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Conserved domains on  [gi|58388720|ref|XP_316491|]
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AGAP006452-PA [Anopheles gambiae str. PEST]

Protein Classification

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List of domain hits

 Name Accession Description Interval E-value
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 1126-1223 2.34e-09

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: 56.08  E-value: 2.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720 1126 EKVNRKMFQKIRQASDYLAVFFYSDDCKQCPRVLAEIEHIDDEADGAG-INFVKID---DKQMAKELGVYALPGIVFFKL 1201
Cdd:cd02961    1 VELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGkVVVAKVDctaNNDLCSEYGVRGYPTIKLFPN 80

                         90       100
                 ....*....|....*....|..
gi 58388720 1202 SSKEPVIYAGDlNDEDEILNWL 1223
Cdd:cd02961   81 GSKEPVKYEGP-RTLESLVEFI 101
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 47-142 4.06e-08

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: 52.61  E-value: 4.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   47 EEVSAKQLERLLEDKDYVAVYWYARSCTTCDTVLAELEHIDDDTDSFG-VDFVKIN---DKRLAKQYGITKFPALTYFR- 121
Cdd:cd02961    1 VELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGkVVVAKVDctaNNDLCSEYGVRGYPTIKLFPn 80

                         90       100
                 ....*....|....*....|..
gi 58388720  122 -EKEPIIYEGDlMDEAGVLDFL 142
Cdd:cd02961   81 gSKEPVKYEGP-RTLESLVEFI 101
ER_PDI_fam super family cl36828
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 697-1009 3.73e-07

protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs).


The actual alignment was detected with superfamily member TIGR01130:

Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 54.68  E-value: 3.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720    697 EVTDEILQDLIDDHEYVCVYF----SGACE----EGEKCDKILDD------LENIDdeldeagiifvTTEDMVTAKKYNI 762
Cdd:TIGR01130    5 VLTKDNFDDFIKSHEFVLVEFyapwCGHCKslapEYEKAADELKKkgppikLAKVD-----------ATEEKDLAQKYGV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720    763 KNLPSLVFFRNKDPLI--YSGDlNDEDEVLAWLTDEETleiPGKIEEVNIKMLEKILSENEHIVVFFYHDDDKKAQKIIA 840
Cdd:TIGR01130   74 SGYPTLKIFRNGEDSVsdYNGP-RDADGIVKYMKKQSG---PAVKEIETVADLEAFLADDDVVVIGFFKDLDSELNDTFL 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720    841 EL-ENIDDECEEkdidFVKTSDEDIDKEYDLETLPALVFYRNKFRT---IYTGDMMKEEEILEWVLEQYNTKPEIIESVD 916
Cdd:TIGR01130  150 SVaEKLRDVYFF----FAHSSDVAAFAKLGAFPDSVVLFKPKDEDEkfsKVDGEMDTDVSDLEKFIRAESLPLVGEFTQE 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720    917 RKTLQVlvnEVEHLAVLFYDDDCETCP--KILEKLETIDDDTDKHHIQFVKANDEKLAHEIGIF-----SFPALVYYETG 989
Cdd:TIGR01130  226 TAAKYF---ESGPLVVLYYNVDESLDPfeELRNRFLEAAKKFRGKFVNFAVADEEDFGRELEYFglkaeKFPAVAIQDLE 302

                          330       340
                   ....*....|....*....|..
gi 58388720    990 VPI--MYDGDLLNEYDVLDWMH 1009
Cdd:TIGR01130  303 GNKkyPMDQEEFSSENLEAFVK 324
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 381-476 1.17e-05

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: 45.68  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720  381 EDVTDEMLDKLIKEGKSIAVLFYDNNDKKSEKVLNELENIDDEC-DQLGINFVKMDDVEE---AKDYGVTKFPKLVYFEQ 456
Cdd:cd02961    1 VELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELkGDGKVVVAKVDCTANndlCSEYGVRGYPTIKLFPN 80

                         90       100
                 ....*....|....*....|..
gi 58388720  457 G--IPTVYEGSLEqEEDVLEWL 476
Cdd:cd02961   81 GskEPVKYEGPRT-LESLVEFI 101
CnoX super family cl34555
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 485-581 3.59e-05

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


The actual alignment was detected with superfamily member COG3118:

Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 44.43  E-value: 3.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720  485 IEDVTDEMLDMIVEKMQH-VAVLFYDKDSKTSQKVLAELENIDDECdQNDIAFVKID-DDNE--AKEWGIEELPTMILFE 560
Cdd:COG3118    2 VVELTDENFEEEVLESDKpVLVDFWAPWCGPCKMLAPVLEELAAEY-GGKVKFVKVDvDENPelAAQFGVRSIPTLLLFK 80

                         90       100
                 ....*....|....*....|.
gi 58388720  561 RGIPHIYEGDLLKEEELLGWL 581
Cdd:COG3118   81 DGQPVDRFVGALPKEQLREFL 101
ER_PDI_fam super family cl36828
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 1123-1335 3.77e-05

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).


The actual alignment was detected with superfamily member TIGR01130:

Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 48.13  E-value: 3.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   1123 DHIEKVNRKMFQKIRQASDYLAVFFYSDDCKQCPRVLAEIEHIDDE--ADGAGINFVKID---DKQMAKELGVYALPGIV 1197
Cdd:TIGR01130    1 EDVLVLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADElkKKGPPIKLAKVDateEKDLAQKYGVSGYPTLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   1198 FFKLSSKEPVIYAGDlNDEDEILNWLMTQKNPGGDVIEDLDgpKLLALIEDSNALAVYFYTDECEQCSGV-LESLENIDD 1276
Cdd:TIGR01130   81 IFRNGEDSVSDYNGP-RDADGIVKYMKKQSGPAVKEIETVA--DLEAFLADDDVVVIGFFKDLDSELNDTfLSVAEKLRD 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58388720   1277 DCDrhgiMFVKTDDLSIAEQYGIS-EYPVLVYF--EDNVPNVFEGSLDEEEEVL-QWLITQKT 1335
Cdd:TIGR01130  158 VYF----FFAHSSDVAAFAKLGAFpDSVVLFKPkdEDEKFSKVDGEMDTDVSDLeKFIRAESL 216
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 1347-1416 3.49e-04

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: 41.39  E-value: 3.49e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58388720 1347 LESMVDETQYLAVYFYKINCNICDQILEGLEVIDDELDvfGIHMVKI---QDPQLAKRYSIKTFPALVYFRNG 1416
Cdd:cd02947    3 FEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYP--KVKFVKVdvdENPELAEEYGVRSIPTFLFFKNG 73
ER_PDI_fam super family cl36828
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 1445-1654 7.92e-03

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).


