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Conserved domains on  [gi|41053774|ref|NP_957186|]
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endoplasmic reticulum resident protein 44 [Danio rerio]

Protein Classification

PDI_a_ERp44 and PDI_b'_ERp44 domain-containing protein( domain architecture ID 10122289)

protein containing domains PDI_a_ERp44, PDI_b_ERp44, and PDI_b'_ERp44

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDI_b'_ERp44 cd03072
PDIb' family, ERp44 subfamily, second redox inactive TRX-like domain b'; ERp44 is an ...
 245-355 1.59e-78

PDIb' family, ERp44 subfamily, second redox inactive TRX-like domain b'; ERp44 is an endoplasmic reticulum (ER)-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. Through the formation of reversible mixed disulfides, 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. ERp44 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. Similar to PDI, the b' domain of ERp44 is likely involved in substrate recognition and may be the primary binding site.


:

Pssm-ID: 239370  Cd Length: 111  Bit Score: 237.67  E-value: 1.59e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774 245 VREITFENGEELTEEGIPFLILFHQKDDTESLEKFQQEVARQLISEKGSINFLHADCDKFRHPLLHIQKTPADCPVIAID 324
Cdd:cd03072   1 VREITFENAEELTEEGLPFLILFHDKDDLESLKEFKQAVARQLISEKGAINFLTADGDKFRHPLLHLGKTPADLPVIAID 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 41053774 325 SFRHMYVFPEFSDLAVPGKLRQFVLDLHSGK 355
Cdd:cd03072  81 SFRHMYLFPDFEDVYVPGKLKQFVLDLHSGK 111
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 29-136 4.76e-73

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: 223.42  E-value: 4.76e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  29 GEITSLDSGNIDDILNGAGVALVNFYADWCRFSQMLHPIFEEASNIVREEYPDATQVVFGRVDCDQHSDLAQRYRISKYP 108
Cdd:cd02996   1 SEIVSLTSGNIDDILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEEFPDAGKVVWGKVDCDKESDIADRYRINKYP 80

                        90       100
                ....*....|....*....|....*...
gi 41053774 109 TLKLFRNGMMMKREYRGQRSVTAIADFI 136
Cdd:cd02996  81 TLKLFRNGMMMKREYRGQRSVEALAEFV 108
PDI_b_ERp44 cd03070
PDIb family, ERp44 subfamily, first redox inactive TRX-like domain b; ERp44 is an endoplasmic ...
 144-234 2.39e-47

PDIb family, ERp44 subfamily, first redox inactive TRX-like domain b; ERp44 is an endoplasmic reticulum (ER)-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. Through the formation of reversible mixed disulfides, 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. ERp44 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. Similar to PDI, the b domain of ERp44 is likely involved in binding to substrates.


:

Pssm-ID: 239368  Cd Length: 91  Bit Score: 156.72  E-value: 2.39e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774 144 IKEIENLEEISTVDRSRRTIIGYFEKRDSDNYRTYEKVANILRDDCAFLAAFGEVSKPERFSGDNIIYKPLGENAPDMVY 223
Cdd:cd03070   1 IKEFRNLDELNNVDRSKRNIIGYFESKDSDEYDNFRKVANILRDDCSFLVGFGDVTKPERPPGDNIIYFPPGHNAPDMVY 80

                        90
                ....*....|.
gi 41053774 224 MGSLTNFDLSY 234
Cdd:cd03070  81 LGSLTNFDLLK 91
 
Name Accession Description Interval E-value
PDI_b'_ERp44 cd03072
PDIb' family, ERp44 subfamily, second redox inactive TRX-like domain b'; ERp44 is an ...
 245-355 1.59e-78

PDIb' family, ERp44 subfamily, second redox inactive TRX-like domain b'; ERp44 is an endoplasmic reticulum (ER)-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. Through the formation of reversible mixed disulfides, 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. ERp44 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. Similar to PDI, the b' domain of ERp44 is likely involved in substrate recognition and may be the primary binding site.


Pssm-ID: 239370  Cd Length: 111  Bit Score: 237.67  E-value: 1.59e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774 245 VREITFENGEELTEEGIPFLILFHQKDDTESLEKFQQEVARQLISEKGSINFLHADCDKFRHPLLHIQKTPADCPVIAID 324
Cdd:cd03072   1 VREITFENAEELTEEGLPFLILFHDKDDLESLKEFKQAVARQLISEKGAINFLTADGDKFRHPLLHLGKTPADLPVIAID 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 41053774 325 SFRHMYVFPEFSDLAVPGKLRQFVLDLHSGK 355
Cdd:cd03072  81 SFRHMYLFPDFEDVYVPGKLKQFVLDLHSGK 111
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 29-136 4.76e-73

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: 223.42  E-value: 4.76e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  29 GEITSLDSGNIDDILNGAGVALVNFYADWCRFSQMLHPIFEEASNIVREEYPDATQVVFGRVDCDQHSDLAQRYRISKYP 108
Cdd:cd02996   1 SEIVSLTSGNIDDILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEEFPDAGKVVWGKVDCDKESDIADRYRINKYP 80

                        90       100
                ....*....|....*....|....*...
gi 41053774 109 TLKLFRNGMMMKREYRGQRSVTAIADFI 136
Cdd:cd02996  81 TLKLFRNGMMMKREYRGQRSVEALAEFV 108
PDI_b_ERp44 cd03070
PDIb family, ERp44 subfamily, first redox inactive TRX-like domain b; ERp44 is an endoplasmic ...
 144-234 2.39e-47

PDIb family, ERp44 subfamily, first redox inactive TRX-like domain b; ERp44 is an endoplasmic reticulum (ER)-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. Through the formation of reversible mixed disulfides, 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. ERp44 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. Similar to PDI, the b domain of ERp44 is likely involved in binding to substrates.


