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Conserved domains on  [gi|727553193|ref|XP_010448955|]
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PREDICTED: 5'-adenylylsulfate reductase 3, chloroplastic [Camelina sativa]

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
 21-456 0e+00

5'-adenylylsulfate reductase


:

Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 901.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  21 FPSSELKAPQIGSLRLLDRINVSAASLSLSGKRSS-VKALNVQSITKESMVASEKLDV-------VEVEDFEELAKRLEK 92
Cdd:PLN02309  16 GASSESKAKQIGSLRLLDRGGLSARAYSLSGKRSSaAKPLNAQPAARQAMIPSAATAVaevpeeeGEVEDFEKLAKELEN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  93 ASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYGIRIEYMFPDAVEV 172
Cdd:PLN02309  96 ASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRLFDAVEKHYGIRIEYMFPDAVEV 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 173 QALVRNKGLFSFYEDGHQECCRIRKVRPLRRALKGLRAWITGQRKDQSPGTRSEIPVVQVDPVFEGLDGGAGSLVKWNPV 252
Cdd:PLN02309 176 QALVRNKGLFSFYEDGHQECCRVRKVRPLRRALKGLRAWITGQRKDQSPGTRAEVPVVQVDPVFEGLDGGPGSLVKWNPL 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 253 ANVEGNDVWNFLRTMDVPVNTLHAAGYVSIGCEPCTRAVLPGQHEREGRWWWEDAKAKECGLHKGNIKENTNGnaTANVN 332
Cdd:PLN02309 256 ANVTGNEVWNFLRTMDVPVNSLHAQGYVSIGCEPCTRPVLPGQHEREGRWWWEDAKAKECGLHKGNIKEEDNG--AANDN 333

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 333 GKSTVADIFNSENVVNLSRQGIENLMKLENRNEAWIVVLYAPWCPFCQAMEASFDELADKLNGNGVKVAKFRADGDQKEF 412
Cdd:PLN02309 334 GNAAVADIFNSQNVVALSRAGIENLLKLENRKEPWLVVLYAPWCPFCQAMEASYEELAEKLAGSGVKVAKFRADGDQKEF 413

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 727553193 413 AKSELQLGSFPTILVFPKNSSRPIKYPSEKRDVDSLTSFLNLVR 456
Cdd:PLN02309 414 AKQELQLGSFPTILLFPKNSSRPIKYPSEKRDVDSLLSFVNSLR 457
 
Name Accession Description Interval E-value
PLN02309 PLN02309
5'-adenylylsulfate reductase
 21-456 0e+00

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 901.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  21 FPSSELKAPQIGSLRLLDRINVSAASLSLSGKRSS-VKALNVQSITKESMVASEKLDV-------VEVEDFEELAKRLEK 92
Cdd:PLN02309  16 GASSESKAKQIGSLRLLDRGGLSARAYSLSGKRSSaAKPLNAQPAARQAMIPSAATAVaevpeeeGEVEDFEKLAKELEN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  93 ASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYGIRIEYMFPDAVEV 172
Cdd:PLN02309  96 ASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRLFDAVEKHYGIRIEYMFPDAVEV 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 173 QALVRNKGLFSFYEDGHQECCRIRKVRPLRRALKGLRAWITGQRKDQSPGTRSEIPVVQVDPVFEGLDGGAGSLVKWNPV 252
Cdd:PLN02309 176 QALVRNKGLFSFYEDGHQECCRVRKVRPLRRALKGLRAWITGQRKDQSPGTRAEVPVVQVDPVFEGLDGGPGSLVKWNPL 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 253 ANVEGNDVWNFLRTMDVPVNTLHAAGYVSIGCEPCTRAVLPGQHEREGRWWWEDAKAKECGLHKGNIKENTNGnaTANVN 332
Cdd:PLN02309 256 ANVTGNEVWNFLRTMDVPVNSLHAQGYVSIGCEPCTRPVLPGQHEREGRWWWEDAKAKECGLHKGNIKEEDNG--AANDN 333

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 333 GKSTVADIFNSENVVNLSRQGIENLMKLENRNEAWIVVLYAPWCPFCQAMEASFDELADKLNGNGVKVAKFRADGDQKEF 412
Cdd:PLN02309 334 GNAAVADIFNSQNVVALSRAGIENLLKLENRKEPWLVVLYAPWCPFCQAMEASYEELAEKLAGSGVKVAKFRADGDQKEF 413

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 727553193 413 AKSELQLGSFPTILVFPKNSSRPIKYPSEKRDVDSLTSFLNLVR 456
Cdd:PLN02309 414 AKQELQLGSFPTILLFPKNSSRPIKYPSEKRDVDSLLSFVNSLR 457
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 1-456 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: 898.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193    1 MALAINVSSSSSSSVISASSFPSSELKAPQIGSLRLLDRINVSAASLSLSGKRSSVKALNVQSITKESMVAS-------- 72
Cdd:TIGR00424   1 MALAVTSSSTAISGISLSRSGESTEAKAAQIGSFRLLDRPHTISPSVNLSRRRLSVKPLNAEPKRNESIVPSaattvape 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193   73 EKLDVVEVEDFEELAKRLEKASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFD 152
Cdd:TIGR00424  81 VEEKVVEVEDFEKLAKKLENASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRFFD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  153 TVEKHYGIRIEYMFPDAVEVQALVRNKGLFSFYEDGHQECCRIRKVRPLRRALKGLRAWITGQRKDQSPGTRSEIPVVQV 232
Cdd:TIGR00424 161 AVEKQYGIRIEYMFPDAVEVQALVRSKGLFSFYEDGHQECCRVRKVRPLRRALKGLKAWITGQRKDQSPGTRSEIPVVQV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  233 DPVFEGLDGGAGSLVKWNPVANVEGNDVWNFLRTMDVPVNTLHAAGYVSIGCEPCTRAVLPGQHEREGRWWWEDAKAKEC 312
Cdd:TIGR00424 241 DPVFEGLDGGVGSLVKWNPVANVEGKDVWNFLRTMDVPVNTLHAQGYVSIGCEPCTRPVLPGQHEREGRWWWEDAKAKEC 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  313 GLHKGNIKENTNgNATANVNGKSTVADIFNSENVVNLSRQGIENLMKLENRNEAWIVVLYAPWCPFCQAMEASFDELADK 392
Cdd:TIGR00424 321 GLHKGNIKEETL-DGAVNGNGSDAVADIFDSNNVVSLSRPGIENLLKLEERKEAWLVVLYAPWCPFCQAMEASYLELAEK 399

