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Conserved domains on  [gi|544186040|ref|NP_001269636|]
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protein disulfide-isomerase A6 isoform e precursor [Homo sapiens]

Protein Classification

protein disulfide isomerase( domain architecture ID 10122318)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P5_C cd02983
P5 family, C-terminal redox inactive TRX-like domain; P5 is a protein disulfide isomerase (PDI) ...
 272-401 1.16e-79

P5 family, C-terminal redox inactive TRX-like domain; P5 is a protein disulfide isomerase (PDI)-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. The C-terminal domain is likely involved in substrate binding, similar to the b and b' domains of PDI.


:

Pssm-ID: 239281  Cd Length: 130  Bit Score: 242.26  E-value: 1.16e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 272 PPELLEIINEDIAKRTCEEHQLCVVAVLPHILDTGAAGRNSYLEVLLKLADKYKKKMWGWLWTEAGAQSELETALGIGGF 351
Cdd:cd02983    1 APEIIELTSEDVFEETCEEKQLCIIAFLPHILDCQASCRNKYLEILKSVAEKFKKKPWGWLWTEAGAQLDLEEALNIGGF 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 544186040 352 GYPAMAAINARKMKFALLKGSFSEQGINEFLRELSFGRGSTAPVGGGAFP 401
Cdd:cd02983   81 GYPAMVAINFRKMKFATLKGSFSEDGINEFLRELSYGRGPTLPVNGLPKV 130
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 23-125 1.71e-68

PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. Some members of this subfamily are P5-like proteins containing only one redox active TRX domain.


:

Pssm-ID: 239299 [Multi-domain]  Cd Length: 103  Bit Score: 212.53  E-value: 1.71e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  23 DVIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIFG 102
Cdd:cd03001    1 DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVFG 80

                         90       100
                 ....*....|....*....|...
gi 544186040 103 SNKNRPEDYQGGRTGEAIVDAAL 125
Cdd:cd03001   81 AGKNSPQDYQGGRTAKAIVSAAL 103
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 158-263 4.23e-61

PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. Some members of this subfamily are P5-like proteins containing only one redox active TRX domain.


:

Pssm-ID: 239299 [Multi-domain]  Cd Length: 103  Bit Score: 193.66  E-value: 4.23e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 158 DVIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVkeqtKGKVKLAAVDATVNQVLASRYGIRGFPTI 237
Cdd:cd03001    1 DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKAL----KGIVKVGAVDADVHQSLAQQYGVRGFPTI 76

                         90       100
                 ....*....|....*....|....*..
gi 544186040 238 KIFQKG-ESPVDYDGGRTRSDIVSRAL 263
Cdd:cd03001   77 KVFGAGkNSPQDYQGGRTAKAIVSAAL 103
 
Name Accession Description Interval E-value
P5_C cd02983
P5 family, C-terminal redox inactive TRX-like domain; P5 is a protein disulfide isomerase (PDI) ...
 272-401 1.16e-79

P5 family, C-terminal redox inactive TRX-like domain; P5 is a protein disulfide isomerase (PDI)-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. The C-terminal domain is likely involved in substrate binding, similar to the b and b' domains of PDI.


Pssm-ID: 239281  Cd Length: 130  Bit Score: 242.26  E-value: 1.16e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 272 PPELLEIINEDIAKRTCEEHQLCVVAVLPHILDTGAAGRNSYLEVLLKLADKYKKKMWGWLWTEAGAQSELETALGIGGF 351
Cdd:cd02983    1 APEIIELTSEDVFEETCEEKQLCIIAFLPHILDCQASCRNKYLEILKSVAEKFKKKPWGWLWTEAGAQLDLEEALNIGGF 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 544186040 352 GYPAMAAINARKMKFALLKGSFSEQGINEFLRELSFGRGSTAPVGGGAFP 401
Cdd:cd02983   81 GYPAMVAINFRKMKFATLKGSFSEDGINEFLRELSYGRGPTLPVNGLPKV 130
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 23-125 1.71e-68

PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. Some members of this subfamily are P5-like proteins containing only one redox active TRX domain.


Pssm-ID: 239299 [Multi-domain]  Cd Length: 103  Bit Score: 212.53  E-value: 1.71e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  23 DVIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIFG 102
Cdd:cd03001    1 DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVFG 80

                         90       100
                 ....*....|....*....|...
gi 544186040 103 SNKNRPEDYQGGRTGEAIVDAAL 125
Cdd:cd03001   81 AGKNSPQDYQGGRTAKAIVSAAL 103
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 158-263 4.23e-61

PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. Some members of this subfamily are P5-like proteins containing only one redox active TRX domain.


Pssm-ID: 239299 [Multi-domain]  Cd Length: 103  Bit Score: 193.66  E-value: 4.23e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 158 DVIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVkeqtKGKVKLAAVDATVNQVLASRYGIRGFPTI 237
Cdd:cd03001    1 DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKAL----KGIVKVGAVDADVHQSLAQQYGVRGFPTI 76

                         90       100
                 ....*....|....*....|....*..
gi 544186040 238 KIFQKG-ESPVDYDGGRTRSDIVSRAL 263
Cdd:cd03001   77 KVFGAGkNSPQDYQGGRTAKAIVSAAL 103
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 162-260 6.28e-47

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


Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 156.68  E-value: 6.28e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  162 LTDDSFDKNVLDSEDVwMVEFYAPWCGHCKNLEPEWAAAASEVKEQtkGKVKLAAVDATVNQVLASRYGIRGFPTIKIFQ 241
Cdd:TIGR01126   1 LTASNFDEIVLSNKDV-LVEFYAPWCGHCKNLAPEYEKLAKELKKD--PKIVLAKVDATAEKDLASRFGVSGFPTIKFFP 77

                          90
                  ....*....|....*....
gi 544186040  242 KGESPVDYDGGRTRSDIVS 260
Cdd:TIGR01126  78 KGSKPVDYEGGRDLEAIVE 96
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 22-259 2.33e-41

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


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 152.52  E-value: 2.33e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040   22 DDVIELTPSNFNrEVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKD---VVKVGAVDADKHHSLGGQYGVQGFPTI 98
Cdd:TIGR01130   1 EDVLVLTKDNFD-DFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKkgpPIKLAKVDATEEKDLAQKYGVSGYPTL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040   99 KIFGSNKNRPEDYQGGRTGEAIV--------------------------------------------------------- 121
Cdd:TIGR01130  80 KIFRNGEDSVSDYNGPRDADGIVkymkkqsgpavkeietvadleafladddvvvigffkdldselndtflsvaeklrdvy 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  122 -------DAALSALRQLVKDRLGGRSGGYSSGKQGRSDSSSKKD---------------VIELTDDSFDK---------- 169
Cdd:TIGR01130 160 fffahssDVAAFAKLGAFPDSVVLFKPKDEDEKFSKVDGEMDTDvsdlekfiraeslplVGEFTQETAAKyfesgplvvl 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  170 --NV---LDSEDVWMVEFY------------------------------------------------------------- 183
Cdd:TIGR01130 240 yyNVdesLDPFEELRNRFLeaakkfrgkfvnfavadeedfgreleyfglkaekfpavaiqdlegnkkypmdqeefssenl 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  184 -----------------------------------------------------APWCGHCKNLEPEWAAAASEVKEQTKg 210
Cdd:TIGR01130 320 eafvkdfldgklkpylksepipeddegpvkvlvgknfdeivldetkdvlvefyAPWCGHCKNLAPIYEELAEKYKDAES- 398

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 544186040  211 KVKLAAVDATVNQVlaSRYGIRGFPTIKIFQKGE--SPVDYDGGRTRSDIV 259
Cdd:TIGR01130 399 DVVIAKMDATANDV--PPFEVEGFPTIKFVPAGKksEPVPYDGDRTLEDFS 447
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 27-122 1.19e-40

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


Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 140.12  E-value: 1.19e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040   27 LTPSNFNrEVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKD--VVKVGAVDADKHHSLGGQYGVQGFPTIKIFGSN 104
Cdd:TIGR01126   1 LTASNFD-EIVLSNKDVLVEFYAPWCGHCKNLAPEYEKLAKELKKdpKIVLAKVDATAEKDLASRFGVSGFPTIKFFPKG 79

                          90
                  ....*....|....*...
gi 544186040  105 KnRPEDYQGGRTGEAIVD 122
Cdd:TIGR01126  80 S-KPVDYEGGRDLEAIVE 96
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 24-127 1.71e-34

