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Conserved domains on  [gi|1949834258|ref|WP_198637371|]
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N-acetyltransferase [Serratia surfactantfaciens]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11418877)

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
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 61-135 1.76e-14

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 64.68  E-value: 1.76e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949834258  61 YAGVGFGLFIPEPLIGGLFVKPEYQSLGIGSALLARVTAWMFEHGAEAIHLTTDPGS-RAEGFYQHHGWVLVGQDE 135
Cdd:COG0456     2 FALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNeAAIALYEKLGFEEVGERP 77
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 61-135 1.76e-14

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 64.68  E-value: 1.76e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949834258  61 YAGVGFGLFIPEPLIGGLFVKPEYQSLGIGSALLARVTAWMFEHGAEAIHLTTDPGS-RAEGFYQHHGWVLVGQDE 135
Cdd:COG0456     2 FALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNeAAIALYEKLGFEEVGERP 77
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 18-128 3.88e-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: 64.46  E-value: 3.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949834258  18 LYEIRFSVEENLLHPHQIQYLQRKQALEDINQGGGWICKHGDDYAGVGFGLFIPEPL----IGGLFVKPEYQSLGIGSAL 93
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPpvgeIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1949834258  94 LARVTAWMFEHGAEAIHLTTDPGS-RAEGFYQHHGW 128
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNlAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 64-112 3.03e-08

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: 47.66  E-value: 3.03e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1949834258  64 VGFGLFIPEPL------IGGLFVKPEYQSLGIGSALLARVTAWMFEHGAEAIHLT 112
Cdd:cd04301    11 VGFASLSPDGSggdtayIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PRK03624 PRK03624
putative acetyltransferase; Provisional
 78-128 6.30e-05

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 40.30  E-value: 6.30e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1949834258  78 LFVKPEYQSLGIGSALLARVTAWMFEHGAEAIHLTTDPGSRA-EGFYQHHGW 128
Cdd:PRK03624   74 LAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAvLGFYEALGY 125
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 61-127 1.17e-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: 36.92  E-value: 1.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949834258  61 YAGVGFGLFipEPLIGGLFVKPEYQSLGIGSALLARVTAWMFEHGAEAIHLTTDPGS-RAEGFYQHHG 127
Cdd:TIGR01575  45 YAGVQIVLD--EAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNiAAQALYKKLG 110
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 61-135 1.76e-14

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 64.68  E-value: 1.76e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949834258  61 YAGVGFGLFIPEPLIGGLFVKPEYQSLGIGSALLARVTAWMFEHGAEAIHLTTDPGS-RAEGFYQHHGWVLVGQDE 135
Cdd:COG0456     2 FALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNeAAIALYEKLGFEEVGERP 77
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 18-128 3.88e-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: 64.46  E-value: 3.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949834258  18 LYEIRFSVEENLLHPHQIQYLQRKQALEDINQGGGWICKHGDDYAGVGFGLFIPEPL----IGGLFVKPEYQSLGIGSAL 93
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPpvgeIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1949834258  94 LARVTAWMFEHGAEAIHLTTDPGS-RAEGFYQHHGW 128
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNlAAIALYEKLGF 116
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 34-146 5.43e-14

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: 64.24  E-value: 5.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949834258  34 QIQYLQRKQALEDiNQGGGWICKHGDDYAGVGFGLFIPEPL--IGGLFVKPEYQSLGIGSALLARVTAWMFEHGAEAIHL 111
Cdd:COG1246    13 AILELIRPYALEE-EIGEFWVAEEDGEIVGCAALHPLDEDLaeLRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFL 91

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1949834258 112 TTdpGSRAEGFYQHHGWVLVGQDEFGQAELVKRKE 146
Cdd:COG1246    92 LT--TSAAIHFYEKLGFEEIDKEDLPYAKVWQRDS 124
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
45-136 1.79e-13

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 63.18  E-value: 1.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949834258  45 EDINQGGGWICKHGDDYagVGFGLFIPEPL--------IGGLFVKPEYQSLGIGSALLARVTAWMFEHGAEAIHLTTDPG 116
Cdd:COG3153    34 EDPAAGLSLVAEDDGEI--VGHVALSPVDIdgegpallLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPS 111

                          90       100
                  ....*....|....*....|
gi 1949834258 117 SRAegFYQHHGWVLVGQDEF 136
Cdd:COG3153   112 LLP--FYERFGFRPAGELGL 129
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
75-132 1.27e-10

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 54.53  E-value: 1.27e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1949834258  75 IGGLFVKPEYQSLGIGSALLARVTAWMFEHGAEAIHLTTDPGS-RAEGFYQHHGWVLVG 132
Cdd:COG3393    18 ISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNpAARRLYERLGFRPVG 76
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 53-129 1.67e-10

