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Conserved domains on  [gi|24642443|ref|NP_727949|]
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endoplasmic reticulum protein 44, isoform C [Drosophila melanogaster]

Protein Classification

glutathione S-transferase; glutathione S-transferase omega family protein( domain architecture ID 10122289)

glutathione S-transferase catalyzes the conjugation of reduced glutathione to a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress| glutathione S-transferase (GST) omega family protein such as class-omega GSTs, which catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins than GSTs

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 ...
 215-325 3.38e-70

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: 215.33  E-value: 3.38e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443 215 VREITFENAEELTEEGLPFLILFHHPTDHNSIKDYKSIIERQLLDEKQNVNFLTADGKRFAHPLHHLGKSEDDLPLIAID 294
Cdd:cd03072   1 VREITFENAEELTEEGLPFLILFHDKDDLESLKEFKQAVARQLISEKGAINFLTADGDKFRHPLLHLGKTPADLPVIAID 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 24642443 295 SFKHMYLFPHFSDMYSPGKLKQFLQDLYSGK 325
Cdd:cd03072  81 SFRHMYLFPDFEDVYVPGKLKQFVLDLHSGK 111
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 1-103 4.08e-65

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: 202.24  E-value: 4.08e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   1 MTSDNIDMTLASNELVFLNFYAEWCRFSNILAPIFAEAADKIKEEFPEAGKVVLGKVDCDKETAIASRFHINKYPTLKIV 80
Cdd:cd02996   6 LTSGNIDDILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEEFPDAGKVVWGKVDCDKESDIADRYRINKYPTLKLF 85

                        90       100
                ....*....|....*....|...
gi 24642443  81 RNGQLSKREYRGQRSAEAFLEFV 103
Cdd:cd02996  86 RNGMMMKREYRGQRSVEALAEFV 108
PDI_b_ERp44 cd03070
PDIb family, ERp44 subfamily, first redox inactive TRX-like domain b; ERp44 is an endoplasmic ...
 111-204 2.36e-39

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: 135.15  E-value: 2.36e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443 111 IQEFKSLKDLENLDSKKRLILGYFDRRDQPEYDIFRKVATNLKEDCQFHVGFGDAAQAMHPPGTPIIVFRPdvaLSHEND 190
Cdd:cd03070   1 IKEFRNLDELNNVDRSKRNIIGYFESKDSDEYDNFRKVANILRDDCSFLVGFGDVTKPERPPGDNIIYFPP---GHNAPD 77

                        90
                ....*....|....
gi 24642443 191 ETYTGSLQNFDELK 204
Cdd:cd03070  78 MVYLGSLTNFDLLK 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 ...
 215-325 3.38e-70

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: 215.33  E-value: 3.38e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443 215 VREITFENAEELTEEGLPFLILFHHPTDHNSIKDYKSIIERQLLDEKQNVNFLTADGKRFAHPLHHLGKSEDDLPLIAID 294
Cdd:cd03072   1 VREITFENAEELTEEGLPFLILFHDKDDLESLKEFKQAVARQLISEKGAINFLTADGDKFRHPLLHLGKTPADLPVIAID 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 24642443 295 SFKHMYLFPHFSDMYSPGKLKQFLQDLYSGK 325
Cdd:cd03072  81 SFRHMYLFPDFEDVYVPGKLKQFVLDLHSGK 111
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 1-103 4.08e-65

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: 202.24  E-value: 4.08e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   1 MTSDNIDMTLASNELVFLNFYAEWCRFSNILAPIFAEAADKIKEEFPEAGKVVLGKVDCDKETAIASRFHINKYPTLKIV 80
Cdd:cd02996   6 LTSGNIDDILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEEFPDAGKVVWGKVDCDKESDIADRYRINKYPTLKLF 85

                        90       100
                ....*....|....*....|...
gi 24642443  81 RNGQLSKREYRGQRSAEAFLEFV 103
Cdd:cd02996  86 RNGMMMKREYRGQRSVEALAEFV 108
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
134-320 1.03e-58

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 188.34  E-value: 1.03e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   134 FDRRDQPEYDIFRKVATNLKEDCQFHVGF-GDAAQAMHPPGTPIIVFRPDvalsHENDETYTGSLQNFDELKIWVQEKCV 212
Cdd:pfam13848   1 FEDKDSPLYEIFRKAAKELKGDVRFGITFsKEVADKYNIKEPAILLFRKF----DEETVHYPGDSINFEDLKKFIQKNCL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   213 PLVREITFENAEELTEEGLPFLILFHHPTDHNSIKDYKSIIERQLLDEKQNVNFLTADGKRFAHPLHHLGKSEDDLPLIA 292
Cdd:pfam13848  77 PLVREFTPENAEELFEEGIPPLLLLFLKKDDESTEEFKKALEKVAKKFRGKINFALVDAKSFGRPLEYFGLSESDLPVIV 156

                         170       180
                  ....*....|....*....|....*....
gi 24642443   293 I-DSFKHMYLFPhFSDMYSPGKLKQFLQD 320
Cdd:pfam13848 157 IvDSFSHMYKYF-PSDEFSPESLKEFIND 184
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 2-326 3.79e-53