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727553193  393 LNGNGVKVAKFRADGDQKEFAKSELQLGSFPTILVFPKNSSRPIKYPSEKRDVDSLTSFLNLVR 456
Cdd:TIGR00424 400 LAGSGVKVAKFRADGDQKEFAKQELQLGSFPTILFFPKHSSRPIKYPSEKRDVDSLMSFVNLLR 463
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 81-314 2.97e-85

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: 260.93  E-value: 2.97e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  81 EDFEELAKRLEkASPLEIMDKALEKFGNDIAIAFS-GAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYG 159
Cdd:COG0175    8 DLLEELNAELE-AEAIEILREAAAEFGGRVVVSSSgGKDSTVLLHLAAKFKPPIPVLFLDTGYEFPETYEFRDRLAERLG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 160 IRIEYMFPDAVEVQALVRnKGLFSFYEDgHQECCRIRKVRPLRRALKGLR--AWITGQRKDQSPgTRSEIPVVQVDPVFE 237
Cdd:COG0175   87 LDLIVVRPEDAFAEQLAE-FGPPLFYRD-PRWCCKIRKVEPLKRALAGYDfdAWITGLRRDESP-TRAKEPVVEWDPVGG 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727553193 238 gldggagsLVKWNPVANVEGNDVWNFLRTMDVPVNTLHAAGYVSIGCEPCTRAVLPGQHEREGRWWWEDAKAKECGL 314
Cdd:COG0175  164 --------LIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIGCAPCTRAVESGEDERAGRWWDEEKERKECGL 232
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 95-283 9.42e-75

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: 232.10  E-value: 9.42e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  95 PLEIMDKALEKFGNDIAIAFS-GAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYGIRIEYMFPDAVEVQ 173
Cdd:cd23945    1 PLEILLWAAEEFGPKLVFATSfGAEDAVILDLLSKVRPDIPVVFLDTGYLFPETYDLIDEVEARYGLNIEVYFPEGTEAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 174 ALVRNKGL--FSFYEDGHQECCRIRKVRPLRRALKGLRAWITGQRKDQSPgTRSEIPVVQVDpvfegldgGAGSLVKWNP 251
Cdd:cd23945   81 EEALEGGLneFYLEDEERYDCCRKRKPFPLALALLGVKAWITGRRRDQSP-TRANLPIVEVD--------EEGGLVKINP 151

                        170       180       190
                 ....*....|....*....|....*....|..
gi 727553193 252 VANVEGNDVWNFLRTMDVPVNTLHAAGYVSIG 283
Cdd:cd23945  152 LADWTWEDVWAYIREHDLPYNPLHDQGYPSIG 183
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 110-290 8.37e-58

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: 188.27  E-value: 8.37e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  110 IAIAFS-GAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYGIRIEYMFPDAVEVQALVRNKGLFSFYedg 188
Cdd:pfam01507   2 LVVSFSgGKDSLVLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSSLY--- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  189 hQECCRIRKVRPLRRALK--GLRAWITGQRKDQSPgTRSEIPVVQVDPVFEGLdggagslVKWNPVANVEGNDVWNFLRT 266
Cdd:pfam01507  79 -RRCCRLRKVEPLKRALKelGFDAWFTGLRRDESP-SRAKLPIVSIDGDFPKV-------IKVFPLLNWTETDVWQYILA 149

                         170       180
                  ....*....|....*....|....
gi 727553193  267 MDVPVNTLHAAGYVSIGCEPCTRA 290
Cdd:pfam01507 150 NNVPYNPLYDQGYRSIGCYPCTGP 173
 
Name Accession Description Interval E-value
PLN02309 PLN02309
5'-adenylylsulfate reductase
 21-456 0e+00

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 901.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  21 FPSSELKAPQIGSLRLLDRINVSAASLSLSGKRSS-VKALNVQSITKESMVASEKLDV-------VEVEDFEELAKRLEK 92
Cdd:PLN02309  16 GASSESKAKQIGSLRLLDRGGLSARAYSLSGKRSSaAKPLNAQPAARQAMIPSAATAVaevpeeeGEVEDFEKLAKELEN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  93 ASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYGIRIEYMFPDAVEV 172
Cdd:PLN02309  96 ASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRLFDAVEKHYGIRIEYMFPDAVEV 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 173 QALVRNKGLFSFYEDGHQECCRIRKVRPLRRALKGLRAWITGQRKDQSPGTRSEIPVVQVDPVFEGLDGGAGSLVKWNPV 252
Cdd:PLN02309 176 QALVRNKGLFSFYEDGHQECCRVRKVRPLRRALKGLRAWITGQRKDQSPGTRAEVPVVQVDPVFEGLDGGPGSLVKWNPL 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 253 ANVEGNDVWNFLRTMDVPVNTLHAAGYVSIGCEPCTRAVLPGQHEREGRWWWEDAKAKECGLHKGNIKENTNGnaTANVN 332
Cdd:PLN02309 256 ANVTGNEVWNFLRTMDVPVNSLHAQGYVSIGCEPCTRPVLPGQHEREGRWWWEDAKAKECGLHKGNIKEEDNG--AANDN 333

