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Conserved domains on  [gi|446465440|ref|WP_000543294|]
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MULTISPECIES: GNAT family N-acetyltransferase [Bacillus]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11450351)

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

CATH:  3.40.630.30
EC:  2.3.-.-
Gene Ontology:  GO:0016746|GO:0008080
PubMed:  27367672|26818562|15581578|10940244
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
9-140 1.65e-49

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


:

Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 154.57  E-value: 1.65e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465440   9 DEQLRDAFSVRKQVFVNEQRVSAEEEYDEFEETSTHVVIYDNDVPVGAGRFRILD-GIGKMERICVLGSHRKKGIGKIVM 87
Cdd:COG2153    1 AEELYDALALRREVFVVEQGVPPYLELDGKDEDARHLLAYDDGELVATARLLPPGdGEAKIGRVAVLPEYRGQGLGRALM 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446465440  88 DALEAYAKENSLPKLKLHAQTHAEDFYKKLGYVTSSDVFMEANIPHVVMIKEL 140
Cdd:COG2153   81 EAAIEEARERGARRIVLSAQAHAVGFYEKLGFVPVGEEFLEAGIPHIDMRKPL 133
 
Name Accession Description Interval E-value
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
9-140 1.65e-49

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 154.57  E-value: 1.65e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465440   9 DEQLRDAFSVRKQVFVNEQRVSAEEEYDEFEETSTHVVIYDNDVPVGAGRFRILD-GIGKMERICVLGSHRKKGIGKIVM 87
Cdd:COG2153    1 AEELYDALALRREVFVVEQGVPPYLELDGKDEDARHLLAYDDGELVATARLLPPGdGEAKIGRVAVLPEYRGQGLGRALM 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446465440  88 DALEAYAKENSLPKLKLHAQTHAEDFYKKLGYVTSSDVFMEANIPHVVMIKEL 140
Cdd:COG2153   81 EAAIEEARERGARRIVLSAQAHAVGFYEKLGFVPVGEEFLEAGIPHIDMRKPL 133
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 43-140 5.41e-19

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: 76.93  E-value: 5.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465440   43 THVVIYDNDVPVGAGRFRildGIGKMERICVLGSHRKKGIGKIVMDALEAYAKEN--SLPKLKLHAQTHAEDFYKKLGYV 120
Cdd:pfam13673  32 FFFVAFEGGQIVGVIALR---DRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDgiKLSELTVNASPYAVPFYEKLGFR 108

                          90       100
                  ....*....|....*....|
gi 446465440  121 TSSDVFMEANIPHVVMIKEL 140
Cdd:pfam13673 109 ATGPEQEFNGIRFVPMEKEL 128
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 44-105 7.32e-09

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: 48.81  E-value: 7.32e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446465440  44 HVVIYDNDVPVGAGRFRILDGIGK---MERICVLGSHRKKGIGKIVMDALEAYAKENSLPKLKLH 105
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDtayIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PRK10314 PRK10314
GNAT family N-acetyltransferase;
11-139 7.33e-07

GNAT family N-acetyltransferase;


Pssm-ID: 182373 [Multi-domain]  Cd Length: 153  Bit Score: 45.60  E-value: 7.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465440  11 QLRDAFSVRKQVFVNEQRVSAEEEYDEFEE-TSTHVVIYDNDVPVGAGRfrILDGIGKME-----RICVLGSHRKKGIGK 84
Cdd:PRK10314  16 QLYALLQLRCAVFVVEQNCPYQDIDGDDLTgDNRHILGWKNDELVAYAR--ILKSDDDLEpvvigRVIVSEALRGEKVGQ 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446465440  85 IVMD-ALEAYAKENSLPKLKLHAQTHAEDFYKKLGYVTSSDVFMEANIPHVVMIKE 139
Cdd:PRK10314  94 QLMSkTLESCTRHWPDKPVYLGAQAHLQNFYQSFGFIPVTEVYEEDGIPHIGMARE 149
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 45-119 5.04e-03