Pssm-ID: 239368  Cd Length: 91  Bit Score: 156.72  E-value: 2.39e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774 144 IKEIENLEEISTVDRSRRTIIGYFEKRDSDNYRTYEKVANILRDDCAFLAAFGEVSKPERFSGDNIIYKPLGENAPDMVY 223
Cdd:cd03070   1 IKEFRNLDELNNVDRSKRNIIGYFESKDSDEYDNFRKVANILRDDCSFLVGFGDVTKPERPPGDNIIYFPPGHNAPDMVY 80

                        90
                ....*....|.
gi 41053774 224 MGSLTNFDLSY 234
Cdd:cd03070  81 LGSLTNFDLLK 91
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
167-350 3.42e-47

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 159.45  E-value: 3.42e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774   167 FEKRDSDNYRTYEKVANILRDDCAFLAAF-GEVSKPERFSGDNII-YKPLGENAPDmvYMGSLTNFDLSYAWTQDKCVPL 244
Cdd:pfam13848   1 FEDKDSPLYEIFRKAAKELKGDVRFGITFsKEVADKYNIKEPAILlFRKFDEETVH--YPGDSINFEDLKKFIQKNCLPL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774   245 VREITFENGEELTEEGIPFLILFHQKDDTESLEKFQQEVARQLISEKGSINFLHADCDKFRHPLLHIQKTPADCPVIAI- 323
Cdd:pfam13848  79 VREFTPENAEELFEEGIPPLLLLFLKKDDESTEEFKKALEKVAKKFRGKINFALVDAKSFGRPLEYFGLSESDLPVIVIv 158

                         170       180
                  ....*....|....*....|....*..
gi 41053774   324 DSFRHMYVFPeFSDLAVPGKLRQFVLD 350
Cdd:pfam13848 159 DSFSHMYKYF-PSDEFSPESLKEFIND 184
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 30-356 8.31e-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: 150.21  E-value: 8.31e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774    30 EITSLDSGNIDDILNGAGVALVNFYADWCRFSQMLHPIFEEASNIVREEYPDatqVVFGRVDCDQHSDLAQRYRISKYPT 109
Cdd:TIGR01130   2 DVLVLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPP---IKLAKVDATEEKDLAQKYGVSGYPT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774   110 LKLFRNGMMMKREYRGQRSVTAIADFIRQQKVDPIKEIENLEEISTVDRSRR-TIIGYFEKRDSDNYRTYEKVANILRDD 188
Cdd:TIGR01130  79 LKIFRNGEDSVSDYNGPRDADGIVKYMKKQSGPAVKEIETVADLEAFLADDDvVVIGFFKDLDSELNDTFLSVAEKLRDV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774   189 CAFLAAFGEV---SKPERFSGDNIIYKPLGENAPDMVYMGSLTNF--DLSyAWTQDKCVPLVREITFENGEELTEEGiPF 263
Cdd:TIGR01130 159 YFFFAHSSDVaafAKLGAFPDSVVLFKPKDEDEKFSKVDGEMDTDvsDLE-KFIRAESLPLVGEFTQETAAKYFESG-PL 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774   264 LILFHqkDDTESLEKFQQEVAR-QLISEKGS---INFLHADCDKFRHPLLHIQKTPADCPVIAI----DSFRHMYVFPEF 335
Cdd:TIGR01130 237 VVLYY--NVDESLDPFEELRNRfLEAAKKFRgkfVNFAVADEEDFGRELEYFGLKAEKFPAVAIqdleGNKKYPMDQEEF 314

                         330       340
                  ....*....|....*....|.
gi 41053774   336 SDLAvpgkLRQFVLDLHSGKL 356
Cdd:TIGR01130 315 SSEN----LEAFVKDFLDGKL 331
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 12-370 1.80e-32

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 127.56  E-value: 1.80e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774   12 LHYFTLLLVTGLYNPGRGE-----ITSLDSGNIDDILNGAGVALVNFYADWCRFSQMLHPIFEEASNIVREEYPDatqVV 86
Cdd:PTZ00102  10 LFLLLILLAFAVFGSAEEHfisehVTVLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSE---IV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774   87 FGRVDCDQHSDLAQRYRISKYPTLKLFRNGmmMKREYRGQRSVTAIADFIRQQKVDPIKEIE-NLEEISTVDRSRRTIIG 165
Cdd:PTZ00102  87 LASVDATEEMELAQEFGVRGYPTIKFFNKG--NPVNYSGGRTADGIVSWIKKLTGPAVTEVEsASEIKLIAKKIFVAFYG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  166 YFEKRDSDNYRTYEKVANILRDDCAFLAAFGEvskperfsGDNIIYKPLGENAPDMVYMGSlTNFDLSYAWTQDKcVPLV 245
Cdd:PTZ00102 165 EYTSKDSELYKKFEEVADKHREHAKFFVKKHE--------GKNKIYVLHKDEEGVELFMGK-TKEELEEFVSTES-FPLF 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  246 REITFENGEELTEEGIpFLILF--HQKDDTESLEKFqQEVARQLiseKGSINFLHADCDKFRHPL---LHIQKTPAdcpv 320
Cdd:PTZ00102 235 AEINAENYRRYISSGK-DLVWFcgTTEDYDKYKSVV-RKVARKL---REKYAFVWLDTEQFGSHAkehLLIEEFPG---- 305

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 41053774  321 IAIDSFRHMYVFPE----FSDLAvpgKLRQFVLDLHSGKLHREFHHGPDPTDST 370
Cdd:PTZ00102 306 LAYQSPAGRYLLPPakesFDSVE---ALIEFFKDVEAGKVEKSIKSEPIPEEQD 356
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 31-138 8.88e-22

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: 89.11  E-value: 8.88e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  31 ITSLDSGNID-DILNGAGVALVNFYADWCRFSQMLHPIFEEASnivrEEYPDatQVVFGRVDCDQHSDLAQRYRISKYPT 109
Cdd:COG3118   2 VVELTDENFEeEVLESDKPVLVDFWAPWCGPCKMLAPVLEELA----AEYGG--KVKFVKVDVDENPELAAQFGVRSIPT 75

                        90       100
                ....*....|....*....|....*....
gi 41053774 110 LKLFRNGMMMKReYRGQRSVTAIADFIRQ 138
Cdd:COG3118  76 LLLFKDGQPVDR-FVGALPKEQLREFLDK 103
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 40-137 5.88e-20

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: 84.21  E-value: 5.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774    40 DDILNGAGVALVNFYADWCRFSQMLHPIFEEASNivreEYPDatQVVFGRVDCDQHSDLAQRYRISKYPTLKLFRNGMMM 119
Cdd:pfam00085  12 EVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQ----EYKG--NVVFAKVDVDENPDLASKYGVRGYPTLIFFKNGQPV 85