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 333 GKSTVADIFNSENVVNLSRQGIENLMKLENRNEAWIVVLYAPWCPFCQAMEASFDELADKLNGNGVKVAKFRADGDQKEF 412
Cdd:PLN02309 334 GNAAVADIFNSQNVVALSRAGIENLLKLENRKEPWLVVLYAPWCPFCQAMEASYEELAEKLAGSGVKVAKFRADGDQKEF 413

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 727553193 413 AKSELQLGSFPTILVFPKNSSRPIKYPSEKRDVDSLTSFLNLVR 456
Cdd:PLN02309 414 AKQELQLGSFPTILLFPKNSSRPIKYPSEKRDVDSLLSFVNSLR 457
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 1-456 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: 898.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193    1 MALAINVSSSSSSSVISASSFPSSELKAPQIGSLRLLDRINVSAASLSLSGKRSSVKALNVQSITKESMVAS-------- 72
Cdd:TIGR00424   1 MALAVTSSSTAISGISLSRSGESTEAKAAQIGSFRLLDRPHTISPSVNLSRRRLSVKPLNAEPKRNESIVPSaattvape 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193   73 EKLDVVEVEDFEELAKRLEKASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFD 152
Cdd:TIGR00424  81 VEEKVVEVEDFEKLAKKLENASPLEIMDKALEKFGNDIAIAFSGAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRFFD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  153 TVEKHYGIRIEYMFPDAVEVQALVRNKGLFSFYEDGHQECCRIRKVRPLRRALKGLRAWITGQRKDQSPGTRSEIPVVQV 232
Cdd:TIGR00424 161 AVEKQYGIRIEYMFPDAVEVQALVRSKGLFSFYEDGHQECCRVRKVRPLRRALKGLKAWITGQRKDQSPGTRSEIPVVQV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  233 DPVFEGLDGGAGSLVKWNPVANVEGNDVWNFLRTMDVPVNTLHAAGYVSIGCEPCTRAVLPGQHEREGRWWWEDAKAKEC 312
Cdd:TIGR00424 241 DPVFEGLDGGVGSLVKWNPVANVEGKDVWNFLRTMDVPVNTLHAQGYVSIGCEPCTRPVLPGQHEREGRWWWEDAKAKEC 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  313 GLHKGNIKENTNgNATANVNGKSTVADIFNSENVVNLSRQGIENLMKLENRNEAWIVVLYAPWCPFCQAMEASFDELADK 392
Cdd:TIGR00424 321 GLHKGNIKEETL-DGAVNGNGSDAVADIFDSNNVVSLSRPGIENLLKLEERKEAWLVVLYAPWCPFCQAMEASYLELAEK 399

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727553193  393 LNGNGVKVAKFRADGDQKEFAKSELQLGSFPTILVFPKNSSRPIKYPSEKRDVDSLTSFLNLVR 456
Cdd:TIGR00424 400 LAGSGVKVAKFRADGDQKEFAKQELQLGSFPTILFFPKHSSRPIKYPSEKRDVDSLMSFVNLLR 463
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
81-320 3.13e-98

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 294.44  E-value: 3.13e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  81 EDFEELAKRLEKASPLEIMDKALEKFGNDIAIAFS-GAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYG 159
Cdd:PRK02090  14 LDLAELNAELEGASAQERLAWALENFGGRLALVSSfGAEDAVLLHLVAQVDPDIPVIFLDTGYLFPETYRFIDELTERLL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 160 IRIEYMFPDAVEVQALVRNKGLFSFYEDGHQECCRIRKVRPLRRALKGLRAWITGQRKDQSPgTRSEIPVVQVDpvfegl 239
Cdd:PRK02090  94 LNLKVYRPDASAAEQEARYGGLWEQSVEDRDECCRIRKVEPLNRALAGLDAWITGLRREQSG-TRANLPVLEID------ 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 240 dggaGSLVKWNPVANVEGNDVWNFLRTMDVPVNTLHAAGYVSIGCEPCTRAVLPGQHEREGRwWWEDAKaKECGLHKGNI 319
Cdd:PRK02090 167 ----GGRFKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTRPVEPGEDERAGR-WWGGLK-KECGLHEGNL 240


                 .
gi 727553193 320 K 320
Cdd:PRK02090 241 P 241
APS_reductase TIGR02055
thioredoxin-dependent adenylylsulfate APS reductase; This model describes recently identified ...
 115-314 1.36e-85

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: 260.47  E-value: 1.36e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  115 SGAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYGIRIEYMFPDAVEVQALVRNKGLFSFYEDGHQECCR 194
Cdd:TIGR02055   1 LGAEDVVLVDLAAKVRPDVKVFFLDTGRLFKETYETIDQVRERYDILIDVLSPPPLTVEEQVKEYGLNLFYRSVPHECCG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  195 IRKVRPLRRALKGLRAWITGQRKDQSPgTRSEIPVVQVDpvfegldgGAGSLVKWNPVANVEGNDVWNFLRTMDVPVNTL 274
Cdd:TIGR02055  81 IRKVEPLKRALAGVSAWITGLRRDQSP-TRAQAPFLEID--------EAFGLVKINPLADWTSEDVWEYIADNELPYNPL 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 727553193  275 HAAGYVSIGCEPCTRAVLPGQHEREGRWWWEDAKAKECGL 314
Cdd:TIGR02055 152 HDRGYPSIGCEPCTRPVAPGEDPRAGRWWWEEAAKKECGL 191
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 81-314 2.97e-85

