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Conserved domains on  [gi|568994344|ref|XP_006521722|]
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thioredoxin domain-containing protein 11 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDI_a_EFP1_N cd03006
PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase ...
 93-205 6.21e-66

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


:

Pssm-ID: 239304  Cd Length: 113  Bit Score: 215.41  E-value: 6.21e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344  93 PVSFFSSRSPVLDLFQGQLDYADHVRQDSEVVVLFFYAPWCGQSIAARAEIEQAASRLSDQVLFVAINCWWNQGKCRKQK 172
Cdd:cd03006    1 PVPFFSQRSPVLDFYKGQLDYAEELRTDAEVSLVMYYAPWDAQSQAARQEFEQVAQKLSDQVLFVAINCWWPQGKCRKQK 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 568994344 173 HFFYFPVIHLYHRSFGPIEYKGPMSAVYIEKFV 205
Cdd:cd03006   81 HFFYFPVIHLYYRSRGPIEYKGPMRAPYMEKFV 113
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 592-694 2.25e-38

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


:

Pssm-ID: 239293 [Multi-domain]  Cd Length: 104  Bit Score: 138.07  E-value: 2.25e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 592 ITEVTTDTFWEVTLR-KQDVLLLYYTQWCGFCPSLNHIFIQLARLLP-EDTFTVARIDVSQNDLPWEFMVDRLPTVLFFP 669
Cdd:cd02995    2 VKVVVGKNFDEVVLDsDKDVLVEFYAPWCGHCKALAPIYEELAEKLKgDDNVVIAKMDATANDVPSEFVVDGFPTILFFP 81

                         90       100
                 ....*....|....*....|....*
gi 568994344 670 CNRKDLSVKYPGDlpITLPNLLRFI 694
Cdd:cd02995   82 AGDKSNPIKYEGD--RTLEDLIKFI 104
PTZ00102 super family cl36508
disulphide isomerase; Provisional
 435-698 1.78e-10

disulphide isomerase; Provisional


The actual alignment was detected with superfamily member PTZ00102:

Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 64.39  E-value: 1.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 435 CCRTISRGMASFTGSEQNVLTapaiEFSSLEksceaTAP--SSIPHieENRYRFpqvgLTSTAFTGLSCRTNKTLNIY-- 510
Cdd:PTZ00102 203 VLHKDEEGVELFMGKTKEELE----EFVSTE-----SFPlfAEINA--ENYRRY----ISSGKDLVWFCGTTEDYDKYks 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 511 --------LLDSNLF-WLYAERLGAPSSAP--VKEFATIVDVKEESHYILDPkqALMKFTLESFIQNFsvlYSPLK--RH 577
Cdd:PTZ00102 268 vvrkvarkLREKYAFvWLDTEQFGSHAKEHllIEEFPGLAYQSPAGRYLLPP--AKESFDSVEALIEF---FKDVEagKV 342

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 578 LTGSDSAQFPTQH--LITEVTTDTFWEVTLRK-QDVLLLYYTQWCGFCPSLNHIFIQLARLLPE-DTFTVARIDVSQNDL 653
Cdd:PTZ00102 343 EKSIKSEPIPEEQdgPVKVVVGNTFEEIVFKSdKDVLLEIYAPWCGHCKNLEPVYNELGEKYKDnDSIIVAKMNGTANET 422

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 568994344 654 PWE-FMVDRLPTVLFFPCNRKDlSVKYPGDLpiTLPNLLRFILHHS 698
Cdd:PTZ00102 423 PLEeFSWSAFPTILFVKAGERT-PIPYEGER--TVEGFKEFVNKHA 465
ATG16 super family cl25514
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 694-804 4.51e-03

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


The actual alignment was detected with superfamily member pfam08614:

Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 39.14  E-value: 4.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344  694 ILHHSDAASAPQDPGISPPTQDCVQSKAVLQREHISHVENAMQKLRSEMSSLRRTQEQVEGRLLSARRDGHRLLRRQRTL 773
Cdd:pfam08614  18 LLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEELQELEKKLRED 97

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568994344  774 EQQHRLLRRHSQKLQALYLKKARELQELARA 804
Cdd:pfam08614  98 ERRLAALEAERAQLEEKLKDREEELREKRKL 128
 
Name Accession Description Interval E-value
PDI_a_EFP1_N cd03006
PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase ...
 93-205 6.21e-66

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


Pssm-ID: 239304  Cd Length: 113  Bit Score: 215.41  E-value: 6.21e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344  93 PVSFFSSRSPVLDLFQGQLDYADHVRQDSEVVVLFFYAPWCGQSIAARAEIEQAASRLSDQVLFVAINCWWNQGKCRKQK 172
Cdd:cd03006    1 PVPFFSQRSPVLDFYKGQLDYAEELRTDAEVSLVMYYAPWDAQSQAARQEFEQVAQKLSDQVLFVAINCWWPQGKCRKQK 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 568994344 173 HFFYFPVIHLYHRSFGPIEYKGPMSAVYIEKFV 205
Cdd:cd03006   81 HFFYFPVIHLYYRSRGPIEYKGPMRAPYMEKFV 113
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 592-694 2.25e-38