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: 182.57  E-value: 3.79e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443     2 TSDNIDMTLASNELVFLNFYAEWCRFSNILAPIFAEAADKIKEEFPeagKVVLGKVDCDKETAIASRFHINKYPTLKIVR 81
Cdd:TIGR01130   7 TKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGP---PIKLAKVDATEEKDLAQKYGVSGYPTLKIFR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443    82 NGQLSKREYRGQRSAEAFLEFVKKQLEDPIQEFKSLKDLENLDSKKRL-ILGYFDRRDQPEYDIFRKVATNLKEDCQFHV 160
Cdd:TIGR01130  84 NGEDSVSDYNGPRDADGIVKYMKKQSGPAVKEIETVADLEAFLADDDVvVIGFFKDLDSELNDTFLSVAEKLRDVYFFFA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   161 GFGDAAQAMH---PPGTPIIVFRPDValsHENDETYTGSLQN-FDELKIWVQEKCVPLVREITFENAEELTEEG-LPFLI 235
Cdd:TIGR01130 164 HSSDVAAFAKlgaFPDSVVLFKPKDE---DEKFSKVDGEMDTdVSDLEKFIRAESLPLVGEFTQETAAKYFESGpLVVLY 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   236 LFHHPTD--HNSIKD-YKSIIERQlldEKQNVNFLTADGKRFAHPLHHLGKSEDDLPLIAIDSFKHMYLFPHFSDMYSPG 312
Cdd:TIGR01130 241 YNVDESLdpFEELRNrFLEAAKKF---RGKFVNFAVADEEDFGRELEYFGLKAEKFPAVAIQDLEGNKKYPMDQEEFSSE 317

                         330
                  ....*....|....
gi 24642443   313 KLKQFLQDLYSGKL 326
Cdd:TIGR01130 318 NLEAFVKDFLDGKL 331
PDI_b_ERp44 cd03070
PDIb family, ERp44 subfamily, first redox inactive TRX-like domain b; ERp44 is an endoplasmic ...
 111-204 2.36e-39

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: 135.15  E-value: 2.36e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443 111 IQEFKSLKDLENLDSKKRLILGYFDRRDQPEYDIFRKVATNLKEDCQFHVGFGDAAQAMHPPGTPIIVFRPdvaLSHEND 190
Cdd:cd03070   1 IKEFRNLDELNNVDRSKRNIIGYFESKDSDEYDNFRKVANILRDDCSFLVGFGDVTKPERPPGDNIIYFPP---GHNAPD 77

                        90
                ....*....|....
gi 24642443 191 ETYTGSLQNFDELK 204
Cdd:cd03070  78 MVYLGSLTNFDLLK 91
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 1-342 6.03e-33

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 128.33  E-value: 6.03e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443    1 MTSDNIDMTLASNELVFLNFYAEWCRFSNILAPIFAEAADKIKEEFPEagkVVLGKVDCDKETAIASRFHINKYPTLKIV 80
Cdd:PTZ00102  37 LTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSE---IVLASVDATEEMELAQEFGVRGYPTIKFF 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   81 RNGqlSKREYRGQRSAEAFLEFVKKQLEDPIQEFKSLKDL-ENLDSKKRLILGYFDRRDQPEYDIFRKVATNLKEDCQFH 159
Cdd:PTZ00102 114 NKG--NPVNYSGGRTADGIVSWIKKLTGPAVTEVESASEIkLIAKKIFVAFYGEYTSKDSELYKKFEEVADKHREHAKFF 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443  160 VGFGDAAQAMHppgtpiiVFRPDvalsHENDETYTGSLQnfDELKIWVQEKCVPLVREITFENAEELTEEGLpFLILFHH 239
Cdd:PTZ00102 192 VKKHEGKNKIY-------VLHKD----EEGVELFMGKTK--EELEEFVSTESFPLFAEINAENYRRYISSGK-DLVWFCG 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443  240 PT-DHNSIKDYKSIIERQLLDEkqnVNFLTADGKRFA-HPLHHLGKSEddLPLIAIDSFKHMYLFPHFSDMY-SPGKLKQ 316
Cdd:PTZ00102 258 TTeDYDKYKSVVRKVARKLREK---YAFVWLDTEQFGsHAKEHLLIEE--FPGLAYQSPAGRYLLPPAKESFdSVEALIE 332

                        330       340
                 ....*....|....*....|....*.
gi 24642443  317 FLQDLYSGKLHREFHYGPDPSNDIEP 342
Cdd:PTZ00102 333 FFKDVEAGKVEKSIKSEPIPEEQDGP 358
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 2-107 7.45e-20

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: 83.72  E-value: 7.45e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   2 TSDNID-MTLASNELVFLNFYAEWCRFSNILAPIFAEAADKIkeefpeAGKVVLGKVDCDKETAIASRFHINKYPTLKIV 80
Cdd:COG3118   6 TDENFEeEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEY------GGKVKFVKVDVDENPELAAQFGVRSIPTLLLF 79

                        90       100
                ....*....|....*....|....*..
gi 24642443  81 RNGQLSKReYRGQRSAEAFLEFVKKQL 107
Cdd:COG3118  80 KDGQPVDR-FVGALPKEQLREFLDKVL 105
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 2-105 2.69e-17