                          90
                  ....*....|....*...
gi 41053774   120 KrEYRGQRSVTAIADFIR 137
Cdd:pfam00085  86 D-DYVGARPKDALAAFLK 102
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 34-121 1.82e-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: 80.03  E-value: 1.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774    34 LDSGNID-DILNGAGVALVNFYADWCRFSQMLHPIFEEASnivrEEYPDatQVVFGRVDCDQHSDLAQRYRISKYPTLKL 112
Cdd:TIGR01068   1 LTDANFDeTIASSDKPVLVDFWAPWCGPCKMIAPILEELA----KEYEG--KVKFVKLNVDENPDIAAKYGIRSIPTLLL 74


                  ....*....
gi 41053774   113 FRNGMMMKR 121
Cdd:TIGR01068  75 FKNGKEVDR 83
PTZ00051 PTZ00051
thioredoxin; Provisional
 30-116 1.01e-14

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 69.52  E-value: 1.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774   30 EITSldSGNIDDILNGAGVALVNFYADWCRFSQMLHPIFEEASnivrEEYPdatQVVFGRVDCDQHSDLAQRYRISKYPT 109
Cdd:PTZ00051   4 IVTS--QAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECS----KEYT---KMVFVKVDVDELSEVAEKENITSMPT 74


                 ....*..
gi 41053774  110 LKLFRNG 116
Cdd:PTZ00051  75 FKVFKNG 81
 
Name Accession Description Interval E-value
PDI_b'_ERp44 cd03072
PDIb' family, ERp44 subfamily, second redox inactive TRX-like domain b'; ERp44 is an ...
 245-355 1.59e-78

PDIb' family, ERp44 subfamily, second redox inactive TRX-like domain b'; ERp44 is an endoplasmic reticulum (ER)-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. Through the formation of reversible mixed disulfides, 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. ERp44 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. Similar to PDI, the b' domain of ERp44 is likely involved in substrate recognition and may be the primary binding site.


Pssm-ID: 239370  Cd Length: 111  Bit Score: 237.67  E-value: 1.59e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774 245 VREITFENGEELTEEGIPFLILFHQKDDTESLEKFQQEVARQLISEKGSINFLHADCDKFRHPLLHIQKTPADCPVIAID 324
Cdd:cd03072   1 VREITFENAEELTEEGLPFLILFHDKDDLESLKEFKQAVARQLISEKGAINFLTADGDKFRHPLLHLGKTPADLPVIAID 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 41053774 325 SFRHMYVFPEFSDLAVPGKLRQFVLDLHSGK 355
Cdd:cd03072  81 SFRHMYLFPDFEDVYVPGKLKQFVLDLHSGK 111
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 29-136 4.76e-73

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: 223.42  E-value: 4.76e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  29 GEITSLDSGNIDDILNGAGVALVNFYADWCRFSQMLHPIFEEASNIVREEYPDATQVVFGRVDCDQHSDLAQRYRISKYP 108
Cdd:cd02996   1 SEIVSLTSGNIDDILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEEFPDAGKVVWGKVDCDKESDIADRYRINKYP 80

                        90       100
                ....*....|....*....|....*...
gi 41053774 109 TLKLFRNGMMMKREYRGQRSVTAIADFI 136
Cdd:cd02996  81 TLKLFRNGMMMKREYRGQRSVEALAEFV 108
PDI_b_ERp44 cd03070
PDIb family, ERp44 subfamily, first redox inactive TRX-like domain b; ERp44 is an endoplasmic ...
 144-234 2.39e-47

PDIb family, ERp44 subfamily, first redox inactive TRX-like domain b; ERp44 is an endoplasmic reticulum (ER)-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. Through the formation of reversible mixed disulfides, 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. ERp44 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. Similar to PDI, the b domain of ERp44 is likely involved in binding to substrates.


Pssm-ID: 239368  Cd Length: 91  Bit Score: 156.72  E-value: 2.39e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774 144 IKEIENLEEISTVDRSRRTIIGYFEKRDSDNYRTYEKVANILRDDCAFLAAFGEVSKPERFSGDNIIYKPLGENAPDMVY 223
Cdd:cd03070   1 IKEFRNLDELNNVDRSKRNIIGYFESKDSDEYDNFRKVANILRDDCSFLVGFGDVTKPERPPGDNIIYFPPGHNAPDMVY 80

                        90
                ....*....|.
gi 41053774 224 MGSLTNFDLSY 234
Cdd:cd03070  81 LGSLTNFDLLK 91
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
167-350 3.42e-47

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 159.45  E-value: 3.42e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774   167 FEKRDSDNYRTYEKVANILRDDCAFLAAF-GEVSKPERFSGDNII-YKPLGENAPDmvYMGSLTNFDLSYAWTQDKCVPL 244
Cdd:pfam13848   1 FEDKDSPLYEIFRKAAKELKGDVRFGITFsKEVADKYNIKEPAILlFRKFDEETVH--YPGDSINFEDLKKFIQKNCLPL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774   245 VREITFENGEELTEEGIPFLILFHQKDDTESLEKFQQEVARQLISEKGSINFLHADCDKFRHPLLHIQKTPADCPVIAI- 323
Cdd:pfam13848  79 VREFTPENAEELFEEGIPPLLLLFLKKDDESTEEFKKALEKVAKKFRGKINFALVDAKSFGRPLEYFGLSESDLPVIVIv 158