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


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 123.88  E-value: 1.71e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040   24 VIELTPSNFNREVIQSDSLW-LVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIFg 102
Cdd:pfam00085   1 VVVVLTDANFDEVVQKSSKPvLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFF- 79

                          90       100
                  ....*....|....*....|....*
gi 544186040  103 sNKNRPEDYQGGRTGEAIVDAALSA 127
Cdd:pfam00085  80 -KNGQPVDDYVGARPKDALAAFLKA 103
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 158-265 5.35e-34

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 132.57  E-value: 5.35e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 158 DVIELTDDSFDKNVLDSEDVwMVEFYAPWCGHCKNLEPEWAAAASEVKEQtKGKVKLAAVDATVNQVLASRYGIRGFPTI 237
Cdd:PTZ00102  33 HVTVLTDSTFDKFITENEIV-LVKFYAPWCGHCKRLAPEYKKAAKMLKEK-KSEIVLASVDATEEMELAQEFGVRGYPTI 110

                         90       100
                 ....*....|....*....|....*...
gi 544186040 238 KIFQKGEsPVDYDGGRTRSDIVSRALDL 265
Cdd:PTZ00102 111 KFFNKGN-PVNYSGGRTADGIVSWIKKL 137
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 159-260 5.97e-34

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


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 122.73  E-value: 5.97e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  159 VIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEvkeqTKGKVKLAAVDATVNQVLASRYGIRGFPTIK 238
Cdd:pfam00085   2 VVVLTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQE----YKGNVVFAKVDVDENPDLASKYGVRGYPTLI 77

                          90       100
                  ....*....|....*....|..
gi 544186040  239 IFQKGESPVDYDGGRTRSDIVS 260
Cdd:pfam00085  78 FFKNGQPVDDYVGARPKDALAA 99
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 3-122 3.60e-28

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 116.00  E-value: 3.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040   3 LGLVSCTFFLAVNGLYSSsDDVIELTPSNFNReVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDV---VKVGAVD 79
Cdd:PTZ00102  14 LILLAFAVFGSAEEHFIS-EHVTVLTDSTFDK-FITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKkseIVLASVD 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 544186040  80 ADKHHSLGGQYGVQGFPTIKIFgsNKNRPEDYQGGRTGEAIVD 122
Cdd:PTZ00102  92 ATEEMELAQEFGVRGYPTIKFF--NKGNPVNYSGGRTADGIVS 132
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 159-248 3.34e-26

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


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 101.82  E-value: 3.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 159 VIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVkeqtKGKVKLAAVDATVNQVLASRYGIRGFPTIK 238
Cdd:COG3118    2 VVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEY----GGKVKFVKVDVDENPELAAQFGVRSIPTLL 77

                         90
                 ....*....|
gi 544186040 239 IFQKGEsPVD 248
Cdd:COG3118   78 LFKDGQ-PVD 86
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 24-101 4.81e-25

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


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 98.74  E-value: 4.81e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544186040  24 VIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIF 101
Cdd:COG3118    2 VVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLF 79
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
225-384 1.80e-03

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 39.27  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  225 LASRYGIRgFPTIKIFQK-GESPVDYDGGRTRSDIVSRaldlFSDNAPPPeLLEIINEDIAKRTCEEHQLCVVAVlphIL 303
Cdd:pfam13848  33 VADKYNIK-EPAILLFRKfDEETVHYPGDSINFEDLKK----FIQKNCLP-LVREFTPENAEELFEEGIPPLLLL---FL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  304 DTGAAGRNSYLEVLLKLADKYKKKMwGWLWTEAGA-QSELETaLGIGGFGYPAMAAIN-ARKMKFALLKGSFSEQGINEF 381
Cdd:pfam13848 104 KKDDESTEEFKKALEKVAKKFRGKI-NFALVDAKSfGRPLEY-FGLSESDLPVIVIVDsFSHMYKYFPSDEFSPESLKEF 181


                  ...
gi 544186040  382 LRE 384
Cdd:pfam13848 182 IND 184
 
Name Accession Description Interval E-value
P5_C cd02983
P5 family, C-terminal redox inactive TRX-like domain; P5 is a protein disulfide isomerase (PDI) ...
 272-401 1.16e-79

P5 family, C-terminal redox inactive TRX-like domain; P5 is a protein disulfide isomerase (PDI)-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. The C-terminal domain is likely involved in substrate binding, similar to the b and b' domains of PDI.


Pssm-ID: 239281  Cd Length: 130  Bit Score: 242.26  E-value: 1.16e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 272 PPELLEIINEDIAKRTCEEHQLCVVAVLPHILDTGAAGRNSYLEVLLKLADKYKKKMWGWLWTEAGAQSELETALGIGGF 351
Cdd:cd02983    1 APEIIELTSEDVFEETCEEKQLCIIAFLPHILDCQASCRNKYLEILKSVAEKFKKKPWGWLWTEAGAQLDLEEALNIGGF 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 544186040 352 GYPAMAAINARKMKFALLKGSFSEQGINEFLRELSFGRGSTAPVGGGAFP 401
Cdd:cd02983   81 GYPAMVAINFRKMKFATLKGSFSEDGINEFLRELSYGRGPTLPVNGLPKV 130
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 23-125 1.71e-68

PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. Some members of this subfamily are P5-like proteins containing only one redox active TRX domain.


Pssm-ID: 239299 [Multi-domain]  Cd Length: 103  Bit Score: 212.53  E-value: 1.71e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  23 DVIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIFG 102
Cdd:cd03001    1 DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVFG 80

                         90       100
                 ....*....|....*....|...
gi 544186040 103 SNKNRPEDYQGGRTGEAIVDAAL 125
Cdd:cd03001   81 AGKNSPQDYQGGRTAKAIVSAAL 103
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 158-263 4.23e-61

PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. Some members of this subfamily are P5-like proteins containing only one redox active TRX domain.


Pssm-ID: 239299 [Multi-domain]  Cd Length: 103  Bit Score: 193.66  E-value: 4.23e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 158 DVIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVkeqtKGKVKLAAVDATVNQVLASRYGIRGFPTI 237
Cdd:cd03001    1 DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKAL----KGIVKVGAVDADVHQSLAQQYGVRGFPTI 76

                         90       100
                 ....*....|....*....|....*..
gi 544186040 238 KIFQKG-ESPVDYDGGRTRSDIVSRAL 263
Cdd:cd03001   77 KVFGAGkNSPQDYQGGRTAKAIVSAAL 103
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 162-260 6.28e-47

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


Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 156.68  E-value: 6.28e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  162 LTDDSFDKNVLDSEDVwMVEFYAPWCGHCKNLEPEWAAAASEVKEQtkGKVKLAAVDATVNQVLASRYGIRGFPTIKIFQ 241
Cdd:TIGR01126   1 LTASNFDEIVLSNKDV-LVEFYAPWCGHCKNLAPEYEKLAKELKKD--PKIVLAKVDATAEKDLASRFGVSGFPTIKFFP 77

                          90
                  ....*....|....*....
gi 544186040  242 KGESPVDYDGGRTRSDIVS 260
Cdd:TIGR01126  78 KGSKPVDYEGGRDLEAIVE 96
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 25-122 3.82e-43

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


Pssm-ID: 239259 [Multi-domain]  Cd Length: 101  Bit Score: 146.99  E-value: 3.82e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  25 IELTPSNFNrEVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALK--DVVKVGAVDADKHHSLGGQYGVQGFPTIKIFG 102
Cdd:cd02961    1 VELTDDNFD-ELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKgdGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFP 79

                         90       100
                 ....*....|....*....|
gi 544186040 103 SNKNRPEDYQGGRTGEAIVD 122
Cdd:cd02961   80 NGSKEPVKYEGPRTLESLVE 99
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 160-260 4.43e-43

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


Pssm-ID: 239259 [Multi-domain]  Cd Length: 101  Bit Score: 146.60  E-value: 4.43e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 160 IELTDDSFDKNVLDSEDvWMVEFYAPWCGHCKNLEPEWAAAASEVKEqtKGKVKLAAVDATVNQVLASRYGIRGFPTIKI 239
Cdd:cd02961    1 VELTDDNFDELVKDSKD-VLVEFYAPWCGHCKALAPEYEKLAKELKG--DGKVVVAKVDCTANNDLCSEYGVRGYPTIKL 77

