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Conserved domains on  [gi|929654899|dbj|BAA92582|]
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KIAA1344 protein [Homo sapiens]

Protein Classification

thioredoxin domain-containing protein 16( domain architecture ID 11554589)

thioredoxin domain-containing protein 16 (TXNDC16), or ERP90, is a protein disulfide isomerase (PDI) family protein that interacts with ERFAD, a flavoprotein involved in ER-associated degradation (ERAD)

CATH:  3.40.30.10
Gene Ontology:  GO:0005783
PubMed:  15158710|15558583|10085220
SCOP:  4000084

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
533-722 1.02e-21

Thioredoxin-like domain;


:

Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 93.20  E-value: 1.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899  533 FSPTMKTAKEDFSEAGNYLKGYVITGIYSEEDVLllsTKYAASLPALLLARHTEGKIESIPLASTHAQDIVQIITDALLE 612
Cdd:pfam13848   1 FEDKDSPLYEIFRKAAKELKGDVRFGITFSKEVA---DKYNIKEPAILLFRKFDEETVHYPGDSINFEDLKKFIQKNCLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899  613 MFPEITVENLPSYFRLQKPLLILF--SDGTVNPQYKKAILTLVKQKYLDSFTPCWLNLKNTPVgrgILRaYFDPLPPLP- 689
Cdd:pfam13848  78 LVREFTPENAEELFEEGIPPLLLLflKKDDESTEEFKKALEKVAKKFRGKINFALVDAKSFGR---PLE-YFGLSESDLp 153

                         170       180       190
                  ....*....|....*....|....*....|...
gi 929654899  690 LLVLVNLHSgGQVFAFPSDQaIIEENLVLWLKK 722
Cdd:pfam13848 154 VIVIVDSFS-HMYKYFPSDE-FSPESLKEFIND 184
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 394-492 6.46e-21

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: 88.05  E-value: 6.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899 394 VELTEETFNATVMAS-DSIVLFYAGWQAVSMAFLQSYIDVAVKLKGTSTMLLTRINCADWSDVCTKQNVTEFPIIKMYKK 472
Cdd:cd02961    1 VELTDDNFDELVKDSkDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPN 80

                         90       100
                 ....*....|....*....|.
gi 929654899 473 G-ENPVSYAGMLGTKDLLKFI 492
Cdd:cd02961   81 GsKEPVKYEGPRTLESLVEFI 101
 
Name Accession Description Interval E-value
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
533-722 1.02e-21

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 93.20  E-value: 1.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899  533 FSPTMKTAKEDFSEAGNYLKGYVITGIYSEEDVLllsTKYAASLPALLLARHTEGKIESIPLASTHAQDIVQIITDALLE 612
Cdd:pfam13848   1 FEDKDSPLYEIFRKAAKELKGDVRFGITFSKEVA---DKYNIKEPAILLFRKFDEETVHYPGDSINFEDLKKFIQKNCLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899  613 MFPEITVENLPSYFRLQKPLLILF--SDGTVNPQYKKAILTLVKQKYLDSFTPCWLNLKNTPVgrgILRaYFDPLPPLP- 689
Cdd:pfam13848  78 LVREFTPENAEELFEEGIPPLLLLflKKDDESTEEFKKALEKVAKKFRGKINFALVDAKSFGR---PLE-YFGLSESDLp 153

                         170       180       190
                  ....*....|....*....|....*....|...
gi 929654899  690 LLVLVNLHSgGQVFAFPSDQaIIEENLVLWLKK 722
Cdd:pfam13848 154 VIVIVDSFS-HMYKYFPSDE-FSPESLKEFIND 184
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 394-492 6.46e-21

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: 88.05  E-value: 6.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899 394 VELTEETFNATVMAS-DSIVLFYAGWQAVSMAFLQSYIDVAVKLKGTSTMLLTRINCADWSDVCTKQNVTEFPIIKMYKK 472
Cdd:cd02961    1 VELTDDNFDELVKDSkDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPN 80

                         90       100
                 ....*....|....*....|.
gi 929654899 473 G-ENPVSYAGMLGTKDLLKFI 492
Cdd:cd02961   81 GsKEPVKYEGPRTLESLVEFI 101
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 393-492 7.89e-10

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: 56.47  E-value: 7.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899  393 TVELTEETFNATVMASDSIVL--FYAGW----QAVS---MAFLQSYIDVAVKLKgtstmlltrINCADWSDVCTKQNVTE 463
Cdd:pfam00085   2 VVVLTDANFDEVVQKSSKPVLvdFYAPWcgpcKMLApeyEELAQEYKGNVVFAK---------VDVDENPDLASKYGVRG 72