                         170       180
                  ....*....|....*....|....*..
gi 41053774   324 DSFRHMYVFPeFSDLAVPGKLRQFVLD 350
Cdd:pfam13848 159 DSFSHMYKYF-PSDEFSPESLKEFIND 184
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 30-356 8.31e-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: 150.21  E-value: 8.31e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774    30 EITSLDSGNIDDILNGAGVALVNFYADWCRFSQMLHPIFEEASNIVREEYPDatqVVFGRVDCDQHSDLAQRYRISKYPT 109
Cdd:TIGR01130   2 DVLVLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPP---IKLAKVDATEEKDLAQKYGVSGYPT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774   110 LKLFRNGMMMKREYRGQRSVTAIADFIRQQKVDPIKEIENLEEISTVDRSRR-TIIGYFEKRDSDNYRTYEKVANILRDD 188
Cdd:TIGR01130  79 LKIFRNGEDSVSDYNGPRDADGIVKYMKKQSGPAVKEIETVADLEAFLADDDvVVIGFFKDLDSELNDTFLSVAEKLRDV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774   189 CAFLAAFGEV---SKPERFSGDNIIYKPLGENAPDMVYMGSLTNF--DLSyAWTQDKCVPLVREITFENGEELTEEGiPF 263
Cdd:TIGR01130 159 YFFFAHSSDVaafAKLGAFPDSVVLFKPKDEDEKFSKVDGEMDTDvsDLE-KFIRAESLPLVGEFTQETAAKYFESG-PL 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774   264 LILFHqkDDTESLEKFQQEVAR-QLISEKGS---INFLHADCDKFRHPLLHIQKTPADCPVIAI----DSFRHMYVFPEF 335
Cdd:TIGR01130 237 VVLYY--NVDESLDPFEELRNRfLEAAKKFRgkfVNFAVADEEDFGRELEYFGLKAEKFPAVAIqdleGNKKYPMDQEEF 314

                         330       340
                  ....*....|....*....|.
gi 41053774   336 SDLAvpgkLRQFVLDLHSGKL 356
Cdd:TIGR01130 315 SSEN----LEAFVKDFLDGKL 331
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 32-136 7.27e-35

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: 124.26  E-value: 7.27e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  32 TSLDSGNIDDILNGAGVALVNFYADWCRFSQMLHPIFEEASnivrEEYPDATQVVFGRVDCDQHSDLAQRYRISKYPTLK 111
Cdd:cd02961   1 VELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLA----KELKGDGKVVVAKVDCTANNDLCSEYGVRGYPTIK 76

                        90       100
                ....*....|....*....|....*
gi 41053774 112 LFRNGMMMKREYRGQRSVTAIADFI 136
Cdd:cd02961  77 LFPNGSKEPVKYEGPRTLESLVEFI 101
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 12-370 1.80e-32

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 127.56  E-value: 1.80e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774   12 LHYFTLLLVTGLYNPGRGE-----ITSLDSGNIDDILNGAGVALVNFYADWCRFSQMLHPIFEEASNIVREEYPDatqVV 86
Cdd:PTZ00102  10 LFLLLILLAFAVFGSAEEHfisehVTVLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSE---IV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774   87 FGRVDCDQHSDLAQRYRISKYPTLKLFRNGmmMKREYRGQRSVTAIADFIRQQKVDPIKEIE-NLEEISTVDRSRRTIIG 165
Cdd:PTZ00102  87 LASVDATEEMELAQEFGVRGYPTIKFFNKG--NPVNYSGGRTADGIVSWIKKLTGPAVTEVEsASEIKLIAKKIFVAFYG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  166 YFEKRDSDNYRTYEKVANILRDDCAFLAAFGEvskperfsGDNIIYKPLGENAPDMVYMGSlTNFDLSYAWTQDKcVPLV 245
Cdd:PTZ00102 165 EYTSKDSELYKKFEEVADKHREHAKFFVKKHE--------GKNKIYVLHKDEEGVELFMGK-TKEELEEFVSTES-FPLF 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  246 REITFENGEELTEEGIpFLILF--HQKDDTESLEKFqQEVARQLiseKGSINFLHADCDKFRHPL---LHIQKTPAdcpv 320
Cdd:PTZ00102 235 AEINAENYRRYISSGK-DLVWFcgTTEDYDKYKSVV-RKVARKL---REKYAFVWLDTEQFGSHAkehLLIEEFPG---- 305

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 41053774  321 IAIDSFRHMYVFPE----FSDLAvpgKLRQFVLDLHSGKLHREFHHGPDPTDST 370
Cdd:PTZ00102 306 LAYQSPAGRYLLPPakesFDSVE---ALIEFFKDVEAGKVEKSIKSEPIPEEQD 356
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 31-136 2.17e-22

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: 91.16  E-value: 2.17e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  31 ITSLDSGNIDDILNGAGV-ALVNFYADWCRFSQMLHPIFEEASNIvreeYPDATQVVFGRVDCDQ-HSDLAQRYRISKYP 108
Cdd:cd02998   2 VVELTDSNFDKVVGDDKKdVLVEFYAPWCGHCKNLAPEYEKLAAV----FANEDDVVIAKVDADEaNKDLAKKYGVSGFP 77

                        90       100
                ....*....|....*....|....*...
gi 41053774 109 TLKLFRNGMMMKREYRGQRSVTAIADFI 136
Cdd:cd02998  78 TLKFFPKGSTEPVKYEGGRDLEDLVKFV 105
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 31-138 8.88e-22

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: 89.11  E-value: 8.88e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  31 ITSLDSGNID-DILNGAGVALVNFYADWCRFSQMLHPIFEEASnivrEEYPDatQVVFGRVDCDQHSDLAQRYRISKYPT 109
Cdd:COG3118   2 VVELTDENFEeEVLESDKPVLVDFWAPWCGPCKMLAPVLEELA----AEYGG--KVKFVKVDVDENPELAAQFGVRSIPT 75

                        90       100
                ....*....|....*....|....*....
gi 41053774 110 LKLFRNGMMMKReYRGQRSVTAIADFIRQ 138
Cdd:COG3118  76 LLLFKDGQPVDR-FVGALPKEQLREFLDK 103
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 40-137 5.88e-20

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: 84.21  E-value: 5.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774    40 DDILNGAGVALVNFYADWCRFSQMLHPIFEEASNivreEYPDatQVVFGRVDCDQHSDLAQRYRISKYPTLKLFRNGMMM 119
Cdd:pfam00085  12 EVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQ----EYKG--NVVFAKVDVDENPDLASKYGVRGYPTLIFFKNGQPV 85

                          90
                  ....*....|....*...
gi 41053774   120 KrEYRGQRSVTAIADFIR 137
Cdd:pfam00085  86 D-DYVGARPKDALAAFLK 102
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 38-136 2.53e-19

