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Conserved domains on  [gi|53135337|emb|CAG32416|]
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hypothetical protein RCJMB04_24o2 [Gallus gallus]

Protein Classification

PDI_a_ERp46 domain-containing protein( domain architecture ID 10122334)

PDI_a_ERp46 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 172-272 1.78e-66

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: 206.75  E-value: 1.78e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 172 GMYELSADNFKTHIAEGNHFIKFFAPWCGHCKALAPTWEQLALAFEH-SETVKIGKVDCTQHYEVCSENQVRGYPTLLWF 250
Cdd:cd03005   1 GVLELTEDNFDHHIAEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFNNeNPSVKIAKVDCTQHRELCSEFQVRGYPTLLLF 80

                        90       100
                ....*....|....*....|..
gi 53135337 251 RNGEKGDQYKGKRDFDSLKEYV 272
Cdd:cd03005  81 KDGEKVDKYKGTRDLDSLKEFV 102
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 305-406 1.33e-62

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: 196.74  E-value: 1.33e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 305 AVLSLSEKDFDETIARGITFIKFYAPWCGHCKNLAPTWEILAKEQFPGLTDVKIAEVDCTVERNVCNRFSVRGYPTLLLF 384
Cdd:cd03005   1 GVLELTEDNFDHHIAEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFNNENPSVKIAKVDCTQHRELCSEFQVRGYPTLLLF 80

                        90       100
                ....*....|....*....|..
gi 53135337 385 RGGKKVSEHNGTRDLESLHSFV 406
Cdd:cd03005  81 KDGEKVDKYKGTRDLDSLKEFV 102
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 43-146 1.19e-57

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: 184.03  E-value: 1.19e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  43 HARHLYSAEMLRHGAVAaPHFVMFFAPWCGHCQRLQPTWNDLGDKYNNmENPQVYVVKVDCTADTPLCSEFGVRGYPTLK 122
Cdd:cd03005   1 GVLELTEDNFDHHIAEG-NHFVKFFAPWCGHCKRLAPTWEQLAKKFNN-ENPSVKIAKVDCTQHRELCSEFQVRGYPTLL 78

                        90       100
                ....*....|....*....|....
gi 53135337 123 LLKPGQEPLKYQGPRDFQALENWM 146
Cdd:cd03005  79 LFKDGEKVDKYKGTRDLDSLKEFV 102
 
Name Accession Description Interval E-value
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 172-272 1.78e-66

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: 206.75  E-value: 1.78e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 172 GMYELSADNFKTHIAEGNHFIKFFAPWCGHCKALAPTWEQLALAFEH-SETVKIGKVDCTQHYEVCSENQVRGYPTLLWF 250
Cdd:cd03005   1 GVLELTEDNFDHHIAEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFNNeNPSVKIAKVDCTQHRELCSEFQVRGYPTLLLF 80

                        90       100
                ....*....|....*....|..
gi 53135337 251 RNGEKGDQYKGKRDFDSLKEYV 272
Cdd:cd03005  81 KDGEKVDKYKGTRDLDSLKEFV 102
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 305-406 1.33e-62

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: 196.74  E-value: 1.33e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 305 AVLSLSEKDFDETIARGITFIKFYAPWCGHCKNLAPTWEILAKEQFPGLTDVKIAEVDCTVERNVCNRFSVRGYPTLLLF 384
Cdd:cd03005   1 GVLELTEDNFDHHIAEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFNNENPSVKIAKVDCTQHRELCSEFQVRGYPTLLLF 80

                        90       100
                ....*....|....*....|..
gi 53135337 385 RGGKKVSEHNGTRDLESLHSFV 406
Cdd:cd03005  81 KDGEKVDKYKGTRDLDSLKEFV 102
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 43-146 1.19e-57

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: 184.03  E-value: 1.19e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  43 HARHLYSAEMLRHGAVAaPHFVMFFAPWCGHCQRLQPTWNDLGDKYNNmENPQVYVVKVDCTADTPLCSEFGVRGYPTLK 122
Cdd:cd03005   1 GVLELTEDNFDHHIAEG-NHFVKFFAPWCGHCKRLAPTWEQLAKKFNN-ENPSVKIAKVDCTQHRELCSEFQVRGYPTLL 78

                        90       100
                ....*....|....*....|....
gi 53135337 123 LLKPGQEPLKYQGPRDFQALENWM 146
Cdd:cd03005  79 LFKDGEKVDKYKGTRDLDSLKEFV 102
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 64-414 2.32e-47

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: 168.31  E-value: 2.32e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337    64 VMFFAPWCGHCQRLQPTWNDLGDKYNNmENPQVYVVKVDCTADTPLCSEFGVRGYPTLKLLKPG-QEPLKYQGPRDFQAL 142
Cdd:TIGR01130  23 VEFYAPWCGHCKSLAPEYEKAADELKK-KGPPIKLAKVDATEEKDLAQKYGVSGYPTLKIFRNGeDSVSDYNGPRDADGI 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   143 ENWM----------------LEKL-----------------------------------------------NGEPSDPES 159
Cdd:TIGR01130 102 VKYMkkqsgpavkeietvadLEAFladddvvvigffkdldselndtflsvaeklrdvyfffahssdvaafaKLGAFPDSV 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   160 AVEPPKAPEPKQGMYELSADN---------------------------------FKTHIAEGNHFIKFFAPWCGHCKALA 206
Cdd:TIGR01130 182 VLFKPKDEDEKFSKVDGEMDTdvsdlekfiraeslplvgeftqetaakyfesgpLVVLYYNVDESLDPFEELRNRFLEAA 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   207 PTWEQLALAFEHSETVKIGKVdcTQHYEVcsenQVRGYPTLLWFrNGEKGDQYK---GKRDFDSLKEYVDSQLqnSGKEP 283
Cdd:TIGR01130 262 KKFRGKFVNFAVADEEDFGRE--LEYFGL----KAEKFPAVAIQ-DLEGNKKYPmdqEEFSSENLEAFVKDFL--DGKLK 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   284 PASKPTEAPQppaeptqAEQAAVLSLSEKDFDETIARGI--TFIKFYAPWCGHCKNLAPTWEILAKEQFPGLTDVKIAEV 361
Cdd:TIGR01130 333 PYLKSEPIPE-------DDEGPVKVLVGKNFDEIVLDETkdVLVEFYAPWCGHCKNLAPIYEELAEKYKDAESDVVIAKM 405

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 53135337   362 DCTveRNVCNRFSVRGYPTLLLFRGGKKVS--EHNGTRDLESLHSFVLRQARDEL 414
Cdd:TIGR01130 406 DAT--ANDVPPFEVEGFPTIKFVPAGKKSEpvPYDGDRTLEDFSKFIAKHATFPL 458
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 309-410 2.29e-38

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


Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 133.95  E-value: 2.29e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   309 LSEKDFDETIARG-ITFIKFYAPWCGHCKNLAPTWEILAKEqFPGLTDVKIAEVDCTVERNVCNRFSVRGYPTLLLFRGG 387
Cdd:TIGR01126   1 LTASNFDEIVLSNkDVLVEFYAPWCGHCKNLAPEYEKLAKE-LKKDPKIVLAKVDATAEKDLASRFGVSGFPTIKFFPKG 79

                          90       100
                  ....*....|....*....|...
gi 53135337   388 KKVSEHNGTRDLESLHSFVLRQA 410
Cdd:TIGR01126  80 SKPVDYEGGRDLEAIVEFVNEKS 102
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 63-149 9.74e-34

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


Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 121.63  E-value: 9.74e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337    63 FVMFFAPWCGHCQRLQPTWNDLGDKYNnmENPQVYVVKVDCTADTPLCSEFGVRGYPTLKLLKPGQEPLKYQGPRDFQAL 142
Cdd:TIGR01126  17 LVEFYAPWCGHCKNLAPEYEKLAKELK--KDPKIVLAKVDATAEKDLASRFGVSGFPTIKFFPKGSKPVDYEGGRDLEAI 94


                  ....*..
gi 53135337   143 ENWMLEK 149
Cdd:TIGR01126  95 VEFVNEK 101
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 64-406 3.03e-29

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 118.70  E-value: 3.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   64 VMFFAPWCGHCQRLQPTWNdlgdKYNNM---ENPQVYVVKVDCTADTPLCSEFGVRGYPTLKLLKpGQEPLKYQGPRDFQ 140
Cdd:PTZ00102  54 VKFYAPWCGHCKRLAPEYK----KAAKMlkeKKSEIVLASVDATEEMELAQEFGVRGYPTIKFFN-KGNPVNYSGGRTAD 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  141 ALENWmLEKLNG----EPSDPESAVEPPKAPEPKQGMYELSADN--FKTHIAEGN----HFiKFFA-PWCGHCKA-LAPT 208
Cdd:PTZ00102 129 GIVSW-IKKLTGpavtEVESASEIKLIAKKIFVAFYGEYTSKDSelYKKFEEVADkhreHA-KFFVkKHEGKNKIyVLHK 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  209 WEQLALAFEHSETVKIGKVDCTQHY----EVCSENQVRgYPT----LLWFRNGEKG------------------------ 256
Cdd:PTZ00102 207 DEEGVELFMGKTKEELEEFVSTESFplfaEINAENYRR-YISsgkdLVWFCGTTEDydkyksvvrkvarklrekyafvwl 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  257 --DQYKGK-------------------------------RDFDSLKEYVDSqlQNSGKEPPASKpteapqppAEPTQAEQ 303
Cdd:PTZ00102 286 dtEQFGSHakehllieefpglayqspagryllppakesfDSVEALIEFFKD--VEAGKVEKSIK--------SEPIPEEQ 355

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  304 -AAVLSLSEKDFDETIARGI--TFIKFYAPWCGHCKNLAPTWEILAkEQFPGLTDVKIAEVDCTVERNVCNRFSVRGYPT 380
Cdd:PTZ00102 356 dGPVKVVVGNTFEEIVFKSDkdVLLEIYAPWCGHCKNLEPVYNELG-EKYKDNDSIIVAKMNGTANETPLEEFSWSAFPT 434

                        410       420
                 ....*....|....*....|....*..
gi 53135337  381 LLLFRGGKKVS-EHNGTRDLESLHSFV 406
Cdd:PTZ00102 435 ILFVKAGERTPiPYEGERTVEGFKEFV 461
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 175-274 3.39e-29

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: 109.63  E-value: 3.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   175 ELSADNFKTHIAEGN--HFIKFFAPWCGHCKALAPTWEqlALAFEHSETVKIGKVDCTQHYEVCSENQVRGYPTLLWFRN 252
Cdd:pfam00085   4 VLTDANFDEVVQKSSkpVLVDFYAPWCGPCKMLAPEYE--ELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKN 81

                          90       100
                  ....*....|....*....|..
gi 53135337   253 GEKGDQYKGKRDFDSLKEYVDS 274
Cdd:pfam00085  82 GQPVDDYVGARPKDALAAFLKA 103
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 306-406 7.98e-29

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: 108.47  E-value: 7.98e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   306 VLSLSEKDFDETIARGITF--IKFYAPWCGHCKNLAPTWEILAKEqFPGltDVKIAEVDCTVERNVCNRFSVRGYPTLLL 383
Cdd:pfam00085   2 VVVLTDANFDEVVQKSSKPvlVDFYAPWCGPCKMLAPEYEELAQE-YKG--NVVFAKVDVDENPDLASKYGVRGYPTLIF 78