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: 76.50  E-value: 2.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443     2 TSDNIDMTLAS-NELVFLNFYAEWCRFSNILAPIFAEAADKIKeefpeaGKVVLGKVDCDKETAIASRFHINKYPTLKIV 80
Cdd:pfam00085   6 TDANFDEVVQKsSKPVLVDFYAPWCGPCKMLAPEYEELAQEYK------GNVVFAKVDVDENPDLASKYGVRGYPTLIFF 79

                          90       100
                  ....*....|....*....|....*
gi 24642443    81 RNGQLSKrEYRGQRSAEAFLEFVKK 105
Cdd:pfam00085  80 KNGQPVD-DYVGARPKDALAAFLKA 103
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 2-107 2.32e-16

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


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 73.86  E-value: 2.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443     2 TSDNIDMTLAS-NELVFLNFYAEWCRFSNILAPIFAEAADKikeefpEAGKVVLGKVDCDKETAIASRFHINKYPTLKIV 80
Cdd:TIGR01068   2 TDANFDETIASsDKPVLVDFWAPWCGPCKMIAPILEELAKE------YEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLF 75

                          90       100
                  ....*....|....*....|....*..
gi 24642443    81 RNGQLSKREYrGQRSAEAFLEFVKKQL 107
Cdd:TIGR01068  76 KNGKEVDRSV-GALPKAALKQLINKNL 101
PTZ00051 PTZ00051
thioredoxin; Provisional
 2-84 7.32e-12

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 61.05  E-value: 7.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443    2 TSDNIDMTLASNELVFLNFYAEWCRFSNILAPIFAEAAdkikEEFPeagKVVLGKVDCDKETAIASRFHINKYPTLKIVR 81
Cdd:PTZ00051   7 SQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECS----KEYT---KMVFVKVDVDELSEVAEKENITSMPTFKVFK 79


                 ...
gi 24642443   82 NGQ 84
Cdd:PTZ00051  80 NGS 82
 
Name Accession Description Interval E-value
PDI_b'_ERp44 cd03072
PDIb' family, ERp44 subfamily, second redox inactive TRX-like domain b'; ERp44 is an ...
 215-325 3.38e-70

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: 215.33  E-value: 3.38e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443 215 VREITFENAEELTEEGLPFLILFHHPTDHNSIKDYKSIIERQLLDEKQNVNFLTADGKRFAHPLHHLGKSEDDLPLIAID 294
Cdd:cd03072   1 VREITFENAEELTEEGLPFLILFHDKDDLESLKEFKQAVARQLISEKGAINFLTADGDKFRHPLLHLGKTPADLPVIAID 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 24642443 295 SFKHMYLFPHFSDMYSPGKLKQFLQDLYSGK 325
Cdd:cd03072  81 SFRHMYLFPDFEDVYVPGKLKQFVLDLHSGK 111
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 1-103 4.08e-65

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: 202.24  E-value: 4.08e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   1 MTSDNIDMTLASNELVFLNFYAEWCRFSNILAPIFAEAADKIKEEFPEAGKVVLGKVDCDKETAIASRFHINKYPTLKIV 80
Cdd:cd02996   6 LTSGNIDDILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEEFPDAGKVVWGKVDCDKESDIADRYRINKYPTLKLF 85

                        90       100
                ....*....|....*....|...
gi 24642443  81 RNGQLSKREYRGQRSAEAFLEFV 103
Cdd:cd02996  86 RNGMMMKREYRGQRSVEALAEFV 108
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
134-320 1.03e-58

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 188.34  E-value: 1.03e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   134 FDRRDQPEYDIFRKVATNLKEDCQFHVGF-GDAAQAMHPPGTPIIVFRPDvalsHENDETYTGSLQNFDELKIWVQEKCV 212
Cdd:pfam13848   1 FEDKDSPLYEIFRKAAKELKGDVRFGITFsKEVADKYNIKEPAILLFRKF----DEETVHYPGDSINFEDLKKFIQKNCL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   213 PLVREITFENAEELTEEGLPFLILFHHPTDHNSIKDYKSIIERQLLDEKQNVNFLTADGKRFAHPLHHLGKSEDDLPLIA 292
Cdd:pfam13848  77 PLVREFTPENAEELFEEGIPPLLLLFLKKDDESTEEFKKALEKVAKKFRGKINFALVDAKSFGRPLEYFGLSESDLPVIV 156

                         170       180
                  ....*....|....*....|....*....
gi 24642443   293 I-DSFKHMYLFPhFSDMYSPGKLKQFLQD 320
Cdd:pfam13848 157 IvDSFSHMYKYF-PSDEFSPESLKEFIND 184
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 2-326 3.79e-53