                         90       100
                 ....*....|....*....|..
gi 544186040 240 FQKGES-PVDYDGGRTRSDIVS 260
Cdd:cd02961   78 FPNGSKePVKYEGPRTLESLVE 99
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 22-259 2.33e-41

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


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 152.52  E-value: 2.33e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040   22 DDVIELTPSNFNrEVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKD---VVKVGAVDADKHHSLGGQYGVQGFPTI 98
Cdd:TIGR01130   1 EDVLVLTKDNFD-DFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKkgpPIKLAKVDATEEKDLAQKYGVSGYPTL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040   99 KIFGSNKNRPEDYQGGRTGEAIV--------------------------------------------------------- 121
Cdd:TIGR01130  80 KIFRNGEDSVSDYNGPRDADGIVkymkkqsgpavkeietvadleafladddvvvigffkdldselndtflsvaeklrdvy 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  122 -------DAALSALRQLVKDRLGGRSGGYSSGKQGRSDSSSKKD---------------VIELTDDSFDK---------- 169
Cdd:TIGR01130 160 fffahssDVAAFAKLGAFPDSVVLFKPKDEDEKFSKVDGEMDTDvsdlekfiraeslplVGEFTQETAAKyfesgplvvl 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  170 --NV---LDSEDVWMVEFY------------------------------------------------------------- 183
Cdd:TIGR01130 240 yyNVdesLDPFEELRNRFLeaakkfrgkfvnfavadeedfgreleyfglkaekfpavaiqdlegnkkypmdqeefssenl 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  184 -----------------------------------------------------APWCGHCKNLEPEWAAAASEVKEQTKg 210
Cdd:TIGR01130 320 eafvkdfldgklkpylksepipeddegpvkvlvgknfdeivldetkdvlvefyAPWCGHCKNLAPIYEELAEKYKDAES- 398

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 544186040  211 KVKLAAVDATVNQVlaSRYGIRGFPTIKIFQKGE--SPVDYDGGRTRSDIV 259
Cdd:TIGR01130 399 DVVIAKMDATANDV--PPFEVEGFPTIKFVPAGKksEPVPYDGDRTLEDFS 447
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 27-122 1.19e-40

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


Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 140.12  E-value: 1.19e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040   27 LTPSNFNrEVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKD--VVKVGAVDADKHHSLGGQYGVQGFPTIKIFGSN 104
Cdd:TIGR01126   1 LTASNFD-EIVLSNKDVLVEFYAPWCGHCKNLAPEYEKLAKELKKdpKIVLAKVDATAEKDLASRFGVSGFPTIKFFPKG 79

                          90
                  ....*....|....*...
gi 544186040  105 KnRPEDYQGGRTGEAIVD 122
Cdd:TIGR01126  80 S-KPVDYEGGRDLEAIVE 96
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 24-125 1.32e-38

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


Pssm-ID: 239300 [Multi-domain]  Cd Length: 109  Bit Score: 135.18  E-value: 1.32e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  24 VIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAV--DADKHHSLGGQYGVQGFPTIKIF 101
Cdd:cd03002    2 VYELTPKNFDKVVHNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKELDGLVQVAAVdcDEDKNKPLCGKYGVQGFPTLKVF 81

                         90       100
                 ....*....|....*....|....*...
gi 544186040 102 ----GSNKNRPEDYQGGRTGEAIVDAAL 125
Cdd:cd03002   82 rppkKASKHAVEDYNGERSAKAIVDFVL 109
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 157-260 1.02e-37

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


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 142.51  E-value: 1.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  157 KDVIELTDDSFDkNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVKEQTKgKVKLAAVDATVNQVLASRYGIRGFPT 236
Cdd:TIGR01130   1 EDVLVLTKDNFD-DFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGP-PIKLAKVDATEEKDLAQKYGVSGYPT 78

                          90       100
                  ....*....|....*....|....*
gi 544186040  237 IKIFQKGE-SPVDYDGGRTRSDIVS 260
Cdd:TIGR01130  79 LKIFRNGEdSVSDYNGPRDADGIVK 103
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 24-113 3.01e-35

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


Pssm-ID: 239302 [Multi-domain]  Cd Length: 104  Bit Score: 126.25  E-value: 3.01e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  24 VIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIFGS 103
Cdd:cd03004    3 VITLTPEDFPELVLNRKEPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLYPG 82

                         90
                 ....*....|
gi 544186040 104 NKNRPEDYQG 113
Cdd:cd03004   83 NASKYHSYNG 92
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 23-121 8.96e-35

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


Pssm-ID: 239296 [Multi-domain]  Cd Length: 105  Bit Score: 124.67  E-value: 8.96e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  23 DVIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALK--DVVKVGAVDADK-HHSLGGQYGVQGFPTIK 99
Cdd:cd02998    1 NVVELTDSNFDKVVGDDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFAneDDVVIAKVDADEaNKDLAKKYGVSGFPTLK 80

                         90       100
                 ....*....|....*....|..
gi 544186040 100 IFGSNKNRPEDYQGGRTGEAIV 121
Cdd:cd02998   81 FFPKGSTEPVKYEGGRDLEDLV 102
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 24-127 1.71e-34

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


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 123.88  E-value: 1.71e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040   24 VIELTPSNFNREVIQSDSLW-LVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIFg 102
Cdd:pfam00085   1 VVVVLTDANFDEVVQKSSKPvLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFF- 79

                          90       100
                  ....*....|....*....|....*
gi 544186040  103 sNKNRPEDYQGGRTGEAIVDAALSA 127
Cdd:pfam00085  80 -KNGQPVDDYVGARPKDALAAFLKA 103
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 158-265 5.35e-34

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 132.57  E-value: 5.35e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 158 DVIELTDDSFDKNVLDSEDVwMVEFYAPWCGHCKNLEPEWAAAASEVKEQtKGKVKLAAVDATVNQVLASRYGIRGFPTI 237
Cdd:PTZ00102  33 HVTVLTDSTFDKFITENEIV-LVKFYAPWCGHCKRLAPEYKKAAKMLKEK-KSEIVLASVDATEEMELAQEFGVRGYPTI 110

                         90       100
                 ....*....|....*....|....*...
gi 544186040 238 KIFQKGEsPVDYDGGRTRSDIVSRALDL 265
Cdd:PTZ00102 111 KFFNKGN-PVNYSGGRTADGIVSWIKKL 137
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 159-260 5.97e-34

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


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 122.73  E-value: 5.97e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  159 VIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEvkeqTKGKVKLAAVDATVNQVLASRYGIRGFPTIK 238
Cdd:pfam00085   2 VVVLTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQE----YKGNVVFAKVDVDENPDLASKYGVRGYPTLI 77

                          90       100
                  ....*....|....*....|..
gi 544186040  239 IFQKGESPVDYDGGRTRSDIVS 260
Cdd:pfam00085  78 FFKNGQPVDDYVGARPKDALAA 99
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 158-260 7.23e-34

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


Pssm-ID: 239296 [Multi-domain]  Cd Length: 105  Bit Score: 122.36  E-value: 7.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 158 DVIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVKEqtKGKVKLAAVDAT-VNQVLASRYGIRGFPT 236
Cdd:cd02998    1 NVVELTDSNFDKVVGDDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFAN--EDDVVIAKVDADeANKDLAKKYGVSGFPT 78

                         90       100
                 ....*....|....*....|....*
gi 544186040 237 IKIFQKGES-PVDYDGGRTRSDIVS 260
Cdd:cd02998   79 LKFFPKGSTePVKYEGGRDLEDLVK 103
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 158-260 1.26e-32

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


Pssm-ID: 239295 [Multi-domain]  Cd Length: 104  Bit Score: 118.96  E-value: 1.26e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 158 DVIELTDDSFDKNVLDSEDVwMVEFYAPWCGHCKNLEPEWAAAASEVKEqtKGKVKLAAVDATV--NQVLASRYGIRGFP 235
Cdd:cd02997    1 DVVHLTDEDFRKFLKKEKHV-LVMFYAPWCGHCKKMKPEFTKAATELKE--DGKGVLAAVDCTKpeHDALKEEYNVKGFP 77

                         90       100
                 ....*....|....*....|....*
gi 544186040 236 TIKIFQKGESPVDYDGGRTRSDIVS 260
Cdd:cd02997   78 TFKYFENGKFVEKYEGERTAEDIIE 102
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 159-263 7.88e-32