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


Pssm-ID: 239293 [Multi-domain]  Cd Length: 104  Bit Score: 138.07  E-value: 2.25e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 592 ITEVTTDTFWEVTLR-KQDVLLLYYTQWCGFCPSLNHIFIQLARLLP-EDTFTVARIDVSQNDLPWEFMVDRLPTVLFFP 669
Cdd:cd02995    2 VKVVVGKNFDEVVLDsDKDVLVEFYAPWCGHCKALAPIYEELAEKLKgDDNVVIAKMDATANDVPSEFVVDGFPTILFFP 81

                         90       100
                 ....*....|....*....|....*
gi 568994344 670 CNRKDLSVKYPGDlpITLPNLLRFI 694
Cdd:cd02995   82 AGDKSNPIKYEGD--RTLEDLIKFI 104
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 538-698 1.49e-13

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: 73.94  E-value: 1.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344  538 IVDVKEESHYILDPKqalmKFTLESfIQNF--SVLYSPLKRHLTgsdSAQFPT--QHLITEVTTDTFWEVTLR-KQDVLL 612
Cdd:TIGR01130 298 IQDLEGNKKYPMDQE----EFSSEN-LEAFvkDFLDGKLKPYLK---SEPIPEddEGPVKVLVGKNFDEIVLDeTKDVLV 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344  613 LYYTQWCGFCPSLNHIFIQLARLL--PEDTFTVARIDVSQNDLPwEFMVDRLPTVLFFPCNRKDLSVKYPGDLpiTLPNL 690
Cdd:TIGR01130 370 EFYAPWCGHCKNLAPIYEELAEKYkdAESDVVIAKMDATANDVP-PFEVEGFPTIKFVPAGKKSEPVPYDGDR--TLEDF 446


                  ....*...
gi 568994344  691 LRFILHHS 698
Cdd:TIGR01130 447 SKFIAKHA 454
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 592-668 1.63e-10

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: 58.68  E-value: 1.63e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568994344 592 ITEVTTDTFWEVTLRKQD-VLLLYYTQWCGFCPSLNHIFIQLARLLpEDTFTVARIDVSQN-DLPWEFMVDRLPTVLFF 668
Cdd:COG3118    2 VVELTDENFEEEVLESDKpVLVDFWAPWCGPCKMLAPVLEELAAEY-GGKVKFVKVDVDENpELAAQFGVRSIPTLLLF 79
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 435-698 1.78e-10

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 64.39  E-value: 1.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 435 CCRTISRGMASFTGSEQNVLTapaiEFSSLEksceaTAP--SSIPHieENRYRFpqvgLTSTAFTGLSCRTNKTLNIY-- 510
Cdd:PTZ00102 203 VLHKDEEGVELFMGKTKEELE----EFVSTE-----SFPlfAEINA--ENYRRY----ISSGKDLVWFCGTTEDYDKYks 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 511 --------LLDSNLF-WLYAERLGAPSSAP--VKEFATIVDVKEESHYILDPkqALMKFTLESFIQNFsvlYSPLK--RH 577
Cdd:PTZ00102 268 vvrkvarkLREKYAFvWLDTEQFGSHAKEHllIEEFPGLAYQSPAGRYLLPP--AKESFDSVEALIEF---FKDVEagKV 342

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 578 LTGSDSAQFPTQH--LITEVTTDTFWEVTLRK-QDVLLLYYTQWCGFCPSLNHIFIQLARLLPE-DTFTVARIDVSQNDL 653
Cdd:PTZ00102 343 EKSIKSEPIPEEQdgPVKVVVGNTFEEIVFKSdKDVLLEIYAPWCGHCKNLEPVYNELGEKYKDnDSIIVAKMNGTANET 422

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 568994344 654 PWE-FMVDRLPTVLFFPCNRKDlSVKYPGDLpiTLPNLLRFILHHS 698
Cdd:PTZ00102 423 PLEeFSWSAFPTILFVKAGERT-PIPYEGER--TVEGFKEFVNKHA 465
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 115-207 4.75e-08

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: 51.85  E-value: 4.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344  115 DHVRQDSEVVVLFFYAPWCG--QSIAarAEIEQAASRLSDQVLFVAINCWWNQGKCRK--QKhffYFPVIHLYHRSFGPI 190
Cdd:pfam00085  12 EVVQKSSKPVLVDFYAPWCGpcKMLA--PEYEELAQEYKGNVVFAKVDVDENPDLASKygVR---GYPTLIFFKNGQPVD 86

                          90
                  ....*....|....*..
gi 568994344  191 EYKGPMSAVYIEKFVRR 207
Cdd:pfam00085  87 DYVGARPKDALAAFLKA 103
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 593-669 1.36e-07

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: 50.31  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344  593 TEVTTDTFWEVTLRK--QDVLLLYYTQWCGFCPSLNHIFIQLARLLPEDtFTVARIDVSQN-DLPWEFMVDRLPTVLFFP 669
Cdd:pfam00085   2 VVVLTDANFDEVVQKssKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGN-VVFAKVDVDENpDLASKYGVRGYPTLIFFK 80
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 112-165 2.89e-07

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: 49.43  E-value: 2.89e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568994344 112 DYADHVRQDSEVVVLFFYAPWCGQSIAARAEIEQAASRLSDQVLFVAINCWWNQ 165
Cdd:COG3118    9 NFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENP 62
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 560-681 4.27e-06