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: 182.57  E-value: 3.79e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443     2 TSDNIDMTLASNELVFLNFYAEWCRFSNILAPIFAEAADKIKEEFPeagKVVLGKVDCDKETAIASRFHINKYPTLKIVR 81
Cdd:TIGR01130   7 TKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGP---PIKLAKVDATEEKDLAQKYGVSGYPTLKIFR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443    82 NGQLSKREYRGQRSAEAFLEFVKKQLEDPIQEFKSLKDLENLDSKKRL-ILGYFDRRDQPEYDIFRKVATNLKEDCQFHV 160
Cdd:TIGR01130  84 NGEDSVSDYNGPRDADGIVKYMKKQSGPAVKEIETVADLEAFLADDDVvVIGFFKDLDSELNDTFLSVAEKLRDVYFFFA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   161 GFGDAAQAMH---PPGTPIIVFRPDValsHENDETYTGSLQN-FDELKIWVQEKCVPLVREITFENAEELTEEG-LPFLI 235
Cdd:TIGR01130 164 HSSDVAAFAKlgaFPDSVVLFKPKDE---DEKFSKVDGEMDTdVSDLEKFIRAESLPLVGEFTQETAAKYFESGpLVVLY 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   236 LFHHPTD--HNSIKD-YKSIIERQlldEKQNVNFLTADGKRFAHPLHHLGKSEDDLPLIAIDSFKHMYLFPHFSDMYSPG 312
Cdd:TIGR01130 241 YNVDESLdpFEELRNrFLEAAKKF---RGKFVNFAVADEEDFGRELEYFGLKAEKFPAVAIQDLEGNKKYPMDQEEFSSE 317

                         330
                  ....*....|....
gi 24642443   313 KLKQFLQDLYSGKL 326
Cdd:TIGR01130 318 NLEAFVKDFLDGKL 331
PDI_b_ERp44 cd03070
PDIb family, ERp44 subfamily, first redox inactive TRX-like domain b; ERp44 is an endoplasmic ...
 111-204 2.36e-39

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: 135.15  E-value: 2.36e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443 111 IQEFKSLKDLENLDSKKRLILGYFDRRDQPEYDIFRKVATNLKEDCQFHVGFGDAAQAMHPPGTPIIVFRPdvaLSHEND 190
Cdd:cd03070   1 IKEFRNLDELNNVDRSKRNIIGYFESKDSDEYDNFRKVANILRDDCSFLVGFGDVTKPERPPGDNIIYFPP---GHNAPD 77

                        90
                ....*....|....
gi 24642443 191 ETYTGSLQNFDELK 204
Cdd:cd03070  78 MVYLGSLTNFDLLK 91
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 1-342 6.03e-33

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 128.33  E-value: 6.03e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443    1 MTSDNIDMTLASNELVFLNFYAEWCRFSNILAPIFAEAADKIKEEFPEagkVVLGKVDCDKETAIASRFHINKYPTLKIV 80
Cdd:PTZ00102  37 LTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSE---IVLASVDATEEMELAQEFGVRGYPTIKFF 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   81 RNGqlSKREYRGQRSAEAFLEFVKKQLEDPIQEFKSLKDL-ENLDSKKRLILGYFDRRDQPEYDIFRKVATNLKEDCQFH 159
Cdd:PTZ00102 114 NKG--NPVNYSGGRTADGIVSWIKKLTGPAVTEVESASEIkLIAKKIFVAFYGEYTSKDSELYKKFEEVADKHREHAKFF 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443  160 VGFGDAAQAMHppgtpiiVFRPDvalsHENDETYTGSLQnfDELKIWVQEKCVPLVREITFENAEELTEEGLpFLILFHH 239
Cdd:PTZ00102 192 VKKHEGKNKIY-------VLHKD----EEGVELFMGKTK--EELEEFVSTESFPLFAEINAENYRRYISSGK-DLVWFCG 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443  240 PT-DHNSIKDYKSIIERQLLDEkqnVNFLTADGKRFA-HPLHHLGKSEddLPLIAIDSFKHMYLFPHFSDMY-SPGKLKQ 316
Cdd:PTZ00102 258 TTeDYDKYKSVVRKVARKLREK---YAFVWLDTEQFGsHAKEHLLIEE--FPGLAYQSPAGRYLLPPAKESFdSVEALIE 332

                        330       340
                 ....*....|....*....|....*.
gi 24642443  317 FLQDLYSGKLHREFHYGPDPSNDIEP 342
Cdd:PTZ00102 333 FFKDVEAGKVEKSIKSEPIPEEQDGP 358
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 2-103 7.66e-30

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: 110.39  E-value: 7.66e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   2 TSDNIDMTLASNELVFLNFYAEWCRFSNILAPIFAEAADKIKEEfpeaGKVVLGKVDCDKETAIASRFHINKYPTLKIVR 81
Cdd:cd02961   4 TDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKGD----GKVVVAKVDCTANNDLCSEYGVRGYPTIKLFP 79

                        90       100
                ....*....|....*....|..
gi 24642443  82 NGQLSKREYRGQRSAEAFLEFV 103
Cdd:cd02961  80 NGSKEPVKYEGPRTLESLVEFI 101
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 2-107 7.45e-20

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: 83.72  E-value: 7.45e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   2 TSDNID-MTLASNELVFLNFYAEWCRFSNILAPIFAEAADKIkeefpeAGKVVLGKVDCDKETAIASRFHINKYPTLKIV 80
Cdd:COG3118   6 TDENFEeEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEY------GGKVKFVKVDVDENPELAAQFGVRSIPTLLLF 79

                        90       100
                ....*....|....*....|....*..
gi 24642443  81 RNGQLSKReYRGQRSAEAFLEFVKKQL 107
Cdd:COG3118  80 KDGQPVDR-FVGALPKEQLREFLDKVL 105
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 1-103 2.35e-18

