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Conserved domains on  [gi|226722304|sp|B7GG21|]
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RecName: Full=Adenosine 5'-phosphosulfate reductase; Short=APS reductase; AltName: Full=5'-adenylylsulfate reductase; AltName: Full=Thioredoxin-dependent 5'-adenylylsulfate reductase

Protein Classification

adenine nucleotide alpha hydrolase family protein( domain architecture ID 188)

AANH (adenine nucleotide alpha hydrolase) family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AANH_superfamily super family cl00292
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase ...
 24-234 4.84e-107

Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase (AANH) superfamily includes N-type ATP PPases, ATP sulfurylases, universal stress response proteins (USPs), and electron transfer flavoproteins (ETFs). The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.


The actual alignment was detected with superfamily member TIGR00434:

Pssm-ID: 469708  Cd Length: 212  Bit Score: 307.48  E-value: 4.84e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304   24 ALHVLSWAYDHYSDDLLYACSFGIEGIVLIDLISQVRDDAEIVFLDTHLHFPETYETIERVKQAYPrLRIHLQTPSLSLA 103
Cdd:TIGR00434   1 AQEIIAWAYVTFGGHLVYSTSFGIQGAVLLDLVSKISPDIPVIFLDTGYHFPETYELIDELTERYP-LNIKVYKPDLSLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304  104 EQEKQFGAELWKTDPNKCCELRKIIPLRQAMTG--KKAWISGLRREQSPTRQHVEFINLDKKFQNIKVCPLIHWTWKDVW 181
Cdd:TIGR00434  80 EQAAKYGDKLWEQDPNKYDYLRKVEPMHRALKElhASAWFTGLRRDQGPSRANLSILNIDEKFGILKVLPLIDWTWKDVY 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 226722304  182 RYVHRHNLSYNPLHDRGYPSIGCAPCTAPAYTEEDLRSGRWAGLGKTECGLHE 234
Cdd:TIGR00434 160 QYIDAHNLPYNPLHDQGYPSIGDYHSTRPVKEGEDERAGRWKGKAKTECGLHE 212
 
Name Accession Description Interval E-value
cysH TIGR00434
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ...
 24-234 4.84e-107

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: 307.48  E-value: 4.84e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304   24 ALHVLSWAYDHYSDDLLYACSFGIEGIVLIDLISQVRDDAEIVFLDTHLHFPETYETIERVKQAYPrLRIHLQTPSLSLA 103
Cdd:TIGR00434   1 AQEIIAWAYVTFGGHLVYSTSFGIQGAVLLDLVSKISPDIPVIFLDTGYHFPETYELIDELTERYP-LNIKVYKPDLSLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304  104 EQEKQFGAELWKTDPNKCCELRKIIPLRQAMTG--KKAWISGLRREQSPTRQHVEFINLDKKFQNIKVCPLIHWTWKDVW 181
Cdd:TIGR00434  80 EQAAKYGDKLWEQDPNKYDYLRKVEPMHRALKElhASAWFTGLRRDQGPSRANLSILNIDEKFGILKVLPLIDWTWKDVY 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 226722304  182 RYVHRHNLSYNPLHDRGYPSIGCAPCTAPAYTEEDLRSGRWAGLGKTECGLHE 234
Cdd:TIGR00434 160 QYIDAHNLPYNPLHDQGYPSIGDYHSTRPVKEGEDERAGRWKGKAKTECGLHE 212
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 21-232 8.87e-96

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: 279.42  E-value: 8.87e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304  21 EKGALHVLSWAYDHYSDDLLYACSFGIEGIVLIDLISQVRDDAEIVFLDTHLHFPETYETIERVKQAYPrLRIHLQTPSL 100
Cdd:COG0175   18 EAEAIEILREAAAEFGGRVVVSSSGGKDSTVLLHLAAKFKPPIPVLFLDTGYEFPETYEFRDRLAERLG-LDLIVVRPED 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304 101 SLAEQEKQFGAELWKTDPNKCCELRKIIPLRQAMTGKK--AWISGLRREQSPTRQHVEFINLDKKFQNIKVCPLIHWTWK 178
Cdd:COG0175   97 AFAEQLAEFGPPLFYRDPRWCCKIRKVEPLKRALAGYDfdAWITGLRRDESPTRAKEPVVEWDPVGGLIKVNPLADWTEL 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 226722304 179 DVWRYVHRHNLSYNPLHDRGYPSIGCAPCTAPAYTEEDLRSGRWAGLGK--TECGL 232
Cdd:COG0175  177 DVWAYIRREDLPYNPLYDQGYPSIGCAPCTRAVESGEDERAGRWWDEEKerKECGL 232
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
24-235 9.83e-96