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 50.13  E-value: 4.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 560 LESFIQNFSVLYSPLKRHLTGSDSAQFPTQHlITEVTTDTFwEVTLRKQD-VLLLYYTQWCGFCPSLNHIFIQLARLLPE 638
Cdd:PTZ00102   3 FRSILSSLFLLLILLAFAVFGSAEEHFISEH-VTVLTDSTF-DKFITENEiVLVKFYAPWCGHCKRLAPEYKKAAKMLKE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568994344 639 DTFTV--ARIDV-SQNDLPWEFMVDRLPTVLFFpcnRKDLSVKYPG 681
Cdd:PTZ00102  81 KKSEIvlASVDAtEEMELAQEFGVRGYPTIKFF---NKGNPVNYSG 123
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 120-211 2.93e-03

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 41.27  E-value: 2.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 120 DSEVVVLFFYAPWCGQSIAARAEIEQAASRLSDQ---VLFVAINCWWNQGKCRKQKHFFYfPVIHLYhRSFGPIEYKGPM 196
Cdd:PTZ00102  48 ENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKkseIVLASVDATEEMELAQEFGVRGY-PTIKFF-NKGNPVNYSGGR 125

                         90
                 ....*....|....*
gi 568994344 197 SAVYIEKFVRRAMKP 211
Cdd:PTZ00102 126 TADGIVSWIKKLTGP 140
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 694-804 4.51e-03

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 39.14  E-value: 4.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344  694 ILHHSDAASAPQDPGISPPTQDCVQSKAVLQREHISHVENAMQKLRSEMSSLRRTQEQVEGRLLSARRDGHRLLRRQRTL 773
Cdd:pfam08614  18 LLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEELQELEKKLRED 97

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568994344  774 EQQHRLLRRHSQKLQALYLKKARELQELARA 804
Cdd:pfam08614  98 ERRLAALEAERAQLEEKLKDREEELREKRKL 128
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 112-160 6.44e-03

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


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 36.88  E-value: 6.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568994344  112 DYADHVRQDSEVVVLFFYAPWCG--QSIAarAEIEQAASRLSDQVLFVAIN 160
Cdd:TIGR01068   5 NFDETIASSDKPVLVDFWAPWCGpcKMIA--PILEELAKEYEGKVKFVKLN 53
 
Name Accession Description Interval E-value
PDI_a_EFP1_N cd03006
PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase ...
 93-205 6.21e-66

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


Pssm-ID: 239304  Cd Length: 113  Bit Score: 215.41  E-value: 6.21e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344  93 PVSFFSSRSPVLDLFQGQLDYADHVRQDSEVVVLFFYAPWCGQSIAARAEIEQAASRLSDQVLFVAINCWWNQGKCRKQK 172
Cdd:cd03006    1 PVPFFSQRSPVLDFYKGQLDYAEELRTDAEVSLVMYYAPWDAQSQAARQEFEQVAQKLSDQVLFVAINCWWPQGKCRKQK 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 568994344 173 HFFYFPVIHLYHRSFGPIEYKGPMSAVYIEKFV 205
Cdd:cd03006   81 HFFYFPVIHLYYRSRGPIEYKGPMRAPYMEKFV 113
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 592-694 2.25e-38

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


Pssm-ID: 239293 [Multi-domain]  Cd Length: 104  Bit Score: 138.07  E-value: 2.25e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 592 ITEVTTDTFWEVTLR-KQDVLLLYYTQWCGFCPSLNHIFIQLARLLP-EDTFTVARIDVSQNDLPWEFMVDRLPTVLFFP 669
Cdd:cd02995    2 VKVVVGKNFDEVVLDsDKDVLVEFYAPWCGHCKALAPIYEELAEKLKgDDNVVIAKMDATANDVPSEFVVDGFPTILFFP 81

                         90       100
                 ....*....|....*....|....*
gi 568994344 670 CNRKDLSVKYPGDlpITLPNLLRFI 694
Cdd:cd02995   82 AGDKSNPIKYEGD--RTLEDLIKFI 104
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 593-694 4.04e-22

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: 91.52  E-value: 4.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 593 TEVTTDTFWEVTLRKQDVLLLYYTQWCGFCPSLNHIFIQLARLL-PEDTFTVARIDVSQN-DLPWEFMVDRLPTVLFFPC 670
Cdd:cd02961    1 VELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELkGDGKVVVAKVDCTANnDLCSEYGVRGYPTIKLFPN 80

                         90       100
                 ....*....|....*....|....
gi 568994344 671 NRKDlSVKYPGdlPITLPNLLRFI 694
Cdd:cd02961   81 GSKE-PVKYEG--PRTLESLVEFI 101
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 115-205 7.41e-20

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: 85.35  E-value: 7.41e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 115 DHVRQDSEVVVLFFYAPWCGQSIAARAEIEQAASRL--SDQVLFVAINCWWNQGKCRKQKHfFYFPVIHLYHR-SFGPIE 191
Cdd:cd02961    9 DELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELkgDGKVVVAKVDCTANNDLCSEYGV-RGYPTIKLFPNgSKEPVK 87

                         90
                 ....*....|....
gi 568994344 192 YKGPMSAVYIEKFV 205
Cdd:cd02961   88 YEGPRTLESLVEFI 101
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 538-698 1.49e-13