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


Pssm-ID: 239300 [Multi-domain]  Cd Length: 109  Bit Score: 117.08  E-value: 7.88e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 159 VIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVkeqtKGKVKLAAV--DATVNQVLASRYGIRGFPT 236
Cdd:cd03002    2 VYELTPKNFDKVVHNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKEL----DGLVQVAAVdcDEDKNKPLCGKYGVQGFPT 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 544186040 237 IKIFQKGE-----SPVDYDGGRTRSDIVSRAL 263
Cdd:cd03002   78 LKVFRPPKkaskhAVEDYNGERSAKAIVDFVL 109
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 3-122 3.60e-28

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 116.00  E-value: 3.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040   3 LGLVSCTFFLAVNGLYSSsDDVIELTPSNFNReVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDV---VKVGAVD 79
Cdd:PTZ00102  14 LILLAFAVFGSAEEHFIS-EHVTVLTDSTFDK-FITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKkseIVLASVD 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 544186040  80 ADKHHSLGGQYGVQGFPTIKIFgsNKNRPEDYQGGRTGEAIVD 122
Cdd:PTZ00102  92 ATEEMELAQEFGVRGYPTIKFF--NKGNPVNYSGGRTADGIVS 132
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 159-263 8.11e-28

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


Pssm-ID: 239298 [Multi-domain]  Cd Length: 104  Bit Score: 106.00  E-value: 8.11e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 159 VIELtDDSFDKNvlDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVKEqTKGKVKLAAVDATVNQVLASRYGIRGFPTIK 238
Cdd:cd03000    2 VLDL-DDSFKDV--RKEDIWLVDFYAPWCGHCKKLEPVWNEVGAELKS-SGSPVRVGKLDATAYSSIASEFGVRGYPTIK 77

                         90       100
                 ....*....|....*....|....*
gi 544186040 239 IFqKGESPVDYDGGRTRSDIVSRAL 263
Cdd:cd03000   78 LL-KGDLAYNYRGPRTKDDIVEFAN 101
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 159-259 2.45e-27

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


Pssm-ID: 239293 [Multi-domain]  Cd Length: 104  Bit Score: 104.95  E-value: 2.45e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 159 VIELTDDSFDKNVLDSE-DVwMVEFYAPWCGHCKNLEPEWAAAASEVKeqTKGKVKLAAVDATVNQVLASrYGIRGFPTI 237
Cdd:cd02995    2 VKVVVGKNFDEVVLDSDkDV-LVEFYAPWCGHCKALAPIYEELAEKLK--GDDNVVIAKMDATANDVPSE-FVVDGFPTI 77

                         90       100
                 ....*....|....*....|....
gi 544186040 238 KIFQKG--ESPVDYDGGRTRSDIV 259
Cdd:cd02995   78 LFFPAGdkSNPIKYEGDRTLEDLI 101
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 159-248 3.34e-26

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


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 101.82  E-value: 3.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 159 VIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVkeqtKGKVKLAAVDATVNQVLASRYGIRGFPTIK 238
Cdd:COG3118    2 VVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEY----GGKVKFVKVDVDENPELAAQFGVRSIPTLL 77

                         90
                 ....*....|
gi 544186040 239 IFQKGEsPVD 248
Cdd:COG3118   78 LFKDGQ-PVD 86
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 159-251 1.46e-25

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


Pssm-ID: 239302 [Multi-domain]  Cd Length: 104  Bit Score: 100.06  E-value: 1.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 159 VIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASevkeQTKGKVKLAAVDATVNQVLASRYGIRGFPTIK 238
Cdd:cd03004    3 VITLTPEDFPELVLNRKEPWLVDFYAPWCGPCQALLPELRKAAR----ALKGKVKVGSVDCQKYESLCQQANIRAYPTIR 78

                         90
                 ....*....|....
gi 544186040 239 IFQKGESPV-DYDG 251
Cdd:cd03004   79 LYPGNASKYhSYNG 92
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 23-122 4.18e-25

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


Pssm-ID: 239295 [Multi-domain]  Cd Length: 104  Bit Score: 98.54  E-value: 4.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  23 DVIELTPSNFnREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKV--GAVDADK--HHSLGGQYGVQGFPTI 98
Cdd:cd02997    1 DVVHLTDEDF-RKFLKKEKHVLVMFYAPWCGHCKKMKPEFTKAATELKEDGKGvlAAVDCTKpeHDALKEEYNVKGFPTF 79

                         90       100
                 ....*....|....*....|....
gi 544186040  99 KIFgSNKNRPEDYQGGRTGEAIVD 122
Cdd:cd02997   80 KYF-ENGKFVEKYEGERTAEDIIE 102
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 24-101 4.81e-25

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


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 98.74  E-value: 4.81e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544186040  24 VIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIF 101
Cdd:COG3118    2 VVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLF 79
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 159-254 5.64e-25

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


Pssm-ID: 239303 [Multi-domain]  Cd Length: 102  Bit Score: 98.13  E-value: 5.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 159 VIELTDDSFDKNVldSEDVWMVEFYAPWCGHCKNLEPEWAA-AASEVKEQTKgkVKLAAVDATVNQVLASRYGIRGFPTI 237
Cdd:cd03005    2 VLELTEDNFDHHI--AEGNHFVKFFAPWCGHCKRLAPTWEQlAKKFNNENPS--VKIAKVDCTQHRELCSEFQVRGYPTL 77

                         90
                 ....*....|....*..
gi 544186040 238 KIFQKGESPVDYDGGRT 254
Cdd:cd03005   78 LLFKDGEKVDKYKGTRD 94
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 40-125 1.92e-24

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


Pssm-ID: 239298 [Multi-domain]  Cd Length: 104  Bit Score: 96.75  E-value: 1.92e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  40 DSLWLVEFYAPWCGHCQRLTPEWKKAATALKDV---VKVGAVDADKHHSLGGQYGVQGFPTIKIFgsNKNRPEDYQGGRT 116
Cdd:cd03000   15 EDIWLVDFYAPWCGHCKKLEPVWNEVGAELKSSgspVRVGKLDATAYSSIASEFGVRGYPTIKLL--KGDLAYNYRGPRT 92


                 ....*....
gi 544186040 117 GEAIVDAAL 125
Cdd:cd03000   93 KDDIVEFAN 101
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 24-122 8.66e-23

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


Pssm-ID: 239293 [Multi-domain]  Cd Length: 104  Bit Score: 92.23  E-value: 8.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  24 VIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDV--VKVGAVDADK--HHSLggqYGVQGFPTIK 99
Cdd:cd02995    2 VKVVVGKNFDEVVLDSDKDVLVEFYAPWCGHCKALAPIYEELAEKLKGDdnVVIAKMDATAndVPSE---FVVDGFPTIL 78

                         90       100
                 ....*....|....*....|....
gi 544186040 100 IF-GSNKNRPEDYQGGRTGEAIVD 122
Cdd:cd02995   79 FFpAGDKSNPIKYEGDRTLEDLIK 102
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 24-120 2.93e-22

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


Pssm-ID: 239303 [Multi-domain]  Cd Length: 102  Bit Score: 90.81  E-value: 2.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  24 VIELTPSNFNREVIQSDSLwlVEFYAPWCGHCQRLTPEWKKAATALKDV---VKVGAVDADKHHSLGGQYGVQGFPTIKI 100
Cdd:cd03005    2 VLELTEDNFDHHIAEGNHF--VKFFAPWCGHCKRLAPTWEQLAKKFNNEnpsVKIAKVDCTQHRELCSEFQVRGYPTLLL 79

                         90       100
                 ....*....|....*....|
gi 544186040 101 FGSNKnRPEDYQGGRTGEAI 120
Cdd:cd03005   80 FKDGE-KVDKYKGTRDLDSL 98
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 22-129 1.12e-21

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


Pssm-ID: 239290 [Multi-domain]  Cd Length: 114  Bit Score: 89.64  E-value: 1.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  22 DDVIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKD---VVKVGAVD--ADKHHSLGGQYGVQGFP 96
Cdd:cd02992    1 DPVIVLDAASFNSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRKwrpVVRVAAVDcaDEENVALCRDFGVTGYP 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 544186040  97 TIKIFGSNKNRPEDYQGGRTGEAIVDAALSALR 129
Cdd:cd02992   81 TLRYFPPFSKEATDGLKQEGPERDVNELREALI 113
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 19-122 2.06e-20

