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Conserved domains on  [gi|1565982447|gb|RXX53170|]
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NADPH-dependent 7-cyano-7-deazaguanine reductase QueF [Enterobacter cloacae]

Protein Classification

NADPH-dependent 7-cyano-7-deazaguanine reductase( domain architecture ID 11485510)

NADPH-dependent 7-cyano-7-deazaguanine reductase catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1) in queuosine biosynthesis

EC:  1.7.1.13
PubMed:  20875425

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
queF PRK11792
7-cyano-7-deazaguanine reductase; Provisional
8-280 0e+00

7-cyano-7-deazaguanine reductase; Provisional


:

Pssm-ID: 236986 [Multi-domain]  Cd Length: 273  Bit Score: 568.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565982447   8 ALSGLTLGKSTDYRDTYDASLLQGVPRSLNRDPLGLRADALPFVGGDIWTLYELSWLNARGLPQVAVGQVELDHASLNLV 87
Cdd:PRK11792    1 ALEHSPLGKSTEYPDQYDPSLLFPIPRSLNRDELGLTADLLPFHGVDIWTAYELSWLNAKGKPQVAIGEFEIPADSPNLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565982447  88 ESKSFKLYLNSFNQTKFTSLEEVQHTLERDLRACAQGNVTVALYRLNELEGQPVAHFNGTCIDDQDIEVDNYEFSAGYLE 167
Cdd:PRK11792   81 ESKSFKLYLNSFNQTRFDSWEAVRQTLERDLSACAGAKVSVRLFPLDEFEGQPIAELPGECIDDLDIEIDNYEPDPDLLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565982447 168 NaASGKIVEETLVSHLLKSNCLITHQPDWGSVQIQYRGPKIDREKLLRYLVSFRHHNEFHEQCVERIFSDIQRFCQPETL 247
Cdd:PRK11792  161 A-AAEEVVEETLVSHLLKSNCLVTGQPDWGSVQIRYRGPKIDREGLLRYLVSFRQHNEFHEQCVERIFTDIMRFCQPEKL 239
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1565982447 248 SVYARYTRRGGLDINPWRTNTDF-VPATGRLVRQ 280
Cdd:PRK11792  240 TVYARYTRRGGLDINPFRSNFEFaPPDNGRLARQ 273
 
Name Accession Description Interval E-value
queF PRK11792
7-cyano-7-deazaguanine reductase; Provisional
8-280 0e+00

7-cyano-7-deazaguanine reductase; Provisional


Pssm-ID: 236986 [Multi-domain]  Cd Length: 273  Bit Score: 568.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565982447   8 ALSGLTLGKSTDYRDTYDASLLQGVPRSLNRDPLGLRADALPFVGGDIWTLYELSWLNARGLPQVAVGQVELDHASLNLV 87
Cdd:PRK11792    1 ALEHSPLGKSTEYPDQYDPSLLFPIPRSLNRDELGLTADLLPFHGVDIWTAYELSWLNAKGKPQVAIGEFEIPADSPNLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565982447  88 ESKSFKLYLNSFNQTKFTSLEEVQHTLERDLRACAQGNVTVALYRLNELEGQPVAHFNGTCIDDQDIEVDNYEFSAGYLE 167
Cdd:PRK11792   81 ESKSFKLYLNSFNQTRFDSWEAVRQTLERDLSACAGAKVSVRLFPLDEFEGQPIAELPGECIDDLDIEIDNYEPDPDLLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565982447 168 NaASGKIVEETLVSHLLKSNCLITHQPDWGSVQIQYRGPKIDREKLLRYLVSFRHHNEFHEQCVERIFSDIQRFCQPETL 247
Cdd:PRK11792  161 A-AAEEVVEETLVSHLLKSNCLVTGQPDWGSVQIRYRGPKIDREGLLRYLVSFRQHNEFHEQCVERIFTDIMRFCQPEKL 239
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1565982447 248 SVYARYTRRGGLDINPWRTNTDF-VPATGRLVRQ 280
Cdd:PRK11792  240 TVYARYTRRGGLDINPFRSNFEFaPPDNGRLARQ 273
QueF TIGR03138
7-cyano-7-deazaguanine reductase; This enzyme catalyzes the 4-electron reduction of the cyano ...
7-280 4.40e-179

