesnAGPAeVTELTGPDVMEDKCGSAAICFVSFLPDiLDSKAEGRnkylem 323
Cdd:TIGR01130  80 KIFRNGEDSVSDYNGPRDADGIVKYMKKQ----SGPA-VKEIETVADLEAFLADDDVVVIGFFKD-LDSELNDT------ 147

                         170
                  ....*....|....*
gi 79336174   324 LLSVADKFKKDPYGF 338
Cdd:TIGR01130 148 FLSVAEKLRDVYFFF 162
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 34-132 1.04e-33

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: 121.97  E-value: 1.04e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  34 VLQLTPSNFKSKVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGIATV--AAIDAD-AHKSVSQDYGVRGFPTIKV 110
Cdd:cd02998   2 VVELTDSNFDKVVGDDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFANEDDVviAKVDADeANKDLAKKYGVSGFPTLKF 81

                        90       100
                ....*....|....*....|...
gi 79336174 111 FVPG-KPPIDYQGARDAKSISQF 132
Cdd:cd02998  82 FPKGsTEPVKYEGGRDLEDLVKF 104
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 170-270 6.35e-33

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: 120.16  E-value: 6.35e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 170 VELNSSNFDELVTESKELWIVEFFAPWCGHCKKLAPEWKKAANNLKGKVKLGHVNCDAEQS--IKSRFKVQGFPTILVF- 246
Cdd:cd03002   3 YELTPKNFDKVVHNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKELDGLVQVAAVDCDEDKNkpLCGKYGVQGFPTLKVFr 82

                        90       100
                ....*....|....*....|....*..
gi 79336174 247 -GSDKSSPVP--YEGARSASAIESFAL 270
Cdd:cd03002  83 pPKKASKHAVedYNGERSAKAIVDFVL 109
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 170-268 2.72e-32

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


Pssm-ID: 239296 [Multi-domain]  Cd Length: 105  Bit Score: 118.51  E-value: 2.72e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 170 VELNSSNFDELVTESKELWIVEFFAPWCGHCKKLAPEWKKAANNLKG--KVKLGHVNCDAEQS-IKSRFKVQGFPTILVF 246
Cdd:cd02998   3 VELTDSNFDKVVGDDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFANedDVVIAKVDADEANKdLAKKYGVSGFPTLKFF 82

                        90       100
                ....*....|....*....|..
gi 79336174 247 GSDKSSPVPYEGARSASAIESF 268
Cdd:cd02998  83 PKGSTEPVKYEGGRDLEDLVKF 104
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 167-269 3.84e-32

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: 117.78  E-value: 3.84e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 167 SASVELNSSNFDELVTESKELWIVEFFAPWCGHCKKLAPEWKKAANNLKGKVKLGHVNCDAEQSIKSRFKVQGFPTILVF 246
Cdd:cd03004   1 PSVITLTPEDFPELVLNRKEPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLY 80

                        90       100
                ....*....|....*....|....
gi 79336174 247 GSDKSSPVPYEG-ARSASAIESFA 269
Cdd:cd03004  81 PGNASKYHSYNGwHRDADSILEFI 104
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 34-133 3.14e-30

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: 112.77  E-value: 3.14e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  34 VLQLTPSNFKSKVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGIATVAAIDADAHKSVSQDYGVRGFPTIKVFVP 113
Cdd:cd03004   3 VITLTPEDFPELVLNRKEPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLYPG 82

                        90       100
                ....*....|....*....|..
gi 79336174 114 GKPPI-DYQG-ARDAKSISQFA 133
Cdd:cd03004  83 NASKYhSYNGwHRDADSILEFI 104
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 34-132 6.77e-30

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: 111.84  E-value: 6.77e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  34 VLQLTPSNFKSKVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGIATVAAIDADAHKSVSQDYGVRGFPTIKVFVP 113
Cdd:COG3118   2 VVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLFKD 81

                        90
                ....*....|....*....
gi 79336174 114 GKPPIDYQGARDAKSISQF 132
Cdd:COG3118  82 GQPVDRFVGALPKEQLREF 100
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 34-132 6.82e-30

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: 111.61  E-value: 6.82e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  34 VLQLTPSNFKSKVlnSNGVVLVEFFAPWCGHCQSLTPTWEKVA-STLKGIATV--AAIDADAHKSVSQDYGVRGFPTIKV 110
Cdd:cd03005   2 VLELTEDNFDHHI--AEGNHFVKFFAPWCGHCKRLAPTWEQLAkKFNNENPSVkiAKVDCTQHRELCSEFQVRGYPTLLL 79

                        90       100
                ....*....|....*....|..
gi 79336174 111 FVPGKPPIDYQGARDAKSISQF 132
Cdd:cd03005  80 FKDGEKVDKYKGTRDLDSLKEF 101
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 170-268 1.42e-29

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


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 110.79  E-value: 1.42e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   170 VELNSSNFDELVTESKELWIVEFFAPWCGHCKKLAPEWKKAANNLKGKVKLGHVNCDAEQSIKSRFKVQGFPTILvFGSD 249
Cdd:pfam00085   3 VVLTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLI-FFKN 81

                          90
                  ....*....|....*....
gi 79336174   250 KSSPVPYEGARSASAIESF 268
Cdd:pfam00085  82 GQPVDDYVGARPKDALAAF 100
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 167-346 5.72e-28

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 115.62  E-value: 5.72e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  167 SASVELNSSNFDELVTEsKELWIVEFFAPWCGHCKKLAPEWKKAANNLK---GKVKLGHVNCDAEQSIKSRFKVQGFPTI 243
Cdd:PTZ00102  32 EHVTVLTDSTFDKFITE-NEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKekkSEIVLASVDATEEMELAQEFGVRGYPTI 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  244 LVFgsDKSSPVPYEGARSASAIESFaLEQLesnAGPAeVTELTGPDVMEDKcgsAAICFVSFLPDILDSKAEGRNKYLEm 323
Cdd:PTZ00102 111 KFF--NKGNPVNYSGGRTADGIVSW-IKKL---TGPA-VTEVESASEIKLI---AKKIFVAFYGEYTSKDSELYKKFEE- 179

