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Conserved domains on  [gi|52487191|ref|NP_055866|]
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endoplasmic reticulum resident protein 44 precursor [Homo sapiens]

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 2.04e-77

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: 234.97  E-value: 2.04e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191 245 VREITFENGEELTEEGLPFLILFHMKEDTESLEIFQNEVARQLISEKGTINFLHADCDKFRHPLLHIQKTPADCPVIAID 324
Cdd:cd03072   1 VREITFENAEELTEEGLPFLILFHDKDDLESLKEFKQAVARQLISEKGAINFLTADGDKFRHPLLHLGKTPADLPVIAID 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 52487191 325 SFRHMYVFGDFKDVLIPGKLKQFVFDLHSGK 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 1.53e-72

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: 222.27  E-value: 1.53e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  29 TEITSLDTENIDEILNNADVALVNFYADWCRFSQMLHPIFEEASDVIKEEFPNENQVVFARVDCDQHSDIAQRYRISKYP 108
Cdd:cd02996   1 SEIVSLTSGNIDDILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEEFPDAGKVVWGKVDCDKESDIADRYRINKYP 80

                        90       100
                ....*....|....*....|....*...
gi 52487191 109 TLKLFRNGMMMKREYRGQRSVKALADYI 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 1.03e-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: 157.49  E-value: 1.03e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191 144 IQEIRDLAEITTLDRSKRNIIGYFEQKDSDNYRVFERVANILHDDCAFLSAFGDVSKPERYSGDNIIYKPPGHSAPDMVY 223
Cdd:cd03070   1 IKEFRNLDELNNVDRSKRNIIGYFESKDSDEYDNFRKVANILRDDCSFLVGFGDVTKPERPPGDNIIYFPPGHNAPDMVY 80

                        90
                ....*....|.
gi 52487191 224 LGAMTNFDVTY 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 2.04e-77

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: 234.97  E-value: 2.04e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191 245 VREITFENGEELTEEGLPFLILFHMKEDTESLEIFQNEVARQLISEKGTINFLHADCDKFRHPLLHIQKTPADCPVIAID 324
Cdd:cd03072   1 VREITFENAEELTEEGLPFLILFHDKDDLESLKEFKQAVARQLISEKGAINFLTADGDKFRHPLLHLGKTPADLPVIAID 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 52487191 325 SFRHMYVFGDFKDVLIPGKLKQFVFDLHSGK 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 1.53e-72

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: 222.27  E-value: 1.53e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  29 TEITSLDTENIDEILNNADVALVNFYADWCRFSQMLHPIFEEASDVIKEEFPNENQVVFARVDCDQHSDIAQRYRISKYP 108
Cdd:cd02996   1 SEIVSLTSGNIDDILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEEFPDAGKVVWGKVDCDKESDIADRYRINKYP 80

                        90       100
                ....*....|....*....|....*...
gi 52487191 109 TLKLFRNGMMMKREYRGQRSVKALADYI 136
Cdd:cd02996  81 TLKLFRNGMMMKREYRGQRSVEALAEFV 108
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
167-350 9.15e-51

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 168.69  E-value: 9.15e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191   167 FEQKDSDNYRVFERVANILHDDCAFLSAF-GDVSKPERYSGDNII-YKPPGHSAPDmvYLGAMTNFDVTYNWIQDKCVPL 244
Cdd:pfam13848   1 FEDKDSPLYEIFRKAAKELKGDVRFGITFsKEVADKYNIKEPAILlFRKFDEETVH--YPGDSINFEDLKKFIQKNCLPL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191   245 VREITFENGEELTEEGLPFLILFHMKEDTESLEIFQNEVARQLISEKGTINFLHADCDKFRHPLLHIQKTPADCPVIAI- 323
Cdd:pfam13848  79 VREFTPENAEELFEEGIPPLLLLFLKKDDESTEEFKKALEKVAKKFRGKINFALVDAKSFGRPLEYFGLSESDLPVIVIv 158

                         170       180
                  ....*....|....*....|....*..
gi 52487191   324 DSFRHMYVFGdFKDVLIPGKLKQFVFD 350
Cdd:pfam13848 159 DSFSHMYKYF-PSDEFSPESLKEFIND 184
PDI_b_ERp44 cd03070
PDIb family, ERp44 subfamily, first redox inactive TRX-like domain b; ERp44 is an endoplasmic ...
 144-234 1.03e-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: 157.49  E-value: 1.03e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191 144 IQEIRDLAEITTLDRSKRNIIGYFEQKDSDNYRVFERVANILHDDCAFLSAFGDVSKPERYSGDNIIYKPPGHSAPDMVY 223
Cdd:cd03070   1 IKEFRNLDELNNVDRSKRNIIGYFESKDSDEYDNFRKVANILRDDCSFLVGFGDVTKPERPPGDNIIYFPPGHNAPDMVY 80

                        90
                ....*....|.
gi 52487191 224 LGAMTNFDVTY 234
Cdd:cd03070  81 LGSLTNFDLLK 91
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 30-356 7.90e-42

