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Conserved domains on  [gi|356543934|ref|XP_003540413|]
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protein disulfide-isomerase 5-4 isoform X2 [Glycine max]

Protein Classification

protein disulfide isomerase family protein( domain architecture ID 10620099)

protein disulfide isomerase (PDI) family protein belongs to the thioredoxin superfamily, and is involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as a catalyst and or a folding assistant

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COPIIcoated_ERV super family cl06835
Endoplasmic reticulum vesicle transporter; This family is conserved from plants and fungi to ...
 293-461 1.23e-34

Endoplasmic reticulum vesicle transporter; This family is conserved from plants and fungi to humans. Erv46 works in close conjunction with Erv41 and together they form a complex which cycles between the endoplasmic reticulum and Golgi complex. Erv46-41 interacts strongly with the endoplasmic reticulum glucosidase II. Mammalian glucosidase II comprises a catalytic alpha-subunit and a 58 kDa beta subunit, which is required for ER localization. All proteins identified biochemically as Erv41p-Erv46p interactors are localized to the early secretory pathway and are involved in protein maturation and processing in the ER and/or sorting into COPII vesicles for transport to the Golgi.


The actual alignment was detected with superfamily member pfam07970:

Pssm-ID: 462327  Cd Length: 225  Bit Score: 129.26  E-value: 1.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934  293 GCRIDGYVRVKKVPGNLIISA-----RSNAHSFDAS-------QMNMSHVINHLSFGRKvslrvmsdvkrlipYVGSSHD 360
Cdd:pfam07970  54 GCRIKGTLEVNKVAGNFHIAPgrsfqQGGMHVHDLSpylklpdKFNFSHTIHHLSFGPD--------------IPGEKVN 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934  361 RLNGrsfINTHDLGANVTIEHYLQIVKTeVITRKEYKLVEEYEY--TAHSSVAQSLHIPVAK-------FHLELSPMQVL 431
Cdd:pfam07970 120 PLDG---TKVQTDTGNYMFQYFLKVVPT-RYEFLDGKKIETNQYsvTSHERPLTGGRDEHGRgglpgvfFNYDISPMKVI 195

                         170       180       190
                  ....*....|....*....|....*....|
gi 356543934  432 ITENQKSFSHFITNVCAIIGGIFTVAGIMD 461
Cdd:pfam07970 196 NTEQRRSFSHFLTSVCAIIGGVFTVASLID 225
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 144-258 8.46e-33

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: 120.02  E-value: 8.46e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934 144 VVLTTQNFDKYAHQFLITVVNFYAPWCYWSQRLKPSWEKTAKIIKErydpemDGRIILGRVDCTEDGDLCRSHHIQGYPS 223
Cdd:cd02961    1 VELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKG------DGKVVVAKVDCTANNDLCSEYGVRGYPT 74

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 356543934 224 IRIFRKGSdvrsdhghHDHESYYGDRDTDSLVKTM 258
Cdd:cd02961   75 IKLFPNGS--------KEPVKYEGPRTLESLVEFI 101
ERGIC_N pfam13850
Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC); This family is the N-terminal of ...
 7-98 2.73e-28

Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC); This family is the N-terminal of ERGIC proteins, ER-Golgi intermediate compartment clusters, otherwise known as Ervs, and is associated with family COPIIcoated_ERV, pfam07970.


:

Pssm-ID: 464000  Cd Length: 91  Bit Score: 107.54  E-value: 2.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934    7 IKSVDFYRKIPRDLTEASLSGAGLSIVAALAMIFLFGMELNSYLSVSTSTQVIVDKSSDGDyLRIDFNISFPALSCEFAA 86
Cdd:pfam13850   1 LKSFDAFPKTPEDYRVRTSSGGIITIISILIILFLFLSELGSYLTGTVDPELVVDKSRGEK-LQINLDITFPAMPCDLLS 79

