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Conserved domains on  [gi|1622849033|ref|XP_028686369|]
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dnaJ homolog subfamily C member 10 isoform X1 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 129-229 1.59e-68

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: 220.86  E-value: 1.59e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 129 PEIITLERREFDAAVNSGELWFVNFYSPGCSHCHDLAPTWRDFAKEVDGLLRIGAVNCGDDRMLCRMKGVNSYPSLFIFR 208
Cdd:cd03003     1 PEIVTLDRGDFDAAVNSGEIWFVNFYSPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDDRMLCRSQGVNSYPSLYVFP 80

                          90       100
                  ....*....|....*....|.
gi 1622849033 209 SGMAPVKYHGDRSKESLVSFA 229
Cdd:cd03003    81 SGMNPEKYYGDRSKESLVKFA 101
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 556-663 1.01e-55

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: 186.34  E-value: 1.01e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 556 PSVVSLTPTTFNELVTQRKhnEVWMVDFYSPWCHPCQVLMPEWKRMARTLTGLINVGSIDCQQYHSFCAQENVQRYPEIR 635
Cdd:cd03004     1 PSVITLTPEDFPELVLNRK--EPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIR 78

                          90       100
                  ....*....|....*....|....*...
gi 1622849033 636 FFPPksnKAYQYHSYNGWNRDAYSLRIW 663
Cdd:cd03004    79 LYPG---NASKYHSYNGWHRDADSILEF 103
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 670-775 4.68e-50

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: 170.94  E-value: 4.68e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 670 QVSTDLTPQTFSEKVLQGKNHWVIDFYAPWCGPCQNFAPEFELLARMIKGKVKAGKVDCQAYAQTCQKAGIRAYPTVKFY 749
Cdd:cd03004     1 PSVITLTPEDFPELVLNRKEPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLY 80

                          90       100
                  ....*....|....*....|....*.
gi 1622849033 750 FYERakRNFQEEQINTRDAKAIAALI 775
Cdd:cd03004    81 PGNA--SKYHSYNGWHRDADSILEFI 104
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 453-550 7.12e-50

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: 170.17  E-value: 7.12e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 453 SHVTTLGPQNFPA---NDKEPWLVDFFAPWCPPCRALLPELRRASNLLYGQLKFGTLDCTVHEGLCNMYNIQAYPTTVVF 529
Cdd:cd03004     1 PSVITLTPEDFPElvlNRKEPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLY 80

                          90       100
                  ....*....|....*....|....
gi 1622849033 530 NQ--SNIHEYEGHHS-AEQILEFI 550
Cdd:cd03004    81 PGnaSKYHSYNGWHRdADSILEFI 104
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 35-97 1.69e-28

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


:

Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 108.33  E-value: 1.69e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622849033  35 DFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKDEDLRKKYD 97
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
ER_PDI_fam super family cl36828
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 130-551 3.91e-15

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


The actual alignment was detected with superfamily member TIGR01130:

Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 78.56  E-value: 3.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 130 EIITLERREFDAAVNSGELWFVNFYSPGCSHCHDLAPTWRDFAKEV---DGLLRIGAVNCGDDRMLCRMKGVNSYPSLFI 206
Cdd:TIGR01130   2 DVLVLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELkkkGPPIKLAKVDATEEKDLAQKYGVSGYPTLKI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 207 FRSG-MAPVKYHGDRSKESLVSFAMQHVRSTVTELWTGNFVNsiqtAFAAGIGWLITFCSKGGDCLTSQTRLRLSGMLDG 285
Cdd:TIGR01130  82 FRNGeDSVSDYNGPRDADGIVKYMKKQSGPAVKEIETVADLE----AFLADDDVVVIGFFKDLDSELNDTFLSVAEKLRD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 286 lVNVGWMDCATQDNLCKSldittsttAYFPPGATLNNREK---NSILFLNSLDAKEIYLE---VIHNLPDFELLSANTLE 359
Cdd:TIGR01130 158 -VYFFFAHSSDVAAFAKL--------GAFPDSVVLFKPKDedeKFSKVDGEMDTDVSDLEkfiRAESLPLVGEFTQETAA 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 360 DRLAhhRWLLFFHFGK-NENSNDHELKKLKTLL--KNDHIQVGRFDCSSAPDicsNLYVFQ---------PSLAVFKGQG 427
Cdd:TIGR01130 229 KYFE--SGPLVVLYYNvDESLDPFEELRNRFLEaaKKFRGKFVNFAVADEED---FGRELEyfglkaekfPAVAIQDLEG 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 428 TKEYEIHHGKKILYDILAFAKESVNSHVT-TLGPQNFPANDKEPW-------------------LVDFFAPWCPPCRALL 487
Cdd:TIGR01130 304 NKKYPMDQEEFSSENLEAFVKDFLDGKLKpYLKSEPIPEDDEGPVkvlvgknfdeivldetkdvLVEFYAPWCGHCKNLA 383

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622849033 488 P---EL-----RRASNLLYGQlkfgtLDCTVHEglCNMYNIQAYPTTVVF---NQSNIHEYEGHHSAEQILEFIE 551
Cdd:TIGR01130 384 PiyeELaekykDAESDVVIAK-----MDATAND--VPPFEVEGFPTIKFVpagKKSEPVPYDGDRTLEDFSKFIA 451
 
Name Accession Description Interval E-value
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 129-229 1.59e-68

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: 220.86  E-value: 1.59e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 129 PEIITLERREFDAAVNSGELWFVNFYSPGCSHCHDLAPTWRDFAKEVDGLLRIGAVNCGDDRMLCRMKGVNSYPSLFIFR 208
Cdd:cd03003     1 PEIVTLDRGDFDAAVNSGEIWFVNFYSPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDDRMLCRSQGVNSYPSLYVFP 80

                          90       100
                  ....*....|....*....|.
gi 1622849033 209 SGMAPVKYHGDRSKESLVSFA 229
Cdd:cd03003    81 SGMNPEKYYGDRSKESLVKFA 101
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 556-663 1.01e-55

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: 186.34  E-value: 1.01e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 556 PSVVSLTPTTFNELVTQRKhnEVWMVDFYSPWCHPCQVLMPEWKRMARTLTGLINVGSIDCQQYHSFCAQENVQRYPEIR 635
Cdd:cd03004     1 PSVITLTPEDFPELVLNRK--EPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIR 78

                          90       100
                  ....*....|....*....|....*...
gi 1622849033 636 FFPPksnKAYQYHSYNGWNRDAYSLRIW 663
Cdd:cd03004    79 LYPG---NASKYHSYNGWHRDADSILEF 103
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 670-775 4.68e-50

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: 170.94  E-value: 4.68e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 670 QVSTDLTPQTFSEKVLQGKNHWVIDFYAPWCGPCQNFAPEFELLARMIKGKVKAGKVDCQAYAQTCQKAGIRAYPTVKFY 749
Cdd:cd03004     1 PSVITLTPEDFPELVLNRKEPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLY 80

                          90       100
                  ....*....|....*....|....*.
gi 1622849033 750 FYERakRNFQEEQINTRDAKAIAALI 775
Cdd:cd03004    81 PGNA--SKYHSYNGWHRDADSILEFI 104
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 453-550 7.12e-50

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: 170.17  E-value: 7.12e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 453 SHVTTLGPQNFPA---NDKEPWLVDFFAPWCPPCRALLPELRRASNLLYGQLKFGTLDCTVHEGLCNMYNIQAYPTTVVF 529
Cdd:cd03004     1 PSVITLTPEDFPElvlNRKEPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLY 80

                          90       100
                  ....*....|....*....|....
gi 1622849033 530 NQ--SNIHEYEGHHS-AEQILEFI 550
Cdd:cd03004    81 PGnaSKYHSYNGWHRdADSILEFI 104
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 35-97 1.69e-28

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 108.33  E-value: 1.69e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622849033  35 DFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKDEDLRKKYD 97
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 35-157 1.72e-28

DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440252 [Multi-domain]  Cd Length: 139  Bit Score: 111.33  E-value: 1.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033  35 DFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLEDNQGGQYES 114
Cdd:COG0484     1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAES 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622849033 115 WNYYRYDFGIYDDDPEIITLERREFDAAVNSGELWFVNFYSPG 157
Cdd:COG0484    81 AAAEAAAAEAKEEAAEAGASEYEAIAEEASQLRLASLLLLLAL 123
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 32-110 1.78e-26

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 112.16  E-value: 1.78e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849033  32 TDQDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLEDNQGG 110
Cdd:PRK10767    2 AKRDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYDQYGHAAFEQGGGG 80
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 675-777 3.61e-24

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: 97.30  E-value: 3.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 675 LTPQTFSEKVLQGKNHWVIDFYAPWCGPCQNFAPEFELLARMIKGKVKAGKVDCQAYAQTCQKAGIRAYPTVKFYfyera 754
Cdd:pfam00085   5 LTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFF----- 79

                          90       100
                  ....*....|....*....|....*
gi 1622849033 755 kRNFQE--EQINTRDAKAIAALINE 777
Cdd:pfam00085  80 -KNGQPvdDYVGARPKDALAAFLKA 103
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 673-749 3.17e-22

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


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 92.19  E-value: 3.17e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622849033 673 TDLTPQTFSEKVLQGKNHWVIDFYAPWCGPCQNFAPEFELLARMIKGKVKAGKVDCQAYAQTCQKAGIRAYPTVKFY 749
Cdd:COG3118     3 VELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLF 79
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 35-89 4.06e-22

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 89.91  E-value: 4.06e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622849033  35 DFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKD 89
Cdd:cd06257     1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
DnaJ smart00271
DnaJ molecular chaperone homology domain;
34-91 5.16e-21

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 86.90  E-value: 5.16e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849033   34 QDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNP-NAHGDFLKINRAYEVLKDED 91
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKeEAEEKFKEINEAYEVLSDPE 59
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 454-554 1.50e-20

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


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 87.18  E-value: 1.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 454 HVTTLGPQNFPA---NDKEPWLVDFFAPWCPPCRALLPELRRASNLLYGQLKFGTLDCTVHEGLCNMYNIQAYPTTVVF- 529
Cdd:COG3118     1 AVVELTDENFEEevlESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLFk 80

                          90       100
                  ....*....|....*....|....*
gi 1622849033 530 NQSNIHEYEGHHSAEQILEFIEDLM 554
Cdd:COG3118    81 DGQPVDRFVGALPKEQLREFLDKVL 105
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
35-110 9.59e-20

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 92.96  E-value: 9.59e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849033  35 DFYSLLGVSKTASSREIRQAFKKLALKLHPDKNpNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLeDNQGG 110
Cdd:NF037946    6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRN-KAPDAAEIFAEINEAYEVLSNPEKRANYDKYGHDGV-DGEGG 79
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 465-552 5.41e-19

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: 82.67  E-value: 5.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 465 ANDKEPWLVDFFAPWCPPCRALLPELRRASNLLYGQLKFGTLDCTVHEGLCNMYNIQAYPTTVVFNQSN-IHEYEGHHSA 543
Cdd:pfam00085  15 QKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKNGQpVDDYVGARPK 94


                  ....*....
gi 1622849033 544 EQILEFIED 552
Cdd:pfam00085  95 DALAAFLKA 103
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 453-749 1.57e-18

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: 89.35  E-value: 1.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 453 SHVTTLGPQNFPA--NDKEPWLVDFFAPWCPPCRALLPELRRASNLLYGQ---LKFGTLDCTVHEGLCNMYNIQAYPTTV 527
Cdd:TIGR01130   1 EDVLVLTKDNFDDfiKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKgppIKLAKVDATEEKDLAQKYGVSGYPTLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 528 VFNQS--NIHEYEGHHSAEQILEFIEDLMNPSVVSLTP---------------------------TTFNEL--------- 569
Cdd:TIGR01130  81 IFRNGedSVSDYNGPRDADGIVKYMKKQSGPAVKEIETvadleafladddvvvigffkdldselnDTFLSVaeklrdvyf 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 570 ----------------------VTQRKH--NEVWMVDFYSPWC------------------------------------- 588
Cdd:TIGR01130 161 ffahssdvaafaklgafpdsvvLFKPKDedEKFSKVDGEMDTDvsdlekfiraeslplvgeftqetaakyfesgplvvly 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 589 -------HPCQVLMPEWKRMARTLTG-LINVGSIDCQQYHSFCAQENV--QRYPEIRFFPPKSNKAYqyhSYNGWNRDAY 658
Cdd:TIGR01130 241 ynvdeslDPFEELRNRFLEAAKKFRGkFVNFAVADEEDFGRELEYFGLkaEKFPAVAIQDLEGNKKY---PMDQEEFSSE 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 659 SLRIWGLGFLpqvSTDLTPQTFSE----------KVLQGKNH--WVID--------FYAPWCGPCQNFAPEFELLARMIK 718
Cdd:TIGR01130 318 NLEAFVKDFL---DGKLKPYLKSEpipeddegpvKVLVGKNFdeIVLDetkdvlveFYAPWCGHCKNLAPIYEELAEKYK 394

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1622849033 719 G---KVKAGKVDcqAYAQTCQKAGIRAYPTVKFY 749
Cdd:TIGR01130 395 DaesDVVIAKMD--ATANDVPPFEVEGFPTIKFV 426
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 675-749 2.91e-18

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: 80.41  E-value: 2.91e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622849033 675 LTPQTFSEKVLQGKNHWVIDFYAPWCGPCQNFAPEFELLARMIKGKVKAGKVDCQAYAQTCQKAGIRAYPTVKFY 749
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLF 75
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 439-559 5.50e-17

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 84.80  E-value: 5.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 439 ILYDILAFAKES---VNSHVTTLGPQNFPA--NDKEPWLVDFFAPWCPPCRALLPELRRASNLLY---GQLKFGTLDCTV 510
Cdd:PTZ00102   15 ILLAFAVFGSAEehfISEHVTVLTDSTFDKfiTENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKekkSEIVLASVDATE 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1622849033 511 HEGLCNMYNIQAYPTTVVFNQSNIHEYEGHHSAEQILEFIEDLMNPSVV 559
Cdd:PTZ00102   95 EMELAQEFGVRGYPTIKFFNKGNPVNYSGGRTADGIVSWIKKLTGPAVT 143
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 130-228 4.94e-16

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: 74.19  E-value: 4.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 130 EIITLERREFDAAVNSGELWF-VNFYSPGCSHCHDLAPTWRDFAKEVDGLLRIGAVNCGDDRMLCRMKGVNSYPSLFIFR 208
Cdd:pfam00085   1 VVVVLTDANFDEVVQKSSKPVlVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFK 80

                          90       100
                  ....*....|....*....|
gi 1622849033 209 SGMAPVKYHGDRSKESLVSF 228
Cdd:pfam00085  81 NGQPVDDYVGARPKDALAAF 100
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 673-777 1.07e-15