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: 79.60  E-value: 2.35e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   1 MTSDNIDMTL-ASNELVFLNFYAEWCRFSNILAPIFAEAADkikeEFPEAGKVVLGKVDCDKE-TAIASRFHINKYPTLK 78
Cdd:cd02998   5 LTDSNFDKVVgDDKKDVLVEFYAPWCGHCKNLAPEYEKLAA----VFANEDDVVIAKVDADEAnKDLAKKYGVSGFPTLK 80

                        90       100
                ....*....|....*....|....*
gi 24642443  79 IVRNGQLSKREYRGQRSAEAFLEFV 103
Cdd:cd02998  81 FFPKGSTEPVKYEGGRDLEDLVKFV 105
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 1-103 7.63e-18

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: 78.10  E-value: 7.63e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   1 MTSDNID-MTLASNELVFLNFYAEWCRFSNILAPIFAEAADKIKeefpeaGKVVLGKVDCDKETAIASRFHINKYPTLKI 79
Cdd:cd03001   5 LTDSNFDkKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALK------GIVKVGAVDADVHQSLAQQYGVRGFPTIKV 78

                        90       100
                ....*....|....*....|....
gi 24642443  80 VRNGQLSKREYRGQRSAEAFLEFV 103
Cdd:cd03001  79 FGAGKNSPQDYQGGRTAKAIVSAA 102
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 2-105 2.69e-17

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: 76.50  E-value: 2.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443     2 TSDNIDMTLAS-NELVFLNFYAEWCRFSNILAPIFAEAADKIKeefpeaGKVVLGKVDCDKETAIASRFHINKYPTLKIV 80
Cdd:pfam00085   6 TDANFDEVVQKsSKPVLVDFYAPWCGPCKMLAPEYEELAQEYK------GNVVFAKVDVDENPDLASKYGVRGYPTLIFF 79

                          90       100
                  ....*....|....*....|....*
gi 24642443    81 RNGQLSKrEYRGQRSAEAFLEFVKK 105
Cdd:pfam00085  80 KNGQPVD-DYVGARPKDALAAFLKA 103
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 1-103 1.01e-16

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: 75.01  E-value: 1.01e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   1 MTSDNIDMTLASnELVFLNFYAEWCRFSNILAPIFAEAADKikeEFPEAGKVVLGKVDCDKETAIASRFHINKYPTLKIV 80
Cdd:cd03005   5 LTEDNFDHHIAE-GNHFVKFFAPWCGHCKRLAPTWEQLAKK---FNNENPSVKIAKVDCTQHRELCSEFQVRGYPTLLLF 80

                        90       100
                ....*....|....*....|...
gi 24642443  81 RNGQLSKrEYRGQRSAEAFLEFV 103
Cdd:cd03005  81 KDGEKVD-KYKGTRDLDSLKEFV 102
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 4-104 1.58e-16

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


Pssm-ID: 239245 [Multi-domain]  Cd Length: 93  Bit Score: 74.13  E-value: 1.58e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   4 DNIDMTLASNELVFLNFYAEWCRFSNILAPIFAEAADkikeefpEAGKVVLGKVDCDKETAIASRFHINKYPTLKIVRNG 83
Cdd:cd02947   1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAE-------EYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNG 73

                        90       100
                ....*....|....*....|.
gi 24642443  84 QLSKREYrGQRSAEAFLEFVK 104
Cdd:cd02947  74 KEVDRVV-GADPKEELEEFLE 93
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 2-107 2.32e-16

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


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 73.86  E-value: 2.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443     2 TSDNIDMTLAS-NELVFLNFYAEWCRFSNILAPIFAEAADKikeefpEAGKVVLGKVDCDKETAIASRFHINKYPTLKIV 80
Cdd:TIGR01068   2 TDANFDETIASsDKPVLVDFWAPWCGPCKMIAPILEELAKE------YEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLF 75

                          90       100
                  ....*....|....*....|....*..
gi 24642443    81 RNGQLSKREYrGQRSAEAFLEFVKKQL 107
Cdd:TIGR01068  76 KNGKEVDRSV-GALPKAALKQLINKNL 101
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 2-102 1.39e-14

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: 68.88  E-value: 1.39e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   2 TSDNIDMTLASNELVFLNFYAEWCRFSNILAPIFAEAAdkikEEFPEAGKVVLGKVDCDKET--AIASRFHINKYPTLKI 79
Cdd:cd02997   6 TDEDFRKFLKKEKHVLVMFYAPWCGHCKKMKPEFTKAA----TELKEDGKGVLAAVDCTKPEhdALKEEYNVKGFPTFKY 81

                        90       100
                ....*....|....*....|...
gi 24642443  80 VRNGQLsKREYRGQRSAEAFLEF 102
Cdd:cd02997  82 FENGKF-VEKYEGERTAEDIIEF 103
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 13-105 1.21e-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: 66.32  E-value: 1.21e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443  13 NELVFLNFYAEWCRFSNILAPIFAEAADKIKEEfpeAGKVVLGKVDCDKETAIASRFHINKYPTLKIVRNGQlsKREYRG 92
Cdd:cd03000  15 EDIWLVDFYAPWCGHCKKLEPVWNEVGAELKSS---GSPVRVGKLDATAYSSIASEFGVRGYPTIKLLKGDL--AYNYRG 89