                          90
                  ....*....|..
gi 356543934   87 VDVSDVLGTNRL 98
Cdd:pfam13850  80 VDVMDASGDRQL 91
 
Name Accession Description Interval E-value
COPIIcoated_ERV pfam07970
Endoplasmic reticulum vesicle transporter; This family is conserved from plants and fungi to ...
 293-461 1.23e-34

Endoplasmic reticulum vesicle transporter; This family is conserved from plants and fungi to humans. Erv46 works in close conjunction with Erv41 and together they form a complex which cycles between the endoplasmic reticulum and Golgi complex. Erv46-41 interacts strongly with the endoplasmic reticulum glucosidase II. Mammalian glucosidase II comprises a catalytic alpha-subunit and a 58 kDa beta subunit, which is required for ER localization. All proteins identified biochemically as Erv41p-Erv46p interactors are localized to the early secretory pathway and are involved in protein maturation and processing in the ER and/or sorting into COPII vesicles for transport to the Golgi.


Pssm-ID: 462327  Cd Length: 225  Bit Score: 129.26  E-value: 1.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934  293 GCRIDGYVRVKKVPGNLIISA-----RSNAHSFDAS-------QMNMSHVINHLSFGRKvslrvmsdvkrlipYVGSSHD 360
Cdd:pfam07970  54 GCRIKGTLEVNKVAGNFHIAPgrsfqQGGMHVHDLSpylklpdKFNFSHTIHHLSFGPD--------------IPGEKVN 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934  361 RLNGrsfINTHDLGANVTIEHYLQIVKTeVITRKEYKLVEEYEY--TAHSSVAQSLHIPVAK-------FHLELSPMQVL 431
Cdd:pfam07970 120 PLDG---TKVQTDTGNYMFQYFLKVVPT-RYEFLDGKKIETNQYsvTSHERPLTGGRDEHGRgglpgvfFNYDISPMKVI 195

                         170       180       190
                  ....*....|....*....|....*....|
gi 356543934  432 ITENQKSFSHFITNVCAIIGGIFTVAGIMD 461
Cdd:pfam07970 196 NTEQRRSFSHFLTSVCAIIGGVFTVASLID 225
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 144-258 8.46e-33

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: 120.02  E-value: 8.46e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934 144 VVLTTQNFDKYAHQFLITVVNFYAPWCYWSQRLKPSWEKTAKIIKErydpemDGRIILGRVDCTEDGDLCRSHHIQGYPS 223
Cdd:cd02961    1 VELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKG------DGKVVVAKVDCTANNDLCSEYGVRGYPT 74

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 356543934 224 IRIFRKGSdvrsdhghHDHESYYGDRDTDSLVKTM 258
Cdd:cd02961   75 IKLFPNGS--------KEPVKYEGPRTLESLVEFI 101
ERGIC_N pfam13850
Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC); This family is the N-terminal of ...
 7-98 2.73e-28

Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC); This family is the N-terminal of ERGIC proteins, ER-Golgi intermediate compartment clusters, otherwise known as Ervs, and is associated with family COPIIcoated_ERV, pfam07970.


Pssm-ID: 464000  Cd Length: 91  Bit Score: 107.54  E-value: 2.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934    7 IKSVDFYRKIPRDLTEASLSGAGLSIVAALAMIFLFGMELNSYLSVSTSTQVIVDKSSDGDyLRIDFNISFPALSCEFAA 86
Cdd:pfam13850   1 LKSFDAFPKTPEDYRVRTSSGGIITIISILIILFLFLSELGSYLTGTVDPELVVDKSRGEK-LQINLDITFPAMPCDLLS 79

                          90
                  ....*....|..
gi 356543934   87 VDVSDVLGTNRL 98
Cdd:pfam13850  80 VDVMDASGDRQL 91
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 141-258 4.87e-26

