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Conserved domains on  [gi|1229777951|ref|XP_022142140|]
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5'-adenylylsulfate reductase 1, chloroplastic-like [Momordica charantia]

Protein Classification

PLN02309 family protein( domain architecture ID 11476616)

PLN02309 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02309 PLN02309
5'-adenylylsulfate reductase
 21-468 0e+00

5'-adenylylsulfate reductase


:

Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 897.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951  21 FSRSIAASDPKAPQIGYLRLSSRPNVPASSVNYYSQRRCSVEPLHAEPKRSDSVAPLAATSVAPGVVEQAEVEDYESLAK 100
Cdd:PLN02309   12 SSRSGASSESKAKQIGSLRLLDRGGLSARAYSLSGKRSSAAKPLNAQPAARQAMIPSAATAVAEVPEEEGEVEDFEKLAK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 101 DLENASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYKFFDEVEKHYGIHIEYMFPD 180
Cdd:PLN02309   92 ELENASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRLFDAVEKHYGIRIEYMFPD 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 181 AVEVQALVRTKGMFSFYEDGHQECCRVRKVRPLRRALKGLRAWITGQRKDQSPGTRSEVPVVQVDPVFEGLDGGVGSLVK 260
Cdd:PLN02309  172 AVEVQALVRNKGLFSFYEDGHQECCRVRKVRPLRRALKGLRAWITGQRKDQSPGTRAEVPVVQVDPVFEGLDGGPGSLVK 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 261 WNPVANVDSKDIWNFLRSMNVPVNTLHSQGYVSIGCEPCTRPVLPWQHEREGRWWWEDAKAKECGLHKGNLKQEDAAelN 340
Cdd:PLN02309  252 WNPLANVTGNEVWNFLRTMDVPVNSLHAQGYVSIGCEPCTRPVLPGQHEREGRWWWEDAKAKECGLHKGNIKEEDNG--A 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 341 GNTNGAATNEDIFESQNLVSLTRAGIENLARLEGRKEPWLVVLYAPWCRFCQAMEASYVELAEKLDGTGVKVGKFRADGD 420
Cdd:PLN02309  330 ANDNGNAAVADIFNSQNVVALSRAGIENLLKLENRKEPWLVVLYAPWCPFCQAMEASYEELAEKLAGSGVKVAKFRADGD 409

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1229777951 421 EKEFAQRELQLGSFPTILFFPKHSSRPIKYPSEKRDVESLTAFVNAFR 468
Cdd:PLN02309  410 QKEFAKQELQLGSFPTILLFPKNSSRPIKYPSEKRDVDSLLSFVNSLR 457
 
Name Accession Description Interval E-value
PLN02309 PLN02309
5'-adenylylsulfate reductase
 21-468 0e+00

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 897.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951  21 FSRSIAASDPKAPQIGYLRLSSRPNVPASSVNYYSQRRCSVEPLHAEPKRSDSVAPLAATSVAPGVVEQAEVEDYESLAK 100
Cdd:PLN02309   12 SSRSGASSESKAKQIGSLRLLDRGGLSARAYSLSGKRSSAAKPLNAQPAARQAMIPSAATAVAEVPEEEGEVEDFEKLAK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 101 DLENASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYKFFDEVEKHYGIHIEYMFPD 180
Cdd:PLN02309   92 ELENASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRLFDAVEKHYGIRIEYMFPD 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 181 AVEVQALVRTKGMFSFYEDGHQECCRVRKVRPLRRALKGLRAWITGQRKDQSPGTRSEVPVVQVDPVFEGLDGGVGSLVK 260
Cdd:PLN02309  172 AVEVQALVRNKGLFSFYEDGHQECCRVRKVRPLRRALKGLRAWITGQRKDQSPGTRAEVPVVQVDPVFEGLDGGPGSLVK 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 261 WNPVANVDSKDIWNFLRSMNVPVNTLHSQGYVSIGCEPCTRPVLPWQHEREGRWWWEDAKAKECGLHKGNLKQEDAAelN 340
Cdd:PLN02309  252 WNPLANVTGNEVWNFLRTMDVPVNSLHAQGYVSIGCEPCTRPVLPGQHEREGRWWWEDAKAKECGLHKGNIKEEDNG--A 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 341 GNTNGAATNEDIFESQNLVSLTRAGIENLARLEGRKEPWLVVLYAPWCRFCQAMEASYVELAEKLDGTGVKVGKFRADGD 420
Cdd:PLN02309  330 ANDNGNAAVADIFNSQNVVALSRAGIENLLKLENRKEPWLVVLYAPWCPFCQAMEASYEELAEKLAGSGVKVAKFRADGD 409

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1229777951 421 EKEFAQRELQLGSFPTILFFPKHSSRPIKYPSEKRDVESLTAFVNAFR 468
Cdd:PLN02309  410 QKEFAKQELQLGSFPTILLFPKNSSRPIKYPSEKRDVDSLLSFVNSLR 457
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 21-468 0e+00

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: 885.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951  21 FSRSIAASDPKAPQIGYLRLSSRPNVPASSVNYySQRRCSVEPLHAEPKRSDSVAPLAATSVAPGV-VEQAEVEDYESLA 99
Cdd:TIGR00424  17 LSRSGESTEAKAAQIGSFRLLDRPHTISPSVNL-SRRRLSVKPLNAEPKRNESIVPSAATTVAPEVeEKVVEVEDFEKLA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 100 KDLENASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYKFFDEVEKHYGIHIEYMFP 179
Cdd:TIGR00424  96 KKLENASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRFFDAVEKQYGIRIEYMFP 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 180 DAVEVQALVRTKGMFSFYEDGHQECCRVRKVRPLRRALKGLRAWITGQRKDQSPGTRSEVPVVQVDPVFEGLDGGVGSLV 259
Cdd:TIGR00424 176 DAVEVQALVRSKGLFSFYEDGHQECCRVRKVRPLRRALKGLKAWITGQRKDQSPGTRSEIPVVQVDPVFEGLDGGVGSLV 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 260 KWNPVANVDSKDIWNFLRSMNVPVNTLHSQGYVSIGCEPCTRPVLPWQHEREGRWWWEDAKAKECGLHKGNLKQE-DAAE 338
Cdd:TIGR00424 256 KWNPVANVEGKDVWNFLRTMDVPVNTLHAQGYVSIGCEPCTRPVLPGQHEREGRWWWEDAKAKECGLHKGNIKEEtLDGA 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 339 LNGntNGAATNEDIFESQNLVSLTRAGIENLARLEGRKEPWLVVLYAPWCRFCQAMEASYVELAEKLDGTGVKVGKFRAD 418
Cdd:TIGR00424 336 VNG--NGSDAVADIFDSNNVVSLSRPGIENLLKLEERKEAWLVVLYAPWCPFCQAMEASYLELAEKLAGSGVKVAKFRAD 413