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: 82.22  E-value: 2.53e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  38 NIDDILNGAGVALVNFYADWCRFSQMLHPIFEEASnivrEEYPDatqVVFGRVDCDQHSDLAQRYRISKYPTLKLFRNGM 117
Cdd:cd02947   2 EFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELA----EEYPK---VKFVKVDVDENPELAEEYGVRSIPTFLFFKNGK 74

                        90
                ....*....|....*....
gi 41053774 118 MMKREYrGQRSVTAIADFI 136
Cdd:cd02947  75 EVDRVV-GADPKEELEEFL 92
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 34-121 1.82e-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: 80.03  E-value: 1.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774    34 LDSGNID-DILNGAGVALVNFYADWCRFSQMLHPIFEEASnivrEEYPDatQVVFGRVDCDQHSDLAQRYRISKYPTLKL 112
Cdd:TIGR01068   1 LTDANFDeTIASSDKPVLVDFWAPWCGPCKMIAPILEELA----KEYEG--KVKFVKLNVDENPDIAAKYGIRSIPTLLL 74


                  ....*....
gi 41053774   113 FRNGMMMKR 121
Cdd:TIGR01068  75 FKNGKEVDR 83
PDI_b'_family cd02982
Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of ...
 246-352 1.11e-17

Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; 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, calsequestrin and other PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5 and PDIR. PDI, ERp57, ERp72, P5 and PDIR 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 contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and one or more redox inactive TRX-like (b) domains. The molecular structure of PDI is abb'a'. Also included in this family is the PDI-related protein ERp27, which contains only redox-inactive TRX-like (b and b') domains. The redox inactive domains are implicated in substrate recognition with the b' domain serving as the primary substrate binding site. Only the b' domain is necessary for the binding of small peptide substrates. In addition to the b' domain, other domains are required for the binding of larger polypeptide substrates. The b' domain is also implicated in chaperone activity.


Pssm-ID: 239280 [Multi-domain]  Cd Length: 103  Bit Score: 78.08  E-value: 1.11e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774 246 REITFENGEELteeGIPFLILFHQKDD--TESLEKFQQEVARQLiseKGSINFLHADCDKF-RHPLLHIQKTpADCPVIA 322
Cdd:cd02982   1 NAETFFNYEES---GKPLLVLFYNKDDseSEELRERFKEVAKKF---KGKLLFVVVDADDFgRHLEYFGLKE-EDLPVIA 73

                        90       100       110
                ....*....|....*....|....*....|..
gi 41053774 323 IDSF--RHMYVFPEFSDlaVPGKLRQFVLDLH 352
Cdd:cd02982  74 IINLsdGKKYLMPEEEL--TAESLEEFVEDFL 103
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 47-136 4.86e-17

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: 76.17  E-value: 4.86e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  47 GVALVNFYADWCRFSQMLHPIFEEASNivrEEYPDATQVVFGRVDCDQHSDLAQRYRISKYPTLKLFRNGmmmKR--EYR 124
Cdd:cd03005  17 GNHFVKFFAPWCGHCKRLAPTWEQLAK---KFNNENPSVKIAKVDCTQHRELCSEFQVRGYPTLLLFKDG---EKvdKYK 90

                        90
                ....*....|..
gi 41053774 125 GQRSVTAIADFI 136
Cdd:cd03005  91 GTRDLDSLKEFV 102
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 34-135 3.46e-16

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: 73.86  E-value: 3.46e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  34 LDSGNIDD-ILNGAGVALVNFYADWCRFSQMLHPIFEEASNIVReeypdaTQVVFGRVDCDQHSDLAQRYRISKYPTLKL 112
Cdd:cd03001   5 LTDSNFDKkVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALK------GIVKVGAVDADVHQSLAQQYGVRGFPTIKV 78

                        90       100
                ....*....|....*....|...
gi 41053774 113 FRNGMMMKREYRGQRSVTAIADF 135
Cdd:cd03001  79 FGAGKNSPQDYQGGRTAKAIVSA 101
PTZ00051 PTZ00051
thioredoxin; Provisional
 30-116 1.01e-14

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 69.52  E-value: 1.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774   30 EITSldSGNIDDILNGAGVALVNFYADWCRFSQMLHPIFEEASnivrEEYPdatQVVFGRVDCDQHSDLAQRYRISKYPT 109
Cdd:PTZ00051   4 IVTS--QAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECS----KEYT---KMVFVKVDVDELSEVAEKENITSMPT 74


                 ....*..
gi 41053774  110 LKLFRNG 116
Cdd:PTZ00051  75 FKVFKNG 81
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 30-136 1.35e-14

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: 69.24  E-value: 1.35e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  30 EITSLDSGNIDD-ILNGAGVALVNFYADWCRFSQMLHPIFEEASNIVREeypdatQVVFGRVDCDQHSDLAQRYRISKYP 108
Cdd:cd03004   2 SVITLTPEDFPElVLNRKEPWLVDFYAPWCGPCQALLPELRKAARALKG------KVKVGSVDCQKYESLCQQANIRAYP 75

                        90       100
                ....*....|....*....|....*....
gi 41053774 109 TLKLFRNGMMMKREYRG-QRSVTAIADFI 136
Cdd:cd03004  76 TIRLYPGNASKYHSYNGwHRDADSILEFI 104
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 47-135 2.14e-14

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: 68.63  E-value: 2.14e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  47 GVALVNFYADWCRFSQMLHPIFEEASNIVREEypdATQVVFGRVDCDQHSDLAQRYRISKYPTLKLFRNGMMMkrEYRGQ 126
Cdd:cd03000  16 DIWLVDFYAPWCGHCKKLEPVWNEVGAELKSS---GSPVRVGKLDATAYSSIASEFGVRGYPTIKLLKGDLAY--NYRGP 90


                ....*....
gi 41053774 127 RSVTAIADF 135
Cdd:cd03000  91 RTKDDIVEF 99
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 31-136 1.45e-13

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: 66.62  E-value: 1.45e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  31 ITSLDSGNIDDILNGAG-VALVNFYADWCRFSQMLHPIFEEASNIVReeypDATQVVfgRVDCDQ--HSDLAQRYRISKY 107
Cdd:cd03002   2 VYELTPKNFDKVVHNTNyTTLVEFYAPWCGHCKNLKPEYAKAAKELD----GLVQVA--AVDCDEdkNKPLCGKYGVQGF 75