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 80.57  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 673 TDLTPQTFsEKVLQGKNHWVIDFYAPWCGPCQNFAPEFELLARMIK---GKVKAGKVDCQAYAQTCQKAGIRAYPTVKFy 749
Cdd:PTZ00102   35 TVLTDSTF-DKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKekkSEIVLASVDATEEMELAQEFGVRGYPTIKF- 112

                          90       100
                  ....*....|....*....|....*...
gi 1622849033 750 FYERAKRNFQeeqiNTRDAKAIAALINE 777
Cdd:PTZ00102  113 FNKGNPVNYS----GGRTADGIVSWIKK 136
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 557-646 1.48e-15

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: 73.04  E-value: 1.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 557 SVVSLTPTTFNELVtqRKHNEVWMVDFYSPWCHPCQVLMPEWKRMARTLTGLINVGSIDCQQYHSFCAQENVQRYPEIRF 636
Cdd:pfam00085   1 VVVVLTDANFDEVV--QKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIF 78

                          90
                  ....*....|
gi 1622849033 637 FPPKSNKAYQ 646
Cdd:pfam00085  79 FKNGQPVDDY 88
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 130-551 3.91e-15

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: 78.56  E-value: 3.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 130 EIITLERREFDAAVNSGELWFVNFYSPGCSHCHDLAPTWRDFAKEV---DGLLRIGAVNCGDDRMLCRMKGVNSYPSLFI 206
Cdd:TIGR01130   2 DVLVLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELkkkGPPIKLAKVDATEEKDLAQKYGVSGYPTLKI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 207 FRSG-MAPVKYHGDRSKESLVSFAMQHVRSTVTELWTGNFVNsiqtAFAAGIGWLITFCSKGGDCLTSQTRLRLSGMLDG 285
Cdd:TIGR01130  82 FRNGeDSVSDYNGPRDADGIVKYMKKQSGPAVKEIETVADLE----AFLADDDVVVIGFFKDLDSELNDTFLSVAEKLRD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 286 lVNVGWMDCATQDNLCKSldittsttAYFPPGATLNNREK---NSILFLNSLDAKEIYLE---VIHNLPDFELLSANTLE 359
Cdd:TIGR01130 158 -VYFFFAHSSDVAAFAKL--------GAFPDSVVLFKPKDedeKFSKVDGEMDTDVSDLEkfiRAESLPLVGEFTQETAA 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 360 DRLAhhRWLLFFHFGK-NENSNDHELKKLKTLL--KNDHIQVGRFDCSSAPDicsNLYVFQ---------PSLAVFKGQG 427
Cdd:TIGR01130 229 KYFE--SGPLVVLYYNvDESLDPFEELRNRFLEaaKKFRGKFVNFAVADEED---FGRELEyfglkaekfPAVAIQDLEG 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 428 TKEYEIHHGKKILYDILAFAKESVNSHVT-TLGPQNFPANDKEPW-------------------LVDFFAPWCPPCRALL 487
Cdd:TIGR01130 304 NKKYPMDQEEFSSENLEAFVKDFLDGKLKpYLKSEPIPEDDEGPVkvlvgknfdeivldetkdvLVEFYAPWCGHCKNLA 383

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622849033 488 P---EL-----RRASNLLYGQlkfgtLDCTVHEglCNMYNIQAYPTTVVF---NQSNIHEYEGHHSAEQILEFIE 551
Cdd:TIGR01130 384 PiyeELaekykDAESDVVIAK-----MDATAND--VPPFEVEGFPTIKFVpagKKSEPVPYDGDRTLEDFSKFIA 451
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 149-262 3.16e-14

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 72.74  E-value: 3.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 149 WFVNFYSPGCSHCHDLAPTWRDFAKEVDGLLRIGAVNCGDDRMLCRMKGVNSYPSLFIFRSGMAPVKYHGDRSKESLVSF 228
Cdd:PTZ00443   55 WFVKFYAPWCSHCRKMAPAWERLAKALKGQVNVADLDATRALNLAKRFAIKGYPTLLLFDKGKMYQYEGGDRSTEKLAAF 134

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622849033 229 AMQHVRSTVtelwtGNFVNSIQTAFAAGIGWLIT 262
Cdd:PTZ00443  135 ALGDFKKAL-----GAPVPAPLSFFALTIDFFVS 163
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 465-553 1.34e-12

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


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 64.62  E-value: 1.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 465 ANDKEPWLVDFFAPWCPPCRALLPELRRASNLLYGQLKFGTLDCTVHEGLCNMYNIQAYPTTVVF-NQSNIHEYEGHHSA 543
Cdd:TIGR01068  11 ASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFkNGKEVDRSVGALPK 90

                          90
                  ....*....|
gi 1622849033 544 EQILEFIEDL 553
Cdd:TIGR01068  91 AALKQLINKN 100
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 131-233 3.96e-12

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: 63.30  E-value: 3.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 131 IITLERREFDAAV-NSGELWFVNFYSPGCSHCHDLAPTWRDFAKEVDGLLRIGAVNCGDDRMLCRMKGVNSYPSLFIFRS 209
Cdd:COG3118     2 VVELTDENFEEEVlESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLFKD 81

                          90       100
                  ....*....|....*....|....
gi 1622849033 210 GMAPVKYHGDRSKESLVSFAMQHV 233
Cdd:COG3118    82 GQPVDRFVGALPKEQLREFLDKVL 105
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 551-663 4.00e-12

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 69.39  E-value: 4.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 551 EDLMNPSVVSLTPTTFNELVTQrkhNEVWMVDFYSPWCHPCQVLMPEWKRMARTLTGL---INVGSIDCQQYHSFCAQEN 627
Cdd:PTZ00102   27 EHFISEHVTVLTDSTFDKFITE---NEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKkseIVLASVDATEEMELAQEFG 103

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1622849033 628 VQRYPEIRFFPPKSNKAYqyhsynGWNRDAYSLRIW 663
Cdd:PTZ00102  104 VRGYPTIKFFNKGNPVNY------SGGRTADGIVSW 133
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 557-637 2.35e-11

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: 60.99  E-value: 2.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 557 SVVSLTPTTFNELVTQRkhNEVWMVDFYSPWCHPCQVLMPEWKRMARTLTGLINVGSIDCQQYHSFCAQENVQRYPEIRF 636
Cdd:COG3118     1 AVVELTDENFEEEVLES--DKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLL 78


                  .
gi 1622849033 637 F 637
Cdd:COG3118    79 F 79
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 480-660 3.56e-08

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: 56.56  E-value: 3.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 480 CPPC-RALLP-ELRRASNLLYGQLKfgTLDCTVHEGlcnmyNIQAYPTTVVFNQsniheyEGHHSAEQILEfiedlmNPS 557
Cdd:TIGR00424 292 CEPCtRPVLPgQHEREGRWWWEDAK--AKECGLHKG-----NIKEETLDGAVNG------NGSDAVADIFD------SNN 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 558 VVSLTPTTFNELVTQRKHNEVWMVDFYSPWCHPCQVLMPEWKRMARTLTGL-INVGSI--DCQQyHSFCAQE-NVQRYPE 633
Cdd:TIGR00424 353 VVSLSRPGIENLLKLEERKEAWLVVLYAPWCPFCQAMEASYLELAEKLAGSgVKVAKFraDGDQ-KEFAKQElQLGSFPT 431

                         170       180
                  ....*....|....*....|....*..
gi 1622849033 634 IRFFPPKSNKAYQYHSYngwNRDAYSL 660
Cdd:TIGR00424 432 ILFFPKHSSRPIKYPSE---KRDVDSL 455
 
Name Accession Description Interval E-value
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 129-229 1.59e-68

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: 220.86  E-value: 1.59e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 129 PEIITLERREFDAAVNSGELWFVNFYSPGCSHCHDLAPTWRDFAKEVDGLLRIGAVNCGDDRMLCRMKGVNSYPSLFIFR 208
Cdd:cd03003     1 PEIVTLDRGDFDAAVNSGEIWFVNFYSPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDDRMLCRSQGVNSYPSLYVFP 80

                          90       100
                  ....*....|....*....|.
gi 1622849033 209 SGMAPVKYHGDRSKESLVSFA 229
Cdd:cd03003    81 SGMNPEKYYGDRSKESLVKFA 101
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 556-663 1.01e-55

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: 186.34  E-value: 1.01e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 556 PSVVSLTPTTFNELVTQRKhnEVWMVDFYSPWCHPCQVLMPEWKRMARTLTGLINVGSIDCQQYHSFCAQENVQRYPEIR 635
Cdd:cd03004     1 PSVITLTPEDFPELVLNRK--EPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIR 78

                          90       100
                  ....*....|....*....|....*...
gi 1622849033 636 FFPPksnKAYQYHSYNGWNRDAYSLRIW 663
Cdd:cd03004    79 LYPG---NASKYHSYNGWHRDADSILEF 103
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 670-775 4.68e-50

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: 170.94  E-value: 4.68e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 670 QVSTDLTPQTFSEKVLQGKNHWVIDFYAPWCGPCQNFAPEFELLARMIKGKVKAGKVDCQAYAQTCQKAGIRAYPTVKFY 749
Cdd:cd03004     1 PSVITLTPEDFPELVLNRKEPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLY 80

                          90       100
                  ....*....|....*....|....*.
gi 1622849033 750 FYERakRNFQEEQINTRDAKAIAALI 775
Cdd:cd03004    81 PGNA--SKYHSYNGWHRDADSILEFI 104
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 453-550 7.12e-50

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: 170.17  E-value: 7.12e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 453 SHVTTLGPQNFPA---NDKEPWLVDFFAPWCPPCRALLPELRRASNLLYGQLKFGTLDCTVHEGLCNMYNIQAYPTTVVF 529
Cdd:cd03004     1 PSVITLTPEDFPElvlNRKEPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLY 80

                          90       100
                  ....*....|....*....|....
gi 1622849033 530 NQ--SNIHEYEGHHS-AEQILEFI 550
Cdd:cd03004    81 PGnaSKYHSYNGWHRdADSILEFI 104
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 132-229 3.88e-30

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


Pssm-ID: 239259 [Multi-domain]  Cd Length: 101  Bit Score: 114.63  E-value: 3.88e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 132 ITLERREFDAAVNSGELWFVNFYSPGCSHCHDLAPTWRDFAKEV--DGLLRIGAVNCGDDRMLCRMKGVNSYPSLFIFRS 209
Cdd:cd02961     1 VELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELkgDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPN 80

                          90       100
                  ....*....|....*....|.
gi 1622849033 210 GMA-PVKYHGDRSKESLVSFA 229
Cdd:cd02961    81 GSKePVKYEGPRTLESLVEFI 101
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 673-775 1.36e-28

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


Pssm-ID: 239259 [Multi-domain]  Cd Length: 101  Bit Score: 110.01  E-value: 1.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 673 TDLTPQTFsEKVLQGKNHWVIDFYAPWCGPCQNFAPEFELLARMIK--GKVKAGKVDCQAYAQTCQKAGIRAYPTVKFYf 750
Cdd:cd02961     1 VELTDDNF-DELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKgdGKVVVAKVDCTANNDLCSEYGVRGYPTIKLF- 78

                          90       100
                  ....*....|....*....|....*
gi 1622849033 751 yeRAKRNFQEEQINTRDAKAIAALI 775
Cdd:cd02961    79 --PNGSKEPVKYEGPRTLESLVEFI 101
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 35-97 1.69e-28

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 108.33  E-value: 1.69e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622849033  35 DFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKDEDLRKKYD 97
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 35-157 1.72e-28

DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440252 [Multi-domain]  Cd Length: 139  Bit Score: 111.33  E-value: 1.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033  35 DFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLEDNQGGQYES 114
Cdd:COG0484     1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAES 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622849033 115 WNYYRYDFGIYDDDPEIITLERREFDAAVNSGELWFVNFYSPG 157
Cdd:COG0484    81 AAAEAAAAEAKEEAAEAGASEYEAIAEEASQLRLASLLLLLAL 123
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 456-550 5.62e-28

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: 108.47  E-value: 5.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 456 TTLGPQNFPA--NDKEPWLVDFFAPWCPPCRALLPELRRASNLLY--GQLKFGTLDCTVHEGLCNMYNIQAYPTTVVF-- 529
Cdd:cd02961     1 VELTDDNFDElvKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKgdGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFpn 80

                          90       100
                  ....*....|....*....|.
gi 1622849033 530 NQSNIHEYEGHHSAEQILEFI 550
Cdd:cd02961    81 GSKEPVKYEGPRTLESLVEFI 101
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 559-663 6.69e-28

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: 108.08  E-value: 6.69e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 559 VSLTPTTFNELVTQRKHnevWMVDFYSPWCHPCQVLMPEWKRMARTL--TGLINVGSIDCQQYHSFCAQENVQRYPEIRF 636
Cdd:cd02961     1 VELTDDNFDELVKDSKD---VLVEFYAPWCGHCKALAPEYEKLAKELkgDGKVVVAKVDCTANNDLCSEYGVRGYPTIKL 77

                          90       100
                  ....*....|....*....|....*..
gi 1622849033 637 FPPKSNKAYQYHSyngwNRDAYSLRIW 663
Cdd:cd02961    78 FPNGSKEPVKYEG----PRTLESLVEF 100
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 673-773 5.44e-27

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: 105.45  E-value: 5.44e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 673 TDLTPQTFSEKVLQGKNHWVIDFYAPWCGPCQNFAPEFELLARMIKGKVKAGKVDCQAYAQTCQKAGIRAYPTVKFYfye 752
Cdd:cd03001     3 VELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVF--- 79

                          90       100
                  ....*....|....*....|.
gi 1622849033 753 RAKRNFQEEQINTRDAKAIAA 773
Cdd:cd03001    80 GAGKNSPQDYQGGRTAKAIVS 100
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 32-110 1.78e-26

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 112.16  E-value: 1.78e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849033  32 TDQDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLEDNQGG 110
Cdd:PRK10767    2 AKRDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYDQYGHAAFEQGGGG 80
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 558-665 3.10e-26

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: 103.52  E-value: 3.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 558 VVSLTPTTFNELVTQrkHNEVWMVDFYSPWCHPCQVLMPEWKRMARTLTGLINVGSIDCQQYHSFCAQENVQRYPEIRFF 637
Cdd:cd03001     2 VVELTDSNFDKKVLN--SDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVF 79

                          90       100
                  ....*....|....*....|....*...
gi 1622849033 638 PPKSNKAYQyhsYNGwNRDAYSLRIWGL 665
Cdd:cd03001    80 GAGKNSPQD---YQG-GRTAKAIVSAAL 103
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 675-777 3.61e-24

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: 97.30  E-value: 3.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 675 LTPQTFSEKVLQGKNHWVIDFYAPWCGPCQNFAPEFELLARMIKGKVKAGKVDCQAYAQTCQKAGIRAYPTVKFYfyera 754
Cdd:pfam00085   5 LTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFF----- 79