7-cyano-7-deazaguanine reductase; This enzyme catalyzes the 4-electron reduction of the cyano group of 7-cyano-7-deazaguanine (preQ0) to an amine. Although related to a large family of GTP cyclohydrolases (pfam01227), the relationship is structural and not germane to the catalytic mechanism. This mode represents the longer, gram-negative version of the enzyme as found in E. coli. The enzymatic step represents the first point at which the biosynthesis of queuosine in bacteria and eukaryotes is distinguished from the biosynthesis of archaeosine in archaea. [Transcription, RNA processing]


Pssm-ID: 274443 [Multi-domain]  Cd Length: 275  Bit Score: 494.10  E-value: 4.40e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565982447   7 QALSGLTLGKSTDYRDTYDASLLQGVPRSLNRDPLGLRADALPFVGGDIWTLYELSWLNARGLPQVAVGQVELDHASLNL 86
Cdd:TIGR03138   1 MTLEHSPLGKSTEYPDEYDPSLLFPIPRSLNRDELGLDADKLPFVGVDIWNAYELSWLNAKGKPQVAIGEFRIPATSPNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565982447  87 VESKSFKLYLNSFNQTKFTSLEEVQHTLERDLRACAQGNVTVALYRLNELEGQPVAHFNGTCIDDQDIEVDNYEFSAGYL 166
Cdd:TIGR03138  81 IESKSFKLYLNSFNQTRFDSWEEVRQTLEKDLSAAAGAEVSVELFPLDEFAELPIAAPDGICIDDLDIEIDNYQPDPSLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565982447 167 ENAASGKIVEETLVSHLLKSNCLITHQPDWGSVQIQYRGPKIDREKLLRYLVSFRHHNEFHEQCVERIFSDIQRFCQPET 246
Cdd:TIGR03138 161 KTDQSDEEVEETLYSHLLKSNCPVTGQPDWGSVQIRYRGKKIDREALLRYLISFRQHNEFHEQCVERIFADIMRFCQPEK 240
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1565982447 247 LSVYARYTRRGGLDINPWRTNTDFV-PATGRLVRQ 280
Cdd:TIGR03138 241 LTVYARYTRRGGLDINPYRSNDEAAtPDNIRLARQ 275
QueFN COG2904
NADPH-dependent 7-cyano-7-deazaguanine reductase QueF, N-terminal domain [Translation, ...
5-280 1.01e-162

NADPH-dependent 7-cyano-7-deazaguanine reductase QueF, N-terminal domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442148 [Multi-domain]  Cd Length: 277  Bit Score: 452.43  E-value: 1.01e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565982447   5 NHQALSGLTLGKSTDYRDTYDASLLQGVPRSLNRDPLGLRADALPFVGGDIWTLYELSWLNARGLPQVAVGQVELDHASL 84
Cdd:COG2904     1 NMNTLEDSPLGKKTAYPDQYDPSLLFPIPRSLNRDELGLDADALPFVGVDIWTAYELSWLNPKGKPQVAIAEFRVPADSP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565982447  85 NLVESKSFKLYLNSFNQTKFTSLEEVQHTLERDLRACAQGNVTVALYRLNELEGQPVAHFNGTCIDDQDIEVDNYEFSAG 164
Cdd:COG2904    81 NLIESKSFKLYLNSFNQTRFASAEEVQATLQKDLSAAAGGPVKVTLFPLDDFAGQPIGELPGECIDDLDIEIDDYQPNPA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565982447 165 YLENAASGKIVEETLVSHLLKSNCLITHQPDWGSVQIQYRGPKIDREKLLRYLVSFRHHNEFHEQCVERIFSDIQRFCQP 244
Cdd:COG2904   161 LLLAAAEEEEVEETLLSLLLKSNCLVTTQPDWGSVQIYYYGPIIDRELLLLYLVSFRQHNEFHEQCVERIFIDLMRRCQP 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1565982447 245 ETLSVYARYTRRGGLDINPWRTNTDFVPATGRLVRQ 280
Cdd:COG2904   241 LKLTVYARYRRRGGLDINPRRSNSEPAPPPNRRRRR 276
QueF_N pfam14819
Nitrile reductase, 7-cyano-7-deazaguanine-reductase N-term; The QueF monomer is made up of two ...
20-130 7.45e-73