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1229777951 419 GDEKEFAQRELQLGSFPTILFFPKHSSRPIKYPSEKRDVESLTAFVNAFR 468
Cdd:TIGR00424 414 GDQKEFAKQELQLGSFPTILFFPKHSSRPIKYPSEKRDVDSLMSFVNLLR 463
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 93-326 4.19e-86

3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 439945 [Multi-domain]  Cd Length: 232  Bit Score: 263.63  E-value: 4.19e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951  93 EDYESLAKDLEnASPLEIMDKALEKFGNDIAIAFS-GAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYKFFDEVEKHYG 171
Cdd:COG0175     8 DLLEELNAELE-AEAIEILREAAAEFGGRVVVSSSgGKDSTVLLHLAAKFKPPIPVLFLDTGYEFPETYEFRDRLAERLG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 172 IHIEYMFPDAVEVQALVRtKGMFSFYEDgHQECCRVRKVRPLRRALKGLR--AWITGQRKDQSPgTRSEVPVVQVDPVFE 249
Cdd:COG0175    87 LDLIVVRPEDAFAEQLAE-FGPPLFYRD-PRWCCKIRKVEPLKRALAGYDfdAWITGLRRDESP-TRAKEPVVEWDPVGG 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229777951 250 gldggvgsLVKWNPVANVDSKDIWNFLRSMNVPVNTLHSQGYVSIGCEPCTRPVLPWQHEREGRWWWEDAKAKECGL 326
Cdd:COG0175   164 --------LIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIGCAPCTRAVESGEDERAGRWWDEEKERKECGL 232
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 107-295 3.66e-72

Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) reductase (or PAPS sulfotransferase EC 1.8.4.8) is part of the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP).


Pssm-ID: 467510 [Multi-domain]  Cd Length: 183  Bit Score: 225.94  E-value: 3.66e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 107 PLEIMDKALEKFGNDIAIAFS-GAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYKFFDEVEKHYGIHIEYMFPDAVEVQ 185
Cdd:cd23945     1 PLEILLWAAEEFGPKLVFATSfGAEDAVILDLLSKVRPDIPVVFLDTGYLFPETYDLIDEVEARYGLNIEVYFPEGTEAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 186 ALVRTKGM--FSFYEDGHQECCRVRKVRPLRRALKGLRAWITGQRKDQSPgTRSEVPVVQVDpvfegldgGVGSLVKWNP 263
Cdd:cd23945    81 EEALEGGLneFYLEDEERYDCCRKRKPFPLALALLGVKAWITGRRRDQSP-TRANLPIVEVD--------EEGGLVKINP 151

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1229777951 264 VANVDSKDIWNFLRSMNVPVNTLHSQGYVSIG 295
Cdd:cd23945   152 LADWTWEDVWAYIREHDLPYNPLHDQGYPSIG 183
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 122-302 1.50e-57

Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine phosphosulfate (PAPS) reductase enzymes or PAPS sulfotransferase. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N type ATP PPases and ATP sulphurylases. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP). It is also found in NodP nodulation protein P from Rhizobium which has ATP sulfurylase activity (sulfate adenylate transferase).


Pssm-ID: 396201 [Multi-domain]  Cd Length: 173  Bit Score: 187.89  E-value: 1.50e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 122 IAIAFS-GAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYKFFDEVEKHYGIHIEYMFPDAVEVQALVRTKGMFSFYedg 200
Cdd:pfam01507   2 LVVSFSgGKDSLVLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSSLY--- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 201 hQECCRVRKVRPLRRALK--GLRAWITGQRKDQSPgTRSEVPVVQVDPVFEGLdggvgslVKWNPVANVDSKDIWNFLRS 278
Cdd:pfam01507  79 -RRCCRLRKVEPLKRALKelGFDAWFTGLRRDESP-SRAKLPIVSIDGDFPKV-------IKVFPLLNWTETDVWQYILA 149

                         170       180
                  ....*....|....*....|....
gi 1229777951 279 MNVPVNTLHSQGYVSIGCEPCTRP 302
Cdd:pfam01507 150 NNVPYNPLYDQGYRSIGCYPCTGP 173
 
Name Accession Description Interval E-value
PLN02309 PLN02309
5'-adenylylsulfate reductase
 21-468 0e+00

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 897.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951  21 FSRSIAASDPKAPQIGYLRLSSRPNVPASSVNYYSQRRCSVEPLHAEPKRSDSVAPLAATSVAPGVVEQAEVEDYESLAK 100
Cdd:PLN02309   12 SSRSGASSESKAKQIGSLRLLDRGGLSARAYSLSGKRSSAAKPLNAQPAARQAMIPSAATAVAEVPEEEGEVEDFEKLAK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 101 DLENASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYKFFDEVEKHYGIHIEYMFPD 180
Cdd:PLN02309   92 ELENASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRLFDAVEKHYGIRIEYMFPD 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 181 AVEVQALVRTKGMFSFYEDGHQECCRVRKVRPLRRALKGLRAWITGQRKDQSPGTRSEVPVVQVDPVFEGLDGGVGSLVK 260
Cdd:PLN02309  172 AVEVQALVRNKGLFSFYEDGHQECCRVRKVRPLRRALKGLRAWITGQRKDQSPGTRAEVPVVQVDPVFEGLDGGPGSLVK 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 261 WNPVANVDSKDIWNFLRSMNVPVNTLHSQGYVSIGCEPCTRPVLPWQHEREGRWWWEDAKAKECGLHKGNLKQEDAAelN 340
Cdd:PLN02309  252 WNPLANVTGNEVWNFLRTMDVPVNSLHAQGYVSIGCEPCTRPVLPGQHEREGRWWWEDAKAKECGLHKGNIKEEDNG--A 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 341 GNTNGAATNEDIFESQNLVSLTRAGIENLARLEGRKEPWLVVLYAPWCRFCQAMEASYVELAEKLDGTGVKVGKFRADGD 420
Cdd:PLN02309  330 ANDNGNAAVADIFNSQNVVALSRAGIENLLKLENRKEPWLVVLYAPWCPFCQAMEASYEELAEKLAGSGVKVAKFRADGD 409