                          90       100
                  ....*....|....*....|....*
gi 1622849033 755 kRNFQE--EQINTRDAKAIAALINE 777
Cdd:pfam00085  80 -KNGQPvdDYVGARPKDALAAFLKA 103
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 673-749 3.17e-22

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


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 92.19  E-value: 3.17e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622849033 673 TDLTPQTFSEKVLQGKNHWVIDFYAPWCGPCQNFAPEFELLARMIKGKVKAGKVDCQAYAQTCQKAGIRAYPTVKFY 749
Cdd:COG3118     3 VELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLF 79
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 455-549 3.84e-22

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


Pssm-ID: 239299 [Multi-domain]  Cd Length: 103  Bit Score: 91.58  E-value: 3.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 455 VTTLGPQNFPA---NDKEPWLVDFFAPWCPPCRALLPELRRASNLLYGQLKFGTLDCTVHEGLCNMYNIQAYPTTVVF-- 529
Cdd:cd03001     2 VVELTDSNFDKkvlNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVFga 81

                          90       100
                  ....*....|....*....|
gi 1622849033 530 NQSNIHEYEGHHSAEQILEF 549
Cdd:cd03001    82 GKNSPQDYQGGRTAKAIVSA 101
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 35-89 4.06e-22

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 89.91  E-value: 4.06e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622849033  35 DFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKD 89
Cdd:cd06257     1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 35-95 5.52e-22

Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 89.67  E-value: 5.52e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622849033  35 DFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKDEDLRKK 95
Cdd:COG5407     1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDPKAEERFKEINEAYELLSDAEKRAR 61
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 32-104 5.55e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 99.11  E-value: 5.55e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622849033  32 TDQDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGL 104
Cdd:PRK14281    1 MKRDYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNKEAEEHFKEVNEAYEVLSNDDKRRRYDQFGHAGV 73
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 35-110 2.86e-21

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 96.84  E-value: 2.86e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849033  35 DFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLEDNQGG 110
Cdd:PRK14284    2 DYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDAEAEKRFKEVSEAYEVLSDAQKRESYDRYGKDGPFAGAGG 77
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 32-127 2.89e-21

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 96.46  E-value: 2.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033  32 TDQDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNpNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLEdnqgGQ 111
Cdd:PRK14298    3 TTRDYYEILGLSKDASVEDIKKAYRKLAMKYHPDKN-KEPDAEEKFKEISEAYAVLSDAEKRAQYDRFGHAGID----NQ 77

                          90
                  ....*....|....*..
gi 1622849033 112 YESWNYYR-YDFGIYDD 127
Cdd:PRK14298   78 YSAEDIFRgADFGGFGD 94
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 32-128 3.24e-21

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 96.38  E-value: 3.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033  32 TDQDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPnNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLEdNQGGQ 111
Cdd:PRK14291    1 AKKDYYEILGVSRNATQEEIKKAYRRLARKYHPDFNK-NPEAEEKFKEINEAYQVLSDPEKRKLYDQFGHAAFS-GSGQQ 78

                          90
                  ....*....|....*..
gi 1622849033 112 YESWNYYRYDFGIYDDD 128
Cdd:PRK14291   79 QQGQEGFSDFGGGNIED 95
DnaJ smart00271
DnaJ molecular chaperone homology domain;
34-91 5.16e-21

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 86.90  E-value: 5.16e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849033   34 QDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNP-NAHGDFLKINRAYEVLKDED 91
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKeEAEEKFKEINEAYEVLSDPE 59
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 130-230 7.09e-21

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: 88.11  E-value: 7.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 130 EIITLERREFDAAV-NSGELWFVNFYSPGCSHCHDLAPTWRDFAKEVDGLLRIGAVNCGDDRMLCRMKGVNSYPSLFIFR 208
Cdd:cd03001     1 DVVELTDSNFDKKVlNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVFG 80

                          90       100
                  ....*....|....*....|...
gi 1622849033 209 SGM-APVKYHGDRSKESLVSFAM 230
Cdd:cd03001    81 AGKnSPQDYQGGRTAKAIVSAAL 103
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 34-111 8.93e-21

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 95.19  E-value: 8.93e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622849033  34 QDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLEDNQGGQ 111
Cdd:PRK14301    4 RDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNPEAEQKFKEAAEAYEVLRDAEKRARYDRFGHAGVNGNGGFG 81
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 454-554 1.50e-20

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


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 87.18  E-value: 1.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 454 HVTTLGPQNFPA---NDKEPWLVDFFAPWCPPCRALLPELRRASNLLYGQLKFGTLDCTVHEGLCNMYNIQAYPTTVVF- 529
Cdd:COG3118     1 AVVELTDENFEEevlESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLFk 80

                          90       100
                  ....*....|....*....|....*
gi 1622849033 530 NQSNIHEYEGHHSAEQILEFIEDLM 554
Cdd:COG3118    81 DGQPVDRFVGALPKEQLREFLDKVL 105
PRK14297 PRK14297
molecular chaperone DnaJ;
34-123 2.57e-20

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 93.69  E-value: 2.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033  34 QDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLedNQGGQYE 113
Cdd:PRK14297    4 KDYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNKEAEEKFKEINEAYQVLSDPQKKAQYDQFGTADF--NGAGGFG 81

                          90
                  ....*....|
gi 1622849033 114 SWNYYRYDFG 123
Cdd:PRK14297   82 SGGFGGFDFS 91
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 674-775 2.65e-20

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: 86.54  E-value: 2.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 674 DLTPQTFSEKVLQGKNHWVIDFYAPWCGPCQNFAPEFELLARMIKG--KVKAGKVDC-QAYAQTCQKAGIRAYPTVKFYf 750
Cdd:cd02998     4 ELTDSNFDKVVGDDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFANedDVVIAKVDAdEANKDLAKKYGVSGFPTLKFF- 82

                          90       100
                  ....*....|....*....|....*.
gi 1622849033 751 yerAKRNFQEEQINT-RDAKAIAALI 775
Cdd:cd02998    83 ---PKGSTEPVKYEGgRDLEDLVKFV 105
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
35-110 9.59e-20

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 92.96  E-value: 9.59e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849033  35 DFYSLLGVSKTASSREIRQAFKKLALKLHPDKNpNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLeDNQGG 110
Cdd:NF037946    6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRN-KAPDAAEIFAEINEAYEVLSNPEKRANYDKYGHDGV-DGEGG 79
PRK14293 PRK14293
molecular chaperone DnaJ;
35-111 4.79e-19

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 89.66  E-value: 4.79e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622849033  35 DFYSLLGVSKTASSREIRQAFKKLALKLHPDKNpNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLEDNQGGQ 111
Cdd:PRK14293    4 DYYEILGVSRDADKDELKRAYRRLARKYHPDVN-KEPGAEDRFKEINRAYEVLSDPETRARYDQFGEAGVSGAAGFP 79
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 465-552 5.41e-19

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: 82.67  E-value: 5.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 465 ANDKEPWLVDFFAPWCPPCRALLPELRRASNLLYGQLKFGTLDCTVHEGLCNMYNIQAYPTTVVFNQSN-IHEYEGHHSA 543
Cdd:pfam00085  15 QKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKNGQpVDDYVGARPK 94


                  ....*....
gi 1622849033 544 EQILEFIED 552
Cdd:pfam00085  95 DALAAFLKA 103
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 138-228 9.35e-19

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: 81.95  E-value: 9.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 138 EFDAAVNSGeLWFVNFYSPGCSHCHDLAPTWRDFAKE---VDGLLRIGAVNCGDDRMLCRMKGVNSYPSLFIFRSGMAPV 214
Cdd:cd03005     9 NFDHHIAEG-NHFVKFFAPWCGHCKRLAPTWEQLAKKfnnENPSVKIAKVDCTQHRELCSEFQVRGYPTLLLFKDGEKVD 87

                          90
                  ....*....|....
gi 1622849033 215 KYHGDRSKESLVSF 228
Cdd:cd03005    88 KYKGTRDLDSLKEF 101
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 34-127 1.34e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 88.70  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033  34 QDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLEdnQGGQYE 113
Cdd:PRK14277    5 KDYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDKEAEQKFKEINEAYEILSDPQKRAQYDQFGHAAFD--PGGFGQ 82

                          90       100
                  ....*....|....*....|..
gi 1622849033 114 --------SWNYYRYDFGIYDD 127
Cdd:PRK14277   83 ggfgqggfGGGGFDFDFGGFGD 104
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 453-749 1.57e-18

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: 89.35  E-value: 1.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 453 SHVTTLGPQNFPA--NDKEPWLVDFFAPWCPPCRALLPELRRASNLLYGQ---LKFGTLDCTVHEGLCNMYNIQAYPTTV 527
Cdd:TIGR01130   1 EDVLVLTKDNFDDfiKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKgppIKLAKVDATEEKDLAQKYGVSGYPTLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 528 VFNQS--NIHEYEGHHSAEQILEFIEDLMNPSVVSLTP---------------------------TTFNEL--------- 569
Cdd:TIGR01130  81 IFRNGedSVSDYNGPRDADGIVKYMKKQSGPAVKEIETvadleafladddvvvigffkdldselnDTFLSVaeklrdvyf 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 570 ----------------------VTQRKH--NEVWMVDFYSPWC------------------------------------- 588
Cdd:TIGR01130 161 ffahssdvaafaklgafpdsvvLFKPKDedEKFSKVDGEMDTDvsdlekfiraeslplvgeftqetaakyfesgplvvly 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 589 -------HPCQVLMPEWKRMARTLTG-LINVGSIDCQQYHSFCAQENV--QRYPEIRFFPPKSNKAYqyhSYNGWNRDAY 658
Cdd:TIGR01130 241 ynvdeslDPFEELRNRFLEAAKKFRGkFVNFAVADEEDFGRELEYFGLkaEKFPAVAIQDLEGNKKY---PMDQEEFSSE 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 659 SLRIWGLGFLpqvSTDLTPQTFSE----------KVLQGKNH--WVID--------FYAPWCGPCQNFAPEFELLARMIK 718
Cdd:TIGR01130 318 NLEAFVKDFL---DGKLKPYLKSEpipeddegpvKVLVGKNFdeIVLDetkdvlveFYAPWCGHCKNLAPIYEELAEKYK 394

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1622849033 719 G---KVKAGKVDcqAYAQTCQKAGIRAYPTVKFY 749
Cdd:TIGR01130 395 DaesDVVIAKMD--ATANDVPPFEVEGFPTIKFV 426
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 129-207 1.63e-18

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: 81.57  E-value: 1.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 129 PEIITLERREFDAAV-NSGELWFVNFYSPGCSHCHDLAPTWRDFAKEVDGLLRIGAVNCGDDRMLCRMKGVNSYPSLFIF 207
Cdd:cd03004     1 PSVITLTPEDFPELVlNRKEPWLVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLY 80
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 32-131 2.41e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 87.74  E-value: 2.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033  32 TDQDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLEDNQGGq 111
Cdd:PRK14286    2 SERSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNKESEEKFKEATEAYEILRDPKKRQAYDQFGKAGVNAGAGG- 80

                          90       100
                  ....*....|....*....|
gi 1622849033 112 yeswnyyrYDFGIYDDDPEI 131
Cdd:PRK14286   81 --------FGQGAYTDFSDI 92
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 35-100 2.60e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 87.64  E-value: 2.60e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849033  35 DFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPnNPNAHGDFLKINRAYEVLKDEDLRKKYDKYG 100
Cdd:PRK14292    3 DYYELLGVSRTASADEIKSAYRKLALKYHPDRNK-EKGAAEKFAQINEAYAVLSDAEKRAHYDRFG 67
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 675-749 2.91e-18

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: 80.41  E-value: 2.91e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622849033 675 LTPQTFSEKVLQGKNHWVIDFYAPWCGPCQNFAPEFELLARMIKGKVKAGKVDCQAYAQTCQKAGIRAYPTVKFY 749
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLF 75
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 131-229 3.47e-18

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: 80.48  E-value: 3.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 131 IITLERREFDAAV-NSGELWFVNFYSPGCSHCHDLAPTWRDFAKEVDGLLRIGAVNCGDD--RMLCRMKGVNSYPSLFIF 207
Cdd:cd03002     2 VYELTPKNFDKVVhNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKELDGLVQVAAVDCDEDknKPLCGKYGVQGFPTLKVF 81

                          90       100
                  ....*....|....*....|....*..
gi 1622849033 208 RSGMAPVK-----YHGDRSKESLVSFA 229
Cdd:cd03002    82 RPPKKASKhavedYNGERSAKAIVDFV 108
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 36-110 3.76e-18

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 87.57  E-value: 3.76e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622849033  36 FYSLLGVSKTASSREIRQAFKKLALKLHPDKNpnnpnahGD---FLKINRAYEVLKDEDLRKKYDKYGEKGLEDNQGG 110
Cdd:PTZ00037   30 LYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKG-------GDpekFKEISRAYEVLSDPEKRKIYDEYGEEGLEGGEQP 100
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 32-109 5.48e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 86.36  E-value: 5.48e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622849033  32 TDQDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLEdNQG 109
Cdd:PRK14294    2 VKRDYYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGDKEAEELFKEAAEAYEVLSDPKKRGIYDQYGHEGLS-GTG 78
PRK14279 PRK14279
molecular chaperone DnaJ;
33-97 5.52e-18

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 86.71  E-value: 5.52e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622849033  33 DQDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKDEDLRKKYD 97
Cdd:PRK14279    8 EKDFYKELGVSSDASAEEIKKAYRKLARELHPDANPGDPAAEERFKAVSEAHDVLSDPAKRKEYD 72
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 34-109 6.25e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 86.54  E-value: 6.25e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849033  34 QDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNpNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLEDNQG 109
Cdd:PRK14296    4 KDYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLN-KSPDAHDKMVEINEAADVLLDKDKRKQYDQFGHAAFDGSSG 78
PRK14289 PRK14289
molecular chaperone DnaJ;
32-110 1.29e-17

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 85.65  E-value: 1.29e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849033  32 TDQDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLEDNQGG 110
Cdd:PRK14289    3 EKRDYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGDKEAEEKFKEAAEAYDVLSDPDKRSRYDQFGHAGVGGAAGG 81
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 34-111 1.41e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 85.52  E-value: 1.41e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622849033  34 QDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNpNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLEDNQGGQ 111
Cdd:PRK14276    4 TEYYDRLGVSKDASQDEIKKAYRKLSKKYHPDIN-KEPGAEEKYKEVQEAYETLSDPQKRAAYDQYGAAGANGGFGGG 80
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 675-773 1.72e-17

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: 78.56  E-value: 1.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 675 LTPQTFsEKVLQGKNHWVI-DFYAPWCGPCQNFAPEFELLARMIKGKVKAGKVDCQAYA--QTCQKAGIRAYPTVKF--- 748
Cdd:cd03002     5 LTPKNF-DKVVHNTNYTTLvEFYAPWCGHCKNLKPEYAKAAKELDGLVQVAAVDCDEDKnkPLCGKYGVQGFPTLKVfrp 83