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 279.80  E-value: 9.83e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304  24 ALHVLSWAYDHYSDDLLYACSFGIEGIVLIDLISQVRDDAEIVFLDTHLHFPETYETIERVKQAYpRLRIHLQTPSLSLA 103
Cdd:PRK02090  28 AQERLAWALENFGGRLALVSSFGAEDAVLLHLVAQVDPDIPVIFLDTGYLFPETYRFIDELTERL-LLNLKVYRPDASAA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304 104 EQEKQFGaELWK---TDPNKCCELRKIIPLRQAMTGKKAWISGLRREQSPTRQHVEFINLDKKFqnIKVCPLIHWTWKDV 180
Cdd:PRK02090 107 EQEARYG-GLWEqsvEDRDECCRIRKVEPLNRALAGLDAWITGLRREQSGTRANLPVLEIDGGR--FKINPLADWTNEDV 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 226722304 181 WRYVHRHNLSYNPLHDRGYPSIGCAPCTAPAYTEEDLRSGRWAGLGKTECGLHES 235
Cdd:PRK02090 184 WAYLKEHDLPYHPLVDQGYPSIGCEPCTRPVEPGEDERAGRWWGGLKKECGLHEG 238
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 24-203 2.59e-73

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: 220.55  E-value: 2.59e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304  24 ALHVLSWAYDHYSDDLLYACSFGIEGIVLIDLISQVRDDAEIVFLDTHLHFPETYETIERVKQAYPrLRIHLQTPSLSLA 103
Cdd:cd23945    1 PLEILLWAAEEFGPKLVFATSFGAEDAVILDLLSKVRPDIPVVFLDTGYLFPETYDLIDEVEARYG-LNIEVYFPEGTEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304 104 EQE--KQFGAELWKTDPNK--CCELRKIIPLRQAMTGKKAWISGLRREQSPTRQHVEFINLDKKFQNIKVCPLIHWTWKD 179
Cdd:cd23945   80 EEEalEGGLNEFYLEDEERydCCRKRKPFPLALALLGVKAWITGRRRDQSPTRANLPIVEVDEEGGLVKINPLADWTWED 159

                        170       180
                 ....*....|....*....|....
gi 226722304 180 VWRYVHRHNLSYNPLHDRGYPSIG 203
Cdd:cd23945  160 VWAYIREHDLPYNPLHDQGYPSIG 183
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 39-210 6.60e-65

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: 199.06  E-value: 6.60e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304   39 LLYACSFGIEGIVLIDLISQVRDDAEIVFLDTHLHFPETYETIERVKQAYPrLRIHLQTPSLSLAEQEKQFGAELWktDP 118
Cdd:pfam01507   2 LVVSFSGGKDSLVLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYG-LNLKVYLPEDSFAEGINPEGIPSS--LY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304  119 NKCCELRKIIPLRQAM--TGKKAWISGLRREQSPTRQHVEFINLDKKFQN-IKVCPLIHWTWKDVWRYVHRHNLSYNPLH 195
Cdd:pfam01507  79 RRCCRLRKVEPLKRALkeLGFDAWFTGLRRDESPSRAKLPIVSIDGDFPKvIKVFPLLNWTETDVWQYILANNVPYNPLY 158

                         170
                  ....*....|....*
gi 226722304  196 DRGYPSIGCAPCTAP 210
Cdd:pfam01507 159 DQGYRSIGCYPCTGP 173
 