The actual alignment was detected with superfamily member TIGR01130:

Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 40.81  E-value: 7.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   1445 DEIEEVNERMLDRLMEQSPLLCVFYYDEDCAECDDILEELELIDGEVDLYGIDfVKVASLDA------AHKYGVTTIPSL 1518
Cdd:TIGR01130    1 EDVLVLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPP-IKLAKVDAteekdlAQKYGVSGYPTL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   1519 VYYRKQIPML--YDGDmHDHERVMNWLTSQD---VFEIKNEieevnrKMLNKLLDENEFLAVYFFEEdhEESEAVLERLE 1593
Cdd:TIGR01130   80 KIFRNGEDSVsdYNGP-RDADGIVKYMKKQSgpaVKEIETV------ADLEAFLADDDVVVIGFFKD--LDSELNDTFLS 150

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58388720   1594 LIDSETDNLDiTFVKMGDPRYARKWGVTKLPAIVYFRKRF---PSIYRGDMYDEQDVLE-WLRKN 1654
Cdd:TIGR01130  151 VAEKLRDVYF-FFAHSSDVAAFAKLGAFPDSVVLFKPKDEdekFSKVDGEMDTDVSDLEkFIRAE 214
PDI_b_family cd02981
Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of ...
 275-373 8.38e-03

Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI, calsequestrin and other PDI-related proteins like ERp72, ERp57, ERp44 and PDIR. PDI, ERp57 (or ERp60), ERp72 and PDIR are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and one or more redox inactive TRX-like (b) domains. The molecular structure of PDI is abb'a'. Also included in this family is the PDI-related protein ERp27, which contains only redox-inactive TRX-like (b and b') domains. The redox inactive b domains are implicated in substrate recognition.


:

Pssm-ID: 239279  Cd Length: 97  Bit Score: 37.32  E-value: 8.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720  275 IEEVNAKT-LKTLIQNIDNLVVLFFDDEDEDSEAVLAELENIDDDcakhGIQFVRIDDPKVSKEYGIDEvPAIVYFEKQI 353
Cdd:cd02981    1 VKELTSKEeLEKFLDKDDVVVVGFFKDEESEEYKTFEKVAESLRD----DYGFGHTSDKEVAKKLKVKP-GSVVLFKPFE 75

                         90       100
                 ....*....|....*....|..
gi 58388720  354 --PNVYDDDLTdEEEILEWLLS 373
Cdd:cd02981   76 eePVEYDGEFT-EESLVEFIKD 96
 
Name Accession Description Interval E-value
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 1126-1223 2.34e-09

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: 56.08  E-value: 2.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720 1126 EKVNRKMFQKIRQASDYLAVFFYSDDCKQCPRVLAEIEHIDDEADGAG-INFVKID---DKQMAKELGVYALPGIVFFKL 1201
Cdd:cd02961    1 VELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGkVVVAKVDctaNNDLCSEYGVRGYPTIKLFPN 80

                         90       100
                 ....*....|....*....|..
gi 58388720 1202 SSKEPVIYAGDlNDEDEILNWL 1223
Cdd:cd02961   81 GSKEPVKYEGP-RTLESLVEFI 101
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 47-142 4.06e-08

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: 52.61  E-value: 4.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   47 EEVSAKQLERLLEDKDYVAVYWYARSCTTCDTVLAELEHIDDDTDSFG-VDFVKIN---DKRLAKQYGITKFPALTYFR- 121
Cdd:cd02961    1 VELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGkVVVAKVDctaNNDLCSEYGVRGYPTIKLFPn 80

                         90       100
                 ....*....|....*....|..
gi 58388720  122 -EKEPIIYEGDlMDEAGVLDFL 142
Cdd:cd02961   81 gSKEPVKYEGP-RTLESLVEFI 101
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 697-1009 3.73e-07

protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs).


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 54.68  E-value: 3.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720    697 EVTDEILQDLIDDHEYVCVYF----SGACE----EGEKCDKILDD------LENIDdeldeagiifvTTEDMVTAKKYNI 762
Cdd:TIGR01130    5 VLTKDNFDDFIKSHEFVLVEFyapwCGHCKslapEYEKAADELKKkgppikLAKVD-----------ATEEKDLAQKYGV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720    763 KNLPSLVFFRNKDPLI--YSGDlNDEDEVLAWLTDEETleiPGKIEEVNIKMLEKILSENEHIVVFFYHDDDKKAQKIIA 840
Cdd:TIGR01130   74 SGYPTLKIFRNGEDSVsdYNGP-RDADGIVKYMKKQSG---PAVKEIETVADLEAFLADDDVVVIGFFKDLDSELNDTFL 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720    841 EL-ENIDDECEEkdidFVKTSDEDIDKEYDLETLPALVFYRNKFRT---IYTGDMMKEEEILEWVLEQYNTKPEIIESVD 916
Cdd:TIGR01130  150 SVaEKLRDVYFF----FAHSSDVAAFAKLGAFPDSVVLFKPKDEDEkfsKVDGEMDTDVSDLEKFIRAESLPLVGEFTQE 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720    917 RKTLQVlvnEVEHLAVLFYDDDCETCP--KILEKLETIDDDTDKHHIQFVKANDEKLAHEIGIF-----SFPALVYYETG 989
Cdd:TIGR01130  226 TAAKYF---ESGPLVVLYYNVDESLDPfeELRNRFLEAAKKFRGKFVNFAVADEEDFGRELEYFglkaeKFPAVAIQDLE 302

                          330       340
                   ....*....|....*....|..
gi 58388720    990 VPI--MYDGDLLNEYDVLDWMH 1009
Cdd:TIGR01130  303 GNKkyPMDQEEFSSENLEAFVK 324
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 381-476 1.17e-05

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: 45.68  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720  381 EDVTDEMLDKLIKEGKSIAVLFYDNNDKKSEKVLNELENIDDEC-DQLGINFVKMDDVEE---AKDYGVTKFPKLVYFEQ 456
Cdd:cd02961    1 VELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELkGDGKVVVAKVDCTANndlCSEYGVRGYPTIKLFPN 80

                         90       100
                 ....*....|....*....|..
gi 58388720  457 G--IPTVYEGSLEqEEDVLEWL 476
Cdd:cd02961   81 GskEPVKYEGPRT-LESLVEFI 101
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 45-145 2.99e-05

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: 44.43  E-value: 2.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   45 TIEEVSAKQLER-LLEDKDYVAVYWYARSCTTCDTVLAELEHIDDDTDSfGVDFVKIN---DKRLAKQYGITKFPALTYF 120
Cdd:COG3118    1 AVVELTDENFEEeVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGG-KVKFVKVDvdeNPELAAQFGVRSIPTLLLF 79