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1229777951 421 EKEFAQRELQLGSFPTILFFPKHSSRPIKYPSEKRDVESLTAFVNAFR 468
Cdd:PLN02309  410 QKEFAKQELQLGSFPTILLFPKNSSRPIKYPSEKRDVDSLLSFVNSLR 457
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 21-468 0e+00

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: 885.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951  21 FSRSIAASDPKAPQIGYLRLSSRPNVPASSVNYySQRRCSVEPLHAEPKRSDSVAPLAATSVAPGV-VEQAEVEDYESLA 99
Cdd:TIGR00424  17 LSRSGESTEAKAAQIGSFRLLDRPHTISPSVNL-SRRRLSVKPLNAEPKRNESIVPSAATTVAPEVeEKVVEVEDFEKLA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 100 KDLENASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYKFFDEVEKHYGIHIEYMFP 179
Cdd:TIGR00424  96 KKLENASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRFFDAVEKQYGIRIEYMFP 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 180 DAVEVQALVRTKGMFSFYEDGHQECCRVRKVRPLRRALKGLRAWITGQRKDQSPGTRSEVPVVQVDPVFEGLDGGVGSLV 259
Cdd:TIGR00424 176 DAVEVQALVRSKGLFSFYEDGHQECCRVRKVRPLRRALKGLKAWITGQRKDQSPGTRSEIPVVQVDPVFEGLDGGVGSLV 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 260 KWNPVANVDSKDIWNFLRSMNVPVNTLHSQGYVSIGCEPCTRPVLPWQHEREGRWWWEDAKAKECGLHKGNLKQE-DAAE 338
Cdd:TIGR00424 256 KWNPVANVEGKDVWNFLRTMDVPVNTLHAQGYVSIGCEPCTRPVLPGQHEREGRWWWEDAKAKECGLHKGNIKEEtLDGA 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 339 LNGntNGAATNEDIFESQNLVSLTRAGIENLARLEGRKEPWLVVLYAPWCRFCQAMEASYVELAEKLDGTGVKVGKFRAD 418
Cdd:TIGR00424 336 VNG--NGSDAVADIFDSNNVVSLSRPGIENLLKLEERKEAWLVVLYAPWCPFCQAMEASYLELAEKLAGSGVKVAKFRAD 413

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1229777951 419 GDEKEFAQRELQLGSFPTILFFPKHSSRPIKYPSEKRDVESLTAFVNAFR 468
Cdd:TIGR00424 414 GDQKEFAKQELQLGSFPTILFFPKHSSRPIKYPSEKRDVDSLMSFVNLLR 463
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
93-332 1.50e-97

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 293.28  E-value: 1.50e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951  93 EDYESLAKDLENASPLEIMDKALEKFGNDIAIAFS-GAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYKFFDEVEKHYG 171
Cdd:PRK02090   14 LDLAELNAELEGASAQERLAWALENFGGRLALVSSfGAEDAVLLHLVAQVDPDIPVIFLDTGYLFPETYRFIDELTERLL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 172 IHIEYMFPDAVEVQALVRTKGMFSFYEDGHQECCRVRKVRPLRRALKGLRAWITGQRKDQSPgTRSEVPVVQVDpvfegl 251
Cdd:PRK02090   94 LNLKVYRPDASAAEQEARYGGLWEQSVEDRDECCRIRKVEPLNRALAGLDAWITGLRREQSG-TRANLPVLEID------ 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 252 dggvGSLVKWNPVANVDSKDIWNFLRSMNVPVNTLHSQGYVSIGCEPCTRPVLPWQHEREGRwWWEDAKaKECGLHKGNL 331
Cdd:PRK02090  167 ----GGRFKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTRPVEPGEDERAGR-WWGGLK-KECGLHEGNL 240


                  .
gi 1229777951 332 K 332
Cdd:PRK02090  241 P 241
APS_reductase TIGR02055
thioredoxin-dependent adenylylsulfate APS reductase; This model describes recently identified ...
 127-326 3.96e-86

thioredoxin-dependent adenylylsulfate APS reductase; This model describes recently identified adenosine 5'-phosphosulfate (APS) reductase activity found in sulfate-assimilatory prokaryotes, thus separating it from the traditionally described phosphoadenosine 5'-phosphosulfate (PAPS) reductases found in bacteria and fungi. Homologous to PAPS reductase in enterobacteria, cyanobacteria, and yeast, APS reductase here clusters with, and demonstrates greater homology to plant APS reductase. Additionally, the presence of two conserved C-terminal motifs (CCXXRKXXPL _ SXGCXXCT) distinguishes APS substrate specificity and serves as a FeS cluster. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 273945  Cd Length: 191  Bit Score: 262.01  E-value: 3.96e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 127 SGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYKFFDEVEKHYGIHIEYMFPDAVEVQALVRTKGMFSFYEDGHQECCR 206
Cdd:TIGR02055   1 LGAEDVVLVDLAAKVRPDVKVFFLDTGRLFKETYETIDQVRERYDILIDVLSPPPLTVEEQVKEYGLNLFYRSVPHECCG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 207 VRKVRPLRRALKGLRAWITGQRKDQSPgTRSEVPVVQVDpvfegldgGVGSLVKWNPVANVDSKDIWNFLRSMNVPVNTL 286
Cdd:TIGR02055  81 IRKVEPLKRALAGVSAWITGLRRDQSP-TRAQAPFLEID--------EAFGLVKINPLADWTSEDVWEYIADNELPYNPL 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1229777951 287 HSQGYVSIGCEPCTRPVLPWQHEREGRWWWEDAKAKECGL 326
Cdd:TIGR02055 152 HDRGYPSIGCEPCTRPVAPGEDPRAGRWWWEEAAKKECGL 191
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 93-326 4.19e-86

3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 439945 [Multi-domain]  Cd Length: 232  Bit Score: 263.63  E-value: 4.19e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951  93 EDYESLAKDLEnASPLEIMDKALEKFGNDIAIAFS-GAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYKFFDEVEKHYG 171
Cdd:COG0175     8 DLLEELNAELE-AEAIEILREAAAEFGGRVVVSSSgGKDSTVLLHLAAKFKPPIPVLFLDTGYEFPETYEFRDRLAERLG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 172 IHIEYMFPDAVEVQALVRtKGMFSFYEDgHQECCRVRKVRPLRRALKGLR--AWITGQRKDQSPgTRSEVPVVQVDPVFE 249
Cdd:COG0175    87 LDLIVVRPEDAFAEQLAE-FGPPLFYRD-PRWCCKIRKVEPLKRALAGYDfdAWITGLRRDESP-TRAKEPVVEWDPVGG 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229777951 250 gldggvgsLVKWNPVANVDSKDIWNFLRSMNVPVNTLHSQGYVSIGCEPCTRPVLPWQHEREGRWWWEDAKAKECGL 326
Cdd:COG0175   164 --------LIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIGCAPCTRAVESGEDERAGRWWDEEKERKECGL 232
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 107-295 3.66e-72

Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) reductase (or PAPS sulfotransferase EC 1.8.4.8) is part of the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP).