                        170       180
                 ....*....|....*....|...
gi 79336174  324 llsVADKFKKDPYGFVWVAAGKQ 346
Cdd:PTZ00102 180 ---VADKHREHAKFFVKKHEGKN 199
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 170-273 6.24e-27

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: 103.75  E-value: 6.24e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 170 VELNSSNFDELVTESKELWIVEFFAPWCGHCKKLAPEWKKAANNLKGKVKLGHVNCDAEQSIKSRFKVQGFPTILVFgsD 249
Cdd:COG3118   3 VELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLF--K 80

                        90       100
                ....*....|....*....|....*
gi 79336174 250 KSSPVP-YEGARSASAIESFaLEQL 273
Cdd:COG3118  81 DGQPVDrFVGALPKEQLREF-LDKV 104
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 33-132 4.08e-26

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


Pssm-ID: 239293 [Multi-domain]  Cd Length: 104  Bit Score: 101.48  E-value: 4.08e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  33 PVLQLTPSNFKSKVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGIA--TVAAIDADAHkSVSQDYGVRGFPTIKV 110
Cdd:cd02995   1 PVKVVVGKNFDEVVLDSDKDVLVEFYAPWCGHCKALAPIYEELAEKLKGDDnvVIAKMDATAN-DVPSEFVVDGFPTILF 79

                        90       100
                ....*....|....*....|....
gi 79336174 111 FVPGK--PPIDYQGARDAKSISQF 132
Cdd:cd02995  80 FPAGDksNPIKYEGDRTLEDLIKF 103
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 30-268 1.53e-25

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: 108.22  E-value: 1.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174    30 SSSPVLQLTPSNFKSKVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGI-ATVAAIDADAHKSVSQDYGV--RGFP 106
Cdd:TIGR01130 215 SLPLVGEFTQETAAKYFESGPLVVLYYNVDESLDPFEELRNRFLEAAKKFRGKfVNFAVADEEDFGRELEYFGLkaEKFP 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   107 TIKVF---VPGKPPIDYqgardaksiSQFAIKQIKALLKDRLDGKtsgtkngggSSEKKKSEP-----SASVE-LNSSNF 177
Cdd:TIGR01130 295 AVAIQdleGNKKYPMDQ---------EEFSSENLEAFVKDFLDGK---------LKPYLKSEPipeddEGPVKvLVGKNF 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   178 DELVTESKELWIVEFFAPWCGHCKKLAPEWKKAANNLKGK------VKLghvncDAEQSIKSRFKVQGFPTILVF-GSDK 250
Cdd:TIGR01130 357 DEIVLDETKDVLVEFYAPWCGHCKNLAPIYEELAEKYKDAesdvviAKM-----DATANDVPPFEVEGFPTIKFVpAGKK 431

                         250
                  ....*....|....*...
gi 79336174   251 SSPVPYEGARSASAIESF 268
Cdd:TIGR01130 432 SEPVPYDGDRTLEDFSKF 449
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 1-137 2.51e-24

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 104.83  E-value: 2.51e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174    1 MERKMYKSTVFPICCLLFALFDRGNALYGSSSpVLQLTPSNFKsKVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLK 80
Cdd:PTZ00102   2 GFRSILSSLFLLLILLAFAVFGSAEEHFISEH-VTVLTDSTFD-KFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLK 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   81 GIAT---VAAIDADAHKSVSQDYGVRGFPTIKVFvPGKPPIDYQGARDAKSISQFaIKQI 137
Cdd:PTZ00102  80 EKKSeivLASVDATEEMELAQEFGVRGYPTIKFF-NKGNPVNYSGGRTADGIVSW-IKKL 137
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 168-268 7.26e-24

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: 95.43  E-value: 7.26e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 168 ASVELNSSNFDELVteSKELWIVEFFAPWCGHCKKLAPEWK---KAANNLKGKVKLGHVNCDAEQSIKSRFKVQGFPTIL 244
Cdd:cd03005   1 GVLELTEDNFDHHI--AEGNHFVKFFAPWCGHCKRLAPTWEqlaKKFNNENPSVKIAKVDCTQHRELCSEFQVRGYPTLL 78

                        90       100
                ....*....|....*....|....
gi 79336174 245 VFgSDKSSPVPYEGARSASAIESF 268
Cdd:cd03005  79 LF-KDGEKVDKYKGTRDLDSLKEF 101
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 170-268 9.60e-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: 9.60e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 170 VELNSSNFDELVTESKELWIVEFFAPWCGHCKKLAPEWKKAANNLKGKVKLGHVNCDAEQ-SIKSRFKVQGFPTILVF-G 247
Cdd:cd02995   3 KVVVGKNFDEVVLDSDKDVLVEFYAPWCGHCKALAPIYEELAEKLKGDDNVVIAKMDATAnDVPSEFVVDGFPTILFFpA 82

                        90       100
                ....*....|....*....|.
gi 79336174 248 SDKSSPVPYEGARSASAIESF 268
Cdd:cd02995  83 GDKSNPIKYEGDRTLEDLIKF 103
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 33-115 1.43e-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: 89.25  E-value: 1.43e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  33 PVLQLTPSNFKSKVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLK---GIATVAAID--ADAHKSVSQDYGVRGFPT 107
Cdd:cd02992   2 PVIVLDAASFNSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRkwrPVVRVAAVDcaDEENVALCRDFGVTGYPT 81


                ....*...
gi 79336174 108 IKVFVPGK 115
Cdd:cd02992  82 LRYFPPFS 89
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 50-133 1.59e-21