                        90
                ....*....|...
gi 24642443  93 QRSAEAFLEFVKK 105
Cdd:cd03000  90 PRTKDDIVEFANR 102
PDI_b'_family cd02982
Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of ...
 216-321 1.75e-13

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: 65.76  E-value: 1.75e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443 216 REITFENAEELteeGLPFLILFHHPTD--HNSIKDYKSIIERQLldeKQNVNFLTADGKRFAHPLHHLGKSEDDLPLIAI 293
Cdd:cd02982   1 NAETFFNYEES---GKPLLVLFYNKDDseSEELRERFKEVAKKF---KGKLLFVVVDADDFGRHLEYFGLKEEDLPVIAI 74

                        90       100       110
                ....*....|....*....|....*....|
gi 24642443 294 DSF--KHMYLFPHFSdmYSPGKLKQFLQDL 321
Cdd:cd02982  75 INLsdGKKYLMPEEE--LTAESLEEFVEDF 102
PTZ00051 PTZ00051
thioredoxin; Provisional
 2-84 7.32e-12

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 61.05  E-value: 7.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443    2 TSDNIDMTLASNELVFLNFYAEWCRFSNILAPIFAEAAdkikEEFPeagKVVLGKVDCDKETAIASRFHINKYPTLKIVR 81
Cdd:PTZ00051   7 SQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECS----KEYT---KMVFVKVDVDELSEVAEKENITSMPTFKVFK 79


                 ...
gi 24642443   82 NGQ 84
Cdd:PTZ00051  80 NGS 82
PRK10996 PRK10996
thioredoxin 2; Provisional
 2-85 8.79e-12

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 62.01  E-value: 8.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443    2 TSDNIDMTLASNELVFLNFYAEWCRFSNILAPIFAEAADKikeefpEAGKVVLGKVDCDKETAIASRFHINKYPTLKIVR 81
Cdd:PRK10996  41 TGETLDKLLQDDLPVVIDFWAPWCGPCRNFAPIFEDVAAE------RSGKVRFVKVNTEAERELSARFRIRSIPTIMIFK 114


                 ....
gi 24642443   82 NGQL 85
Cdd:PRK10996 115 NGQV 118
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 2-104 4.91e-11

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: 59.30  E-value: 4.91e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   2 TSDNIDMTLA-SNELVFLNFYAEWCRFSNILAPIFAEAADKIKeefpeaGKVVLGKVDCDKET--AIASRFHINKYPTLK 78
Cdd:cd03002   6 TPKNFDKVVHnTNYTTLVEFYAPWCGHCKNLKPEYAKAAKELD------GLVQVAAVDCDEDKnkPLCGKYGVQGFPTLK 79

                        90       100       110
                ....*....|....*....|....*....|
gi 24642443  79 IVRNGQLSKR----EYRGQRSAEAFLEFVK 104
Cdd:cd03002  80 VFRPPKKASKhaveDYNGERSAKAIVDFVL 109
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 16-115 3.27e-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: 61.23  E-value: 3.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443    16 VFLNFYAEWCRFSNILAPIFAEAADKIKEEFPeagKVVLGKVDCdkeTA-IASRFHINKYPTLKIVRNGqlSKRE---YR 91
Cdd:TIGR01130 367 VLVEFYAPWCGHCKNLAPIYEELAEKYKDAES---DVVIAKMDA---TAnDVPPFEVEGFPTIKFVPAG--KKSEpvpYD 438

                          90       100
                  ....*....|....*....|....
gi 24642443    92 GQRSAEAFLEFVKKQLEDPIQEFK 115
Cdd:TIGR01130 439 GDRTLEDFSKFIAKHATFPLEGKA 462
PDI_b_family cd02981
Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of ...
 111-203 1.32e-09

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: 54.65  E-value: 1.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443 111 IQEFKSLKDLE-NLDSKKRLILGYFDRRDQPEYDIFRKVATNLKEDCQF-HVGFGDAAQAMHPPGTPIIVFRPDVALSHE 188
Cdd:cd02981   1 VKELTSKEELEkFLDKDDVVVVGFFKDEESEEYKTFEKVAESLRDDYGFgHTSDKEVAKKLKVKPGSVVLFKPFEEEPVE 80

                        90
                ....*....|....*.
gi 24642443 189 -NDETYTGSLQNFDEL 203
Cdd:cd02981  81 yDGEFTEESLVEFIKD 96
trxA PRK09381
thioredoxin TrxA;
1-107 3.32e-09

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 53.91  E-value: 3.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443    1 MTSDNIDM-TLASNELVFLNFYAEWCRFSNILAPIFaeaaDKIKEEFpeAGKVVLGKVDCDKETAIASRFHINKYPTLKI 79
Cdd:PRK09381   8 LTDDSFDTdVLKADGAILVDFWAEWCGPCKMIAPIL----DEIADEY--QGKLTVAKLNIDQNPGTAPKYGIRGIPTLLL 81