Pssm-ID: 467510 [Multi-domain]  Cd Length: 183  Bit Score: 225.94  E-value: 3.66e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 107 PLEIMDKALEKFGNDIAIAFS-GAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYKFFDEVEKHYGIHIEYMFPDAVEVQ 185
Cdd:cd23945     1 PLEILLWAAEEFGPKLVFATSfGAEDAVILDLLSKVRPDIPVVFLDTGYLFPETYDLIDEVEARYGLNIEVYFPEGTEAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 186 ALVRTKGM--FSFYEDGHQECCRVRKVRPLRRALKGLRAWITGQRKDQSPgTRSEVPVVQVDpvfegldgGVGSLVKWNP 263
Cdd:cd23945    81 EEALEGGLneFYLEDEERYDCCRKRKPFPLALALLGVKAWITGRRRDQSP-TRANLPIVEVD--------EEGGLVKINP 151

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1229777951 264 VANVDSKDIWNFLRSMNVPVNTLHSQGYVSIG 295
Cdd:cd23945   152 LADWTWEDVWAYIREHDLPYNPLHDQGYPSIG 183
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 357-464 2.19e-61

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: 195.36  E-value: 2.19e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 357 NLVSLTRAGIENLARLEGRKEPWLVVLYAPWCRFCQAMEASYVELAEKLDGTGVKVGKFRADGDEKEFAQRELQLGSFPT 436
Cdd:cd02993     2 AVVTLSRAEIEALAKGERRNQSTLVVLYAPWCPFCQAMEASYEELAEKLAGSNVKVAKFNADGEQREFAKEELQLKSFPT 81

                          90       100
                  ....*....|....*....|....*...
gi 1229777951 437 ILFFPKHSSRPIKYPSEKRDVESLTAFV 464
Cdd:cd02993    82 ILFFPKNSRQPIKYPSEQRDVDSLLMFV 109
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 122-302 1.50e-57

Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine phosphosulfate (PAPS) reductase enzymes or PAPS sulfotransferase. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N type ATP PPases and ATP sulphurylases. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP). It is also found in NodP nodulation protein P from Rhizobium which has ATP sulfurylase activity (sulfate adenylate transferase).


Pssm-ID: 396201 [Multi-domain]  Cd Length: 173  Bit Score: 187.89  E-value: 1.50e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 122 IAIAFS-GAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYKFFDEVEKHYGIHIEYMFPDAVEVQALVRTKGMFSFYedg 200
Cdd:pfam01507   2 LVVSFSgGKDSLVLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSSLY--- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 201 hQECCRVRKVRPLRRALK--GLRAWITGQRKDQSPgTRSEVPVVQVDPVFEGLdggvgslVKWNPVANVDSKDIWNFLRS 278
Cdd:pfam01507  79 -RRCCRLRKVEPLKRALKelGFDAWFTGLRRDESP-SRAKLPIVSIDGDFPKV-------IKVFPLLNWTETDVWQYILA 149

                         170       180
                  ....*....|....*....|....
gi 1229777951 279 MNVPVNTLHSQGYVSIGCEPCTRP 302
Cdd:pfam01507 150 NNVPYNPLYDQGYRSIGCYPCTGP 173
cysH TIGR00434
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ...
 107-327 2.87e-46

phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of inorganic sulfate, is designated cysH in Bacteria and MET16 in Saccharomyces cerevisiae. Synonyms include phosphoadenosine phosphosulfate reductase, PAPS reductase, and PAPS reductase, thioredoxin-dependent. In a reaction requiring reduced thioredoxin and NADPH, it converts 3(prime)-phosphoadenylylsulfate (PAPS) to sulfite and adenosine 3(prime),5(prime) diphosphate (PAP). A related family of plant enzymes, scoring below the trusted cutoff, differs in having a thioredoxin-like C-terminal domain, not requiring thioredoxin, and in having a preference for 5(prime)-adenylylsulfate (APS) over PAPS. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 129526  Cd Length: 212  Bit Score: 159.57  E-value: 2.87e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 107 PLEIMDKALEKFGNDIAIAFS-GAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYKFFDEVEKHYGIHIEYMFPDavEVQ 185
Cdd:TIGR00434   1 AQEIIAWAYVTFGGHLVYSTSfGIQGAVLLDLVSKISPDIPVIFLDTGYHFPETYELIDELTERYPLNIKVYKPD--LSL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 186 ALVRTKGMFSFYEDGHQECCRVRKVRPLRRALKGL--RAWITGQRKDQSPgTRSEVPVVQVDPVFEgldggvgsLVKWNP 263
Cdd:TIGR00434  79 AEQAAKYGDKLWEQDPNKYDYLRKVEPMHRALKELhaSAWFTGLRRDQGP-SRANLSILNIDEKFG--------ILKVLP 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229777951 264 VANVDSKDIWNFLRSMNVPVNTLHSQGYVSIGCEPCTRPVLPWQHEREGRWwweDAKAK-ECGLH 327
Cdd:TIGR00434 150 LIDWTWKDVYQYIDAHNLPYNPLHDQGYPSIGDYHSTRPVKEGEDERAGRW---KGKAKtECGLH 211
PAPS_reductase TIGR02057
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ...
 98-327 8.94e-39

phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an electron donor, phosphoadenosine phosphosulfate reductase catalyzes the reduction of 3'-phosphoadenylylsulfate (PAPS) to sulfite and phospho-adenosine-phosphate (PAP). Found in enterobacteria, cyanobacteria, and yeast, PAPS reductase is related to a group of plant (TIGR00424) and bacterial (TIGR02055) enzymes preferring 5'-adenylylsulfate (APS) over PAPS as a substrate for reduction to sulfite. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 131112  Cd Length: 226  Bit Score: 140.35  E-value: 8.94e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951  98 LAKDLENASPLEIMDKALEKFGNDIAI--AFSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYKFFDEVEKHYGIHIE 175
Cdd:TIGR02057   4 LNEQLEKLTPQEIIAWSIVTFPHGLVQtsAFGIQALVTLHLLSSISEPMIPVIFIDTLYHFPQTLTLKDELTKKYYQTLN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 176 YMFPDAVEVQALVRTKgMFSFYEDGHQECC-RVRKVRPLRRALKGLR--AWITGQRKDQSpGTRSEVPVVQVDpvfegld 252
Cdd:TIGR02057  84 LYKYDGCESEADFEAK-YGKLLWQKDIEKYdYIAKVEPMQRALKELNasAWFTGRRRDQG-SARANLPVIEID------- 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229777951 253 gGVGSLVKWNPVANVDSKDIWNFLRSMNVPVNTLHSQGYVSIGCEPCTRPVLPWQHEREGRWWwedAKAK-ECGLH 327
Cdd:TIGR02057 155 -EQNGILKVNPLIDWTFEQVYQYLDAHNVPYNPLLDQGYRSIGDYHSTRKVKEGEDERAGRWK---GKLKtECGIH 226
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 367-464 1.11e-21

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


Pssm-ID: 239259 [Multi-domain]  Cd Length: 101  Bit Score: 89.21  E-value: 1.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 367 ENLARLEGRKEPWLVVLYAPWCRFCQAMEASYVELAEKLDGTG-VKVGKFRADgDEKEFAQRELQLGsFPTILFFPKHSS 445
Cdd:cd02961     6 DNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGkVVVAKVDCT-ANNDLCSEYGVRG-YPTIKLFPNGSK 83

                          90
                  ....*....|....*....
gi 1229777951 446 RPIKYPSEkRDVESLTAFV 464
Cdd:cd02961    84 EPVKYEGP-RTLESLVEFI 101
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 108-301 3.97e-19

uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to Escherichia coli YbdN; This subgroup contains Escherichia coli YbdN and other phosphoadenosine phosphosulfate (PAPS) reductase (or PAPS sulfotransferase EC 1.8.4.8)-like proteins. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N-type ATP PPases and ATP sulfurylases. A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP).


Pssm-ID: 467512 [Multi-domain]  Cd Length: 206  Bit Score: 85.52  E-value: 3.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 108 LEIMDKALEKFgNDIAIAFSGAED--VAL---IEYAHLTGRPFRVFSLDTGRLNPETYKFFDEVEKHYGIHIEY----MF 178
Cdd:cd23947     2 LERIRKVFEEF-DPVIVSFSGGKDslVLLhlaLEALRRLRKDVYVVFIDTGIEFPETIDFVEKLAETLGLDVEAarppLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 179 PDAVEVQALVRTKGM-----FSFYEDGhqeCCRVRKVRPLRRALKGLR----AWITGQRKDQSPgTRSEVPVVQvdpvfe 249
Cdd:cd23947    81 LEWLTSNFQPQWDPIwdnppPPRDYRW---CCDELKLEPFTKWLKEKKpegvLLLVGIRADESL-NRAKRPRVY------ 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1229777951 250 gldGGVGSLVKWNPVANV-------DSKDIWNFLRSMNVPVNTLHSQGYVSIGCEPCTR 301
Cdd:cd23947   151 ---RKYGWRNSTLPGQIVaypikdwSVEDVWLYILRHGLPYNPLYDLGFDRGGCLVCPR 206
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 376-464 1.24e-17

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: 78.06  E-value: 1.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 376 KEPWLVVLYAPWCRFCQAMEASYVELAEKLDGT-GVKVGKFRADGDEKEFAQReLQLGSFPTILFFPKHSSRPIKYpSEK 454
Cdd:cd02998    18 KKDVLVEFYAPWCGHCKNLAPEYEKLAAVFANEdDVVIAKVDADEANKDLAKK-YGVSGFPTLKFFPKGSTEPVKY-EGG 95

                          90
                  ....*....|
gi 1229777951 455 RDVESLTAFV 464
Cdd:cd02998    96 RDLEDLVKFV 105
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 380-464 1.93e-17

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: 77.60  E-value: 1.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 380 LVVLYAPWCRFCQAMEASYVELAEKL-DGTGVKVGKFraDGDEKEFaQRELQLGSFPTILFFPK-HSSRPIKYpSEKRDV 457
Cdd:cd02995    22 LVEFYAPWCGHCKALAPIYEELAEKLkGDDNVVIAKM--DATANDV-PSEFVVDGFPTILFFPAgDKSNPIKY-EGDRTL 97


                  ....*..
gi 1229777951 458 ESLTAFV 464
Cdd:cd02995    98 EDLIKFI 104
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 380-465 9.08e-14

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


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 73.17  E-value: 9.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 380 LVVLYAPWCRFCQAMEASYVELAEKLDGTGVKVGKFRADGDEKEFAQRELQlgSFPTILFFPKHSSR-PIKYpSEKRDVE 458
Cdd:TIGR01130 368 LVEFYAPWCGHCKNLAPIYEELAEKYKDAESDVVIAKMDATANDVPPFEVE--GFPTIKFVPAGKKSePVPY-DGDRTLE 444


                  ....*..
gi 1229777951 459 SLTAFVN 465
Cdd:TIGR01130 445 DFSKFIA 451
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 358-464 1.49e-13

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: 66.55  E-value: 1.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 358 LVSLTRAGIENLARleGRKEPWLVVLYAPWCRFCQAMEASYVELAEKLDGTgVKVGKFraDGDEKE-FAQRElQLGSFPT 436
Cdd:cd03004     3 VITLTPEDFPELVL--NRKEPWLVDFYAPWCGPCQALLPELRKAARALKGK-VKVGSV--DCQKYEsLCQQA-NIRAYPT 76

                          90       100
                  ....*....|....*....|....*...
gi 1229777951 437 ILFFPKHSSRPIKYPSEKRDVESLTAFV 464
Cdd:cd03004    77 IRLYPGNASKYHSYNGWHRDADSILEFI 104
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 376-464 2.14e-12

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: 63.07  E-value: 2.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 376 KEPWLVVLYAPWCRFCQAMEASYVELAEKLDGTgVKVGKFRADGDEKEFAQRELQlgSFPTILFFPKHSSRPIKYPSEkR 455
Cdd:cd03001    18 DDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGI-VKVGAVDADVHQSLAQQYGVR--GFPTIKVFGAGKNSPQDYQGG-R 93