                          90       100
                  ....*....|....*....|....*..
gi 1622849033 749 --YFYERAKRNFQEEqintRDAKAIAA 773
Cdd:cd03002    84 pkKASKHAVEDYNGE----RSAKAIVD 106
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 454-550 1.81e-17

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: 78.56  E-value: 1.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 454 HVTTLGPQNFP---ANDKEPWLVDFFAPWCPPCRALLPELRRASNLLYGQLKFGTLDCT--VHEGLCNMYNIQAYPTTVV 528
Cdd:cd03002     1 PVYELTPKNFDkvvHNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKELDGLVQVAAVDCDedKNKPLCGKYGVQGFPTLKV 80

                          90       100
                  ....*....|....*....|....*...
gi 1622849033 529 FNQSNIH------EYEGHHSAEQILEFI 550
Cdd:cd03002    81 FRPPKKAskhaveDYNGERSAKAIVDFV 108
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 34-116 3.46e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 84.27  E-value: 3.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033  34 QDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLEDnqGGQYE 113
Cdd:PRK14285    3 RDYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKEAESIFKEATEAYEVLIDDNKRAQYDRFGHTAFEG--GGGFE 80


                  ...
gi 1622849033 114 SWN 116
Cdd:PRK14285   81 GFS 83
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 674-749 4.44e-17

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: 77.32  E-value: 4.44e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849033 674 DLTPQTFSEKVLQGkNHWvIDFYAPWCGPCQNFAPEFELLARMI---KGKVKAGKVDCQAYAQTCQKAGIRAYPTVKFY 749
Cdd:cd03005     4 ELTEDNFDHHIAEG-NHF-VKFFAPWCGHCKRLAPTWEQLAKKFnneNPSVKIAKVDCTQHRELCSEFQVRGYPTLLLF 80
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 439-559 5.50e-17

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 84.80  E-value: 5.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 439 ILYDILAFAKES---VNSHVTTLGPQNFPA--NDKEPWLVDFFAPWCPPCRALLPELRRASNLLY---GQLKFGTLDCTV 510
Cdd:PTZ00102   15 ILLAFAVFGSAEehfISEHVTVLTDSTFDKfiTENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKekkSEIVLASVDATE 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1622849033 511 HEGLCNMYNIQAYPTTVVFNQSNIHEYEGHHSAEQILEFIEDLMNPSVV 559
Cdd:PTZ00102   95 EMELAQEFGVRGYPTIKFFNKGNPVNYSGGRTADGIVSWIKKLTGPAVT 143
PRK14295 PRK14295
molecular chaperone DnaJ;
33-111 5.84e-17

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 83.74  E-value: 5.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033  33 DQDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKDEDLRKKYDK----YGEKGLEDNQ 108
Cdd:PRK14295    8 EKDYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDAKAEERFKEISEAYDVLSDEKKRKEYDEarslFGNGGFRPGP 87


                  ...
gi 1622849033 109 GGQ 111
Cdd:PRK14295   88 GGG 90
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
34-97 6.70e-17

Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 76.30  E-value: 6.70e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622849033  34 QDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPN-AHGDFLKINRAYEVLKDEDLRKKYD 97
Cdd:COG2214     5 KDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKAlAEELFQRLNEAYEVLSDPERRAEYD 69
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 673-772 7.54e-17

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: 76.92  E-value: 7.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 673 TDLTPQTFsEKVLQGKNH-WVIDFYAPWCGPCQNFAPEFELLARMIK---GKVKAGKVDC--QAYAQTCQKAGIRAYPTV 746
Cdd:cd02992     4 IVLDAASF-NSALLGSPSaWLVEFYASWCGHCRAFAPTWKKLARDLRkwrPVVRVAAVDCadEENVALCRDFGVTGYPTL 82

                          90       100
                  ....*....|....*....|....*...
gi 1622849033 747 KFY--FYERAKRNFQEEqINTRDAKAIA 772
Cdd:cd02992    83 RYFppFSKEATDGLKQE-GPERDVNELR 109
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 34-100 8.58e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 81.52  E-value: 8.58e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622849033  34 QDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNpNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYG 100
Cdd:PRK14299    4 KDYYAILGVPKNASQDEIKKAFKKLARKYHPDVN-KSPGAEEKFKEINEAYTVLSDPEKRRIYDTYG 69
PRK14280 PRK14280
molecular chaperone DnaJ;
34-126 1.26e-16

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 82.46  E-value: 1.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033  34 QDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNpNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLEDNQGGQYE 113
Cdd:PRK14280    4 RDYYEVLGVSKSASKDEIKKAYRKLSKKYHPDIN-KEEGADEKFKEISEAYEVLSDDQKRAQYDQFGHAGPNQGFGGGGF 82

                          90
                  ....*....|...
gi 1622849033 114 SWNYYRYDFGIYD 126
Cdd:PRK14280   83 GGGDFGGGFGFED 95
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 675-778 2.01e-16

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: 82.80  E-value: 2.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 675 LTPQTFSEkVLQGKNHWVIDFYAPWCGPCQNFAPEFELLARMIKGK---VKAGKVDCQAYAQTCQKAGIRAYPTVKFYfy 751
Cdd:TIGR01130   6 LTKDNFDD-FIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKgppIKLAKVDATEEKDLAQKYGVSGYPTLKIF-- 82

                          90       100
                  ....*....|....*....|....*..
gi 1622849033 752 eRAKRNFQEEQINTRDAKAIAALINEK 778
Cdd:TIGR01130  83 -RNGEDSVSDYNGPRDADGIVKYMKKQ 108
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 34-108 2.03e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 81.98  E-value: 2.03e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622849033  34 QDFYSLLGVSKTASSREIRQAFKKLALKLHPDkNPNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLEDNQ 108
Cdd:PRK14300    3 QDYYQILGVSKTASQADLKKAYLKLAKQYHPD-TTDAKDAEKKFKEINAAYDVLKDEQKRAAYDRFGHDAFQNQQ 76
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 558-652 3.37e-16

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: 75.09  E-value: 3.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 558 VVSLTPTTFNELVtqRKHNEVWMVDFYSPWCHPCQVLMPEWKRMARTLTGLINVGSIDC--QQYHSFCAQENVQRYPEIR 635
Cdd:cd03002     2 VYELTPKNFDKVV--HNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKELDGLVQVAAVDCdeDKNKPLCGKYGVQGFPTLK 79

                          90       100
                  ....*....|....*....|
gi 1622849033 636 FFPPKsnKAYQYHS---YNG 652
Cdd:cd03002    80 VFRPP--KKASKHAvedYNG 97
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 678-749 3.50e-16

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


Pssm-ID: 239245 [Multi-domain]  Cd Length: 93  Bit Score: 74.52  E-value: 3.50e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622849033 678 QTFSEKVLQGKNHwVIDFYAPWCGPCQNFAPEFELLARMiKGKVKAGKVDCQAYAQTCQKAGIRAYPTVKFY 749
Cdd:cd02947     1 EEFEELIKSAKPV-VVDFWAPWCGPCKAIAPVLEELAEE-YPKVKFVKVDVDENPELAEEYGVRSIPTFLFF 70
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 131-228 4.04e-16

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: 74.59  E-value: 4.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 131 IITLERREFDAAV-NSGELWFVNFYSPGCSHCHDLAPTW----RDFAKEvDGLLrIGAVNCGDD-RMLCRMKGVNSYPSL 204
Cdd:cd02998     2 VVELTDSNFDKVVgDDKKDVLVEFYAPWCGHCKNLAPEYeklaAVFANE-DDVV-IAKVDADEAnKDLAKKYGVSGFPTL 79

                          90       100
                  ....*....|....*....|....*
gi 1622849033 205 FIFRSG-MAPVKYHGDRSKESLVSF 228
Cdd:cd02998    80 KFFPKGsTEPVKYEGGRDLEDLVKF 104
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 130-228 4.94e-16

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: 74.19  E-value: 4.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 130 EIITLERREFDAAVNSGELWF-VNFYSPGCSHCHDLAPTWRDFAKEVDGLLRIGAVNCGDDRMLCRMKGVNSYPSLFIFR 208
Cdd:pfam00085   1 VVVVLTDANFDEVVQKSSKPVlVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFK 80

                          90       100
                  ....*....|....*....|
gi 1622849033 209 SGMAPVKYHGDRSKESLVSF 228
Cdd:pfam00085  81 NGQPVDDYVGARPKDALAAF 100
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 556-642 5.52e-16

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


Pssm-ID: 239301 [Multi-domain]  Cd Length: 101  Bit Score: 74.10  E-value: 5.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 556 PSVVSLTPTTFNELVTQrkhNEVWMVDFYSPWCHPCQVLMPEWKRMARTLTGLINVGSIDCQQYHSFCAQENVQRYPEIR 635
Cdd:cd03003     1 PEIVTLDRGDFDAAVNS---GEIWFVNFYSPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDDRMLCRSQGVNSYPSLY 77


                  ....*..
gi 1622849033 636 FFPPKSN 642
Cdd:cd03003    78 VFPSGMN 84
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 35-110 8.38e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 80.10  E-value: 8.38e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849033  35 DFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPnNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKgLEDNQGG 110
Cdd:PRK14278    4 DYYGLLGVSRNASDAEIKRAYRKLARELHPDVNP-DEEAQEKFKEISVAYEVLSDPEKRRIVDLGGDP-LESAGGG 77
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 128-213 1.03e-15

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


Pssm-ID: 239290 [Multi-domain]  Cd Length: 114  Bit Score: 73.84  E-value: 1.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 128 DPeIITLERREFDAAV-NSGELWFVNFYSPGCSHCHDLAPTWRDFAKEVD---GLLRIGAVNCGDD--RMLCRMKGVNSY 201
Cdd:cd02992     1 DP-VIVLDAASFNSALlGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRkwrPVVRVAAVDCADEenVALCRDFGVTGY 79

                          90
                  ....*....|..
gi 1622849033 202 PSLFIFRSGMAP 213
Cdd:cd02992    80 PTLRYFPPFSKE 91
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 673-777 1.07e-15

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 80.57  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 673 TDLTPQTFsEKVLQGKNHWVIDFYAPWCGPCQNFAPEFELLARMIK---GKVKAGKVDCQAYAQTCQKAGIRAYPTVKFy 749
Cdd:PTZ00102   35 TVLTDSTF-DKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKekkSEIVLASVDATEEMELAQEFGVRGYPTIKF- 112

                          90       100
                  ....*....|....*....|....*...
gi 1622849033 750 FYERAKRNFQeeqiNTRDAKAIAALINE 777
Cdd:PTZ00102  113 FNKGNPVNYS----GGRTADGIVSWIKK 136
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 34-105 1.23e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 79.48  E-value: 1.23e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622849033  34 QDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNpNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLE 105
Cdd:PRK14283    5 RDYYEVLGVDRNADKKEIKKAYRKLARKYHPDVS-EEEGAEEKFKEISEAYAVLSDDEKRQRYDQFGHAGMD 75
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 34-103 1.45e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 79.07  E-value: 1.45e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622849033  34 QDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNN-PNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKG 103
Cdd:PRK14282    4 KDYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENrKEAEQKFKEIQEAYEVLSDPQKRAMYDRFGYVG 74
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 34-131 1.47e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 79.20  E-value: 1.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033  34 QDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNN-PNAHGDFLKINRAYEVLKDEDLRKKYDKYGEkgLEDNQGGQY 112
Cdd:PRK14290    3 KDYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGNkAEAEEKFKEISEAYEVLSDPQKRRQYDQTGT--VDFGAGGSN 80

                          90
                  ....*....|....*....
gi 1622849033 113 ESWNyyryDFGIYDDDPEI 131
Cdd:PRK14290   81 FNWD----NFTHFSDINDI 95
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 557-646 1.48e-15

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: 73.04  E-value: 1.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 557 SVVSLTPTTFNELVtqRKHNEVWMVDFYSPWCHPCQVLMPEWKRMARTLTGLINVGSIDCQQYHSFCAQENVQRYPEIRF 636
Cdd:pfam00085   1 VVVVLTDANFDEVV--QKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIF 78

                          90
                  ....*....|
gi 1622849033 637 FPPKSNKAYQ 646
Cdd:pfam00085  79 FKNGQPVDDY 88
PRK10996 PRK10996
thioredoxin 2; Provisional
 676-749 1.48e-15

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 74.33  E-value: 1.48e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622849033 676 TPQTFSeKVLQGKNHWVIDFYAPWCGPCQNFAPEFELLARMIKGKVKAGKVDCQAYAQTCQKAGIRAYPTVKFY 749
Cdd:PRK10996   41 TGETLD-KLLQDDLPVVIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIF 113
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 130-551 3.91e-15

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: 78.56  E-value: 3.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 130 EIITLERREFDAAVNSGELWFVNFYSPGCSHCHDLAPTWRDFAKEV---DGLLRIGAVNCGDDRMLCRMKGVNSYPSLFI 206
Cdd:TIGR01130   2 DVLVLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELkkkGPPIKLAKVDATEEKDLAQKYGVSGYPTLKI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 207 FRSG-MAPVKYHGDRSKESLVSFAMQHVRSTVTELWTGNFVNsiqtAFAAGIGWLITFCSKGGDCLTSQTRLRLSGMLDG 285
Cdd:TIGR01130  82 FRNGeDSVSDYNGPRDADGIVKYMKKQSGPAVKEIETVADLE----AFLADDDVVVIGFFKDLDSELNDTFLSVAEKLRD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 286 lVNVGWMDCATQDNLCKSldittsttAYFPPGATLNNREK---NSILFLNSLDAKEIYLE---VIHNLPDFELLSANTLE 359
Cdd:TIGR01130 158 -VYFFFAHSSDVAAFAKL--------GAFPDSVVLFKPKDedeKFSKVDGEMDTDVSDLEkfiRAESLPLVGEFTQETAA 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 360 DRLAhhRWLLFFHFGK-NENSNDHELKKLKTLL--KNDHIQVGRFDCSSAPDicsNLYVFQ---------PSLAVFKGQG 427
Cdd:TIGR01130 229 KYFE--SGPLVVLYYNvDESLDPFEELRNRFLEaaKKFRGKFVNFAVADEED---FGRELEyfglkaekfPAVAIQDLEG 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 428 TKEYEIHHGKKILYDILAFAKESVNSHVT-TLGPQNFPANDKEPW-------------------LVDFFAPWCPPCRALL 487
Cdd:TIGR01130 304 NKKYPMDQEEFSSENLEAFVKDFLDGKLKpYLKSEPIPEDDEGPVkvlvgknfdeivldetkdvLVEFYAPWCGHCKNLA 383

