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Conserved domains on  [gi|394256730|gb|EJE01657|]
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acetyltransferase, GNAT family [Staphylococcus epidermidis NIHLM040]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10008168)

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

CATH:  3.40.630.30
EC:  2.3.1.-
Gene Ontology:  GO:0008080
PubMed:  9175471|10940244|15581578
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
1-166 6.99e-55

Predicted acetyltransferase [General function prediction only];


:

Pssm-ID: 443180  Cd Length: 170  Bit Score: 170.86  E-value: 6.99e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256730   1 MEEIRPiTYQDKEAYYYYIQEWYENEekvVPGNTDIANYSSFNNMVDRL----NCSEVDEGFVPSTTLFYF-KDSIIIGA 75
Cdd:COG3981    2 MELVRP-TLEDEESYLEYLAEFLKEH---IDGSGYLVSFEDFEAWLERLldeeKGEELPEGWVPATTYWLVdEDGRIVGA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256730  76 VDIRHQLNDKLSNIGGHVGYGVAKSYRGKGYATILLEKALDELKTLNVEVVLMTCNPLNFASQTVMKKCGGYQIESYIKK 155
Cdd:COG3981   78 INLRHELNEFLLRVGGHIGYGVRPSERGKGYATEMLRLALEEARELGLDRVLITCDKDNIASRKVIEANGGVLEDEVVDE 157

                        170
                 ....*....|..
gi 394256730 156 -NGKPVHRYHIP 166
Cdd:COG3981  158 eDGRPVRRYWID 169
 
Name Accession Description Interval E-value
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
1-166 6.99e-55

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 170.86  E-value: 6.99e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256730   1 MEEIRPiTYQDKEAYYYYIQEWYENEekvVPGNTDIANYSSFNNMVDRL----NCSEVDEGFVPSTTLFYF-KDSIIIGA 75
Cdd:COG3981    2 MELVRP-TLEDEESYLEYLAEFLKEH---IDGSGYLVSFEDFEAWLERLldeeKGEELPEGWVPATTYWLVdEDGRIVGA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256730  76 VDIRHQLNDKLSNIGGHVGYGVAKSYRGKGYATILLEKALDELKTLNVEVVLMTCNPLNFASQTVMKKCGGYQIESYIKK 155
Cdd:COG3981   78 INLRHELNEFLLRVGGHIGYGVRPSERGKGYATEMLRLALEEARELGLDRVLITCDKDNIASRKVIEANGGVLEDEVVDE 157

                        170
                 ....*....|..
gi 394256730 156 -NGKPVHRYHIP 166
Cdd:COG3981  158 eDGRPVRRYWID 169
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 4-145 2.07e-12

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 60.82  E-value: 2.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256730    4 IRPITYQDKEAYYyyiqEWYENEEKV---VPGNTDIAN-YSSFNNMVDRLNCSEvDEGFVpsttlFYFKDSIIIGAVDIR 79
Cdd:pfam13302   4 LRPLTEEDAEALF----ELLSDPEVMrygVPWPLTLEEaREWLARIWAADEAER-GYGWA-----IELKDTGFIGSIGLY 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256730   80 HQLNDklsNIGGHVGYGVAKSYRGKGYAT----ILLEKALDElktLNVEVVLMTCNPLNFASQTVMKKCG 145
Cdd:pfam13302  74 DIDGE---PERAELGYWLGPDYWGKGYATeavrALLEYAFEE---LGLPRLVARIDPENTASRRVLEKLG 137
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 64-126 7.30e-06

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: 41.88  E-value: 7.30e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 394256730  64 LFYFKDSIIIGAVDIRHQlndklsNIGGHVGY----GVAKSYRGKGYATILLEKALDELKTLNVEVV 126
Cdd:cd04301    2 LVAEDDGEIVGFASLSPD------GSGGDTAYigdlAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
PRK07757 PRK07757
N-acetyltransferase;
97-150 5.45e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 35.56  E-value: 5.45e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 394256730  97 VAKSYRGKGYATILLEKALDELKTLNVEVVL-MTCNPLNFasqtvmKKCGGYQIE 150
Cdd:PRK07757  73 VSEDYRGQGIGRMLVEACLEEARELGVKRVFaLTYQPEFF------EKLGFREVD 121
 
