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Conserved domains on  [gi|1196865725|ref|WP_086310542|]
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N-acetyltransferase [Enterococcus sp. 3G1_DIV0629]

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 ...
 46-127 1.15e-16

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 70.45  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196865725  46 ILIYIVREKEFEIVNVAVEPSHQGKGIGGKLLETAFQKLSQLASSQTQIIVRTGSTssAALHLYQKMGYVEIGRVKDYFI 125
Cdd:COG0456     4 LLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNE--AAIALYEKLGFEEVGERPNYYG 81


                  ..
gi 1196865725 126 HH 127
Cdd:COG0456    82 DD 83
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 46-127 1.15e-16

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 70.45  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196865725  46 ILIYIVREKEFEIVNVAVEPSHQGKGIGGKLLETAFQKLSQLASSQTQIIVRTGSTssAALHLYQKMGYVEIGRVKDYFI 125
Cdd:COG0456     4 LLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNE--AAIALYEKLGFEEVGERPNYYG 81


                  ..
gi 1196865725 126 HH 127
Cdd:COG0456    82 DD 83
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 35-116 3.01e-12

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 58.62  E-value: 3.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196865725  35 WIWKEKEKTIGILIYIVREKEFEI--VNVAVEPSHQGKGIGGKLLETAfqklsQLASSQTQIIVRTGSTSSAALHLYQKM 112
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLDDEGALaeLRLAVHPEYRGQGIGRALLEAA-----EAAAKEGGIKLLELETTNRAAAFYEKL 80


                  ....
gi 1196865725 113 GYVE 116
Cdd:pfam13508  81 GFEE 84
PRK03624 PRK03624
putative acetyltransferase; Provisional
 61-120 2.65e-07

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 46.85  E-value: 2.65e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196865725  61 VAVEPSHQGKGIGGKLLETAFQKLSQLASSQTQIIVRTGSTssAALHLYQKMGYVEIGRV 120
Cdd:PRK03624   74 LAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDND--AVLGFYEALGYEEQDRI 131
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 35-87 1.13e-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: 43.80  E-value: 1.13e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1196865725  35 WIWKEKEKTIGILIYIVRE---KEFEIVNVAVEPSHQGKGIGGKLLETAFQKLSQL 87
Cdd:cd04301     2 LVAEDDGEIVGFASLSPDGsggDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARER 57
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 46-127 1.15e-16

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 70.45  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196865725  46 ILIYIVREKEFEIVNVAVEPSHQGKGIGGKLLETAFQKLSQLASSQTQIIVRTGSTssAALHLYQKMGYVEIGRVKDYFI 125
Cdd:COG0456     4 LLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNE--AAIALYEKLGFEEVGERPNYYG 81


                  ..
gi 1196865725 126 HH 127
Cdd:COG0456    82 DD 83
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 39-130 1.19e-12

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 61.22  E-value: 1.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196865725  39 EKEKTIGILIY-IVREKEFEIVNVAVEPSHQGKGIGGKLLETAFQKLsqLASSQTQIIVRTGSTSSAALHLYQKMGYVEI 117
Cdd:COG0454    41 DKGEPIGFAGLrRLDDKVLELKRLYVLPEYRGKGIGKALLEALLEWA--RERGCTALELDTLDGNPAAIRFYERLGFKEI 118

                          90
                  ....*....|...
gi 1196865725 118 GRVKDYFIHHYSK 130
Cdd:COG0454   119 ERYVAYVGGEFEK 131
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 27-119 1.75e-12

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: 60.78  E-value: 1.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196865725  27 VYVSKGNGWIWKEKEKTIG-ILIYIVREKEFEIVNVAVEPSHQGKGIGGKLLETAFQKLSQLasSQTQIIVrtgSTSSAA 105
Cdd:COG1246    23 LEEEIGEFWVAEEDGEIVGcAALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEAREL--GLKRLFL---LTTSAA 97

                          90
                  ....*....|....
gi 1196865725 106 LHLYQKMGYVEIGR 119
Cdd:COG1246    98 IHFYEKLGFEEIDK 111
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 35-116 3.01e-12

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 58.62  E-value: 3.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196865725  35 WIWKEKEKTIGILIYIVREKEFEI--VNVAVEPSHQGKGIGGKLLETAfqklsQLASSQTQIIVRTGSTSSAALHLYQKM 112
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLDDEGALaeLRLAVHPEYRGQGIGRALLEAA-----EAAAKEGGIKLLELETTNRAAAFYEKL 80


                  ....
gi 1196865725 113 GYVE 116
Cdd:pfam13508  81 GFEE 84
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
57-125 7.74e-11