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: 73.94  E-value: 1.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344  538 IVDVKEESHYILDPKqalmKFTLESfIQNF--SVLYSPLKRHLTgsdSAQFPT--QHLITEVTTDTFWEVTLR-KQDVLL 612
Cdd:TIGR01130 298 IQDLEGNKKYPMDQE----EFSSEN-LEAFvkDFLDGKLKPYLK---SEPIPEddEGPVKVLVGKNFDEIVLDeTKDVLV 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344  613 LYYTQWCGFCPSLNHIFIQLARLL--PEDTFTVARIDVSQNDLPwEFMVDRLPTVLFFPCNRKDLSVKYPGDLpiTLPNL 690
Cdd:TIGR01130 370 EFYAPWCGHCKNLAPIYEELAEKYkdAESDVVIAKMDATANDVP-PFEVEGFPTIKFVPAGKKSEPVPYDGDR--TLEDF 446


                  ....*...
gi 568994344  691 LRFILHHS 698
Cdd:TIGR01130 447 SKFIAKHA 454
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 592-668 1.63e-10

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: 58.68  E-value: 1.63e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568994344 592 ITEVTTDTFWEVTLRKQD-VLLLYYTQWCGFCPSLNHIFIQLARLLpEDTFTVARIDVSQN-DLPWEFMVDRLPTVLFF 668
Cdd:COG3118    2 VVELTDENFEEEVLESDKpVLVDFWAPWCGPCKMLAPVLEELAAEY-GGKVKFVKVDVDENpELAAQFGVRSIPTLLLF 79
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 435-698 1.78e-10

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 64.39  E-value: 1.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 435 CCRTISRGMASFTGSEQNVLTapaiEFSSLEksceaTAP--SSIPHieENRYRFpqvgLTSTAFTGLSCRTNKTLNIY-- 510
Cdd:PTZ00102 203 VLHKDEEGVELFMGKTKEELE----EFVSTE-----SFPlfAEINA--ENYRRY----ISSGKDLVWFCGTTEDYDKYks 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 511 --------LLDSNLF-WLYAERLGAPSSAP--VKEFATIVDVKEESHYILDPkqALMKFTLESFIQNFsvlYSPLK--RH 577
Cdd:PTZ00102 268 vvrkvarkLREKYAFvWLDTEQFGSHAKEHllIEEFPGLAYQSPAGRYLLPP--AKESFDSVEALIEF---FKDVEagKV 342

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 578 LTGSDSAQFPTQH--LITEVTTDTFWEVTLRK-QDVLLLYYTQWCGFCPSLNHIFIQLARLLPE-DTFTVARIDVSQNDL 653
Cdd:PTZ00102 343 EKSIKSEPIPEEQdgPVKVVVGNTFEEIVFKSdKDVLLEIYAPWCGHCKNLEPVYNELGEKYKDnDSIIVAKMNGTANET 422

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 568994344 654 PWE-FMVDRLPTVLFFPCNRKDlSVKYPGDLpiTLPNLLRFILHHS 698
Cdd:PTZ00102 423 PLEeFSWSAFPTILFVKAGERT-PIPYEGER--TVEGFKEFVNKHA 465
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 592-694 4.44e-10

PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar to the P5-like protein first isolated from alfalfa, which contains two redox active TRX (a) domains at the N-terminus, like human P5, and a C-terminal domain with homology to the C-terminal domain of ERp29, unlike human P5. The cDNA clone of this protein (named G1) was isolated from an alfalfa cDNA library by screening with human protein disulfide isomerase (PDI) cDNA. The G1 protein is constitutively expressed in all major organs of the plant and its expression is induced by treatment with tunicamycin, indicating that it may be a glucose-regulated protein. The G1 homolog in the eukaryotic social amoeba Dictyostelium discoideum is also described as a P5-like protein, which is located in the endoplasmic reticulum (ER) despite the absence of an ER-retrieval signal. G1 homologs from Aspergillus niger and Neurospora crassa have also been characterized, and are named TIGA and ERp38, respectively. Also included in the alignment is an atypical PDI from Leishmania donovani containing a single a domain, and the C-terminal a domain of a P5-like protein from Entamoeba histolytica.


Pssm-ID: 239296 [Multi-domain]  Cd Length: 105  Bit Score: 57.65  E-value: 4.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 592 ITEVTTDTFWEVTLR-KQDVLLLYYTQWCGFCPSLNHIFIQLARLLP-EDTFTVARI--DVSQNDLPWEFMVDRLPTVLF 667
Cdd:cd02998    2 VVELTDSNFDKVVGDdKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFAnEDDVVIAKVdaDEANKDLAKKYGVSGFPTLKF 81

                         90       100
                 ....*....|....*....|....*..
gi 568994344 668 FPCNRKDlSVKYPGDLpiTLPNLLRFI 694
Cdd:cd02998   82 FPKGSTE-PVKYEGGR--DLEDLVKFV 105
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 115-207 4.75e-08

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: 51.85  E-value: 4.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344  115 DHVRQDSEVVVLFFYAPWCG--QSIAarAEIEQAASRLSDQVLFVAINCWWNQGKCRK--QKhffYFPVIHLYHRSFGPI 190
Cdd:pfam00085  12 EVVQKSSKPVLVDFYAPWCGpcKMLA--PEYEELAQEYKGNVVFAKVDVDENPDLASKygVR---GYPTLIFFKNGQPVD 86