Name Accession Description Interval E-value
cysH TIGR00434
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ...
 24-234 4.84e-107

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: 307.48  E-value: 4.84e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304   24 ALHVLSWAYDHYSDDLLYACSFGIEGIVLIDLISQVRDDAEIVFLDTHLHFPETYETIERVKQAYPrLRIHLQTPSLSLA 103
Cdd:TIGR00434   1 AQEIIAWAYVTFGGHLVYSTSFGIQGAVLLDLVSKISPDIPVIFLDTGYHFPETYELIDELTERYP-LNIKVYKPDLSLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304  104 EQEKQFGAELWKTDPNKCCELRKIIPLRQAMTG--KKAWISGLRREQSPTRQHVEFINLDKKFQNIKVCPLIHWTWKDVW 181
Cdd:TIGR00434  80 EQAAKYGDKLWEQDPNKYDYLRKVEPMHRALKElhASAWFTGLRRDQGPSRANLSILNIDEKFGILKVLPLIDWTWKDVY 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 226722304  182 RYVHRHNLSYNPLHDRGYPSIGCAPCTAPAYTEEDLRSGRWAGLGKTECGLHE 234
Cdd:TIGR00434 160 QYIDAHNLPYNPLHDQGYPSIGDYHSTRPVKEGEDERAGRWKGKAKTECGLHE 212
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 21-232 8.87e-96

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: 279.42  E-value: 8.87e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304  21 EKGALHVLSWAYDHYSDDLLYACSFGIEGIVLIDLISQVRDDAEIVFLDTHLHFPETYETIERVKQAYPrLRIHLQTPSL 100
Cdd:COG0175   18 EAEAIEILREAAAEFGGRVVVSSSGGKDSTVLLHLAAKFKPPIPVLFLDTGYEFPETYEFRDRLAERLG-LDLIVVRPED 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304 101 SLAEQEKQFGAELWKTDPNKCCELRKIIPLRQAMTGKK--AWISGLRREQSPTRQHVEFINLDKKFQNIKVCPLIHWTWK 178
Cdd:COG0175   97 AFAEQLAEFGPPLFYRDPRWCCKIRKVEPLKRALAGYDfdAWITGLRRDESPTRAKEPVVEWDPVGGLIKVNPLADWTEL 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 226722304 179 DVWRYVHRHNLSYNPLHDRGYPSIGCAPCTAPAYTEEDLRSGRWAGLGK--TECGL 232
Cdd:COG0175  177 DVWAYIRREDLPYNPLYDQGYPSIGCAPCTRAVESGEDERAGRWWDEEKerKECGL 232
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
24-235 9.83e-96

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 279.80  E-value: 9.83e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304  24 ALHVLSWAYDHYSDDLLYACSFGIEGIVLIDLISQVRDDAEIVFLDTHLHFPETYETIERVKQAYpRLRIHLQTPSLSLA 103
Cdd:PRK02090  28 AQERLAWALENFGGRLALVSSFGAEDAVLLHLVAQVDPDIPVIFLDTGYLFPETYRFIDELTERL-LLNLKVYRPDASAA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304 104 EQEKQFGaELWK---TDPNKCCELRKIIPLRQAMTGKKAWISGLRREQSPTRQHVEFINLDKKFqnIKVCPLIHWTWKDV 180
Cdd:PRK02090 107 EQEARYG-GLWEqsvEDRDECCRIRKVEPLNRALAGLDAWITGLRREQSGTRANLPVLEIDGGR--FKINPLADWTNEDV 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 226722304 181 WRYVHRHNLSYNPLHDRGYPSIGCAPCTAPAYTEEDLRSGRWAGLGKTECGLHES 235
Cdd:PRK02090 184 WAYLKEHDLPYHPLVDQGYPSIGCEPCTRPVEPGEDERAGRWWGGLKKECGLHEG 238
APS_reductase TIGR02055
thioredoxin-dependent adenylylsulfate APS reductase; This model describes recently identified ...
 45-232 2.15e-90