                         90       100
                 ....*....|....*....|....*
gi 58388720  121 REKEPIIYEGDLMDEAGVLDFLTSL 145
Cdd:COG3118   80 KDGQPVDRFVGALPKEQLREFLDKV 104
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 485-581 3.59e-05

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: 44.43  E-value: 3.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720  485 IEDVTDEMLDMIVEKMQH-VAVLFYDKDSKTSQKVLAELENIDDECdQNDIAFVKID-DDNE--AKEWGIEELPTMILFE 560
Cdd:COG3118    2 VVELTDENFEEEVLESDKpVLVDFWAPWCGPCKMLAPVLEELAAEY-GGKVKFVKVDvDENPelAAQFGVRSIPTLLLFK 80

                         90       100
                 ....*....|....*....|.
gi 58388720  561 RGIPHIYEGDLLKEEELLGWL 581
Cdd:COG3118   81 DGQPVDRFVGALPKEQLREFL 101
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 1123-1335 3.77e-05

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: 48.13  E-value: 3.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   1123 DHIEKVNRKMFQKIRQASDYLAVFFYSDDCKQCPRVLAEIEHIDDE--ADGAGINFVKID---DKQMAKELGVYALPGIV 1197
Cdd:TIGR01130    1 EDVLVLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADElkKKGPPIKLAKVDateEKDLAQKYGVSGYPTLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   1198 FFKLSSKEPVIYAGDlNDEDEILNWLMTQKNPGGDVIEDLDgpKLLALIEDSNALAVYFYTDECEQCSGV-LESLENIDD 1276
Cdd:TIGR01130   81 IFRNGEDSVSDYNGP-RDADGIVKYMKKQSGPAVKEIETVA--DLEAFLADDDVVVIGFFKDLDSELNDTfLSVAEKLRD 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58388720   1277 DCDrhgiMFVKTDDLSIAEQYGIS-EYPVLVYF--EDNVPNVFEGSLDEEEEVL-QWLITQKT 1335
Cdd:TIGR01130  158 VYF----FFAHSSDVAAFAKLGAFpDSVVLFKPkdEDEKFSKVDGEMDTDVSDLeKFIRAESL 216
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 378-528 6.55e-05

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 47.44  E-value: 6.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   378 DEIEDVTDEMLDKLIKEGKSIAVLFY-------DNNDKKSEKVLNELENIDDEcdqlgINFVKMDDVEE---AKDYGVTK 447
Cdd:PTZ00102   32 EHVTVLTDSTFDKFITENEIVLVKFYapwcghcKRLAPEYKKAAKMLKEKKSE-----IVLASVDATEEmelAQEFGVRG 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   448 FPKLVYFEQGIPTVYEGSlEQEEDVLEWLErQTSSDEIEDVTDEmlDMIVEKMQHVAVLFYDKDSKTSQKVLAELENIDD 527
Cdd:PTZ00102  107 YPTIKFFNKGNPVNYSGG-RTADGIVSWIK-KLTGPAVTEVESA--SEIKLIAKKIFVAFYGEYTSKDSELYKKFEEVAD 182


                  .
gi 58388720   528 E 528
Cdd:PTZ00102  183 K 183
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 694-793 2.32e-04

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: 42.11  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720  694 TIEEVTDE-ILQDLIDDHEYVCVYFSGA-CEEgekCDKILDDLENIDDELDEAgIIFV---TTEDMVTAKKYNIKNLPSL 768
Cdd:COG3118    1 AVVELTDEnFEEEVLESDKPVLVDFWAPwCGP---CKMLAPVLEELAAEYGGK-VKFVkvdVDENPELAAQFGVRSIPTL 76

                         90       100
                 ....*....|....*....|....*.
gi 58388720  769 VFFRNKDPLI-YSGDLnDEDEVLAWL 793
Cdd:COG3118   77 LLFKDGQPVDrFVGAL-PKEQLREFL 101
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 1117-1287 2.43e-04

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 45.51  E-value: 2.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720  1117 HNMEMTDHIEKVNRKMFQKIRQASDYLAVFFYSDDCKQCPRVLAEIEHIDDE--ADGAGINFVKID---DKQMAKELGVY 1191
Cdd:PTZ00102   26 EEHFISEHVTVLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMlkEKKSEIVLASVDateEMELAQEFGVR 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720  1192 ALPGIVFFKlsSKEPVIYAGDlNDEDEILNWLmtqKNPGGDVIEDLDGPKLLALIEDSNALAvyFYTDECEQCSGVLESL 1271
Cdd:PTZ00102  106 GYPTIKFFN--KGNPVNYSGG-RTADGIVSWI---KKLTGPAVTEVESASEIKLIAKKIFVA--FYGEYTSKDSELYKKF 177

                         170
                  ....*....|....*.
gi 58388720  1272 ENIDDDCDRHGIMFVK 1287
Cdd:PTZ00102  178 EEVADKHREHAKFFVK 193
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 695-864 2.67e-04

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 45.51  E-value: 2.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   695 IEEVTDEILQDLIDDHEYVCV-YFSGACEEgekCDKILDDLENIDDELDEAG--IIFVT---TEDMVTAKKYNIKNLPSL 768
Cdd:PTZ00102   34 VTVLTDSTFDKFITENEIVLVkFYAPWCGH---CKRLAPEYKKAAKMLKEKKseIVLASvdaTEEMELAQEFGVRGYPTI 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   769 VFFRNKDPLIYSGDlNDEDEVLAWLTDeetLEIPGkIEEVNiKMLEKILSENEhIVVFFYHDDDKKAQKIIAELENIDDE 848
Cdd:PTZ00102  111 KFFNKGNPVNYSGG-RTADGIVSWIKK---LTGPA-VTEVE-SASEIKLIAKK-IFVAFYGEYTSKDSELYKKFEEVADK 183

                         170
                  ....*....|....*...
gi 58388720   849 CEE--KDIDFVKTSDEDI 864
Cdd:PTZ00102  184 HREhaKFFVKKHEGKNKI 201
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 1347-1416 3.49e-04

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: 41.39  E-value: 3.49e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58388720 1347 LESMVDETQYLAVYFYKINCNICDQILEGLEVIDDELDvfGIHMVKI---QDPQLAKRYSIKTFPALVYFRNG 1416
Cdd:cd02947    3 FEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYP--KVKFVKVdvdENPELAEEYGVRSIPTFLFFKNG 73
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
297-477 7.85e-04