                          90       100
                  ....*....|....*....|....*....
gi 929654899  464 FPIIKMYKKGENPVSYAGMLGTKDLLKFI 492
Cdd:pfam00085  73 YPTLIFFKNGQPVDDYVGARPKDALAAFL 101
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 391-661 7.15e-08

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: 55.84  E-value: 7.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899  391 ELTVELTEETFNATVMASDSI-VLFYAGWQAVSMAFLQSYIDVAVKLKG-TSTMLLTRINCADWSDVCTKQNVTEFPIIK 468
Cdd:TIGR01130   1 EDVLVLTKDNFDDFIKSHEFVlVEFYAPWCGHCKSLAPEYEKAADELKKkGPPIKLAKVDATEEKDLAQKYGVSGYPTLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899  469 MYKKGENPVS-YAGMLGTKDLLKFiqLNRISYP--VNITSIQEAEEYLSGElykdlilysSVSVLGLFSPTMKTAKEDFS 545
Cdd:TIGR01130  81 IFRNGEDSVSdYNGPRDADGIVKY--MKKQSGPavKEIETVADLEAFLADD---------DVVVIGFFKDLDSELNDTFL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899  546 EAGNYLKGYVITGIYSEEDVLLLSTKYAASLPALLLARHTEGKIESIPLA-STHAQDIVQIITDALLEMFPEITVENLPS 624
Cdd:TIGR01130 150 SVAEKLRDVYFFFAHSSDVAAFAKLGAFPDSVVLFKPKDEDEKFSKVDGEmDTDVSDLEKFIRAESLPLVGEFTQETAAK 229

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 929654899  625 YFrLQKPL--LILFSDGTVNP-QYKKAILTLVKQKYLDSF 661
Cdd:TIGR01130 230 YF-ESGPLvvLYYNVDESLDPfEELRNRFLEAAKKFRGKF 268
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 391-667 9.09e-06

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 48.98  E-value: 9.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899 391 ELTVELTEETFNATVMASDS-IVLFYAGWQAVSMAFLQSYIDVAVKLK-GTSTMLLTRINCADWSDVCTKQNVTEFPIIK 468
Cdd:PTZ00102  32 EHVTVLTDSTFDKFITENEIvLVKFYAPWCGHCKRLAPEYKKAAKMLKeKKSEIVLASVDATEEMELAQEFGVRGYPTIK 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899 469 MYKKGeNPVSYAGMLGTKDLLKFIQlnRISYPVnitsIQEAEEYLSGELYKDLILYSSVSVLGLF-SPTMKTAKEDFSEA 547
Cdd:PTZ00102 112 FFNKG-NPVNYSGGRTADGIVSWIK--KLTGPA----VTEVESASEIKLIAKKIFVAFYGEYTSKdSELYKKFEEVADKH 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899 548 GNYLKGYVITGIYSEEDVLLlstkyaaslpalllarHTEGKIESIPLASThAQDIVQIITDALLEMFPEITVENLPSYFr 627
Cdd:PTZ00102 185 REHAKFFVKKHEGKNKIYVL----------------HKDEEGVELFMGKT-KEELEEFVSTESFPLFAEINAENYRRYI- 246

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 929654899 628 lQKPLLILFSDGTvNPQYKKA--ILTLVKQKYLDSFTPCWLN 667
Cdd:PTZ00102 247 -SSGKDLVWFCGT-TEDYDKYksVVRKVARKLREKYAFVWLD 286
PTZ00051 PTZ00051
thioredoxin; Provisional
 397-474 3.45e-04

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 40.63  E-value: 3.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899 397 TEETFNATVmASDSIVL--FYAGWQAVSMAFLQSYIDVAvklKGTSTMLLTRINCADWSDVCTKQNVTEFPIIKMYKKGE 474
Cdd:PTZ00051   7 SQAEFESTL-SQNELVIvdFYAEWCGPCKRIAPFYEECS---KEYTKMVFVKVDVDELSEVAEKENITSMPTFKVFKNGS 82
 
Name Accession Description Interval E-value
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
533-722 1.02e-21

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 93.20  E-value: 1.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899  533 FSPTMKTAKEDFSEAGNYLKGYVITGIYSEEDVLllsTKYAASLPALLLARHTEGKIESIPLASTHAQDIVQIITDALLE 612
Cdd:pfam13848   1 FEDKDSPLYEIFRKAAKELKGDVRFGITFSKEVA---DKYNIKEPAILLFRKFDEETVHYPGDSINFEDLKKFIQKNCLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899  613 MFPEITVENLPSYFRLQKPLLILF--SDGTVNPQYKKAILTLVKQKYLDSFTPCWLNLKNTPVgrgILRaYFDPLPPLP- 689
Cdd:pfam13848  78 LVREFTPENAEELFEEGIPPLLLLflKKDDESTEEFKKALEKVAKKFRGKINFALVDAKSFGR---PLE-YFGLSESDLp 153