                          90
                  ....*....|....*..
gi 568994344  191 EYKGPMSAVYIEKFVRR 207
Cdd:pfam00085  87 DYVGARPKDALAAFLKA 103
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 593-669 1.36e-07

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: 50.31  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344  593 TEVTTDTFWEVTLRK--QDVLLLYYTQWCGFCPSLNHIFIQLARLLPEDtFTVARIDVSQN-DLPWEFMVDRLPTVLFFP 669
Cdd:pfam00085   2 VVVLTDANFDEVVQKssKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGN-VVFAKVDVDENpDLASKYGVRGYPTLIFFK 80
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 109-205 1.64e-07

PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a protein containing an N-terminal DnaJ domain and four redox active TRX domains. This subfamily is composed of the three TRX domains located at the C-terminal half of the protein. ERdj5 is a ubiquitous protein localized in the endoplasmic reticulum (ER) and is abundant in secretory cells. It's transcription is induced during ER stress. It interacts with BiP through its DnaJ domain in an ATP-dependent manner. BiP, an ER-resident member of the Hsp70 chaperone family, functions in ER-associated degradation and protein translocation. Also included in the alignment is the single complete TRX domain of an uncharacterized protein from Tetraodon nigroviridis, which also contains a DnaJ domain at its N-terminus.


Pssm-ID: 239302 [Multi-domain]  Cd Length: 104  Bit Score: 50.37  E-value: 1.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 109 GQLDYADHVRQDSEVVVLFFYAPWCGQSIAARAEIEQAASRLSDQVLFVAINCWWNQGKCRKQKHFFYfPVIHLYHRSFG 188
Cdd:cd03004    7 TPEDFPELVLNRKEPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAY-PTIRLYPGNAS 85

                         90
                 ....*....|....*....
gi 568994344 189 PI-EYKGPMS-AVYIEKFV 205
Cdd:cd03004   86 KYhSYNGWHRdADSILEFI 104
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 112-165 2.89e-07

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: 49.43  E-value: 2.89e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568994344 112 DYADHVRQDSEVVVLFFYAPWCGQSIAARAEIEQAASRLSDQVLFVAINCWWNQ 165
Cdd:COG3118    9 NFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENP 62
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 102-205 6.87e-07

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


Pssm-ID: 239300 [Multi-domain]  Cd Length: 109  Bit Score: 48.51  E-value: 6.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 102 PVLDLFQGQLDYADHVRQDSEVVVlfFYAPWCGQSIAARAEIEQAASRLSDQVLFVAINCWWNQGK--CRKqkhffY--- 176
Cdd:cd03002    1 PVYELTPKNFDKVVHNTNYTTLVE--FYAPWCGHCKNLKPEYAKAAKELDGLVQVAAVDCDEDKNKplCGK-----Ygvq 73

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568994344 177 -FPVIHL-----YHRSFGPIEYKGPMSAVYIEKFV 205
Cdd:cd03002   74 gFPTLKVfrppkKASKHAVEDYNGERSAKAIVDFV 108
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 606-694 9.34e-07

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


Pssm-ID: 239291 [Multi-domain]  Cd Length: 109  Bit Score: 48.22  E-value: 9.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 606 RKQDVLLLYYTQWCGFCPSLNHIFIQLARLLPEDTFTVARIDVSQNDLPW---EFMVDRLPTVLFFPCNRKDLsVKYPGD 682
Cdd:cd02993   20 RNQSTLVVLYAPWCPFCQAMEASYEELAEKLAGSNVKVAKFNADGEQREFakeELQLKSFPTILFFPKNSRQP-IKYPSE 98

                         90
                 ....*....|..
gi 568994344 683 LPiTLPNLLRFI 694
Cdd:cd02993   99 QR-DVDSLLMFV 109
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 102-205 2.95e-06

PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. Some members of this subfamily are P5-like proteins containing only one redox active TRX domain.


Pssm-ID: 239299 [Multi-domain]  Cd Length: 103  Bit Score: 46.51  E-value: 2.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 102 PVLDLFQGQLDyaDHVRQDSEVVVLFFYAPWCGQSIAARAEIEQAASRLSDQVLFVAINCWWNQGKCRKqkhffY----F 177
Cdd:cd03001    1 DVVELTDSNFD--KKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQ-----YgvrgF 73

                         90       100       110
                 ....*....|....*....|....*....|...
gi 568994344 178 PVIhlyhRSFG-----PIEYKGPMSAVYIEKFV 205
Cdd:cd03001   74 PTI----KVFGagknsPQDYQGGRTAKAIVSAA 102
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 560-681 4.27e-06

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 50.13  E-value: 4.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 560 LESFIQNFSVLYSPLKRHLTGSDSAQFPTQHlITEVTTDTFwEVTLRKQD-VLLLYYTQWCGFCPSLNHIFIQLARLLPE 638
Cdd:PTZ00102   3 FRSILSSLFLLLILLAFAVFGSAEEHFISEH-VTVLTDSTF-DKFITENEiVLVKFYAPWCGHCKRLAPEYKKAAKMLKE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568994344 639 DTFTV--ARIDV-SQNDLPWEFMVDRLPTVLFFpcnRKDLSVKYPG 681
Cdd:PTZ00102  81 KKSEIvlASVDAtEEMELAQEFGVRGYPTIKFF---NKGNPVNYSG 123
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 606-692 2.41e-05