                  ....*....
gi 1229777951 456 DVESLTAFV 464
Cdd:cd03001    94 TAKAIVSAA 102
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 376-465 2.54e-12

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 68.62  E-value: 2.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 376 KEPWLVVLYAPWCRFCQAMEASYVELAEKL-DGTGVKVGKFraDGDEKEFAQRELQLGSFPTILFFPKHSSRPIKYPSEk 454
Cdd:PTZ00102  375 DKDVLLEIYAPWCGHCKNLEPVYNELGEKYkDNDSIIVAKM--NGTANETPLEEFSWSAFPTILFVKAGERTPIPYEGE- 451

                          90
                  ....*....|.
gi 1229777951 455 RDVESLTAFVN 465
Cdd:PTZ00102  452 RTVEGFKEFVN 462
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 354-463 1.26e-09

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 58.10  E-value: 1.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 354 ESQN-LVSLTRAGIENL--ARLEGRKEPWLVVLYAPWCRFCQAMEASYVELAEKLDGTgVKVgkfrADGDekefAQRELQ 430
Cdd:PTZ00443   27 EDANaLVLLNDKNFEKLtqASTGATTGPWFVKFYAPWCSHCRKMAPAWERLAKALKGQ-VNV----ADLD----ATRALN 97

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1229777951 431 LGS------FPTILFFpkHSSRPIKYPSEKRDVESLTAF 463
Cdd:PTZ00443   98 LAKrfaikgYPTLLLF--DKGKMYQYEGGDRSTEKLAAF 134
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 357-440 1.50e-09

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: 55.21  E-value: 1.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 357 NLVSLTRAGIEnlARLEGRKEPWLVVLYAPWCRFCQAMEASYVELAEKLDGtGVKVGKFRADgDEKEFAQReLQLGSFPT 436
Cdd:COG3118     1 AVVELTDENFE--EEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGG-KVKFVKVDVD-ENPELAAQ-FGVRSIPT 75


                  ....
gi 1229777951 437 ILFF 440
Cdd:COG3118    76 LLLF 79
PRK13794 PRK13794
hypothetical protein; Provisional
 92-299 5.24e-09

hypothetical protein; Provisional


Pssm-ID: 237509 [Multi-domain]  Cd Length: 479  Bit Score: 58.14  E-value: 5.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951  92 VEDYESLAKDLENASpLEIMDKALEKFGNDIAIAFSGAED--VALIEYAHLTGRPFRVFSLDTGRLNPETYKFFDEVEKH 169
Cdd:PRK13794  221 VEANKNVLDKYERNS-IGFIRNTAEKINKPVTVAYSGGKDslATLLLALKALGINFPVLFNDTGLEFPETLENVEDVEKH 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 170 YGIHIeymfpdavevqalVRTKGMfSFYEDGHQE---------CCRVRKVRPLRRAL-----KGLRAWItGQRKDQSpGT 235
Cdd:PRK13794  300 YGLEI-------------IRTKSE-EFWEKLEEYgppardnrwCSEVCKLEPLGKLIdekyeGECLSFV-GQRKYES-FN 363

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229777951 236 RSEVPVVQVDPVfegldggVGSLVKWNPVANVDSKDIWNFLRSMNVPVNTLHSQGYVSIGCEPC 299
Cdd:PRK13794  364 RSKKPRIWRNPY-------IKKQILAAPILHWTAMHVWIYLFREKAPYNKLYEQGFDRIGCFMC 420
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 376-466 1.09e-08

Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 52.62  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 376 KEPWLVVLYAPWCRFCQAMEASYVELAEKLDGTgVKVGKFRADgDEKEFAQrELQLGSFPTILFFPKhsSRPIKYPSEKR 455
Cdd:pfam00085  18 SKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGN-VVFAKVDVD-ENPDLAS-KYGVRGYPTLIFFKN--GQPVDDYVGAR 92

                          90
                  ....*....|.
gi 1229777951 456 DVESLTAFVNA 466
Cdd:pfam00085  93 PKDALAAFLKA 103
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 108-295 3.12e-08

FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; Flavin adenine dinucleotide synthase (FADS); EC 2.7.7.2) is involved in the biochemical pathway for converting riboflavin into FAD. By sequence comparison, bacterial and eukaryotic FMNAT enzymes belong to two different protein superfamilies and apparently utilize different sets of active-site residues to accomplish the same chemistry. This subfamily includes eukaryotic FMNATs, which are members of the 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductase-like family belonging to the adenine nucleotide alpha hydrolase superfamily, which has conserved motifs different from those of nucleotidylyl transferases.


Pssm-ID: 467513 [Multi-domain]  Cd Length: 179  Bit Score: 53.29  E-value: 3.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 108 LEIMDKALEKFGND-IAIAFSGAED-VALIE------YAHLTGRPFRVFSLDTGRLN--PETYKFFDEVEKHYG---IHI 174
Cdd:cd23948     6 LEVIEEALDKYGPEeIAISFNGGKDcTVLLHllraalKRKYPSPLTPLKALYIKSPDpfPEVEEFVEDTAKRYNldlITI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 175 EYMFPDAVEVqalvrtkgmfsfYEDGHQEccrvrkvrplrralkgLRAWITGQRKDqspgtrsevpvvqvDP------VF 248
Cdd:cd23948    86 DGPMKEGLEE------------LLKEHPI----------------IKAVFMGTRRT--------------DPhgenlkPF 123

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1229777951 249 EGLDGGVGSLVKWNPVANVDSKDIWNFLRSMNVPVNTLHSQGYVSIG 295
Cdd:cd23948   124 SPTDPGWPQFMRVNPILDWSYHDVWEFLRTLNLPYCSLYDQGYTSLG 170
PRK13795 PRK13795
hypothetical protein; Provisional
 116-299 5.62e-08

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 55.00  E-value: 5.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 116 EKFGNDIAIAFSGAED--VALieyaHLT---GRPFRVFSLDTGRLNPETYKFFDEVEKHYGIHIEYM-----FPDAVEVq 185
Cdd:PRK13795  240 EKYNLPVSVSFSGGKDslVVL----DLAreaLKDFKAFFNNTGLEFPETVENVKEVAEEYGIELIEAdagdaFWRAVEK- 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 186 alvrtkgmFSFYEDGHQECCRVRKVRPLRRALK--GLRAWIT--GQRKDQSpGTRSEVPVVQVDPVfegldggVGSLVKW 261
Cdd:PRK13795  315 --------FGPPARDYRWCCKVCKLGPITRAIKenFPKGCLTfvGQRKYES-FSRAKSPRVWRNPW-------VPNQIGA 378