                         170       180       190
                  ....*....|....*....|....*....|...
gi 929654899  690 LLVLVNLHSgGQVFAFPSDQaIIEENLVLWLKK 722
Cdd:pfam13848 154 VIVIVDSFS-HMYKYFPSDE-FSPESLKEFIND 184
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 394-492 6.46e-21

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: 88.05  E-value: 6.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899 394 VELTEETFNATVMAS-DSIVLFYAGWQAVSMAFLQSYIDVAVKLKGTSTMLLTRINCADWSDVCTKQNVTEFPIIKMYKK 472
Cdd:cd02961    1 VELTDDNFDELVKDSkDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPN 80

                         90       100
                 ....*....|....*....|.
gi 929654899 473 G-ENPVSYAGMLGTKDLLKFI 492
Cdd:cd02961   81 GsKEPVKYEGPRTLESLVEFI 101
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 393-492 7.89e-10

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: 56.47  E-value: 7.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899  393 TVELTEETFNATVMASDSIVL--FYAGW----QAVS---MAFLQSYIDVAVKLKgtstmlltrINCADWSDVCTKQNVTE 463
Cdd:pfam00085   2 VVVLTDANFDEVVQKSSKPVLvdFYAPWcgpcKMLApeyEELAQEYKGNVVFAK---------VDVDENPDLASKYGVRG 72

                          90       100
                  ....*....|....*....|....*....
gi 929654899  464 FPIIKMYKKGENPVSYAGMLGTKDLLKFI 492
Cdd:pfam00085  73 YPTLIFFKNGQPVDDYVGARPKDALAAFL 101
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 394-492 1.64e-08

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


Pssm-ID: 239293 [Multi-domain]  Cd Length: 104  Bit Score: 52.94  E-value: 1.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899 394 VELTEETFNATVMAS--DSIVLFYAGWQAVSMAFLQSYIDVAVKLKGTSTMLLTRINcADWSDVCTKQNVTEFPIIKMYK 471
Cdd:cd02995    3 KVVVGKNFDEVVLDSdkDVLVEFYAPWCGHCKALAPIYEELAEKLKGDDNVVIAKMD-ATANDVPSEFVVDGFPTILFFP 81

                         90       100
                 ....*....|....*....|...
gi 929654899 472 KG--ENPVSYAGMLGTKDLLKFI 492
Cdd:cd02995   82 AGdkSNPIKYEGDRTLEDLIKFI 104
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 394-492 3.32e-08

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: 51.91  E-value: 3.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899 394 VELTEETFNATVMASDS--IVLFYAGWQAVSMAFLQSYIDVAVKLKGTstMLLTRINCADWSDVCTKQNVTEFPIIKMYK 471
Cdd:cd03004    4 ITLTPEDFPELVLNRKEpwLVDFYAPWCGPCQALLPELRKAARALKGK--VKVGSVDCQKYESLCQQANIRAYPTIRLYP 81

                         90       100
                 ....*....|....*....|...
gi 929654899 472 KGE-NPVSYAG-MLGTKDLLKFI 492
Cdd:cd03004   82 GNAsKYHSYNGwHRDADSILEFI 104
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 391-661 7.15e-08

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: 55.84  E-value: 7.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899  391 ELTVELTEETFNATVMASDSI-VLFYAGWQAVSMAFLQSYIDVAVKLKG-TSTMLLTRINCADWSDVCTKQNVTEFPIIK 468
Cdd:TIGR01130   1 EDVLVLTKDNFDDFIKSHEFVlVEFYAPWCGHCKSLAPEYEKAADELKKkGPPIKLAKVDATEEKDLAQKYGVSGYPTLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899  469 MYKKGENPVS-YAGMLGTKDLLKFiqLNRISYP--VNITSIQEAEEYLSGElykdlilysSVSVLGLFSPTMKTAKEDFS 545
Cdd:TIGR01130  81 IFRNGEDSVSdYNGPRDADGIVKY--MKKQSGPavKEIETVADLEAFLADD---------DVVVIGFFKDLDSELNDTFL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899  546 EAGNYLKGYVITGIYSEEDVLLLSTKYAASLPALLLARHTEGKIESIPLA-STHAQDIVQIITDALLEMFPEITVENLPS 624
Cdd:TIGR01130 150 SVAEKLRDVYFFFAHSSDVAAFAKLGAFPDSVVLFKPKDEDEKFSKVDGEmDTDVSDLEKFIRAESLPLVGEFTQETAAK 229

