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Conserved domains on  [gi|446555745|ref|WP_000633091|]
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MULTISPECIES: lipopolysaccharide core heptose(II) kinase RfaY [Enterobacteriaceae]

Protein Classification

protein kinase family protein( domain architecture ID 229378)

protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to substrates such as serine/threonine and/or tyrosine residues on proteins, or may be a pseudokinase

CATH:  1.10.510.10
PubMed:  16244704
SCOP:  4003661

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
 1-229 2.48e-139

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member pfam06176:

Pssm-ID: 473864  Cd Length: 229  Bit Score: 389.58  E-value: 2.48e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446555745    1 MITSIRYRGFSFYYKDNDNKYKEIFDEILAYNFKTVKVLRNIDDTKVSLIDTKYGRYVFKVFAPKTKRNERFLKSFVKGD 80
Cdd:pfam06176   1 MITSIKIKGFSVFYKDNDNKYKEIFDDFLSYNFKTIKVFRNIDDTKVSLIDTDYGKYILKVFSPKVKRNERFFKSLVKGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446555745   81 YYQNLIVETDRVRSAGLTFPNDFYFLAERKIFNYASVFIMLIEYVEGVELNDMPIIPENVKTEIKASMEKLHALNMLSGD 160
Cdd:pfam06176  81 YYENLFVQTDRVRSEGLTFLNDFYLLAERKTLRYVSTYIMIIEYIEGIELNDMPIIPDNVKAKIKQSIEKLHQHGMVSGD 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446555745  161 PHRGNFIVSKDGVRIIDLSGKSCTAERKARDRLAMERHLGIANEIKDYGYYSVIYRTKLRKFIKKLKGK 229
Cdd:pfam06176 161 PHRGNFIVSKDEVRIIDLSGKRCSAQRKAKDRIDLERHYGIKNEIRDYGYYLLIYRKKLRNFIRRLKGK 229
 
Name Accession Description Interval E-value
WaaY pfam06176
Lipopolysaccharide core biosynthesis protein (WaaY); This family consists of several bacterial ...
 1-229 2.48e-139

Lipopolysaccharide core biosynthesis protein (WaaY); This family consists of several bacterial lipopolysaccharide core biosynthesis proteins (WaaY or RfaY). The waaY, waaQ, and waaP genes are located in the central operon of the waa (formerly rfa) locus on the chromosome of Escherichia coli. This locus contains genes whose products are involved in the assembly of the core region of the lipopolysaccharide molecule. WaaY is the enzyme that phosphorylates HepII in this system.


Pssm-ID: 283765  Cd Length: 229  Bit Score: 389.58  E-value: 2.48e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446555745    1 MITSIRYRGFSFYYKDNDNKYKEIFDEILAYNFKTVKVLRNIDDTKVSLIDTKYGRYVFKVFAPKTKRNERFLKSFVKGD 80
Cdd:pfam06176   1 MITSIKIKGFSVFYKDNDNKYKEIFDDFLSYNFKTIKVFRNIDDTKVSLIDTDYGKYILKVFSPKVKRNERFFKSLVKGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446555745   81 YYQNLIVETDRVRSAGLTFPNDFYFLAERKIFNYASVFIMLIEYVEGVELNDMPIIPENVKTEIKASMEKLHALNMLSGD 160
Cdd:pfam06176  81 YYENLFVQTDRVRSEGLTFLNDFYLLAERKTLRYVSTYIMIIEYIEGIELNDMPIIPDNVKAKIKQSIEKLHQHGMVSGD 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446555745  161 PHRGNFIVSKDGVRIIDLSGKSCTAERKARDRLAMERHLGIANEIKDYGYYSVIYRTKLRKFIKKLKGK 229
Cdd:pfam06176 161 PHRGNFIVSKDEVRIIDLSGKRCSAQRKAKDRIDLERHYGIKNEIRDYGYYLLIYRKKLRNFIRRLKGK 229
PRK10359 PRK10359
lipopolysaccharide core heptose(II) kinase RfaY;
1-230 1.62e-129

lipopolysaccharide core heptose(II) kinase RfaY;