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: 89.05  E-value: 1.59e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  50 NGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGIAT---VAAIDADAHKSVSQDYGVRGFPTIKvFVPGKPPIDYQGARDA 126
Cdd:cd03000  15 EDIWLVDFYAPWCGHCKKLEPVWNEVGAELKSSGSpvrVGKLDATAYSSIASEFGVRGYPTIK-LLKGDLAYNYRGPRTK 93


                ....*..
gi 79336174 127 KSISQFA 133
Cdd:cd03000  94 DDIVEFA 100
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 170-268 4.00e-21

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: 87.76  E-value: 4.00e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 170 VELNSSNFDELVTESKELwIVEFFAPWCGHCKKLAPEWKKAANNLK--GKVKLGHVNC--DAEQSIKSRFKVQGFPTILV 245
Cdd:cd02997   3 VHLTDEDFRKFLKKEKHV-LVMFYAPWCGHCKKMKPEFTKAATELKedGKGVLAAVDCtkPEHDALKEEYNVKGFPTFKY 81

                        90       100
                ....*....|....*....|...
gi 79336174 246 FGSDKSSpVPYEGARSASAIESF 268
Cdd:cd02997  82 FENGKFV-EKYEGERTAEDIIEF 103
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 167-283 4.12e-21

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 91.61  E-value: 4.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  167 SASVELNSSNFDELVTESKEL----WIVEFFAPWCGHCKKLAPEWKKAANNLKGKVKLGHVNCDAEQSIKSRFKVQGFPT 242
Cdd:PTZ00443  30 NALVLLNDKNFEKLTQASTGAttgpWFVKFYAPWCSHCRKMAPAWERLAKALKGQVNVADLDATRALNLAKRFAIKGYPT 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 79336174  243 ILVFgsDKSSPVPYE-GARSASAIESFALEQLE---SNAGPAEVT 283
Cdd:PTZ00443 110 LLLF--DKGKMYQYEgGDRSTEKLAAFALGDFKkalGAPVPAPLS 152
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 34-132 3.04e-20

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: 85.45  E-value: 3.04e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  34 VLQLTPSNFKsKVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLK--GIATVAAIDA--DAHKSVSQDYGVRGFPTIK 109
Cdd:cd02997   2 VVHLTDEDFR-KFLKKEKHVLVMFYAPWCGHCKKMKPEFTKAATELKedGKGVLAAVDCtkPEHDALKEEYNVKGFPTFK 80

                        90       100
                ....*....|....*....|...
gi 79336174 110 VFVPGKPPIDYQGARDAKSISQF 132
Cdd:cd02997  81 YFENGKFVEKYEGERTAEDIIEF 103
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 178-270 3.61e-20

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: 85.20  E-value: 3.61e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 178 DELVTESK--ELWIVEFFAPWCGHCKKLAPEWKKAANNLKG---KVKLGHVNCDAEQSIKSRFKVQGFPTILVFGSDKSs 252
Cdd:cd03000   6 DDSFKDVRkeDIWLVDFYAPWCGHCKKLEPVWNEVGAELKSsgsPVRVGKLDATAYSSIASEFGVRGYPTIKLLKGDLA- 84

                        90
                ....*....|....*...
gi 79336174 253 pVPYEGARSASAIESFAL 270
Cdd:cd03000  85 -YNYRGPRTKDDIVEFAN 101
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 172-246 4.54e-20

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


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 84.65  E-value: 4.54e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79336174   172 LNSSNFDELVTESKELWIVEFFAPWCGHCKKLAPEWKKAANNLKGKVKLGHVNCDAEQSIKSRFKVQGFPTILVF 246
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLF 75
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 37-132 5.17e-20

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


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 84.65  E-value: 5.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174    37 LTPSNFKSKVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGIATVAAIDADAHKSVSQDYGVRGFPTIKVFVPGKP 116
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKE 80

                          90
                  ....*....|....*.
gi 79336174   117 PIDYQGARDAKSISQF 132
Cdd:TIGR01068  81 VDRSVGALPKAALKQL 96
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 14-138 2.76e-19

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 86.22  E-value: 2.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   14 CCLLFAL---------FDRGNAlygssSPVLQLTPSNFKSKVLNSNGVV----LVEFFAPWCGHCQSLTPTWEKVASTLK 80
Cdd:PTZ00443   8 CCILFGLiadeatnvkLDAEDA-----NALVLLNDKNFEKLTQASTGATtgpwFVKFYAPWCSHCRKMAPAWERLAKALK 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79336174   81 GIATVAAIDADAHKSVSQDYGVRGFPTIKVFVPGKPpidYQ---GARDAKSISQFAIKQIK 138
Cdd:PTZ00443  83 GQVNVADLDATRALNLAKRFAIKGYPTLLLFDKGKM---YQyegGDRSTEKLAAFALGDFK 140
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 170-269 4.95e-19

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: 81.80  E-value: 4.95e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 170 VELNSSNFDELVTeSKELWIVEFFAPWCGHCKKLAPEWKKAANNLKGKVKLGHVNCDAEQSIKSRFKVQGFPTILVFGSD 249
Cdd:cd03003   4 VTLDRGDFDAAVN-SGEIWFVNFYSPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDDRMLCRSQGVNSYPSLYVFPSG 82

                        90       100
                ....*....|....*....|
gi 79336174 250 kSSPVPYEGARSASAIESFA 269
Cdd:cd03003  83 -MNPEKYYGDRSKESLVKFA 101
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 40-132 4.86e-18

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: 78.75  E-value: 4.86e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  40 SNFKSKVLnSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGIaTVAAIDADAHKSVSQDYGVRGFPTIKVFVPGKPPID 119
Cdd:cd02947   1 EEFEELIK-SAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKV-KFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDR 78

                        90
                ....*....|...
gi 79336174 120 YQGARDAKSISQF 132
Cdd:cd02947  79 VVGADPKEELEEF 91
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 170-252 4.14e-17