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 42.35  E-value: 7.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720    297 FFDDEDEDSEAVLAELENIDDDCakhgiQFVRIDDPKVSKEYGIDEVPAIVY--FEKQIpNVYDDDLTDEEEILEWLLSQ 374
Cdd:pfam13848    1 FEDKDSPLYEIFRKAAKELKGDV-----RFGITFSKEVADKYNIKEPAILLFrkFDEET-VHYPGDSINFEDLKKFIQKN 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720    375 LEKDEIEdVTDEMLDKLIKEGKSIAV-LFYDNNDKKSEKVLNELENI-DDECDQlgINFVKMDDVEEA---KDYGVT--K 447
Cdd:pfam13848   75 CLPLVRE-FTPENAEELFEEGIPPLLlLFLKKDDESTEEFKKALEKVaKKFRGK--INFALVDAKSFGrplEYFGLSesD 151

                          170       180       190
                   ....*....|....*....|....*....|...
gi 58388720    448 FPKLVY---FEQGIPTVYEGSLEqEEDVLEWLE 477
Cdd:pfam13848  152 LPVIVIvdsFSHMYKYFPSDEFS-PESLKEFIN 183
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 46-173 8.73e-04

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 43.97  E-value: 8.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720    46 IEEVSAKQLERLLEDKDYVAVYWYARSCTTCDTVLAELEHIDDDTDSFG--VDFVKIN---DKRLAKQYGITKFPALTYF 120
Cdd:PTZ00102   34 VTVLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKseIVLASVDateEMELAQEFGVRGYPTIKFF 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 58388720   121 REKEPIIYEGDLMDEAgvldFLTSLEAMDLPdRIEEVNAKILSKIIEDSDYVA 173
Cdd:PTZ00102  114 NKGNPVNYSGGRTADG----IVSWIKKLTGP-AVTEVESASEIKLIAKKIFVA 161
Calsequestrin pfam01216
Calsequestrin;
1041-1250 1.80e-03

Calsequestrin;


Pssm-ID: 395972 [Multi-domain]  Cd Length: 350  Bit Score: 42.70  E-value: 1.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   1041 VEDDPNTPKILRHIELIDDEAA------DYGILLVKCS-DRLMAKKFGFRNPPGVTYFRKGKSINYDGDIDDE---EELL 1110
Cdd:pfam01216   39 PEDDKAAQKQFELEEIILELAAqvledkDIGFGLVDAEkDAALAKKLGFDEEDSLYVFKGDETIEFDGEFAADtivEFLL 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   1111 DWLTDPhnmemtdhIEKVNRKM-FQKIRQASDYLAV--FFYSDDCKQCPRVLAEIEHIDDEadgagINFVKIDDKQMAKE 1187
Cdd:pfam01216  119 DLIEDP--------VEIIEGELeLQAFENIEDEIKLigFFKSEDSEHYKAFEDAAEEFHPY-----IKFFATFDKGVAKK 185

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58388720   1188 LGVyALPGIVFFKLSSKEPVIYAGDLNDEDEILNWLMTQKNPG------GDVIE----DLDGPKLLALIEDSN 1250
Cdd:pfam01216  186 LSL-KLNEIDFYEAFMDEPIAIPDKPNSEEEIVEFVEEHQRPTlrklkpEDMFEtwedDLDGIHIVAFAEEAD 257
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 1359-1435 1.81e-03

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: 39.42  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720 1359 VYFYKINCNICDQILEGLEVIDDELDvfG-IHMVKI---QDPQLAKRYSIKTFPALVYFRNGNPLIYEGDLQNEQSVLEW 1434
Cdd:COG3118   23 VDFWAPWCGPCKMLAPVLEELAAEYG--GkVKFVKVdvdENPELAAQFGVRSIPTLLLFKDGQPVDRFVGALPKEQLREF 100


                 .
gi 58388720 1435 L 1435
Cdd:COG3118  101 L 101
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 696-793 2.28e-03

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: 39.13  E-value: 2.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720  696 EEVTDEILQDLIDDHEYVCVYF-SGACEEgekCDKILDDLENIDDELDEAGIIFVT----TEDMVTAKKYNIKNLPSLVF 770
Cdd:cd02961    1 VELTDDNFDELVKDSKDVLVEFyAPWCGH---CKALAPEYEKLAKELKGDGKVVVAkvdcTANNDLCSEYGVRGYPTIKL 77

                         90       100
                 ....*....|....*....|....*
gi 58388720  771 FRN--KDPLIYSGDlNDEDEVLAWL 793
Cdd:cd02961   78 FPNgsKEPVKYEGP-RTLESLVEFI 101
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 1235-1324 4.41e-03

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: 38.36  E-value: 4.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720 1235 EDLDGPKLLALIEDSNALAVYFYTDECEQCSGVLESLENIDDDCDRHG-IMFVK---TDDLSIAEQYGISEYPVLVYFED 1310
Cdd:cd02961    1 VELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGkVVVAKvdcTANNDLCSEYGVRGYPTIKLFPN 80

                         90
                 ....*....|....*.
gi 58388720 1311 NVPNV--FEGSLDEEE 1324
Cdd:cd02961   81 GSKEPvkYEGPRTLES 96
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 1445-1654 7.92e-03

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: 40.81  E-value: 7.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   1445 DEIEEVNERMLDRLMEQSPLLCVFYYDEDCAECDDILEELELIDGEVDLYGIDfVKVASLDA------AHKYGVTTIPSL 1518
Cdd:TIGR01130    1 EDVLVLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPP-IKLAKVDAteekdlAQKYGVSGYPTL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   1519 VYYRKQIPML--YDGDmHDHERVMNWLTSQD---VFEIKNEieevnrKMLNKLLDENEFLAVYFFEEdhEESEAVLERLE 1593
Cdd:TIGR01130   80 KIFRNGEDSVsdYNGP-RDADGIVKYMKKQSgpaVKEIETV------ADLEAFLADDDVVVIGFFKD--LDSELNDTFLS 150

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58388720   1594 LIDSETDNLDiTFVKMGDPRYARKWGVTKLPAIVYFRKRF---PSIYRGDMYDEQDVLE-WLRKN 1654
Cdd:TIGR01130  151 VAEKLRDVYF-FFAHSSDVAAFAKLGAFPDSVVLFKPKDEdekFSKVDGEMDTDVSDLEkFIRAE 214
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 695-795 8.07e-03

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: 37.60  E-value: 8.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720    695 IEEVTDEILQDLI-DDHEYVCVYFSGACeeGEKCDKILDDLENIDDELDEaGIIFV---TTEDMVTAKKYNIKNLPSLVF 770
Cdd:pfam00085    2 VVVLTDANFDEVVqKSSKPVLVDFYAPW--CGPCKMLAPEYEELAQEYKG-NVVFAkvdVDENPDLASKYGVRGYPTLIF 78

                           90       100
                   ....*....|....*....|....*
gi 58388720    771 FRNKDPLIYSGDLNDEDEVLAWLTD 795
Cdd:pfam00085   79 FKNGQPVDDYVGARPKDALAAFLKA 103
PDI_b_family cd02981
Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of ...
 275-373 8.38e-03

Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI, calsequestrin and other PDI-related proteins like ERp72, ERp57, ERp44 and PDIR. PDI, ERp57 (or ERp60), ERp72 and PDIR are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and one or more redox inactive TRX-like (b) domains. The molecular structure of PDI is abb'a'. Also included in this family is the PDI-related protein ERp27, which contains only redox-inactive TRX-like (b and b') domains. The redox inactive b domains are implicated in substrate recognition.