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: 264.32  E-value: 2.15e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304   45 FGIEGIVLIDLISQVRDDAEIVFLDTHLHFPETYETIERVKQAYPRLRIHLQTPSLSLAEQEKQFGAELW-KTDPNKCCE 123
Cdd:TIGR02055   1 LGAEDVVLVDLAAKVRPDVKVFFLDTGRLFKETYETIDQVRERYDILIDVLSPPPLTVEEQVKEYGLNLFyRSVPHECCG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304  124 LRKIIPLRQAMTGKKAWISGLRREQSPTRQHVEFINLDKKFQNIKVCPLIHWTWKDVWRYVHRHNLSYNPLHDRGYPSIG 203
Cdd:TIGR02055  81 IRKVEPLKRALAGVSAWITGLRRDQSPTRAQAPFLEIDEAFGLVKINPLADWTSEDVWEYIADNELPYNPLHDRGYPSIG 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 226722304  204 CAPCTAPAYTEEDLRSGRWAGL--GKTECGL 232
Cdd:TIGR02055 161 CEPCTRPVAPGEDPRAGRWWWEeaAKKECGL 191
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 24-203 2.59e-73

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: 220.55  E-value: 2.59e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304  24 ALHVLSWAYDHYSDDLLYACSFGIEGIVLIDLISQVRDDAEIVFLDTHLHFPETYETIERVKQAYPrLRIHLQTPSLSLA 103
Cdd:cd23945    1 PLEILLWAAEEFGPKLVFATSFGAEDAVILDLLSKVRPDIPVVFLDTGYLFPETYDLIDEVEARYG-LNIEVYFPEGTEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304 104 EQE--KQFGAELWKTDPNK--CCELRKIIPLRQAMTGKKAWISGLRREQSPTRQHVEFINLDKKFQNIKVCPLIHWTWKD 179
Cdd:cd23945   80 EEEalEGGLNEFYLEDEERydCCRKRKPFPLALALLGVKAWITGRRRDQSPTRANLPIVEVDEEGGLVKINPLADWTWED 159

                        170       180
                 ....*....|....*....|....
gi 226722304 180 VWRYVHRHNLSYNPLHDRGYPSIG 203
Cdd:cd23945  160 VWAYIREHDLPYNPLHDQGYPSIG 183
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 39-210 6.60e-65

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: 199.06  E-value: 6.60e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304   39 LLYACSFGIEGIVLIDLISQVRDDAEIVFLDTHLHFPETYETIERVKQAYPrLRIHLQTPSLSLAEQEKQFGAELWktDP 118
Cdd:pfam01507   2 LVVSFSGGKDSLVLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYG-LNLKVYLPEDSFAEGINPEGIPSS--LY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304  119 NKCCELRKIIPLRQAM--TGKKAWISGLRREQSPTRQHVEFINLDKKFQN-IKVCPLIHWTWKDVWRYVHRHNLSYNPLH 195
Cdd:pfam01507  79 RRCCRLRKVEPLKRALkeLGFDAWFTGLRRDESPSRAKLPIVSIDGDFPKvIKVFPLLNWTETDVWQYILANNVPYNPLY 158

                         170
                  ....*....|....*
gi 226722304  196 DRGYPSIGCAPCTAP 210
Cdd:pfam01507 159 DQGYRSIGCYPCTGP 173
PAPS_reductase TIGR02057
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ...
 27-233 1.02e-54

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: 175.02  E-value: 1.02e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304   27 VLSWAYDHYSDDLLYACSFGIEGIVLIDLISQVRD-DAEIVFLDTHLHFPETYETIERVKQAYpRLRIHLQTP--SLSLA 103
Cdd:TIGR02057  16 IIAWSIVTFPHGLVQTSAFGIQALVTLHLLSSISEpMIPVIFIDTLYHFPQTLTLKDELTKKY-YQTLNLYKYdgCESEA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304  104 EQEKQFGAELWKTDPNKCCELRKIIPLRQAMT--GKKAWISGLRREQSPTRQHVEFINLDKKFQNIKVCPLIHWTWKDVW 181
Cdd:TIGR02057  95 DFEAKYGKLLWQKDIEKYDYIAKVEPMQRALKelNASAWFTGRRRDQGSARANLPVIEIDEQNGILKVNPLIDWTFEQVY 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 226722304  182 RYVHRHNLSYNPLHDRGYPSIGCAPCTAPAYTEEDLRSGRWAGLGKTECGLH 233
Cdd:TIGR02057 175 QYLDAHNVPYNPLLDQGYRSIGDYHSTRKVKEGEDERAGRWKGKLKTECGIH 226
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 25-234 2.15e-33