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: 76.92  E-value: 4.14e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 170 VELNSSNFDELVTESKELWIVEFFAPWCGHCKKLAPEWKKAANNLK---GKVKLGHVNCDAEQSIK--SRFKVQGFPTIL 244
Cdd:cd02992   4 IVLDAASFNSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRkwrPVVRVAAVDCADEENVAlcRDFGVTGYPTLR 83


                ....*...
gi 79336174 245 VFGSDKSS 252
Cdd:cd02992  84 YFPPFSKE 91
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 175-246 2.29e-16

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: 74.13  E-value: 2.29e-16
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79336174 175 SNFDELVTESKELwIVEFFAPWCGHCKKLAPEWKKAANNlKGKVKLGHVNCDAEQSIKSRFKVQGFPTILVF 246
Cdd:cd02947   1 EEFEELIKSAKPV-VVDFWAPWCGPCKAIAPVLEELAEE-YPKVKFVKVDVDENPELAEEYGVRSIPTFLFF 70
trxA PRK09381
thioredoxin TrxA;
31-132 2.79e-15

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 71.63  E-value: 2.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   31 SSPVLQLTPSNFKSKVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGIATVAAIDADAHKSVSQDYGVRGFPTIKV 110
Cdd:PRK09381   2 SDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLL 81

                         90       100
                 ....*....|....*....|..
gi 79336174  111 FVPGKPPIDYQGARDAKSISQF 132
Cdd:PRK09381  82 FKNGEVAATKVGALSKGQLKEF 103
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 167-268 2.91e-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: 71.65  E-value: 2.91e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 167 SASVELNSSNFDElVTESKELWIVEFFAPWCGHCKKLAPEWKKAANNLK------GKVKLGHVNCDAEQSIKSRFKVQGF 240
Cdd:cd02996   1 SEIVSLTSGNIDD-ILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKeefpdaGKVVWGKVDCDKESDIADRYRINKY 79

                        90       100
                ....*....|....*....|....*...
gi 79336174 241 PTILVFGSDKSSPVPYEGARSASAIESF 268
Cdd:cd02996  80 PTLKLFRNGMMMKREYRGQRSVEALAEF 107
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 34-133 3.62e-15

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: 71.02  E-value: 3.62e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  34 VLQLTPSNFKSKVlNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGIATVAAIDADAHKSVSQDYGVRGFPTIKVFVP 113
Cdd:cd03003   3 IVTLDRGDFDAAV-NSGEIWFVNFYSPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDDRMLCRSQGVNSYPSLYVFPS 81

                        90       100
                ....*....|....*....|
gi 79336174 114 GKPPIDYQGARDAKSISQFA 133
Cdd:cd03003  82 GMNPEKYYGDRSKESLVKFA 101
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 31-143 4.54e-15

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 77.10  E-value: 4.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   31 SSPVLQLTPSNFKSKVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLK--GIATVAAIDADAHKSVSQDYGVRGFPTI 108
Cdd:PTZ00102 356 DGPVKVVVGNTFEEIVFKSDKDVLLEIYAPWCGHCKNLEPVYNELGEKYKdnDSIIVAKMNGTANETPLEEFSWSAFPTI 435

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 79336174  109 KVFVPG-KPPIDYQGARDAKSISQFAIKQIKALLKD 143
Cdd:PTZ00102 436 LFVKAGeRTPIPYEGERTVEGFKEFVNKHATNPFED 471
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 40-131 5.38e-15

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: 70.38  E-value: 5.38e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  40 SNFKSKVLNSNGV-VLVEFFAPWCGHCQSLTPTWEKVASTLKGIATVAAIDADAHKSVSQDYGVRGFPTIKVFVPGKPPI 118
Cdd:cd02956   1 QNFQQVLQESTQVpVVVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVD 80

                        90
                ....*....|...
gi 79336174 119 DYQGARDAKSISQ 131
Cdd:cd02956  81 GFQGAQPEEQLRQ 93
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 175-266 9.12e-15

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: 69.61  E-value: 9.12e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 175 SNFDELVTESKE-LWIVEFFAPWCGHCKKLAPEWKKAANNLKGKVKLGHVNCDAEQSIKSRFKVQGFPTILVFgsDKSSP 253
Cdd:cd02956   1 QNFQQVLQESTQvPVVVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLF--AAGQP 78

                        90
                ....*....|....
gi 79336174 254 VP-YEGARSASAIE 266
Cdd:cd02956  79 VDgFQGAQPEEQLR 92
PRK10996 PRK10996
thioredoxin 2; Provisional
 170-246 2.54e-14

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 69.71  E-value: 2.54e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79336174  170 VELNSSNFDELVTESKELwIVEFFAPWCGHCKKLAPEWKKAANNLKGKVKLGHVNCDAEQSIKSRFKVQGFPTILVF 246
Cdd:PRK10996  38 INATGETLDKLLQDDLPV-VIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIF 113
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 32-132 3.65e-14

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: 68.19  E-value: 3.65e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  32 SPVLQLTPSNFKsKVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLK------GIATVAAIDADAHKSVSQDYGVRGF 105
Cdd:cd02996   1 SEIVSLTSGNID-DILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKeefpdaGKVVWGKVDCDKESDIADRYRINKY 79

                        90       100
                ....*....|....*....|....*...
gi 79336174 106 PTIKVFVPGKPP-IDYQGARDAKSISQF 132
Cdd:cd02996  80 PTLKLFRNGMMMkREYRGQRSVEALAEF 107
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 170-271 3.15e-13

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


Pssm-ID: 239292 [Multi-domain]  Cd Length: 101  Bit Score: 65.48  E-value: 3.15e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 170 VELNSSNFDELVTESkelWIVEFFAPWCGHCKKLAPEWKKAANNLKG-KVKLGHVNCDAEQSIKSRFKVQGFPTIL---- 244
Cdd:cd02994   4 VELTDSNWTLVLEGE---WMIEFYAPWCPACQQLQPEWEEFADWSDDlGINVAKVDVTQEPGLSGRFFVTALPTIYhakd 80