                          90       100
                  ....*....|....*....|...
gi 53135337   384 FRGGKKVSEHNGTRDLESLHSFV 406
Cdd:pfam00085  79 FKNGQPVDDYVGARPKDALAAFL 101
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 302-407 4.62e-26

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 104.71  E-value: 4.62e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  302 EQAAVLSLSEKDFDETI------ARGITFIKFYAPWCGHCKNLAPTWEILAKEqFPGLtdVKIAEVDCTVERNVCNRFSV 375
Cdd:PTZ00443  28 DANALVLLNDKNFEKLTqastgaTTGPWFVKFYAPWCSHCRKMAPAWERLAKA-LKGQ--VNVADLDATRALNLAKRFAI 104

                         90       100       110
                 ....*....|....*....|....*....|..
gi 53135337  376 RGYPTLLLFRGGKKVSEHNGTRDLESLHSFVL 407
Cdd:PTZ00443 105 KGYPTLLLFDKGKMYQYEGGDRSTEKLAAFAL 136
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 61-148 1.03e-25

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: 100.00  E-value: 1.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337    61 PHFVMFFAPWCGHCQRLQPTWNDLGDKYNNmenpQVYVVKVDCTADTPLCSEFGVRGYPTLKLLKPGQEPLKYQGPRDFQ 140
Cdd:pfam00085  20 PVLVDFYAPWCGPCKMLAPEYEELAQEYKG----NVVFAKVDVDENPDLASKYGVRGYPTLIFFKNGQPVDDYVGARPKD 95


                  ....*...
gi 53135337   141 ALENWMLE 148
Cdd:pfam00085  96 ALAAFLKA 103
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 173-276 9.28e-23

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: 92.19  E-value: 9.28e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 173 MYELSADNFKTHIAEGNH--FIKFFAPWCGHCKALAPTWEQLALafEHSETVKIGKVDCTQHYEVCSENQVRGYPTLLWF 250
Cdd:COG3118   2 VVELTDENFEEEVLESDKpvLVDFWAPWCGPCKMLAPVLEELAA--EYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLF 79

                        90       100
                ....*....|....*....|....*.
gi 53135337 251 RNGEKGDQYKGKRDFDSLKEYVDSQL 276
Cdd:COG3118  80 KDGQPVDRFVGALPKEQLREFLDKVL 105
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 305-406 2.26e-22

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


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 91.03  E-value: 2.26e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 305 AVLSLSEKDFDETI--ARGITFIKFYAPWCGHCKNLAPTWEILAKEqFPGltDVKIAEVDCTVERNVCNRFSVRGYPTLL 382
Cdd:COG3118   1 AVVELTDENFEEEVleSDKPVLVDFWAPWCGPCKMLAPVLEELAAE-YGG--KVKFVKVDVDENPELAAQFGVRSIPTLL 77

                        90       100
                ....*....|....*....|....
gi 53135337 383 LFRGGKKVSEHNGTRDLESLHSFV 406
Cdd:COG3118  78 LFKDGQPVDRFVGALPKEQLREFL 101
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 61-150 1.31e-17

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: 77.94  E-value: 1.31e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  61 PHFVMFFAPWCGHCQRLQPTWNDLGDKYNnmenPQVYVVKVDCTADTPLCSEFGVRGYPTLKLLKPGQEPLKYQGPRDFQ 140
Cdd:COG3118  20 PVLVDFWAPWCGPCKMLAPVLEELAAEYG----GKVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQPVDRFVGALPKE 95

                        90
                ....*....|
gi 53135337 141 ALENWmLEKL 150
Cdd:COG3118  96 QLREF-LDKV 104
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 56-187 7.44e-14

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 70.42  E-value: 7.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   56 GAVAAPHFVMFFAPWCGHCQRLQPTWNDLGDKYNNmenpQVYVVKVDCTADTPLCSEFGVRGYPTLKLLKPGQEPLKYQG 135
Cdd:PTZ00443  49 GATTGPWFVKFYAPWCSHCRKMAPAWERLAKALKG----QVNVADLDATRALNLAKRFAIKGYPTLLLFDKGKMYQYEGG 124

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 53135337  136 PRDFQALENWMLeklngepSDPESAVEPPkAPEPKQgMYELSADNFKTHIAE 187
Cdd:PTZ00443 125 DRSTEKLAAFAL-------GDFKKALGAP-VPAPLS-FFALTIDFFVSGTNE 167
 
Name Accession Description Interval E-value
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 172-272 1.78e-66

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: 206.75  E-value: 1.78e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 172 GMYELSADNFKTHIAEGNHFIKFFAPWCGHCKALAPTWEQLALAFEH-SETVKIGKVDCTQHYEVCSENQVRGYPTLLWF 250
Cdd:cd03005   1 GVLELTEDNFDHHIAEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFNNeNPSVKIAKVDCTQHRELCSEFQVRGYPTLLLF 80

                        90       100
                ....*....|....*....|..
gi 53135337 251 RNGEKGDQYKGKRDFDSLKEYV 272
Cdd:cd03005  81 KDGEKVDKYKGTRDLDSLKEFV 102
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 305-406 1.33e-62

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: 196.74  E-value: 1.33e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 305 AVLSLSEKDFDETIARGITFIKFYAPWCGHCKNLAPTWEILAKEQFPGLTDVKIAEVDCTVERNVCNRFSVRGYPTLLLF 384
Cdd:cd03005   1 GVLELTEDNFDHHIAEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFNNENPSVKIAKVDCTQHRELCSEFQVRGYPTLLLF 80

                        90       100
                ....*....|....*....|..
gi 53135337 385 RGGKKVSEHNGTRDLESLHSFV 406
Cdd:cd03005  81 KDGEKVDKYKGTRDLDSLKEFV 102
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 43-146 1.19e-57

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: 184.03  E-value: 1.19e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  43 HARHLYSAEMLRHGAVAaPHFVMFFAPWCGHCQRLQPTWNDLGDKYNNmENPQVYVVKVDCTADTPLCSEFGVRGYPTLK 122
Cdd:cd03005   1 GVLELTEDNFDHHIAEG-NHFVKFFAPWCGHCKRLAPTWEQLAKKFNN-ENPSVKIAKVDCTQHRELCSEFQVRGYPTLL 78

                        90       100
                ....*....|....*....|....
gi 53135337 123 LLKPGQEPLKYQGPRDFQALENWM 146
Cdd:cd03005  79 LFKDGEKVDKYKGTRDLDSLKEFV 102
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 64-414 2.32e-47

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: 168.31  E-value: 2.32e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337    64 VMFFAPWCGHCQRLQPTWNDLGDKYNNmENPQVYVVKVDCTADTPLCSEFGVRGYPTLKLLKPG-QEPLKYQGPRDFQAL 142
Cdd:TIGR01130  23 VEFYAPWCGHCKSLAPEYEKAADELKK-KGPPIKLAKVDATEEKDLAQKYGVSGYPTLKIFRNGeDSVSDYNGPRDADGI 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   143 ENWM----------------LEKL-----------------------------------------------NGEPSDPES 159
Cdd:TIGR01130 102 VKYMkkqsgpavkeietvadLEAFladddvvvigffkdldselndtflsvaeklrdvyfffahssdvaafaKLGAFPDSV 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   160 AVEPPKAPEPKQGMYELSADN---------------------------------FKTHIAEGNHFIKFFAPWCGHCKALA 206
Cdd:TIGR01130 182 VLFKPKDEDEKFSKVDGEMDTdvsdlekfiraeslplvgeftqetaakyfesgpLVVLYYNVDESLDPFEELRNRFLEAA 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   207 PTWEQLALAFEHSETVKIGKVdcTQHYEVcsenQVRGYPTLLWFrNGEKGDQYK---GKRDFDSLKEYVDSQLqnSGKEP 283
Cdd:TIGR01130 262 KKFRGKFVNFAVADEEDFGRE--LEYFGL----KAEKFPAVAIQ-DLEGNKKYPmdqEEFSSENLEAFVKDFL--DGKLK 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   284 PASKPTEAPQppaeptqAEQAAVLSLSEKDFDETIARGI--TFIKFYAPWCGHCKNLAPTWEILAKEQFPGLTDVKIAEV 361
Cdd:TIGR01130 333 PYLKSEPIPE-------DDEGPVKVLVGKNFDEIVLDETkdVLVEFYAPWCGHCKNLAPIYEELAEKYKDAESDVVIAKM 405

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 53135337   362 DCTveRNVCNRFSVRGYPTLLLFRGGKKVS--EHNGTRDLESLHSFVLRQARDEL 414
Cdd:TIGR01130 406 DAT--ANDVPPFEVEGFPTIKFVPAGKKSEpvPYDGDRTLEDFSKFIAKHATFPL 458
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 175-272 1.03e-41

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: 142.36  E-value: 1.03e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 175 ELSADNFKTHIAEGNH-FIKFFAPWCGHCKALAPTWEQLALAFEHSETVKIGKVDCTQHYEVCSENQVRGYPTLLWFRNG 253
Cdd:cd02961   2 ELTDDNFDELVKDSKDvLVEFYAPWCGHCKALAPEYEKLAKELKGDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPNG 81

                        90       100
                ....*....|....*....|
gi 53135337 254 -EKGDQYKGKRDFDSLKEYV 272
Cdd:cd02961  82 sKEPVKYEGPRTLESLVEFI 101
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 176-275 5.14e-40

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


Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 138.19  E-value: 5.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   176 LSADNFKTHIAEGNH-FIKFFAPWCGHCKALAPTWEQLALAFEHSETVKIGKVDCTQHYEVCSENQVRGYPTLLWFRNGE 254
Cdd:TIGR01126   1 LTASNFDEIVLSNKDvLVEFYAPWCGHCKNLAPEYEKLAKELKKDPKIVLAKVDATAEKDLASRFGVSGFPTIKFFPKGS 80

                          90       100
                  ....*....|....*....|.
gi 53135337   255 KGDQYKGKRDFDSLKEYVDSQ 275
Cdd:TIGR01126  81 KPVDYEGGRDLEAIVEFVNEK 101
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 307-406 2.24e-38

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: 133.89  E-value: 2.24e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 307 LSLSEKDFDETIARG-ITFIKFYAPWCGHCKNLAPTWEILAKEqFPGLTDVKIAEVDCTVERNVCNRFSVRGYPTLLLFR 385
Cdd:cd02961   1 VELTDDNFDELVKDSkDVLVEFYAPWCGHCKALAPEYEKLAKE-LKGDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFP 79

                        90       100
                ....*....|....*....|..
gi 53135337 386 GG-KKVSEHNGTRDLESLHSFV 406
Cdd:cd02961  80 NGsKEPVKYEGPRTLESLVEFI 101
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 309-410 2.29e-38

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


Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 133.95  E-value: 2.29e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   309 LSEKDFDETIARG-ITFIKFYAPWCGHCKNLAPTWEILAKEqFPGLTDVKIAEVDCTVERNVCNRFSVRGYPTLLLFRGG 387
Cdd:TIGR01126   1 LTASNFDEIVLSNkDVLVEFYAPWCGHCKNLAPEYEKLAKE-LKKDPKIVLAKVDATAEKDLASRFGVSGFPTIKFFPKG 79

                          90       100
                  ....*....|....*....|...
gi 53135337   388 KKVSEHNGTRDLESLHSFVLRQA 410
Cdd:TIGR01126  80 SKPVDYEGGRDLEAIVEFVNEKS 102
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 61-146 1.19e-35