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: 260.93  E-value: 2.97e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  81 EDFEELAKRLEkASPLEIMDKALEKFGNDIAIAFS-GAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYG 159
Cdd:COG0175    8 DLLEELNAELE-AEAIEILREAAAEFGGRVVVSSSgGKDSTVLLHLAAKFKPPIPVLFLDTGYEFPETYEFRDRLAERLG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 160 IRIEYMFPDAVEVQALVRnKGLFSFYEDgHQECCRIRKVRPLRRALKGLR--AWITGQRKDQSPgTRSEIPVVQVDPVFE 237
Cdd:COG0175   87 LDLIVVRPEDAFAEQLAE-FGPPLFYRD-PRWCCKIRKVEPLKRALAGYDfdAWITGLRRDESP-TRAKEPVVEWDPVGG 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727553193 238 gldggagsLVKWNPVANVEGNDVWNFLRTMDVPVNTLHAAGYVSIGCEPCTRAVLPGQHEREGRWWWEDAKAKECGL 314
Cdd:COG0175  164 --------LIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIGCAPCTRAVESGEDERAGRWWDEEKERKECGL 232
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 95-283 9.42e-75

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: 232.10  E-value: 9.42e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  95 PLEIMDKALEKFGNDIAIAFS-GAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYGIRIEYMFPDAVEVQ 173
Cdd:cd23945    1 PLEILLWAAEEFGPKLVFATSfGAEDAVILDLLSKVRPDIPVVFLDTGYLFPETYDLIDEVEARYGLNIEVYFPEGTEAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 174 ALVRNKGL--FSFYEDGHQECCRIRKVRPLRRALKGLRAWITGQRKDQSPgTRSEIPVVQVDpvfegldgGAGSLVKWNP 251
Cdd:cd23945   81 EEALEGGLneFYLEDEERYDCCRKRKPFPLALALLGVKAWITGRRRDQSP-TRANLPIVEVD--------EEGGLVKINP 151

                        170       180       190
                 ....*....|....*....|....*....|..
gi 727553193 252 VANVEGNDVWNFLRTMDVPVNTLHAAGYVSIG 283
Cdd:cd23945  152 LADWTWEDVWAYIREHDLPYNPLHDQGYPSIG 183
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 344-452 1.42e-64

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: 203.45  E-value: 1.42e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 344 ENVVNLSRQGIENLMKLENRNEAWIVVLYAPWCPFCQAMEASFDELADKLNGNGVKVAKFRADGDQKEFAKSELQLGSFP 423
Cdd:cd02993    1 EAVVTLSRAEIEALAKGERRNQSTLVVLYAPWCPFCQAMEASYEELAEKLAGSNVKVAKFNADGEQREFAKEELQLKSFP 80

                         90       100
                 ....*....|....*....|....*....
gi 727553193 424 TILVFPKNSSRPIKYPSEKRDVDSLTSFL 452
Cdd:cd02993   81 TILFFPKNSRQPIKYPSEQRDVDSLLMFV 109
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 110-290 8.37e-58

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: 188.27  E-value: 8.37e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  110 IAIAFS-GAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYGIRIEYMFPDAVEVQALVRNKGLFSFYedg 188
Cdd:pfam01507   2 LVVSFSgGKDSLVLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPEDSFAEGINPEGIPSSLY--- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  189 hQECCRIRKVRPLRRALK--GLRAWITGQRKDQSPgTRSEIPVVQVDPVFEGLdggagslVKWNPVANVEGNDVWNFLRT 266
Cdd:pfam01507  79 -RRCCRLRKVEPLKRALKelGFDAWFTGLRRDESP-SRAKLPIVSIDGDFPKV-------IKVFPLLNWTETDVWQYILA 149

                         170       180
                  ....*....|....*....|....
gi 727553193  267 MDVPVNTLHAAGYVSIGCEPCTRA 290
Cdd:pfam01507 150 NNVPYNPLYDQGYRSIGCYPCTGP 173
cysH TIGR00434
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ...
 95-315 3.09e-44

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: 154.17  E-value: 3.09e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193   95 PLEIMDKALEKFGNDIAIAFS-GAEDVALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYGIRIEYMFPD--AVE 171
Cdd:TIGR00434   1 AQEIIAWAYVTFGGHLVYSTSfGIQGAVLLDLVSKISPDIPVIFLDTGYHFPETYELIDELTERYPLNIKVYKPDlsLAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  172 VQALVRNKglfsFYEDGHQECCRIRKVRPLRRALKGL--RAWITGQRKDQSPgTRSEIPVVQVDPVFEgldggagsLVKW 249
Cdd:TIGR00434  81 QAAKYGDK----LWEQDPNKYDYLRKVEPMHRALKELhaSAWFTGLRRDQGP-SRANLSILNIDEKFG--------ILKV 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727553193  250 NPVANVEGNDVWNFLRTMDVPVNTLHAAGYVSIGCEPCTRAVLPGQHEREGRWwweDAKAK-ECGLH 315
Cdd:TIGR00434 148 LPLIDWTWKDVYQYIDAHNLPYNPLHDQGYPSIGDYHSTRPVKEGEDERAGRW---KGKAKtECGLH 211
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 355-452 1.17e-22

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


Pssm-ID: 239259 [Multi-domain]  Cd Length: 101  Bit Score: 91.90  E-value: 1.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 355 ENLMKLENRNEAWIVVLYAPWCPFCQAMEASFDELADKLNGNG-VKVAKFRADgDQKEFAkSELQLGSFPTILVFPKNSS 433
Cdd:cd02961    6 DNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGkVVVAKVDCT-ANNDLC-SEYGVRGYPTIKLFPNGSK 83

                         90
                 ....*....|....*....
gi 727553193 434 RPIKYPSEkRDVDSLTSFL 452
Cdd:cd02961   84 EPVKYEGP-RTLESLVEFI 101
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 369-452 3.15e-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: 76.83  E-value: 3.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 369 VVLYAPWCPFCQAMEASFDELADKL-NGNGVKVAKFraDGDQKEFAkSELQLGSFPTILVFPKNS-SRPIKYpSEKRDVD 446
Cdd:cd02995   23 VEFYAPWCGHCKALAPIYEELAEKLkGDDNVVIAKM--DATANDVP-SEFVVDGFPTILFFPAGDkSNPIKY-EGDRTLE 98