Pssm-ID: 182407  Cd Length: 232  Bit Score: 364.84  E-value: 1.62e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446555745   1 MITSIRYRGFSFYYKDNDNKYKEIFDEILAYNFKTVKVLRNIDDTKVSLIDTKYGRYVFKVFAPKTKRNERFLKSFVKGD 80
Cdd:PRK10359   1 MITKKKIKGYTVFYKDNDNKYKEIFDDFLSYNIKTIKVFRNIDDTKVSLIDTDYGKYILKVFAPKVKRTERFLKSFVKGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446555745  81 YYQNLIVETDRVRSAGLTFPNDFYFLAERKIFNYASVFIMLIEYVEGVELNDMPIIPENVKTEIKASMEKLHALNMLSGD 160
Cdd:PRK10359  81 YYENLIVQTDRVRSEGLASLNDFYLLAERKTLRYAHTYIMLIEYIEGVELNDMPEISEDVKAKIKASIESLHQHGMVSGD 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446555745 161 PHRGNFIVSKDGVRIIDLSGKSCTAERKARDRLAMERHLGIANEIKDYGYYSVIYRTKLRKFIKKLKGKA 230
Cdd:PRK10359 161 PHKGNFIVSKNGLRIIDLSGKRCTAQRKAKDRIDLERHYGIKNEIKDLGYYLLIYKKKLRKFIRKLKGKA 230
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 118-197 6.52e-07

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 47.65  E-value: 6.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446555745 118 FIMLIEYVEGVELNDMPIIPENVKTEIKASME---KLHALNMLSGDPHRGNFIVSKDGVRIID--LSGKSCTAERKARDR 192
Cdd:COG3642   31 ADLVMEYIEGETLADLLEEGELPPELLRELGRllaRLHRAGIVHGDLTTSNILVDDGGVYLIDfgLARYSDPLEDKAVDL 110


                 ....*
gi 446555745 193 LAMER 197
Cdd:COG3642  111 AVLKR 115
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
 118-207 3.00e-06

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 46.43  E-value: 3.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446555745  118 FIMLIEYVEGVELND-MPIIPENVKTEIKASMEKLHALNMLSGDPHRGNFIVSKDGVRIID--LSGKSCTAERKARDRLA 194
Cdd:TIGR03724  72 KTIVMEYIEGKPLKDvIEENGDELAREIGRLVGKLHKAGIVHGDLTTSNIIVRDDKVYLIDfgLGKYSDEIEDKAVDLHV 151

                          90
                  ....*....|....
gi 446555745  195 MERHL-GIANEIKD 207
Cdd:TIGR03724 152 LKRSLeSTHPDKAE 165
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
 119-177 7.92e-06

Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic choline kinases, as well as eukaryotic ethanolamine kinase. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. Bacterial ChoK is also referred to as licA protein. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270700 [Multi-domain]  Cd Length: 152  Bit Score: 44.47  E-value: 7.92e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446555745 119 IMLIEYVEGVELNDMPIIPENVKTEIKASMEKLHALNMLS-----GDPHRGNFIVSKDGVRIID 177
Cdd:cd05151   67 VKITEFIEGATLLTNDFSDPENLERIAALLRKLHSSPLEDlvlchNDLVPGNFLLDDDRLYLID 130
 
Name Accession Description Interval E-value
WaaY pfam06176
Lipopolysaccharide core biosynthesis protein (WaaY); This family consists of several bacterial ...
 1-229 2.48e-139

Lipopolysaccharide core biosynthesis protein (WaaY); This family consists of several bacterial lipopolysaccharide core biosynthesis proteins (WaaY or RfaY). The waaY, waaQ, and waaP genes are located in the central operon of the waa (formerly rfa) locus on the chromosome of Escherichia coli. This locus contains genes whose products are involved in the assembly of the core region of the lipopolysaccharide molecule. WaaY is the enzyme that phosphorylates HepII in this system.


