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Conserved domains on  [gi|516001317|ref|WP_017431900|]
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GNAT family N-acetyltransferase [Staphylococcus aureus]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11447421)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 8-152 7.39e-11

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 59.63  E-value: 7.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516001317   8 EGITLKAFAEQYRSAINDFDLNERQQIYSSLPKEVIDDAINDVDRIAN-----------VAINDKNEVVGFFVLHRYyqh 76
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLAdwadggalpfaIEDKEDGELIGVVGLYDI--- 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516001317  77 egyDTPENVVYIrSLSINEKYQGFGYGTKIMMSLPQYVQGVFpDFNHLYLVVDAENDNAWNLYERAGFMHTATKEE 152
Cdd:COG1670   83 ---DRANRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEEL-GLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRD 153
NAT_SF super family cl17182
N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of ...
 193-250 6.97e-04

N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase which catalyze the transfer of an acetyl group to a substrate. The mechanism is an ordered Bi-Bi ternary complex kinetic mechanism for most GNATs: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and then CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/ph enylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


The actual alignment was detected with superfamily member TIGR01575:

Pssm-ID: 473072 [Multi-domain]  Cd Length: 131  Bit Score: 38.85  E-value: 6.97e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 516001317  193 IDGQKVGFIALEQIGERMNIAAIEVDKSYRFNGIGSSALRQLPTYLRKNydNLNVITM 250
Cdd:TIGR01575  38 IGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGR--GVNEIFL 93
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 8-152 7.39e-11

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 59.63  E-value: 7.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516001317   8 EGITLKAFAEQYRSAINDFDLNERQQIYSSLPKEVIDDAINDVDRIAN-----------VAINDKNEVVGFFVLHRYyqh 76
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLAdwadggalpfaIEDKEDGELIGVVGLYDI--- 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516001317  77 egyDTPENVVYIrSLSINEKYQGFGYGTKIMMSLPQYVQGVFpDFNHLYLVVDAENDNAWNLYERAGFMHTATKEE 152
Cdd:COG1670   83 ---DRANRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEEL-GLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRD 153
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 56-144 3.77e-10

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 56.37  E-value: 3.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516001317   56 VAINDKNEVVGFFVLHRYYQhegydtPENVVYIRSLSINEKYQGFGYGTKIMMSLPQYVQGVfpDFNHLYLVVDAENDNA 135
Cdd:pfam00583  36 FVAEEDGELVGFASLSIIDD------EPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARER--GCERIFLEVAADNLAA 107


                  ....*....
gi 516001317  136 WNLYERAGF 144
Cdd:pfam00583 108 IALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 56-107 2.40e-04

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 38.41  E-value: 2.40e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 516001317  56 VAINDkNEVVGFFVLHRYYQHEGYdtpenvVYIRSLSINEKYQGFGYGTKIM 107
Cdd:cd04301    3 VAEDD-GEIVGFASLSPDGSGGDT------AYIGDLAVLPEYRGKGIGSALL 47
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 193-250 6.97e-04

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 38.85  E-value: 6.97e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 516001317  193 IDGQKVGFIALEQIGERMNIAAIEVDKSYRFNGIGSSALRQLPTYLRKNydNLNVITM 250
Cdd:TIGR01575  38 IGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGR--GVNEIFL 93
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 176-240 6.43e-03

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 35.96  E-value: 6.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516001317  176 EEESRSEVTNVHIINLMIDGQKVGFIALEQIGERMNIAAIE---VDKSYRFNGIGSSALRQLPTYLRK 240
Cdd:pfam00583  23 LLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVGEIEglaVAPEYRGKGIGTALLQALLEWARE 90
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 8-152 7.39e-11

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 59.63  E-value: 7.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516001317   8 EGITLKAFAEQYRSAINDFDLNERQQIYSSLPKEVIDDAINDVDRIAN-----------VAINDKNEVVGFFVLHRYyqh 76
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLAdwadggalpfaIEDKEDGELIGVVGLYDI--- 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516001317  77 egyDTPENVVYIrSLSINEKYQGFGYGTKIMMSLPQYVQGVFpDFNHLYLVVDAENDNAWNLYERAGFMHTATKEE 152
Cdd:COG1670   83 ---DRANRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEEL-GLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRD 153
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 56-144 3.77e-10

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 56.37  E-value: 3.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516001317   56 VAINDKNEVVGFFVLHRYYQhegydtPENVVYIRSLSINEKYQGFGYGTKIMMSLPQYVQGVfpDFNHLYLVVDAENDNA 135
Cdd:pfam00583  36 FVAEEDGELVGFASLSIIDD------EPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARER--GCERIFLEVAADNLAA 107


                  ....*....
gi 516001317  136 WNLYERAGF 144
Cdd:pfam00583 108 IALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
56-165 4.75e-10

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 57.31  E-value: 4.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516001317  56 VAINDkNEVVGFFVLHRYYQHEGYD-TPENVVYIRslsinEKYQGFGYGTKIMmslpQYVQGVFPD--FNHLYLVVDAEN 132
Cdd:COG1247   56 VAEED-GEVVGFASLGPFRPRPAYRgTAEESIYVD-----PDARGRGIGRALL----EALIERARArgYRRLVAVVLADN 125