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: 110.15  E-value: 4.87e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934  141 EGSVVLTTQNFDKY--AHQFLItvVNFYAPWCYWSQRLKPSWEKTAKIIKERydpemDGRIILGRVDCTEDGDLCRSHHI 218
Cdd:TIGR01130   1 EDVLVLTKDNFDDFikSHEFVL--VEFYAPWCGHCKSLAPEYEKAADELKKK-----GPPIKLAKVDATEEKDLAQKYGV 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 356543934  219 QGYPSIRIFRKGSDVRSDhghhdhesYYGDRDTDSLVKTM 258
Cdd:TIGR01130  74 SGYPTLKIFRNGEDSVSD--------YNGPRDADGIVKYM 105
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 144-281 1.29e-18

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 88.27  E-value: 1.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934 144 VVLTTQNFDKYAHQFLITVVNFYAPWCYWSQRLKPSWEKTAKIIKERYDPemdgrIILGRVDCTEDGDLCRSHHIQGYPS 223
Cdd:PTZ00102  35 TVLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSE-----IVLASVDATEEMELAQEFGVRGYPT 109

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356543934 224 IRIFRKGSDVrsdhghhdheSYYGDRDTDSLVKTMENL----VASLPSESQKLPLEDKSNVA 281
Cdd:PTZ00102 110 IKFFNKGNPV----------NYSGGRTADGIVSWIKKLtgpaVTEVESASEIKLIAKKIFVA 161
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 144-259 7.90e-16

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: 73.04  E-value: 7.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934  144 VVLTTQNFDKY-AHQFLITVVNFYAPWCYWSQRLKPSWEKTAKiikerydpEMDGRIILGRVDCTEDGDLCRSHHIQGYP 222
Cdd:pfam00085   3 VVLTDANFDEVvQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQ--------EYKGNVVFAKVDVDENPDLASKYGVRGYP 74

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 356543934  223 SIRIFRKGSDVrsdhghhdhESYYGDRDTDSLVKTME 259
Cdd:pfam00085  75 TLIFFKNGQPV---------DDYVGARPKDALAAFLK 102
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 144-230 3.44e-11

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: 59.83  E-value: 3.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934 144 VVLTTQNFDKYAHQF-LITVVNFYAPWCYWSQRLKPSWEKTAKiikerydpEMDGRIILGRVDCTEDGDLCRSHHIQGYP 222
Cdd:COG3118    3 VELTDENFEEEVLESdKPVLVDFWAPWCGPCKMLAPVLEELAA--------EYGGKVKFVKVDVDENPELAAQFGVRSIP 74


                 ....*...
gi 356543934 223 SIRIFRKG 230
Cdd:COG3118   75 TLLLFKDG 82
 
Name Accession Description Interval E-value
COPIIcoated_ERV pfam07970
Endoplasmic reticulum vesicle transporter; This family is conserved from plants and fungi to ...
 293-461 1.23e-34

Endoplasmic reticulum vesicle transporter; This family is conserved from plants and fungi to humans. Erv46 works in close conjunction with Erv41 and together they form a complex which cycles between the endoplasmic reticulum and Golgi complex. Erv46-41 interacts strongly with the endoplasmic reticulum glucosidase II. Mammalian glucosidase II comprises a catalytic alpha-subunit and a 58 kDa beta subunit, which is required for ER localization. All proteins identified biochemically as Erv41p-Erv46p interactors are localized to the early secretory pathway and are involved in protein maturation and processing in the ER and/or sorting into COPII vesicles for transport to the Golgi.


Pssm-ID: 462327  Cd Length: 225  Bit Score: 129.26  E-value: 1.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934  293 GCRIDGYVRVKKVPGNLIISA-----RSNAHSFDAS-------QMNMSHVINHLSFGRKvslrvmsdvkrlipYVGSSHD 360
Cdd:pfam07970  54 GCRIKGTLEVNKVAGNFHIAPgrsfqQGGMHVHDLSpylklpdKFNFSHTIHHLSFGPD--------------IPGEKVN 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934  361 RLNGrsfINTHDLGANVTIEHYLQIVKTeVITRKEYKLVEEYEY--TAHSSVAQSLHIPVAK-------FHLELSPMQVL 431
Cdd:pfam07970 120 PLDG---TKVQTDTGNYMFQYFLKVVPT-RYEFLDGKKIETNQYsvTSHERPLTGGRDEHGRgglpgvfFNYDISPMKVI 195