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


Pssm-ID: 239259 [Multi-domain]  Cd Length: 101  Bit Score: 126.57  E-value: 1.19e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  61 PHFVMFFAPWCGHCQRLQPTWNDLGDKYNNmeNPQVYVVKVDCTADTPLCSEFGVRGYPTLKLLKPG-QEPLKYQGPRDF 139
Cdd:cd02961  17 DVLVEFYAPWCGHCKALAPEYEKLAKELKG--DGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPNGsKEPVKYEGPRTL 94


                ....*..
gi 53135337 140 QALENWM 146
Cdd:cd02961  95 ESLVEFI 101
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 63-149 9.74e-34

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


Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 121.63  E-value: 9.74e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337    63 FVMFFAPWCGHCQRLQPTWNDLGDKYNnmENPQVYVVKVDCTADTPLCSEFGVRGYPTLKLLKPGQEPLKYQGPRDFQAL 142
Cdd:TIGR01126  17 LVEFYAPWCGHCKNLAPEYEKLAKELK--KDPKIVLAKVDATAEKDLASRFGVSGFPTIKFFPKGSKPVDYEGGRDLEAI 94


                  ....*..
gi 53135337   143 ENWMLEK 149
Cdd:TIGR01126  95 VEFVNEK 101
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 175-272 1.38e-33

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: 121.20  E-value: 1.38e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 175 ELSADNFKTHIAEG--NHFIKFFAPWCGHCKALAPTWEQLALAFEHSETVKIGKVDCTQ-HYEVCSENQVRGYPTLLWFR 251
Cdd:cd02998   4 ELTDSNFDKVVGDDkkDVLVEFYAPWCGHCKNLAPEYEKLAAVFANEDDVVIAKVDADEaNKDLAKKYGVSGFPTLKFFP 83

                        90       100
                ....*....|....*....|..
gi 53135337 252 NG-EKGDQYKGKRDFDSLKEYV 272
Cdd:cd02998  84 KGsTEPVKYEGGRDLEDLVKFV 105
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 305-406 4.55e-32

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: 117.35  E-value: 4.55e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 305 AVLSLSEKDFDETI--ARGITFIKFYAPWCGHCKNLAPTWEILAKEqFPGLTDVKIAEVDCTVE-RNVCNRFSVRGYPTL 381
Cdd:cd02998   1 NVVELTDSNFDKVVgdDKKDVLVEFYAPWCGHCKNLAPEYEKLAAV-FANEDDVVIAKVDADEAnKDLAKKYGVSGFPTL 79

                        90       100
                ....*....|....*....|....*.
gi 53135337 382 LLF-RGGKKVSEHNGTRDLESLHSFV 406
Cdd:cd02998  80 KFFpKGSTEPVKYEGGRDLEDLVKFV 105
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 175-292 5.44e-32

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: 126.33  E-value: 5.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   175 ELSADNFKTHIAEGNHFI-KFFAPWCGHCKALAPTWEQLA--LAfEHSETVKIGKVDCTQHYEVCSENQVRGYPTLLWFR 251
Cdd:TIGR01130   5 VLTKDNFDDFIKSHEFVLvEFYAPWCGHCKSLAPEYEKAAdeLK-KKGPPIKLAKVDATEEKDLAQKYGVSGYPTLKIFR 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 53135337   252 NGEKGDQ-YKGKRDFDSLKEYVDSQLQnsgkepPASKPTEAP 292
Cdd:TIGR01130  84 NGEDSVSdYNGPRDADGIVKYMKKQSG------PAVKEIETV 119
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 305-410 5.69e-31

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: 123.25  E-value: 5.69e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   305 AVLSLSEKDFDETIARG-ITFIKFYAPWCGHCKNLAPTWEILA---KEQFPgltDVKIAEVDCTVERNVCNRFSVRGYPT 380
Cdd:TIGR01130   2 DVLVLTKDNFDDFIKSHeFVLVEFYAPWCGHCKSLAPEYEKAAdelKKKGP---PIKLAKVDATEEKDLAQKYGVSGYPT 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 53135337   381 LLLFRGGKK-VSEHNGTRDLESLHSFVLRQA 410
Cdd:TIGR01130  79 LKIFRNGEDsVSDYNGPRDADGIVKYMKKQS 109
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 64-406 3.03e-29

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 118.70  E-value: 3.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   64 VMFFAPWCGHCQRLQPTWNdlgdKYNNM---ENPQVYVVKVDCTADTPLCSEFGVRGYPTLKLLKpGQEPLKYQGPRDFQ 140
Cdd:PTZ00102  54 VKFYAPWCGHCKRLAPEYK----KAAKMlkeKKSEIVLASVDATEEMELAQEFGVRGYPTIKFFN-KGNPVNYSGGRTAD 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  141 ALENWmLEKLNG----EPSDPESAVEPPKAPEPKQGMYELSADN--FKTHIAEGN----HFiKFFA-PWCGHCKA-LAPT 208
Cdd:PTZ00102 129 GIVSW-IKKLTGpavtEVESASEIKLIAKKIFVAFYGEYTSKDSelYKKFEEVADkhreHA-KFFVkKHEGKNKIyVLHK 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  209 WEQLALAFEHSETVKIGKVDCTQHY----EVCSENQVRgYPT----LLWFRNGEKG------------------------ 256
Cdd:PTZ00102 207 DEEGVELFMGKTKEELEEFVSTESFplfaEINAENYRR-YISsgkdLVWFCGTTEDydkyksvvrkvarklrekyafvwl 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  257 --DQYKGK-------------------------------RDFDSLKEYVDSqlQNSGKEPPASKpteapqppAEPTQAEQ 303
Cdd:PTZ00102 286 dtEQFGSHakehllieefpglayqspagryllppakesfDSVEALIEFFKD--VEAGKVEKSIK--------SEPIPEEQ 355

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  304 -AAVLSLSEKDFDETIARGI--TFIKFYAPWCGHCKNLAPTWEILAkEQFPGLTDVKIAEVDCTVERNVCNRFSVRGYPT 380
Cdd:PTZ00102 356 dGPVKVVVGNTFEEIVFKSDkdVLLEIYAPWCGHCKNLEPVYNELG-EKYKDNDSIIVAKMNGTANETPLEEFSWSAFPT 434

                        410       420
                 ....*....|....*....|....*..
gi 53135337  381 LLLFRGGKKVS-EHNGTRDLESLHSFV 406
Cdd:PTZ00102 435 ILFVKAGERTPiPYEGERTVEGFKEFV 461
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 175-274 3.39e-29

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: 109.63  E-value: 3.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   175 ELSADNFKTHIAEGN--HFIKFFAPWCGHCKALAPTWEqlALAFEHSETVKIGKVDCTQHYEVCSENQVRGYPTLLWFRN 252
Cdd:pfam00085   4 VLTDANFDEVVQKSSkpVLVDFYAPWCGPCKMLAPEYE--ELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKN 81

                          90       100
                  ....*....|....*....|..
gi 53135337   253 GEKGDQYKGKRDFDSLKEYVDS 274
Cdd:pfam00085  82 GQPVDDYVGARPKDALAAFLKA 103
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 306-406 7.98e-29

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: 108.47  E-value: 7.98e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   306 VLSLSEKDFDETIARGITF--IKFYAPWCGHCKNLAPTWEILAKEqFPGltDVKIAEVDCTVERNVCNRFSVRGYPTLLL 383
Cdd:pfam00085   2 VVVLTDANFDEVVQKSSKPvlVDFYAPWCGPCKMLAPEYEELAQE-YKG--NVVFAKVDVDENPDLASKYGVRGYPTLIF 78

                          90       100
                  ....*....|....*....|...
gi 53135337   384 FRGGKKVSEHNGTRDLESLHSFV 406
Cdd:pfam00085  79 FKNGQPVDDYVGARPKDALAAFL 101
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 306-407 2.27e-26

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: 102.06  E-value: 2.27e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 306 VLSLSEKDFDETIARG--ITFIKFYAPWCGHCKNLAPTWEILAKEqFPGLTDVkiAEVDCTVERN--VCNRFSVRGYPTL 381
Cdd:cd03002   2 VYELTPKNFDKVVHNTnyTTLVEFYAPWCGHCKNLKPEYAKAAKE-LDGLVQV--AAVDCDEDKNkpLCGKYGVQGFPTL 78

                        90       100       110
                ....*....|....*....|....*....|.
gi 53135337 382 LLFRGGKKVSEH-----NGTRDLESLHSFVL 407
Cdd:cd03002  79 KVFRPPKKASKHavedyNGERSAKAIVDFVL 109
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 302-407 4.62e-26

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 104.71  E-value: 4.62e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  302 EQAAVLSLSEKDFDETI------ARGITFIKFYAPWCGHCKNLAPTWEILAKEqFPGLtdVKIAEVDCTVERNVCNRFSV 375
Cdd:PTZ00443  28 DANALVLLNDKNFEKLTqastgaTTGPWFVKFYAPWCSHCRKMAPAWERLAKA-LKGQ--VNVADLDATRALNLAKRFAI 104

                         90       100       110
                 ....*....|....*....|....*....|..
gi 53135337  376 RGYPTLLLFRGGKKVSEHNGTRDLESLHSFVL 407
Cdd:PTZ00443 105 KGYPTLLLFDKGKMYQYEGGDRSTEKLAAFAL 136
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 174-272 5.03e-26

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: 101.09  E-value: 5.03e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 174 YELSADNFKTHIAEG--NHFIKFFAPWCGHCKALAPTWEQLALAFEHSETVKIGKVDCTQHyEVCSENQVRGYPTLLWFR 251
Cdd:cd02995   3 KVVVGKNFDEVVLDSdkDVLVEFYAPWCGHCKALAPIYEELAEKLKGDDNVVIAKMDATAN-DVPSEFVVDGFPTILFFP 81

                        90       100
                ....*....|....*....|...
gi 53135337 252 NGEKGD--QYKGKRDFDSLKEYV 272
Cdd:cd02995  82 AGDKSNpiKYEGDRTLEDLIKFI 104
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 61-148 1.03e-25

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: 100.00  E-value: 1.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337    61 PHFVMFFAPWCGHCQRLQPTWNDLGDKYNNmenpQVYVVKVDCTADTPLCSEFGVRGYPTLKLLKPGQEPLKYQGPRDFQ 140
Cdd:pfam00085  20 PVLVDFYAPWCGPCKMLAPEYEELAQEYKG----NVVFAKVDVDENPDLASKYGVRGYPTLIFFKNGQPVDDYVGARPKD 95


                  ....*...
gi 53135337   141 ALENWMLE 148
Cdd:pfam00085  96 ALAAFLKA 103
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 63-145 6.15e-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: 98.09  E-value: 6.15e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  63 FVMFFAPWCGHCQRLQPTWNDLGDKYNNmeNPQVYVVKVDCTAD-TPLCSEFGVRGYPTLKLLKPG-QEPLKYQGPRDFQ 140
Cdd:cd02998  22 LVEFYAPWCGHCKNLAPEYEKLAAVFAN--EDDVVIAKVDADEAnKDLAKKYGVSGFPTLKFFPKGsTEPVKYEGGRDLE 99


                ....*
gi 53135337 141 ALENW 145
Cdd:cd02998 100 DLVKF 104
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 305-406 1.04e-24

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 105.60  E-value: 1.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  305 AVLSLSEKDFDETIARG-ITFIKFYAPWCGHCKNLAPTWEILAKEQFPGLTDVKIAEVDCTVERNVCNRFSVRGYPTLLL 383
Cdd:PTZ00102  33 HVTVLTDSTFDKFITENeIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSEIVLASVDATEEMELAQEFGVRGYPTIKF 112