                        90       100
                ....*....|....*....|....*...
gi 79336174 245 -VFGSdksspvpYEGARSASAIESFALE 271
Cdd:cd02994  81 gVFRR-------YQGPRDKEDLISFIEE 101
PRK10996 PRK10996
thioredoxin 2; Provisional
 34-115 7.64e-13

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 65.48  E-value: 7.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   34 VLQLTPSNFkSKVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGIATVAAIDADAHKSVSQDYGVRGFPTIKVFVP 113
Cdd:PRK10996  37 VINATGETL-DKLLQDDLPVVIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFKN 115


                 ..
gi 79336174  114 GK 115
Cdd:PRK10996 116 GQ 117
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 184-260 6.70e-12

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


Pssm-ID: 239291 [Multi-domain]  Cd Length: 109  Bit Score: 62.08  E-value: 6.70e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 184 SKELWIVEFFAPWCGHCKKLAPEWKKAANNLKG-KVKLGHVNCDAEQSI--KSRFKVQGFPTILVFGSDKSSPVPYEGAR 260
Cdd:cd02993  20 RNQSTLVVLYAPWCPFCQAMEASYEELAEKLAGsNVKVAKFNADGEQREfaKEELQLKSFPTILFFPKNSRQPIKYPSEQ 99
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 48-132 1.66e-11

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


Pssm-ID: 239297 [Multi-domain]  Cd Length: 100  Bit Score: 60.45  E-value: 1.66e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  48 NSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGIATVAAIDADAHKSVSQDYGVRGFPTIkVFVPGKPPIDYQGARDAK 127
Cdd:cd02999  16 NREDYTAVLFYASWCPFSASFRPHFNALSSMFPQIRHLAIEESSIKPSLLSRYGVVGFPTI-LLFNSTPRVRYNGTRTLD 94


                ....*
gi 79336174 128 SISQF 132
Cdd:cd02999  95 SLAAF 99
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 183-268 1.99e-10

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: 62.34  E-value: 1.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   183 ESKELWIVEFFAPWCGHCKKLAPEWKKAANNLKGK-VKLGHVNCDAEQS--IKSRFKVQGFPTILVFGSDKSSPVPYEGA 259
Cdd:TIGR00424 369 ERKEAWLVVLYAPWCPFCQAMEASYLELAEKLAGSgVKVAKFRADGDQKefAKQELQLGSFPTILFFPKHSSRPIKYPSE 448

                          90
                  ....*....|
gi 79336174   260 -RSASAIESF 268
Cdd:TIGR00424 449 kRDVDSLMSF 458
PTZ00051 PTZ00051
thioredoxin; Provisional
 45-125 2.07e-10

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 57.19  E-value: 2.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   45 KVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGIATVaAIDADAHKSVSQDYGVRGFPTIKVFVPGKPPIDYQGAR 124
Cdd:PTZ00051  13 STLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFV-KVDVDELSEVAEKENITSMPTFKVFKNGSVVDTLLGAN 91


                 .
gi 79336174  125 D 125
Cdd:PTZ00051  92 D 92
trxA PRK09381
thioredoxin TrxA;
170-268 3.73e-10

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 57.00  E-value: 3.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  170 VELNSSNFDELVTESKELWIVEFFAPWCGHCKKLAPEWKKAANNLKGKVKLGHVNCDAEQSIKSRFKVQGFPTILVFGSD 249
Cdd:PRK09381   6 IHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNG 85

                         90
                 ....*....|....*....
gi 79336174  250 KSSPVPYeGARSASAIESF 268
Cdd:PRK09381  86 EVAATKV-GALSKGQLKEF 103
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 32-132 4.18e-10

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: 56.62  E-value: 4.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  32 SPVLQLTPSNFkSKVLNsnGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGIAT-VAAIDADAHKSVSQDYGVRGFPTI-- 108
Cdd:cd02994   1 SNVVELTDSNW-TLVLE--GEWMIEFYAPWCPACQQLQPEWEEFADWSDDLGInVAKVDVTQEPGLSGRFFVTALPTIyh 77

                        90       100
                ....*....|....*....|....*..
gi 79336174 109 ---KVFVpgkppiDYQGARDAKSISQF 132
Cdd:cd02994  78 akdGVFR------RYQGPRDKEDLISF 98
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 29-142 4.36e-10

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 57.78  E-value: 4.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  29 GSSSPVLQLTPSNFKSKVLNS--NGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGIATVA-AID---------------- 89
Cdd:COG0526   5 GKPAPDFTLTDLDGKPLSLADlkGKPVLVNFWATWCPPCRAEMPVLKELAEEYGGVVFVGvDVDenpeavkaflkelglp 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 79336174  90 ----ADAHKSVSQDYGVRGFPTIKVFVP-GKPPIDYQGARDAKSISQFaikqIKALLK 142
Cdd:COG0526  85 ypvlLDPDGELAKAYGVRGIPTTVLIDKdGKIVARHVGPLSPEELEEA----LEKLLA 138
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 54-116 1.33e-09

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


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 54.24  E-value: 1.33e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79336174  54 LVEFFAPWCGHCQSLTPTWEKVASTLKGIaTVAAIDAD---AHKSVSQDYGVRGFPTIKVFVPGKP 116
Cdd:cd01659   1 LVLFYAPWCPFCQALRPVLAELALLNKGV-KFEAVDVDedpALEKELKRYGVGGVPTLVVFGPGIG 65
PLN02309 PLN02309
5'-adenylylsulfate reductase
 140-256 1.34e-09

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 59.80  E-value: 1.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  140 LLKDRLDGKTSGTKNGGGSSEKKKSEPSAS-VELNSSNFDELVTES--KELWIVEFFAPWCGHCKKLAPEWKKAANNLKG 216
Cdd:PLN02309 317 LHKGNIKEEDNGAANDNGNAAVADIFNSQNvVALSRAGIENLLKLEnrKEPWLVVLYAPWCPFCQAMEASYEELAEKLAG 396