                         90       100       110
                 ....*....|....*....|....*....|...
gi 516001317 133 DNAWNLYERAGFMHTATKEEgpIGKERLYYLDL 165
Cdd:COG1247  126 EASIALYEKLGFEEVGTLPE--VGFKFGRWLDL 156
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 78-166 2.01e-08

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 50.81  E-value: 2.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516001317  78 GYDTPENVVYIRSLSINEKYQGFGYGTKIMMSLPQYVQGVfpDFNHLYLVVDAENDNAWNLYERAGFMHTATKEEGPIGK 157
Cdd:COG0456    6 GLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARER--GARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDD 83


                 ....*....
gi 516001317 158 ERLYYLDLD 166
Cdd:COG0456   84 ALVMEKELA 92
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
56-165 1.33e-06

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 47.00  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516001317  56 VAINDkNEVVGFFVLHRYyqheGYDTPENVVYIRSLSINEKYQGFGYGTKIMmslpQYVQGVFPDFNHLYLVVDAeNDNA 135
Cdd:COG3153   43 VAEDD-GEIVGHVALSPV----DIDGEGPALLLGPLAVDPEYRGQGIGRALM----RAALEAARERGARAVVLLG-DPSL 112

                         90       100       110
                 ....*....|....*....|....*....|
gi 516001317 136 WNLYERAGFMHTATKEEGPIGKERLYYLDL 165
Cdd:COG3153  113 LPFYERFGFRPAGELGLTLGPDEVFLAKEL 142
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 56-166 1.44e-06

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 46.52  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516001317  56 VAINDkNEVVGFFVLHRYyqhegydtPENVVYIRSLSINEKYQGFGYGTKIMMSLPQY--VQGvfpdFNHLYLVVdaeND 133
Cdd:COG1246   32 VAEED-GEIVGCAALHPL--------DEDLAELRSLAVHPDYRGRGIGRRLLEALLAEarELG----LKRLFLLT---TS 95

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 516001317 134 NAWNLYERAGFmHTATKEEGPIGK-----ERLYYLDLD 166
Cdd:COG1246   96 AAIHFYEKLGF-EEIDKEDLPYAKvwqrdSVVMEKDLE 132
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 56-144 1.95e-06

N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 46.20  E-value: 1.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516001317  56 VAINDKNEVVGFFVLHRYyqhegydtPENVVYIRSLSINEKYQGFGYGTKIMMSLPQYVQGVfpDFNHLYLVVDAENDNA 135
Cdd:COG0454   37 IAVDDKGEPIGFAGLRRL--------DDKVLELKRLYVLPEYRGKGIGKALLEALLEWARER--GCTALELDTLDGNPAA 106


                 ....*....
gi 516001317 136 WNLYERAGF 144
Cdd:COG0454  107 IRFYERLGF 115
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 56-107 2.40e-04

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 38.41  E-value: 2.40e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 516001317  56 VAINDkNEVVGFFVLHRYYQHEGYdtpenvVYIRSLSINEKYQGFGYGTKIM 107
Cdd:cd04301    3 VAEDD-GEIVGFASLSPDGSGGDT------AYIGDLAVLPEYRGKGIGSALL 47
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 193-250 6.97e-04

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 38.85  E-value: 6.97e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 516001317  193 IDGQKVGFIALEQIGERMNIAAIEVDKSYRFNGIGSSALRQLPTYLRKNydNLNVITM 250
Cdd:TIGR01575  38 IGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGR--GVNEIFL 93
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 56-144 1.01e-03

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 37.43  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516001317   56 VAINDkNEVVGFFVLHRYYQHEgydtpenVVYIRSLSINEKYQGFGYGTKIMmslpQYVQGVFPDFNHLYLVVDAENDNA 135
Cdd:pfam13508   7 VAEDD-GKIVGFAALLPLDDEG-------ALAELRLAVHPEYRGQGIGRALL----EAAEAAAKEGGIKLLELETTNRAA 74


                  ....*....
gi 516001317  136 wNLYERAGF 144
Cdd:pfam13508  75 -AFYEKLGF 82
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
82-149 4.89e-03

Predicted acetyltransferase, GNAT family [General function prediction only];


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 35.27  E-value: 4.89e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516001317  82 PENVVYIRSLSINEKYQGFGYGTKIMMSLPQYVQGVFPDfnHLYLVVDAENDNAWNLYERAGFMHTAT 149
Cdd:COG3393   12 SPGVAEISGVYTHPEYRGRGLASALVAALAREALARGAR--TPFLYVDADNPAARRLYERLGFRPVGE 77
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 176-240 6.43e-03

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 35.96  E-value: 6.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516001317  176 EEESRSEVTNVHIINLMIDGQKVGFIALEQIGERMNIAAIE---VDKSYRFNGIGSSALRQLPTYLRK 240
Cdd:pfam00583  23 LLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVGEIEglaVAPEYRGKGIGTALLQALLEWARE 90
 
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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