                         90       100
                 ....*....|....*....|....*...
gi 24642443   80 VRNGQLSKREYrGQRSAEAFLEFVKKQL 107
Cdd:PRK09381  82 FKNGEVAATKV-GALSKGQLKEFLDANL 108
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 1-105 3.64e-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: 53.54  E-value: 3.64e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   1 MTSDNIDMTLASNELVflNFYAEWCRFSNILAPIFAEAADKikeefPEAGKVVLGKVDCDKETAIASRFHINKYPTLKIV 80
Cdd:cd02994   6 LTDSNWTLVLEGEWMI--EFYAPWCPACQQLQPEWEEFADW-----SDDLGINVAKVDVTQEPGLSGRFFVTALPTIYHA 78

                        90       100
                ....*....|....*....|....*
gi 24642443  81 RNGQLskREYRGQRSAEAFLEFVKK 105
Cdd:cd02994  79 KDGVF--RRYQGPRDKEDLISFIEE 101
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 12-103 6.37e-09

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: 53.06  E-value: 6.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443  12 SNELVFLNFYAEWCRFSNILAPIFAEAADKIKeefpeaGKVVLGKVDCDKETAIASRFHINKYPTLKIVRNGQLSKREYR 91
Cdd:cd03004  18 RKEPWLVDFYAPWCGPCQALLPELRKAARALK------GKVKVGSVDCQKYESLCQQANIRAYPTIRLYPGNASKYHSYN 91

                        90
                ....*....|...
gi 24642443  92 G-QRSAEAFLEFV 103
Cdd:cd03004  92 GwHRDADSILEFI 104
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 17-111 6.65e-09

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 55.79  E-value: 6.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   17 FLNFYAEWCRFSNILAPIFAEAADKIKeefpeaGKVVLGKVDCDKETAIASRFHINKYPTLKIVRNGQLSKREyRGQRSA 96
Cdd:PTZ00443  56 FVKFYAPWCSHCRKMAPAWERLAKALK------GQVNVADLDATRALNLAKRFAIKGYPTLLLFDKGKMYQYE-GGDRST 128

                         90
                 ....*....|....*....
gi 24642443   97 EAFLEFV----KKQLEDPI 111
Cdd:PTZ00443 129 EKLAAFAlgdfKKALGAPV 147
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 16-84 7.73e-09

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: 52.66  E-value: 7.73e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24642443  16 VFLNFYAEWCRFSNILAPIFaeaaDKIKEEFPeaGKVVLGKVDCDKETAIASRFHINKYPTLKIVRNGQ 84
Cdd:cd02956  15 VVVDFWAPRSPPSKELLPLL----ERLAEEYQ--GQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQ 77
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 7-103 7.79e-09

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


Pssm-ID: 239293 [Multi-domain]  Cd Length: 104  Bit Score: 52.94  E-value: 7.79e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   7 DMTLASNELVFLNFYAEWCRFSNILAPIFAEAAdkikEEFPEAGKVVLGKVDCdkeTA--IASRFHINKYPTLKIVRNGq 84
Cdd:cd02995  12 EVVLDSDKDVLVEFYAPWCGHCKALAPIYEELA----EKLKGDDNVVIAKMDA---TAndVPSEFVVDGFPTILFFPAG- 83

                        90       100
                ....*....|....*....|..
gi 24642443  85 lSKRE---YRGQRSAEAFLEFV 103
Cdd:cd02995  84 -DKSNpikYEGDRTLEDLIKFI 104
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 7-102 4.07e-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: 50.60  E-value: 4.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   7 DMTLASNELVFLNFYAEWCRFSNILAPIFAEAADKIKeefpeaGKVVLGKVDCDKETAIASRFHINKYPTLKIVRNGqLS 86
Cdd:cd03003  12 DAAVNSGEIWFVNFYSPRCSHCHDLAPTWREFAKEMD------GVIRIGAVNCGDDRMLCRSQGVNSYPSLYVFPSG-MN 84

                        90
                ....*....|....*.
gi 24642443  87 KREYRGQRSAEAFLEF 102
Cdd:cd03003  85 PEKYYGDRSKESLVKF 100
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 6-113 2.63e-07

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 52.45  E-value: 2.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443    6 IDMTLASNELVFLNFYAEWCRFSNILAPIFAEAADKIKEEfpeaGKVVLGKVDCDKETAIASRFHINKYPTLKIVRNGQL 85
Cdd:PTZ00102 368 EEIVFKSDKDVLLEIYAPWCGHCKNLEPVYNELGEKYKDN----DSIIVAKMNGTANETPLEEFSWSAFPTILFVKAGER 443

                         90       100
                 ....*....|....*....|....*...
gi 24642443   86 SKREYRGQRSAEAFLEFVKKQLEDPIQE 113
Cdd:PTZ00102 444 TPIPYEGERTVEGFKEFVNKHATNPFED 471
Calsequestrin pfam01216
Calsequestrin;
2-162 1.42e-06

Calsequestrin;