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 79336174  217 K-VKLGHVNCDAEQS--IKSRFKVQGFPTILVFGSDKSSPVPY 256
Cdd:PLN02309 397 SgVKVAKFRADGDQKefAKQELQLGSFPTILLFPKNSSRPIKY 439
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 189-249 2.67e-09

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


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 53.47  E-value: 2.67e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79336174 189 IVEFFAPWCGHCKKLAPEWKKAANNLKGkVKLGHVNCD---AEQSIKSRFKVQGFPTILVFGSD 249
Cdd:cd01659   1 LVLFYAPWCPFCQALRPVLAELALLNKG-VKFEAVDVDedpALEKELKRYGVGGVPTLVVFGPG 63
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 48-133 9.86e-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: 52.84  E-value: 9.86e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  48 NSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGIAT-VAAIDADAHKSV--SQDYGVRGFPTIKVFVPG-KPPIDYQG- 122
Cdd:cd02993  19 RRNQSTLVVLYAPWCPFCQAMEASYEELAEKLAGSNVkVAKFNADGEQREfaKEELQLKSFPTILFFPKNsRQPIKYPSe 98

                        90
                ....*....|.
gi 79336174 123 ARDAKSISQFA 133
Cdd:cd02993  99 QRDVDSLLMFV 109
PDI_a_EFP1_N cd03006
PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase ...
 178-268 1.03e-08

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: 52.86  E-value: 1.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 178 DELVTESkELWIVEFFAPWCGHCKKLAPEWKKAANNLKGKVKLGHVNCDAEQSiKSRFKVQ--GFPTILVFgSDKSSPVP 255
Cdd:cd03006  23 EELRTDA-EVSLVMYYAPWDAQSQAARQEFEQVAQKLSDQVLFVAINCWWPQG-KCRKQKHffYFPVIHLY-YRSRGPIE 99

                        90
                ....*....|...
gi 79336174 256 YEGARSASAIESF 268
Cdd:cd03006 100 YKGPMRAPYMEKF 112
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
201-391 2.07e-08

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 53.90  E-value: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   201 KKLAPEWKKAANNLKGKVKLGHVNcDAEQSIKSRFKvqgFPTILVFGSDKSSPVPYEG-ARSASAIESFALEQLESNAGp 279
Cdd:pfam13848   6 SPLYEIFRKAAKELKGDVRFGITF-SKEVADKYNIK---EPAILLFRKFDEETVHYPGdSINFEDLKKFIQKNCLPLVR- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   280 aEVTELTGPDVMEDKCGSAAICFvsflpdiLDSKAEGRNKYLEMLLSVADKFkKDPYGFVWVAAGKQPDLEKRVGVGGYG 359
Cdd:pfam13848  81 -EFTPENAEELFEEGIPPLLLLF-------LKKDDESTEEFKKALEKVAKKF-RGKINFALVDAKSFGRPLEYFGLSESD 151

                         170       180       190
                  ....*....|....*....|....*....|...
gi 79336174   360 YPAMVALNAKKGAYAPLKSG-FEVKHLKDFVKE 391
Cdd:pfam13848 152 LPVIVIVDSFSHMYKYFPSDeFSPESLKEFIND 184
PTZ00051 PTZ00051
thioredoxin; Provisional
 177-251 5.73e-08

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 50.26  E-value: 5.73e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79336174  177 FDELVTESkELWIVEFFAPWCGHCKKLAPEWKKAANNLKgKVKLGHVNCDAEQSIKSRFKVQGFPTILVFGSDKS 251
Cdd:PTZ00051  11 FESTLSQN-ELVIVDFYAEWCGPCKRIAPFYEECSKEYT-KMVFVKVDVDELSEVAEKENITSMPTFKVFKNGSV 83
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 188-249 6.50e-07

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 48.53  E-value: 6.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 188 WIVEFFAPWCGHCKKLAPEWKKAANNLKG--------------------KVKLGH-VNCDAEQSIKSRFKVQGFPTILVF 246
Cdd:COG0526  31 VLVNFWATWCPPCRAEMPVLKELAEEYGGvvfvgvdvdenpeavkaflkELGLPYpVLLDPDGELAKAYGVRGIPTTVLI 110


                ...
gi 79336174 247 GSD 249
Cdd:COG0526 111 DKD 113
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 49-111 8.23e-07

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


Pssm-ID: 239247 [Multi-domain]  Cd Length: 97  Bit Score: 47.11  E-value: 8.23e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79336174  49 SNGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGIATVAAIDADAHKSVSQDYGVRGFPTIKVF 111
Cdd:cd02949  12 SDRLILVLYTSPTCGPCRTLKPILNKVIDEFDGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFF 74
PLN02309 PLN02309
5'-adenylylsulfate reductase
 54-132 2.55e-06

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 49.40  E-value: 2.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174   54 LVEFFAPWCGHCQSLTPTWEKVASTLKGIA-TVAAIDAD-AHKSVSQD-YGVRGFPTIKVFVPGKP-PIDYQGA-RDAKS 128
Cdd:PLN02309 369 LVVLYAPWCPFCQAMEASYEELAEKLAGSGvKVAKFRADgDQKEFAKQeLQLGSFPTILLFPKNSSrPIKYPSEkRDVDS 448


                 ....
gi 79336174  129 ISQF 132
Cdd:PLN02309 449 LLSF 452
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 54-132 3.01e-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: 49.24  E-value: 3.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174    54 LVEFFAPWCGHCQSLTPTWEKVASTLKGIATVAA---IDADAHKSVSQDYGVRGFPTIKVFVPGKP-PIDYQGA-RDAKS 128
Cdd:TIGR00424 375 LVVLYAPWCPFCQAMEASYLELAEKLAGSGVKVAkfrADGDQKEFAKQELQLGSFPTILFFPKHSSrPIKYPSEkRDVDS 454