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


Pssm-ID: 273072 [Multi-domain]  Cd Length: 463  Bit Score: 47.70  E-value: 2.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344  606 RKQDVLLLYYTQWCGFCPSLNHIFIQLARLLPEDTFTVA--RIDVSQNDLP-WEFMVDRLPTVLFFPcNRKDLSVKYPG- 681
Cdd:TIGR00424 370 RKEAWLVVLYAPWCPFCQAMEASYLELAEKLAGSGVKVAkfRADGDQKEFAkQELQLGSFPTILFFP-KHSSRPIKYPSe 448

                          90
                  ....*....|....*
gi 568994344  682 ----DLPITLPNLLR 692
Cdd:TIGR00424 449 krdvDSLMSFVNLLR 463
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 125-188 3.30e-05

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


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 42.69  E-value: 3.30e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568994344 125 VLFFYAPWCGQSIAARAEIEQAAsRLSDQVLFVAINCWWNQGKCRKQKHF--FYFPVIHLYHRSFG 188
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELA-LLNKGVKFEAVDVDEDPALEKELKRYgvGGVPTLVVFGPGIG 65
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 598-668 6.64e-05

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: 42.55  E-value: 6.64e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568994344 598 DTFWEVTLRKQDVLLLYYTQWCGFCPSLNHIFIQLARLLPEdtFTVARIDVSQN-DLPWEFMVDRLPTVLFF 668
Cdd:cd02947    1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPK--VKFVKVDVDENpELAEEYGVRSIPTFLFF 70
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 592-681 7.22e-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: 46.21  E-value: 7.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344  592 ITEVTTDTFWEVTLRKQDVLLLYYTQWCGFCPSLNHIFIQLARLLPEDTFTV--ARIDVSQN-DLPWEFMVDRLPTVLFF 668
Cdd:TIGR01130   3 VLVLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPPIklAKVDATEEkDLAQKYGVSGYPTLKIF 82

                          90
                  ....*....|...
gi 568994344  669 PcNRKDLSVKYPG 681
Cdd:TIGR01130  83 R-NGEDSVSDYNG 94
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 592-692 1.71e-04

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


Pssm-ID: 239290 [Multi-domain]  Cd Length: 114  Bit Score: 41.87  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 592 ITEVTTDTFWEVTLRKQDVLLL-YYTQWCGFCPSLNHIFIQLARLLPE--DTFTVARIDVSQ---NDLPWEFMVDRLPTV 665
Cdd:cd02992    3 VIVLDAASFNSALLGSPSAWLVeFYASWCGHCRAFAPTWKKLARDLRKwrPVVRVAAVDCADeenVALCRDFGVTGYPTL 82

                         90       100
                 ....*....|....*....|....*..
gi 568994344 666 LFFPCNRKDLSVKYPGDLPITLPNLLR 692
Cdd:cd02992   83 RYFPPFSKEATDGLKQEGPERDVNELR 109
PLN02309 PLN02309
5'-adenylylsulfate reductase
 606-680 3.29e-04

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 44.01  E-value: 3.29e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568994344 606 RKQDVLLLYYTQWCGFCPSLNHIFIQLARLLPEDTFTVARIDVSQNDLPW---EFMVDRLPTVLFFPCNRKDLsVKYP 680
Cdd:PLN02309 364 RKEPWLVVLYAPWCPFCQAMEASYEELAEKLAGSGVKVAKFRADGDQKEFakqELQLGSFPTILLFPKNSSRP-IKYP 440
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 595-669 4.02e-04

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


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 40.35  E-value: 4.02e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568994344  595 VTTDTFWEVTLRKQD-VLLLYYTQWCGFCPSLNHIFIQLARLLPeDTFTVARIDVSQN-DLPWEFMVDRLPTVLFFP 669
Cdd:TIGR01068   1 LTDANFDETIASSDKpVLVDFWAPWCGPCKMIAPILEELAKEYE-GKVKFVKLNVDENpDIAAKYGIRSIPTLLLFK 76
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 112-184 4.22e-04

PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide Isomerase Related). PDIR is composed of three redox active TRX (a) domains and an N-terminal redox inactive TRX-like (b) domain. Similar to PDI, it is involved in oxidative protein folding in the endoplasmic reticulum (ER) through its isomerase and chaperone activities. These activities are lower compared to PDI, probably due to PDIR acting only on a subset of proteins. PDIR is preferentially expressed in cells actively secreting proteins and its expression is induced by stress. Similar to PDI, the isomerase and chaperone activities of PDIR are independent; CXXC mutants lacking isomerase activity retain chaperone activity.