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622849033 488 P---EL-----RRASNLLYGQlkfgtLDCTVHEglCNMYNIQAYPTTVVF---NQSNIHEYEGHHSAEQILEFIE 551
Cdd:TIGR01130 384 PiyeELaekykDAESDVVIAK-----MDATAND--VPPFEVEGFPTIKFVpagKKSEPVPYDGDRTLEDFSKFIA 451
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 574-647 4.00e-15

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: 71.72  E-value: 4.00e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622849033 574 KHNEVWMVDFYSPWCHPCQVLMPEWKRMARTLTGL---INVGSIDCQQYHSFCAQENVQRYPEIRFFppKSNKAYQY 647
Cdd:cd03000    13 RKEDIWLVDFYAPWCGHCKKLEPVWNEVGAELKSSgspVRVGKLDATAYSSIASEFGVRGYPTIKLL--KGDLAYNY 87
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 472-551 7.08e-15

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: 70.66  E-value: 7.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 472 LVDFFAPWCPPCRALLPELRRASNlLYGQLKFGTLDCTVHEGLCNMYNIQAYPTTVVFNQSN-IHEYEGHHSAEQILEFI 550
Cdd:cd02947    14 VVDFWAPWCGPCKAIAPVLEELAE-EYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKeVDRVVGADPKEELEEFL 92


                  .
gi 1622849033 551 E 551
Cdd:cd02947    93 E 93
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 557-660 1.86e-14

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: 69.97  E-value: 1.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 557 SVVSLTPTTFNELVTQRKHNEvwMVDFYSPWCHPCQVLMPEWKRMARTLTG--LINVGSIDCQQYHS-FCAQENVQRYPE 633
Cdd:cd02998     1 NVVELTDSNFDKVVGDDKKDV--LVEFYAPWCGHCKNLAPEYEKLAAVFANedDVVIAKVDADEANKdLAKKYGVSGFPT 78

                          90       100
                  ....*....|....*....|....*..
gi 1622849033 634 IRFFPPKSNKAYQYhsYNGwnRDAYSL 660
Cdd:cd02998    79 LKFFPKGSTEPVKY--EGG--RDLEDL 101
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 149-262 3.16e-14

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 72.74  E-value: 3.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 149 WFVNFYSPGCSHCHDLAPTWRDFAKEVDGLLRIGAVNCGDDRMLCRMKGVNSYPSLFIFRSGMAPVKYHGDRSKESLVSF 228
Cdd:PTZ00443   55 WFVKFYAPWCSHCRKMAPAWERLAKALKGQVNVADLDATRALNLAKRFAIKGYPTLLLFDKGKMYQYEGGDRSTEKLAAF 134

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622849033 229 AMQHVRSTVtelwtGNFVNSIQTAFAAGIGWLIT 262
Cdd:PTZ00443  135 ALGDFKKAL-----GAPVPAPLSFFALTIDFFVS 163
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 691-749 1.01e-13

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


Pssm-ID: 239298 [Multi-domain]  Cd Length: 104  Bit Score: 67.86  E-value: 1.01e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622849033 691 WVIDFYAPWCGPCQNFAPEFELLARMIKG---KVKAGKVDCQAYAQTCQKAGIRAYPTVKFY 749
Cdd:cd03000    18 WLVDFYAPWCGHCKKLEPVWNEVGAELKSsgsPVRVGKLDATAYSSIASEFGVRGYPTIKLL 79
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 147-229 1.28e-13

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


Pssm-ID: 239298 [Multi-domain]  Cd Length: 104  Bit Score: 67.48  E-value: 1.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 147 ELWFVNFYSPGCSHCHDLAPTWRDFAKEVDGL---LRIGAVNCGDDRMLCRMKGVNSYPSLFIFRSGMApVKYHGDRSKE 223
Cdd:cd03000    16 DIWLVDFYAPWCGHCKKLEPVWNEVGAELKSSgspVRVGKLDATAYSSIASEFGVRGYPTIKLLKGDLA-YNYRGPRTKD 94


                  ....*.
gi 1622849033 224 SLVSFA 229
Cdd:cd03000    95 DIVEFA 100
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 454-550 1.40e-13

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: 67.28  E-value: 1.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 454 HVTTLGPQNFPA---NDKEPWLVDFFAPWCPPCRALLPELRRASNLLYGQ--LKFGTLDCT-VHEGLCNMYNIQAYPTTV 527
Cdd:cd02998     1 NVVELTDSNFDKvvgDDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFANEddVVIAKVDADeANKDLAKKYGVSGFPTLK 80

                          90       100
                  ....*....|....*....|....*
gi 1622849033 528 VF--NQSNIHEYEGHHSAEQILEFI 550
Cdd:cd02998    81 FFpkGSTEPVKYEGGRDLEDLVKFV 105
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 467-550 2.37e-13

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: 66.57  E-value: 2.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 467 DKEPWLVDFFAPWCPPCRALLPELRRASNLLYGQLK--FGTLDCTV--HEGLCNMYNIQAYPTTVVF-NQSNIHEYEGHH 541
Cdd:cd02997    16 KEKHVLVMFYAPWCGHCKKMKPEFTKAATELKEDGKgvLAAVDCTKpeHDALKEEYNVKGFPTFKYFeNGKFVEKYEGER 95


                  ....*....
gi 1622849033 542 SAEQILEFI 550
Cdd:cd02997    96 TAEDIIEFM 104
PRK14288 PRK14288
molecular chaperone DnaJ;
36-128 2.85e-13

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 72.03  E-value: 2.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033  36 FYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLedNQGGQYES- 114
Cdd:PRK14288    5 YYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKEAEEKFKLINEAYGVLSDEKKRALYDRYGKKGL--NQAGASQSd 82

                          90
                  ....*....|....
gi 1622849033 115 WNYYRYDFGIYDDD 128
Cdd:PRK14288   83 FSDFFEDLGSFFED 96
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 453-549 5.44e-13

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 69.27  E-value: 5.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 453 SHVTTLGPQNFPANDKE-------PWLVDFFAPWCPPCRALLPELRRASNLLYGQLKFGTLDCTVHEGLCNMYNIQAYPT 525
Cdd:PTZ00443   30 NALVLLNDKNFEKLTQAstgattgPWFVKFYAPWCSHCRKMAPAWERLAKALKGQVNVADLDATRALNLAKRFAIKGYPT 109

                          90       100
                  ....*....|....*....|....*
gi 1622849033 526 TVVFNQSNIHEYE-GHHSAEQILEF 549
Cdd:PTZ00443  110 LLLFDKGKMYQYEgGDRSTEKLAAF 134
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 465-553 1.34e-12

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


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 64.62  E-value: 1.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 465 ANDKEPWLVDFFAPWCPPCRALLPELRRASNLLYGQLKFGTLDCTVHEGLCNMYNIQAYPTTVVF-NQSNIHEYEGHHSA 543
Cdd:TIGR01068  11 ASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFkNGKEVDRSVGALPK 90

                          90
                  ....*....|
gi 1622849033 544 EQILEFIEDL 553
Cdd:TIGR01068  91 AALKQLINKN 100
PRK10266 PRK10266
curved DNA-binding protein;
34-127 1.74e-12

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 69.08  E-value: 1.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033  34 QDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNpNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLEDNQGGQYE 113
Cdd:PRK10266    4 KDYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVS-KEPDAEARFKEVAEAWEVLSDEQRRAEYDQLWQHRNDPQFNRQFQ 82

                          90
                  ....*....|....
gi 1622849033 114 SWNYYRYDFGIYDD 127
Cdd:PRK10266   83 HGDGQSFNAEDFDD 96
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 556-663 2.08e-12

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: 64.01  E-value: 2.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 556 PSVVSLTPTTFNELVTQRKHNEVWMVDFYSPWCHPCQVLMPEWKRMARTLTGL-INVGSIDCQQYHSFCAQEN--VQRYP 632
Cdd:cd02993     1 EAVVTLSRAEIEALAKGERRNQSTLVVLYAPWCPFCQAMEASYEELAEKLAGSnVKVAKFNADGEQREFAKEElqLKSFP 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1622849033 633 EIRFFPPKSNKAYQYHSYngwNRDAYSLRIW 663
Cdd:cd02993    81 TILFFPKNSRQPIKYPSE---QRDVDSLLMF 108
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 455-549 3.09e-12

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: 63.31  E-value: 3.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 455 VTTLGPQNFPA--NDKEPWLVDFFAPWCPPCRALLPELRRASNLLYGQLKFGTLDCTVHEGLCNMYNIQAYPTTVVFNQS 532
Cdd:cd03003     3 IVTLDRGDFDAavNSGEIWFVNFYSPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDDRMLCRSQGVNSYPSLYVFPSG 82

                          90
                  ....*....|....*...
gi 1622849033 533 NIHE-YEGHHSAEQILEF 549
Cdd:cd03003    83 MNPEkYYGDRSKESLVKF 100
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 675-775 3.65e-12

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: 63.49  E-value: 3.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 675 LTPQTFsEKVLQGKNHWVIDFYAPWCGPCQNFAPEFELLARMIK--GKVKAGKVDC--QAYAQTCQKAGIRAYPTVKFYF 750
Cdd:cd02997     5 LTDEDF-RKFLKKEKHVLVMFYAPWCGHCKKMKPEFTKAATELKedGKGVLAAVDCtkPEHDALKEEYNVKGFPTFKYFE 83

                          90       100
                  ....*....|....*....|....*
gi 1622849033 751 YERAKRNFQEEqintRDAKAIAALI 775
Cdd:cd02997    84 NGKFVEKYEGE----RTAEDIIEFM 104
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 460-555 3.77e-12

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 64.33  E-value: 3.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 460 PQNFPANDKEPWLVDFFAPWCPPCRALLPELRRASNlLYGQLKFGTLDctVHEG------------------------LC 515
Cdd:COG0526    20 PLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAE-EYGGVVFVGVD--VDENpeavkaflkelglpypvlldpdgeLA 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1622849033 516 NMYNIQAYPTTVVFNQSN--IHEYEGHHSAEQILEFIEDLMN 555
Cdd:COG0526    97 KAYGVRGIPTTVLIDKDGkiVARHVGPLSPEELEEALEKLLA 138
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 131-233 3.96e-12

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: 63.30  E-value: 3.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 131 IITLERREFDAAV-NSGELWFVNFYSPGCSHCHDLAPTWRDFAKEVDGLLRIGAVNCGDDRMLCRMKGVNSYPSLFIFRS 209
Cdd:COG3118     2 VVELTDENFEEEVlESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLFKD 81

                          90       100
                  ....*....|....*....|....
gi 1622849033 210 GMAPVKYHGDRSKESLVSFAMQHV 233
Cdd:COG3118    82 GQPVDRFVGALPKEQLREFLDKVL 105
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 551-663 4.00e-12

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 69.39  E-value: 4.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 551 EDLMNPSVVSLTPTTFNELVTQrkhNEVWMVDFYSPWCHPCQVLMPEWKRMARTLTGL---INVGSIDCQQYHSFCAQEN 627
Cdd:PTZ00102   27 EHFISEHVTVLTDSTFDKFITE---NEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKkseIVLASVDATEEMELAQEFG 103

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1622849033 628 VQRYPEIRFFPPKSNKAYqyhsynGWNRDAYSLRIW 663
Cdd:PTZ00102  104 VRGYPTIKFFNKGNPVNY------SGGRTADGIVSW 133
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 467-549 4.71e-12

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: 62.86  E-value: 4.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 467 DKEPWLVDFFAPWCPPCRALLP-------ELRRASNllygQLKFGTLDCTVHEGLCNMYNIQAYPTTVVFNQSNIHEYEG 539
Cdd:cd03000    14 KEDIWLVDFYAPWCGHCKKLEPvwnevgaELKSSGS----PVRVGKLDATAYSSIASEFGVRGYPTIKLLKGDLAYNYRG 89

                          90
                  ....*....|
gi 1622849033 540 HHSAEQILEF 549
Cdd:cd03000    90 PRTKDDIVEF 99
PTZ00051 PTZ00051
thioredoxin; Provisional
 675-749 5.16e-12

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 62.59  E-value: 5.16e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622849033 675 LTPQTFSEKVLQGKNHWVIDFYAPWCGPCQNFAPEFELLARMiKGKVKAGKVDCQAYAQTCQKAGIRAYPTVKFY 749
Cdd:PTZ00051    5 VTSQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKE-YTKMVFVKVDVDELSEVAEKENITSMPTFKVF 78
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 32-109 5.47e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 68.11  E-value: 5.47e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622849033  32 TDQDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNpNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKglEDNQG 109
Cdd:PRK14287    2 SKRDYYEVLGVDRNASVDEVKKAYRKLARKYHPDVN-KAPDAEDKFKEVKEAYDTLSDPQKKAHYDQFGHT--DPNQG 76
PLN02309 PLN02309
5'-adenylylsulfate reductase
 530-663 1.42e-11

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 67.51  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 530 NQSNIHEYEGHHSAEQILEFIEDLMN-PSVVSLTPTTFNELVTQRKHNEVWMVDFYSPWCHPCQVLMPEWKRMARTLTGL 608
Cdd:PLN02309  318 HKGNIKEEDNGAANDNGNAAVADIFNsQNVVALSRAGIENLLKLENRKEPWLVVLYAPWCPFCQAMEASYEELAEKLAGS 397

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622849033 609 -INVGSIDCQQYHSFCAQENVQ--RYPEIRFFPPKSNKAYQYHSYngwNRDAYSLRIW 663
Cdd:PLN02309  398 gVKVAKFRADGDQKEFAKQELQlgSFPTILLFPKNSSRPIKYPSE---KRDVDSLLSF 452
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 130-235 1.63e-11

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 67.47  E-value: 1.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 130 EIITLERREFDAAVNSGELWFVNFYSPGCSHCHDLAPTWRDFAKEVDGL---LRIGAVNCGDDRMLCRMKGVNSYPSLFI 206
Cdd:PTZ00102   33 HVTVLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKkseIVLASVDATEEMELAQEFGVRGYPTIKF 112

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1622849033 207 FRSGmAPVKYHGDRSKESLVSF-------AMQHVRS 235
Cdd:PTZ00102  113 FNKG-NPVNYSGGRTADGIVSWikkltgpAVTEVES 147
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 557-637 2.35e-11

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: 60.99  E-value: 2.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 557 SVVSLTPTTFNELVTQRkhNEVWMVDFYSPWCHPCQVLMPEWKRMARTLTGLINVGSIDCQQYHSFCAQENVQRYPEIRF 636
Cdd:COG3118     1 AVVELTDENFEEEVLES--DKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLL 78


                  .
gi 1622849033 637 F 637
Cdd:COG3118    79 F 79
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 557-644 2.46e-11

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: 61.13  E-value: 2.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 557 SVVSLTPTTFNE-LVTQRKhneVWMVDFYSPWCHPCQVLMPEWKRMARTL---TGLINVGSIDCQQYHSF--CAQENVQR 630
Cdd:cd02992     2 PVIVLDAASFNSaLLGSPS---AWLVEFYASWCGHCRAFAPTWKKLARDLrkwRPVVRVAAVDCADEENValCRDFGVTG 78