                 ....*.
gi 727553193 447 SLTSFL 452
Cdd:cd02995   99 DLIKFI 104
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 368-452 1.77e-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: 74.98  E-value: 1.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 368 IVVLYAPWCPFCQAMEASFDELADKL-NGNGVKVAKFRADGDQKEFAKsELQLGSFPTILVFPKNSSRPIKYpSEKRDVD 446
Cdd:cd02998   22 LVEFYAPWCGHCKNLAPEYEKLAAVFaNEDDVVIAKVDADEANKDLAK-KYGVSGFPTLKFFPKGSTEPVKY-EGGRDLE 99


                 ....*.
gi 727553193 447 SLTSFL 452
Cdd:cd02998  100 DLVKFV 105
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 346-452 1.62e-15

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: 71.94  E-value: 1.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 346 VVNLSRQGIENLMKleNRNEAWIVVLYAPWCPFCQAMEASFDELADKLNGNgVKVAKFraDGDQKEFAKSELQLGSFPTI 425
Cdd:cd03004    3 VITLTPEDFPELVL--NRKEPWLVDFYAPWCGPCQALLPELRKAARALKGK-VKVGSV--DCQKYESLCQQANIRAYPTI 77

                         90       100
                 ....*....|....*....|....*..
gi 727553193 426 LVFPKNSSRPIKYPSEKRDVDSLTSFL 452
Cdd:cd03004   78 RLYPGNASKYHSYNGWHRDADSILEFI 104
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 96-289 4.31e-14

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: 70.88  E-value: 4.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  96 LEIMDKALEKFgNDIAIAFSGAED--VAL---IEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKHYGIRIEYMFPD-- 168
Cdd:cd23947    2 LERIRKVFEEF-DPVIVSFSGGKDslVLLhlaLEALRRLRKDVYVVFIDTGIEFPETIDFVEKLAETLGLDVEAARPPlf 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 169 ------AVEVQALVRNKGL-FSFYEDGhqeCCRIRKVRPLRRALKGLR----AWITGQRKDQSPgTRSEIPVVQvdpvfe 237
Cdd:cd23947   81 lewltsNFQPQWDPIWDNPpPPRDYRW---CCDELKLEPFTKWLKEKKpegvLLLVGIRADESL-NRAKRPRVY------ 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 727553193 238 gldGGAGSLVKWNPVANV-------EGNDVWNFLRTMDVPVNTLHAAGYVSIGCEPCTR 289
Cdd:cd23947  151 ---RKYGWRNSTLPGQIVaypikdwSVEDVWLYILRHGLPYNPLYDLGFDRGGCLVCPR 206
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 369-453 8.50e-13

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


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 70.09  E-value: 8.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  369 VVLYAPWCPFCQAMEASFDELADKLNGNGVKVAKFRADGDQKEFAKSELQlgSFPTILVFPKNSSR-PIKYpSEKRDVDS 447
Cdd:TIGR01130 369 VEFYAPWCGHCKNLAPIYEELAEKYKDAESDVVIAKMDATANDVPPFEVE--GFPTIKFVPAGKKSePVPY-DGDRTLED 445


                  ....*.
gi 727553193  448 LTSFLN 453
Cdd:TIGR01130 446 FSKFIA 451
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 362-451 1.39e-11

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: 60.76  E-value: 1.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 362 NRNEAWIVVLYAPWCPFCQAMEASFDELADKLNGNgVKVAKFRADGDQKEFAKSELQlgSFPTILVFPKNSSRPIKYPSE 441
Cdd:cd03001   16 NSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGI-VKVGAVDADVHQSLAQQYGVR--GFPTIKVFGAGKNSPQDYQGG 92

                         90
                 ....*....|
gi 727553193 442 kRDVDSLTSF 451
Cdd:cd03001   93 -RTAKAIVSA 101
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 371-453 4.61e-11

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 64.77  E-value: 4.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 371 LYAPWCPFCQAMEASFDELADKLNGNG-VKVAKFraDGDQKEFAKSELQLGSFPTILVFPKNSSRPIKYPSEkRDVDSLT 449
Cdd:PTZ00102 382 IYAPWCGHCKNLEPVYNELGEKYKDNDsIIVAKM--NGTANETPLEEFSWSAFPTILFVKAGERTPIPYEGE-RTVEGFK 458


                 ....
gi 727553193 450 SFLN 453
Cdd:PTZ00102 459 EFVN 462
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 369-452 1.23e-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: 58.06  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 369 VVLYAPWCPFCQAMEASFDELADKLN--GNGVKVAKfrADGDQKEFAKSELQLGSFPTILVFpKNSSRPIKYpSEKRDVD 446
Cdd:cd03005   21 VKFFAPWCGHCKRLAPTWEQLAKKFNneNPSVKIAK--VDCTQHRELCSEFQVRGYPTLLLF-KDGEKVDKY-KGTRDLD 96


                 ....*.
gi 727553193 447 SLTSFL 452
Cdd:cd03005   97 SLKEFV 102
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 345-428 1.75e-10

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


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 57.91  E-value: 1.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 345 NVVNLSRQGIENlmKLENRNEAWIVVLYAPWCPFCQAMEASFDELADKLNGNgVKVAKFRADgDQKEFAKsELQLGSFPT 424
Cdd:COG3118    1 AVVELTDENFEE--EVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGK-VKFVKVDVD-ENPELAA-QFGVRSIPT 75


                 ....
gi 727553193 425 ILVF 428
Cdd:COG3118   76 LLLF 79
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 360-455 2.75e-09

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: 54.38  E-value: 2.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 360 LENRNEA-WIVVLYAPWCPFCQAMEASFDELADKLNGNGVKVAKFRADGDQKEFAKSELQLGSFPTILVFPKNSSRPIKY 438
Cdd:cd03000   10 KDVRKEDiWLVDFYAPWCGHCKKLEPVWNEVGAELKSSGSPVRVGKLDATAYSSIASEFGVRGYPTIKLLKGDLAYNYRG 89