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


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 93.20  E-value: 2.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040   19 SSSDDVIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDV---VKVGAVDADKHHSLGgqYGVQGF 95
Cdd:TIGR01130 343 DDEGPVKVLVGKNFDEIVLDETKDVLVEFYAPWCGHCKNLAPIYEELAEKYKDAesdVVIAKMDATANDVPP--FEVEGF 420

                          90       100
                  ....*....|....*....|....*...
gi 544186040   96 PTIKIF-GSNKNRPEDYQGGRTGEAIVD 122
Cdd:TIGR01130 421 PTIKFVpAGKKSEPVPYDGDRTLEDFSK 448
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 152-279 2.24e-20

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 89.30  E-value: 2.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 152 DSSSKKDVIELTDDSFDKNVLDSEDV----WMVEFYAPWCGHCKNLEPEWAAAASEVkeqtKGKVKLAAVDATVNQVLAS 227
Cdd:PTZ00443  25 DAEDANALVLLNDKNFEKLTQASTGAttgpWFVKFYAPWCSHCRKMAPAWERLAKAL----KGQVNVADLDATRALNLAK 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 544186040 228 RYGIRGFPTIKIFQKGESpVDYDGG-RTRSDIVSRALDLFSD--NAPPPELLEII 279
Cdd:PTZ00443 101 RFAIKGYPTLLLFDKGKM-YQYEGGdRSTEKLAAFALGDFKKalGAPVPAPLSFF 154
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 159-240 5.21e-20

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


Pssm-ID: 239290 [Multi-domain]  Cd Length: 114  Bit Score: 85.01  E-value: 5.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 159 VIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVKEQtKGKVKLAAVD--ATVNQVLASRYGIRGFPT 236
Cdd:cd02992    3 VIVLDAASFNSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRKW-RPVVRVAAVDcaDEENVALCRDFGVTGYPT 81


                 ....
gi 544186040 237 IKIF 240
Cdd:cd02992   82 LRYF 85
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 24-132 2.27e-19

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 86.60  E-value: 2.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  24 VIELTPSNFNREVIQSDSL----WLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIK 99
Cdd:PTZ00443  32 LVLLNDKNFEKLTQASTGAttgpWFVKFYAPWCSHCRKMAPAWERLAKALKGQVNVADLDATRALNLAKRFAIKGYPTLL 111

                         90       100       110
                 ....*....|....*....|....*....|....
gi 544186040 100 IFgsNKNRPEDYQGG-RTGEAIVDAALSALRQLV 132
Cdd:PTZ00443 112 LF--DKGKMYQYEGGdRSTEKLAAFALGDFKKAL 143
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 162-248 1.33e-18

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


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 80.41  E-value: 1.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  162 LTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVkeqtKGKVKLAAVDATVNQVLASRYGIRGFPTIKIFQ 241
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEY----EGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFK 76


                  ....*..
gi 544186040  242 KGEsPVD 248
Cdd:TIGR01068  77 NGK-EVD 82
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 23-124 4.67e-18

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


Pssm-ID: 239301 [Multi-domain]  Cd Length: 101  Bit Score: 79.11  E-value: 4.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  23 DVIELTPSNFNREVIQSDsLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIFG 102
Cdd:cd03003    2 EIVTLDRGDFDAAVNSGE-IWFVNFYSPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDDRMLCRSQGVNSYPSLYVFP 80

                         90       100
                 ....*....|....*....|..
gi 544186040 103 SNKNrPEDYQGGRTGEAIVDAA 124
Cdd:cd03003   81 SGMN-PEKYYGDRSKESLVKFA 101
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 165-244 2.94e-17

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


Pssm-ID: 239245 [Multi-domain]  Cd Length: 93  Bit Score: 76.44  E-value: 2.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 165 DSFDKNVLDSEDVwMVEFYAPWCGHCKNLEPEWAAAASEvkeqtKGKVKLAAVDATVNQVLASRYGIRGFPTIKIFQKGE 244
Cdd:cd02947    1 EEFEELIKSAKPV-VVDFWAPWCGPCKAIAPVLEELAEE-----YPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGK 74
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 158-262 3.01e-17

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


Pssm-ID: 239301 [Multi-domain]  Cd Length: 101  Bit Score: 76.79  E-value: 3.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 158 DVIELTDDSFDKNVlDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVkeqtKGKVKLAAVDATVNQVLASRYGIRGFPTI 237
Cdd:cd03003    2 EIVTLDRGDFDAAV-NSGEIWFVNFYSPRCSHCHDLAPTWREFAKEM----DGVIRIGAVNCGDDRMLCRSQGVNSYPSL 76

                         90       100
                 ....*....|....*....|....*
gi 544186040 238 KIFQKGESPVDYDGGRTRSDIVSRA 262
Cdd:cd03003   77 YVFPSGMNPEKYYGDRSKESLVKFA 101
trxA PRK09381
thioredoxin TrxA;
159-244 7.25e-17

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 75.87  E-value: 7.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 159 VIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPewaaAASEVKEQTKGKVKLAAVDATVNQVLASRYGIRGFPTIK 238
Cdd:PRK09381   5 IIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAP----ILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLL 80


                 ....*.
gi 544186040 239 IFQKGE 244
Cdd:PRK09381  81 LFKNGE 86
PRK10996 PRK10996
thioredoxin 2; Provisional
 158-244 9.18e-17

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 76.65  E-value: 9.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 158 DVIELTDDSFDKnVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEvkeqTKGKVKLAAVDATVNQVLASRYGIRGFPTI 237
Cdd:PRK10996  36 EVINATGETLDK-LLQDDLPVVIDFWAPWCGPCRNFAPIFEDVAAE----RSGKVRFVKVNTEAERELSARFRIRSIPTI 110


                 ....*..
gi 544186040 238 KIFQKGE 244
Cdd:PRK10996 111 MIFKNGQ 117
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 27-101 1.21e-16

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


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 75.02  E-value: 1.21e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544186040   27 LTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIF 101
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLF 75
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 158-260 1.40e-16

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


Pssm-ID: 239292 [Multi-domain]  Cd Length: 101  Bit Score: 75.11  E-value: 1.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 158 DVIELTDDSFDKnVLDSEdvWMVEFYAPWCGHCKNLEPEWAAAASEVKEQtkgKVKLAAVDATVNQVLASRYGIRGFPTI 237
Cdd:cd02994    2 NVVELTDSNWTL-VLEGE--WMIEFYAPWCPACQQLQPEWEEFADWSDDL---GINVAKVDVTQEPGLSGRFFVTALPTI 75

                         90       100
                 ....*....|....*....|....*...
gi 544186040 238 -----KIFQKgespvdYDGGRTRSDIVS 260
Cdd:cd02994   76 yhakdGVFRR------YQGPRDKEDLIS 97
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 23-121 4.68e-16

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


Pssm-ID: 239292 [Multi-domain]  Cd Length: 101  Bit Score: 73.57  E-value: 4.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  23 DVIELTPSNFNReVIQSDslWLVEFYAPWCGHCQRLTPEWKKAATALKDV-VKVGAVDADKHHSLGGQYGVQGFPTikIF 101
Cdd:cd02994    2 NVVELTDSNWTL-VLEGE--WMIEFYAPWCPACQQLQPEWEEFADWSDDLgINVAKVDVTQEPGLSGRFFVTALPT--IY 76

                         90       100
                 ....*....|....*....|
gi 544186040 102 GSNKNRPEDYQGGRTGEAIV 121
Cdd:cd02994   77 HAKDGVFRRYQGPRDKEDLI 96
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 157-254 2.93e-15

PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain, similar to that of PDIa, with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. The CXFS motif in the N-terminal domain allows ERp44 to form stable reversible mixed disulfides with its substrates. Through this activity, ERp44 mediates the ER localization of Ero1alpha, a protein that oxidizes protein disulfide isomerases into their active form. ERp44 also prevents the secretion of unassembled cargo protein with unpaired cysteines. It also modulates the activity of inositol 1,4,5-triphosphate type I receptor (IP3R1), an intracellular channel protein that mediates calcium release from the ER to the cytosol.