                         170       180       190
                  ....*....|....*....|....*....|
gi 356543934  432 ITENQKSFSHFITNVCAIIGGIFTVAGIMD 461
Cdd:pfam07970 196 NTEQRRSFSHFLTSVCAIIGGVFTVASLID 225
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 144-258 8.46e-33

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: 120.02  E-value: 8.46e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934 144 VVLTTQNFDKYAHQFLITVVNFYAPWCYWSQRLKPSWEKTAKIIKErydpemDGRIILGRVDCTEDGDLCRSHHIQGYPS 223
Cdd:cd02961    1 VELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKG------DGKVVVAKVDCTANNDLCSEYGVRGYPT 74

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 356543934 224 IRIFRKGSdvrsdhghHDHESYYGDRDTDSLVKTM 258
Cdd:cd02961   75 IKLFPNGS--------KEPVKYEGPRTLESLVEFI 101
ERGIC_N pfam13850
Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC); This family is the N-terminal of ...
 7-98 2.73e-28

Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC); This family is the N-terminal of ERGIC proteins, ER-Golgi intermediate compartment clusters, otherwise known as Ervs, and is associated with family COPIIcoated_ERV, pfam07970.


Pssm-ID: 464000  Cd Length: 91  Bit Score: 107.54  E-value: 2.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934    7 IKSVDFYRKIPRDLTEASLSGAGLSIVAALAMIFLFGMELNSYLSVSTSTQVIVDKSSDGDyLRIDFNISFPALSCEFAA 86
Cdd:pfam13850   1 LKSFDAFPKTPEDYRVRTSSGGIITIISILIILFLFLSELGSYLTGTVDPELVVDKSRGEK-LQINLDITFPAMPCDLLS 79

                          90
                  ....*....|..
gi 356543934   87 VDVSDVLGTNRL 98
Cdd:pfam13850  80 VDVMDASGDRQL 91
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 141-258 4.87e-26

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: 110.15  E-value: 4.87e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934  141 EGSVVLTTQNFDKY--AHQFLItvVNFYAPWCYWSQRLKPSWEKTAKIIKERydpemDGRIILGRVDCTEDGDLCRSHHI 218
Cdd:TIGR01130   1 EDVLVLTKDNFDDFikSHEFVL--VEFYAPWCGHCKSLAPEYEKAADELKKK-----GPPIKLAKVDATEEKDLAQKYGV 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 356543934  219 QGYPSIRIFRKGSDVRSDhghhdhesYYGDRDTDSLVKTM 258
Cdd:TIGR01130  74 SGYPTLKIFRNGEDSVSD--------YNGPRDADGIVKYM 105
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 144-256 3.81e-21

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: 88.08  E-value: 3.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934 144 VVLTTQNFDKYAHQFLITV-VNFYAPWCYWSQRLKPSWEKTAKIIKERYDpemdgrIILGRVDCTEDG-DLCRSHHIQGY 221
Cdd:cd02998    3 VELTDSNFDKVVGDDKKDVlVEFYAPWCGHCKNLAPEYEKLAAVFANEDD------VVIAKVDADEANkDLAKKYGVSGF 76

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 356543934 222 PSIRIFRKGSDvrsdhghhDHESYYGDRDTDSLVK 256
Cdd:cd02998   77 PTLKFFPKGST--------EPVKYEGGRDLEDLVK 103
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 146-258 3.80e-20