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: 153.29  E-value: 7.90e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191    30 EITSLDTENIDEILNNADVALVNFYADWCRFSQMLHPIFEEASDVIKEEFPNenqVVFARVDCDQHSDIAQRYRISKYPT 109
Cdd:TIGR01130   2 DVLVLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPP---IKLAKVDATEEKDLAQKYGVSGYPT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191   110 LKLFRNGMMMKREYRGQRSVKALADYIRQQKSDPIQEIRDLAEITTLDRSKRN-IIGYFEQKDSDNYRVFERVANILHDD 188
Cdd:TIGR01130  79 LKIFRNGEDSVSDYNGPRDADGIVKYMKKQSGPAVKEIETVADLEAFLADDDVvVIGFFKDLDSELNDTFLSVAEKLRDV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191   189 CAFLSAFGDVSKPERY---SGDNIIYKPPGHSAPDMVYLGAMTNFDVTY-NWIQDKCVPLVREITFENGEELTEEG-LPF 263
Cdd:TIGR01130 159 YFFFAHSSDVAAFAKLgafPDSVVLFKPKDEDEKFSKVDGEMDTDVSDLeKFIRAESLPLVGEFTQETAAKYFESGpLVV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191   264 LILFHMKEDTESLEI---FQnEVARQliSEKGTINFLHADCDKFRHPLLHIQKTPADCPVIAIDSFRHM--YVFGDFKDV 338
Cdd:TIGR01130 239 LYYNVDESLDPFEELrnrFL-EAAKK--FRGKFVNFAVADEEDFGRELEYFGLKAEKFPAVAIQDLEGNkkYPMDQEEFS 315

                         330
                  ....*....|....*...
gi 52487191   339 liPGKLKQFVFDLHSGKL 356
Cdd:TIGR01130 316 --SENLEAFVKDFLDGKL 331
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 9-368 1.00e-32

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 128.33  E-value: 1.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191    9 LPDLRCSLLLLVTWVFT-----PVTTEITSLDTENIDEILNNADVALVNFYADWCRFSQMLHPIFEEASDVIKEEFPnen 83
Cdd:PTZ00102   7 LSSLFLLLILLAFAVFGsaeehFISEHVTVLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKS--- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191   84 QVVFARVDCDQHSDIAQRYRISKYPTLKLFRNGmmMKREYRGQRSVKALADYIRQQKSDPIQEIRDLAEIT-TLDRSKRN 162
Cdd:PTZ00102  84 EIVLASVDATEEMELAQEFGVRGYPTIKFFNKG--NPVNYSGGRTADGIVSWIKKLTGPAVTEVESASEIKlIAKKIFVA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  163 IIGYFEQKDSDNYRVFERVANILHDDCAFLSAFGdvskperySGDNIIYKPpgHSAPDMVYLGAMTNFDVTYNWIQDKCV 242
Cdd:PTZ00102 162 FYGEYTSKDSELYKKFEEVADKHREHAKFFVKKH--------EGKNKIYVL--HKDEEGVELFMGKTKEELEEFVSTESF 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  243 PLVREITFENGEELTEEGLPFLILFHMKEDTESLEIFQNEVARQLiseKGTINFLHADCDKFRHPL---LHIQKTPAdcp 319
Cdd:PTZ00102 232 PLFAEINAENYRRYISSGKDLVWFCGTTEDYDKYKSVVRKVARKL---REKYAFVWLDTEQFGSHAkehLLIEEFPG--- 305

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 52487191  320 vIAIDSFRHMYVFG----DFKDVlipGKLKQFVFDLHSGKLHREFHHGPDPTD 368
Cdd:PTZ00102 306 -LAYQSPAGRYLLPpakeSFDSV---EALIEFFKDVEAGKVEKSIKSEPIPEE 354
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 31-138 4.33e-21

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: 87.18  E-value: 4.33e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  31 ITSLDTENIDE-ILNNADVALVNFYADWCRFSQMLHPIFEEASdvikEEFpnENQVVFARVDCDQHSDIAQRYRISKYPT 109
Cdd:COG3118   2 VVELTDENFEEeVLESDKPVLVDFWAPWCGPCKMLAPVLEELA----AEY--GGKVKFVKVDVDENPELAAQFGVRSIPT 75

                        90       100
                ....*....|....*....|....*....
gi 52487191 110 LKLFRNGMMMKReYRGQRSVKALADYIRQ 138
Cdd:COG3118  76 LLLFKDGQPVDR-FVGALPKEQLREFLDK 103
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 30-137 1.64e-19

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: 83.05  E-value: 1.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191    30 EITSLDTENIDEILNNAD-VALVNFYADWCRFSQMLHPIFEEASDVIKeefpneNQVVFARVDCDQHSDIAQRYRISKYP 108
Cdd:pfam00085   1 VVVVLTDANFDEVVQKSSkPVLVDFYAPWCGPCKMLAPEYEELAQEYK------GNVVFAKVDVDENPDLASKYGVRGYP 74

                          90       100
                  ....*....|....*....|....*....
gi 52487191   109 TLKLFRNGMMMKrEYRGQRSVKALADYIR 137
Cdd:pfam00085  75 TLIFFKNGQPVD-DYVGARPKDALAAFLK 102
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 34-121 1.04e-17

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: 77.71  E-value: 1.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191    34 LDTENIDEILNNAD-VALVNFYADWCRFSQMLHPIFEEASdviKEEfpnENQVVFARVDCDQHSDIAQRYRISKYPTLKL 112
Cdd:TIGR01068   1 LTDANFDETIASSDkPVLVDFWAPWCGPCKMIAPILEELA---KEY---EGKVKFVKLNVDENPDIAAKYGIRSIPTLLL 74


                  ....*....
gi 52487191   113 FRNGMMMKR 121
Cdd:TIGR01068  75 FKNGKEVDR 83
PTZ00051 PTZ00051
thioredoxin; Provisional
 30-116 8.25e-15

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 69.52  E-value: 8.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191   30 EITSldTENIDEILNNADVALVNFYADWCRFSQMLHPIFEEASdvikEEFPNenqVVFARVDCDQHSDIAQRYRISKYPT 109
Cdd:PTZ00051   4 IVTS--QAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECS----KEYTK---MVFVKVDVDELSEVAEKENITSMPT 74