Name Accession Description Interval E-value
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
1-166 6.99e-55

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 170.86  E-value: 6.99e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256730   1 MEEIRPiTYQDKEAYYYYIQEWYENEekvVPGNTDIANYSSFNNMVDRL----NCSEVDEGFVPSTTLFYF-KDSIIIGA 75
Cdd:COG3981    2 MELVRP-TLEDEESYLEYLAEFLKEH---IDGSGYLVSFEDFEAWLERLldeeKGEELPEGWVPATTYWLVdEDGRIVGA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256730  76 VDIRHQLNDKLSNIGGHVGYGVAKSYRGKGYATILLEKALDELKTLNVEVVLMTCNPLNFASQTVMKKCGGYQIESYIKK 155
Cdd:COG3981   78 INLRHELNEFLLRVGGHIGYGVRPSERGKGYATEMLRLALEEARELGLDRVLITCDKDNIASRKVIEANGGVLEDEVVDE 157

                        170
                 ....*....|..
gi 394256730 156 -NGKPVHRYHIP 166
Cdd:COG3981  158 eDGRPVRRYWID 169
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 4-164 6.52e-15

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: 68.49  E-value: 6.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256730   4 IRPITYQDKEAYYyyiqEWYENEEKVVPGNTDIANYSSFNNMVDRLNCSEVDEGFVPsTTLFYFKDSIIIGAVDIRHQLN 83
Cdd:COG1670   10 LRPLRPEDAEALA----ELLNDPEVARYLPGPPYSLEEARAWLERLLADWADGGALP-FAIEDKEDGELIGVVGLYDIDR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256730  84 DKLSnigGHVGYGVAKSYRGKGYATILLEKALDEL-KTLNVEVVLMTCNPLNFASQTVMKKCgGYQIESYIKKNGKPVHR 162
Cdd:COG1670   85 ANRS---AEIGYWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDNTASIRVLEKL-GFRLEGTLRDALVIDGR 160


                 ..
gi 394256730 163 YH 164
Cdd:COG1670  161 YR 162
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 4-145 2.07e-12

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 60.82  E-value: 2.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256730    4 IRPITYQDKEAYYyyiqEWYENEEKV---VPGNTDIAN-YSSFNNMVDRLNCSEvDEGFVpsttlFYFKDSIIIGAVDIR 79
Cdd:pfam13302   4 LRPLTEEDAEALF----ELLSDPEVMrygVPWPLTLEEaREWLARIWAADEAER-GYGWA-----IELKDTGFIGSIGLY 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256730   80 HQLNDklsNIGGHVGYGVAKSYRGKGYAT----ILLEKALDElktLNVEVVLMTCNPLNFASQTVMKKCG 145
Cdd:pfam13302  74 DIDGE---PERAELGYWLGPDYWGKGYATeavrALLEYAFEE---LGLPRLVARIDPENTASRRVLEKLG 137
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 60-145 4.21e-09

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: 51.75  E-value: 4.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256730   60 PSTTLFYFKDSIIIGAVDIRhqLNDKLSNIGGHVGYGVAKSYRGKGYATILLEKALDELKTLNVEVVLMTCNPLNFASQT 139
Cdd:pfam00583  32 SEGFFVAEEDGELVGFASLS--IIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIA 109


                  ....*.
gi 394256730  140 VMKKCG 145
Cdd:pfam00583 110 LYEKLG 115
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 90-154 2.06e-06

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 43.88  E-value: 2.06e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 394256730  90 GGHVGY----GVAKSYRGKGYATILLEKALDELKTLNVEVVLMTCNPLNFASQTVMKKCgGYQIESYIK 154
Cdd:COG0456   10 GGDEAEiedlAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKL-GFEEVGERP 77
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 64-126 7.30e-06

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: 41.88  E-value: 7.30e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 394256730  64 LFYFKDSIIIGAVDIRHQlndklsNIGGHVGY----GVAKSYRGKGYATILLEKALDELKTLNVEVV 126
Cdd:cd04301    2 LVAEDDGEIVGFASLSPD------GSGGDTAYigdlAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
91-164 2.12e-05

