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Conserved domains on  [gi|1247056359|ref|XP_022466794|]
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hypothetical protein KNAG_0K01850 [Huiozyma naganishii CBS 8797]

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 ...
 43-238 6.60e-52

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 cd23948:

Pssm-ID: 469708 [Multi-domain]  Cd Length: 179  Bit Score: 168.85  E-value: 6.60e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1247056359  43 FLEDIFTRWSPldGEISFSYNGGKDCQVLlllylgclweFFVVQAGKSQYalqfQLFPMHSLPSVFINLDETFPILYRFI 122
Cdd:cd23948     8 VIEEALDKYGP--EEIAISFNGGKDCTVL----------LHLLRAALKRK----YPSPLTPLKALYIKSPDPFPEVEEFV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1247056359 123 NESAARYHLELYEScpqcndgPCDMPSQFRRFLDGPGEgTRAIVIGVRYTDPFGDQLEPIQRTDSNWPDFVRLQPLLHWR 202
Cdd:cd23948    72 EDTAKRYNLDLITI-------DGPMKEGLEELLKEHPI-IKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWS 143

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1247056359 203 LSNVWSFLLYSGEPISELYKVGFTSIGSIEGTTPNP 238
Cdd:cd23948   144 YHDVWEFLRTLNLPYCSLYDQGYTSLGSVDNTLPNP 179
 
Name Accession Description Interval E-value
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 43-238 6.60e-52

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: 168.85  E-value: 6.60e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1247056359  43 FLEDIFTRWSPldGEISFSYNGGKDCQVLlllylgclweFFVVQAGKSQYalqfQLFPMHSLPSVFINLDETFPILYRFI 122
Cdd:cd23948     8 VIEEALDKYGP--EEIAISFNGGKDCTVL----------LHLLRAALKRK----YPSPLTPLKALYIKSPDPFPEVEEFV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1247056359 123 NESAARYHLELYEScpqcndgPCDMPSQFRRFLDGPGEgTRAIVIGVRYTDPFGDQLEPIQRTDSNWPDFVRLQPLLHWR 202
Cdd:cd23948    72 EDTAKRYNLDLITI-------DGPMKEGLEELLKEHPI-IKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWS 143

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1247056359 203 LSNVWSFLLYSGEPISELYKVGFTSIGSIEGTTPNP 238
Cdd:cd23948   144 YHDVWEFLRTLNLPYCSLYDQGYTSLGSVDNTLPNP 179
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 57-229 1.84e-23

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: 94.29  E-value: 1.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1247056359  57 EISFSYNGGKDCQVLLLLYLGCLWEFFVVqagksqyalqfqlfpmhslpsvFINLDETFPILYRFINESAARY--HLELY 134
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHLASKAFPPGPVI----------------------FIDTGYEFPETYEFVDELEEKYglNLKVY 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1247056359 135 ES--CPQCNDGPCDMPSQF-------------RRFLDGPGEgtRAIVIGVRYTDPFGDQLEPIQRTDSNWPDFVRLQPLL 199
Cdd:pfam01507  59 LPedSFAEGINPEGIPSSLyrrccrlrkveplKRALKELGF--DAWFTGLRRDESPSRAKLPIVSIDGDFPKVIKVFPLL 136

                         170       180       190
                  ....*....|....*....|....*....|
gi 1247056359 200 HWRLSNVWSFLLYSGEPISELYKVGFTSIG 229
Cdd:pfam01507 137 NWTETDVWQYILANNVPYNPLYDQGYRSIG 166
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 115-229 2.24e-05

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: 44.84  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1247056359 115 FPILYRFINESAARYHLELYESCPQ-------CNDGP----------CDM----PSqfRRFLDGpgEGTRAIVIGVRytd 173
Cdd:COG0175    71 FPETYEFRDRLAERLGLDLIVVRPEdafaeqlAEFGPplfyrdprwcCKIrkvePL--KRALAG--YDFDAWITGLR--- 143