Nitrile reductase, 7-cyano-7-deazaguanine-reductase N-term; The QueF monomer is made up of two ferredoxin-like domains aligned together with their beta-sheets that have additional embellishments. This subunit is composed of a three-stranded beta-sheet and two alpha-helices. QueF reduces a nitrile bond to a primary amine. The two monomer units together create suitable substrate-binding pockets.


Pssm-ID: 464334  Cd Length: 111  Bit Score: 218.54  E-value: 7.45e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565982447  20 YRDTYDASLLQGVPRSLNRDPLGLRADALPFVGGDIWTLYELSWLNARGLPQVAVGQVELDHASLNLVESKSFKLYLNSF 99
Cdd:pfam14819   1 YPDQYDPSLLFPIPRALNRDELGLTGDALPFHGVDIWTAYELSWLNAKGKPQVAIAEFRIPADSPNLIESKSFKLYLNSF 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1565982447 100 NQTKFTSLEEVQHTLERDLRACAQGNVTVAL 130
Cdd:pfam14819  81 NQTRFASAEAVRQTLERDLSAAAGAPVSVTL 111
 
Name Accession Description Interval E-value
queF PRK11792
7-cyano-7-deazaguanine reductase; Provisional
8-280 0e+00

7-cyano-7-deazaguanine reductase; Provisional


Pssm-ID: 236986 [Multi-domain]  Cd Length: 273  Bit Score: 568.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565982447   8 ALSGLTLGKSTDYRDTYDASLLQGVPRSLNRDPLGLRADALPFVGGDIWTLYELSWLNARGLPQVAVGQVELDHASLNLV 87
Cdd:PRK11792    1 ALEHSPLGKSTEYPDQYDPSLLFPIPRSLNRDELGLTADLLPFHGVDIWTAYELSWLNAKGKPQVAIGEFEIPADSPNLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565982447  88 ESKSFKLYLNSFNQTKFTSLEEVQHTLERDLRACAQGNVTVALYRLNELEGQPVAHFNGTCIDDQDIEVDNYEFSAGYLE 167
Cdd:PRK11792   81 ESKSFKLYLNSFNQTRFDSWEAVRQTLERDLSACAGAKVSVRLFPLDEFEGQPIAELPGECIDDLDIEIDNYEPDPDLLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565982447 168 NaASGKIVEETLVSHLLKSNCLITHQPDWGSVQIQYRGPKIDREKLLRYLVSFRHHNEFHEQCVERIFSDIQRFCQPETL 247
Cdd:PRK11792  161 A-AAEEVVEETLVSHLLKSNCLVTGQPDWGSVQIRYRGPKIDREGLLRYLVSFRQHNEFHEQCVERIFTDIMRFCQPEKL 239
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1565982447 248 SVYARYTRRGGLDINPWRTNTDF-VPATGRLVRQ 280
Cdd:PRK11792  240 TVYARYTRRGGLDINPFRSNFEFaPPDNGRLARQ 273
QueF TIGR03138
7-cyano-7-deazaguanine reductase; This enzyme catalyzes the 4-electron reduction of the cyano ...
7-280 4.40e-179

7-cyano-7-deazaguanine reductase; This enzyme catalyzes the 4-electron reduction of the cyano group of 7-cyano-7-deazaguanine (preQ0) to an amine. Although related to a large family of GTP cyclohydrolases (pfam01227), the relationship is structural and not germane to the catalytic mechanism. This mode represents the longer, gram-negative version of the enzyme as found in E. coli. The enzymatic step represents the first point at which the biosynthesis of queuosine in bacteria and eukaryotes is distinguished from the biosynthesis of archaeosine in archaea. [Transcription, RNA processing]