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: 125.13  E-value: 2.15e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304   25 LHVLSWAYDHYSDDLLYACSfGIEGIVLIDLISQVRDDAEIVFLDTHLHFPETYETIERVKQAYPrLRIHLQTPSL---- 100
Cdd:TIGR00424 104 LEIMDKALEKFGNDIAIAFS-GAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRFFDAVEKQYG-IRIEYMFPDAvevq 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304  101 SLAEQEKQFgaELWKTDPNKCCELRKIIPLRQAMTGKKAWISGLRREQSP-TRQHVEFINLDKKFQNIK--VCPLIHWT- 176
Cdd:TIGR00424 182 ALVRSKGLF--SFYEDGHQECCRVRKVRPLRRALKGLKAWITGQRKDQSPgTRSEIPVVQVDPVFEGLDggVGSLVKWNp 259

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226722304  177 -----WKDVWRYVHRHNLSYNPLHDRGYPSIGCAPCTAPAYTEEDLRSGR--WAGLGKTECGLHE 234
Cdd:TIGR00424 260 vanveGKDVWNFLRTMDVPVNTLHAQGYVSIGCEPCTRPVLPGQHEREGRwwWEDAKAKECGLHK 324
PLN02309 PLN02309
5'-adenylylsulfate reductase
 25-233 1.19e-30

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 117.58  E-value: 1.19e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304  25 LHVLSWAYDHYSDDLLYACSfGIEGIVLIDLISQVRDDAEIVFLDTHLHFPETYETIERVKQAYpRLRIHLQTP-SLSLA 103
Cdd:PLN02309  99 LEIMDKALEKFGNDIAIAFS-GAEDVALIEYAHLTGRPFRVFSLDTGRLNPETYRLFDAVEKHY-GIRIEYMFPdAVEVQ 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304 104 EQEKQFGAELWKTDPNK-CCELRKIIPLRQAMTGKKAWISGLRREQSP-TRQHVEFINLDKKFQN--------IKVCPLI 173
Cdd:PLN02309 177 ALVRNKGLFSFYEDGHQeCCRVRKVRPLRRALKGLRAWITGQRKDQSPgTRAEVPVVQVDPVFEGldggpgslVKWNPLA 256

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226722304 174 HWTWKDVWRYVHRHNLSYNPLHDRGYPSIGCAPCTAPAYTEEDLRSGRW---AGLGKtECGLH 233
Cdd:PLN02309 257 NVTGNEVWNFLRTMDVPVNSLHAQGYVSIGCEPCTRPVLPGQHEREGRWwweDAKAK-ECGLH 318
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 53-207 2.20e-17

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: 77.43  E-value: 2.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304  53 IDLISQVRDDAEIVFLDTHLHFPETYETIERVKQAYprlRIHLQTPSLSLAEQEKQFGAELWKTDPNK----------CC 122
Cdd:cd23947   33 LEALRRLRKDVYVVFIDTGIEFPETIDFVEKLAETL---GLDVEAARPPLFLEWLTSNFQPQWDPIWDnpppprdyrwCC 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304 123 ELRKIIPLRQA-----------MTGKKAWISgLRREQSPTRQHVEFINLDKKFQNIKVCPLIHWTWKDVWRYVHRHNLSY 191
Cdd:cd23947  110 DELKLEPFTKWlkekkpegvllLVGIRADES-LNRAKRPRVYRKYGWRNSTLPGQIVAYPIKDWSVEDVWLYILRHGLPY 188