Pssm-ID: 239294 [Multi-domain]  Cd Length: 108  Bit Score: 71.27  E-value: 2.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 157 KDVIELTDDSFDkNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVKEQ--TKGKVKLAAVDATVNQVLASRYGIRGF 234
Cdd:cd02996    1 SEIVSLTSGNID-DILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEEfpDAGKVVWGKVDCDKESDIADRYRINKY 79

                         90       100
                 ....*....|....*....|.
gi 544186040 235 PTIKIFQKGESP-VDYDGGRT 254
Cdd:cd02996   80 PTLKLFRNGMMMkREYRGQRS 100
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 23-122 6.65e-15

PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain, similar to that of PDIa, with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. The CXFS motif in the N-terminal domain allows ERp44 to form stable reversible mixed disulfides with its substrates. Through this activity, ERp44 mediates the ER localization of Ero1alpha, a protein that oxidizes protein disulfide isomerases into their active form. ERp44 also prevents the secretion of unassembled cargo protein with unpaired cysteines. It also modulates the activity of inositol 1,4,5-triphosphate type I receptor (IP3R1), an intracellular channel protein that mediates calcium release from the ER to the cytosol.


Pssm-ID: 239294 [Multi-domain]  Cd Length: 108  Bit Score: 70.50  E-value: 6.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  23 DVIELTPSNFNrEVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDV------VKVGAVDADKHHSLGGQYGVQGFP 96
Cdd:cd02996    2 EIVSLTSGNID-DILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEEfpdagkVVWGKVDCDKESDIADRYRINKYP 80

                         90       100
                 ....*....|....*....|....*...
gi 544186040  97 TIKIF--GSNKNRpeDYQGGRTGEAIVD 122
Cdd:cd02996   81 TLKLFrnGMMMKR--EYRGQRSVEALAE 106
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 30-101 1.62e-14

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


Pssm-ID: 239245 [Multi-domain]  Cd Length: 93  Bit Score: 68.74  E-value: 1.62e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544186040  30 SNFNREVIQSDSLwLVEFYAPWCGHCQRLTPEWKKAATALKDvVKVGAVDADKHHSLGGQYGVQGFPTIKIF 101
Cdd:cd02947    1 EEFEELIKSAKPV-VVDFWAPWCGPCKAIAPVLEELAEEYPK-VKFVKVDVDENPELAEEYGVRSIPTFLFF 70
trxA PRK09381
thioredoxin TrxA;
21-101 5.03e-12

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 62.39  E-value: 5.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  21 SDDVIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKI 100
Cdd:PRK09381   2 SDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLL 81


                 .
gi 544186040 101 F 101
Cdd:PRK09381  82 F 82
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 31-122 1.33e-10

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 62.85  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  31 NFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDV--VKVGAVDADKHHSLGGQYGVQGFPTIKIFGSNKNRP 108
Cdd:PTZ00102 366 TFEEIVFKSDKDVLLEIYAPWCGHCKNLEPVYNELGEKYKDNdsIIVAKMNGTANETPLEEFSWSAFPTILFVKAGERTP 445

                         90
                 ....*....|....
gi 544186040 109 EDYQGGRTGEAIVD 122
Cdd:PTZ00102 446 IPYEGERTVEGFKE 459
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 44-107 2.31e-10

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


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 56.17  E-value: 2.31e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544186040  44 LVEFYAPWCGHCQRLTPEWKKAATALKDV--VKVGAVDADKHHSLGGQYGVQGFPTIKIFGSNKNR 107
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELALLNKGVkfEAVDVDEDPALEKELKRYGVGGVPTLVVFGPGIGV 66
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 180-248 2.84e-10

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


Pssm-ID: 239254 [Multi-domain]  Cd Length: 96  Bit Score: 56.90  E-value: 2.84e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544186040 180 VEFYAPWCGHCKNLEPewaaAASEVKEQTKGKVKLAAVDATVNQVLASRYGIRGFPTIKIFQKGEsPVD 248
Cdd:cd02956   17 VDFWAPRSPPSKELLP----LLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQ-PVD 80
PTZ00051 PTZ00051
thioredoxin; Provisional
 163-245 1.04e-09

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 55.27  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 163 TDDSFDKnVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEvkeqtKGKVKLAAVDATVNQVLASRYGIRGFPTIKIFQK 242
Cdd:PTZ00051   7 SQAEFES-TLSQNELVIVDFYAEWCGPCKRIAPFYEECSKE-----YTKMVFVKVDVDELSEVAEKENITSMPTFKVFKN 80


                 ...
gi 544186040 243 GES 245
Cdd:PTZ00051  81 GSV 83
PTZ00051 PTZ00051
thioredoxin; Provisional
 36-105 1.30e-09

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 55.27  E-value: 1.30e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  36 VIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVgAVDADKHHSLGGQYGVQGFPTIKIFGSNK 105
Cdd:PTZ00051  14 TLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFV-KVDVDELSEVAEKENITSMPTFKVFKNGS 82
PRK10996 PRK10996
thioredoxin 2; Provisional
 23-101 4.04e-09

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 54.69  E-value: 4.04e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544186040  23 DVIELTPSNFNrEVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIF 101
Cdd:PRK10996  36 EVINATGETLD-KLLQDDLPVVIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIF 113
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 43-115 7.53e-09

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


Pssm-ID: 239291 [Multi-domain]  Cd Length: 109  Bit Score: 53.23  E-value: 7.53e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544186040  43 WLVEFYAPWCGHCQRLTPEWKKAATALKDV-VKVGAVDADKHHSLGGQ--YGVQGFPTIKIFGSNKNRPEDYQGGR 115
Cdd:cd02993   24 TLVVLYAPWCPFCQAMEASYEELAEKLAGSnVKVAKFNADGEQREFAKeeLQLKSFPTILFFPKNSRQPIKYPSEQ 99
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 43-130 9.49e-09

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 53.93  E-value: 9.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  43 WLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVG-AVD--------------------ADKHHSLGGQYGVQGFPTIKIF 101
Cdd:COG0526   31 VLVNFWATWCPPCRAEMPVLKELAEEYGGVVFVGvDVDenpeavkaflkelglpypvlLDPDGELAKAYGVRGIPTTVLI 110

                         90       100
                 ....*....|....*....|....*....
gi 544186040 102 GSNKNRPEDYQGGRTGEAIVDAALSALRQ 130
Cdd:COG0526  111 DKDGKIVARHVGPLSPEELEEALEKLLAK 139
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 44-122 1.75e-08

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


Pssm-ID: 239297 [Multi-domain]  Cd Length: 100  Bit Score: 51.98  E-value: 1.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  44 LVEFYAPWCGHCQRLTPEWKKAATALKDVvKVGAVDADK-HHSLGGQYGVQGFPTIKIFGSNKN-RpedYQGGRTGEAIV 121
Cdd:cd02999   22 AVLFYASWCPFSASFRPHFNALSSMFPQI-RHLAIEESSiKPSLLSRYGVVGFPTILLFNSTPRvR---YNGTRTLDSLA 97


                 .
gi 544186040 122 D 122
Cdd:cd02999   98 A 98
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 30-120 4.34e-08

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


Pssm-ID: 239254 [Multi-domain]  Cd Length: 96  Bit Score: 50.73  E-value: 4.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  30 SNFNREVIQSD-SLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIFgsNKNRP 108
Cdd:cd02956    1 QNFQQVLQESTqVPVVVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLF--AAGQP 78

                         90
                 ....*....|...
gi 544186040 109 ED-YQGGRTGEAI 120
Cdd:cd02956   79 VDgFQGAQPEEQL 91
PLN02309 PLN02309
5'-adenylylsulfate reductase
 43-111 6.40e-08

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 54.41  E-value: 6.40e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544186040  43 WLVEFYAPWCGHCQRLTPEWKKAATALKDV-VKVGAVDADKHHSLGGQYGVQ--GFPTIKIFGSNKNRPEDY 111
Cdd:PLN02309 368 WLVVLYAPWCPFCQAMEASYEELAEKLAGSgVKVAKFRADGDQKEFAKQELQlgSFPTILLFPKNSSRPIKY 439
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 179-244 7.79e-08

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


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 49.23  E-value: 7.79e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544186040 179 MVEFYAPWCGHCKNLEPEWAAAASEvkeqtKGKVKLAAVDATVNQVL---ASRYGIRGFPTIKIFQKGE 244
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELALL-----NKGVKFEAVDVDEDPALekeLKRYGVGGVPTLVVFGPGI 64
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 175-254 9.17e-08