                 ....*..
gi 52487191  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 2.04e-77

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: 234.97  E-value: 2.04e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191 245 VREITFENGEELTEEGLPFLILFHMKEDTESLEIFQNEVARQLISEKGTINFLHADCDKFRHPLLHIQKTPADCPVIAID 324
Cdd:cd03072   1 VREITFENAEELTEEGLPFLILFHDKDDLESLKEFKQAVARQLISEKGAINFLTADGDKFRHPLLHLGKTPADLPVIAID 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 52487191 325 SFRHMYVFGDFKDVLIPGKLKQFVFDLHSGK 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 1.53e-72

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: 222.27  E-value: 1.53e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  29 TEITSLDTENIDEILNNADVALVNFYADWCRFSQMLHPIFEEASDVIKEEFPNENQVVFARVDCDQHSDIAQRYRISKYP 108
Cdd:cd02996   1 SEIVSLTSGNIDDILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEEFPDAGKVVWGKVDCDKESDIADRYRINKYP 80

                        90       100
                ....*....|....*....|....*...
gi 52487191 109 TLKLFRNGMMMKREYRGQRSVKALADYI 136
Cdd:cd02996  81 TLKLFRNGMMMKREYRGQRSVEALAEFV 108
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
167-350 9.15e-51

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 168.69  E-value: 9.15e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191   167 FEQKDSDNYRVFERVANILHDDCAFLSAF-GDVSKPERYSGDNII-YKPPGHSAPDmvYLGAMTNFDVTYNWIQDKCVPL 244
Cdd:pfam13848   1 FEDKDSPLYEIFRKAAKELKGDVRFGITFsKEVADKYNIKEPAILlFRKFDEETVH--YPGDSINFEDLKKFIQKNCLPL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191   245 VREITFENGEELTEEGLPFLILFHMKEDTESLEIFQNEVARQLISEKGTINFLHADCDKFRHPLLHIQKTPADCPVIAI- 323
Cdd:pfam13848  79 VREFTPENAEELFEEGIPPLLLLFLKKDDESTEEFKKALEKVAKKFRGKINFALVDAKSFGRPLEYFGLSESDLPVIVIv 158

                         170       180
                  ....*....|....*....|....*..
gi 52487191   324 DSFRHMYVFGdFKDVLIPGKLKQFVFD 350
Cdd:pfam13848 159 DSFSHMYKYF-PSDEFSPESLKEFIND 184
PDI_b_ERp44 cd03070
PDIb family, ERp44 subfamily, first redox inactive TRX-like domain b; ERp44 is an endoplasmic ...
 144-234 1.03e-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: 157.49  E-value: 1.03e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191 144 IQEIRDLAEITTLDRSKRNIIGYFEQKDSDNYRVFERVANILHDDCAFLSAFGDVSKPERYSGDNIIYKPPGHSAPDMVY 223
Cdd:cd03070   1 IKEFRNLDELNNVDRSKRNIIGYFESKDSDEYDNFRKVANILRDDCSFLVGFGDVTKPERPPGDNIIYFPPGHNAPDMVY 80

                        90
                ....*....|.
gi 52487191 224 LGAMTNFDVTY 234
Cdd:cd03070  81 LGSLTNFDLLK 91
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 30-356 7.90e-42

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: 153.29  E-value: 7.90e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191    30 EITSLDTENIDEILNNADVALVNFYADWCRFSQMLHPIFEEASDVIKEEFPNenqVVFARVDCDQHSDIAQRYRISKYPT 109
Cdd:TIGR01130   2 DVLVLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPP---IKLAKVDATEEKDLAQKYGVSGYPT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191   110 LKLFRNGMMMKREYRGQRSVKALADYIRQQKSDPIQEIRDLAEITTLDRSKRN-IIGYFEQKDSDNYRVFERVANILHDD 188
Cdd:TIGR01130  79 LKIFRNGEDSVSDYNGPRDADGIVKYMKKQSGPAVKEIETVADLEAFLADDDVvVIGFFKDLDSELNDTFLSVAEKLRDV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191   189 CAFLSAFGDVSKPERY---SGDNIIYKPPGHSAPDMVYLGAMTNFDVTY-NWIQDKCVPLVREITFENGEELTEEG-LPF 263
Cdd:TIGR01130 159 YFFFAHSSDVAAFAKLgafPDSVVLFKPKDEDEKFSKVDGEMDTDVSDLeKFIRAESLPLVGEFTQETAAKYFESGpLVV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191   264 LILFHMKEDTESLEI---FQnEVARQliSEKGTINFLHADCDKFRHPLLHIQKTPADCPVIAIDSFRHM--YVFGDFKDV 338
Cdd:TIGR01130 239 LYYNVDESLDPFEELrnrFL-EAAKK--FRGKFVNFAVADEEDFGRELEYFGLKAEKFPAVAIQDLEGNkkYPMDQEEFS 315

                         330
                  ....*....|....*...
gi 52487191   339 liPGKLKQFVFDLHSGKL 356
Cdd:TIGR01130 316 --SENLEAFVKDFLDGKL 331
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 32-136 8.90e-36

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: 126.57  E-value: 8.90e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  32 TSLDTENIDEILNNADVALVNFYADWCRFSQMLHPIFEEASdvikEEFPNENQVVFARVDCDQHSDIAQRYRISKYPTLK 111
Cdd:cd02961   1 VELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLA----KELKGDGKVVVAKVDCTANNDLCSEYGVRGYPTIK 76