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: 85.49  E-value: 3.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934 146 LTTQNFDKYAHQF-LITVVNFYAPWCYWSQRLKPSWEKTAKiikerydpEMDGRIILGRVDCTEDG--DLCRSHHIQGYP 222
Cdd:cd03002    5 LTPKNFDKVVHNTnYTTLVEFYAPWCGHCKNLKPEYAKAAK--------ELDGLVQVAAVDCDEDKnkPLCGKYGVQGFP 76

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 356543934 223 SIRIFRKGsdvrSDHGHHDHESYYGDRDTDSLVKTM 258
Cdd:cd03002   77 TLKVFRPP----KKASKHAVEDYNGERSAKAIVDFV 108
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 142-237 4.73e-20

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: 85.13  E-value: 4.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934 142 GSVVLTTQNFDKYAHQFLITVVNFYAPWCYWSQRLKPSWEKTAKIIKERYdPEmDGRIILGRVDCTEDGDLCRSHHIQGY 221
Cdd:cd02996    2 EIVSLTSGNIDDILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEEF-PD-AGKVVWGKVDCDKESDIADRYRINKY 79

                         90
                 ....*....|....*.
gi 356543934 222 PSIRIFRKGSDVRSDH 237
Cdd:cd02996   80 PTLKLFRNGMMMKREY 95
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 144-256 1.02e-19

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


Pssm-ID: 239301 [Multi-domain]  Cd Length: 101  Bit Score: 84.11  E-value: 1.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934 144 VVLTTQNFDKYAHQFLITVVNFYAPWCYWSQRLKPSWEKTAKiikerydpEMDGRIILGRVDCTEDGDLCRSHHIQGYPS 223
Cdd:cd03003    4 VTLDRGDFDAAVNSGEIWFVNFYSPRCSHCHDLAPTWREFAK--------EMDGVIRIGAVNCGDDRMLCRSQGVNSYPS 75

                         90       100       110
                 ....*....|....*....|....*....|...
gi 356543934 224 IRIFRKGSdvrsdhghhDHESYYGDRDTDSLVK 256
Cdd:cd03003   76 LYVFPSGM---------NPEKYYGDRSKESLVK 99
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 142-254 5.12e-19

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: 81.95  E-value: 5.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934 142 GSVVLTTQNFDKYAHQFlITVVNFYAPWCYWSQRLKPSWEKTAKIikerYDPEMDGRIIlGRVDCTEDGDLCRSHHIQGY 221
Cdd:cd03005    1 GVLELTEDNFDHHIAEG-NHFVKFFAPWCGHCKRLAPTWEQLAKK----FNNENPSVKI-AKVDCTQHRELCSEFQVRGY 74

                         90       100       110
                 ....*....|....*....|....*....|...
gi 356543934 222 PSIRIFRKGSDVrsdhghhdhESYYGDRDTDSL 254
Cdd:cd03005   75 PTLLLFKDGEKV---------DKYKGTRDLDSL 98
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 144-281 1.29e-18

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 88.27  E-value: 1.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934 144 VVLTTQNFDKYAHQFLITVVNFYAPWCYWSQRLKPSWEKTAKIIKERYDPemdgrIILGRVDCTEDGDLCRSHHIQGYPS 223
Cdd:PTZ00102  35 TVLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSE-----IVLASVDATEEMELAQEFGVRGYPT 109

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356543934 224 IRIFRKGSDVrsdhghhdheSYYGDRDTDSLVKTMENL----VASLPSESQKLPLEDKSNVA 281
Cdd:PTZ00102 110 IKFFNKGNPV----------NYSGGRTADGIVSWIKKLtgpaVTEVESASEIKLIAKKIFVA 161
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 143-254 2.76e-17

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: 77.33  E-value: 2.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934 143 SVVLTTQNFDKYAHQFLIT-VVNFYAPWCYWSQRLKPSWEKTAKIIKerydpemdGRIILGRVDCTEDGDLCRSHHIQGY 221
Cdd:cd03004    3 VITLTPEDFPELVLNRKEPwLVDFYAPWCGPCQALLPELRKAARALK--------GKVKVGSVDCQKYESLCQQANIRAY 74