                         90       100
                 ....*....|....*....|...
gi 53135337  384 FRGGKKVsEHNGTRDLESLHSFV 406
Cdd:PTZ00102 113 FNKGNPV-NYSGGRTADGIVSWI 134
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 324-406 1.53e-24

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: 96.86  E-value: 1.53e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 324 FIKFYAPWCGHCKNLAPTWEILAKEqFPGLTDVKIAEVDCTveRN-VCNRFSVRGYPTLLLFRGGKK--VSEHNGTRDLE 400
Cdd:cd02995  22 LVEFYAPWCGHCKALAPIYEELAEK-LKGDDNVVIAKMDAT--ANdVPSEFVVDGFPTILFFPAGDKsnPIKYEGDRTLE 98


                ....*.
gi 53135337 401 SLHSFV 406
Cdd:cd02995  99 DLIKFI 104
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 305-407 2.63e-24

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: 96.20  E-value: 2.63e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 305 AVLSLSEKDFDETI--ARGITFIKFYAPWCGHCKNLAPTWEILAKEqFPGLtdVKIAEVDCTVERNVCNRFSVRGYPTLL 382
Cdd:cd03001   1 DVVELTDSNFDKKVlnSDDVWLVEFYAPWCGHCKNLAPEWKKAAKA-LKGI--VKVGAVDADVHQSLAQQYGVRGFPTIK 77

                        90       100
                ....*....|....*....|....*.
gi 53135337 383 LFRGGKKVS-EHNGTRDLESLHSFVL 407
Cdd:cd03001  78 VFGAGKNSPqDYQGGRTAKAIVSAAL 103
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 111-292 1.12e-23

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: 102.45  E-value: 1.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   111 SEFGV--RGYPTLKLLKpGQEPLKY---QGPRDFQALENWMLEKLNG--EP---SDPesaveppkAPEPKQG-MYELSAD 179
Cdd:TIGR01130 284 EYFGLkaEKFPAVAIQD-LEGNKKYpmdQEEFSSENLEAFVKDFLDGklKPylkSEP--------IPEDDEGpVKVLVGK 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   180 NFKTHI--AEGNHFIKFFAPWCGHCKALAPTWEQLALAFEHSET-VKIGKVDCTQHyEVcSENQVRGYPTLLWFRNGEKG 256
Cdd:TIGR01130 355 NFDEIVldETKDVLVEFYAPWCGHCKNLAPIYEELAEKYKDAESdVVIAKMDATAN-DV-PPFEVEGFPTIKFVPAGKKS 432

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 53135337   257 D--QYKGKRDFDSLKEYVDSQlqnsgkeppASKPTEAP 292
Cdd:TIGR01130 433 EpvPYDGDRTLEDFSKFIAKH---------ATFPLEGK 461
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 63-146 2.19e-23

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


Pssm-ID: 239293 [Multi-domain]  Cd Length: 104  Bit Score: 93.78  E-value: 2.19e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  63 FVMFFAPWCGHCQRLQPTWNDLGDKYNNMENpqVYVVKVDCTA-DTPlcSEFGVRGYPTLKLLKPG--QEPLKYQGPRDF 139
Cdd:cd02995  22 LVEFYAPWCGHCKALAPIYEELAEKLKGDDN--VVIAKMDATAnDVP--SEFVVDGFPTILFFPAGdkSNPIKYEGDRTL 97


                ....*..
gi 53135337 140 QALENWM 146
Cdd:cd02995  98 EDLIKFI 104
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 63-137 2.75e-23

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: 93.67  E-value: 2.75e-23
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53135337  63 FVMFFAPWCGHCQRLQPTWNDLGDKYNNMENPqVYVVKVDCTADTPLCSEFGVRGYPTLKLLKpGQEPLKYQGPR 137
Cdd:cd03000  19 LVDFYAPWCGHCKKLEPVWNEVGAELKSSGSP-VRVGKLDATAYSSIASEFGVRGYPTIKLLK-GDLAYNYRGPR 91
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 63-147 3.00e-23

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: 93.51  E-value: 3.00e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  63 FVMFFAPWCGHCQRLQPTWndlgDKYNNMENPQVYVVKVDCTADTPLCSEFGVRGYPTLKLLKPGQE-PLKYQGPRDFQA 141
Cdd:cd03001  22 LVEFYAPWCGHCKNLAPEW----KKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVFGAGKNsPQDYQGGRTAKA 97


                ....*.
gi 53135337 142 LENWML 147
Cdd:cd03001  98 IVSAAL 103
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 305-410 5.00e-23

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: 92.90  E-value: 5.00e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 305 AVLSLSEKdFDETIARGITFIKFYAPWCGHCKNLAPTWEILAKEQFPGLTDVKIAEVDCTVERNVCNRFSVRGYPTLLLF 384
Cdd:cd03000   1 LVLDLDDS-FKDVRKEDIWLVDFYAPWCGHCKKLEPVWNEVGAELKSSGSPVRVGKLDATAYSSIASEFGVRGYPTIKLL 79

                        90       100
                ....*....|....*....|....*.
gi 53135337 385 RGGkKVSEHNGTRDLESLHSFVLRQA 410
Cdd:cd03000  80 KGD-LAYNYRGPRTKDDIVEFANRVA 104
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 173-276 9.28e-23

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: 92.19  E-value: 9.28e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 173 MYELSADNFKTHIAEGNH--FIKFFAPWCGHCKALAPTWEQLALafEHSETVKIGKVDCTQHYEVCSENQVRGYPTLLWF 250
Cdd:COG3118   2 VVELTDENFEEEVLESDKpvLVDFWAPWCGPCKMLAPVLEELAA--EYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLF 79

                        90       100
                ....*....|....*....|....*.
gi 53135337 251 RNGEKGDQYKGKRDFDSLKEYVDSQL 276
Cdd:COG3118  80 KDGQPVDRFVGALPKEQLREFLDKVL 105
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 175-268 1.18e-22

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: 91.58  E-value: 1.18e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 175 ELSADNFKTHIAEGNH--FIKFFAPWCGHCKALAPTWEQLALAFEhsETVKIGKVDCTQHYEVCSENQVRGYPTLLWFRN 252
Cdd:cd03001   4 ELTDSNFDKKVLNSDDvwLVEFYAPWCGHCKNLAPEWKKAAKALK--GIVKVGAVDADVHQSLAQQYGVRGFPTIKVFGA 81

                        90
                ....*....|....*..
gi 53135337 253 G-EKGDQYKGKRDFDSL 268
Cdd:cd03001  82 GkNSPQDYQGGRTAKAI 98
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 179-271 1.28e-22

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: 91.75  E-value: 1.28e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 179 DNFKTHIAEGNHFIKFFAPWCGHCKALAPTWEQLALAFEHSET-VKIGKVDCTQHYEVCSENQVRGYPTLLWFRNGEKGD 257
Cdd:cd03000   7 DSFKDVRKEDIWLVDFYAPWCGHCKKLEPVWNEVGAELKSSGSpVRVGKLDATAYSSIASEFGVRGYPTIKLLKGDLAYN 86

                        90
                ....*....|....
gi 53135337 258 qYKGKRDFDSLKEY 271
Cdd:cd03000  87 -YRGPRTKDDIVEF 99
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 175-272 1.60e-22

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: 91.20  E-value: 1.60e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 175 ELSADNFKTHIAEGNHF--IKFFAPWCGHCKALAPTWEQLALAFEHseTVKIGKVDCTQHYEVCSENQVRGYPTL-LWFR 251
Cdd:cd03004   5 TLTPEDFPELVLNRKEPwlVDFYAPWCGPCQALLPELRKAARALKG--KVKVGSVDCQKYESLCQQANIRAYPTIrLYPG 82

                        90       100
                ....*....|....*....|..
gi 53135337 252 NGEKGDQYKG-KRDFDSLKEYV 272
Cdd:cd03004  83 NASKYHSYNGwHRDADSILEFI 104
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 64-147 1.96e-22

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: 91.27  E-value: 1.96e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  64 VMFFAPWCGHCQRLQPTWNDLGDKYNNMenpqVYVVKVDCTADT--PLCSEFGVRGYPTLKLLKPGQEPLK-----YQGP 136
Cdd:cd03002  23 VEFYAPWCGHCKNLKPEYAKAAKELDGL----VQVAAVDCDEDKnkPLCGKYGVQGFPTLKVFRPPKKASKhavedYNGE 98

                        90
                ....*....|.
gi 53135337 137 RDFQALENWML 147
Cdd:cd03002  99 RSAKAIVDFVL 109
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 305-406 2.26e-22

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


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 91.03  E-value: 2.26e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 305 AVLSLSEKDFDETI--ARGITFIKFYAPWCGHCKNLAPTWEILAKEqFPGltDVKIAEVDCTVERNVCNRFSVRGYPTLL 382
Cdd:COG3118   1 AVVELTDENFEEEVleSDKPVLVDFWAPWCGPCKMLAPVLEELAAE-YGG--KVKFVKVDVDENPELAAQFGVRSIPTLL 77

                        90       100
                ....*....|....*....|....
gi 53135337 383 LFRGGKKVSEHNGTRDLESLHSFV 406
Cdd:COG3118  78 LFKDGQPVDRFVGALPKEQLREFL 101
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 312-406 3.34e-21

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: 87.23  E-value: 3.34e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 312 KDFDETIAR-GITFIKFYAPWCGHCKNLAPTWEILAKEQfpglTDVKIAEVDCTVERNVCNRFSVRGYPTLLLFRGGKKV 390
Cdd:cd02947   1 EEFEELIKSaKPVVVDFWAPWCGPCKAIAPVLEELAEEY----PKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEV 76

                        90
                ....*....|....*.
gi 53135337 391 SEHNGTRDLESLHSFV 406
Cdd:cd02947  77 DRVVGADPKEELEEFL 92
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 63-143 5.13e-21

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: 94.74  E-value: 5.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337    63 FVMFFAPWCGHCQRLQPTWNDLGDKYNNMEnPQVYVVKVDCTA-DTPlcsEFGVRGYPTLKLLKPG--QEPLKYQGPRDF 139
Cdd:TIGR01130 368 LVEFYAPWCGHCKNLAPIYEELAEKYKDAE-SDVVIAKMDATAnDVP---PFEVEGFPTIKFVPAGkkSEPVPYDGDRTL 443


                  ....
gi 53135337   140 QALE 143
Cdd:TIGR01130 444 EDFS 447
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 179-273 1.28e-20

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: 85.69  E-value: 1.28e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 179 DNFKTHIAE-GNHFIKFFAPWCGHCKALAPTWEQLAlafEHSETVKIGKVDCTQHYEVCSENQVRGYPTLLWFRNGEKGD 257
Cdd:cd02947   1 EEFEELIKSaKPVVVDFWAPWCGPCKAIAPVLEELA---EEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVD 77

                        90
                ....*....|....*.
gi 53135337 258 QYKGKRDFDSLKEYVD 273
Cdd:cd02947  78 RVVGADPKEELEEFLE 93
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 175-311 1.56e-20

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 93.28  E-value: 1.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  175 ELSADNFKTHIAEGNH-FIKFFAPWCGHCKALAPTWEQLA--LAFEHSEtVKIGKVDCTQHYEVCSENQVRGYPTLLWFR 251
Cdd:PTZ00102  36 VLTDSTFDKFITENEIvLVKFYAPWCGHCKRLAPEYKKAAkmLKEKKSE-IVLASVDATEEMELAQEFGVRGYPTIKFFN 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  252 NGEKgDQYKGKRDFDSLKEYVdsqLQNSGkepPASKPTEAPQppAEPTQAEQAAVLSLSE 311
Cdd:PTZ00102 115 KGNP-VNYSGGRTADGIVSWI---KKLTG---PAVTEVESAS--EIKLIAKKIFVAFYGE 165
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 175-271 1.79e-20