Pssm-ID: 239295 [Multi-domain]  Cd Length: 104  Bit Score: 40.38  E-value: 4.22e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568994344 112 DYADHVRQDSEVVVLFfYAPWCGQSIAARAEIEQAASRLSDQ--VLFVAINCW-WNQGKCRKQKHFFYFPVIHLYH 184
Cdd:cd02997    9 DFRKFLKKEKHVLVMF-YAPWCGHCKKMKPEFTKAATELKEDgkGVLAAVDCTkPEHDALKEEYNVKGFPTFKYFE 83
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 119-160 5.31e-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: 39.85  E-value: 5.31e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 568994344 119 QDSEVVVLFFYAPWCGQSIAARAEIEQAASRlSDQVLFVAIN 160
Cdd:cd02947    8 KSAKPVVVDFWAPWCGPCKAIAPVLEELAEE-YPKVKFVKVD 48
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 611-668 6.10e-04

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


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 39.22  E-value: 6.10e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568994344 611 LLLYYTQWCGFCPSLNHIFIQLArlLPEDTFTVARIDVSQNDLP----WEFMVDRLPTVLFF 668
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELA--LLNKGVKFEAVDVDEDPALekelKRYGVGGVPTLVVF 60
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 112-205 1.03e-03

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


Pssm-ID: 239293 [Multi-domain]  Cd Length: 104  Bit Score: 39.46  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 112 DYADHVRQDSEVVVLFFYAPWCGQSIAARAEIEQAASRLSDQ--VLFVAINCWWNQgkcrKQKHFFY--FPVIHLY--HR 185
Cdd:cd02995    9 NFDEVVLDSDKDVLVEFYAPWCGHCKALAPIYEELAEKLKGDdnVVIAKMDATAND----VPSEFVVdgFPTILFFpaGD 84

                         90       100
                 ....*....|....*....|
gi 568994344 186 SFGPIEYKGPMSAVYIEKFV 205
Cdd:cd02995   85 KSNPIKYEGDRTLEDLIKFI 104
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 598-682 1.20e-03

PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX related transmembrane protein containing one redox active TRX domain at the N-terminus and a classical ER retrieval sequence for type I transmembrane proteins at the C-terminus. The TMX3 transcript is found in a variety of tissues with the highest levels detected in skeletal muscle and the heart. In vitro, TMX3 showed oxidase activity albeit slightly lower than that of protein disulfide isomerase.


Pssm-ID: 239298 [Multi-domain]  Cd Length: 104  Bit Score: 39.36  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 598 DTFWEVtlRKQDV-LLLYYTQWCGFCPSLNHIFIQLARLLPE--DTFTVARIDVSQ-NDLPWEFMVDRLPTVLFFpcnRK 673
Cdd:cd03000    7 DSFKDV--RKEDIwLVDFYAPWCGHCKKLEPVWNEVGAELKSsgSPVRVGKLDATAySSIASEFGVRGYPTIKLL---KG 81


                 ....*....
gi 568994344 674 DLSVKYPGD 682
Cdd:cd03000   82 DLAYNYRGP 90
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 103-205 1.35e-03

PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar to the P5-like protein first isolated from alfalfa, which contains two redox active TRX (a) domains at the N-terminus, like human P5, and a C-terminal domain with homology to the C-terminal domain of ERp29, unlike human P5. The cDNA clone of this protein (named G1) was isolated from an alfalfa cDNA library by screening with human protein disulfide isomerase (PDI) cDNA. The G1 protein is constitutively expressed in all major organs of the plant and its expression is induced by treatment with tunicamycin, indicating that it may be a glucose-regulated protein. The G1 homolog in the eukaryotic social amoeba Dictyostelium discoideum is also described as a P5-like protein, which is located in the endoplasmic reticulum (ER) despite the absence of an ER-retrieval signal. G1 homologs from Aspergillus niger and Neurospora crassa have also been characterized, and are named TIGA and ERp38, respectively. Also included in the alignment is an atypical PDI from Leishmania donovani containing a single a domain, and the C-terminal a domain of a P5-like protein from Entamoeba histolytica.


Pssm-ID: 239296 [Multi-domain]  Cd Length: 105  Bit Score: 39.16  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 103 VLDLfqGQLDYADHVRQDSEVVVLFFYAPWCGQSIAARAEIEQAASRLS--DQVLFVAINCWWNQGKCRKQKHFFYFPVI 180
Cdd:cd02998    2 VVEL--TDSNFDKVVGDDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFAneDDVVIAKVDADEANKDLAKKYGVSGFPTL 79

                         90       100
                 ....*....|....*....|....*.
gi 568994344 181 HLYH-RSFGPIEYKGPMSAVYIEKFV 205
Cdd:cd02998   80 KFFPkGSTEPVKYEGGRDLEDLVKFV 105
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 594-694 1.66e-03

PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident protein containing three redox active TRX domains. Yeast complementation studies show that ERp46 can substitute for protein disulfide isomerase (PDI) function in vivo. It has been detected in many tissues, however, transcript and protein levels do not correlate in all tissues, suggesting regulation at a posttranscriptional level. An identical protein, named endoPDI, has been identified as an endothelial PDI that is highly expressed in the endothelium of tumors and hypoxic lesions. It has a protective effect on cells exposed to hypoxia.


Pssm-ID: 239303 [Multi-domain]  Cd Length: 102  Bit Score: 38.81  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 594 EVTTDTFwEVTLRKQDVLLLYYTQWCGFCPSLNHIFIQLARLL--PEDTFTVARIDVSQ-NDLPWEFMVDRLPTVLFFPC 670
Cdd:cd03005    4 ELTEDNF-DHHIAEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFnnENPSVKIAKVDCTQhRELCSEFQVRGYPTLLLFKD 82

                         90       100
                 ....*....|....*....|....
gi 568994344 671 NRKdlSVKYPGdlPITLPNLLRFI 694
Cdd:cd03005   83 GEK--VDKYKG--TRDLDSLKEFV 102
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 592-681 1.81e-03

PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. Some members of this subfamily are P5-like proteins containing only one redox active TRX domain.