                  ....
gi 79336174   129 ISQF 132
Cdd:TIGR00424 455 LMSF 458
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 36-107 3.56e-06

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


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 45.69  E-value: 3.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  36 QLTPSNFKSKVlnsngvVLVEFFAPWCGHCQSLTPTWEKVASTLK--GIATVA-AID---------------------AD 91
Cdd:cd02966  11 PVSLSDLKGKV------VLVNFWASWCPPCRAEMPELEALAKEYKddGVEVVGvNVDdddpaavkaflkkygitfpvlLD 84

                        90
                ....*....|....*.
gi 79336174  92 AHKSVSQDYGVRGFPT 107
Cdd:cd02966  85 PDGELAKAYGVRGLPT 100
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 53-115 1.32e-05

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


Pssm-ID: 239309 [Multi-domain]  Cd Length: 123  Bit Score: 44.21  E-value: 1.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  53 VLVEFFAPWCGHCQSLTPTWEKVAS--TLKGIATVAAID-----------------ADAHKSVSQDYGVRGFPTIKVFVP 113
Cdd:cd03011  23 VLVYFWATWCPVCRFTSPTVNQLAAdyPVVSVALRSGDDgavarfmqkkgygfpviNDPDGVISARWGVSVTPAIVIVDP 102


                ..
gi 79336174 114 GK 115
Cdd:cd03011 103 GG 104
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 179-246 1.66e-05

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: 43.26  E-value: 1.66e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79336174 179 ELVTESKELWIVEFFAPWCGHCKKLAPEWKKAANNLKGKVKLGHVNCDAEQSIKSRFKVQGFPTILVF 246
Cdd:cd02949   7 KLYHESDRLILVLYTSPTCGPCRTLKPILNKVIDEFDGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFF 74
PDI_a_EFP1_N cd03006
PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase ...
 31-132 3.40e-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: 42.84  E-value: 3.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  31 SSPVLQLTPSNFKSKVLNSNG--VVLVEFFAPWCGHCQSLTPTWEKVASTLKGIATVAAIDA-DAHKSVSQDYGVRGFPT 107
Cdd:cd03006   8 RSPVLDFYKGQLDYAEELRTDaeVSLVMYYAPWDAQSQAARQEFEQVAQKLSDQVLFVAINCwWPQGKCRKQKHFFYFPV 87

                        90       100
                ....*....|....*....|....*
gi 79336174 108 IKVFVPGKPPIDYQGARDAKSISQF 132
Cdd:cd03006  88 IHLYYRSRGPIEYKGPMRAPYMEKF 112
TMX2 cd02962
TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related ...
 166-246 5.73e-05

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


Pssm-ID: 239260 [Multi-domain]  Cd Length: 152  Bit Score: 43.14  E-value: 5.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 166 PSASVELNSSNFDELVTESKE-LWIVEFFAPWCGHCKKLAPEW-----KKAANNLK-GKVKLGHVncdAEQSIKSRFKVQ 238
Cdd:cd02962  27 PEHIKYFTPKTLEEELERDKRvTWLVEFFTTWSPECVNFAPVFaelslKYNNNNLKfGKIDIGRF---PNVAEKFRVSTS 103

                        90
                ....*....|..
gi 79336174 239 GF----PTILVF 246
Cdd:cd02962 104 PLskqlPTIILF 115
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 190-268 1.22e-04

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


Pssm-ID: 239297 [Multi-domain]  Cd Length: 100  Bit Score: 40.80  E-value: 1.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 190 VEFFAPWCGHCKKLAPEWKKAANNLKgkvKLGHVNCDAEQ---SIKSRFKVQGFPTILVFgsdKSSP-VPYEGARSASAI 265
Cdd:cd02999  23 VLFYASWCPFSASFRPHFNALSSMFP---QIRHLAIEESSikpSLLSRYGVVGFPTILLF---NSTPrVRYNGTRTLDSL 96


                ...
gi 79336174 266 ESF 268
Cdd:cd02999  97 AAF 99
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 189-277 1.44e-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: 41.94  E-value: 1.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 189 IVEFFAPWCGHCKKLAPEWKKAANNLKGKVKLGHVNCDAEQSIKS--RFKVQGFPTiLVFGSDKSSPVpyegarsASAIE 266
Cdd:cd02950  24 LVEFYADWCTVCQEMAPDVAKLKQKYGDQVNFVMLNVDNPKWLPEidRYRVDGIPH-FVFLDREGNEE-------GQSIG 95

                        90
                ....*....|.
gi 79336174 267 SFALEQLESNA 277
Cdd:cd02950  96 LQPKQVLAQNL 106
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
53-131 2.11e-04

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 40.49  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174    53 VLVEFFAPWCGHCQSL---TPTWEKVASTLKGIATVAAIDADA-------------HKSVSQDYGVRGFPTIkVFVPGKP 116
Cdd:pfam13098   7 VLVVFTDPDCPYCKKLkkeLLEDPDVTVYLGPNFVFIAVNIWCakevakaftdileNKELGRKYGVRGTPTI-VFFDGKG 85

                          90
                  ....*....|....*.
gi 79336174   117 PID-YQGARDAKSISQ 131
Cdd:pfam13098  86 ELLrLPGYVPAEEFLA 101
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
40-122 2.91e-04

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 40.62  E-value: 2.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  40 SNFKSKVlnsngvVLVEFFAPWCGHCQSLTPTWEKVASTLK--GIATVA-AID-------------------ADAHKSVS 97
Cdd:COG1225  17 SDLRGKP------VVLYFYATWCPGCTAELPELRDLYEEFKdkGVEVLGvSSDsdeahkkfaekyglpfpllSDPDGEVA 90