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


Pssm-ID: 239297 [Multi-domain]  Cd Length: 100  Bit Score: 49.66  E-value: 9.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 175 EDVWMVEFYAPWCGHCKNLEPEWAAAASEVKEqtkgkVKLAAVDATVNQ-VLASRYGIRGFPTIKIFQkgESP-VDYDGG 252
Cdd:cd02999   18 EDYTAVLFYASWCPFSASFRPHFNALSSMFPQ-----IRHLAIEESSIKpSLLSRYGVVGFPTILLFN--STPrVRYNGT 90


                 ..
gi 544186040 253 RT 254
Cdd:cd02999   91 RT 92
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 178-253 1.04e-07

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


Pssm-ID: 239291 [Multi-domain]  Cd Length: 109  Bit Score: 50.14  E-value: 1.04e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544186040 178 WMVEFYAPWCGHCKNLEPEWAAAASEVKEQtkgKVKLAAVDATVNQVLASR--YGIRGFPTIKIFQKGES-PVDYDGGR 253
Cdd:cd02993   24 TLVVLYAPWCPFCQAMEASYEELAEKLAGS---NVKVAKFNADGEQREFAKeeLQLKSFPTILFFPKNSRqPIKYPSEQ 99
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 43-111 1.32e-06

5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the assimilation of inorganic sulfate, is closely related to the thioredoxin-dependent PAPS reductase of Bacteria (CysH) and Saccharomyces cerevisiae. However, it has its own C-terminal thioredoxin-like domain and is not thioredoxin-dependent. Also, it has a substrate preference for 5'-adenylylsulfate (APS) over 3'-phosphoadenylylsulfate (PAPS) so the pathway does not require an APS kinase (CysC) to convert APS to PAPS. Arabidopsis thaliana appears to have three isozymes, all able to complement E. coli CysH mutants (even in backgrounds lacking thioredoxin or APS kinase) but likely localized to different compartments in Arabidopsis. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 273072 [Multi-domain]  Cd Length: 463  Bit Score: 50.40  E-value: 1.32e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544186040   43 WLVEFYAPWCGHCQRLTPEWKKAATALKDV-VKVGAVDADKHHSLGGQYGVQ--GFPTIKIFGSNKNRPEDY 111
Cdd:TIGR00424 374 WLVVLYAPWCPFCQAMEASYLELAEKLAGSgVKVAKFRADGDQKEFAKQELQlgSFPTILFFPKHSSRPIKY 445
DsbDgamma cd02953
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
 179-248 2.12e-06

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


Pssm-ID: 239251 [Multi-domain]  Cd Length: 104  Bit Score: 46.06  E-value: 2.12e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544186040 179 MVEFYAPWCGHCKNLEPEwAAAASEVKEQTKGKVKLAAVDAT----VNQVLASRYGIRGFPTIKIFQKGESPVD 248
Cdd:cd02953   15 FVDFTADWCVTCKVNEKV-VFSDPEVQAALKKDVVLLRADWTkndpEITALLKRFGVFGPPTYLFYGPGGEPEP 87
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 160-264 2.60e-06

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 46.61  E-value: 2.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 160 IELTDdsFDKNVLDSED----VWMVEFYAPWCGHCKNLEPEWAAAASEVK---------EQTKGKVKLAAVDATV----- 221
Cdd:COG0526   11 FTLTD--LDGKPLSLADlkgkPVLVNFWATWCPPCRAEMPVLKELAEEYGgvvfvgvdvDENPEAVKAFLKELGLpypvl 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 544186040 222 ---NQVLASRYGIRGFPTIKIFQKGESPVDYDGGRTRSDIVSRALD 264
Cdd:COG0526   89 ldpDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALE 134
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 38-113 2.79e-06

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


Pssm-ID: 239247 [Multi-domain]  Cd Length: 97  Bit Score: 45.57  E-value: 2.79e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544186040  38 QSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIFgSNKNRPEDYQG 113
Cdd:cd02949   11 ESDRLILVLYTSPTCGPCRTLKPILNKVIDEFDGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFF-KDKELVKEISG 85
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 179-273 6.72e-06

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


Pssm-ID: 239248 [Multi-domain]  Cd Length: 142  Bit Score: 45.79  E-value: 6.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 179 MVEFYAPWCGHCKNLEPEWAaaasEVKEQTKGKVKLAA--VDATVNQVLASRYGIRGFPTIKIFQKGESPVDYDGGRTRS 256
Cdd:cd02950   24 LVEFYADWCTVCQEMAPDVA----KLKQKYGDQVNFVMlnVDNPKWLPEIDRYRVDGIPHFVFLDREGNEEGQSIGLQPK 99

                         90
                 ....*....|....*..
gi 544186040 257 DIVSRALDLFSDNAPPP 273
Cdd:cd02950  100 QVLAQNLDALVAGEPLP 116
PDI_a_EFP1_N cd03006
PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase ...
 159-252 2.39e-05

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


Pssm-ID: 239304  Cd Length: 113  Bit Score: 43.23  E-value: 2.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 159 VIELTDDSFDKNVLDSE--DVWMVEFYAPWCGHCKNLEPEWAAAASEVKEQtkgkVKLAAVDATVNQVLASR-YGIRGFP 235
Cdd:cd03006   11 VLDFYKGQLDYAEELRTdaEVSLVMYYAPWDAQSQAARQEFEQVAQKLSDQ----VLFVAINCWWPQGKCRKqKHFFYFP 86

                         90
                 ....*....|....*..
gi 544186040 236 TIKIFQKGESPVDYDGG 252
Cdd:cd03006   87 VIHLYYRSRGPIEYKGP 103
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 169-249 6.83e-05

5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the assimilation of inorganic sulfate, is closely related to the thioredoxin-dependent PAPS reductase of Bacteria (CysH) and Saccharomyces cerevisiae. However, it has its own C-terminal thioredoxin-like domain and is not thioredoxin-dependent. Also, it has a substrate preference for 5'-adenylylsulfate (APS) over 3'-phosphoadenylylsulfate (PAPS) so the pathway does not require an APS kinase (CysC) to convert APS to PAPS. Arabidopsis thaliana appears to have three isozymes, all able to complement E. coli CysH mutants (even in backgrounds lacking thioredoxin or APS kinase) but likely localized to different compartments in Arabidopsis. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 273072 [Multi-domain]  Cd Length: 463  Bit Score: 45.01  E-value: 6.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  169 KNVLDSE---DVWMVEFYAPWCGHCKNLEpewaAAASEVKEQTKGK-VKLAAVDATVNQVLASRYGIR--GFPTIKIFQK 242
Cdd:TIGR00424 362 ENLLKLEerkEAWLVVLYAPWCPFCQAME----ASYLELAEKLAGSgVKVAKFRADGDQKEFAKQELQlgSFPTILFFPK 437


                  ....*...
gi 544186040  243 GES-PVDY 249
Cdd:TIGR00424 438 HSSrPIKY 445
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 179-240 8.35e-05

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 42.58  E-value: 8.35e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544186040 179 MVEFYAPWCGHCKNLEPEwAAAASEVKEQTKGKVKLAAVDA-------------TVNQVLASRYGIRGFPTIKIF 240
Cdd:COG2143   44 LLFFESDWCPYCKKLHKE-VFSDPEVAAYLKENFVVVQLDAegdkevtdfdgetLTEKELARKYGVRGTPTLVFF 117
PDI_a_EFP1_N cd03006
PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase ...
 18-116 8.49e-05

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


Pssm-ID: 239304  Cd Length: 113  Bit Score: 41.69  E-value: 8.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  18 YSSSDDVIELTPSNFNR--EVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDAdkHHSLG---GQYGV 92
Cdd:cd03006    5 FSQRSPVLDFYKGQLDYaeELRTDAEVSLVMYYAPWDAQSQAARQEFEQVAQKLSDQVLFVAINC--WWPQGkcrKQKHF 82

                         90       100
                 ....*....|....*....|....
gi 544186040  93 QGFPTIKIFGSNKNRPEDYQGGRT 116
Cdd:cd03006   83 FYFPVIHLYYRSRGPIEYKGPMRA 106
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 44-101 9.91e-05

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 42.20  E-value: 9.91e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544186040  44 LVEFYAPWCGHCQRL------TPEWKKAATALKDVVKvgaVDAD-------------KHHSLGGQYGVQGFPTIKIF 101
Cdd:COG2143   44 LLFFESDWCPYCKKLhkevfsDPEVAAYLKENFVVVQ---LDAEgdkevtdfdgetlTEKELARKYGVRGTPTLVFF 117
Thioredoxin_7 pfam13899
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 179-240 1.04e-04