Pssm-ID: 274443 [Multi-domain]  Cd Length: 275  Bit Score: 494.10  E-value: 4.40e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565982447   7 QALSGLTLGKSTDYRDTYDASLLQGVPRSLNRDPLGLRADALPFVGGDIWTLYELSWLNARGLPQVAVGQVELDHASLNL 86
Cdd:TIGR03138   1 MTLEHSPLGKSTEYPDEYDPSLLFPIPRSLNRDELGLDADKLPFVGVDIWNAYELSWLNAKGKPQVAIGEFRIPATSPNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565982447  87 VESKSFKLYLNSFNQTKFTSLEEVQHTLERDLRACAQGNVTVALYRLNELEGQPVAHFNGTCIDDQDIEVDNYEFSAGYL 166
Cdd:TIGR03138  81 IESKSFKLYLNSFNQTRFDSWEEVRQTLEKDLSAAAGAEVSVELFPLDEFAELPIAAPDGICIDDLDIEIDNYQPDPSLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565982447 167 ENAASGKIVEETLVSHLLKSNCLITHQPDWGSVQIQYRGPKIDREKLLRYLVSFRHHNEFHEQCVERIFSDIQRFCQPET 246
Cdd:TIGR03138 161 KTDQSDEEVEETLYSHLLKSNCPVTGQPDWGSVQIRYRGKKIDREALLRYLISFRQHNEFHEQCVERIFADIMRFCQPEK 240
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1565982447 247 LSVYARYTRRGGLDINPWRTNTDFV-PATGRLVRQ 280
Cdd:TIGR03138 241 LTVYARYTRRGGLDINPYRSNDEAAtPDNIRLARQ 275
QueFN COG2904
NADPH-dependent 7-cyano-7-deazaguanine reductase QueF, N-terminal domain [Translation, ...
5-280 1.01e-162

NADPH-dependent 7-cyano-7-deazaguanine reductase QueF, N-terminal domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442148 [Multi-domain]  Cd Length: 277  Bit Score: 452.43  E-value: 1.01e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565982447   5 NHQALSGLTLGKSTDYRDTYDASLLQGVPRSLNRDPLGLRADALPFVGGDIWTLYELSWLNARGLPQVAVGQVELDHASL 84
Cdd:COG2904     1 NMNTLEDSPLGKKTAYPDQYDPSLLFPIPRSLNRDELGLDADALPFVGVDIWTAYELSWLNPKGKPQVAIAEFRVPADSP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565982447  85 NLVESKSFKLYLNSFNQTKFTSLEEVQHTLERDLRACAQGNVTVALYRLNELEGQPVAHFNGTCIDDQDIEVDNYEFSAG 164
Cdd:COG2904    81 NLIESKSFKLYLNSFNQTRFASAEEVQATLQKDLSAAAGGPVKVTLFPLDDFAGQPIGELPGECIDDLDIEIDDYQPNPA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565982447 165 YLENAASGKIVEETLVSHLLKSNCLITHQPDWGSVQIQYRGPKIDREKLLRYLVSFRHHNEFHEQCVERIFSDIQRFCQP 244
Cdd:COG2904   161 LLLAAAEEEEVEETLLSLLLKSNCLVTTQPDWGSVQIYYYGPIIDRELLLLYLVSFRQHNEFHEQCVERIFIDLMRRCQP 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1565982447 245 ETLSVYARYTRRGGLDINPWRTNTDFVPATGRLVRQ 280
Cdd:COG2904   241 LKLTVYARYRRRGGLDINPRRSNSEPAPPPNRRRRR 276
QueF_N pfam14819
Nitrile reductase, 7-cyano-7-deazaguanine-reductase N-term; The QueF monomer is made up of two ...
20-130 7.45e-73

Nitrile reductase, 7-cyano-7-deazaguanine-reductase N-term; The QueF monomer is made up of two ferredoxin-like domains aligned together with their beta-sheets that have additional embellishments. This subunit is composed of a three-stranded beta-sheet and two alpha-helices. QueF reduces a nitrile bond to a primary amine. The two monomer units together create suitable substrate-binding pockets.