Pssm-ID: 283765  Cd Length: 229  Bit Score: 389.58  E-value: 2.48e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446555745    1 MITSIRYRGFSFYYKDNDNKYKEIFDEILAYNFKTVKVLRNIDDTKVSLIDTKYGRYVFKVFAPKTKRNERFLKSFVKGD 80
Cdd:pfam06176   1 MITSIKIKGFSVFYKDNDNKYKEIFDDFLSYNFKTIKVFRNIDDTKVSLIDTDYGKYILKVFSPKVKRNERFFKSLVKGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446555745   81 YYQNLIVETDRVRSAGLTFPNDFYFLAERKIFNYASVFIMLIEYVEGVELNDMPIIPENVKTEIKASMEKLHALNMLSGD 160
Cdd:pfam06176  81 YYENLFVQTDRVRSEGLTFLNDFYLLAERKTLRYVSTYIMIIEYIEGIELNDMPIIPDNVKAKIKQSIEKLHQHGMVSGD 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446555745  161 PHRGNFIVSKDGVRIIDLSGKSCTAERKARDRLAMERHLGIANEIKDYGYYSVIYRTKLRKFIKKLKGK 229
Cdd:pfam06176 161 PHRGNFIVSKDEVRIIDLSGKRCSAQRKAKDRIDLERHYGIKNEIRDYGYYLLIYRKKLRNFIRRLKGK 229
PRK10359 PRK10359
lipopolysaccharide core heptose(II) kinase RfaY;
1-230 1.62e-129

lipopolysaccharide core heptose(II) kinase RfaY;


Pssm-ID: 182407  Cd Length: 232  Bit Score: 364.84  E-value: 1.62e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446555745   1 MITSIRYRGFSFYYKDNDNKYKEIFDEILAYNFKTVKVLRNIDDTKVSLIDTKYGRYVFKVFAPKTKRNERFLKSFVKGD 80
Cdd:PRK10359   1 MITKKKIKGYTVFYKDNDNKYKEIFDDFLSYNIKTIKVFRNIDDTKVSLIDTDYGKYILKVFAPKVKRTERFLKSFVKGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446555745  81 YYQNLIVETDRVRSAGLTFPNDFYFLAERKIFNYASVFIMLIEYVEGVELNDMPIIPENVKTEIKASMEKLHALNMLSGD 160
Cdd:PRK10359  81 YYENLIVQTDRVRSEGLASLNDFYLLAERKTLRYAHTYIMLIEYIEGVELNDMPEISEDVKAKIKASIESLHQHGMVSGD 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446555745 161 PHRGNFIVSKDGVRIIDLSGKSCTAERKARDRLAMERHLGIANEIKDYGYYSVIYRTKLRKFIKKLKGKA 230
Cdd:PRK10359 161 PHKGNFIVSKNGLRIIDLSGKRCTAQRKAKDRIDLERHYGIKNEIKDLGYYLLIYKKKLRKFIRKLKGKA 230
PRK14879 PRK14879
Kae1-associated kinase Bud32;
118-227 1.17e-07

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 50.68  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446555745 118 FIMLIEYVEGVELNDmpIIPENVKTEIKASME------KLHALNMLSGDPHRGNFIVSKDGVRIID--LSGKSCTAERKA 189
Cdd:PRK14879  74 FIIVMEYIEGEPLKD--LINSNGMEELELSREigrlvgKLHSAGIIHGDLTTSNMILSGGKIYLIDfgLAEFSKDLEDRA 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446555745 190 RD----RLAME-RHLGIANEIKDY---GYYSViYRTKLRKFIKKLK 227
Cdd:PRK14879 152 VDlhvlLRSLEsTHPDWAEELFEAfleGYREV-MGEKAEEVLERVK 196
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 118-197 6.52e-07