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: 35.00  E-value: 5.04e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446465440   45 VVIYDNDVPVGAGRFRILDGIGKMERICVLGSHRKKGIGKIVMDALEAYAKENSLPKLKLHAQTH---AEDFYKKLGY 119
Cdd:TIGR01575  34 LLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSniaAQALYKKLGF 111
 
Name Accession Description Interval E-value
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
9-140 1.65e-49

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 154.57  E-value: 1.65e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465440   9 DEQLRDAFSVRKQVFVNEQRVSAEEEYDEFEETSTHVVIYDNDVPVGAGRFRILD-GIGKMERICVLGSHRKKGIGKIVM 87
Cdd:COG2153    1 AEELYDALALRREVFVVEQGVPPYLELDGKDEDARHLLAYDDGELVATARLLPPGdGEAKIGRVAVLPEYRGQGLGRALM 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446465440  88 DALEAYAKENSLPKLKLHAQTHAEDFYKKLGYVTSSDVFMEANIPHVVMIKEL 140
Cdd:COG2153   81 EAAIEEARERGARRIVLSAQAHAVGFYEKLGFVPVGEEFLEAGIPHIDMRKPL 133
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 43-140 5.41e-19

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: 76.93  E-value: 5.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465440   43 THVVIYDNDVPVGAGRFRildGIGKMERICVLGSHRKKGIGKIVMDALEAYAKEN--SLPKLKLHAQTHAEDFYKKLGYV 120
Cdd:pfam13673  32 FFFVAFEGGQIVGVIALR---DRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDgiKLSELTVNASPYAVPFYEKLGFR 108

                          90       100
                  ....*....|....*....|
gi 446465440  121 TSSDVFMEANIPHVVMIKEL 140
Cdd:pfam13673 109 ATGPEQEFNGIRFVPMEKEL 128
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 43-140 1.30e-17

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 73.55  E-value: 1.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465440  43 THVVIYDNDVPVGAGRFRILDG-IGKMERICVLGSHRKKGIGKIVMDALEAYAKENSLPKLKLH---AQTHAEDFYKKLG 118
Cdd:COG0454   35 EFIAVDDKGEPIGFAGLRRLDDkVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDtldGNPAAIRFYERLG 114

                         90       100
                 ....*....|....*....|..
gi 446465440 119 YVTSSDVfmeANIPHVVMIKEL 140
Cdd:COG0454  115 FKEIERY---VAYVGGEFEKEL 133
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 45-140 3.16e-15

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: 67.32  E-value: 3.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465440  45 VVIYDNDVPVGAGRFRILD-GIGKMERICVLGSHRKKGIGKIVMDALEAYAKENSLPKLKLHAQTHAEDFYKKLGYV--- 120
Cdd:COG1246   31 WVAEEDGEIVGCAALHPLDeDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSAAIHFYEKLGFEeid 110

                         90       100
                 ....*....|....*....|.
gi 446465440 121 -TSSDVFMEANIPHVVMIKEL 140
Cdd:COG1246  111 kEDLPYAKVWQRDSVVMEKDL 131
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
45-140 5.40e-15

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 67.03  E-value: 5.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465440  45 VVIYDNDVPVGAGRFRILDGIGK-----MERICVLGSHRKKGIGKIVMDALEAYAKENSLPKLKLHAQTHAEDFYKKLGY 119
Cdd:COG3153   42 LVAEDDGEIVGHVALSPVDIDGEgpallLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGF 121

                         90       100
                 ....*....|....*....|.
gi 446465440 120 VTSSDVFMEANIPHVVMIKEL 140
Cdd:COG3153  122 RPAGELGLTLGPDEVFLAKEL 142
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 42-120 7.08e-15