                          90
                  ....*....|....
gi 1622849033 631 YPEIRFFPPKSNKA 644
Cdd:cd02992    79 YPTLRYFPPFSKEA 92
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 33-148 6.37e-11

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 66.35  E-value: 6.37e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033   33 DQDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHgDFLKINRAYEVLKDEDLRKKYDKYGEKGLEdnQGGQY 112
Cdd:PTZ00341   572 DTLFYDILGVGVNADMKEISERYFKLAENYYPPKRSGNEGFH-KFKKINEAYQILGDIDKKKMYNKFGYDGIK--GVNFI 648

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1622849033  113 ESWNYYRY----DFGIYDDDPEIITLERREFDAAVNSGEL 148
Cdd:PTZ00341   649 HPSIFYLLasleKFADFTGSPQIVTLLKFFFEKKLSMNDL 688
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 558-663 6.69e-11

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: 59.61  E-value: 6.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 558 VVSLTPTTFNELVTQRKHnevwMVDFYSPWCHPCQVLMPEWKRMA-RTLTGLINV--GSIDCQQYHSFCAQENVQRYPEI 634
Cdd:cd03005     2 VLELTEDNFDHHIAEGNH----FVKFFAPWCGHCKRLAPTWEQLAkKFNNENPSVkiAKVDCTQHRELCSEFQVRGYPTL 77

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1622849033 635 RFFPP--KSNKayqyhsYNGwNRDAYSLRIW 663
Cdd:cd03005    78 LLFKDgeKVDK------YKG-TRDLDSLKEF 101
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 557-681 8.54e-11

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 62.72  E-value: 8.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 557 SVVSLTPTTFNELvTQRKHNEV---WMVDFYSPWCHPCQVLMPEWKRMARTLTGLINVGSIDCQQYHSFCAQENVQRYPE 633
Cdd:PTZ00443   31 ALVLLNDKNFEKL-TQASTGATtgpWFVKFYAPWCSHCRKMAPAWERLAKALKGQVNVADLDATRALNLAKRFAIKGYPT 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622849033 634 IRFFppKSNKAYQyhsYNGWNRDAYSLRIWGLGFLPQVSTDLTPQTFS 681
Cdd:PTZ00443  110 LLLF--DKGKMYQ---YEGGDRSTEKLAAFALGDFKKALGAPVPAPLS 152
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 470-546 9.11e-11

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: 59.21  E-value: 9.11e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622849033 470 PWLVDFFAPWCPPCRALLPELRRASNLLYGQLKFGTLDCTVHEGLCNMYNIQAYPTTVVFNQSN-IHEYEGHHSAEQI 546
Cdd:cd02956    14 PVVVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQpVDGFQGAQPEEQL 91
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 691-760 1.37e-10

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 61.95  E-value: 1.37e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849033 691 WVIDFYAPWCGPCQNFAPEFELLARMIKGKVKAGKVDCQAYAQTCQKAGIRAYPTV------KFYFYERAKRNFQE 760
Cdd:PTZ00443   55 WFVKFYAPWCSHCRKMAPAWERLAKALKGQVNVADLDATRALNLAKRFAIKGYPTLllfdkgKMYQYEGGDRSTEK 130
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 150-228 2.68e-10

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: 57.95  E-value: 2.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 150 FVNFYSPGCSHCHDLAPTWRDFAKE---VDGLL--RI-GAVNcgDdrmLCRMKGVNSYPSLFIFRSGMA--PVKYHGDRS 221
Cdd:cd02995    22 LVEFYAPWCGHCKALAPIYEELAEKlkgDDNVViaKMdATAN--D---VPSEFVVDGFPTILFFPAGDKsnPIKYEGDRT 96


                  ....*..
gi 1622849033 222 KESLVSF 228
Cdd:cd02995    97 LEDLIKF 103
trxA PRK09381
thioredoxin TrxA;
675-749 3.82e-10

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 57.77  E-value: 3.82e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622849033 675 LTPQTFSEKVLQGKNHWVIDFYAPWCGPCQNFAPEFELLARMIKGKVKAGKVDCQAYAQTCQKAGIRAYPTVKFY 749
Cdd:PRK09381    8 LTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLF 82
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 453-550 5.50e-10

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: 57.40  E-value: 5.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 453 SHVTTLGPQNFPA--NDKEPWLVDFFAPWCPPCRALLPELRRASNLLY------GQLKFGTLDCTVHEGLCNMYNIQAYP 524
Cdd:cd02996     1 SEIVSLTSGNIDDilQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKeefpdaGKVVWGKVDCDKESDIADRYRINKYP 80

                          90       100
                  ....*....|....*....|....*...
gi 1622849033 525 TTVVFNQSNI--HEYEGHHSAEQILEFI 550
Cdd:cd02996    81 TLKLFRNGMMmkREYRGQRSVEALAEFV 108
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 130-228 5.94e-10

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: 57.01  E-value: 5.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 130 EIITLERREFDAAVNSGELWFVNFYSPGCSHCHDLAPTWRDFAKEV------DGLLRIGAVNCGDDRMLCRMKGVNSYPS 203
Cdd:cd02996     2 EIVSLTSGNIDDILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIkeefpdAGKVVWGKVDCDKESDIADRYRINKYPT 81

                          90       100
                  ....*....|....*....|....*.
gi 1622849033 204 LFIFRSGMAP-VKYHGDRSKESLVSF 228
Cdd:cd02996    82 LKLFRNGMMMkREYRGQRSVEALAEF 107
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 691-749 7.50e-10

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: 56.76  E-value: 7.50e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849033 691 WVIDFYAPWCGPCQNFAPEFELLARMIKGKVKAGKVDCQAYAQTCQKAGIRAYPTVKFY 749
Cdd:cd03003    21 WFVNFYSPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDDRMLCRSQGVNSYPSLYVF 79
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 472-537 9.57e-10

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: 55.40  E-value: 9.57e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849033 472 LVDFFAPWCPPCRALLPELRRASnLLYGQLKFGTLDCTVHEGLCN---MYNIQAYPTTVVFNQSNIHEY 537
Cdd:cd01659     1 LVLFYAPWCPFCQALRPVLAELA-LLNKGVKFEAVDVDEDPALEKelkRYGVGGVPTLVVFGPGIGVKY 68
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 472-550 9.64e-10

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: 56.52  E-value: 9.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 472 LVDFFAPWCPPCRALLP---ELRRASNLLYGQLKFGTLDCTVHEGLCNMYNIQAYPTTVVF-NQSNIHEYEGHHSAEQIL 547
Cdd:cd03005    20 FVKFFAPWCGHCKRLAPtweQLAKKFNNENPSVKIAKVDCTQHRELCSEFQVRGYPTLLLFkDGEKVDKYKGTRDLDSLK 99


                  ...
gi 1622849033 548 EFI 550
Cdd:cd03005   100 EFV 102
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 146-228 1.38e-09

PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human transmembrane protein, TMX. TMX is a type I integral membrane protein; the N-terminal redox active TRX domain is present in the endoplasmic reticulum (ER) lumen while the C-terminus is oriented towards the cytoplasm. It is expressed in many cell types and its active site motif (CPAC) is unique. In vitro, TMX reduces interchain disulfides of insulin and renatures inactive RNase containing incorrect disulfide bonds. The C. elegans homolog, DPY-11, is expressed only in the hypodermis and resides in the cytoplasm. It is required for body and sensory organ morphogeneis. Another uncharacterized TRX-related transmembrane protein, human TMX4, is included in the alignment. The active site sequence of TMX4 is CPSC.


Pssm-ID: 239292 [Multi-domain]  Cd Length: 101  Bit Score: 55.85  E-value: 1.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 146 GElWFVNFYSPGCSHCHDLAPTWRDFAKEVDGL-LRIGAVNCGDDRMLCRMKGVNSYPSLF-----IFRsgmapvKYHGD 219
Cdd:cd02994    17 GE-WMIEFYAPWCPACQQLQPEWEEFADWSDDLgINVAKVDVTQEPGLSGRFFVTALPTIYhakdgVFR------RYQGP 89


                  ....*....
gi 1622849033 220 RSKESLVSF 228
Cdd:cd02994    90 RDKEDLISF 98
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 679-749 3.93e-09

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


Pssm-ID: 239293 [Multi-domain]  Cd Length: 104  Bit Score: 54.48  E-value: 3.93e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622849033 679 TFSEKVLQGKNHWVIDFYAPWCGPCQNFAPEFELLARMIKG--KVKAGKVDcqAYAQTCQKAGI-RAYPTVKFY 749
Cdd:cd02995     9 NFDEVVLDSDKDVLVEFYAPWCGHCKALAPIYEELAEKLKGddNVVIAKMD--ATANDVPSEFVvDGFPTILFF 80
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 557-618 4.47e-09

PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human transmembrane protein, TMX. TMX is a type I integral membrane protein; the N-terminal redox active TRX domain is present in the endoplasmic reticulum (ER) lumen while the C-terminus is oriented towards the cytoplasm. It is expressed in many cell types and its active site motif (CPAC) is unique. In vitro, TMX reduces interchain disulfides of insulin and renatures inactive RNase containing incorrect disulfide bonds. The C. elegans homolog, DPY-11, is expressed only in the hypodermis and resides in the cytoplasm. It is required for body and sensory organ morphogeneis. Another uncharacterized TRX-related transmembrane protein, human TMX4, is included in the alignment. The active site sequence of TMX4 is CPSC.


Pssm-ID: 239292 [Multi-domain]  Cd Length: 101  Bit Score: 54.31  E-value: 4.47e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622849033 557 SVVSLTPTTFNELVTQRkhnevWMVDFYSPWCHPCQVLMPEWKRMARTLTGL-INVGSIDCQQ 618
Cdd:cd02994     2 NVVELTDSNWTLVLEGE-----WMIEFYAPWCPACQQLQPEWEEFADWSDDLgINVAKVDVTQ 59
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 471-552 4.70e-09

PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human transmembrane protein, TMX. TMX is a type I integral membrane protein; the N-terminal redox active TRX domain is present in the endoplasmic reticulum (ER) lumen while the C-terminus is oriented towards the cytoplasm. It is expressed in many cell types and its active site motif (CPAC) is unique. In vitro, TMX reduces interchain disulfides of insulin and renatures inactive RNase containing incorrect disulfide bonds. The C. elegans homolog, DPY-11, is expressed only in the hypodermis and resides in the cytoplasm. It is required for body and sensory organ morphogeneis. Another uncharacterized TRX-related transmembrane protein, human TMX4, is included in the alignment. The active site sequence of TMX4 is CPSC.


Pssm-ID: 239292 [Multi-domain]  Cd Length: 101  Bit Score: 54.31  E-value: 4.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 471 WLVDFFAPWCPPCRALLP---ELRRASNLLygQLKFGTLDCTVHEGLCNMYNIQAYPTTV-----VFNQsniheYEGHHS 542
Cdd:cd02994    19 WMIEFYAPWCPACQQLQPeweEFADWSDDL--GINVAKVDVTQEPGLSGRFFVTALPTIYhakdgVFRR-----YQGPRD 91

                          90
                  ....*....|
gi 1622849033 543 AEQILEFIED 552
Cdd:cd02994    92 KEDLISFIEE 101
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 678-746 6.63e-09

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


Pssm-ID: 239254 [Multi-domain]  Cd Length: 96  Bit Score: 53.81  E-value: 6.63e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 678 QTFSEKVLQGKNH-WVIDFYAPWCGPCQNFAPEFELLARMIKGKVKAGKVDCQAYAQTCQKAGIRAYPTV 746
Cdd:cd02956     1 QNFQQVLQESTQVpVVVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTV 70
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 138-228 9.25e-09

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: 53.33  E-value: 9.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 138 EFDAAVNSGELWFVNFYSPGCSHCHDLAPTWRDFAKEVDGlLRIGAVNCGDDRMLCRMKGVNSYPSLFIFRSGMAPVKYH 217
Cdd:cd02947     2 EFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPK-VKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVV 80

                          90
                  ....*....|.
gi 1622849033 218 GDRSKESLVSF 228
Cdd:cd02947    81 GADPKEELEEF 91
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 684-727 2.10e-08

PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human transmembrane protein, TMX. TMX is a type I integral membrane protein; the N-terminal redox active TRX domain is present in the endoplasmic reticulum (ER) lumen while the C-terminus is oriented towards the cytoplasm. It is expressed in many cell types and its active site motif (CPAC) is unique. In vitro, TMX reduces interchain disulfides of insulin and renatures inactive RNase containing incorrect disulfide bonds. The C. elegans homolog, DPY-11, is expressed only in the hypodermis and resides in the cytoplasm. It is required for body and sensory organ morphogeneis. Another uncharacterized TRX-related transmembrane protein, human TMX4, is included in the alignment. The active site sequence of TMX4 is CPSC.