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


Pssm-ID: 433567 [Multi-domain]  Cd Length: 84  Bit Score: 40.81  E-value: 1.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544186040  179 MVEFYAPWCGHCKNLEpEWAAAASEVKEQTKGK-VKLAAVDATVNQVLASRYGIRGFPTIKIF 240
Cdd:pfam13899  21 LVDFGADWCFTCQVLE-RDFLSHEEVKAALAKNfVLLRLDWTSRDANITRAFDGQGVPHIAFL 82
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 173-257 1.11e-04

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


Pssm-ID: 239247 [Multi-domain]  Cd Length: 97  Bit Score: 40.95  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 173 DSEDVWMVEFYAPWCGHCKNLEPEwaaaASEVKEQTKGKVKLAAVDATVNQVLASRYGIRGFPTIKIFQKGESPVDYDGG 252
Cdd:cd02949   11 ESDRLILVLYTSPTCGPCRTLKPI----LNKVIDEFDGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDKELVKEISGV 86


                 ....*
gi 544186040 253 RTRSD 257
Cdd:cd02949   87 KMKSE 91
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 44-128 1.80e-04

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


Pssm-ID: 239248 [Multi-domain]  Cd Length: 142  Bit Score: 41.55  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  44 LVEFYAPWCGHCQRLTPEWKKAATALKD---VVKVGaVDADKHHSLGGQYGVQGFPTIKIFgSNKNRPEDYQGGRTGEAI 120
Cdd:cd02950   24 LVEFYADWCTVCQEMAPDVAKLKQKYGDqvnFVMLN-VDNPKWLPEIDRYRVDGIPHFVFL-DREGNEEGQSIGLQPKQV 101


                 ....*...
gi 544186040 121 VDAALSAL 128
Cdd:cd02950  102 LAQNLDAL 109
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
179-263 2.59e-04

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 40.10  E-value: 2.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  179 MVEFYAPWCGHCKNLEPE---WAAAASEVKEQTKGK---------VKLAAVDATVNQVLASRYGIRGFPTIkIFQKGESP 246
Cdd:pfam13098   8 LVVFTDPDCPYCKKLKKElleDPDVTVYLGPNFVFIavniwcakeVAKAFTDILENKELGRKYGVRGTPTI-VFFDGKGE 86

                          90
                  ....*....|....*..
gi 544186040  247 VDYDGGRTRSDIVSRAL 263
Cdd:pfam13098  87 LLRLPGYVPAEEFLALL 103
TRX_GRX_like cd02973
Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins ...
 182-239 3.30e-04

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


Pssm-ID: 239271 [Multi-domain]  Cd Length: 67  Bit Score: 38.70  E-value: 3.30e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 544186040 182 FYAPWCGHCknlePEWAAAASEVKEqTKGKVKLAAVDATVNQVLASRYGIRGFPTIKI 239
Cdd:cd02973    6 FVSPTCPYC----PDAVQAANRIAA-LNPNISAEMIDAAEFPDLADEYGVMSVPAIVI 58
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 161-259 5.77e-04

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


Pssm-ID: 239261 [Multi-domain]  Cd Length: 111  Bit Score: 39.28  E-value: 5.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 161 ELTDDSFDKnvldsedVWMVEFYAPWCGHCKNLEPEWAAAASEVKEQTKGkvkLAAVDATVNQVLASRYGIRGFPTIKIF 240
Cdd:cd02963   17 EIVPKSFKK-------PYLIKITSDWCFSCIHIEPVWKEVIQELEPLGVG---IATVNAGHERRLARKLGAHSVPAIVGI 86

                         90
                 ....*....|....*....
gi 544186040 241 QKGESPVDYDGGRTRSDIV 259
Cdd:cd02963   87 INGQVTFYHDSSFTKQHVV 105
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 19-98 9.29e-04

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


Pssm-ID: 239261 [Multi-domain]  Cd Length: 111  Bit Score: 38.89  E-value: 9.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  19 SSSDDVIELTPSNFNREVIqSDSL---WLVEFYAPWCGHCQRLTPEWKKAATALKDV-VKVGAVDADKHHSLGGQYGVQG 94
Cdd:cd02963    1 DSFDYKYSLTFSQYENEIV-PKSFkkpYLIKITSDWCFSCIHIEPVWKEVIQELEPLgVGIATVNAGHERRLARKLGAHS 79


                 ....
gi 544186040  95 FPTI 98
Cdd:cd02963   80 VPAI 83
PLN02309 PLN02309
5'-adenylylsulfate reductase
 175-260 1.02e-03

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 41.31  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 175 EDVWMVEFYAPWCGHCKNLEpewaAAASEVKEQTKGK-VKLAAVDATVNQVLASRYGI--RGFPTIKIFQKGES-PVDYd 250
Cdd:PLN02309 365 KEPWLVVLYAPWCPFCQAME----ASYEELAEKLAGSgVKVAKFRADGDQKEFAKQELqlGSFPTILLFPKNSSrPIKY- 439

                         90
                 ....*....|
gi 544186040 251 gGRTRSDIVS 260
Cdd:PLN02309 440 -PSEKRDVDS 448
DsbDgamma cd02953
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
 44-108 1.64e-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: 37.97  E-value: 1.64e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544186040  44 LVEFYAPWCGHCQ---RLT---PEWKKAATalKDVVkvgAVDAD------KHHSLGGQYGVQGFPTIKIFGSNKNRP 108
Cdd:cd02953   15 FVDFTADWCVTCKvneKVVfsdPEVQAALK--KDVV---LLRADwtkndpEITALLKRFGVFGPPTYLFYGPGGEPE 86
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
225-384 1.80e-03

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 39.27  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  225 LASRYGIRgFPTIKIFQK-GESPVDYDGGRTRSDIVSRaldlFSDNAPPPeLLEIINEDIAKRTCEEHQLCVVAVlphIL 303
Cdd:pfam13848  33 VADKYNIK-EPAILLFRKfDEETVHYPGDSINFEDLKK----FIQKNCLP-LVREFTPENAEELFEEGIPPLLLL---FL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040  304 DTGAAGRNSYLEVLLKLADKYKKKMwGWLWTEAGA-QSELETaLGIGGFGYPAMAAIN-ARKMKFALLKGSFSEQGINEF 381
Cdd:pfam13848 104 KKDDESTEEFKKALEKVAKKFRGKI-NFALVDAKSfGRPLEY-FGLSESDLPVIVIVDsFSHMYKYFPSDEFSPESLKEF 181


                  ...
gi 544186040  382 LRE 384
Cdd:pfam13848 182 IND 184
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
44-101 1.94e-03

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 37.79  E-value: 1.94e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544186040   44 LVEFYAPWCGHCQRL--------------TPEWKKAATALK--DVVKVGAVDADKHHSLGGQYGVQGFPTIKIF 101
Cdd:pfam13098   8 LVVFTDPDCPYCKKLkkelledpdvtvylGPNFVFIAVNIWcaKEVAKAFTDILENKELGRKYGVRGTPTIVFF 81
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 180-254 3.85e-03

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


Pssm-ID: 239309 [Multi-domain]  Cd Length: 123  Bit Score: 37.28  E-value: 3.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186040 180 VEFYAPWCGHCKNLEPEWAAAASEV-------KEQTKGKVK--LAAVD---ATVNQ---VLASRYGIRGFPTIKIFQKGE 244
Cdd:cd03011   25 VYFWATWCPVCRFTSPTVNQLAADYpvvsvalRSGDDGAVArfMQKKGygfPVINDpdgVISARWGVSVTPAIVIVDPGG 104

                         90
                 ....*....|
gi 544186040 245 SpVDYDGGRT 254
Cdd:cd03011  105 I-VFVTTGVT 113
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 44-97 6.72e-03

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


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 36.45  E-value: 6.72e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544186040  44 LVEFYAPWCGHCQRLTPEWKKAA--TALKDVVKVG-AVD---------------------ADKHHSLGGQYGVQGFPT 97
Cdd:cd02966   23 LVNFWASWCPPCRAEMPELEALAkeYKDDGVEVVGvNVDdddpaavkaflkkygitfpvlLDPDGELAKAYGVRGLPT 100
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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