Pssm-ID: 239279  Cd Length: 97  Bit Score: 37.32  E-value: 8.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720  275 IEEVNAKT-LKTLIQNIDNLVVLFFDDEDEDSEAVLAELENIDDDcakhGIQFVRIDDPKVSKEYGIDEvPAIVYFEKQI 353
Cdd:cd02981    1 VKELTSKEeLEKFLDKDDVVVVGFFKDEESEEYKTFEKVAESLRD----DYGFGHTSDKEVAKKLKVKP-GSVVLFKPFE 75

                         90       100
                 ....*....|....*....|..
gi 58388720  354 --PNVYDDDLTdEEEILEWLLS 373
Cdd:cd02981   76 eePVEYDGEFT-EESLVEFIKD 96
 
Name Accession Description Interval E-value
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 1126-1223 2.34e-09

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: 56.08  E-value: 2.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720 1126 EKVNRKMFQKIRQASDYLAVFFYSDDCKQCPRVLAEIEHIDDEADGAG-INFVKID---DKQMAKELGVYALPGIVFFKL 1201
Cdd:cd02961    1 VELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGkVVVAKVDctaNNDLCSEYGVRGYPTIKLFPN 80

                         90       100
                 ....*....|....*....|..
gi 58388720 1202 SSKEPVIYAGDlNDEDEILNWL 1223
Cdd:cd02961   81 GSKEPVKYEGP-RTLESLVEFI 101
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 47-142 4.06e-08

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: 52.61  E-value: 4.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   47 EEVSAKQLERLLEDKDYVAVYWYARSCTTCDTVLAELEHIDDDTDSFG-VDFVKIN---DKRLAKQYGITKFPALTYFR- 121
Cdd:cd02961    1 VELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGkVVVAKVDctaNNDLCSEYGVRGYPTIKLFPn 80

                         90       100
                 ....*....|....*....|..
gi 58388720  122 -EKEPIIYEGDlMDEAGVLDFL 142
Cdd:cd02961   81 gSKEPVKYEGP-RTLESLVEFI 101
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 697-1009 3.73e-07

protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs).


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 54.68  E-value: 3.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720    697 EVTDEILQDLIDDHEYVCVYF----SGACE----EGEKCDKILDD------LENIDdeldeagiifvTTEDMVTAKKYNI 762
Cdd:TIGR01130    5 VLTKDNFDDFIKSHEFVLVEFyapwCGHCKslapEYEKAADELKKkgppikLAKVD-----------ATEEKDLAQKYGV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720    763 KNLPSLVFFRNKDPLI--YSGDlNDEDEVLAWLTDEETleiPGKIEEVNIKMLEKILSENEHIVVFFYHDDDKKAQKIIA 840
Cdd:TIGR01130   74 SGYPTLKIFRNGEDSVsdYNGP-RDADGIVKYMKKQSG---PAVKEIETVADLEAFLADDDVVVIGFFKDLDSELNDTFL 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720    841 EL-ENIDDECEEkdidFVKTSDEDIDKEYDLETLPALVFYRNKFRT---IYTGDMMKEEEILEWVLEQYNTKPEIIESVD 916
Cdd:TIGR01130  150 SVaEKLRDVYFF----FAHSSDVAAFAKLGAFPDSVVLFKPKDEDEkfsKVDGEMDTDVSDLEKFIRAESLPLVGEFTQE 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720    917 RKTLQVlvnEVEHLAVLFYDDDCETCP--KILEKLETIDDDTDKHHIQFVKANDEKLAHEIGIF-----SFPALVYYETG 989
Cdd:TIGR01130  226 TAAKYF---ESGPLVVLYYNVDESLDPfeELRNRFLEAAKKFRGKFVNFAVADEEDFGRELEYFglkaeKFPAVAIQDLE 302

                          330       340
                   ....*....|....*....|..
gi 58388720    990 VPI--MYDGDLLNEYDVLDWMH 1009
Cdd:TIGR01130  303 GNKkyPMDQEEFSSENLEAFVK 324
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 381-476 1.17e-05

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: 45.68  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720  381 EDVTDEMLDKLIKEGKSIAVLFYDNNDKKSEKVLNELENIDDEC-DQLGINFVKMDDVEE---AKDYGVTKFPKLVYFEQ 456
Cdd:cd02961    1 VELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELkGDGKVVVAKVDCTANndlCSEYGVRGYPTIKLFPN 80

                         90       100
                 ....*....|....*....|..
gi 58388720  457 G--IPTVYEGSLEqEEDVLEWL 476
Cdd:cd02961   81 GskEPVKYEGPRT-LESLVEFI 101
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 45-145 2.99e-05

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: 44.43  E-value: 2.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   45 TIEEVSAKQLER-LLEDKDYVAVYWYARSCTTCDTVLAELEHIDDDTDSfGVDFVKIN---DKRLAKQYGITKFPALTYF 120
Cdd:COG3118    1 AVVELTDENFEEeVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGG-KVKFVKVDvdeNPELAAQFGVRSIPTLLLF 79

                         90       100
                 ....*....|....*....|....*
gi 58388720  121 REKEPIIYEGDLMDEAGVLDFLTSL 145
Cdd:COG3118   80 KDGQPVDRFVGALPKEQLREFLDKV 104
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 485-581 3.59e-05

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: 44.43  E-value: 3.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720  485 IEDVTDEMLDMIVEKMQH-VAVLFYDKDSKTSQKVLAELENIDDECdQNDIAFVKID-DDNE--AKEWGIEELPTMILFE 560
Cdd:COG3118    2 VVELTDENFEEEVLESDKpVLVDFWAPWCGPCKMLAPVLEELAAEY-GGKVKFVKVDvDENPelAAQFGVRSIPTLLLFK 80