Pssm-ID: 239292 [Multi-domain]  Cd Length: 101  Bit Score: 52.38  E-value: 2.10e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1622849033 684 VLQGknHWVIDFYAPWCGPCQNFAPEFELLARMIKG-KVKAGKVD 727
Cdd:cd02994    14 VLEG--EWMIEFYAPWCPACQQLQPEWEEFADWSDDlGINVAKVD 56
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 682-775 2.13e-08

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: 52.78  E-value: 2.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 682 EKVLQGKNHWVIDFYAPWCGPCQNFAPEFELLARMIK------GKVKAGKVDCQAYAQTCQKAGIRAYPTVKFYFY-ERA 754
Cdd:cd02996    12 DDILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKeefpdaGKVVWGKVDCDKESDIADRYRINKYPTLKLFRNgMMM 91

                          90       100
                  ....*....|....*....|.
gi 1622849033 755 KRNFQeeqiNTRDAKAIAALI 775
Cdd:cd02996    92 KREYR----GQRSVEALAEFV 108
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
32-90 2.15e-08

DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 51.72  E-value: 2.15e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033  32 TDQDFYSLLGVSKTASSREIRQAFKKLALKLHPDKnpnnpNAHG---DFLK--------INRAYEVLKDE 90
Cdd:COG1076     2 QLDDAFELLGLPPDADDAELKRAYRKLQREHHPDR-----LAAGlpeEEQRlalqkaaaINEAYETLKDP 66
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 480-660 3.56e-08

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: 56.56  E-value: 3.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 480 CPPC-RALLP-ELRRASNLLYGQLKfgTLDCTVHEGlcnmyNIQAYPTTVVFNQsniheyEGHHSAEQILEfiedlmNPS 557
Cdd:TIGR00424 292 CEPCtRPVLPgQHEREGRWWWEDAK--AKECGLHKG-----NIKEETLDGAVNG------NGSDAVADIFD------SNN 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 558 VVSLTPTTFNELVTQRKHNEVWMVDFYSPWCHPCQVLMPEWKRMARTLTGL-INVGSI--DCQQyHSFCAQE-NVQRYPE 633
Cdd:TIGR00424 353 VVSLSRPGIENLLKLEERKEAWLVVLYAPWCPFCQAMEASYLELAEKLAGSgVKVAKFraDGDQ-KEFAKQElQLGSFPT 431

                         170       180
                  ....*....|....*....|....*..
gi 1622849033 634 IRFFPPKSNKAYQYHSYngwNRDAYSL 660
Cdd:TIGR00424 432 ILFFPKHSSRPIKYPSE---KRDVDSL 455
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 455-541 4.07e-08

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: 52.27  E-value: 4.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 455 VTTLGPQNFPA---NDKEPWLVDFFAPWCPPCRALLPELRRASNLLY---GQLKFGTLDCT--VHEGLCNMYNIQAYPTT 526
Cdd:cd02992     3 VIVLDAASFNSallGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRkwrPVVRVAAVDCAdeENVALCRDFGVTGYPTL 82

                          90       100
                  ....*....|....*....|
gi 1622849033 527 VVF-----NQSNIHEYEGHH 541
Cdd:cd02992    83 RYFppfskEATDGLKQEGPE 102
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 129-229 8.89e-08

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: 50.91  E-value: 8.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 129 PEIITLERREFDAAV---NSGELWFVNFYSPGCSHCHDLAPTWRDFAKEVDGL-LRIGAVNC-GDDRMLCRMK-GVNSYP 202
Cdd:cd02993     1 EAVVTLSRAEIEALAkgeRRNQSTLVVLYAPWCPFCQAMEASYEELAEKLAGSnVKVAKFNAdGEQREFAKEElQLKSFP 80

                          90       100
                  ....*....|....*....|....*....
gi 1622849033 203 SLFIFRSGMA-PVKYHGD-RSKESLVSFA 229
Cdd:cd02993    81 TILFFPKNSRqPIKYPSEqRDVDSLLMFV 109
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 150-232 2.98e-07

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


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 53.91  E-value: 2.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 150 FVNFYSPGCSHCHDLAPTWRDFAKEVDgllrigavNCGDDRMLCRMKG---------VNSYPSLFIFRSG--MAPVKYHG 218
Cdd:TIGR01130 368 LVEFYAPWCGHCKNLAPIYEELAEKYK--------DAESDVVIAKMDAtandvppfeVEGFPTIKFVPAGkkSEPVPYDG 439

                          90
                  ....*....|....
gi 1622849033 219 DRSKESLVSFAMQH 232
Cdd:TIGR01130 440 DRTLEDFSKFIAKH 453
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 154-233 5.28e-07

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 52.83  E-value: 5.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 154 YSPGCSHCHDLAPTWRDFAKEV--DGLLRIGAVNcGDDRMLcRMKGVN--SYPSLFIFRSG-MAPVKYHGDRSKESLVSF 228
Cdd:PTZ00102  383 YAPWCGHCKNLEPVYNELGEKYkdNDSIIVAKMN-GTANET-PLEEFSwsAFPTILFVKAGeRTPIPYEGERTVEGFKEF 460


                  ....*
gi 1622849033 229 AMQHV 233
Cdd:PTZ00102  461 VNKHA 465
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 673-719 5.67e-07

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 49.69  E-value: 5.67e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1622849033 673 TDLTPQTFSEKVLQGKnHWVIDFYAPWCGPCQNFAPEFELLARMIKG 719
Cdd:COG0526    14 TDLDGKPLSLADLKGK-PVLVNFWATWCPPCRAEMPVLKELAEEYGG 59
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 472-550 5.73e-07

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: 48.32  E-value: 5.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 472 LVDFFAPWCPPCRALLPELRRASNLLYGQ--LKFGTLDCTVHEgLCNMYNIQAYPTTVVF---NQSNIHEYEGHHSAEQI 546
Cdd:cd02995    22 LVEFYAPWCGHCKALAPIYEELAEKLKGDdnVVIAKMDATAND-VPSEFVVDGFPTILFFpagDKSNPIKYEGDRTLEDL 100


                  ....
gi 1622849033 547 LEFI 550
Cdd:cd02995   101 IKFI 104
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 34-97 6.48e-07

Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 52.34  E-value: 6.48e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849033  34 QDFYSLLGVSK---TASSREIRQAFKKLALKLHPDKNP--NNPNAHGDFLKINRAYEVLKDEDLRKKYD 97
Cdd:COG5269    43 VDLYALLGLSKyrtKAIPPQILKAHKKKVYKYHPDKTAagGNKGCDEFFKLIQKAREVLGDRKLRLQYD 111
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 557-637 9.37e-07

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: 48.08  E-value: 9.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 557 SVVSLTPTTFNELVTQRKHNevwMVDFYSPWCHPCQVLMPEWKRMARTL--TGLINVGSIDC-QQYHSFCAQE-NVQRYP 632
Cdd:cd02997     1 DVVHLTDEDFRKFLKKEKHV---LVMFYAPWCGHCKKMKPEFTKAATELkeDGKGVLAAVDCtKPEHDALKEEyNVKGFP 77


                  ....*
gi 1622849033 633 EIRFF 637
Cdd:cd02997    78 TFKYF 82
trxA PRK09381
thioredoxin TrxA;
472-551 1.42e-06

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 47.75  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 472 LVDFFAPWCPPCRALLPELRRASNLLYGQLKFGTLDCTVHEGLCNMYNIQAYPTTVVFNQSNIHEYE-GHHSAEQILEFI 550
Cdd:PRK09381   25 LVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKvGALSKGQLKEFL 104


                  .
gi 1622849033 551 E 551
Cdd:PRK09381  105 D 105
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
400-552 1.43e-06

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 49.28  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 400 RFDCSSAPDICSNLYVFQPSLAVFKGQGTKEYEIHHGKKILYDILAFAKESVNSHVTTLGPQNFPA---NDKEPWLVDFF 476
Cdd:pfam13848  24 RFGITFSKEVADKYNIKEPAILLFRKFDEETVHYPGDSINFEDLKKFIQKNCLPLVREFTPENAEElfeEGIPPLLLLFL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 477 APWCPPCRALLPELRRASNLLYGQLKFGTLDCTVHEGLCNMYNIQ--AYPTTVVFNQSNiHEY----EGHHSAEQILEFI 550
Cdd:pfam13848 104 KKDDESTEEFKKALEKVAKKFRGKINFALVDAKSFGRPLEYFGLSesDLPVIVIVDSFS-HMYkyfpSDEFSPESLKEFI 182


                  ..
gi 1622849033 551 ED 552
Cdd:pfam13848 183 ND 184
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 682-775 1.93e-06

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


Pssm-ID: 239291 [Multi-domain]  Cd Length: 109  Bit Score: 47.06  E-value: 1.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 682 EKVLQGKNH---WVIDFYAPWCGPCQNFAPEFELLARMIKG-KVKAGKV----DCQAYAQtcQKAGIRAYPTVkFYFYER 753
Cdd:cd02993    12 EALAKGERRnqsTLVVLYAPWCPFCQAMEASYEELAEKLAGsNVKVAKFnadgEQREFAK--EELQLKSFPTI-LFFPKN 88

                          90       100
                  ....*....|....*....|....
gi 1622849033 754 AKR--NFQEEQintRDAKAIAALI 775
Cdd:cd02993    89 SRQpiKYPSEQ---RDVDSLLMFV 109
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 565-637 2.04e-06

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: 46.78  E-value: 2.04e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622849033 565 TFNELVTQrkhNEVWMVDFYSPWCHPCQVLMPEWKRMARTLTGlINVGSIDCQQYHSFCAQENVQRYPEIRFF 637
Cdd:cd02947     2 EFEELIKS---AKPVVVDFWAPWCGPCKAIAPVLEELAEEYPK-VKFVKVDVDENPELAEEYGVRSIPTFLFF 70
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 150-211 2.30e-06

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: 45.77  E-value: 2.30e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622849033 150 FVNFYSPGCSHCHDLAPTWRDFAKEVDGlLRIGAVNCGDDRMLCRMK---GVNSYPSLFIFRSGM 211
Cdd:cd01659     1 LVLFYAPWCPFCQALRPVLAELALLNKG-VKFEAVDVDEDPALEKELkryGVGGVPTLVVFGPGI 64
TMX2 cd02962
TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related ...
 669-747 2.33e-06

TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related transmembrane protein, identified and characterized through the cloning of its cDNA from a human fetal library. It contains a TRX domain but the redox active CXXC motif is replaced with SXXC. Sequence analysis predicts that TMX2 may be a Type I membrane protein, with its C-terminal half protruding on the luminal side of the endoplasmic reticulum (ER). In addition to the TRX domain, transmembrane region and ER-retention signal, TMX2 also contains a Myb DNA-binding domain repeat signature and a dileucine motif in the tail.


Pssm-ID: 239260 [Multi-domain]  Cd Length: 152  Bit Score: 48.15  E-value: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 669 PQVSTDLTPQTFSEKVLQGKN-HWVIDFYAPWCGPCQNFAPEFELLARMIKGK-VKAGKVDCQAYAQTCQKAGIRAYPTV 746
Cdd:cd02962    27 PEHIKYFTPKTLEEELERDKRvTWLVEFFTTWSPECVNFAPVFAELSLKYNNNnLKFGKIDIGRFPNVAEKFRVSTSPLS 106


                  .
gi 1622849033 747 K 747
Cdd:cd02962   107 K 107
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 466-550 3.02e-06

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


Pssm-ID: 239291 [Multi-domain]  Cd Length: 109  Bit Score: 46.68  E-value: 3.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 466 NDKEPWLVDFFAPWCPPCRALLPELRRASNLLYGQ-LKFGTLDCTVHEGLCNMYNIQ--AYPTTVVF--NQSNIHEYEG- 539
Cdd:cd02993    19 RRNQSTLVVLYAPWCPFCQAMEASYEELAEKLAGSnVKVAKFNADGEQREFAKEELQlkSFPTILFFpkNSRQPIKYPSe 98

                          90
                  ....*....|.
gi 1622849033 540 HHSAEQILEFI 550
Cdd:cd02993    99 QRDVDSLLMFV 109
PTZ00051 PTZ00051
thioredoxin; Provisional
 566-644 3.78e-06

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 46.02  E-value: 3.78e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849033 566 FNELVTQrkhNEVWMVDFYSPWCHPCQVLMPEWKRMARTLTGLINVgSIDCQQYHSFCAQENVQRYPEIRFFppKSNKA 644
Cdd:PTZ00051   11 FESTLSQ---NELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFV-KVDVDELSEVAEKENITSMPTFKVF--KNGSV 83
PRK10996 PRK10996
thioredoxin 2; Provisional
 466-531 5.40e-06

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 46.60  E-value: 5.40e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849033 466 NDKEPWLVDFFAPWCPPCRALLPELRRASNLLYGQLKFGTLDCTVHEGLCNMYNIQAYPTTVVFNQ 531
Cdd:PRK10996   50 QDDLPVVIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFKN 115
PTZ00051 PTZ00051
thioredoxin; Provisional
 472-531 9.64e-06

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 44.87  E-value: 9.64e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 472 LVDFFAPWCPPCRALLPELRRASNlLYGQLKFGTLDCTVHEGLCNMYNIQAYPTTVVFNQ 531
Cdd:PTZ00051   22 IVDFYAEWCGPCKRIAPFYEECSK-EYTKMVFVKVDVDELSEVAEKENITSMPTFKVFKN 80
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 692-749 1.17e-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: 43.84  E-value: 1.17e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622849033 692 VIDFYAPWCGPCQNFAPEFELLARMIKGkVKAGKVDCQAYAQTCQKA---GIRAYPTVKFY 749
Cdd:cd01659     1 LVLFYAPWCPFCQALRPVLAELALLNKG-VKFEAVDVDEDPALEKELkryGVGGVPTLVVF 60
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 557-652 1.26e-05

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: 44.85  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 557 SVVSLTPTTFNELVTQRKHNeVwMVDFYSPWCHPCQVLMPEWKRMARTLTG--LINVGSIDcqqyhsfcAQEN------- 627
Cdd:cd02995     1 PVKVVVGKNFDEVVLDSDKD-V-LVEFYAPWCGHCKALAPIYEELAEKLKGddNVVIAKMD--------ATANdvpsefv 70

                          90       100
                  ....*....|....*....|....*
gi 1622849033 628 VQRYPEIRFFPpkSNKAYQYHSYNG 652
Cdd:cd02995    71 VDGFPTILFFP--AGDKSNPIKYEG 93
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 561-638 1.40e-05

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: 44.59  E-value: 1.40e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622849033 561 LTPTTFNELVTQRkhNEVWMVDFYSPWCHPCQVLMPEWKRMARTLTGLINVGSIDCQQYHSFCAQENVQRYPEIRFFP 638
Cdd:TIGR01068   1 LTDANFDETIASS--DKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFK 76
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 673-720 1.70e-05

TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 44.53  E-value: 1.70e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622849033 673 TDLTPQTFSEKVLQGKnHWVIDFYAPWCGPCQNFAPEFELLARMIKGK 720
Cdd:cd02966     5 PDLDGKPVSLSDLKGK-VVLVNFWASWCPPCRAEMPELEALAKEYKDD 51
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 470-495 3.06e-05

TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 43.76  E-value: 3.06e-05
                          10        20
                  ....*....|....*....|....*.
gi 1622849033 470 PWLVDFFAPWCPPCRALLPELRRASN 495
Cdd:cd02966    21 VVLVNFWASWCPPCRAEMPELEALAK 46
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 688-776 3.92e-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: 46.93  E-value: 3.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 688 KNHWVIDFYAPWCGPCQNFAPEFELLARMIKGK-VKAGKV----DCQAYAQtcQKAGIRAYPTVKFyFYERAKR--NFQE 760
Cdd:TIGR00424 371 KEAWLVVLYAPWCPFCQAMEASYLELAEKLAGSgVKVAKFradgDQKEFAK--QELQLGSFPTILF-FPKHSSRpiKYPS 447

                          90
                  ....*....|....*.
gi 1622849033 761 EQintRDAKAIAALIN 776
Cdd:TIGR00424 448 EK---RDVDSLMSFVN 460
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
465-550 5.53e-05

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 42.80  E-value: 5.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 465 ANDKEPWLVDFFAPWCPPCRALLPE----------LRRASNLLY------GQLKFGTLDCTVHEGLCNMYNIQAYPTTVV 528
Cdd:pfam13098   1 KGNGKPVLVVFTDPDCPYCKKLKKElledpdvtvyLGPNFVFIAvniwcaKEVAKAFTDILENKELGRKYGVRGTPTIVF 80

                          90       100
                  ....*....|....*....|...
gi 1622849033 529 FNQS-NIHEYEGHHSAEQILEFI 550
Cdd:pfam13098  81 FDGKgELLRLPGYVPAEEFLALL 103
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 130-228 5.63e-05