Pssm-ID: 395972 [Multi-domain]  Cd Length: 350  Bit Score: 49.63  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443     2 TSDNIDMTLASNELVFLNFYAEWcrfsNILAPIFAEA--ADKIKEEFPEAGKVVL--------------GKVDCDKETAI 65
Cdd:pfam01216   6 EYDGKDRVINLNAKNFKNVFKKY----DVLALLYHEPpeDDKAAQKQFELEEIILelaaqvledkdigfGLVDAEKDAAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443    66 ASRFHINKYPTLKIVRNGQLSkrEYRGQRSAEAFLEFVKKQLEDPIQEFKS---LKDLENLDSKKRLIlGYFDRRDQPEY 142
Cdd:pfam01216  82 AKKLGFDEEDSLYVFKGDETI--EFDGEFAADTIVEFLLDLIEDPVEIIEGeleLQAFENIEDEIKLI-GFFKSEDSEHY 158

                         170       180
                  ....*....|....*....|
gi 24642443   143 DIFRKVATNLKEDCQFHVGF 162
Cdd:pfam01216 159 KAFEDAAEEFHPYIKFFATF 178
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 20-103 4.44e-06

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: 44.66  E-value: 4.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443  20 FYAEWCRFSNILAPIFaeaaDKIKEEFPEAgkVVLGKVDCDKETAIASRFHINKYPTLKIVRNGQLSKreYRGQRSAEAF 99
Cdd:cd02999  25 FYASWCPFSASFRPHF----NALSSMFPQI--RHLAIEESSIKPSLLSRYGVVGFPTILLFNSTPRVR--YNGTRTLDSL 96


                ....
gi 24642443 100 LEFV 103
Cdd:cd02999  97 AAFY 100
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 16-108 2.38e-05

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 43.91  E-value: 2.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443  16 VFLNFYAEWCRFSNILAPIFAEAADKIK---------EEFPEAGKVVLGK------VDCDKETAIASRFHINKYPTLKIV 80
Cdd:COG0526  31 VLVNFWATWCPPCRAEMPVLKELAEEYGgvvfvgvdvDENPEAVKAFLKElglpypVLLDPDGELAKAYGVRGIPTTVLI 110

                        90       100
                ....*....|....*....|....*....
gi 24642443  81 -RNGQLSKReYRGQRSAEAFLEFVKKQLE 108
Cdd:COG0526 111 dKDGKIVAR-HVGPLSPEELEEALEKLLA 138
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 4-78 9.65e-05

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: 41.49  E-value: 9.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   4 DN-IDMTLASNELVFLN--------FYAEWCRFSNILAPIFAEAADKIKeEFPEAgkVVLGKVDCDKET--AIASRFHIN 72
Cdd:cd02992   1 DPvIVLDAASFNSALLGspsawlveFYASWCGHCRAFAPTWKKLARDLR-KWRPV--VRVAAVDCADEEnvALCRDFGVT 77


                ....*.
gi 24642443  73 KYPTLK 78
Cdd:cd02992  78 GYPTLR 83
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 8-88 1.55e-03

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: 37.64  E-value: 1.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   8 MTLASNELVFLNFYAEWCRFSNILAPIFAEAAdkiKEEFPEagkVVLGKVDCDKETAIASRFHINKYPTLKIVRNGQLSK 87
Cdd:cd02984   9 LKSDASKLLVLHFWAPWAEPCKQMNQVFEELA---KEAFPS---VLFLSIEAEELPEISEKFEITAVPTFVFFRNGTIVD 82


                .
gi 24642443  88 R 88
Cdd:cd02984  83 R 83
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 17-83 4.02e-03

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


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 35.75  E-value: 4.02e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443  17 FLNFYAEWCRFSNILAPIFAEAADkikeefpEAGKVVLGKVDCDKETAI---ASRFHINKYPTLKIVRNG 83
Cdd:cd01659   1 LVLFYAPWCPFCQALRPVLAELAL-------LNKGVKFEAVDVDEDPALekeLKRYGVGGVPTLVVFGPG 63
DsbDgamma cd02953
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
 6-101 4.02e-03

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


Pssm-ID: 239251 [Multi-domain]  Cd Length: 104  Bit Score: 36.43  E-value: 4.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443   6 IDMTLASNELVFLNFYAEWCrfsniLA----PIFAEAADKIKEEFpeAGKVVLGKVDC----DKETAIASRFHINKYPTL 77
Cdd:cd02953   4 LAQALAQGKPVFVDFTADWC-----VTckvnEKVVFSDPEVQAAL--KKDVVLLRADWtkndPEITALLKRFGVFGPPTY 76

                        90       100
                ....*....|....*....|....*....
gi 24642443  78 KIVRNGQlskrEYRGQR-----SAEAFLE 101
Cdd:cd02953  77 LFYGPGG----EPEPLRlpgflTADEFLE 101
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 13-103 7.41e-03

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


Pssm-ID: 239291 [Multi-domain]  Cd Length: 109  Bit Score: 35.89  E-value: 7.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642443  13 NELVFLnfYAEWCRFSNILAPIFAEAADKIKEEfpeagKVVLGKVDCDKETAIASR--FHINKYPTLKIVRNGQLSKREY 90
Cdd:cd02993  23 STLVVL--YAPWCPFCQAMEASYEELAEKLAGS-----NVKVAKFNADGEQREFAKeeLQLKSFPTILFFPKNSRQPIKY 95

                        90
                ....*....|....
gi 24642443  91 RG-QRSAEAFLEFV 103
Cdd:cd02993  96 PSeQRDVDSLLMFV 109
 
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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