                        90       100
                ....*....|....*....|....*
gi 52487191 112 LFRNGMMMKREYRGQRSVKALADYI 136
Cdd:cd02961  77 LFPNGSKEPVKYEGPRTLESLVEFI 101
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 9-368 1.00e-32

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 128.33  E-value: 1.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191    9 LPDLRCSLLLLVTWVFT-----PVTTEITSLDTENIDEILNNADVALVNFYADWCRFSQMLHPIFEEASDVIKEEFPnen 83
Cdd:PTZ00102   7 LSSLFLLLILLAFAVFGsaeehFISEHVTVLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKS--- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191   84 QVVFARVDCDQHSDIAQRYRISKYPTLKLFRNGmmMKREYRGQRSVKALADYIRQQKSDPIQEIRDLAEIT-TLDRSKRN 162
Cdd:PTZ00102  84 EIVLASVDATEEMELAQEFGVRGYPTIKFFNKG--NPVNYSGGRTADGIVSWIKKLTGPAVTEVESASEIKlIAKKIFVA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  163 IIGYFEQKDSDNYRVFERVANILHDDCAFLSAFGdvskperySGDNIIYKPpgHSAPDMVYLGAMTNFDVTYNWIQDKCV 242
Cdd:PTZ00102 162 FYGEYTSKDSELYKKFEEVADKHREHAKFFVKKH--------EGKNKIYVL--HKDEEGVELFMGKTKEELEEFVSTESF 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  243 PLVREITFENGEELTEEGLPFLILFHMKEDTESLEIFQNEVARQLiseKGTINFLHADCDKFRHPL---LHIQKTPAdcp 319
Cdd:PTZ00102 232 PLFAEINAENYRRYISSGKDLVWFCGTTEDYDKYKSVVRKVARKL---REKYAFVWLDTEQFGSHAkehLLIEEFPG--- 305

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 52487191  320 vIAIDSFRHMYVFG----DFKDVlipGKLKQFVFDLHSGKLHREFHHGPDPTD 368
Cdd:PTZ00102 306 -LAYQSPAGRYLLPpakeSFDSV---EALIEFFKDVEAGKVEKSIKSEPIPEE 354
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 31-136 1.30e-25

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: 99.63  E-value: 1.30e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  31 ITSLDTENIDEILNN-ADVALVNFYADWCRFSQMLHPIFEEASDVikeeFPNENQVVFARVDCDQ-HSDIAQRYRISKYP 108
Cdd:cd02998   2 VVELTDSNFDKVVGDdKKDVLVEFYAPWCGHCKNLAPEYEKLAAV----FANEDDVVIAKVDADEaNKDLAKKYGVSGFP 77

                        90       100
                ....*....|....*....|....*...
gi 52487191 109 TLKLFRNGMMMKREYRGQRSVKALADYI 136
Cdd:cd02998  78 TLKFFPKGSTEPVKYEGGRDLEDLVKFV 105
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 31-138 4.33e-21

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: 87.18  E-value: 4.33e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  31 ITSLDTENIDE-ILNNADVALVNFYADWCRFSQMLHPIFEEASdvikEEFpnENQVVFARVDCDQHSDIAQRYRISKYPT 109
Cdd:COG3118   2 VVELTDENFEEeVLESDKPVLVDFWAPWCGPCKMLAPVLEELA----AEY--GGKVKFVKVDVDENPELAAQFGVRSIPT 75

                        90       100
                ....*....|....*....|....*....
gi 52487191 110 LKLFRNGMMMKReYRGQRSVKALADYIRQ 138
Cdd:COG3118  76 LLLFKDGQPVDR-FVGALPKEQLREFLDK 103
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 37-136 1.38e-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: 82.99  E-value: 1.38e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  37 ENIDEILNNADVALVNFYADWCRFSQMLHPIFEEASdvikEEFPNenqVVFARVDCDQHSDIAQRYRISKYPTLKLFRNG 116
Cdd:cd02947   1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELA----EEYPK---VKFVKVDVDENPELAEEYGVRSIPTFLFFKNG 73

                        90       100
                ....*....|....*....|
gi 52487191 117 MMMKREYrGQRSVKALADYI 136
Cdd:cd02947  74 KEVDRVV-GADPKEELEEFL 92
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 30-137 1.64e-19

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: 83.05  E-value: 1.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191    30 EITSLDTENIDEILNNAD-VALVNFYADWCRFSQMLHPIFEEASDVIKeefpneNQVVFARVDCDQHSDIAQRYRISKYP 108
Cdd:pfam00085   1 VVVVLTDANFDEVVQKSSkPVLVDFYAPWCGPCKMLAPEYEELAQEYK------GNVVFAKVDVDENPDLASKYGVRGYP 74

                          90       100
                  ....*....|....*....|....*....
gi 52487191   109 TLKLFRNGMMMKrEYRGQRSVKALADYIR 137
Cdd:pfam00085  75 TLIFFKNGQPVD-DYVGARPKDALAAFLK 102
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 33-136 2.08e-18

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: 80.02  E-value: 2.08e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  33 SLDTENIDEILNNAdVALVNFYADWCRFSQMLHPIFEEASdviKEEFPNENQVVFARVDCDQHSDIAQRYRISKYPTLKL 112
Cdd:cd03005   4 ELTEDNFDHHIAEG-NHFVKFFAPWCGHCKRLAPTWEQLA---KKFNNENPSVKIAKVDCTQHRELCSEFQVRGYPTLLL 79