                        170
                 ....*....|....*.
gi 226722304 192 NPLHDRGYPSIGCAPC 207
Cdd:cd23947  189 NPLYDLGFDRGGCLVC 204
PRK13794 PRK13794
hypothetical protein; Provisional
 64-209 8.45e-15

hypothetical protein; Provisional


Pssm-ID: 237509 [Multi-domain]  Cd Length: 479  Bit Score: 72.78  E-value: 8.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304  64 EIVFLDTHLHFPETYETIERVKQAYpRLRIhLQTPSLSLAEQEKQFGAElwKTDPNKCCELRKIIPLRQAMTGK--KAWI 141
Cdd:PRK13794 276 PVLFNDTGLEFPETLENVEDVEKHY-GLEI-IRTKSEEFWEKLEEYGPP--ARDNRWCSEVCKLEPLGKLIDEKyeGECL 351

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226722304 142 S--GLRREQSPTRQHVEFI--NLDKKFQnIKVCPLIHWTWKDVWRYVHRHNLSYNPLHDRGYPSIGCAPCTA 209
Cdd:PRK13794 352 SfvGQRKYESFNRSKKPRIwrNPYIKKQ-ILAAPILHWTAMHVWIYLFREKAPYNKLYEQGFDRIGCFMCPA 422
PRK08557 PRK08557
hypothetical protein; Provisional
 55-218 1.22e-14

hypothetical protein; Provisional


Pssm-ID: 181465 [Multi-domain]  Cd Length: 417  Bit Score: 72.09  E-value: 1.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304  55 LISQVRDDAEIVFLDTHLHFPETyetIERVKQAYPRLRIHLQTPslslaeQEKQFGAELWK----TDPNKCC-ELRKIIP 129
Cdd:PRK08557 200 LAKEVIPDLEVIFIDTGLEYPET---INYVKDFAKKYDLNLDTL------DGDNFWENLEKegipTKDNRWCnSACKLMP 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304 130 LRQAM----TGKKAW-ISGLRREQSPTRQHVE------FINldkkFQnIKVCPLIHWTWKDVWRYVHRHNLSYNPLHDRG 198
Cdd:PRK08557 271 LKEYLkkkyGNKKVLtIDGSRKYESFTRANLDyerksgFID----FQ-TNVFPILDWNSLDIWSYIYLNDILYNPLYDKG 345

                        170       180
                 ....*....|....*....|
gi 226722304 199 YPSIGCAPCTApAYTEEDLR 218
Cdd:PRK08557 346 FERIGCYLCPS-ALNSEFLR 364
PRK13795 PRK13795
hypothetical protein; Provisional
 51-209 2.15e-14

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 71.95  E-value: 2.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304  51 VLIDLISQVRDDAEIVFLDTHLHFPETYETIERVKQAYprlRIHLQTPSLSLA--EQEKQFGAelwktdPNK----CCEL 124
Cdd:PRK13795 258 VVLDLAREALKDFKAFFNNTGLEFPETVENVKEVAEEY---GIELIEADAGDAfwRAVEKFGP------PARdyrwCCKV 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304 125 RKIIPLRQAM--TGKKAWIS--GLRREQSPTRQHVEFINLDKKFQN-IKVCPLIHWTWKDVWRYVHRHNLSYNPLHDRGY 199
Cdd:PRK13795 329 CKLGPITRAIkeNFPKGCLTfvGQRKYESFSRAKSPRVWRNPWVPNqIGASPIQDWTALEVWLYIFWRKLPYNPLYERGF 408

                        170
                 ....*....|
gi 226722304 200 PSIGCAPCTA 209
Cdd:PRK13795 409 DRIGCWLCPS 418
PRK05253 PRK05253
sulfate adenylyltransferase subunit CysD;
69-210 1.62e-09

sulfate adenylyltransferase subunit CysD;