                        90       100       110
                ....*....|....*....|....*....|...
gi 41053774 108 PTLKLFRNGMMMKR----EYRGQRSVTAIADFI 136
Cdd:cd03002  76 PTLKVFRPPKKASKhaveDYNGERSAKAIVDFV 108
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 30-136 4.48e-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: 65.03  E-value: 4.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  30 EITSLDSGNIDDILNGAGVALVNFYADWCRFSQMLHPIFEEASNIVREEYPdatqVVFGRVDC--DQHSDLAQRYRISKY 107
Cdd:cd02997   1 DVVHLTDEDFRKFLKKEKHVLVMFYAPWCGHCKKMKPEFTKAATELKEDGK----GVLAAVDCtkPEHDALKEEYNVKGF 76

                        90       100
                ....*....|....*....|....*....
gi 41053774 108 PTLKLFRNGMMMkREYRGQRSVTAIADFI 136
Cdd:cd02997  77 PTFKYFENGKFV-EKYEGERTAEDIIEFM 104
PDI_b_family cd02981
Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of ...
 144-234 3.64e-12

Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; 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, calsequestrin and other PDI-related proteins like ERp72, ERp57, ERp44 and PDIR. PDI, ERp57 (or ERp60), ERp72 and PDIR 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 contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and one or more redox inactive TRX-like (b) domains. The molecular structure of PDI is abb'a'. Also included in this family is the PDI-related protein ERp27, which contains only redox-inactive TRX-like (b and b') domains. The redox inactive b domains are implicated in substrate recognition.


Pssm-ID: 239279  Cd Length: 97  Bit Score: 62.36  E-value: 3.64e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774 144 IKEIENLEEI-STVDRSRRTIIGYFEKRDSDNYRTYEKVANILRDDcaflAAFGEVSKPERFS------GDNIIYKPLGE 216
Cdd:cd02981   1 VKELTSKEELeKFLDKDDVVVVGFFKDEESEEYKTFEKVAESLRDD----YGFGHTSDKEVAKklkvkpGSVVLFKPFEE 76

                        90       100
                ....*....|....*....|.
gi 41053774 217 --NAPDMVYM-GSLTNFDLSY 234
Cdd:cd02981  77 epVEYDGEFTeESLVEFIKDN 97
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 31-139 3.28e-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: 59.97  E-value: 3.28e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  31 ITSLDSGNIDDILNGAGVA-LVNFYADWCRFSQMLHPIFEEASNIVREEYPdatQVVFGRVDC--DQHSDLAQRYRISKY 107
Cdd:cd02992   3 VIVLDAASFNSALLGSPSAwLVEFYASWCGHCRAFAPTWKKLARDLRKWRP---VVRVAAVDCadEENVALCRDFGVTGY 79

                        90       100       110
                ....*....|....*....|....*....|..
gi 41053774 108 PTLKLFRNGMMMKREYRGQRSVTAIADFIRQQ 139
Cdd:cd02992  80 PTLRYFPPFSKEATDGLKQEGPERDVNELREA 111
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 50-136 2.73e-10

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: 56.98  E-value: 2.73e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  50 LVNFYADWCRFSQMLHPIFEEASNIvreeYPdatQVVFGRVD-CDQHSDLAQRYRISKYPTLKLFRNGMMMKreYRGQRS 128
Cdd:cd02999  22 AVLFYASWCPFSASFRPHFNALSSM----FP---QIRHLAIEeSSIKPSLLSRYGVVGFPTILLFNSTPRVR--YNGTRT 92


                ....*...
gi 41053774 129 VTAIADFI 136
Cdd:cd02999  93 LDSLAAFY 100
trxA PRK09381
thioredoxin TrxA;
41-116 5.95e-10

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 56.23  E-value: 5.95e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41053774   41 DILNGAGVALVNFYADWCRFSQMLHPIFEEasniVREEYpdATQVVFGRVDCDQHSDLAQRYRISKYPTLKLFRNG 116
Cdd:PRK09381  16 DVLKADGAILVDFWAEWCGPCKMIAPILDE----IADEY--QGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNG 85
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 50-136 8.99e-10

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: 55.64  E-value: 8.99e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  50 LVNFYADWCRFSQMLHPIFEEASnivrEEYPDATQVVFGRVDCDQhSDLAQRYRISKYPTLKLFRNGMMMKR-EYRGQRS 128
Cdd:cd02995  22 LVEFYAPWCGHCKALAPIYEELA----EKLKGDDNVVIAKMDATA-NDVPSEFVVDGFPTILFFPAGDKSNPiKYEGDRT 96


                ....*...
gi 41053774 129 VTAIADFI 136
Cdd:cd02995  97 LEDLIKFI 104
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 29-136 1.04e-09

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: 55.46  E-value: 1.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  29 GEITSLDSGNIDDILNGAgvALVNFYADWCRFSQMLHPIFEEASnivreEYPDATQVVFGRVDCDQHSDLAQRYRISKYP 108
Cdd:cd02994   1 SNVVELTDSNWTLVLEGE--WMIEFYAPWCPACQQLQPEWEEFA-----DWSDDLGINVAKVDVTQEPGLSGRFFVTALP 73

                        90       100
                ....*....|....*....|....*...
gi 41053774 109 TLKLFRNGMMmkREYRGQRSVTAIADFI 136
Cdd:cd02994  74 TIYHAKDGVF--RRYQGPRDKEDLISFI 99
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 30-135 1.57e-09

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: 54.84  E-value: 1.57e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  30 EITSLDSGNIDDILNGAGVALVNFYADWCRFSQMLHPIFEEASNIVreeypDATQVVfGRVDCDQHSDLAQRYRISKYPT 109
Cdd:cd03003   2 EIVTLDRGDFDAAVNSGEIWFVNFYSPRCSHCHDLAPTWREFAKEM-----DGVIRI-GAVNCGDDRMLCRSQGVNSYPS 75

                        90       100
                ....*....|....*....|....*.
gi 41053774 110 LKLFRNGmMMKREYRGQRSVTAIADF 135
Cdd:cd03003  76 LYVFPSG-MNPEKYYGDRSKESLVKF 100
PRK10996 PRK10996
thioredoxin 2; Provisional
 29-118 2.95e-08