                        90       100
                ....*....|....*....|....*.
gi 52487191 113 FRNGmmmKR--EYRGQRSVKALADYI 136
Cdd:cd03005  80 FKDG---EKvdKYKGTRDLDSLKEFV 102
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 34-121 1.04e-17

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: 77.71  E-value: 1.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191    34 LDTENIDEILNNAD-VALVNFYADWCRFSQMLHPIFEEASdviKEEfpnENQVVFARVDCDQHSDIAQRYRISKYPTLKL 112
Cdd:TIGR01068   1 LTDANFDETIASSDkPVLVDFWAPWCGPCKMIAPILEELA---KEY---EGKVKFVKLNVDENPDIAAKYGIRSIPTLLL 74


                  ....*....
gi 52487191   113 FRNGMMMKR 121
Cdd:TIGR01068  75 FKNGKEVDR 83
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 40-134 1.48e-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: 74.63  E-value: 1.48e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  40 DEILNNADVALVNFYADWCRFSQMLHPIFEEASDVIKeefpneNQVVFARVDCDQHSDIAQRYRISKYPTLKLFRNGMMM 119
Cdd:cd03001  12 KKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALK------GIVKVGAVDADVHQSLAQQYGVRGFPTIKVFGAGKNS 85

                        90
                ....*....|....*
gi 52487191 120 KREYRGQRSVKALAD 134
Cdd:cd03001  86 PQDYQGGRTAKAIVS 100
PDI_b'_family cd02982
Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of ...
 246-352 1.62e-16

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: 74.62  E-value: 1.62e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191 246 REITFENGEELteeGLPFLILFHMKEDTESLEI--FQNEVARQLiseKGTINFLHADCDKF-RHPLLHIQKTpADCPVIA 322
Cdd:cd02982   1 NAETFFNYEES---GKPLLVLFYNKDDSESEELreRFKEVAKKF---KGKLLFVVVDADDFgRHLEYFGLKE-EDLPVIA 73

                        90       100       110
                ....*....|....*....|....*....|..
gi 52487191 323 IDSF--RHMYVFGDFKdvLIPGKLKQFVFDLH 352
Cdd:cd02982  74 IINLsdGKKYLMPEEE--LTAESLEEFVEDFL 103
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 30-136 3.22e-16

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: 73.89  E-value: 3.22e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  30 EITSLDTENIDEILNNADVALVNFYADWCRFSQMLHPIFEEASDVIKEEFPnenqVVFARVDC--DQHSDIAQRYRISKY 107
Cdd:cd02997   1 DVVHLTDEDFRKFLKKEKHVLVMFYAPWCGHCKKMKPEFTKAATELKEDGK----GVLAAVDCtkPEHDALKEEYNVKGF 76

                        90       100
                ....*....|....*....|....*....
gi 52487191 108 PTLKLFRNGMMMkREYRGQRSVKALADYI 136
Cdd:cd02997  77 PTFKYFENGKFV-EKYEGERTAEDIIEFM 104
PTZ00051 PTZ00051
thioredoxin; Provisional
 30-116 8.25e-15

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 69.52  E-value: 8.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191   30 EITSldTENIDEILNNADVALVNFYADWCRFSQMLHPIFEEASdvikEEFPNenqVVFARVDCDQHSDIAQRYRISKYPT 109
Cdd:PTZ00051   4 IVTS--QAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECS----KEYTK---MVFVKVDVDELSEVAEKENITSMPT 74


                 ....*..
gi 52487191  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 ...
 29-136 1.49e-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: 1.49e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  29 TEITSLDTENIDE-ILNNADVALVNFYADWCRFSQMLHPIFEEASDVIKEefpnenQVVFARVDCDQHSDIAQRYRISKY 107
Cdd:cd03004   1 PSVITLTPEDFPElVLNRKEPWLVDFYAPWCGPCQALLPELRKAARALKG------KVKVGSVDCQKYESLCQQANIRAY 74

                        90       100       110
                ....*....|....*....|....*....|
gi 52487191 108 PTLKLFRNGMMMKREYRG-QRSVKALADYI 136
Cdd:cd03004  75 PTIRLYPGNASKYHSYNGwHRDADSILEFI 104
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 31-136 1.59e-14

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: 69.31  E-value: 1.59e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  31 ITSLDTENID-EILNNADVALVNFYADWCRFSQMLHPIFEEASDVIKEEFPnenqvvFARVDCDQ--HSDIAQRYRISKY 107
Cdd:cd03002   2 VYELTPKNFDkVVHNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKELDGLVQ------VAAVDCDEdkNKPLCGKYGVQGF 75

                        90       100       110
                ....*....|....*....|....*....|...
gi 52487191 108 PTLKLFRNGMMMKR----EYRGQRSVKALADYI 136
Cdd:cd03002  76 PTLKVFRPPKKASKhaveDYNGERSAKAIVDFV 108
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 47-135 3.02e-13

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: 65.55  E-value: 3.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  47 DVALVNFYADWCRFSQMLHPIFEEASDVIKEEFPNenqVVFARVDCDQHSDIAQRYRISKYPTLKLFRNGMMMkrEYRGQ 126
Cdd:cd03000  16 DIWLVDFYAPWCGHCKKLEPVWNEVGAELKSSGSP---VRVGKLDATAYSSIASEFGVRGYPTIKLLKGDLAY--NYRGP 90


                ....*....
gi 52487191 127 RSVKALADY 135
Cdd:cd03000  91 RTKDDIVEF 99
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 36-136 1.50e-12