                         90       100       110
                 ....*....|....*....|....*....|....
gi 356543934 222 PSIRIF-RKGSDVRSDHGHHdhesyygdRDTDSL 254
Cdd:cd03004   75 PTIRLYpGNASKYHSYNGWH--------RDADSI 100
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 142-256 4.62e-17

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: 76.56  E-value: 4.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934 142 GSVVLTTQNFDKYAHQF-LITVVNFYAPWCYWSQRLKPSWEKTAKIIKerydpemdGRIILGRVDCTEDGDLCRSHHIQG 220
Cdd:cd03001    1 DVVELTDSNFDKKVLNSdDVWLVEFYAPWCGHCKNLAPEWKKAAKALK--------GIVKVGAVDADVHQSLAQQYGVRG 72

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 356543934 221 YPSIRIFRKGSdvrsdhghHDHESYYGDRDTDSLVK 256
Cdd:cd03001   73 FPTIKVFGAGK--------NSPQDYQGGRTAKAIVS 100
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 144-259 7.90e-16

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: 73.04  E-value: 7.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934  144 VVLTTQNFDKY-AHQFLITVVNFYAPWCYWSQRLKPSWEKTAKiikerydpEMDGRIILGRVDCTEDGDLCRSHHIQGYP 222
Cdd:pfam00085   3 VVLTDANFDEVvQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQ--------EYKGNVVFAKVDVDENPDLASKYGVRGYP 74

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 356543934  223 SIRIFRKGSDVrsdhghhdhESYYGDRDTDSLVKTME 259
Cdd:pfam00085  75 TLIFFKNGQPV---------DDYVGARPKDALAAFLK 102
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 143-230 1.35e-13

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: 66.57  E-value: 1.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934 143 SVV-LTTQNFDKYAHQFLITVVNFYAPWCYWSQRLKPSWEKTAKIIKErydpemDGRIILGRVDCTEDG-DLCRS-HHIQ 219
Cdd:cd02997    1 DVVhLTDEDFRKFLKKEKHVLVMFYAPWCGHCKKMKPEFTKAATELKE------DGKGVLAAVDCTKPEhDALKEeYNVK 74

                         90
                 ....*....|.
gi 356543934 220 GYPSIRIFRKG 230
Cdd:cd02997   75 GFPTFKYFENG 85
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 162-228 2.75e-11

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


Pssm-ID: 239290 [Multi-domain]  Cd Length: 114  Bit Score: 60.36  E-value: 2.75e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 356543934 162 VVNFYAPWCYWSQRLKPSWEKTAKIIKERYdpemdGRIILGRVDCTED--GDLCRSHHIQGYPSIRIFR 228
Cdd:cd02992   23 LVEFYASWCGHCRAFAPTWKKLARDLRKWR-----PVVRVAAVDCADEenVALCRDFGVTGYPTLRYFP 86
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 144-230 3.44e-11

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: 59.83  E-value: 3.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934 144 VVLTTQNFDKYAHQF-LITVVNFYAPWCYWSQRLKPSWEKTAKiikerydpEMDGRIILGRVDCTEDGDLCRSHHIQGYP 222
Cdd:COG3118    3 VELTDENFEEEVLESdKPVLVDFWAPWCGPCKMLAPVLEELAA--------EYGGKVKFVKVDVDENPELAAQFGVRSIP 74


                 ....*...
gi 356543934 223 SIRIFRKG 230
Cdd:COG3118   75 TLLLFKDG 82
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 134-230 1.04e-10

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 61.56  E-value: 1.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934 134 EVNEESVEGSVVLTTQNFDKY--AHQFLIT---VVNFYAPWCYWSQRLKPSWEKTAKiikerydpEMDGRIILGRVDCTE 208
Cdd:PTZ00443  23 KLDAEDANALVLLNDKNFEKLtqASTGATTgpwFVKFYAPWCSHCRKMAPAWERLAK--------ALKGQVNVADLDATR 94