                         90       100
                 ....*....|....*....|.
gi 58388720  561 RGIPHIYEGDLLKEEELLGWL 581
Cdd:COG3118   81 DGQPVDRFVGALPKEQLREFL 101
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 1123-1335 3.77e-05

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: 48.13  E-value: 3.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   1123 DHIEKVNRKMFQKIRQASDYLAVFFYSDDCKQCPRVLAEIEHIDDE--ADGAGINFVKID---DKQMAKELGVYALPGIV 1197
Cdd:TIGR01130    1 EDVLVLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADElkKKGPPIKLAKVDateEKDLAQKYGVSGYPTLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   1198 FFKLSSKEPVIYAGDlNDEDEILNWLMTQKNPGGDVIEDLDgpKLLALIEDSNALAVYFYTDECEQCSGV-LESLENIDD 1276
Cdd:TIGR01130   81 IFRNGEDSVSDYNGP-RDADGIVKYMKKQSGPAVKEIETVA--DLEAFLADDDVVVIGFFKDLDSELNDTfLSVAEKLRD 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58388720   1277 DCDrhgiMFVKTDDLSIAEQYGIS-EYPVLVYF--EDNVPNVFEGSLDEEEEVL-QWLITQKT 1335
Cdd:TIGR01130  158 VYF----FFAHSSDVAAFAKLGAFpDSVVLFKPkdEDEKFSKVDGEMDTDVSDLeKFIRAESL 216
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 378-528 6.55e-05

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 47.44  E-value: 6.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   378 DEIEDVTDEMLDKLIKEGKSIAVLFY-------DNNDKKSEKVLNELENIDDEcdqlgINFVKMDDVEE---AKDYGVTK 447
Cdd:PTZ00102   32 EHVTVLTDSTFDKFITENEIVLVKFYapwcghcKRLAPEYKKAAKMLKEKKSE-----IVLASVDATEEmelAQEFGVRG 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   448 FPKLVYFEQGIPTVYEGSlEQEEDVLEWLErQTSSDEIEDVTDEmlDMIVEKMQHVAVLFYDKDSKTSQKVLAELENIDD 527
Cdd:PTZ00102  107 YPTIKFFNKGNPVNYSGG-RTADGIVSWIK-KLTGPAVTEVESA--SEIKLIAKKIFVAFYGEYTSKDSELYKKFEEVAD 182


                  .
gi 58388720   528 E 528
Cdd:PTZ00102  183 K 183
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 694-793 2.32e-04

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: 42.11  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720  694 TIEEVTDE-ILQDLIDDHEYVCVYFSGA-CEEgekCDKILDDLENIDDELDEAgIIFV---TTEDMVTAKKYNIKNLPSL 768
Cdd:COG3118    1 AVVELTDEnFEEEVLESDKPVLVDFWAPwCGP---CKMLAPVLEELAAEYGGK-VKFVkvdVDENPELAAQFGVRSIPTL 76

                         90       100
                 ....*....|....*....|....*.
gi 58388720  769 VFFRNKDPLI-YSGDLnDEDEVLAWL 793
Cdd:COG3118   77 LLFKDGQPVDrFVGAL-PKEQLREFL 101
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 1117-1287 2.43e-04

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 45.51  E-value: 2.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720  1117 HNMEMTDHIEKVNRKMFQKIRQASDYLAVFFYSDDCKQCPRVLAEIEHIDDE--ADGAGINFVKID---DKQMAKELGVY 1191
Cdd:PTZ00102   26 EEHFISEHVTVLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMlkEKKSEIVLASVDateEMELAQEFGVR 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720  1192 ALPGIVFFKlsSKEPVIYAGDlNDEDEILNWLmtqKNPGGDVIEDLDGPKLLALIEDSNALAvyFYTDECEQCSGVLESL 1271
Cdd:PTZ00102  106 GYPTIKFFN--KGNPVNYSGG-RTADGIVSWI---KKLTGPAVTEVESASEIKLIAKKIFVA--FYGEYTSKDSELYKKF 177

                         170
                  ....*....|....*.
gi 58388720  1272 ENIDDDCDRHGIMFVK 1287
Cdd:PTZ00102  178 EEVADKHREHAKFFVK 193
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 695-864 2.67e-04

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 45.51  E-value: 2.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   695 IEEVTDEILQDLIDDHEYVCV-YFSGACEEgekCDKILDDLENIDDELDEAG--IIFVT---TEDMVTAKKYNIKNLPSL 768
Cdd:PTZ00102   34 VTVLTDSTFDKFITENEIVLVkFYAPWCGH---CKRLAPEYKKAAKMLKEKKseIVLASvdaTEEMELAQEFGVRGYPTI 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   769 VFFRNKDPLIYSGDlNDEDEVLAWLTDeetLEIPGkIEEVNiKMLEKILSENEhIVVFFYHDDDKKAQKIIAELENIDDE 848
Cdd:PTZ00102  111 KFFNKGNPVNYSGG-RTADGIVSWIKK---LTGPA-VTEVE-SASEIKLIAKK-IFVAFYGEYTSKDSELYKKFEEVADK 183

                         170
                  ....*....|....*...
gi 58388720   849 CEE--KDIDFVKTSDEDI 864
Cdd:PTZ00102  184 HREhaKFFVKKHEGKNKI 201
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 1347-1416 3.49e-04

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: 41.39  E-value: 3.49e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58388720 1347 LESMVDETQYLAVYFYKINCNICDQILEGLEVIDDELDvfGIHMVKI---QDPQLAKRYSIKTFPALVYFRNG 1416
Cdd:cd02947    3 FEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYP--KVKFVKVdvdENPELAEEYGVRSIPTFLFFKNG 73
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 1137-1223 4.05e-04

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: 41.67  E-value: 4.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720 1137 RQASDYLAVFfYSDDCKQCPRVLAEIEHIDDEADGAGINFVK----IDDKQMAKE-LGVYALPGIVFFKLSSKEPVIYAG 1211
Cdd:cd02993   19 RRNQSTLVVL-YAPWCPFCQAMEASYEELAEKLAGSNVKVAKfnadGEQREFAKEeLQLKSFPTILFFPKNSRQPIKYPS 97

                         90
                 ....*....|..
gi 58388720 1212 DLNDEDEILNWL 1223
Cdd:cd02993   98 EQRDVDSLLMFV 109
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 1133-1200 5.10e-04

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: 40.62  E-value: 5.10e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58388720 1133 FQKIRQASDYLAVFFYSDDCKQCPRVLAEIEHIDDEADGagINFVKID---DKQMAKELGVYALPGIVFFK 1200
Cdd:cd02947    3 FEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPK--VKFVKVDvdeNPELAEEYGVRSIPTFLFFK 71
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 52-126 6.98e-04