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: 63.34  E-value: 1.50e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  36 TENIDEILNNA--DVaLVNFYADWCRFSQMLHPIFEEasdvIKEEFPNENQVVFARVDCDQhSDIAQRYRISKYPTLKLF 113
Cdd:cd02995   7 GKNFDEVVLDSdkDV-LVEFYAPWCGHCKALAPIYEE----LAEKLKGDDNVVIAKMDATA-NDVPSEFVVDGFPTILFF 80

                        90       100
                ....*....|....*....|....
gi 52487191 114 RNGMMMKR-EYRGQRSVKALADYI 136
Cdd:cd02995  81 PAGDKSNPiKYEGDRTLEDLIKFI 104
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 44-136 1.60e-12

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: 63.15  E-value: 1.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  44 NNADVALVNFYADWCRFSQMLHPIFeeasDVIKEEFPnenQV-VFARVDCDQHSDIAQRYRISKYPTLKLFRNGMMMKre 122
Cdd:cd02999  16 NREDYTAVLFYASWCPFSASFRPHF----NALSSMFP---QIrHLAIEESSIKPSLLSRYGVVGFPTILLFNSTPRVR-- 86

                        90
                ....*....|....
gi 52487191 123 YRGQRSVKALADYI 136
Cdd:cd02999  87 YNGTRTLDSLAAFY 100
PDI_b_family cd02981
Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of ...
 144-234 1.61e-10

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: 57.35  E-value: 1.61e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191 144 IQEIRDLAEI-TTLDRSKRNIIGYFEQKDSDNYRVFERVANILHDDCAFLSAF--GDVSKPERYSGDNIIYKPP--GHSA 218
Cdd:cd02981   1 VKELTSKEELeKFLDKDDVVVVGFFKDEESEEYKTFEKVAESLRDDYGFGHTSdkEVAKKLKVKPGSVVLFKPFeeEPVE 80

                        90
                ....*....|....*..
gi 52487191 219 PDMVYL-GAMTNFDVTY 234
Cdd:cd02981  81 YDGEFTeESLVEFIKDN 97
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 37-147 2.05e-10

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: 62.00  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191    37 ENIDEILNNA--DVaLVNFYADWCRFSQMLHPIFEEASDVIKEEFPNenqVVFARVDCDQhSDIAQrYRISKYPTLKLFR 114
Cdd:TIGR01130 354 KNFDEIVLDEtkDV-LVEFYAPWCGHCKNLAPIYEELAEKYKDAESD---VVIAKMDATA-NDVPP-FEVEGFPTIKFVP 427

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 52487191   115 NGmmMKRE---YRGQRSVKALADYIRQQKSDPIQEI 147
Cdd:TIGR01130 428 AG--KKSEpvpYDGDRTLEDFSKFIAKHATFPLEGK 461
trxA PRK09381
thioredoxin TrxA;
27-116 2.47e-09

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 54.69  E-value: 2.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191   27 VTTEITSLDTENID-EILNNADVALVNFYADWCRFSQMLHPIFEEasdvIKEEFpnENQVVFARVDCDQHSDIAQRYRIS 105
Cdd:PRK09381   1 MSDKIIHLTDDSFDtDVLKADGAILVDFWAEWCGPCKMIAPILDE----IADEY--QGKLTVAKLNIDQNPGTAPKYGIR 74

                         90
                 ....*....|.
gi 52487191  106 KYPTLKLFRNG 116
Cdd:PRK09381  75 GIPTLLLFKNG 85
PRK10996 PRK10996
thioredoxin 2; Provisional
 36-118 3.69e-09

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 54.69  E-value: 3.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191   36 TENIDEILNNADVALVNFYADWCRFSQMLHPIFEeasDVIKEefpNENQVVFARVDCDQHSDIAQRYRISKYPTLKLFRN 115
Cdd:PRK10996  42 GETLDKLLQDDLPVVIDFWAPWCGPCRNFAPIFE---DVAAE---RSGKVRFVKVNTEAERELSARFRIRSIPTIMIFKN 115


                 ...
gi 52487191  116 GMM 118
Cdd:PRK10996 116 GQV 118
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 37-121 4.31e-09

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: 53.43  E-value: 4.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  37 ENIDEILNNA--DVALVNFYADWCRFSQMLHPIFEEASdviKEEFPnenQVVFARVDCDQHSDIAQRYRISKYPTLKLFR 114
Cdd:cd02984   3 EEFEELLKSDasKLLVLHFWAPWAEPCKQMNQVFEELA---KEAFP---SVLFLSIEAEELPEISEKFEITAVPTFVFFR 76


                ....*..
gi 52487191 115 NGMMMKR 121
Cdd:cd02984  77 NGTIVDR 83
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 31-139 5.27e-09

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: 53.81  E-value: 5.27e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  31 ITSLDTENIDEILNNADVA-LVNFYADWCRFSQMLHPIFEE-ASDVIKEefpnENQVVFARVDC--DQHSDIAQRYRISK 106
Cdd:cd02992   3 VIVLDAASFNSALLGSPSAwLVEFYASWCGHCRAFAPTWKKlARDLRKW----RPVVRVAAVDCadEENVALCRDFGVTG 78

                        90       100       110
                ....*....|....*....|....*....|...
gi 52487191 107 YPTLKLFRNGMMMKREYRGQRSVKALADYIRQQ 139
Cdd:cd02992  79 YPTLRYFPPFSKEATDGLKQEGPERDVNELREA 111
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 50-135 6.20e-09