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 54.00  E-value: 1.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949834258  53 WICKHGDDYAGVGFGLFIPEP---LIGGLFVKPEYQSLGIGSALLARVTAWMFEHGAEAIHLTTDPgsRAEGFYQHHGWV 129
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLDDEgalAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTN--RAAAFYEKLGFE 83
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 64-133 9.46e-10

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 53.13  E-value: 9.46e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949834258  64 VGFGLFIPEP----LIGGLFVKPEYQSLGIGSALLARVTAWMFEHGAEAIHLTT-DPGSRAEGFYQHHGWVLVGQ 133
Cdd:COG0454    46 IGFAGLRRLDdkvlELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTlDGNPAAIRFYERLGFKEIER 120
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
75-136 5.79e-09

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 50.95  E-value: 5.79e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949834258  75 IGGLFVKPEYQSLGIGSALLARVTAWMFEHGAEAIHLTTDpgSRAEGFYQHHGWVLVGqDEF 136
Cdd:COG2153    61 IGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQ--AHAVGFYEKLGFVPVG-EEF 119
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 36-132 2.70e-08

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: 49.19  E-value: 2.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949834258  36 QYLQRKQALEDINQGG--GWICKHGDDYagVGFGLFIPEPLIGGLFVKPEYQSLGIGSALLARVTAWMFEHGAEAIHLTT 113
Cdd:pfam13673  15 EFISPEALRERIDQGEyfFFVAFEGGQI--VGVIALRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTV 92

                          90
                  ....*....|....*....
gi 1949834258 114 DPGSRAEGFYQHHGWVLVG 132
Cdd:pfam13673  93 NASPYAVPFYEKLGFRATG 111
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 64-112 3.03e-08

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: 47.66  E-value: 3.03e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1949834258  64 VGFGLFIPEPL------IGGLFVKPEYQSLGIGSALLARVTAWMFEHGAEAIHLT 112
Cdd:cd04301    11 VGFASLSPDGSggdtayIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
78-135 4.98e-08

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 49.22  E-value: 4.98e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1949834258  78 LFVKPEYQSLGIGSALLARVTAWMFEHGAEAIHLTTDPGS-RAEGFYQHHGWVLVGQDE 135
Cdd:COG1247    86 IYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNeASIALYEKLGFEEVGTLP 144
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 5-132 2.90e-05

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: 41.91  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949834258   5 LTFEKLTAQHLPYLYEI-------RFSVEENLLHPHQIQYLQRKQALEDINQGGGW--ICKHGDDYAGVgFGLFIPEPLI 75
Cdd:COG1670     8 LRLRPLRPEDAEALAELlndpevaRYLPGPPYSLEEARAWLERLLADWADGGALPFaiEDKEDGELIGV-VGLYDIDRAN 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949834258  76 G----GLFVKPEYQSLGIGSALLARVTAWMFEH-GAEAIHLTTDPG-SRAEGFYQHHGWVLVG 132
Cdd:COG1670    87 RsaeiGYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDnTASIRVLEKLGFRLEG 149
PRK03624 PRK03624
putative acetyltransferase; Provisional
 78-128 6.30e-05

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 40.30  E-value: 6.30e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1949834258  78 LFVKPEYQSLGIGSALLARVTAWMFEHGAEAIHLTTDPGSRA-EGFYQHHGW 128
Cdd:PRK03624   74 LAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAvLGFYEALGY 125
PRK10514 PRK10514
putative acetyltransferase; Provisional
 64-135 1.10e-03

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 36.90  E-value: 1.10e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949834258  64 VGFgLFIPEPLIGGLFVKPEYQSLGIGSALLarvtawmfEHG-AEAIHLTTD---PGSRAEGFYQHHGWVLVGQDE 135
Cdd:PRK10514   62 VGF-MLLSGGHMEALFVDPDVRGCGVGRMLV--------EHAlSLHPELTTDvneQNEQAVGFYKKMGFKVTGRSE 128
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 61-127 1.17e-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: 36.92  E-value: 1.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949834258  61 YAGVGFGLFipEPLIGGLFVKPEYQSLGIGSALLARVTAWMFEHGAEAIHLTTDPGS-RAEGFYQHHG 127
Cdd:TIGR01575  45 YAGVQIVLD--EAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNiAAQALYKKLG 110
PRK09831 PRK09831
GNAT family N-acetyltransferase;
64-133 1.69e-03

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 36.47  E-value: 1.69e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949834258  64 VGFGLFIpEPLIGGLFVKPEYQSLGIGSALLarvTAWMFEHGAeaihLTTDPGSRAEGFYQHHGWVLVGQ 133
Cdd:PRK09831   65 VGFITCI-EHYIDMLFVDPEYTRRGVASALL---KPLIKSESE----LTVDASITAKPFFERYGFQTVKQ 126
 
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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