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1247056359 174 pfGDQ-----LEPIQRTDSNwPDFVRLQPLLHWRLSNVWSFLLYSGEPISELYKVGFTSIG 229
Cdd:COG0175   144 --RDEsptraKEPVVEWDPV-GGLIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIG 201
 
Name Accession Description Interval E-value
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 43-238 6.60e-52

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: 168.85  E-value: 6.60e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1247056359  43 FLEDIFTRWSPldGEISFSYNGGKDCQVLlllylgclweFFVVQAGKSQYalqfQLFPMHSLPSVFINLDETFPILYRFI 122
Cdd:cd23948     8 VIEEALDKYGP--EEIAISFNGGKDCTVL----------LHLLRAALKRK----YPSPLTPLKALYIKSPDPFPEVEEFV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1247056359 123 NESAARYHLELYEScpqcndgPCDMPSQFRRFLDGPGEgTRAIVIGVRYTDPFGDQLEPIQRTDSNWPDFVRLQPLLHWR 202
Cdd:cd23948    72 EDTAKRYNLDLITI-------DGPMKEGLEELLKEHPI-IKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWS 143

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1247056359 203 LSNVWSFLLYSGEPISELYKVGFTSIGSIEGTTPNP 238
Cdd:cd23948   144 YHDVWEFLRTLNLPYCSLYDQGYTSLGSVDNTLPNP 179
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 57-229 1.84e-23

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: 94.29  E-value: 1.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1247056359  57 EISFSYNGGKDCQVLLLLYLGCLWEFFVVqagksqyalqfqlfpmhslpsvFINLDETFPILYRFINESAARY--HLELY 134
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHLASKAFPPGPVI----------------------FIDTGYEFPETYEFVDELEEKYglNLKVY 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1247056359 135 ES--CPQCNDGPCDMPSQF-------------RRFLDGPGEgtRAIVIGVRYTDPFGDQLEPIQRTDSNWPDFVRLQPLL 199
Cdd:pfam01507  59 LPedSFAEGINPEGIPSSLyrrccrlrkveplKRALKELGF--DAWFTGLRRDESPSRAKLPIVSIDGDFPKVIKVFPLL 136

                         170       180       190
                  ....*....|....*....|....*....|
gi 1247056359 200 HWRLSNVWSFLLYSGEPISELYKVGFTSIG 229
Cdd:pfam01507 137 NWTETDVWQYILANNVPYNPLYDQGYRSIG 166
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 115-229 2.24e-05

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: 44.84  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1247056359 115 FPILYRFINESAARYHLELYESCPQ-------CNDGP----------CDM----PSqfRRFLDGpgEGTRAIVIGVRytd 173
Cdd:COG0175    71 FPETYEFRDRLAERLGLDLIVVRPEdafaeqlAEFGPplfyrdprwcCKIrkvePL--KRALAG--YDFDAWITGLR--- 143

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1247056359 174 pfGDQ-----LEPIQRTDSNwPDFVRLQPLLHWRLSNVWSFLLYSGEPISELYKVGFTSIG 229
Cdd:COG0175   144 --RDEsptraKEPVVEWDPV-GGLIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIG 201
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 107-230 9.60e-03

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: 36.60  E-value: 9.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1247056359 107 VFINLDETFPILYRFINESAARYHLELYESCP---------------QCNDGPCDMPSQFR------------RFLDGPG 159
Cdd:cd23947    46 VFIDTGIEFPETIDFVEKLAETLGLDVEAARPplflewltsnfqpqwDPIWDNPPPPRDYRwccdelklepftKWLKEKK 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1247056359 160 EGTRAIVIGVRYTDPF----GDQLEPIQRTDSNW-PDFVRLQPLLHWRLSNVWSFLLYSGEPISELYKVGFTSIGS 230
Cdd:cd23947   126 PEGVLLLVGIRADESLnrakRPRVYRKYGWRNSTlPGQIVAYPIKDWSVEDVWLYILRHGLPYNPLYDLGFDRGGC 201
 
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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