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 55.79  E-value: 6.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191   50 LVNFYADWCRFSQMLHPIFEEASDVIKeefpneNQVVFARVDCDQHSDIAQRYRISKYPTLKLFRNGMMMKREyRGQRSV 129
Cdd:PTZ00443  56 FVKFYAPWCSHCRKMAPAWERLAKALK------GQVNVADLDATRALNLAKRFAIKGYPTLLLFDKGKMYQYE-GGDRST 128


                 ....*.
gi 52487191  130 KALADY 135
Cdd:PTZ00443 129 EKLAAF 134
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 29-136 1.86e-08

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: 51.61  E-value: 1.86e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  29 TEITSLDTENIDEILNnaDVALVNFYADWCRFSQMLHPIFEEASDVIKEEfpnenQVVFARVDCDQHSDIAQRYRISKYP 108
Cdd:cd02994   1 SNVVELTDSNWTLVLE--GEWMIEFYAPWCPACQQLQPEWEEFADWSDDL-----GINVAKVDVTQEPGLSGRFFVTALP 73

                        90       100
                ....*....|....*....|....*...
gi 52487191 109 TLKLFRNGMMmkREYRGQRSVKALADYI 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 2.49e-08

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: 51.37  E-value: 2.49e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  30 EITSLDTENIDEILNNADVALVNFYADWCRFSQMLHPIFEEASDVIkeefpnENQVVFARVDCDQHSDIAQRYRISKYPT 109
Cdd:cd03003   2 EIVTLDRGDFDAAVNSGEIWFVNFYSPRCSHCHDLAPTWREFAKEM------DGVIRIGAVNCGDDRMLCRSQGVNSYPS 75

                        90       100
                ....*....|....*....|....*.
gi 52487191 110 LKLFRNGmMMKREYRGQRSVKALADY 135
Cdd:cd03003  76 LYVFPSG-MNPEKYYGDRSKESLVKF 100
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 50-120 5.64e-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: 5.64e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52487191  50 LVNFYADWCRFSQMLHPIFEEASDVIKeefpnenQVVFARVDCDQHSDI---AQRYRISKYPTLKLFRNGMMMK 120
Cdd:cd01659   1 LVLFYAPWCPFCQALRPVLAELALLNK-------GVKFEAVDVDEDPALekeLKRYGVGGVPTLVVFGPGIGVK 67
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 37-116 1.54e-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: 48.81  E-value: 1.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  37 ENIDEILNNADVA--LVNFYADWCRFSQMLHPIFEEasdvIKEEFPNenQVVFARVDCDQHSDIAQRYRISKYPTLKLFR 114
Cdd:cd02956   1 QNFQQVLQESTQVpvVVDFWAPRSPPSKELLPLLER----LAEEYQG--QFVLAKVNCDAQPQIAQQFGVQALPTVYLFA 74


                ..
gi 52487191 115 NG 116
Cdd:cd02956  75 AG 76
Calsequestrin pfam01216
Calsequestrin;
62-195 2.08e-07

Calsequestrin;


Pssm-ID: 395972 [Multi-domain]  Cd Length: 350  Bit Score: 52.33  E-value: 2.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191    62 QMLHPIFEEASDVIKEEfpnenQVVFARVDCDQHSDIAQRYRISKYPTLKLFRNGMMMkrEYRGQRSVKALADYIRQQKS 141
Cdd:pfam01216  50 ELEEIILELAAQVLEDK-----DIGFGLVDAEKDAALAKKLGFDEEDSLYVFKGDETI--EFDGEFAADTIVEFLLDLIE 122

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 52487191   142 DPIQEIRDLAEITTLDRSKRNI--IGYFEQKDSDNYRVFERVANILHDDCAFLSAF 195
Cdd:pfam01216 123 DPVEIIEGELELQAFENIEDEIklIGFFKSEDSEHYKAFEDAAEEFHPYIKFFATF 178
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 48-138 7.97e-06

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 45.07  E-value: 7.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  48 VALVNFYADWCRFSQMLHPIFEEASD------VIK----------EEFPNENQVVFARVDcDQHSDIAQRYRISKYPTLK 111
Cdd:COG0526  30 PVLVNFWATWCPPCRAEMPVLKELAEeyggvvFVGvdvdenpeavKAFLKELGLPYPVLL-DPDGELAKAYGVRGIPTTV 108

                        90       100
                ....*....|....*....|....*...
gi 52487191 112 LF-RNGMMMKReYRGQRSVKALADYIRQ 138
Cdd:COG0526 109 LIdKDGKIVAR-HVGPLSPEELEEALEK 135
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 50-146 7.98e-06

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 47.82  E-value: 7.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191   50 LVNFYADWCRFSQMLHPIFEEASDVIKEefpNENQVVfARVDCDQHSDIAQRYRISKYPTLKLFRNGMMMKREYRGQRSV 129
Cdd:PTZ00102 379 LLEIYAPWCGHCKNLEPVYNELGEKYKD---NDSIIV-AKMNGTANETPLEEFSWSAFPTILFVKAGERTPIPYEGERTV 454

                         90
                 ....*....|....*..
gi 52487191  130 KALADYIRQQKSDPIQE 146
Cdd:PTZ00102 455 EGFKEFVNKHATNPFED 471
HyaE pfam07449
Hydrogenase-1 expression protein HyaE; This family contains bacterial hydrogenase-1 expression ...
 34-125 1.05e-04

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: 41.27  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191    34 LDTENIDEILNNADVALVNFYADWCRFSqmlhpifeEASDV------IKEEFPN-ENQVVFArvDCDQHSDIAQRYRISK 106
Cdd:pfam07449  14 VDASTLDDWLTAGGDGVLLLAGDPNRFP--------EVSDVavvlpeLLRAFPNaFRQAVVA--DREQEEALGDRFGVLR 83