Pssm-ID: 235375  Cd Length: 301  Bit Score: 56.68  E-value: 1.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304  69 DTHLHFPETYETI-ERVKQAYPRLRIHlqtpslSLAEQEKQfGAELWKTDPNKCCELRKIIPLRQAMTGKK--AWISGLR 145
Cdd:PRK05253  64 DTGWKFPEMIEFRdRRAKELGLELIVH------SNPEGIAR-GINPFRHGSAKHTNAMKTEGLKQALEKYGfdAAFGGAR 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304 146 R--EQS-----------------PTRQHVEFINLDK----KFQNIKVCPLIHWTWKDVWRYVHRHNLSYNPL---HDRG- 198
Cdd:PRK05253 137 RdeEKSrakerifsfrdefgqwdPKNQRPELWNLYNgrinKGEHIRVFPLSNWTELDIWQYIERENIPIVPLyfaHERPv 216

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 226722304 199 ----------------------------YPSIGCAPCTAP 210
Cdd:PRK05253 217 verdgmlimvddrmplrpgevveermvrFRTLGCYPCTGA 256
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 169-203 1.21e-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: 52.91  E-value: 1.21e-08
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 226722304 169 VCPLIHWTWKDVWRYVHRHNLSYNPLHDRGYPSIG 203
Cdd:cd23948  136 VNPILDWSYHDVWEFLRTLNLPYCSLYDQGYTSLG 170
Sulfate_adenylyltransferase_2 cd23946
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ...
 21-195 7.47e-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: 48.26  E-value: 7.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304  21 EKGALHVLSWAYDHYSDD-LLYacSFGIEGIVLIDLISQVRDDAEIVF----LDTHLHFPETYETIERVKQAYP-RLRIH 94
Cdd:cd23946    6 EAESIHIIREVAAEFSNPvMLY--SIGKDSSVMLHLARKAFYPGKPPFpllhVDTTWKFREMIEFRDRVAKEYGlDLIVH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304  95 LQTPSLSLaeqekqfGAELWKTDPNKCCELRKIIPLRQAMT--GKKAWISGLRREQS-------------------PTRQ 153
Cdd:cd23946   84 VNPDGVEA-------GINPFTHGSAKHTDIMKTEGLKQALDkyGFDAAFGGARRDEEksrakervysfrdsnhrwdPKNQ 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 226722304 154 HVEFINL----DKKFQNIKVCPLIHWTWKDVWRYVHRHNLSYNPLH 195
Cdd:cd23946  157 RPELWNQyngrVKKGESIRVFPLSNWTELDIWQYIYLENIPIVPLY 202
PRK08576 PRK08576
hypothetical protein; Provisional
 55-217 4.73e-06

hypothetical protein; Provisional


Pssm-ID: 236300 [Multi-domain]  Cd Length: 438  Bit Score: 46.61  E-value: 4.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304  55 LISQVRDDAEIVFLDTHLHFPETYETIERVKQaypRLRIHLQTPSLSLAEQEKQFGAelwKTDPNKCCELRKIIPLRQA- 133
Cdd:PRK08576 253 LAKKAFGDVTAVYVDTGYEMPLTDEYVEKVAE---KLGVDLIRAGVDVPMPIEKYGM---PTHSNRWCTKLKVEALEEAi 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226722304 134 --------MTGKKAWISGLRREQSPTRQHVEfinldKKFQNIKVCPLIHWTWKDVWRYVHRHNLSYNPLHDRGYPSIGCA 205
Cdd:PRK08576 327 reledgllVVGDRDGESARRRLRPPVVERKT-----NFGKILVVMPIKFWSGAMVQLYILMNGLELNPLYYKGFYRLGCY 401

                        170
                 ....*....|..
gi 226722304 206 PCTAPAYTEEDL 217
Cdd:PRK08576 402 ICPSLRSWEIEL 413
PRK12563 PRK12563
sulfate adenylyltransferase subunit CysD;
138-195 2.43e-03

sulfate adenylyltransferase subunit CysD;


Pssm-ID: 237138  Cd Length: 312  Bit Score: 38.23  E-value: 2.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226722304 138 KAWISGLRREQ---SPTRQHVEFINL----DKKFQNIKVCPLIHWTWKDVWRYVHRHNLSYNPLH 195
Cdd:PRK12563 155 KERIFSFRSAFhrwDPKAQRPELWSLynarLRRGESLRVFPLSNWTELDVWQYIAREKIPLVPLY 219
 
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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