                        90       100
                ....*....|....*....|....*
gi 79336174  98 QDYGVRGFPTikVFVpgkppIDYQG 122
Cdd:COG1225  91 KAYGVRGTPT--TFL-----IDPDG 108
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 189-220 4.39e-04

DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) S-transferase kappa (GSTK), 2-hydroxychromene-2-carboxylate (HCCA) isomerase, an oxidoreductase (FrnE) presumed to be involved in frenolicin biosynthesis, a 27-kDa outer membrane protein, and similar proteins. Members of this family contain a redox active CXXC motif (except GSTK and HCCA isomerase) imbedded in a TRX fold, and an alpha helical insert of about 75 residues (shorter in DsbC and DsbG) relative to TRX. DsbA is involved in the oxidative protein folding pathway in prokaryotes, catalyzing disulfide bond formation of proteins secreted into the bacterial periplasm. DsbC and DsbG function as protein disulfide isomerases and chaperones to correct non-native disulfide bonds formed by DsbA and prevent aggregation of incorrectly folded proteins.


Pssm-ID: 239270 [Multi-domain]  Cd Length: 98  Bit Score: 39.31  E-value: 4.39e-04
                        10        20        30
                ....*....|....*....|....*....|..
gi 79336174 189 IVEFFAPWCGHCKKLAPEWKKAANNLKGKVKL 220
Cdd:cd02972   1 IVEFFDPLCPYCYLFEPELEKLLYADDGGVRV 32
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 35-133 1.00e-03

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


Pssm-ID: 239261 [Multi-domain]  Cd Length: 111  Bit Score: 38.51  E-value: 1.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  35 LQLTPSNFKSKVL--NSNGVVLVEFFAPWCGHCQSLTPTWEKVASTL----KGIATVaaiDADAHKSVSQDYGVRGFPTI 108
Cdd:cd02963   7 YSLTFSQYENEIVpkSFKKPYLIKITSDWCFSCIHIEPVWKEVIQELeplgVGIATV---NAGHERRLARKLGAHSVPAI 83

                        90       100
                ....*....|....*....|....*
gi 79336174 109 KVFVPGKPPIDYQGARDAKSISQFA 133
Cdd:cd02963  84 VGIINGQVTFYHDSSFTKQHVVDFV 108
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 189-249 1.44e-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: 38.37  E-value: 1.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 189 IVEFFAPWCGHCKKLAPEWKKAANNLKGK--------------------VKLGHVN----CDAEQSIKSRFKVQGFPTIL 244
Cdd:cd02966  23 LVNFWASWCPPCRAEMPELEALAKEYKDDgvevvgvnvddddpaavkafLKKYGITfpvlLDPDGELAKAYGVRGLPTTF 102


                ....*
gi 79336174 245 VFGSD 249
Cdd:cd02966 103 LIDRD 107
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 178-245 1.79e-03

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


Pssm-ID: 239261 [Multi-domain]  Cd Length: 111  Bit Score: 38.12  E-value: 1.79e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174 178 DELVTES-KELWIVEFFAPWCGHCKKLAPEWKKAANNLKG-KVKLGHVNCDAEQSIKSRFKVQGFPTILV 245
Cdd:cd02963  16 NEIVPKSfKKPYLIKITSDWCFSCIHIEPVWKEVIQELEPlGVGIATVNAGHERRLARKLGAHSVPAIVG 85
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 189-220 1.92e-03

Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 38.83  E-value: 1.92e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 79336174 189 IVEFFAPWCGHCKKLAPEWKKAANNL-KGKVKL 220
Cdd:COG1651   4 VVEFFDYQCPYCARFHPELPELLKKYvDGKVRV 36
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 33-106 2.79e-03

TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, periplasmic TRX-like reductase containing a CXXC motif that specifically donates reducing equivalents to apocytochrome c via CcmH, another cytochrome c maturation (Ccm) factor with a redox active CXXC motif. Assembly of cytochrome c requires the ligation of heme to reduced thiols of the apocytochrome. In bacteria, this assembly occurs in the periplasm. The reductase activity of DsbE in the oxidizing environment of the periplasm is crucial in the maturation of cytochrome c.


Pssm-ID: 239308 [Multi-domain]  Cd Length: 127  Bit Score: 37.56  E-value: 2.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  33 PVLQLTPSNFKskvlnsNGVVLVEFFAPWCGHCQSLTPTWEKVAStlKGIATVAAID----------------------- 89
Cdd:cd03010  14 PDKTLTSADLK------GKPYLLNVWASWCAPCREEHPVLMALAR--QGRVPIYGINykdnpenalawlarhgnpyaavg 85

                        90
                ....*....|....*..
gi 79336174  90 ADAHKSVSQDYGVRGFP 106
Cdd:cd03010  86 FDPDGRVGIDLGVYGVP 102
DsbDgamma cd02953
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
 53-117 2.80e-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: 37.20  E-value: 2.80e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79336174  53 VLVEFFAPWCGHCQSL---TPTWEKVASTLKgiATVAAIDAD------AHKSVSQDYGVRGFPTIKVFVPGKPP 117
Cdd:cd02953  14 VFVDFTADWCVTCKVNekvVFSDPEVQAALK--KDVVLLRADwtkndpEITALLKRFGVFGPPTYLFYGPGGEP 85
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 49-149 4.73e-03

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: 37.32  E-value: 4.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79336174  49 SNG-VVLVEFFAPWCGHCQSLTPTWEKVASTLKGIATVAAIDADAHKSVS--QDYGVRGFPTIKVFvpgkppiDYQGARD 125
Cdd:cd02950  18 SNGkPTLVEFYADWCTVCQEMAPDVAKLKQKYGDQVNFVMLNVDNPKWLPeiDRYRVDGIPHFVFL-------DREGNEE 90

                        90       100
                ....*....|....*....|....
gi 79336174 126 AKSISQFAIKQIKALLKDRLDGKT 149
Cdd:cd02950  91 GQSIGLQPKQVLAQNLDALVAGEP 114
 
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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