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 52.38  E-value: 2.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774   29 GEITSLDSGNIDDILNGAGVALVNFYADWCRFSQMLHPIFEEasniVREEypDATQVVFGRVDCDQHSDLAQRYRISKYP 108
Cdd:PRK10996  35 GEVINATGETLDKLLQDDLPVVIDFWAPWCGPCRNFAPIFED----VAAE--RSGKVRFVKVNTEAERELSARFRIRSIP 108

                         90
                 ....*....|
gi 41053774  109 TLKLFRNGMM 118
Cdd:PRK10996 109 TIMIFKNGQV 118
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 50-120 5.00e-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: 49.62  E-value: 5.00e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41053774  50 LVNFYADWCRFSQMLHPIFEEASnivrEEYPDatqVVFGRVDCDQHSDL---AQRYRISKYPTLKLFRNGMMMK 120
Cdd:cd01659   1 LVLFYAPWCPFCQALRPVLAELA----LLNKG---VKFEAVDVDEDPALekeLKRYGVGGVPTLVVFGPGIGVK 67
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 47-135 9.08e-08

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 52.32  E-value: 9.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774   47 GVALVNFYADWCRFSQMLHPIFEEASNIVReeypdaTQVVFGRVDCDQHSDLAQRYRISKYPTLKLFRNGMMMKREyRGQ 126
Cdd:PTZ00443  53 GPWFVKFYAPWCSHCRKMAPAWERLAKALK------GQVNVADLDATRALNLAKRFAIKGYPTLLLFDKGKMYQYE-GGD 125


                 ....*....
gi 41053774  127 RSVTAIADF 135
Cdd:PTZ00443 126 RSTEKLAAF 134
Calsequestrin pfam01216
Calsequestrin;
62-357 1.21e-07

Calsequestrin;


Pssm-ID: 395972 [Multi-domain]  Cd Length: 350  Bit Score: 53.10  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774    62 QMLHPIFEEASNIVREEypdatQVVFGRVDCDQHSDLAQRYRISKYPTLKLFRNGMMMkrEYRGQRSVTAIADFIRQQKV 141
Cdd:pfam01216  50 ELEEIILELAAQVLEDK-----DIGFGLVDAEKDAALAKKLGFDEEDSLYVFKGDETI--EFDGEFAADTIVEFLLDLIE 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774   142 DPIKEIENLEEISTVDRSRRTI--IGYFEKRDSDNYRTYEKVANILRDDCAFLAAFGE-VSKPERFSGDNI-IYKPLGEN 217
Cdd:pfam01216 123 DPVEIIEGELELQAFENIEDEIklIGFFKSEDSEHYKAFEDAAEEFHPYIKFFATFDKgVAKKLSLKLNEIdFYEAFMDE 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774   218 A---PDMVYM-GSLTNFdlsyawTQDKCVPLVREITFENGEELTEE---GIpFLILFHQKDDTESLEKFQ--QEVARQlI 288
Cdd:pfam01216 203 PiaiPDKPNSeEEIVEF------VEEHQRPTLRKLKPEDMFETWEDdldGI-HIVAFAEEADPDGFEFLEilKAVAQD-N 274

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41053774   289 SEKGSINFLHADCDKFrhPLL--HIQKT-------PADCPVIAIDSFRHMYVFPEFSDLAVPGKLRQFVLDLHSGKLH 357
Cdd:pfam01216 275 TDNPDLSIIWIDPDDF--PLLvaYWEKTfdidlfaPQIGVVNVTDADSVWMEIDDDDDLPSAEELEDWIEDVLEGEIN 350
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 38-147 2.07e-07

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: 52.75  E-value: 2.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774    38 NIDDILNGAG--VaLVNFYADWCRFSQMLHPIFEEASnivrEEYPDATQ-VVFGRVDCDQhSDLAQrYRISKYPTLKLFR 114
Cdd:TIGR01130 355 NFDEIVLDETkdV-LVEFYAPWCGHCKNLAPIYEELA----EKYKDAESdVVIAKMDATA-NDVPP-FEVEGFPTIKFVP 427

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 41053774   115 NGmmMKRE---YRGQRSVTAIADFIRQQKVDPIKEI 147
Cdd:TIGR01130 428 AG--KKSEpvpYDGDRTLEDFSKFIAKHATFPLEGK 461
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 50-116 5.70e-07

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: 47.27  E-value: 5.70e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41053774  50 LVNFYADWCRFSQMLHPIFEEasniVREEYPDatQVVFGRVDCDQHSDLAQRYRISKYPTLKLFRNG 116
Cdd:cd02956  16 VVDFWAPRSPPSKELLPLLER----LAEEYQG--QFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAG 76
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 48-121 7.24e-07

TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT contains an N-terminal TRX-like domain, which does not contain the catalytic CXXC motif, followed by one to three glutaredoxin domains. The TRX-like domain is required for interaction with PKC theta. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli.


Pssm-ID: 239282 [Multi-domain]  Cd Length: 97  Bit Score: 47.27  E-value: 7.24e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41053774  48 VALVNFYADWCRFSQMLHPIFEEASNivrEEYPdatQVVFGRVDCDQHSDLAQRYRISKYPTLKLFRNGMMMKR 121
Cdd:cd02984  16 LLVLHFWAPWAEPCKQMNQVFEELAK---EAFP---SVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTIVDR 83
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 48-138 3.65e-06

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 46.22  E-value: 3.65e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  48 VALVNFYADWCRFSQMLHPIFEEasniVREEYPDAtQVVF--------------------GRVDCDQHSDLAQRYRISKY 107
Cdd:COG0526  30 PVLVNFWATWCPPCRAEMPVLKE----LAEEYGGV-VFVGvdvdenpeavkaflkelglpYPVLLDPDGELAKAYGVRGI 104

                        90       100       110
                ....*....|....*....|....*....|..
gi 41053774 108 PTLKLF-RNGMMMKReYRGQRSVTAIADFIRQ 138
Cdd:COG0526 105 PTTVLIdKDGKIVAR-HVGPLSPEELEEALEK 135
HyaE pfam07449
Hydrogenase-1 expression protein HyaE; This family contains bacterial hydrogenase-1 expression ...
 34-125 5.46e-05

Hydrogenase-1 expression protein HyaE; This family contains bacterial hydrogenase-1 expression proteins approximately 120 residues long. This includes the E. coli protein HyaE, and the homologous proteins HoxO of R. eutropha and HupG of R. leguminosarum. Deletion of the hoxO gene in R. eutropha led to complete loss of the uptake [NiFe] hydrogenase activity, suggesting that it has a critical role in hydrogenase assembly.