                         90
                 ....*....|....*..
gi 727553193 439 PSEKrdvDSLTSFLNLV 455
Cdd:cd03000   90 PRTK---DDIVEFANRV 103
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 367-453 7.24e-09

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: 53.01  E-value: 7.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  367 WIVV-LYAPWCPFCQAMEASFDELADKLNGNgVKVAKFRADgDQKEFAkSELQLGSFPTILVFpKNSSRPIKYpSEKRDV 445
Cdd:pfam00085  20 PVLVdFYAPWCGPCKMLAPEYEELAQEYKGN-VVFAKVDVD-ENPDLA-SKYGVRGYPTLIFF-KNGQPVDDY-VGARPK 94


                  ....*...
gi 727553193  446 DSLTSFLN 453
Cdd:pfam00085  95 DALAAFLK 102
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 341-452 3.33e-08

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 55.53  E-value: 3.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 341 FNSENVVNLSRQGIENLMKlenRNEAWIVVLYAPWCPFCQAMEASFDELADKLN--GNGVKVAKFRADGDQkEFAKsELQ 418
Cdd:PTZ00102  29 FISEHVTVLTDSTFDKFIT---ENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKekKSEIVLASVDATEEM-ELAQ-EFG 103

                         90       100       110
                 ....*....|....*....|....*....|....
gi 727553193 419 LGSFPTILVFpkNSSRPIKYPSeKRDVDSLTSFL 452
Cdd:PTZ00102 104 VRGYPTIKFF--NKGNPVNYSG-GRTADGIVSWI 134
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 360-430 6.94e-08

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: 50.44  E-value: 6.94e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727553193 360 LENRNEAWIVVLYAPWCPFCQAMEASFDELADKLNGNgVKVAKFRADGDQKEFAKSELQLGSFPTILVFPK 430
Cdd:cd03002   14 VHNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKELDGL-VQVAAVDCDEDKNKPLCGKYGVQGFPTLKVFRP 83
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 345-452 1.43e-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: 49.62  E-value: 1.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 345 NVVNLSRQGIENLMKlenRNEAWIVVLYAPWCPFCQAMEASFDELADKLNGNG------VKVAKFRADGDQKEFAKSElq 418
Cdd:cd02997    1 DVVHLTDEDFRKFLK---KEKHVLVMFYAPWCGHCKKMKPEFTKAATELKEDGkgvlaaVDCTKPEHDALKEEYNVKG-- 75

                         90       100       110
                 ....*....|....*....|....*....|....
gi 727553193 419 lgsFPTILVFpKNSSRPIKYPSEkRDVDSLTSFL 452
Cdd:cd02997   76 ---FPTFKYF-ENGKFVEKYEGE-RTAEDIIEFM 104
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 368-428 3.03e-07

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: 48.32  E-value: 3.03e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727553193 368 IVVLYAPWCPFCQAMEASFDELADKlnGNGVKVAKFRADgDQKEFAKsELQLGSFPTILVF 428
Cdd:cd02947   14 VVDFWAPWCGPCKAIAPVLEELAEE--YPKVKFVKVDVD-ENPELAE-EYGVRSIPTFLFF 70
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 367-451 4.33e-07

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 50.78  E-value: 4.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 367 WIVVLYAPWCPFCQAMEASFDELADKLNGNgVKVAKF---RADGDQKEFakselQLGSFPTILVFPKnsSRPIKYPSEKR 443
Cdd:PTZ00443  55 WFVKFYAPWCSHCRKMAPAWERLAKALKGQ-VNVADLdatRALNLAKRF-----AIKGYPTLLLFDK--GKMYQYEGGDR 126


                 ....*...
gi 727553193 444 DVDSLTSF 451
Cdd:PTZ00443 127 STEKLAAF 134
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 367-402 4.61e-07

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: 47.76  E-value: 4.61e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 727553193 367 WIVVLYAPWCPFCQAMEASFDELADKLNGNGVKVAK 402
Cdd:cd02994   19 WMIEFYAPWCPACQQLQPEWEEFADWSDDLGINVAK 54
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 368-428 7.83e-07

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: 46.54  E-value: 7.83e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727553193 368 IVVLYAPWCPFCQAMEASFDELADKLngNGVKVAKFRADGDQKEF-AKSELQLGSFPTILVF 428
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELALLN--KGVKFEAVDVDEDPALEkELKRYGVGGVPTLVVF 60
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 344-453 1.25e-06

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: 50.44  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  344 ENVVNLSRqgiENLMKLENRNEAWIVVLYAPWCPFCQAMEASFDELADKL--NGNGVKVAKFRADgDQKEFAkSELQLGS 421
Cdd:TIGR01130   1 EDVLVLTK---DNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELkkKGPPIKLAKVDAT-EEKDLA-QKYGVSG 75

                          90       100       110
                  ....*....|....*....|....*....|..
gi 727553193  422 FPTILVFPKNSSRPIKYpSEKRDVDSLTSFLN 453
Cdd:TIGR01130  76 YPTLKIFRNGEDSVSDY-NGPRDADGIVKYMK 106
PRK13794 PRK13794
hypothetical protein; Provisional
 80-287 3.65e-06

hypothetical protein; Provisional


Pssm-ID: 237509 [Multi-domain]  Cd Length: 479  Bit Score: 49.28  E-value: 3.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  80 VEDFEELAKRLEKASpLEIMDKALEKFGNDIAIAFSGAED--VALIEYAHLTGRPYRVFSLDTGRLNPETYRLFDTVEKH 157
Cdd:PRK13794 221 VEANKNVLDKYERNS-IGFIRNTAEKINKPVTVAYSGGKDslATLLLALKALGINFPVLFNDTGLEFPETLENVEDVEKH 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 158 YGIRIeymfpdavevqalVRNKGLfSFYEDGHQE---------CCRIRKVRPLRRAL-----KGLRAWItGQRKDQSpGT 223
Cdd:PRK13794 300 YGLEI-------------IRTKSE-EFWEKLEEYgppardnrwCSEVCKLEPLGKLIdekyeGECLSFV-GQRKYES-FN 363