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


Pssm-ID: 239290 [Multi-domain]  Cd Length: 114  Bit Score: 86.17  E-value: 1.79e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 175 ELSADNFKTHIAEGNHF--IKFFAPWCGHCKALAPTWEQLALAF-EHSETVKIGKVDCTQ--HYEVCSENQVRGYPTLLW 249
Cdd:cd02992   5 VLDAASFNSALLGSPSAwlVEFYASWCGHCRAFAPTWKKLARDLrKWRPVVRVAAVDCADeeNVALCRDFGVTGYPTLRY 84

                        90       100
                ....*....|....*....|....*..
gi 53135337 250 F----RNGEKGDQYKG-KRDFDSLKEY 271
Cdd:cd02992  85 FppfsKEATDGLKQEGpERDVNELREA 111
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 305-406 2.18e-20

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: 85.42  E-value: 2.18e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 305 AVLSLSEKDFDETIARG--ITFIKFYAPWCGHCKNLAPTWEILAKEQFPgltDVKIAEVDCTVERNVCNRFSVRGYPTLL 382
Cdd:cd03004   2 SVITLTPEDFPELVLNRkePWLVDFYAPWCGPCQALLPELRKAARALKG---KVKVGSVDCQKYESLCQQANIRAYPTIR 78

                        90       100
                ....*....|....*....|....*.
gi 53135337 383 LFRG-GKKVSEHNG-TRDLESLHSFV 406
Cdd:cd03004  79 LYPGnASKYHSYNGwHRDADSILEFI 104
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 306-405 6.47e-20

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


Pssm-ID: 239301 [Multi-domain]  Cd Length: 101  Bit Score: 84.11  E-value: 6.47e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 306 VLSLSEKDFDETIARG-ITFIKFYAPWCGHCKNLAPTWEILAKEqFPGLtdVKIAEVDCTVERNVCNRFSVRGYPTLLLF 384
Cdd:cd03003   3 IVTLDRGDFDAAVNSGeIWFVNFYSPRCSHCHDLAPTWREFAKE-MDGV--IRIGAVNCGDDRMLCRSQGVNSYPSLYVF 79

                        90       100
                ....*....|....*....|.
gi 53135337 385 RGGKKVSEHNGTRDLESLHSF 405
Cdd:cd03003  80 PSGMNPEKYYGDRSKESLVKF 100
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 174-272 6.55e-20

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


Pssm-ID: 239300 [Multi-domain]  Cd Length: 109  Bit Score: 84.34  E-value: 6.55e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 174 YELSADNFKTHIAEGNH--FIKFFAPWCGHCKALAPTWEQLALAFehSETVKIGKVDCTQ--HYEVCSENQVRGYPTLLW 249
Cdd:cd03002   3 YELTPKNFDKVVHNTNYttLVEFYAPWCGHCKNLKPEYAKAAKEL--DGLVQVAAVDCDEdkNKPLCGKYGVQGFPTLKV 80

                        90       100
                ....*....|....*....|....*...
gi 53135337 250 FRNGEKGDQ-----YKGKRDFDSLKEYV 272
Cdd:cd03002  81 FRPPKKASKhavedYNGERSAKAIVDFV 108
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 176-276 1.80e-19

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: 82.72  E-value: 1.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   176 LSADNFKTHIAEGNH--FIKFFAPWCGHCKALAPTWEQLALAFEHSetVKIGKVDCTQHYEVCSENQVRGYPTLLWFRNG 253
Cdd:TIGR01068   1 LTDANFDETIASSDKpvLVDFWAPWCGPCKMIAPILEELAKEYEGK--VKFVKLNVDENPDIAAKYGIRSIPTLLLFKNG 78

                          90       100
                  ....*....|....*....|...
gi 53135337   254 EKGDQYKGKRDFDSLKEYVDSQL 276
Cdd:TIGR01068  79 KEVDRSVGALPKAALKQLINKNL 101
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 309-406 2.15e-19

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: 82.72  E-value: 2.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   309 LSEKDFDETIARG--ITFIKFYAPWCGHCKNLAPTWEILAKEQFPgltDVKIAEVDCTVERNVCNRFSVRGYPTLLLFRG 386
Cdd:TIGR01068   1 LTDANFDETIASSdkPVLVDFWAPWCGPCKMIAPILEELAKEYEG---KVKFVKLNVDENPDIAAKYGIRSIPTLLLFKN 77

                          90       100
                  ....*....|....*....|
gi 53135337   387 GKKVSEHNGTRDLESLHSFV 406
Cdd:TIGR01068  78 GKEVDRSVGALPKAALKQLI 97
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 168-294 1.50e-18

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 83.91  E-value: 1.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  168 EPKQGMYELSADNFK------THIAEGNHFIKFFAPWCGHCKALAPTWEQLALAFEHseTVKIGKVDCTQHYEVCSENQV 241
Cdd:PTZ00443  27 EDANALVLLNDKNFEkltqasTGATTGPWFVKFYAPWCSHCRKMAPAWERLAKALKG--QVNVADLDATRALNLAKRFAI 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 53135337  242 RGYPTLLWFRNGeKGDQYK-GKRDFDSLKEYVDSQLQNSGKEPpaskpteAPQP 294
Cdd:PTZ00443 105 KGYPTLLLFDKG-KMYQYEgGDRSTEKLAAFALGDFKKALGAP-------VPAP 150
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 305-389 2.59e-18

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: 80.01  E-value: 2.59e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 305 AVLSLSEKDFDETI--ARGITFIKFYAPWCGHCKNLAPTWEILAK--EQFPGLtdVKIAEVDCTVERN--VCNRFSVRGY 378
Cdd:cd02992   2 PVIVLDAASFNSALlgSPSAWLVEFYASWCGHCRAFAPTWKKLARdlRKWRPV--VRVAAVDCADEENvaLCRDFGVTGY 79

                        90
                ....*....|.
gi 53135337 379 PTLLLFRGGKK 389
Cdd:cd02992  80 PTLRYFPPFSK 90
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 305-397 1.10e-17

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: 78.13  E-value: 1.10e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 305 AVLSLSEKDFDETIARGI-TFIKFYAPWCGHCKNLAPTWEiLAKEQFPGLTDVKIAEVDCTVERN--VCNRFSVRGYPTL 381
Cdd:cd02997   1 DVVHLTDEDFRKFLKKEKhVLVMFYAPWCGHCKKMKPEFT-KAATELKEDGKGVLAAVDCTKPEHdaLKEEYNVKGFPTF 79

                        90
                ....*....|....*.
gi 53135337 382 LLFRGGKKVSEHNGTR 397
Cdd:cd02997  80 KYFENGKFVEKYEGER 95
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 61-150 1.31e-17

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: 77.94  E-value: 1.31e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  61 PHFVMFFAPWCGHCQRLQPTWNDLGDKYNnmenPQVYVVKVDCTADTPLCSEFGVRGYPTLKLLKPGQEPLKYQGPRDFQ 140
Cdd:COG3118  20 PVLVDFWAPWCGPCKMLAPVLEELAAEYG----GKVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQPVDRFVGALPKE 95

                        90
                ....*....|
gi 53135337 141 ALENWmLEKL 150
Cdd:COG3118  96 QLREF-LDKV 104
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 304-406 1.10e-16

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: 75.50  E-value: 1.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 304 AAVLSLSEKDFDETI-ARGITFIKFYAPWCGHCKNLAPTWEILA---KEQFPGLTDVKIAEVDCTVERNVCNRFSVRGYP 379
Cdd:cd02996   1 SEIVSLTSGNIDDILqSAELVLVNFYADWCRFSQMLHPIFEEAAakiKEEFPDAGKVVWGKVDCDKESDIADRYRINKYP 80

                        90       100
                ....*....|....*....|....*...
gi 53135337 380 TLLLFRGGKKV-SEHNGTRDLESLHSFV 406
Cdd:cd02996  81 TLKLFRNGMMMkREYRGQRSVEALAEFV 108
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 64-146 2.30e-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: 74.28  E-value: 2.30e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  64 VMFFAPWCGHCQRLQPTWNDLGDKYNnmENPQVYVVKVDCTADT--PLCSEFGVRGYPTLKLLKPGQEPLKYQGPRDFQA 141
Cdd:cd02997  22 VMFYAPWCGHCKKMKPEFTKAATELK--EDGKGVLAAVDCTKPEhdALKEEYNVKGFPTFKYFENGKFVEKYEGERTAED 99


                ....*
gi 53135337 142 LENWM 146
Cdd:cd02997 100 IIEFM 104
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 191-271 3.10e-16

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: 73.71  E-value: 3.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 191 FIKFFAPWCGHCKALAPTWEQLALafEHSETVKIGKVDCTQHYEVCSENQVRGYPTLLWFRNGEKGDQYKGKRDFDSLKE 270
Cdd:cd03003  22 FVNFYSPRCSHCHDLAPTWREFAK--EMDGVIRIGAVNCGDDRMLCRSQGVNSYPSLYVFPSGMNPEKYYGDRSKESLVK 99


                .
gi 53135337 271 Y 271
Cdd:cd03003 100 F 100
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 61-145 3.22e-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: 73.36  E-value: 3.22e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  61 PHFVMFFAPWCGHCQRLQPTWNDLGDKYnnmenPQVYVVKVDCTADTPLCSEFGVRGYPTLKLLKPGQEPLKYQGPRDFQ 140
Cdd:cd02947  12 PVVVDFWAPWCGPCKAIAPVLEELAEEY-----PKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVVGADPKE 86


                ....*
gi 53135337 141 ALENW 145
Cdd:cd02947  87 ELEEF 91
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 63-145 6.71e-16

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: 73.09  E-value: 6.71e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  63 FVMFFAPWCGHCQRLQPTWndlgDKYNNMENPQVYVVKVDCTADTPLCSEFGVRGYPTLKLLKPGQEPL-KYQG-PRDFQ 140
Cdd:cd03004  23 LVDFYAPWCGPCQALLPEL----RKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLYPGNASKYhSYNGwHRDAD 98


                ....*
gi 53135337 141 ALENW 145
Cdd:cd03004  99 SILEF 103
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 175-272 1.21e-15

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: 72.03  E-value: 1.21e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 175 ELSADNFkTHIAEGNHFIKFFAPWCGHCKALAPTWEQLAlafEHSET--VKIGKVDCTQHYEVCSENQVRGYPTLLWFRN 252
Cdd:cd02994   5 ELTDSNW-TLVLEGEWMIEFYAPWCPACQQLQPEWEEFA---DWSDDlgINVAKVDVTQEPGLSGRFFVTALPTIYHAKD 80

                        90       100
                ....*....|....*....|
gi 53135337 253 GEKgDQYKGKRDFDSLKEYV 272
Cdd:cd02994  81 GVF-RRYQGPRDKEDLISFI 99
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 174-271 1.54e-15

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: 71.97  E-value: 1.54e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 174 YELSADNFKTHIAEGNH-FIKFFAPWCGHCKALAPTWEQLALAFEHSETVKIGKVDCT--QHYEVCSENQVRGYPTLLWF 250
Cdd:cd02997   3 VHLTDEDFRKFLKKEKHvLVMFYAPWCGHCKKMKPEFTKAATELKEDGKGVLAAVDCTkpEHDALKEEYNVKGFPTFKYF 82