Pssm-ID: 400018  Cd Length: 108  Bit Score: 42.04  E-value: 5.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774    34 LDSGNIDDILNGAGVALVNFYADWCRFSqmlhpifEEASNIV-----REEYPDAT-QVVFGrvDCDQHSDLAQRYRISKY 107
Cdd:pfam07449  14 VDASTLDDWLTAGGDGVLLLAGDPNRFP-------EVSDVAVvlpelLRAFPNAFrQAVVA--DREQEEALGDRFGVLRF 84

                          90
                  ....*....|....*...
gi 41053774   108 PTLKLFRNGmmmkrEYRG 125
Cdd:pfam07449  85 PALLFFRDG-----DFVG 97
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 50-115 9.85e-05

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


Pssm-ID: 239248 [Multi-domain]  Cd Length: 142  Bit Score: 41.94  E-value: 9.85e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41053774  50 LVNFYADWCRFSQMLHPIFEEasniVREEYPDATQVVFGRVDCDQHSDLAQRYRISKYPTLKLFRN 115
Cdd:cd02950  24 LVEFYADWCTVCQEMAPDVAK----LKQKYGDQVNFVMLNVDNPKWLPEIDRYRVDGIPHFVFLDR 85
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 50-146 1.27e-04

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 43.97  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774   50 LVNFYADWCRFSQMLHPIFEEASnivrEEYPDATQVVFGRVDCDQHSDLAQRYRISKYPTLKLFRNGMMMKREYRGQRSV 129
Cdd:PTZ00102 379 LLEIYAPWCGHCKNLEPVYNELG----EKYKDNDSIIVAKMNGTANETPLEEFSWSAFPTILFVKAGERTPIPYEGERTV 454

                         90
                 ....*....|....*..
gi 41053774  130 TAIADFIRQQKVDPIKE 146
Cdd:PTZ00102 455 EGFKEFVNKHATNPFED 471
PDI_b_family cd02981
Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of ...
 30-137 2.03e-04

Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; 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, calsequestrin and other PDI-related proteins like ERp72, ERp57, ERp44 and PDIR. PDI, ERp57 (or ERp60), ERp72 and PDIR 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 contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and one or more redox inactive TRX-like (b) domains. The molecular structure of PDI is abb'a'. Also included in this family is the PDI-related protein ERp27, which contains only redox-inactive TRX-like (b and b') domains. The redox inactive b domains are implicated in substrate recognition.


Pssm-ID: 239279  Cd Length: 97  Bit Score: 40.01  E-value: 2.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  30 EITSLDSgnIDDILNGAGVALVNFYADwcrFSQMLHPIFEEASNIVREEYPdatqvvFGRVDcdqHSDLAQRYRISKyPT 109
Cdd:cd02981   3 ELTSKEE--LEKFLDKDDVVVVGFFKD---EESEEYKTFEKVAESLRDDYG------FGHTS---DKEVAKKLKVKP-GS 67

                        90       100
                ....*....|....*....|....*...
gi 41053774 110 LKLFRNGMMMKREYRGQRSVTAIADFIR 137
Cdd:cd02981  68 VVLFKPFEEEPVEYDGEFTEESLVEFIK 95
TMX2 cd02962
TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related ...
 14-116 9.13e-04

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


Pssm-ID: 239260 [Multi-domain]  Cd Length: 152  Bit Score: 39.67  E-value: 9.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  14 YFTLLLVTGLYNP-----GRGEITSLDSGNIDDIL--NGAGVALVNFYADWCRFSQMLHPIFEEASNIvreeYpDATQVV 86
Cdd:cd02962   8 YLLLCIVVYLLAPqplymGPEHIKYFTPKTLEEELerDKRVTWLVEFFTTWSPECVNFAPVFAELSLK----Y-NNNNLK 82

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 41053774  87 FGRVDCDQHSDLAQRYRIS------KYPTLKLFRNG 116
Cdd:cd02962  83 FGKIDIGRFPNVAEKFRVStsplskQLPTIILFQGG 118
PLN02309 PLN02309
5'-adenylylsulfate reductase
 20-113 1.87e-03

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 40.16  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774   20 VTGLYNpgRGEITSLDSGNIDDIL---NGAGVALVNFYADWCRFSQMLHPIFEEASnivreEYPDATQVVFG--RVDCDQ 94
Cdd:PLN02309 338 VADIFN--SQNVVALSRAGIENLLkleNRKEPWLVVLYAPWCPFCQAMEASYEELA-----EKLAGSGVKVAkfRADGDQ 410

                         90
                 ....*....|....*....
gi 41053774   95 HSDLAQRYRISKYPTLKLF 113
Cdd:PLN02309 411 KEFAKQELQLGSFPTILLF 429
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
44-113 2.53e-03

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 37.02  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774    44 NGAGVALVnFYADWCRFSQMLHP----------IFEEASNIVREEYPDATQVVFGRVDCDQHSDLAQRYRISKYPTLKLF 113
Cdd:pfam13098   3 NGKPVLVV-FTDPDCPYCKKLKKelledpdvtvYLGPNFVFIAVNIWCAKEVAKAFTDILENKELGRKYGVRGTPTIVFF 81
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 50-124 3.32e-03

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: 36.71  E-value: 3.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053774  50 LVNFYADWCRFSQMLHPIFeeasNIVREEYPDATQVVfgRVDCDQHSDLAQRYRISKYPTLKLFRN--------GMMMKR 121
Cdd:cd02949  17 LVLYTSPTCGPCRTLKPIL----NKVIDEFDGAVHFV--EIDIDEDQEIAEAAGIMGTPTVQFFKDkelvkeisGVKMKS 90


                ...
gi 41053774 122 EYR 124
Cdd:cd02949  91 EYR 93
 
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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