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1229777951 262 NPVANVDSKDIWNFLRSMNVPVNTLHSQGYVSIGCEPC 299
Cdd:PRK13795  379 SPIQDWTALEVWLYIFWRKLPYNPLYERGFDRIGCWLC 416
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 372-457 6.14e-08

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: 50.53  E-value: 6.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 372 LEGRKEP-WLVVLYAPWCRFCQAMEASYVELAEKLD--GTGVKVGKFraDGDEKEFAQRELQLGSFPTILFFPKHSSRPI 448
Cdd:cd03000    10 KDVRKEDiWLVDFYAPWCGHCKKLEPVWNEVGAELKssGSPVRVGKL--DATAYSSIASEFGVRGYPTIKLLKGDLAYNY 87


                  ....*....
gi 1229777951 449 KYPSEKRDV 457
Cdd:cd03000    88 RGPRTKDDI 96
Sulfate_adenylyltransferase_2 cd23946
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ...
 100-287 1.37e-07

Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in the sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN, coupled to ATP hydrolysis by CysD. CysD belongs to the ATP pyrophosphatase (ATP PPase) family of proteins, members of which include PAPS reductase, GMP synthetase, asparagine synthetase, and NAD(+) synthetase. This subunit is responsible for directly forming APS under control of the G protein. A modified version of the P loop (PP-loop), the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues.


Pssm-ID: 467511  Cd Length: 214  Bit Score: 52.12  E-value: 1.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 100 KDLENASpLEIMDKALEKFGNdIAIAFSGAEDVA----LIEYAHLTGR-PFRVFSLDTGRLNPETYKFFDEVEKHYGIH- 173
Cdd:cd23946     3 RQLEAES-IHIIREVAAEFSN-PVMLYSIGKDSSvmlhLARKAFYPGKpPFPLLHVDTTWKFREMIEFRDRVAKEYGLDl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 174 IEYMFPDAVEvqalvrtKGMFSFYEdGHQECCRVRKVRPLRRALK--GLRAWITGQRKDQSpGTRSEVPVVQVDPVFEGL 251
Cdd:cd23946    81 IVHVNPDGVE-------AGINPFTH-GSAKHTDIMKTEGLKQALDkyGFDAAFGGARRDEE-KSRAKERVYSFRDSNHRW 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1229777951 252 DG---------------GVGSLVKWNPVANVDSKDIWNFLRSMNVPVNTLH 287
Cdd:cd23946   152 DPknqrpelwnqyngrvKKGESIRVFPLSNWTELDIWQYIYLENIPIVPLY 202
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 380-464 1.85e-07

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: 49.21  E-value: 1.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 380 LVVLYAPWCRFCQAMEASYVELAEKL--DGTGVKVGKFRADgdekefAQREL----QLGSFPTILFFpKHSSRPIKYpSE 453
Cdd:cd03005    20 FVKFFAPWCGHCKRLAPTWEQLAKKFnnENPSVKIAKVDCT------QHRELcsefQVRGYPTLLLF-KDGEKVDKY-KG 91

                          90
                  ....*....|.
gi 1229777951 454 KRDVESLTAFV 464
Cdd:cd03005    92 TRDLDSLKEFV 102
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 353-464 5.01e-07

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 52.06  E-value: 5.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 353 FESQNLVSLTRAGIENLARlegRKEPWLVVLYAPWCRFCQAMEASYVELAEKL--DGTGVKVGKFRADGdEKEFAQrELQ 430
Cdd:PTZ00102   29 FISEHVTVLTDSTFDKFIT---ENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLkeKKSEIVLASVDATE-EMELAQ-EFG 103

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1229777951 431 LGSFPTILFFPKhsSRPIKYPSeKRDVESLTAFV 464
Cdd:PTZ00102  104 VRGYPTIKFFNK--GNPVNYSG-GRTADGIVSWI 134
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 380-464 6.62e-07

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


Pssm-ID: 239300 [Multi-domain]  Cd Length: 109  Bit Score: 47.74  E-value: 6.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 380 LVVLYAPWCRFCQAMEASYVELAEKLDGTgVKVGKFRADGDE-KEF-AQRELQlgSFPTILFFP------KHSSRPIKYP 451
Cdd:cd03002    22 LVEFYAPWCGHCKNLKPEYAKAAKELDGL-VQVAAVDCDEDKnKPLcGKYGVQ--GFPTLKVFRppkkasKHAVEDYNGE 98

                          90
                  ....*....|...
gi 1229777951 452 sekRDVESLTAFV 464
Cdd:cd03002    99 ---RSAKAIVDFV 108
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 357-465 9.79e-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: 50.83  E-value: 9.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 357 NLVSLTRagiENLARLEGRKEPWLVVLYAPWCRFCQAMEASYVELAEKL--DGTGVKVGKFRADgDEKEFAQrELQLGSF 434
Cdd:TIGR01130   2 DVLVLTK---DNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELkkKGPPIKLAKVDAT-EEKDLAQ-KYGVSGY 76

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1229777951 435 PTILFFPKHSSRPIKYpSEKRDVESLTAFVN 465
Cdd:TIGR01130  77 PTLKIFRNGEDSVSDY-NGPRDADGIVKYMK 106
PRK08557 PRK08557
hypothetical protein; Provisional
 87-299 1.45e-06

hypothetical protein; Provisional


Pssm-ID: 181465 [Multi-domain]  Cd Length: 417  Bit Score: 50.52  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951  87 VEQAEVEDYESLAKD----LENASpLEIMDKALEKFGND---IAIAFSGAEDVALIEY-AHLTGRPFRVFSLDTGRLNPE 158
Cdd:PRK08557  143 LDFEKIEDYLEKNKEriekLEENS-LSILKDYIEKYKNKgyaINASFSGGKDSSVSTLlAKEVIPDLEVIFIDTGLEYPE 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 159 TYKFFDEVEKHYGIHIEYM----FPDAVEVQAlVRTKGmfsfyedgHQECCRVRKVRPLRRALKGLRAW-----ITGQRK 229
Cdd:PRK08557  222 TINYVKDFAKKYDLNLDTLdgdnFWENLEKEG-IPTKD--------NRWCNSACKLMPLKEYLKKKYGNkkvltIDGSRK 292