                         90       100
                 ....*....|....*....|..
gi 356543934 209 DGDLCRSHHIQGYPSIRIFRKG 230
Cdd:PTZ00443  95 ALNLAKRFAIKGYPTLLLFDKG 116
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 163-255 2.69e-10

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


Pssm-ID: 239298 [Multi-domain]  Cd Length: 104  Bit Score: 57.46  E-value: 2.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934 163 VNFYAPWCYWSQRLKPSWEKTAKIIKERYDPemdgrIILGRVDCTEDGDLCRSHHIQGYPSIRIFRKgsdvrsdhghhDH 242
Cdd:cd03000   20 VDFYAPWCGHCKKLEPVWNEVGAELKSSGSP-----VRVGKLDATAYSSIASEFGVRGYPTIKLLKG-----------DL 83

                         90
                 ....*....|....
gi 356543934 243 E-SYYGDRDTDSLV 255
Cdd:cd03000   84 AyNYRGPRTKDDIV 97
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 103-260 3.21e-09

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: 58.92  E-value: 3.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934  103 TVRKFSIDSNLR--PTGAEFHSEP------------AANSIKHDN--EVNEESVegsVVLTTQNFDKYAHQFLITV-VNF 165
Cdd:TIGR01130 295 AVAIQDLEGNKKypMDQEEFSSENleafvkdfldgkLKPYLKSEPipEDDEGPV---KVLVGKNFDEIVLDETKDVlVEF 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934  166 YAPWCYWSQRLKPSWEKTAKIIKERydpemDGRIILGRVDCTEDgDLcRSHHIQGYPSIRIFRKGSDVRSdhghhdhESY 245
Cdd:TIGR01130 372 YAPWCGHCKNLAPIYEELAEKYKDA-----ESDVVIAKMDATAN-DV-PPFEVEGFPTIKFVPAGKKSEP-------VPY 437

                         170
                  ....*....|....*
gi 356543934  246 YGDRDTDSLVKTMEN 260
Cdd:TIGR01130 438 DGDRTLEDFSKFIAK 452
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 144-256 3.99e-09

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: 54.10  E-value: 3.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934 144 VVLTTQNFDKYAHQFLITV-VNFYAPWCYWSQRLKPSWEKTAKIIKerydpeMDGRIILGRVDCTEDgDLCRSHHIQGYP 222
Cdd:cd02995    3 KVVVGKNFDEVVLDSDKDVlVEFYAPWCGHCKALAPIYEELAEKLK------GDDNVVIAKMDATAN-DVPSEFVVDGFP 75

                         90       100       110
                 ....*....|....*....|....*....|....
gi 356543934 223 SIRIFRKGSDVRSdhghhdhESYYGDRDTDSLVK 256
Cdd:cd02995   76 TILFFPAGDKSNP-------IKYEGDRTLEDLIK 102
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 149-230 3.27e-08

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: 51.02  E-value: 3.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934 149 QNFDKYAHQFLITVVNFYAPWCYWSQRLKPSWEKTAkiikerydpEMDGRIILGRVDCTEDGDLCRSHHIQGYPSIRIFR 228
Cdd:cd02947    1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELA---------EEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFK 71


                 ..
gi 356543934 229 KG 230
Cdd:cd02947   72 NG 73
PTZ00051 PTZ00051
thioredoxin; Provisional
 145-233 1.24e-04

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 41.01  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934 145 VLTTQNFDKYAHQFLITVVNFYAPWCYWSQRLKPSWEKTAKiikeRYdpemdGRIILGRVDCTEDGDLCRSHHIQGYPSI 224
Cdd:PTZ00051   5 VTSQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSK----EY-----TKMVFVKVDVDELSEVAEKENITSMPTF 75


                 ....*....
gi 356543934 225 RIFRKGSDV 233
Cdd:PTZ00051  76 KVFKNGSVV 84
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 163-255 1.60e-04