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 929654899  625 YFrLQKPL--LILFSDGTVNP-QYKKAILTLVKQKYLDSF 661
Cdd:TIGR01130 230 YF-ESGPLvvLYYNVDESLDPfEELRNRFLEAAKKFRGKF 268
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 393-488 1.17e-06

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: 47.66  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899 393 TVELTEETFNATVMASDSIVLFYAGWQAVSMAFLQSYIDVAVKL-KGTSTMLLTRINCADWSDVCTKQNVTEFPIIKMYK 471
Cdd:cd03005    2 VLELTEDNFDHHIAEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFnNENPSVKIAKVDCTQHRELCSEFQVRGYPTLLLFK 81

                         90
                 ....*....|....*..
gi 929654899 472 KGENPVSYAgmlGTKDL 488
Cdd:cd03005   82 DGEKVDKYK---GTRDL 95
PDI_a_EFP1_N cd03006
PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase ...
 410-492 1.27e-06

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: 47.85  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899 410 SIVLFYAGWQAVSMAFLQSYIDVAVKLkgTSTMLLTRINCADWSDVCTKQ-NVTEFPIIKMYKKGENPVSYAGMLGTKDL 488
Cdd:cd03006   32 SLVMYYAPWDAQSQAARQEFEQVAQKL--SDQVLFVAINCWWPQGKCRKQkHFFYFPVIHLYYRSRGPIEYKGPMRAPYM 109


                 ....
gi 929654899 489 LKFI 492
Cdd:cd03006  110 EKFV 113
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 394-481 1.45e-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: 47.28  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899 394 VELTEETFNATVMASDS--IVLFYAGWQAVSMAFLQSYIDVAVKLKGTSTmlLTRINCADWSDVCTKQNVTEFPIIKMYK 471
Cdd:cd03001    3 VELTDSNFDKKVLNSDDvwLVEFYAPWCGHCKNLAPEWKKAAKALKGIVK--VGAVDADVHQSLAQQYGVRGFPTIKVFG 80

                         90
                 ....*....|.
gi 929654899 472 KGEN-PVSYAG 481
Cdd:cd03001   81 AGKNsPQDYQG 91
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 391-667 9.09e-06

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 48.98  E-value: 9.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899 391 ELTVELTEETFNATVMASDS-IVLFYAGWQAVSMAFLQSYIDVAVKLK-GTSTMLLTRINCADWSDVCTKQNVTEFPIIK 468
Cdd:PTZ00102  32 EHVTVLTDSTFDKFITENEIvLVKFYAPWCGHCKRLAPEYKKAAKMLKeKKSEIVLASVDATEEMELAQEFGVRGYPTIK 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899 469 MYKKGeNPVSYAGMLGTKDLLKFIQlnRISYPVnitsIQEAEEYLSGELYKDLILYSSVSVLGLF-SPTMKTAKEDFSEA 547
Cdd:PTZ00102 112 FFNKG-NPVNYSGGRTADGIVSWIK--KLTGPA----VTEVESASEIKLIAKKIFVAFYGEYTSKdSELYKKFEEVADKH 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899 548 GNYLKGYVITGIYSEEDVLLlstkyaaslpalllarHTEGKIESIPLASThAQDIVQIITDALLEMFPEITVENLPSYFr 627
Cdd:PTZ00102 185 REHAKFFVKKHEGKNKIYVL----------------HKDEEGVELFMGKT-KEELEEFVSTESFPLFAEINAENYRRYI- 246

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 929654899 628 lQKPLLILFSDGTvNPQYKKA--ILTLVKQKYLDSFTPCWLN 667
Cdd:PTZ00102 247 -SSGKDLVWFCGT-TEDYDKYksVVRKVARKLREKYAFVWLD 286
PTZ00051 PTZ00051
thioredoxin; Provisional
 397-474 3.45e-04

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 40.63  E-value: 3.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654899 397 TEETFNATVmASDSIVL--FYAGWQAVSMAFLQSYIDVAvklKGTSTMLLTRINCADWSDVCTKQNVTEFPIIKMYKKGE 474
Cdd:PTZ00051   7 SQAEFESTL-SQNELVIvdFYAEWCGPCKRIAPFYEECS---KEYTKMVFVKVDVDELSEVAEKENITSMPTFKVFKNGS 82
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 447-491 6.76e-04

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


Pssm-ID: 239301 [Multi-domain]  Cd Length: 101  Bit Score: 39.82  E-value: 6.76e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 929654899 447 INCADWSDVCTKQNVTEFPIIKMYKKGENPVSYAGMLGTKDLLKF 491
Cdd:cd03003   56 VNCGDDRMLCRSQGVNSYPSLYVFPSGMNPEKYYGDRSKESLVKF 100
 
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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