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 65.17  E-value: 7.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465440   42 STHVVIYDNDVPVGAGRFRILDGIGKME--RICVLGSHRKKGIGKIVMDALEAYAKENSLPKLKLHAQTHAEDFYKKLGY 119
Cdd:pfam13508   3 GRFFVAEDDGKIVGFAALLPLDDEGALAelRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGF 82


                  .
gi 446465440  120 V 120
Cdd:pfam13508  83 E 83
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 42-119 1.23e-14

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: 65.23  E-value: 1.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465440   42 STHVVIYDNDVPVGAGRFRILD---GIGKMERICVLGSHRKKGIGKIVMDALEAYAKENSLPKLKLH---AQTHAEDFYK 115
Cdd:pfam00583  33 EGFFVAEEDGELVGFASLSIIDdepPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEvaaDNLAAIALYE 112


                  ....
gi 446465440  116 KLGY 119
Cdd:pfam00583 113 KLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 56-140 1.23e-12

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 59.67  E-value: 1.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465440  56 AGRFRILDGIGKMERICVLGSHRKKGIGKIVMDALEAYAKENSLPKLKLHAQTH---AEDFYKKLGYVTSSDVFMEANIP 132
Cdd:COG0456    4 LLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDneaAIALYEKLGFEEVGERPNYYGDD 83


                 ....*...
gi 446465440 133 HVVMIKEL 140
Cdd:COG0456   84 ALVMEKEL 91
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 44-105 7.32e-09

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: 48.81  E-value: 7.32e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446465440  44 HVVIYDNDVPVGAGRFRILDGIGK---MERICVLGSHRKKGIGKIVMDALEAYAKENSLPKLKLH 105
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDtayIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
53-127 1.48e-07

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 46.06  E-value: 1.48e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446465440  53 PVGAGRFRI-LDGIGKMERICVLGSHRKKGIGKIVMDALEAYAKENSLPKLKLH---AQTHAEDFYKKLGYVTSSDVFM 127
Cdd:COG3393    2 LVAMAGVRAeSPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYvdaDNPAARRLYERLGFRPVGEYAT 80
PRK10314 PRK10314
GNAT family N-acetyltransferase;
11-139 7.33e-07

GNAT family N-acetyltransferase;


Pssm-ID: 182373 [Multi-domain]  Cd Length: 153  Bit Score: 45.60  E-value: 7.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465440  11 QLRDAFSVRKQVFVNEQRVSAEEEYDEFEE-TSTHVVIYDNDVPVGAGRfrILDGIGKME-----RICVLGSHRKKGIGK 84
Cdd:PRK10314  16 QLYALLQLRCAVFVVEQNCPYQDIDGDDLTgDNRHILGWKNDELVAYAR--ILKSDDDLEpvvigRVIVSEALRGEKVGQ 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446465440  85 IVMD-ALEAYAKENSLPKLKLHAQTHAEDFYKKLGYVTSSDVFMEANIPHVVMIKE 139
Cdd:PRK10314  94 QLMSkTLESCTRHWPDKPVYLGAQAHLQNFYQSFGFIPVTEVYEEDGIPHIGMARE 149
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
45-121 7.98e-06

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 43.06  E-value: 7.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465440  45 VVIYDNDVPVG---AGRFRILDGIGKM--ERICVLGSHRKKGIGKIVMDALEAYAKENSLPKLKLH---AQTHAEDFYKK 116
Cdd:COG1247   55 LVAEEDGEVVGfasLGPFRPRPAYRGTaeESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVvlaDNEASIALYEK 134


                 ....*
gi 446465440 117 LGYVT 121
Cdd:COG1247  135 LGFEE 139
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 45-119 5.04e-03

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: 35.00  E-value: 5.04e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446465440   45 VVIYDNDVPVGAGRFRILDGIGKMERICVLGSHRKKGIGKIVMDALEAYAKENSLPKLKLHAQTH---AEDFYKKLGY 119
Cdd:TIGR01575  34 LLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSniaAQALYKKLGF 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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