Pssm-ID: 464334  Cd Length: 111  Bit Score: 218.54  E-value: 7.45e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565982447  20 YRDTYDASLLQGVPRSLNRDPLGLRADALPFVGGDIWTLYELSWLNARGLPQVAVGQVELDHASLNLVESKSFKLYLNSF 99
Cdd:pfam14819   1 YPDQYDPSLLFPIPRALNRDELGLTGDALPFHGVDIWTAYELSWLNAKGKPQVAIAEFRIPADSPNLIESKSFKLYLNSF 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1565982447 100 NQTKFTSLEEVQHTLERDLRACAQGNVTVAL 130
Cdd:pfam14819  81 NQTRFASAEAVRQTLERDLSAAAGAPVSVTL 111
QueFC COG0780
NADPH-dependent 7-cyano-7-deazaguanine reductase QueF, C-terminal domain, T-fold superfamily ...
141-267 3.55e-68

NADPH-dependent 7-cyano-7-deazaguanine reductase QueF, C-terminal domain, T-fold superfamily [Translation, ribosomal structure and biogenesis]; NADPH-dependent 7-cyano-7-deazaguanine reductase QueF, C-terminal domain, T-fold superfamily is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440543  Cd Length: 133  Bit Score: 207.75  E-value: 3.55e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565982447 141 VAHFNGTCIDDQDiEVDNYEFSAGYLE---NAASGKIVEETLVSHLLKSNCLITHQPDWGSVQIQYRG--PKIDREKLLR 215
Cdd:COG0780     1 MTELDGLCLDGLD-EIDPYSPDPALLEtfpNPHPGRDYEITLTSPEFTSLCPVTGQPDFATIVIRYVPdkKCVELKSLKL 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1565982447 216 YLVSFRHHNEFHEQCVERIFSDIQRFCQPETLSVYARYTRRGGLDINPWRTN 267
Cdd:COG0780    80 YLVSFRNHGIFHEQCVNRIFDDLVAACKPRWLRVYARFTPRGGIDINPFRSS 131
QueF pfam14489
QueF-like protein; This protein is involved in the biosynthesis of queuosine. In some proteins ...
194-269 3.26e-27

QueF-like protein; This protein is involved in the biosynthesis of queuosine. In some proteins this domain appears to be fused to pfam06508.


Pssm-ID: 464186 [Multi-domain]  Cd Length: 81  Bit Score: 100.78  E-value: 3.26e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1565982447 194 PDWGSVQIQYRGPK--IDREKLLRYLVSFRHHNEFHEQCVERIFSDIQRFCQPETLSVYARYTRRGGLDINPWRTNTD 269
Cdd:pfam14489   1 PDFATLVIRYIPDKkvVELKSLKLYLNSFRNHGIFHEACTNRILDDLVEALDPKWLRVVGDFNPRGGIHTVVEARHGK 78
QueF-II TIGR03139
7-cyano-7-deazaguanine reductase; This enzyme catalyzes the 4-electron reduction of the cyano ...
188-266 5.39e-14

7-cyano-7-deazaguanine reductase; This enzyme catalyzes the 4-electron reduction of the cyano group of 7-cyano-7-deazaguanine (proQ1) to an amine. Although related to a large family of GTP cyclohydrolases (pfam01227), the relationship is structural and not germane to the catalytic mechanism. This mode represents the shorter, gram-positive version of the enzyme as found in B. subtilis. The enzymatic step represents the first point at which the biosynthesis of queuosine in bacteria and eukaryotes is distinguished from the biosynthesis of archaeosine in archaea.


Pssm-ID: 213775 [Multi-domain]  Cd Length: 115  Bit Score: 66.97  E-value: 5.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565982447 188 CLITHQPDWGSVQIQYRgPK---IDREKLLRYLVSFRHHNEFHEQCVERIFSDIQRFCQPETLSVYARYTRRGGLDINPW 264
Cdd:TIGR03139  31 CPKTGQPDFATIVISYI-PDqrcVELKSLKLYLFSFRNHGIFHEDVTNTILDDLVALLDPRYLEVIGDFTPRGGIKTIVF 109

                  ..
gi 1565982447 265 RT 266
Cdd:TIGR03139 110 VE 111
 
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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