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: 40.83  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934 163 VNFYAPWCYWSQRLKPSWEKTAKIIKerydpemDGRIILGRVDCTEDGDLCRSHHIQGYPSIR-----IFRKgsdvrsdh 237
Cdd:cd02994   21 IEFYAPWCPACQQLQPEWEEFADWSD-------DLGINVAKVDVTQEPGLSGRFFVTALPTIYhakdgVFRR-------- 85

                         90
                 ....*....|....*...
gi 356543934 238 ghhdhesYYGDRDTDSLV 255
Cdd:cd02994   86 -------YQGPRDKEDLI 96
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 146-233 1.98e-04

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: 40.35  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934  146 LTTQNFDK-YAHQFLITVVNFYAPWCYWSQRLKPSWEKTAKiikerydpEMDGRIILGRVDCTEDGDLCRSHHIQGYPSI 224
Cdd:TIGR01068   1 LTDANFDEtIASSDKPVLVDFWAPWCGPCKMIAPILEELAK--------EYEGKVKFVKLNVDENPDIAAKYGIRSIPTL 72


                  ....*....
gi 356543934  225 RIFRKGSDV 233
Cdd:TIGR01068  73 LLFKNGKEV 81
PRK10996 PRK10996
thioredoxin 2; Provisional
 141-230 2.60e-04

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 41.21  E-value: 2.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934 141 EGSVV-LTTQNFDKYAHQFLITVVNFYAPWCYWSQRLKPSWEKTAKiikerydpEMDGRIILGRVDCTEDGDLCRSHHIQ 219
Cdd:PRK10996  34 DGEVInATGETLDKLLQDDLPVVIDFWAPWCGPCRNFAPIFEDVAA--------ERSGKVRFVKVNTEAERELSARFRIR 105

                         90
                 ....*....|.
gi 356543934 220 GYPSIRIFRKG 230
Cdd:PRK10996 106 SIPTIMIFKNG 116
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 162-230 3.03e-04

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: 39.95  E-value: 3.03e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 356543934 162 VVNFYAPWCYWSQRLKPSWEKTAkiikERYDpemdGRIILGRVDCTEDGDLCRSHHIQGYPSIRIFRKG 230
Cdd:cd02956   16 VVDFWAPRSPPSKELLPLLERLA----EEYQ----GQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAG 76
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 161-256 3.90e-04

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


Pssm-ID: 239297 [Multi-domain]  Cd Length: 100  Bit Score: 39.65  E-value: 3.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356543934 161 TVVNFYAPWCYWSQRLKPSWEKTAKIIKERYDPEMDGRIILGRVdctedgdLCRsHHIQGYPSIRIFRKGSDVRsdhghh 240
Cdd:cd02999   21 TAVLFYASWCPFSASFRPHFNALSSMFPQIRHLAIEESSIKPSL-------LSR-YGVVGFPTILLFNSTPRVR------ 86

                         90
                 ....*....|....*.
gi 356543934 241 dhesYYGDRDTDSLVK 256
Cdd:cd02999   87 ----YNGTRTLDSLAA 98
Thioredoxin_7 pfam13899
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 163-229 4.52e-03

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: 36.18  E-value: 4.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 356543934  163 VNFYAPWCYWSQRLKpSWEKTAKIIKErydpEMDGRIILGRVDCTE-DGDLCRSHHIQGYPSIRIFRK 229
Cdd:pfam13899  22 VDFGADWCFTCQVLE-RDFLSHEEVKA----ALAKNFVLLRLDWTSrDANITRAFDGQGVPHIAFLDP 84
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 162-230 8.28e-03

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: 34.98  E-value: 8.28e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356543934 162 VVNFYAPWCYWSQRLKPSWEKTAKiikerydpeMDGRIILGRVDCTEDGDLCRS---HHIQGYPSIRIFRKG 230
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELAL---------LNKGVKFEAVDVDEDPALEKElkrYGVGGVPTLVVFGPG 63
 
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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