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727553193 224 RSEIPVVQVDPVFEGLDGGAgslvkwnPVANVEGNDVWNFLRTMDVPVNTLHAAGYVSIGCEPC 287
Cdd:PRK13794 364 RSKKPRIWRNPYIKKQILAA-------PILHWTAMHVWIYLFREKAPYNKLYEQGFDRIGCFMC 420
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 368-430 5.08e-06

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: 44.97  E-value: 5.08e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727553193  368 IVVLYAPWCPFCQAMEASFDELADKLNGnGVKVAKFRADGDQKEFAKSELQlgSFPTILVFPK 430
Cdd:TIGR01068  18 LVDFWAPWCGPCKMIAPILEELAKEYEG-KVKFVKLNVDENPDIAAKYGIR--SIPTLLLFKN 77
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 96-283 5.45e-06

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: 46.75  E-value: 5.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  96 LEIMDKALEKFGND-IAIAFSGAED-VALIeyaHLTgrpYRVFsldtGRLNPETYRLFDTVekhYgIRIEYMFPdavEVQ 173
Cdd:cd23948    6 LEVIEEALDKYGPEeIAISFNGGKDcTVLL---HLL---RAAL----KRKYPSPLTPLKAL---Y-IKSPDPFP---EVE 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 174 ALVrnkglfsfyedghQECCR------IRKVRPLRRALKGL-------RAWITGQRKDqSPGTRSEIPVVQVDPvfegld 240
Cdd:cd23948   69 EFV-------------EDTAKrynldlITIDGPMKEGLEELlkehpiiKAVFMGTRRT-DPHGENLKPFSPTDP------ 128

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 727553193 241 ggagslvKW------NPVANVEGNDVWNFLRTMDVPVNTLHAAGYVSIG 283
Cdd:cd23948  129 -------GWpqfmrvNPILDWSYHDVWEFLRTLNLPYCSLYDQGYTSLG 170
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 358-451 7.48e-06

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: 44.66  E-value: 7.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 358 MKLENRNEAWIVVLYAPWCPFCQAMEASFDELADKLngNGVKVAKFRADgDQKEFAKSELQLGSFPTILVFpkNSSRPIK 437
Cdd:cd02999   12 LMAFNREDYTAVLFYASWCPFSASFRPHFNALSSMF--PQIRHLAIEES-SIKPSLLSRYGVVGFPTILLF--NSTPRVR 86

                         90
                 ....*....|....
gi 727553193 438 YpSEKRDVDSLTSF 451
Cdd:cd02999   87 Y-NGTRTLDSLAAF 99
PRK13795 PRK13795
hypothetical protein; Provisional
 76-287 1.05e-05

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 48.07  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  76 DVVEVEDfEELAKRLEKAspLEIMDKALEKFGNDIAIAFSGAED--VALieyaHLT---GRPYRVFSLDTGRLNPETYRL 150
Cdd:PRK13795 215 DAIEANR-KHLEEKEKEA--VNFIRGVAEKYNLPVSVSFSGGKDslVVL----DLAreaLKDFKAFFNNTGLEFPETVEN 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 151 FDTVEKHYGIRIEYM-----FPDAVEVqalvrnkglFSFYEDGHQECCRIRKVRPLRRALK--GLRAWIT--GQRKDQSp 221
Cdd:PRK13795 288 VKEVAEEYGIELIEAdagdaFWRAVEK---------FGPPARDYRWCCKVCKLGPITRAIKenFPKGCLTfvGQRKYES- 357

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727553193 222 GTRSEIPVVQVDPvFEGLDGGAGSLVKWNPVanvegnDVWNFLRTMDVPVNTLHAAGYVSIGCEPC 287
Cdd:PRK13795 358 FSRAKSPRVWRNP-WVPNQIGASPIQDWTAL------EVWLYIFWRKLPYNPLYERGFDRIGCWLC 416
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 345-452 1.73e-05

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: 43.53  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 345 NVVNLSRQGIENLMkleNRNEAWIVVLYAPWCPFCQAMEASFDELADKLNG---NGVKVAKFRADGDQKEFAKSELQLGS 421
Cdd:cd02996    2 EIVSLTSGNIDDIL---QSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEefpDAGKVVWGKVDCDKESDIADRYRINK 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 727553193 422 FPTILVFpKNSSRPIKYPSEKRDVDSLTSFL 452
Cdd:cd02996   79 YPTLKLF-RNGMMMKREYRGQRSVEALAEFV 108
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
368-431 2.04e-05

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 43.18  E-value: 2.04e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727553193  368 IVVLYAPWCPFCQAMEA---SFDELADKLNGNGVKVAK-----------FRADGDQKEFAKsELQLGSFPTILVFPKN 431
Cdd:pfam13098   8 LVVFTDPDCPYCKKLKKellEDPDVTVYLGPNFVFIAVniwcakevakaFTDILENKELGR-KYGVRGTPTIVFFDGK 84
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 346-451 2.56e-05

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: 42.90  E-value: 2.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 346 VVNLSRQGIENLMkleNRNEAWIVVLYAPWCPFCQAMEASFDELADKLNGNgVKVAKFRAdGDQKEFAKSElQLGSFPTI 425
Cdd:cd03003    3 IVTLDRGDFDAAV---NSGEIWFVNFYSPRCSHCHDLAPTWREFAKEMDGV-IRIGAVNC-GDDRMLCRSQ-GVNSYPSL 76

                         90       100
                 ....*....|....*....|....*.
gi 727553193 426 LVFPkNSSRPIKYPSEkRDVDSLTSF 451
Cdd:cd03003   77 YVFP-SGMNPEKYYGD-RSKESLVKF 100
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 361-431 3.13e-05