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: 40.23  E-value: 6.98e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58388720   52 KQLERLLEDKDYVAVYWYARSCTTCDTVLAELEHIDDDTDSfgVDFVKIN---DKRLAKQYGITKFPALTYFREKEPI 126
Cdd:cd02947    1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPK--VKFVKVDvdeNPELAEEYGVRSIPTFLFFKNGKEV 76
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
297-477 7.85e-04

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 42.35  E-value: 7.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720    297 FFDDEDEDSEAVLAELENIDDDCakhgiQFVRIDDPKVSKEYGIDEVPAIVY--FEKQIpNVYDDDLTDEEEILEWLLSQ 374
Cdd:pfam13848    1 FEDKDSPLYEIFRKAAKELKGDV-----RFGITFSKEVADKYNIKEPAILLFrkFDEET-VHYPGDSINFEDLKKFIQKN 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720    375 LEKDEIEdVTDEMLDKLIKEGKSIAV-LFYDNNDKKSEKVLNELENI-DDECDQlgINFVKMDDVEEA---KDYGVT--K 447
Cdd:pfam13848   75 CLPLVRE-FTPENAEELFEEGIPPLLlLFLKKDDESTEEFKKALEKVaKKFRGK--INFALVDAKSFGrplEYFGLSesD 151

                          170       180       190
                   ....*....|....*....|....*....|...
gi 58388720    448 FPKLVY---FEQGIPTVYEGSLEqEEDVLEWLE 477
Cdd:pfam13848  152 LPVIVIvdsFSHMYKYFPSDEFS-PESLKEFIN 183
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 46-173 8.73e-04

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 43.97  E-value: 8.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720    46 IEEVSAKQLERLLEDKDYVAVYWYARSCTTCDTVLAELEHIDDDTDSFG--VDFVKIN---DKRLAKQYGITKFPALTYF 120
Cdd:PTZ00102   34 VTVLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKseIVLASVDateEMELAQEFGVRGYPTIKFF 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 58388720   121 REKEPIIYEGDLMDEAgvldFLTSLEAMDLPdRIEEVNAKILSKIIEDSDYVA 173
Cdd:PTZ00102  114 NKGNPVNYSGGRTADG----IVSWIKKLTGP-AVTEVESASEIKLIAKKIFVA 161
Calsequestrin pfam01216
Calsequestrin;
1041-1250 1.80e-03

Calsequestrin;


Pssm-ID: 395972 [Multi-domain]  Cd Length: 350  Bit Score: 42.70  E-value: 1.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   1041 VEDDPNTPKILRHIELIDDEAA------DYGILLVKCS-DRLMAKKFGFRNPPGVTYFRKGKSINYDGDIDDE---EELL 1110
Cdd:pfam01216   39 PEDDKAAQKQFELEEIILELAAqvledkDIGFGLVDAEkDAALAKKLGFDEEDSLYVFKGDETIEFDGEFAADtivEFLL 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   1111 DWLTDPhnmemtdhIEKVNRKM-FQKIRQASDYLAV--FFYSDDCKQCPRVLAEIEHIDDEadgagINFVKIDDKQMAKE 1187
Cdd:pfam01216  119 DLIEDP--------VEIIEGELeLQAFENIEDEIKLigFFKSEDSEHYKAFEDAAEEFHPY-----IKFFATFDKGVAKK 185

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58388720   1188 LGVyALPGIVFFKLSSKEPVIYAGDLNDEDEILNWLMTQKNPG------GDVIE----DLDGPKLLALIEDSN 1250
Cdd:pfam01216  186 LSL-KLNEIDFYEAFMDEPIAIPDKPNSEEEIVEFVEEHQRPTlrklkpEDMFEtwedDLDGIHIVAFAEEAD 257
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 1359-1435 1.81e-03

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: 39.42  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720 1359 VYFYKINCNICDQILEGLEVIDDELDvfG-IHMVKI---QDPQLAKRYSIKTFPALVYFRNGNPLIYEGDLQNEQSVLEW 1434
Cdd:COG3118   23 VDFWAPWCGPCKMLAPVLEELAAEYG--GkVKFVKVdvdENPELAAQFGVRSIPTLLLFKDGQPVDRFVGALPKEQLREF 100


                 .
gi 58388720 1435 L 1435
Cdd:COG3118  101 L 101
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 696-793 2.28e-03

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: 39.13  E-value: 2.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720  696 EEVTDEILQDLIDDHEYVCVYF-SGACEEgekCDKILDDLENIDDELDEAGIIFVT----TEDMVTAKKYNIKNLPSLVF 770
Cdd:cd02961    1 VELTDDNFDELVKDSKDVLVEFyAPWCGH---CKALAPEYEKLAKELKGDGKVVVAkvdcTANNDLCSEYGVRGYPTIKL 77

                         90       100
                 ....*....|....*....|....*
gi 58388720  771 FRN--KDPLIYSGDlNDEDEVLAWL 793
Cdd:cd02961   78 FPNgsKEPVKYEGP-RTLESLVEFI 101
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 789-970 2.66e-03

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 42.43  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   789 VLAWLTDEETLEIPGKIEEVNIKMLEKILSENEHIVVFFYHDDDKKAQKIIAELENIDDECEEK--DIDFVK---TSDED 863
Cdd:PTZ00102   18 AFAVFGSAEEHFISEHVTVLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKksEIVLASvdaTEEME 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   864 IDKEYDLETLPALVFYRNKFRTIYTGDMMKeEEILEWVLEQynTKPEIIESVDRKTLQVLVNEVehlAVLFYDDDCETCP 943
Cdd:PTZ00102   98 LAQEFGVRGYPTIKFFNKGNPVNYSGGRTA-DGIVSWIKKL--TGPAVTEVESASEIKLIAKKI---FVAFYGEYTSKDS 171

                         170       180
                  ....*....|....*....|....*..
gi 58388720   944 KILEKLETIDDDTDKHHIQFVKANDEK 970
Cdd:PTZ00102  172 ELYKKFEEVADKHREHAKFFVKKHEGK 198
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 1235-1324 4.41e-03

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: 38.36  E-value: 4.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720 1235 EDLDGPKLLALIEDSNALAVYFYTDECEQCSGVLESLENIDDDCDRHG-IMFVK---TDDLSIAEQYGISEYPVLVYFED 1310
Cdd:cd02961    1 VELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGkVVVAKvdcTANNDLCSEYGVRGYPTIKLFPN 80

                         90
                 ....*....|....*.
gi 58388720 1311 NVPNV--FEGSLDEEE 1324
Cdd:cd02961   81 GSKEPvkYEGPRTLES 96
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 632-997 5.72e-03