                          90
                  ....*....|....*....
gi 52487191   107 YPTLKLFRNGmmmkrEYRG 125
Cdd:pfam07449  84 FPALLFFRDG-----DFVG 97
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
50-136 2.48e-04

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 40.10  E-value: 2.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191    50 LVNFYADWCRFSQMLHP----------IFEEASDVIKEEFPNENQVVFARVDCDQHSDIAQRYRISKYPTLkLFRNGMMM 119
Cdd:pfam13098   8 LVVFTDPDCPYCKKLKKelledpdvtvYLGPNFVFIAVNIWCAKEVAKAFTDILENKELGRKYGVRGTPTI-VFFDGKGE 86

                          90
                  ....*....|....*..
gi 52487191   120 KREYRGQRSVKALADYI 136
Cdd:pfam13098  87 LLRLPGYVPAEEFLALL 103
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 39-115 2.70e-04

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


Pssm-ID: 239248 [Multi-domain]  Cd Length: 142  Bit Score: 40.78  E-value: 2.70e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52487191  39 IDEILNNADVALVNFYADWCRFSQMLHPIFEEasdvIKEEFPNENQVVFARVDCDQHSDIAQRYRISKYPTLKLFRN 115
Cdd:cd02950  13 PEVALSNGKPTLVEFYADWCTVCQEMAPDVAK----LKQKYGDQVNFVMLNVDNPKWLPEIDRYRVDGIPHFVFLDR 85
PLN02309 PLN02309
5'-adenylylsulfate reductase
 30-113 1.56e-03

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 40.54  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191   30 EITSLDTENIDEIL---NNADVALVNFYADWCRFSQMLHPIFEEASdvikEEFPNENqVVFA--RVDCDQHSDIAQRYRI 104
Cdd:PLN02309 346 NVVALSRAGIENLLkleNRKEPWLVVLYAPWCPFCQAMEASYEELA----EKLAGSG-VKVAkfRADGDQKEFAKQELQL 420


                 ....*....
gi 52487191  105 SKYPTLKLF 113
Cdd:PLN02309 421 GSFPTILLF 429
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 16-137 2.33e-03

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 38.35  E-value: 2.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  16 LLLLVTWVFTPVTTEITSLDTeNIDEILNNADVA----LVNFYADWCRFSQMLHP-IF--EEASDVIKEEFpnenqvVFA 88
Cdd:COG2143   7 LLLLLLLLAAAAAAQEISFLL-DLEEDLALAKAEgkpiLLFFESDWCPYCKKLHKeVFsdPEVAAYLKENF------VVV 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52487191  89 RVDCD-------------QHSDIAQRYRISKYPTLKLF-RNGMMMKReYRGQRSVKALADYIR 137
Cdd:COG2143  80 QLDAEgdkevtdfdgetlTEKELARKYGVRGTPTLVFFdAEGKEIAR-IPGYLKPETFLALLK 141
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 50-124 3.15e-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: 3.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  50 LVNFYADWCRFSQMLHPIFEEASDvikeEFpnENQVVFARVDCDQHSDIAQRYRISKYPTLKLFRN--------GMMMKR 121
Cdd:cd02949  17 LVLYTSPTCGPCRTLKPILNKVID----EF--DGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDkelvkeisGVKMKS 90


                ...
gi 52487191 122 EYR 124
Cdd:cd02949  91 EYR 93
TMX2 cd02962
TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related ...
 31-116 4.17e-03

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: 37.75  E-value: 4.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  31 ITSLDTENIDEIL-NNADVA-LVNFYADWCRFSQMLHPIFEEASdvikEEFPNENqVVFARVDCDQHSDIAQRYRIS--- 105
Cdd:cd02962  30 IKYFTPKTLEEELeRDKRVTwLVEFFTTWSPECVNFAPVFAELS----LKYNNNN-LKFGKIDIGRFPNVAEKFRVStsp 104

                        90
                ....*....|....
gi 52487191 106 ---KYPTLKLFRNG 116
Cdd:cd02962 105 lskQLPTIILFQGG 118
PDI_b_family cd02981
Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of ...
 29-137 4.95e-03

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: 36.16  E-value: 4.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  29 TEITSLdtENIDEILNNADVALVNFYADwcrFSQMLHPIFEEASDVIKEEFPnenqvvFARVDcdqHSDIAQRYRISKyP 108
Cdd:cd02981   2 KELTSK--EELEKFLDKDDVVVVGFFKD---EESEEYKTFEKVAESLRDDYG------FGHTS---DKEVAKKLKVKP-G 66

                        90       100
                ....*....|....*....|....*....
gi 52487191 109 TLKLFRNGMMMKREYRGQRSVKALADYIR 137
Cdd:cd02981  67 SVVLFKPFEEEPVEYDGEFTEESLVEFIK 95
PDI_a_EFP1_N cd03006
PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase ...
 40-129 7.83e-03

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


Pssm-ID: 239304  Cd Length: 113  Bit Score: 35.91  E-value: 7.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52487191  40 DEILNNADVALVNFYADWCRFSQMLHPIFEEASDVIkeefpnENQVVFARVDC-DQHSDIAQRYRISKYPTLKLFRNGMM 118
Cdd:cd03006  23 EELRTDAEVSLVMYYAPWDAQSQAARQEFEQVAQKL------SDQVLFVAINCwWPQGKCRKQKHFFYFPVIHLYYRSRG 96

                        90
                ....*....|.
gi 52487191 119 MKREYRGQRSV 129
Cdd:cd03006  97 PIEYKGPMRAP 107
 
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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