                        90       100
                ....*....|....*....|.
gi 53135337 251 RNGEKGDQYKGKRDFDSLKEY 271
Cdd:cd02997  83 ENGKFVEKYEGERTAEDIIEF 103
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 306-406 2.43e-15

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: 71.26  E-value: 2.43e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 306 VLSLSEKDFDETIaRGITFIKFYAPWCGHCKNLAPTWEILAkEQFPGLtDVKIAEVDCTVERNVCNRFSVRGYPTLL--- 382
Cdd:cd02994   3 VVELTDSNWTLVL-EGEWMIEFYAPWCPACQQLQPEWEEFA-DWSDDL-GINVAKVDVTQEPGLSGRFFVTALPTIYhak 79

                        90       100
                ....*....|....*....|....*.
gi 53135337 383 --LFRggkkvsEHNGTRDLESLHSFV 406
Cdd:cd02994  80 dgVFR------RYQGPRDKEDLISFI 99
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 62-126 4.31e-15

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: 71.15  E-value: 4.31e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  62 HFVMFFAPWCGHCQRLQPTWNDLG---DKYnnmeNPQVYVVKVDCTADT--PLCSEFGVRGYPTLKLLKP 126
Cdd:cd02992  22 WLVEFYASWCGHCRAFAPTWKKLArdlRKW----RPVVRVAAVDCADEEnvALCRDFGVTGYPTLRYFPP 87
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 64-148 4.79e-15

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: 70.49  E-value: 4.79e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  64 VMFFAPWCGHCQRLQPTWNDLGDkynNMENPQVYVVKVDCTADTPLCSEFGVRGYPTLKLLKPGqEPLKYQGPRDFQALE 143
Cdd:cd02994  21 IEFYAPWCPACQQLQPEWEEFAD---WSDDLGINVAKVDVTQEPGLSGRFFVTALPTIYHAKDG-VFRRYQGPRDKEDLI 96


                ....*
gi 53135337 144 NWMLE 148
Cdd:cd02994  97 SFIEE 101
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 56-187 7.44e-14

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 70.42  E-value: 7.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   56 GAVAAPHFVMFFAPWCGHCQRLQPTWNDLGDKYNNmenpQVYVVKVDCTADTPLCSEFGVRGYPTLKLLKPGQEPLKYQG 135
Cdd:PTZ00443  49 GATTGPWFVKFYAPWCSHCRKMAPAWERLAKALKG----QVNVADLDATRALNLAKRFAIKGYPTLLLFDKGKMYQYEGG 124

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 53135337  136 PRDFQALENWMLeklngepSDPESAVEPPkAPEPKQgMYELSADNFKTHIAE 187
Cdd:PTZ00443 125 DRSTEKLAAFAL-------GDFKKALGAP-VPAPLS-FFALTIDFFVSGTNE 167
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 63-145 1.08e-13

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: 66.78  E-value: 1.08e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  63 FVMFFAPWCGHCQRLQPTWNDLGDKYNNMenpqVYVVKVDCTADTPLCSEFGVRGYPTLKLLKPGQEPLKYQGPRDFQAL 142
Cdd:cd03003  22 FVNFYSPRCSHCHDLAPTWREFAKEMDGV----IRIGAVNCGDDRMLCRSQGVNSYPSLYVFPSGMNPEKYYGDRSKESL 97


                ...
gi 53135337 143 ENW 145
Cdd:cd03003  98 VKF 100
trxA PRK09381
thioredoxin TrxA;
176-276 8.95e-13

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 64.32  E-value: 8.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  176 LSADNFKTHI--AEGNHFIKFFAPWCGHCKALAPTWEQLALAFEHSETVkiGKVDCTQHYEVCSENQVRGYPTLLWFRNG 253
Cdd:PRK09381   8 LTDDSFDTDVlkADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTV--AKLNIDQNPGTAPKYGIRGIPTLLLFKNG 85

                         90       100
                 ....*....|....*....|...
gi 53135337  254 EKGDQYKGKRDFDSLKEYVDSQL 276
Cdd:PRK09381  86 EVAATKVGALSKGQLKEFLDANL 108
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 175-272 2.30e-12

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: 63.18  E-value: 2.30e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 175 ELSADNFKtHIAEGNH--FIKFFAPWCGHCKALAPTWEQLAL----AFEHSETVKIGKVDCTQHYEVCSENQVRGYPTLL 248
Cdd:cd02996   5 SLTSGNID-DILQSAElvLVNFYADWCRFSQMLHPIFEEAAAkikeEFPDAGKVVWGKVDCDKESDIADRYRINKYPTLK 83

                        90       100
                ....*....|....*....|....*
gi 53135337 249 WFRNGEKGDQ-YKGKRDFDSLKEYV 272
Cdd:cd02996  84 LFRNGMMMKReYRGQRSVEALAEFV 108
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 64-145 2.51e-12

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: 62.69  E-value: 2.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337    64 VMFFAPWCGHCQRLQPTWNDLGDKYNNmenpQVYVVKVDCTADTPLCSEFGVRGYPTLKLLKPGQEPLKYQGPRDFQALE 143
Cdd:TIGR01068  19 VDFWAPWCGPCKMIAPILEELAKEYEG----KVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKEVDRSVGALPKAALK 94


                  ..
gi 53135337   144 NW 145
Cdd:TIGR01068  95 QL 96
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 327-406 7.44e-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: 61.22  E-value: 7.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 327 FYAPWCGHCKNLAPTWEILAKeQFPGLTDVKIAEvdCTVERNVCNRFSVRGYPTLLLFRGGKKVsEHNGTRDLESLHSFV 406
Cdd:cd02999  25 FYASWCPFSASFRPHFNALSS-MFPQIRHLAIEE--SSIKPSLLSRYGVVGFPTILLFNSTPRV-RYNGTRTLDSLAAFY 100
PRK10996 PRK10996
thioredoxin 2; Provisional
 325-395 2.50e-11

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 61.24  E-value: 2.50e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 53135337  325 IKFYAPWCGHCKNLAPTWEILAKEQFPGLTDVKiaeVDCTVERNVCNRFSVRGYPTLLLFRGGKKVSEHNG 395
Cdd:PRK10996  57 IDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVK---VNTEAERELSARFRIRSIPTIMIFKNGQVVDMLNG 124
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 63-142 2.76e-11

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: 60.10  E-value: 2.76e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  63 FVMFFAPWCGHCQRLQPTWNDLGDKYNNmENP---QVYVVKVDCTADTPLCSEFGVRGYPTLKLLKPGQEPLK-YQGPRD 138
Cdd:cd02996  22 LVNFYADWCRFSQMLHPIFEEAAAKIKE-EFPdagKVVWGKVDCDKESDIADRYRINKYPTLKLFRNGMMMKReYRGQRS 100


                ....
gi 53135337 139 FQAL 142
Cdd:cd02996 101 VEAL 104
trxA PRK09381
thioredoxin TrxA;
306-406 5.27e-11

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 59.31  E-value: 5.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  306 VLSLSEKDFDETI--ARGITFIKFYAPWCGHCKNLAPTWEILAKEQFPGLTdvkIAEVDCTVERNVCNRFSVRGYPTLLL 383
Cdd:PRK09381   5 IIHLTDDSFDTDVlkADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLT---VAKLNIDQNPGTAPKYGIRGIPTLLL 81

                         90       100
                 ....*....|....*....|...
gi 53135337  384 FRGGKKVSEHNGTRDLESLHSFV 406
Cdd:PRK09381  82 FKNGEVAATKVGALSKGQLKEFL 104
PTZ00051 PTZ00051
thioredoxin; Provisional
 310-398 9.49e-11

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 58.35  E-value: 9.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  310 SEKDFDETIARG-ITFIKFYAPWCGHCKNLAPTWEILAKEqFPGLTDVKIaEVDCTVErnVCNRFSVRGYPTLLLFRGGK 388
Cdd:PTZ00051   7 SQAEFESTLSQNeLVIVDFYAEWCGPCKRIAPFYEECSKE-YTKMVFVKV-DVDELSE--VAEKENITSMPTFKVFKNGS 82

                         90
                 ....*....|
gi 53135337  389 KVSEHNGTRD 398
Cdd:PTZ00051  83 VVDTLLGAND 92
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 61-152 1.18e-09

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 56.24  E-value: 1.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  61 PHFVMFFAPWCGHCQRLQPTWNDLGDKYNNM--------ENPQV-----------YVVKVDctADTPLCSEFGVRGYPTL 121
Cdd:COG0526  30 PVLVNFWATWCPPCRAEMPVLKELAEEYGGVvfvgvdvdENPEAvkaflkelglpYPVLLD--PDGELAKAYGVRGIPTT 107

                        90       100       110
                ....*....|....*....|....*....|..
gi 53135337 122 KLLKP-GQEPLKYQGPRDFQALENWMLEKLNG 152
Cdd:COG0526 108 VLIDKdGKIVARHVGPLSPEELEEALEKLLAK 139
PRK10996 PRK10996
thioredoxin 2; Provisional
 192-267 2.22e-09

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 55.46  E-value: 2.22e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 53135337  192 IKFFAPWCGHCKALAPTWEQLALafEHSETVKIGKVDCTQHYEVCSENQVRGYPTLLWFRNGEKGDQYKG---KRDFDS 267
Cdd:PRK10996  57 IDFWAPWCGPCRNFAPIFEDVAA--ERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFKNGQVVDMLNGavpKAPFDS 133
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 191-255 2.39e-09

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: 53.47  E-value: 2.39e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 53135337 191 FIKFFAPWCGHCKALAPTWEQLALAFEHsetVKIGKVDCTQHYEVC---SENQVRGYPTLLWFRNGEK 255
Cdd:cd01659   1 LVLFYAPWCPFCQALRPVLAELALLNKG---VKFEAVDVDEDPALEkelKRYGVGGVPTLVVFGPGIG 65
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 64-142 2.46e-09

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: 54.29  E-value: 2.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  64 VMFFAPWCGHCQRLQPTWNDLGDKYnnmenPQVYVVKVDCTADTP-LCSEFGVRGYPTLKLLKpgQEPL-KYQGPRDFQA 141
Cdd:cd02999  23 VLFYASWCPFSASFRPHFNALSSMF-----PQIRHLAIEESSIKPsLLSRYGVVGFPTILLFN--STPRvRYNGTRTLDS 95


                .
gi 53135337 142 L 142
Cdd:cd02999  96 L 96
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 324-390 3.61e-09

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: 52.70  E-value: 3.61e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 324 FIKFYAPWCGHCKNLAPTWEILAKEQfpglTDVKIAEVDCTVERNVCN---RFSVRGYPTLLLFRGGKKV 390
Cdd:cd01659   1 LVLFYAPWCPFCQALRPVLAELALLN----KGVKFEAVDVDEDPALEKelkRYGVGGVPTLVVFGPGIGV 66
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 63-127 1.69e-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: 50.77  E-value: 1.69e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 53135337  63 FVMFFAPWCGHCQRLQPTWNDLGDkynnmENPQVYVVKVDCTADTPLC---SEFGVRGYPTLKLLKPG 127
Cdd:cd01659   1 LVLFYAPWCPFCQALRPVLAELAL-----LNKGVKFEAVDVDEDPALEkelKRYGVGGVPTLVVFGPG 63
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 296-408 1.83e-08