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: 41.20  E-value: 5.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720    632 DELEKE--EIVIARLDNAEE---AREYGLDHLPALVYFENEIPAI--YEGDlMNEEEVLEWLKLQKYSATIEEVTDEILQ 704
Cdd:TIGR01130   45 DELKKKgpPIKLAKVDATEEkdlAQKYGVSGYPTLKIFRNGEDSVsdYNGP-RDADGIVKYMKKQSGPAVKEIETVADLE 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720    705 DLIDDHEYVCVYFSgACEEGEKCDKILDDLENIDDELDeagiiFVTTEDMVTAKKYNIKNLPSLVFFRNKD----PLIYS 780
Cdd:TIGR01130  124 AFLADDDVVVIGFF-KDLDSELNDTFLSVAEKLRDVYF-----FFAHSSDVAAFAKLGAFPDSVVLFKPKDedekFSKVD 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720    781 GDLNDEDEVLAWLTDEETLeipGKIEEVNIKMLEKILsENEHIVVFFYHDD--DKKAQKIIAELENIDDECEEKDIDFVK 858
Cdd:TIGR01130  198 GEMDTDVSDLEKFIRAESL---PLVGEFTQETAAKYF-ESGPLVVLYYNVDesLDPFEELRNRFLEAAKKFRGKFVNFAV 273

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720    859 TSDEDIDKE-----YDLETLPALVFYRN----KFR---TIYTGDMMKE--EEILEWVLEQYNTKPEIIESVDR--KTL-- 920
Cdd:TIGR01130  274 ADEEDFGREleyfgLKAEKFPAVAIQDLegnkKYPmdqEEFSSENLEAfvKDFLDGKLKPYLKSEPIPEDDEGpvKVLvg 353

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720    921 ----QVLVNEVEHLAVLFYDDDCETCPK---ILEKL-ETIDDDTDKHHIQFVKA--NDeklAHEIGIFSFPALVYYETG- 989
Cdd:TIGR01130  354 knfdEIVLDETKDVLVEFYAPWCGHCKNlapIYEELaEKYKDAESDVVIAKMDAtaND---VPPFEVEGFPTIKFVPAGk 430

                          410
                   ....*....|
gi 58388720    990 --VPIMYDGD 997
Cdd:TIGR01130  431 ksEPVPYDGD 440
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 1342-1435 5.85e-03

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: 37.98  E-value: 5.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720 1342 ITRVMLESMVDETQYLAVYFYKINCNICDQILEGLEVIDDELDVFG-IHMVKI---QDPQLAKRYSIKTFPALVYFRNG- 1416
Cdd:cd02961    3 LTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGkVVVAKVdctANNDLCSEYGVRGYPTIKLFPNGs 82

                         90       100
                 ....*....|....*....|
gi 58388720 1417 -NPLIYEGDlQNEQSVLEWL 1435
Cdd:cd02961   83 kEPVKYEGP-RTLESLVEFI 101
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 1445-1654 7.92e-03

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: 40.81  E-value: 7.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   1445 DEIEEVNERMLDRLMEQSPLLCVFYYDEDCAECDDILEELELIDGEVDLYGIDfVKVASLDA------AHKYGVTTIPSL 1518
Cdd:TIGR01130    1 EDVLVLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPP-IKLAKVDAteekdlAQKYGVSGYPTL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720   1519 VYYRKQIPML--YDGDmHDHERVMNWLTSQD---VFEIKNEieevnrKMLNKLLDENEFLAVYFFEEdhEESEAVLERLE 1593
Cdd:TIGR01130   80 KIFRNGEDSVsdYNGP-RDADGIVKYMKKQSgpaVKEIETV------ADLEAFLADDDVVVIGFFKD--LDSELNDTFLS 150

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58388720   1594 LIDSETDNLDiTFVKMGDPRYARKWGVTKLPAIVYFRKRF---PSIYRGDMYDEQDVLE-WLRKN 1654
Cdd:TIGR01130  151 VAEKLRDVYF-FFAHSSDVAAFAKLGAFPDSVVLFKPKDEdekFSKVDGEMDTDVSDLEkFIRAE 214
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 695-795 8.07e-03

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: 37.60  E-value: 8.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720    695 IEEVTDEILQDLI-DDHEYVCVYFSGACeeGEKCDKILDDLENIDDELDEaGIIFV---TTEDMVTAKKYNIKNLPSLVF 770
Cdd:pfam00085    2 VVVLTDANFDEVVqKSSKPVLVDFYAPW--CGPCKMLAPEYEELAQEYKG-NVVFAkvdVDENPDLASKYGVRGYPTLIF 78

                           90       100
                   ....*....|....*....|....*
gi 58388720    771 FRNKDPLIYSGDLNDEDEVLAWLTD 795
Cdd:pfam00085   79 FKNGQPVDDYVGARPKDALAAFLKA 103
PDI_b_family cd02981
Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of ...
 275-373 8.38e-03

Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI, calsequestrin and other PDI-related proteins like ERp72, ERp57, ERp44 and PDIR. PDI, ERp57 (or ERp60), ERp72 and PDIR are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and one or more redox inactive TRX-like (b) domains. The molecular structure of PDI is abb'a'. Also included in this family is the PDI-related protein ERp27, which contains only redox-inactive TRX-like (b and b') domains. The redox inactive b domains are implicated in substrate recognition.


Pssm-ID: 239279  Cd Length: 97  Bit Score: 37.32  E-value: 8.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720  275 IEEVNAKT-LKTLIQNIDNLVVLFFDDEDEDSEAVLAELENIDDDcakhGIQFVRIDDPKVSKEYGIDEvPAIVYFEKQI 353
Cdd:cd02981    1 VKELTSKEeLEKFLDKDDVVVVGFFKDEESEEYKTFEKVAESLRD----DYGFGHTSDKEVAKKLKVKP-GSVVLFKPFE 75

                         90       100
                 ....*....|....*....|..
gi 58388720  354 --PNVYDDDLTdEEEILEWLLS 373
Cdd:cd02981   76 eePVEYDGEFT-EESLVEFIKD 96
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 1242-1324 9.74e-03

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: 37.15  E-value: 9.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58388720 1242 LLALIEDSNALAVYFYTDECEQCSGVLESLENIDDDCDRHGIMFVKTDDLS-IAEQYGISEYPVLVYFEDNVP-NVFEGS 1319
Cdd:cd02947    3 FEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPeLAEEYGVRSIPTFLFFKNGKEvDRVVGA 82


                 ....*
gi 58388720 1320 LDEEE 1324
Cdd:cd02947   83 DPKEE 87
 
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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