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 230 DQSpGTRSEVPvvqvdpvFEGLDGGVGSLVKWNPVANVDSKDIWNFLRSMNVPVNTLHSQGYVSIGCEPC 299
Cdd:PRK08557  293 YES-FTRANLD-------YERKSGFIDFQTNVFPILDWNSLDIWSYIYLNDILYNPLYDKGFERIGCYLC 354
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 356-463 1.52e-06

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: 46.36  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 356 QNLVSLTRAGIEnlaRLEGRKEPWLVVLYAPWCRFCQAMEASYVELAEKLDGTgVKVGKFRAdGDEKEFAQRElQLGSFP 435
Cdd:cd03003     1 PEIVTLDRGDFD---AAVNSGEIWFVNFYSPRCSHCHDLAPTWREFAKEMDGV-IRIGAVNC-GDDRMLCRSQ-GVNSYP 74

                          90       100
                  ....*....|....*....|....*...
gi 1229777951 436 TILFFPKhSSRPIKYPSEkRDVESLTAF 463
Cdd:cd03003    75 SLYVFPS-GMNPEKYYGD-RSKESLVKF 100
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 367-442 4.35e-06

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: 45.39  E-value: 4.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 367 ENLARLEGRKEPWLVVLYAPWCRFCQAMEASYVELAE--KLDGTGVKVGkfrADGDEKEFA--QRELQLGSFPTILFFPK 442
Cdd:cd02997     8 EDFRKFLKKEKHVLVMFYAPWCGHCKKMKPEFTKAATelKEDGKGVLAA---VDCTKPEHDalKEEYNVKGFPTFKYFEN 84
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 357-414 7.05e-06

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: 44.68  E-value: 7.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1229777951 357 NLVSLTRagiENLAR-LEGRkepWLVVLYAPWCRFCQAMEASYVELAEKLDGTGVKVGK 414
Cdd:cd02994     2 NVVELTD---SNWTLvLEGE---WMIEFYAPWCPACQQLQPEWEEFADWSDDLGINVAK 54
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 380-440 1.12e-05

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


Pssm-ID: 239245 [Multi-domain]  Cd Length: 93  Bit Score: 43.70  E-value: 1.12e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229777951 380 LVVLYAPWCRFCQAMEASYVELAEKldGTGVKVGKFRADgDEKEFAQReLQLGSFPTILFF 440
Cdd:cd02947    14 VVDFWAPWCGPCKAIAPVLEELAEE--YPKVKFVKVDVD-ENPELAEE-YGVRSIPTFLFF 70
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 380-440 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: 43.07  E-value: 1.17e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229777951 380 LVVLYAPWCRFCQAMEASYVELAEKLDgtGVKVGKFRADGDEKEF-AQRELQLGSFPTILFF 440
Cdd:cd01659     1 LVLFYAPWCPFCQALRPVLAELALLNK--GVKFEAVDVDEDPALEkELKRYGVGGVPTLVVF 60
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
373-440 1.28e-05

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 43.95  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 373 EGRKEPWLVVLYAPWCRFCQAME--------------ASYVELAEKLDGTGVKVGKFRADGDEKEFAqRELQLGSFPTIL 438
Cdd:pfam13098   1 KGNGKPVLVVFTDPDCPYCKKLKkelledpdvtvylgPNFVFIAVNIWCAKEVAKAFTDILENKELG-RKYGVRGTPTIV 79


                  ..
gi 1229777951 439 FF 440
Cdd:pfam13098  80 FF 81
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 376-442 1.43e-04

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


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 40.74  E-value: 1.43e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229777951 376 KEPWLVVLYAPWCRFCQAMEASYVELAEKLDGTgVKVGKFRADgDEKEFAQReLQLGSFPTILFFPK 442
Cdd:TIGR01068  14 DKPVLVDFWAPWCGPCKMIAPILEELAKEYEGK-VKFVKLNVD-ENPDIAAK-YGIRSIPTLLLFKN 77
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 368-440 1.90e-04

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 41.60  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 368 NLARLEGRkePWLVVLYAPWCRFCQAMEASYVELAEKLDGT---GVKVGKFRADG---------------DEKEFAQREL 429
Cdd:COG0526    22 SLADLKGK--PVLVNFWATWCPPCRAEMPVLKELAEEYGGVvfvGVDVDENPEAVkaflkelglpypvllDPDGELAKAY 99

                          90
                  ....*....|.
gi 1229777951 430 QLGSFPTILFF 440
Cdd:COG0526   100 GVRGIPTTVLI 110
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 369-440 5.09e-03

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 37.58  E-value: 5.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 369 LARLEGRKEpwLVVLYAPWCRFCQAMEASYVELAE------------KLDGTG-VKVGKFraDG---DEKEFAqRELQLG 432
Cdd:COG2143    35 LAKAEGKPI--LLFFESDWCPYCKKLHKEVFSDPEvaaylkenfvvvQLDAEGdKEVTDF--DGetlTEKELA-RKYGVR 109


                  ....*...
gi 1229777951 433 SFPTILFF 440
Cdd:COG2143   110 GTPTLVFF 117
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 357-464 5.31e-03

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


Pssm-ID: 239294 [Multi-domain]  Cd Length: 108  Bit Score: 36.60  E-value: 5.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 357 NLVSLTRAGIENLArleGRKEPWLVVLYAPWCRFCQAMEASYVELAEKL-----DGTGVKVGKFRADgDEKEFAQReLQL 431
Cdd:cd02996     2 EIVSLTSGNIDDIL---QSAELVLVNFYADWCRFSQMLHPIFEEAAAKIkeefpDAGKVVWGKVDCD-KESDIADR-YRI 76

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1229777951 432 GSFPTI-LFFPKHSSRpIKYPSEkRDVESLTAFV 464
Cdd:cd02996    77 NKYPTLkLFRNGMMMK-REYRGQ-RSVEALAEFV 108
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 357-441 8.31e-03

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: 36.09  E-value: 8.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229777951 357 NLVSLTRAGIEnlARLEGRKEPWLVVLYAPWCRFCQAMEASYVELAEKLDG--TGVKVGkfRADGDEKEFAQ--RELQLG 432
Cdd:cd02992     2 PVIVLDAASFN--SALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRKwrPVVRVA--AVDCADEENVAlcRDFGVT 77


                  ....*....
gi 1229777951 433 SFPTILFFP 441
Cdd:cd02992    78 GYPTLRYFP 86
 
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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