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 52.77  E-value: 1.83e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 296 AEPTQAEQAAVLSLSEKDFDETIARG-ITFIKFYAPWCGHCKNLAPTWEILAKEqFPGLTDVKIA--------------- 359
Cdd:COG0526   3 AVGKPAPDFTLTDLDGKPLSLADLKGkPVLVNFWATWCPPCRAEMPVLKELAEE-YGGVVFVGVDvdenpeavkaflkel 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 53135337 360 EVDCTV----ERNVCNRFSVRGYPTLLLF-RGGKKVSEHNGTRDLESLHSFVLR 408
Cdd:COG0526  82 GLPYPVlldpDGELAKAYGVRGIPTTVLIdKDGKIVARHVGPLSPEELEEALEK 135
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 310-395 2.33e-08

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: 51.50  E-value: 2.33e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 310 SEKDFDETI---ARGITFIKFYAPWCGHCKNLAPTWEILAKEQFPGLTDVKIaEVDCTVErnVCNRFSVRGYPTLLLFRG 386
Cdd:cd02984   1 SEEEFEELLksdASKLLVLHFWAPWAEPCKQMNQVFEELAKEAFPSVLFLSI-EAEELPE--ISEKFEITAVPTFVFFRN 77


                ....*....
gi 53135337 387 GKKVSEHNG 395
Cdd:cd02984  78 GTIVDRVSG 86
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 61-145 2.44e-08

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


Pssm-ID: 239254 [Multi-domain]  Cd Length: 96  Bit Score: 51.12  E-value: 2.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  61 PHFVMFFAPWCGHCQRLQPTWNDLGDKYNNmenpQVYVVKVDCTADTPLCSEFGVRGYPTLKLLKPGQEPLKYQGPRDFQ 140
Cdd:cd02956  14 PVVVDFWAPRSPPSKELLPLLERLAEEYQG----QFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVDGFQGAQPEE 89


                ....*
gi 53135337 141 ALENW 145
Cdd:cd02956  90 QLRQM 94
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 325-403 3.71e-08

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


Pssm-ID: 239254 [Multi-domain]  Cd Length: 96  Bit Score: 50.73  E-value: 3.71e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 53135337 325 IKFYAPWCGHCKNLAPTWEILAkEQFPGltDVKIAEVDCTVERNVCNRFSVRGYPTLLLFRGGKKVSEHNGTRDLESLH 403
Cdd:cd02956  17 VDFWAPRSPPSKELLPLLERLA-EEYQG--QFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVDGFQGAQPEEQLR 92
PTZ00051 PTZ00051
thioredoxin; Provisional
 192-270 5.41e-08

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 50.26  E-value: 5.41e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 53135337  192 IKFFAPWCGHCKALAPTWEqlALAFEHSETVKIgKVDCTQHYEVCSENQVRGYPTLLWFRNGEKGDQYKGKRDfDSLKE 270
Cdd:PTZ00051  23 VDFYAEWCGPCKRIAPFYE--ECSKEYTKMVFV-KVDVDELSEVAEKENITSMPTFKVFKNGSVVDTLLGAND-EALKQ 97
PRK10996 PRK10996
thioredoxin 2; Provisional
 61-128 8.26e-08

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 50.84  E-value: 8.26e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 53135337   61 PHFVMFFAPWCGHCQRLQPTWNDLGDKynnmENPQVYVVKVDCTADTPLCSEFGVRGYPTLKLLKPGQ 128
Cdd:PRK10996  54 PVVIDFWAPWCGPCRNFAPIFEDVAAE----RSGKVRFVKVNTEAERELSARFRIRSIPTIMIFKNGQ 117
PLN02309 PLN02309
5'-adenylylsulfate reductase
 195-274 1.06e-07

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 53.64  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  195 FAPWCGHCKALAPTWEQLALAFEHSEtVKIGK--VDCTQHyEVCSEN-QVRGYPTLLWF-RNGEKGDQYKG-KRDFDSLK 269
Cdd:PLN02309 373 YAPWCPFCQAMEASYEELAEKLAGSG-VKVAKfrADGDQK-EFAKQElQLGSFPTILLFpKNSSRPIKYPSeKRDVDSLL 450


                 ....*
gi 53135337  270 EYVDS 274
Cdd:PLN02309 451 SFVNS 455
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 194-272 2.05e-07

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: 48.89  E-value: 2.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 194 FFAPWCGHCKALAPTWEQLA--------LAFEHSetvkigkvdcTQHYEVCSENQVRGYPTLLWFRNGEKGdQYKGKRDF 265
Cdd:cd02999  25 FYASWCPFSASFRPHFNALSsmfpqirhLAIEES----------SIKPSLLSRYGVVGFPTILLFNSTPRV-RYNGTRTL 93


                ....*..
gi 53135337 266 DSLKEYV 272
Cdd:cd02999  94 DSLAAFY 100
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 63-149 4.35e-07

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 49.13  E-value: 4.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  63 FVMFFAPWCGHCQRLqptwndlgDKyNNMENPQV--------YVVKVDCTADTP-------------LCSEFGVRGYPTL 121
Cdd:COG2143  44 LLFFESDWCPYCKKL--------HK-EVFSDPEVaaylkenfVVVQLDAEGDKEvtdfdgetltekeLARKYGVRGTPTL 114

                        90       100       110
                ....*....|....*....|....*....|..
gi 53135337 122 KLLKPGQEPLK----YQGPRDFQALENWMLEK 149
Cdd:COG2143 115 VFFDAEGKEIAripgYLKPETFLALLKYVAEG 146
PTZ00051 PTZ00051
thioredoxin; Provisional
 64-128 4.80e-07

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 47.56  E-value: 4.80e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53135337   64 VMFFAPWCGHCQRLQPTWNDLGDKYnnmenPQVYVVKVDCTADTPLCSEFGVRGYPTLKLLKPGQ 128
Cdd:PTZ00051  23 VDFYAEWCGPCKRIAPFYEECSKEY-----TKMVFVKVDVDELSEVAEKENITSMPTFKVFKNGS 82
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 61-146 5.62e-07

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


Pssm-ID: 239291 [Multi-domain]  Cd Length: 109  Bit Score: 47.83  E-value: 5.62e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  61 PHFVMFFAPWCGHCQRLQPTWNDLGDKynnMENPQVYVVKVDC-TADTPLC-SEFGVRGYPTLKLLKPG-QEPLKYQGP- 136
Cdd:cd02993  23 STLVVLYAPWCPFCQAMEASYEELAEK---LAGSNVKVAKFNAdGEQREFAkEELQLKSFPTILFFPKNsRQPIKYPSEq 99

                        90
                ....*....|
gi 53135337 137 RDFQALENWM 146
Cdd:cd02993 100 RDVDSLLMFV 109
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 195-272 9.59e-07

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


Pssm-ID: 239291 [Multi-domain]  Cd Length: 109  Bit Score: 47.06  E-value: 9.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 195 FAPWCGHCKALAPTWEQLAlafEH--SETVKIGKV--DCTQHyEVCSEN-QVRGYPTLLWF-RNGEKGDQYKG-KRDFDS 267
Cdd:cd02993  29 YAPWCPFCQAMEASYEELA---EKlaGSNVKVAKFnaDGEQR-EFAKEElQLKSFPTILFFpKNSRQPIKYPSeQRDVDS 104


                ....*
gi 53135337 268 LKEYV 272
Cdd:cd02993 105 LLMFV 109
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 191-278 2.15e-06

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 46.99  E-value: 2.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 191 FIKFFAPWCGHCKALAPTWEQLA-----LAF------EHSETVKIGKVDCTQHYEVCSEN--------QVRGYPTLLWF- 250
Cdd:COG0526  32 LVNFWATWCPPCRAEMPVLKELAeeyggVVFvgvdvdENPEAVKAFLKELGLPYPVLLDPdgelakayGVRGIPTTVLId 111

                        90       100
                ....*....|....*....|....*...
gi 53135337 251 RNGEKGDQYKGKRDFDSLKEYVDSQLQN 278
Cdd:COG0526 112 KDGKIVARHVGPLSPEELEEALEKLLAK 139
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 192-273 2.53e-06

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: 45.73  E-value: 2.53e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 192 IKFFAPWCGHCKALAPTWEQLALafEHSETVKIGKVDCTQHYEVCSENQVRGYPTLLWFRNGEKGDQYKGKRDFDSLKEY 271
Cdd:cd02956  17 VDFWAPRSPPSKELLPLLERLAE--EYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVDGFQGAQPEEQLRQM 94


                ..
gi 53135337 272 VD 273
Cdd:cd02956  95 LD 96
PLN02309 PLN02309
5'-adenylylsulfate reductase
 328-406 3.01e-06

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 49.02  E-value: 3.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  328 YAPWCGHCKNLAPTWEILAkEQFPGlTDVKIAE--VDcTVERNVCNR-FSVRGYPTLLLF-RGGKKV----SEHngtRDL 399
Cdd:PLN02309 373 YAPWCPFCQAMEASYEELA-EKLAG-SGVKVAKfrAD-GDQKEFAKQeLQLGSFPTILLFpKNSSRPikypSEK---RDV 446


                 ....*..
gi 53135337  400 ESLHSFV 406
Cdd:PLN02309 447 DSLLSFV 453
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 194-273 4.35e-06

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


Pssm-ID: 273072 [Multi-domain]  Cd Length: 463  Bit Score: 48.86  E-value: 4.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   194 FFAPWCGHCKALAPTWEQLALAFEHSeTVKIGK--VDCTQHYEVCSENQVRGYPTLLWF-RNGEKGDQYKG-KRDFDSLK 269
Cdd:TIGR00424 378 LYAPWCPFCQAMEASYLELAEKLAGS-GVKVAKfrADGDQKEFAKQELQLGSFPTILFFpKHSSRPIKYPSeKRDVDSLM 456


                  ....
gi 53135337   270 EYVD 273
Cdd:TIGR00424 457 SFVN 460
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 323-406 4.50e-06

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: 45.14  E-value: 4.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 323 TFIKFYAPWCGHCKNLAPTWEILAKEqfPGLTDVKIAEVDCTVE-RNVCNR-FSVRGYPTLLLF-RGGKKVSEHNG-TRD 398
Cdd:cd02993  24 TLVVLYAPWCPFCQAMEASYEELAEK--LAGSNVKVAKFNADGEqREFAKEeLQLKSFPTILFFpKNSRQPIKYPSeQRD 101


                ....*...
gi 53135337 399 LESLHSFV 406
Cdd:cd02993 102 VDSLLMFV 109
trxA PRK09381
thioredoxin TrxA;
63-128 5.53e-06

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 45.06  E-value: 5.53e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 53135337   63 FVMFFAPWCGHCQRLQPTWNDLGDKYNNmenpQVYVVKVDCTADTPLCSEFGVRGYPTLKLLKPGQ 128
Cdd:PRK09381  25 LVDFWAEWCGPCKMIAPILDEIADEYQG----KLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGE 86
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
61-146 6.41e-06

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 44.72  E-value: 6.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337    61 PHFVMFFAPWCGHCQRLQP---TWNDLGDKYNnmENPQVYVVKVDCTADTP-----------LCSEFGVRGYPTLKLLKP 126
Cdd:pfam13098   6 PVLVVFTDPDCPYCKKLKKellEDPDVTVYLG--PNFVFIAVNIWCAKEVAkaftdilenkeLGRKYGVRGTPTIVFFDG 83