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: 42.69  E-value: 5.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 130 EIITLERREFDAAVNSGELWFVNFYSPGCSHCHDLAPTWRDFAKEV--DGLLRIGAVNC--GDDRMLCRMKGVNSYPSLF 205
Cdd:cd02997     1 DVVHLTDEDFRKFLKKEKHVLVMFYAPWCGHCKKMKPEFTKAATELkeDGKGVLAAVDCtkPEHDALKEEYNVKGFPTFK 80

                          90       100
                  ....*....|....*....|...
gi 1622849033 206 IFRSGMAPVKYHGDRSKESLVSF 228
Cdd:cd02997    81 YFENGKFVEKYEGERTAEDIIEF 103
trxA PRK09381
thioredoxin TrxA;
130-228 7.33e-05

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 42.74  E-value: 7.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 130 EIITLERREFDAAVNSGE-LWFVNFYSPGCSHCHDLAPTWRDFAKEVDGLLRIGAVNCGDDRMLCRMKGVNSYPSLFIFR 208
Cdd:PRK09381    4 KIIHLTDDSFDTDVLKADgAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFK 83

                          90       100
                  ....*....|....*....|
gi 1622849033 209 SGMAPVKYHGDRSKESLVSF 228
Cdd:PRK09381   84 NGEVAATKVGALSKGQLKEF 103
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 151-229 7.39e-05

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


Pssm-ID: 239261 [Multi-domain]  Cd Length: 111  Bit Score: 42.75  E-value: 7.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 151 VNFYSPGCSHCHDLAPTWRDFAKEVDGL-LRIGAVNCGDDRMLCRMKGVNSYPSLFIFRSGMAPVKYHGDRSKESLVSFA 229
Cdd:cd02963    29 IKITSDWCFSCIHIEPVWKEVIQELEPLgVGIATVNAGHERRLARKLGAHSVPAIVGIINGQVTFYHDSSFTKQHVVDFV 108
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
470-550 1.05e-04

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 42.93  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 470 PWLVDFFAPWCPPCRALLPELRRASNllygqlKFGTLDCTV----------------------------HEGLCNMYNIQ 521
Cdd:COG1225    23 PVVLYFYATWCPGCTAELPELRDLYE------EFKDKGVEVlgvssdsdeahkkfaekyglpfpllsdpDGEVAKAYGVR 96

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1622849033 522 AYPTTVVFN------QSNIHEYEGHHSAEQILEFI 550
Cdd:COG1225    97 GTPTTFLIDpdgkirYVWVGPVDPRPHLEEVLEAL 131
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 128-228 1.06e-04

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 43.14  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 128 DPEIITLERREFDAAVNSGELWFVNFYSPGCSHCHDLAPTWRDFAKEVDGlLRIGAVNCGDDR----------------- 190
Cdd:COG0526    10 DFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYGG-VVFVGVDVDENPeavkaflkelglpypvl 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622849033 191 -----MLCRMKGVNSYPSLFIF-RSGMAPVKYHGDRSKESLVSF 228
Cdd:COG0526    89 ldpdgELAKAYGVRGIPTTVLIdKDGKIVARHVGPLSPEELEEA 132
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 578-608 1.27e-04

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 42.75  E-value: 1.27e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1622849033 578 VWMVDFYSPWCHPCQVLMPEWKRMARTLTGL 608
Cdd:COG0526    30 PVLVNFWATWCPPCRAEMPVLKELAEEYGGV 60
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 692-776 3.06e-04

TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT contains an N-terminal TRX-like domain, which does not contain the catalytic CXXC motif, followed by one to three glutaredoxin domains. The TRX-like domain is required for interaction with PKC theta. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli.


Pssm-ID: 239282 [Multi-domain]  Cd Length: 97  Bit Score: 40.72  E-value: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 692 VIDFYAPWCGPCQNFAPEFELLARMIKGKVKAGKVDCQAYAQTCQKAGIRAYPTVKFYfyerakRNFQE-EQINTRDAKA 770
Cdd:cd02984    18 VLHFWAPWAEPCKQMNQVFEELAKEAFPSVLFLSIEAEELPEISEKFEITAVPTFVFF------RNGTIvDRVSGADPKE 91


                  ....*.
gi 1622849033 771 IAALIN 776
Cdd:cd02984    92 LAKKVE 97
PLN02309 PLN02309
5'-adenylylsulfate reductase
 682-756 3.21e-04

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 44.01  E-value: 3.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 682 EKVLQGKNH---WVIDFYAPWCGPCQNFAPEFELLA-RMIKGKVKAGKV----DCQAYAQtcQKAGIRAYPTVkFYFYER 753
Cdd:PLN02309  356 ENLLKLENRkepWLVVLYAPWCPFCQAMEASYEELAeKLAGSGVKVAKFradgDQKEFAK--QELQLGSFPTI-LLFPKN 432


                  ...
gi 1622849033 754 AKR 756
Cdd:PLN02309  433 SSR 435
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 445-491 3.37e-04

TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, periplasmic TRX-like reductase containing a CXXC motif that specifically donates reducing equivalents to apocytochrome c via CcmH, another cytochrome c maturation (Ccm) factor with a redox active CXXC motif. Assembly of cytochrome c requires the ligation of heme to reduced thiols of the apocytochrome. In bacteria, this assembly occurs in the periplasm. The reductase activity of DsbE in the oxidizing environment of the periplasm is crucial in the maturation of cytochrome c.


Pssm-ID: 239308 [Multi-domain]  Cd Length: 127  Bit Score: 41.02  E-value: 3.37e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1622849033 445 AFAKESVNSHVTTLGPQNFPandKEPWLVDFFAPWCPPCRALLPELR 491
Cdd:cd03010     5 AFSLPALPGPDKTLTSADLK---GKPYLLNVWASWCAPCREEHPVLM 48
PRK10996 PRK10996
thioredoxin 2; Provisional
 128-210 3.70e-04

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 41.21  E-value: 3.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 128 DPEIITLERREFDAAVNSGELWFVNFYSPGCSHCHDLAPTWRDFAKEVDGLLRIGAVNCGDDRMLCRMKGVNSYPSLFIF 207
Cdd:PRK10996   34 DGEVINATGETLDKLLQDDLPVVIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIF 113


                  ...
gi 1622849033 208 RSG 210
Cdd:PRK10996  114 KNG 116
trxA PRK09381
thioredoxin TrxA;
554-637 3.82e-04

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 40.82  E-value: 3.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 554 MNPSVVSLTPTTFNELVTqrKHNEVWMVDFYSPWCHPCQVLMPEWKRMARTLTGLINVGSIDCQQYHSFCAQENVQRYPE 633
Cdd:PRK09381    1 MSDKIIHLTDDSFDTDVL--KADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPT 78


                  ....
gi 1622849033 634 IRFF 637
Cdd:PRK09381   79 LLLF 82
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 455-495 4.39e-04

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


Pssm-ID: 239309 [Multi-domain]  Cd Length: 123  Bit Score: 40.74  E-value: 4.39e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1622849033 455 VTTLGPQNF--PANDKEPWLVDFFAPWCPPCRALLPELRRASN 495
Cdd:cd03011     5 ATTLDGEQFdlESLSGKPVLVYFWATWCPVCRFTSPTVNQLAA 47
PLN02309 PLN02309
5'-adenylylsulfate reductase
 129-230 5.43e-04

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 43.24  E-value: 5.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 129 PEIITLERREFDAAV---NSGELWFVNFYSPGCSHCHDLAPTWRDFAKEVDGL-LRIGAVNC-GDDRMLCRMK-GVNSYP 202
Cdd:PLN02309  345 QNVVALSRAGIENLLkleNRKEPWLVVLYAPWCPFCQAMEASYEELAEKLAGSgVKVAKFRAdGDQKEFAKQElQLGSFP 424

                          90       100       110
                  ....*....|....*....|....*....|
gi 1622849033 203 SLFIFRSGMA-PVKYHGD-RSKESLVSFAM 230
Cdd:PLN02309  425 TILLFPKNSSrPIKYPSEkRDVDSLLSFVN 454
PTZ00051 PTZ00051
thioredoxin; Provisional
 138-212 5.73e-04

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 39.86  E-value: 5.73e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622849033 138 EFDAAVNSGELWFVNFYSPGCSHCHDLAPTWRDFAKEVDGLLRIgAVNCGDDRMLCRMKGVNSYPSLFIFRSGMA 212
Cdd:PTZ00051   10 EFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFV-KVDVDELSEVAEKENITSMPTFKVFKNGSV 83
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 472-550 8.67e-04

PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of uncharacterized PDI-like eukaryotic proteins containing only one redox active TRX (a) domain with a CXXS motif, similar to ERp44. CXXS is still a redox active motif; however, the mixed disulfide formed with the substrate is more stable than those formed by CXXC motif proteins. PDI-related proteins are usually involved in the oxidative protein folding in the ER by acting as catalysts and folding assistants. ERp44 is involved in thiol-mediated retention in the ER.


Pssm-ID: 239297 [Multi-domain]  Cd Length: 100  Bit Score: 39.26  E-value: 8.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 472 LVDFFAPWCPPCRALLPELRRASNlLYGQLKFGTLD-CTVHEGLCNMYNIQAYPTTVVFNQSNIHEYEGHHSAEQILEFI 550
Cdd:cd02999    22 AVLFYASWCPFSASFRPHFNALSS-MFPQIRHLAIEeSSIKPSLLSRYGVVGFPTILLFNSTPRVRYNGTRTLDSLAAFY 100
TraF pfam13728
F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated ...
 148-216 8.72e-04

F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated with export. The 19 amino acids at the amino terminus of the polypeptides appear to constitute a typical membrane leader peptide - not included in this family, while the remainder of the molecule is predicted to be primarily hydrophilic in character. F plasmid TraF and TraH are required for F pilus assembly and F plasmid transfer, and they are both localized to the outer membrane in the presence of the complete F transfer region, especially TraV, the putative anchor.


Pssm-ID: 433436 [Multi-domain]  Cd Length: 224  Bit Score: 41.52  E-value: 8.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 148 LWFvnFYSPGCSHCHDLAPTWRDFAKE---------VDGLLRIGAVNCGDDRMLCRMKGVNSYPSLFIFRSG---MAPVK 215
Cdd:pfam13728 133 LIF--FYRGDCPYCEAQAPILQAFADKygwtvrpvsVDGRPLPGFPNYRVDNGQAARLGVKRTPALFLVNPPsgdVVPVA 210


                  .
gi 1622849033 216 Y 216
Cdd:pfam13728 211 A 211
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 145-208 1.95e-03

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


Pssm-ID: 239247 [Multi-domain]  Cd Length: 97  Bit Score: 38.25  E-value: 1.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622849033 145 SGELWFVNFYSPGCSHCHDLAPTWRDFAKEVDGLLRIGAVNCGDDRMLCRMKGVNSYPSLFIFR 208
Cdd:cd02949    12 SDRLILVLYTSPTCGPCRTLKPILNKVIDEFDGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFFK 75
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 695-749 2.34e-03

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


Pssm-ID: 239247 [Multi-domain]  Cd Length: 97  Bit Score: 38.25  E-value: 2.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622849033 695 FYAPWCGPCQNFAPEFELLARMIKGKVKAGKVDCQAYAQTCQKAGIRAYPTVKFY 749
Cdd:cd02949    20 YTSPTCGPCRTLKPILNKVIDEFDGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFF 74
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 557-637 2.44e-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: 38.14  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 557 SVVSLTPTTFNELVtqrKHNEVWMVDFYSPWCHPCQVLMPEWKRMARTL------TGLINVGSIDCQQYHSFCAQENVQR 630
Cdd:cd02996     2 EIVSLTSGNIDDIL---QSAELVLVNFYADWCRFSQMLHPIFEEAAAKIkeefpdAGKVVWGKVDCDKESDIADRYRINK 78


                  ....*..
gi 1622849033 631 YPEIRFF 637
Cdd:cd02996    79 YPTLKLF 85
PDI_a_EFP1_N cd03006
PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase ...
 467-550 2.81e-03

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: 38.22  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 467 DKEPWLVDFFAPWCPPCRALLPELRRASNLLYGQLKFGTLDCTVHEGLC-NMYNIQAYPTTVVFNQS-NIHEYEGHHSAE 544
Cdd:cd03006    28 DAEVSLVMYYAPWDAQSQAARQEFEQVAQKLSDQVLFVAINCWWPQGKCrKQKHFFYFPVIHLYYRSrGPIEYKGPMRAP 107


                  ....*.
gi 1622849033 545 QILEFI 550
Cdd:cd03006   108 YMEKFV 113
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 566-637 4.12e-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: 4.12e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622849033 566 FNELVTQRKHNEVwMVDFYSPWCHPCQVLMPEWKRMARTLTGLINVGSIDCQQYHSFCAQENVQRYPEIRFF 637
Cdd:cd02956     3 FQQVLQESTQVPV-VVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLF 73
PTZ00100 PTZ00100
DnaJ chaperone protein; Provisional
 37-87 4.33e-03

DnaJ chaperone protein; Provisional


Pssm-ID: 240265  Cd Length: 116  Bit Score: 37.91  E-value: 4.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622849033  37 YSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHgdflKINRAYEVL 87
Cdd:PTZ00100   68 YKILNISPTASKERIREAHKQLMLRNHPDNGGSTYIAS----KVNEAKDLL 114
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 580-645 4.73e-03

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


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 36.52  E-value: 4.73e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849033 580 MVDFYSPWCHPCQVLMPEWKRMARTLTGlINVGSIDCQQYHSFC---AQENVQRYPEIRFFPPKSNKAY 645
Cdd:cd01659     1 LVLFYAPWCPFCQALRPVLAELALLNKG-VKFEAVDVDEDPALEkelKRYGVGGVPTLVVFGPGIGVKY 68
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 144-228 6.69e-03

PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of uncharacterized PDI-like eukaryotic proteins containing only one redox active TRX (a) domain with a CXXS motif, similar to ERp44. CXXS is still a redox active motif; however, the mixed disulfide formed with the substrate is more stable than those formed by CXXC motif proteins. PDI-related proteins are usually involved in the oxidative protein folding in the ER by acting as catalysts and folding assistants. ERp44 is involved in thiol-mediated retention in the ER.


Pssm-ID: 239297 [Multi-domain]  Cd Length: 100  Bit Score: 36.95  E-value: 6.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849033 144 NSGELWFVNFYSPGCSHCHDLAPTWRDFAKEVDGL--LRIGAVNCgDDRMLCRMkGVNSYPSLFIFRSGMApVKYHGDRS 221
Cdd:cd02999    16 NREDYTAVLFYASWCPFSASFRPHFNALSSMFPQIrhLAIEESSI-KPSLLSRY-GVVGFPTILLFNSTPR-VRYNGTRT 92


                  ....*..
gi 1622849033 222 KESLVSF 228
Cdd:cd02999    93 LDSLAAF 99
 
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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