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 42.29  E-value: 2.12e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 394256730  91 GHVGYGVAKSYRGKGYATILLEKALDELKTLNVEVVLMTCNPLNFASQTVMKKCgGYQIESYIKKNGKPVHRYH 164
Cdd:COG1247   82 AEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKL-GFEEVGTLPEVGFKFGRWL 154
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
4-132 1.37e-04

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 40.07  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256730   4 IRPITYQDKEAyyyyIQEWYEneekvvpgntdianySSFNNMVDRLNCSEVDEGFVPSTTLFYFKDSIIIGAVDIRHqln 83
Cdd:COG3153    1 IRPATPEDAEA----IAALLR---------------AAFGPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALSP--- 58

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 394256730  84 dklSNIGGHVGYG------VAKSYRGKGYATILLEKALDELKTLNVEVVLMTCNP 132
Cdd:COG3153   59 ---VDIDGEGPALllgplaVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDP 110
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
97-145 4.12e-04

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 37.58  E-value: 4.12e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 394256730  97 VAKSYRGKGYATILLEKALDELKTLNVEVVLMTCNPLNFASQTVMKKCG 145
Cdd:COG3393   23 THPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLG 71
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 97-129 9.40e-04

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: 37.28  E-value: 9.40e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 394256730  97 VAKSYRGKGYATILLEKALDELKTLNVE-VVLMT 129
Cdd:COG1246   60 VHPDYRGRGIGRRLLEALLAEARELGLKrLFLLT 93
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
97-126 2.73e-03

Predicted N-acyltransferase, GNAT family [General function prediction only];


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 35.93  E-value: 2.73e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 394256730  97 VAKSYRGKGYATILLEKALDELKTLNVEVV 126
Cdd:COG2153   66 VLPEYRGQGLGRALMEAAIEEARERGARRI 95
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 69-145 2.77e-03

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 36.18  E-value: 2.77e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 394256730  69 DSIIIGAVDIRHqLNDKlsniGGHVG--YgVAKSYRGKGYATILLEKALDELKTLNVEVVLMTCNPLNFASQTVMKKCG 145
Cdd:COG0454   42 KGEPIGFAGLRR-LDDK----VLELKrlY-VLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLG 114
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 61-131 3.05e-03

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 35.12  E-value: 3.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 394256730   61 STTLFYFKDSIIIGAVDIRHQLNDklsNIGGHVGYGVAKSYRGKGYATILLEKALDELKTLNVEVVLMTCN 131
Cdd:pfam13508   3 GRFFVAEDDGKIVGFAALLPLDDE---GALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETT 70
Eis COG4552
Predicted acetyltransferase [General function prediction only];
3-119 3.36e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 36.80  E-value: 3.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256730   3 EIRPITYQDKEAYYyyiqewyeneekvvpgntDIANYSsFNNMVDRLNCSEVDEGFVPSTTLFYFKDSIIIGAVdirhQL 82
Cdd:COG4552    2 EIRPLTEDDLDAFA------------------RLLAYA-FGPEPDDEELEAYRPLLEPGRVLGVFDDGELVGTL----AL 58

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 394256730  83 NDKLSNIGGHV-------GYGVAKSYRGKGYATILLEKALDELK 119
Cdd:COG4552   59 YPFTLNVGGARvpmagitGVAVAPEHRRRGVARALLREALAELR 102
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 62-131 3.53e-03

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


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 35.71  E-value: 3.53e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 394256730   62 TTLFYFKDSIIIGAVDIRHqlndklsniGGHV-GYGVAKSYRGKGYATILLEKALDELKTLNVEVVLMTCN 131
Cdd:pfam13673  32 FFFVAFEGGQIVGVIALRD---------RGHIsLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVN 93
PRK07757 PRK07757
N-acetyltransferase;
97-150 5.45e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 35.56  E-value: 5.45e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 394256730  97 VAKSYRGKGYATILLEKALDELKTLNVEVVL-MTCNPLNFasqtvmKKCGGYQIE 150
Cdd:PRK07757  73 VSEDYRGQGIGRMLVEACLEEARELGVKRVFaLTYQPEFF------EKLGFREVD 121
 
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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