                          90       100
                  ....*....|....*....|
gi 53135337   127 GQEPLKYQGPRDFQALENWM 146
Cdd:pfam13098  84 KGELLRLPGYVPAEEFLALL 103
TMX2 cd02962
TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related ...
 291-391 8.68e-06

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: 45.45  E-value: 8.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 291 APQPPaePTQAEQaaVLSLSEKDFDETIARGIT---FIKFYAPWCGHCKNLAPTW-EILAKEQFPGLtdvKIAEVDCTVE 366
Cdd:cd02962  19 APQPL--YMGPEH--IKYFTPKTLEEELERDKRvtwLVEFFTTWSPECVNFAPVFaELSLKYNNNNL---KFGKIDIGRF 91

                        90       100       110
                ....*....|....*....|....*....|.
gi 53135337 367 RNVCNRFSV------RGYPTLLLFRGGKKVS 391
Cdd:cd02962  92 PNVAEKFRVstsplsKQLPTIILFQGGKEVA 122
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 64-125 2.27e-05

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: 42.87  E-value: 2.27e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 53135337  64 VMFFAPWCGHCQRLQPTWNDLGDKYNNmenpQVYVVKVDCTADTPLCSEFGVRGYPTLKLLK 125
Cdd:cd02949  18 VLYTSPTCGPCRTLKPILNKVIDEFDG----AVHFVEIDIDEDQEIAEAAGIMGTPTVQFFK 75
DsbDgamma cd02953
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
 57-130 8.69e-05

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: 41.43  E-value: 8.69e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 53135337  57 AVAAPHFVMFFAPWCGHCQRLQP-TWNDlgDKYNNMENPQVYVVKVDCT----ADTPLCSEFGVRGYPTLKLLKPGQEP 130
Cdd:cd02953   9 AQGKPVFVDFTADWCVTCKVNEKvVFSD--PEVQAALKKDVVLLRADWTkndpEITALLKRFGVFGPPTYLFYGPGGEP 85
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 325-406 1.23e-04

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


Pssm-ID: 239261 [Multi-domain]  Cd Length: 111  Bit Score: 41.21  E-value: 1.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 325 IKFYAPWCGHCKNLAPTWEILAKEQFPglTDVKIAEVDCTVERNVCNRFSVRGYPTLLLFRGGKKVSEHNGTRDLESLHS 404
Cdd:cd02963  29 IKITSDWCFSCIHIEPVWKEVIQELEP--LGVGIATVNAGHERRLARKLGAHSVPAIVGIINGQVTFYHDSSFTKQHVVD 106


                ..
gi 53135337 405 FV 406
Cdd:cd02963 107 FV 108
PLN02309 PLN02309
5'-adenylylsulfate reductase
 59-145 1.40e-04

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 44.01  E-value: 1.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   59 AAPHFVMFFAPWCGHCQRLQPTWNDLGDKynnMENPQVYVVK--VDcTADTPLCS-EFGVRGYPTLKLLKPGQ-EPLKYQ 134
Cdd:PLN02309 365 KEPWLVVLYAPWCPFCQAMEASYEELAEK---LAGSGVKVAKfrAD-GDQKEFAKqELQLGSFPTILLFPKNSsRPIKYP 440

                         90
                 ....*....|..
gi 53135337  135 GP-RDFQALENW 145
Cdd:PLN02309 441 SEkRDVDSLLSF 452
PDI_a_EFP1_N cd03006
PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase ...
 46-136 1.48e-04

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: 40.92  E-value: 1.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  46 HLYSAEMLRHGAVAAphFVMFFAPWCGHCQRLQPTWNDLGDKYNNmenpQVYVVKVDCTADTPLC-SEFGVRGYPTLKLL 124
Cdd:cd03006  18 QLDYAEELRTDAEVS--LVMYYAPWDAQSQAARQEFEQVAQKLSD----QVLFVAINCWWPQGKCrKQKHFFYFPVIHLY 91

                        90
                ....*....|..
gi 53135337 125 KPGQEPLKYQGP 136
Cdd:cd03006  92 YRSRGPIEYKGP 103
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 327-406 4.80e-04

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


Pssm-ID: 273072 [Multi-domain]  Cd Length: 463  Bit Score: 42.31  E-value: 4.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337   327 FYAPWCGHCKNLAPTWEILAkEQFPGlTDVKIAE--VDCTVERNVCNRFSVRGYPTLLLF-----RGGKKVSEHngtRDL 399
Cdd:TIGR00424 378 LYAPWCPFCQAMEASYLELA-EKLAG-SGVKVAKfrADGDQKEFAKQELQLGSFPTILFFpkhssRPIKYPSEK---RDV 452


                  ....*..
gi 53135337   400 ESLHSFV 406
Cdd:TIGR00424 453 DSLMSFV 459
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 307-384 7.90e-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: 39.63  E-value: 7.90e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 53135337 307 LSLSEKDFDETIARG-ITFIKFYAPWCGHCKNLAPTWEILaKEQFPGLTDVKIAEVDCTVERNVCNRFSVRGYPTLLLF 384
Cdd:cd02950   6 LAASSTPPEVALSNGkPTLVEFYADWCTVCQEMAPDVAKL-KQKYGDQVNFVMLNVDNPKWLPEIDRYRVDGIPHFVFL 83
Phd_like cd02957
Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as ...
 306-388 8.05e-04

Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as cytosolic regulators of G protein functions. Phd and PhLPs specifically bind G protein betagamma (Gbg)-subunits with high affinity, resulting in the solubilization of Gbg from the plasma membrane and impeding G protein-mediated signal transduction by inhibiting the formation of a functional G protein trimer (G protein alphabetagamma). Phd also inhibits the GTPase activity of G protein alpha. Phd can be phosphorylated by protein kinase A and G protein-coupled receptor kinase 2, leading to its inactivation. Phd was originally isolated from the retina, where it is highly expressed and has been implicated to play an important role in light adaptation. It is also found in the pineal gland, liver, spleen, striated muscle and the brain. The C-terminal domain of Phd adopts a thioredoxin fold, but it does not contain a CXXC motif. Phd interacts with G protein beta mostly through the N-terminal helical domain. Also included in this family is a PhLP characterized as a viral inhibitor of apoptosis (IAP)-associated factor, named VIAF, that functions in caspase activation during apoptosis.


Pssm-ID: 239255 [Multi-domain]  Cd Length: 113  Bit Score: 38.69  E-value: 8.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 306 VLSLSEKDF----DETIARGITFIKFYAPWCGHCKNLAPTWEILAKEqFPGLTDVKI-AEVDCtvernVCNRFSVRGYPT 380
Cdd:cd02957   6 VREISSKEFleevTKASKGTRVVVHFYEPGFPRCKILDSHLEELAAK-YPETKFVKInAEKAF-----LVNYLDIKVLPT 79


                ....*...
gi 53135337 381 LLLFRGGK 388
Cdd:cd02957  80 LLVYKNGE 87
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 192-273 8.54e-04

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


Pssm-ID: 239247 [Multi-domain]  Cd Length: 97  Bit Score: 38.25  E-value: 8.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 192 IKFFAPWCGHCKALAPTWEQLALAFEHSetVKIGKVDCTQHYEVCSENQVRGYPTLLWFRNGEKGDQYKGKRDFDSLKEY 271
Cdd:cd02949  18 VLYTSPTCGPCRTLKPILNKVIDEFDGA--VHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDKELVKEISGVKMKSEYREF 95


                ..
gi 53135337 272 VD 273
Cdd:cd02949  96 IE 97
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 194-261 1.45e-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: 1.45e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 53135337 194 FFAPWCGHCKALAPTWEQLALafEHSETVKIGKVDCTQHYEVCSENQVRGYPTLLWFRNGEKGDQYKG 261
Cdd:cd02984  21 FWAPWAEPCKQMNQVFEELAK--EAFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTIVDRVSG 86
TMX2 cd02962
TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related ...
 163-253 3.07e-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: 38.13  E-value: 3.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337 163 PPKAPE------PKQGMYELSADNFKTHIAEgnhfikFFAPWCGHCKALAPTWEQLALAFEHSeTVKIGKVD------CT 230
Cdd:cd02962  23 LYMGPEhikyftPKTLEEELERDKRVTWLVE------FFTTWSPECVNFAPVFAELSLKYNNN-NLKFGKIDigrfpnVA 95

                        90       100
                ....*....|....*....|...
gi 53135337 231 QHYEVCSENQVRGYPTLLWFRNG 253
Cdd:cd02962  96 EKFRVSTSPLSKQLPTIILFQGG 118
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 61-124 5.73e-03

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: 36.93  E-value: 5.73e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 53135337  61 PHFVMFFAPWCGHCQRLQPTWNDLGDKYNNMENpqVYVVKVDCTADTPLCSEFGVRGYPTLKLL 124
Cdd:cd02950  22 PTLVEFYADWCTVCQEMAPDVAKLKQKYGDQVN--FVMLNVDNPKWLPEIDRYRVDGIPHFVFL 83
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 325-397 6.49e-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: 35.94  E-value: 6.49e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53135337 325 IKFYAPWCGHCKNLAPtweILAK--EQFPGltDVKIAEVDCTVERNVCNRFSVRGYPTLLLFRGGKKVSEHNGTR 397
Cdd:cd02949  18 VLYTSPTCGPCRTLKP---ILNKviDEFDG--AVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDKELVKEISGVK 87
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 61-127 6.63e-03

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


Pssm-ID: 239309 [Multi-domain]  Cd Length: 123  Bit Score: 36.51  E-value: 6.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53135337  61 PHFVMFFAPWCGHCQRLQPTWNDLGDKYNNM-------ENPQV--YVVKVDCT------ADTPLCSEFGVRGYPTLKLLK 125
Cdd:cd03011  22 PVLVYFWATWCPVCRFTSPTVNQLAADYPVVsvalrsgDDGAVarFMQKKGYGfpvindPDGVISARWGVSVTPAIVIVD 101


                ..
gi 53135337 126 PG 127
Cdd:cd03011 102 PG 103
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 194-216 7.66e-03

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


Pssm-ID: 239309 [Multi-domain]  Cd Length: 123  Bit Score: 36.12  E-value: 7.66e-03
                        10        20
                ....*....|....*....|...
gi 53135337 194 FFAPWCGHCKALAPTWEQLALAF 216
Cdd:cd03011  27 FWATWCPVCRFTSPTVNQLAADY 49
HyaE cd02965
HyaE family; HyaE is also called HupG and HoxO. They are proteins serving a critical role in ...
 349-398 9.44e-03

HyaE family; HyaE is also called HupG and HoxO. They are proteins serving a critical role in the assembly of multimeric [NiFe] hydrogenases, the enzymes that catalyze the oxidation of molecular hydrogen to enable microorganisms to utilize hydrogen as the sole energy source. The E. coli HyaE protein is a chaperone that specifically interacts with the twin-arginine translocation (Tat) signal peptide of the [NiFe] hydrogenase-1 beta subunit precursor. Tat signal peptides target precursor proteins to the Tat protein export system, which facilitates the transport of fully folded proteins across the inner membrane. HyaE may be involved in regulating the traffic of [NiFe] hydrogenase-1 on the Tat transport pathway.


Pssm-ID: 239263  Cd Length: 111  Bit Score: 35.75  E-value: 9.44e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 53135337 349 QFPGLTDvkIAEVDCTVERNVCNRFSVRGYPTLLLFRGGKKVSEHNGTRD 398
Cdd:cd02965  57 AFPGRFR--AAVVGRADEQALAARFGVLRTPALLFFRDGRYVGVLAGIRD 104
 
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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