Pssm-ID: 239299 [Multi-domain]  Cd Length: 103  Bit Score: 38.81  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 592 ITEVTTDTFWEVTLRKQD-VLLLYYTQWCGFCPSLNHIFIQLARLLpEDTFTVARIDVSQND-LPWEFMVDRLPTVLFFP 669
Cdd:cd03001    2 VVELTDSNFDKKVLNSDDvWLVEFYAPWCGHCKNLAPEWKKAAKAL-KGIVKVGAVDADVHQsLAQQYGVRGFPTIKVFG 80

                         90
                 ....*....|..
gi 568994344 670 CNRKDlSVKYPG 681
Cdd:cd03001   81 AGKNS-PQDYQG 91
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 120-211 2.93e-03

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 41.27  E-value: 2.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 120 DSEVVVLFFYAPWCGQSIAARAEIEQAASRLSDQ---VLFVAINCWWNQGKCRKQKHFFYfPVIHLYhRSFGPIEYKGPM 196
Cdd:PTZ00102  48 ENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKkseIVLASVDATEEMELAQEFGVRGY-PTIKFF-NKGNPVNYSGGR 125

                         90
                 ....*....|....*
gi 568994344 197 SAVYIEKFVRRAMKP 211
Cdd:PTZ00102 126 TADGIVSWIKKLTGP 140
PRK10996 PRK10996
thioredoxin 2; Provisional
 105-160 3.44e-03

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 38.51  E-value: 3.44e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568994344 105 DLFQGQL-----DYADHVRQDSEVVVLFFYAPWCGQSIAARAEIEQAASRLSDQVLFVAIN 160
Cdd:PRK10996  31 DLFDGEVinatgETLDKLLQDDLPVVIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKVN 91
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 694-804 4.51e-03

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 39.14  E-value: 4.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344  694 ILHHSDAASAPQDPGISPPTQDCVQSKAVLQREHISHVENAMQKLRSEMSSLRRTQEQVEGRLLSARRDGHRLLRRQRTL 773
Cdd:pfam08614  18 LLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEELQELEKKLRED 97

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568994344  774 EQQHRLLRRHSQKLQALYLKKARELQELARA 804
Cdd:pfam08614  98 ERRLAALEAERAQLEEKLKDREEELREKRKL 128
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 124-161 4.77e-03

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


Pssm-ID: 239254 [Multi-domain]  Cd Length: 96  Bit Score: 37.25  E-value: 4.77e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 568994344 124 VVLFFYAPWCGQSIAARAEIEQAASRLSDQVLFVAINC 161
Cdd:cd02956   15 VVVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNC 52
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 595-668 5.44e-03

PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide Isomerase Related). PDIR is composed of three redox active TRX (a) domains and an N-terminal redox inactive TRX-like (b) domain. Similar to PDI, it is involved in oxidative protein folding in the endoplasmic reticulum (ER) through its isomerase and chaperone activities. These activities are lower compared to PDI, probably due to PDIR acting only on a subset of proteins. PDIR is preferentially expressed in cells actively secreting proteins and its expression is induced by stress. Similar to PDI, the isomerase and chaperone activities of PDIR are independent; CXXC mutants lacking isomerase activity retain chaperone activity.


Pssm-ID: 239295 [Multi-domain]  Cd Length: 104  Bit Score: 37.30  E-value: 5.44e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568994344 595 VTTDTFWEVTLRKQDVLLLYYTQWCGFCPSLNHIFIQLARLLPEDTFTV-ARIDV--SQND-LPWEFMVDRLPTVLFF 668
Cdd:cd02997    5 LTDEDFRKFLKKEKHVLVMFYAPWCGHCKKMKPEFTKAATELKEDGKGVlAAVDCtkPEHDaLKEEYNVKGFPTFKYF 82
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 112-160 6.44e-03

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


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 36.88  E-value: 6.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568994344  112 DYADHVRQDSEVVVLFFYAPWCG--QSIAarAEIEQAASRLSDQVLFVAIN 160
Cdd:TIGR01068   5 NFDETIASSDKPVLVDFWAPWCGpcKMIA--PILEELAKEYEGKVKFVKLN 53
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 592-668 7.16e-03

PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain, similar to that of PDIa, with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. The CXFS motif in the N-terminal domain allows ERp44 to form stable reversible mixed disulfides with its substrates. Through this activity, ERp44 mediates the ER localization of Ero1alpha, a protein that oxidizes protein disulfide isomerases into their active form. ERp44 also prevents the secretion of unassembled cargo protein with unpaired cysteines. It also modulates the activity of inositol 1,4,5-triphosphate type I receptor (IP3R1), an intracellular channel protein that mediates calcium release from the ER to the cytosol.


Pssm-ID: 239294 [Multi-domain]  Cd Length: 108  Bit Score: 36.98  E-value: 7.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568994344 592 ITEVTTDTFWEVTLRKQDVLLLYYTQWCGFCPSLNHIFIQLARLL----PEDTFTV-ARID-VSQNDLPWEFMVDRLPTV 665
Cdd:cd02996    3 IVSLTSGNIDDILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIkeefPDAGKVVwGKVDcDKESDIADRYRINKYPTL 82


                 ...
gi 568994344 666 LFF 668
Cdd:cd02996   83 KLF 85
 
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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