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 47.65  E-value: 6.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446555745 118 FIMLIEYVEGVELNDMPIIPENVKTEIKASME---KLHALNMLSGDPHRGNFIVSKDGVRIID--LSGKSCTAERKARDR 192
Cdd:COG3642   31 ADLVMEYIEGETLADLLEEGELPPELLRELGRllaRLHRAGIVHGDLTTSNILVDDGGVYLIDfgLARYSDPLEDKAVDL 110


                 ....*
gi 446555745 193 LAMER 197
Cdd:COG3642  111 AVLKR 115
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
 118-207 3.00e-06

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 46.43  E-value: 3.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446555745  118 FIMLIEYVEGVELND-MPIIPENVKTEIKASMEKLHALNMLSGDPHRGNFIVSKDGVRIID--LSGKSCTAERKARDRLA 194
Cdd:TIGR03724  72 KTIVMEYIEGKPLKDvIEENGDELAREIGRLVGKLHKAGIVHGDLTTSNIIVRDDKVYLIDfgLGKYSDEIEDKAVDLHV 151

                          90
                  ....*....|....
gi 446555745  195 MERHL-GIANEIKD 207
Cdd:TIGR03724 152 LKRSLeSTHPDKAE 165
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
 119-177 7.92e-06

Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic choline kinases, as well as eukaryotic ethanolamine kinase. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. Bacterial ChoK is also referred to as licA protein. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270700 [Multi-domain]  Cd Length: 152  Bit Score: 44.47  E-value: 7.92e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446555745 119 IMLIEYVEGVELNDMPIIPENVKTEIKASMEKLHALNMLS-----GDPHRGNFIVSKDGVRIID 177
Cdd:cd05151   67 VKITEFIEGATLLTNDFSDPENLERIAALLRKLHSSPLEDlvlchNDLVPGNFLLDDDRLYLID 130
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
120-199 4.58e-04

bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 40.64  E-value: 4.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446555745 120 MLIEYVEGVELND-MPIIPENVKtEIKASMEKLHALNMLSGDPHRGNFIVSKDGVRIID--LSGKSCTAERKARDRLAME 196
Cdd:PRK09605 413 IVMEYIGGKDLKDvLEGNPELVR-KVGEIVAKLHKAGIVHGDLTTSNFIVRDDRLYLIDfgLGKYSDLIEDKAVDLHVLK 491


                 ...
gi 446555745 197 RHL 199
Cdd:PRK09605 492 QSL 494
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
 36-194 1.31e-03

ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. These proteins have a nuclear or mitochondrial subcellular location in eukaryotes. The exact molecular functions of these proteins is not clear, however yeast ABC1 suppresses a cytochrome b mRNA translation defect and is essential for the electron transfer in the bc 1 complex and E. coli AarF is required for ubiquinone production. It has been suggested that members of the ABC1 family are novel chaperonins. These proteins are unrelated to the ABC transporter proteins.


Pssm-ID: 427143 [Multi-domain]  Cd Length: 245  Bit Score: 38.75  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446555745   36 VKVLRNiDDTKVSLIDTKYGRYVFKVFAPKTKRNERFLKsfVKGDYYQNLIVETDRVRSAGLT------FPNDFYFLAER 109
Cdd:pfam03109  59 VKVQRP-GVKKRIRSDLLLLRFLAKVAKRFFPGFRRLDW--LVDEFRKSLPQELDFLREAANAekfrenFADDPDVYVPK 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446555745  110 KIFNYASVFIMLIEYVEGVELNDMPIIPEN-------VKTEIKASMEKLHALNMLSGDPHRGNFIVSKDGvRIIDLS-GK 181
Cdd:pfam03109 136 VYWELTTERVLTMEYVDGIKIDDLDALSEAgidrkeiARRLVELFLEQIFRDGFFHADPHPGNILVRKDG-RIVLLDfGL 214

                         170
                  ....*....|...
gi 446555745  182 SCTAERKARDRLA 194
Cdd:pfam03109 215 MGRLDEKFRRLYA 227
 
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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