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 43.53  E-value: 3.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 361 ENRNEAWIVVLYAPWCPFCQAMEASFDELADKLNG----------NGVKVAKFRADG--------DQKEFAKSELQLGSF 422
Cdd:COG0526   25 DLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYGGvvfvgvdvdeNPEAVKAFLKELglpypvllDPDGELAKAYGVRGI 104


                 ....*....
gi 727553193 423 PTILVFPKN 431
Cdd:COG0526  105 PTTVLIDKD 113
TMX2 cd02962
TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related ...
 343-456 6.52e-05

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: 43.14  E-value: 6.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 343 SENVVNLSRQGIENLMKlENRNEAWIVVLYAPWCPFCQAMEASFDELADKLNGNGVKVAKF---RADGDQKEFAKSELQL 419
Cdd:cd02962   27 PEHIKYFTPKTLEEELE-RDKRVTWLVEFFTTWSPECVNFAPVFAELSLKYNNNNLKFGKIdigRFPNVAEKFRVSTSPL 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 727553193 420 GS-FPTILVFPKN---SSRPIKYPSEKRDVDSLTSFLNLVR 456
Cdd:cd02962  106 SKqLPTIILFQGGkevARRPYYNDSKGRAVPFTFSKENVIR 146
Sulfate_adenylyltransferase_2 cd23946
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ...
 88-277 8.81e-05

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: 43.64  E-value: 8.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  88 KRLEkASPLEIMDKALEKFGNdIAIAFSGAEDVA----LIEYAHLTGR-PYRVFSLDTGRLNPETYRLFDTVEKHYGIR- 161
Cdd:cd23946    3 RQLE-AESIHIIREVAAEFSN-PVMLYSIGKDSSvmlhLARKAFYPGKpPFPLLHVDTTWKFREMIEFRDRVAKEYGLDl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 162 IEYMFPDAVEvqalvrnKGLFSFYEdGHQECCRIRKVRPLRRALK--GLRAWITGQRKDQSpGTRSEIPVVQVDPVFEGL 239
Cdd:cd23946   81 IVHVNPDGVE-------AGINPFTH-GSAKHTDIMKTEGLKQALDkyGFDAAFGGARRDEE-KSRAKERVYSFRDSNHRW 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 727553193 240 DG---------------GAGSLVKWNPVANVEGNDVWNFLRTMDVPVNTLHAA 277
Cdd:cd23946  152 DPknqrpelwnqyngrvKKGESIRVFPLSNWTELDIWQYIYLENIPIVPLYFA 204
PRK08557 PRK08557
hypothetical protein; Provisional
 59-291 1.59e-04

hypothetical protein; Provisional


Pssm-ID: 181465 [Multi-domain]  Cd Length: 417  Bit Score: 43.97  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193  59 LNVQSITKESMVASEKLDVVeVEDFEELAKRLEKASpLEIMDKALEKFGND---IAIAFSGAEDVALIEY-AHLTGRPYR 134
Cdd:PRK08557 132 IKIKDLSLKKELDFEKIEDY-LEKNKERIEKLEENS-LSILKDYIEKYKNKgyaINASFSGGKDSSVSTLlAKEVIPDLE 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 135 VFSLDTGRLNPETYRLFDTVEKHYGIRIEYMFPDavevqalvrnkglfSFYEDGHQE---------CCRIRKVRPLRRAL 205
Cdd:PRK08557 210 VIFIDTGLEYPETINYVKDFAKKYDLNLDTLDGD--------------NFWENLEKEgiptkdnrwCNSACKLMPLKEYL 275

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 206 KGLRAW-----ITGQRKDQSpGTRSEIPvvqvdpvFEGLDGGAGSLVKWNPVANVEGNDVWNFLRTMDVPVNTLHAAGYV 280
Cdd:PRK08557 276 KKKYGNkkvltIDGSRKYES-FTRANLD-------YERKSGFIDFQTNVFPILDWNSLDIWSYIYLNDILYNPLYDKGFE 347

                        250
                 ....*....|.
gi 727553193 281 SIGCEPCTRAV 291
Cdd:PRK08557 348 RIGCYLCPSAL 358
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 368-431 6.04e-04

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 39.89  E-value: 6.04e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727553193 368 IVVLYAPWCPFCQAMEASF---DELADKLNGNgVKVAKFRADGD------------QKEFAKsELQLGSFPTILVFPKN 431
Cdd:COG2143   44 LLFFESDWCPYCKKLHKEVfsdPEVAAYLKEN-FVVVQLDAEGDkevtdfdgetltEKELAR-KYGVRGTPTLVFFDAE 120
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
368-400 1.57e-03

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 38.69  E-value: 1.57e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 727553193 368 IVVLYAPWCPFCQAMEASFDELADKLNGNGVKV 400
Cdd:COG1225   25 VLYFYATWCPGCTAELPELRDLYEEFKDKGVEV 57
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 368-428 5.24e-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: 36.10  E-value: 5.24e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727553193 368 IVVLYAPWCPFCQAMEASFDELADKLNGNGVkVAKFRADgDQKEFAkSELQLGSFPTILVF 428
Cdd:cd02956   16 VVDFWAPRSPPSKELLPLLERLAEEYQGQFV-LAKVNCD-AQPQIA-QQFGVQALPTVYLF 73
PRK10996 PRK10996
thioredoxin 2; Provisional
 355-434 6.41e-03

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 36.97  E-value: 6.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727553193 355 ENLMKLENRNEAWIVVLYAPWCPFCQAMEASFDELADKLNGNgVKVAKFRADgDQKEFAkSELQLGSFPTILVFpKNSSR 434
Cdd:PRK10996  43 ETLDKLLQDDLPVVIDFWAPWCGPCRNFAPIFEDVAAERSGK-VRFVKVNTE-AERELS-ARFRIRSIPTIMIF-KNGQV 118
 
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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