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 55.30  E-value: 7.74e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196865725  57 EIVNVAVEPSHQGKGIGGKLLETAFQKLsqLASSQTQIIVRTGSTSSAALHLYQKMGYVEIGRVKDYFI 125
Cdd:COG3393    17 EISGVYTHPEYRGRGLASALVAALAREA--LARGARTPFLYVDADNPAARRLYERLGFRPVGEYATVLF 83
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 35-114 4.55e-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: 54.06  E-value: 4.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196865725  35 WIWKEKEKTIG-ILIYIVREKEF--EIVNVAVEPSHQGKGIGGKLLETAFQKLsqLASSQTQIIVRTGSTSSAALHLYQK 111
Cdd:pfam00583  36 FVAEEDGELVGfASLSIIDDEPPvgEIEGLAVAPEYRGKGIGTALLQALLEWA--RERGCERIFLEVAADNLAAIALYEK 113


                  ...
gi 1196865725 112 MGY 114
Cdd:pfam00583 114 LGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
61-127 7.00e-10

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 54.23  E-value: 7.00e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196865725  61 VAVEPSHQGKGIGGKLLETAFQKlsqlASSQ--TQIIVRTGSTSSAALHLYQKMGYVEIGRVKDYFIHH 127
Cdd:COG1247    86 IYVDPDARGRGIGRALLEALIER----ARARgyRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKF 150
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
56-119 6.25e-08

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 48.93  E-value: 6.25e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1196865725  56 FEIVNVAVEPSHQGKGIGGKLLETAfqkLSQLASSQTQIIVRTGSTSSAAlhLYQKMGYVEIGR 119
Cdd:COG3153    68 LLLGPLAVDPEYRGQGIGRALMRAA---LEAARERGARAVVLLGDPSLLP--FYERFGFRPAGE 126
PRK03624 PRK03624
putative acetyltransferase; Provisional
 61-120 2.65e-07

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 46.85  E-value: 2.65e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196865725  61 VAVEPSHQGKGIGGKLLETAFQKLSQLASSQTQIIVRTGSTssAALHLYQKMGYVEIGRV 120
Cdd:PRK03624   74 LAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDND--AVLGFYEALGYEEQDRI 131
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 35-87 1.13e-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: 43.80  E-value: 1.13e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1196865725  35 WIWKEKEKTIGILIYIVRE---KEFEIVNVAVEPSHQGKGIGGKLLETAFQKLSQL 87
Cdd:cd04301     2 LVAEDDGEIVGFASLSPDGsggDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARER 57
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 58-120 1.69e-06

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: 44.57  E-value: 1.69e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196865725  58 IVNVAVEPSHQGKGIGGKLLETAFQKLSQLASSQTQIIVRtgsTSSAALHLYQKMGYVEIGRV 120
Cdd:pfam13673  54 ISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVN---ASPYAVPFYEKLGFRATGPE 113
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
61-120 2.59e-06

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 44.40  E-value: 2.59e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196865725  61 VAVEPSHQGKGIGGKLLETAFQKLSQLASSQTQIivrtgSTSSAALHLYQKMGYVEIGRV 120
Cdd:COG2153    64 VAVLPEYRGQGLGRALMEAAIEEARERGARRIVL-----SAQAHAVGFYEKLGFVPVGEE 118
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 60-124 3.57e-06

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 44.15  E-value: 3.57e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1196865725  60 NVAVEPSHQGKGIGGKLLETAFQKLSQLASSQTQIIVRtgSTSSAALHLYQKMGYVEIGRVKDYF 124
Cdd:PRK09491   68 NIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVR--ASNAAAIALYESLGFNEVTIRRNYY 130
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 23-127 2.29e-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: 42.29  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196865725  23 EKVQVYVSKGNGWIW----KEKEKTIGILIYIVREKEFEIVNVA--VEPSHQGKGIG----GKLLETAFQKLSQlassqT 92
Cdd:COG1670    49 ERLLADWADGGALPFaiedKEDGELIGVVGLYDIDRANRSAEIGywLAPAYWGKGYAtealRALLDYAFEELGL-----H 123

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1196865725  93 QIIVRTGSTSSAALHLYQKMGYVEIGRVKDYFIHH 127
Cdd:COG1670   124 RVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVID 158
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
 36-82 6.95e-05

GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both CoA and acetyl-CoA. They are characterized by highly conserved glycine, a cysteine residue in the acetyl-CoA binding site near the acetyl group, their small size compared with other GNATs and a lack of of an obvious substrate-binding site. It is proposed that they transfer an acetyl group from acetyl-CoA to one or more unidentified aliphatic amines via an acetyl (cysteine) enzyme intermediate. The substrate might be another macromolecule.


Pssm-ID: 434030 [Multi-domain]  Cd Length: 79  Bit Score: 39.04  E-value: 6.95e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1196865725  36 IWKEKEKTIGILIYIVREKEFEIVNVAVEPSHQGKGIGGKLLETAFQ 82
Cdd:pfam14542   4 IRVDGGAEVAFLTYRRGDGVLIITHTEVPPALRGQGIASKLVKAALD 50
PRK07757 PRK07757
N-acetyltransferase;
35-126 3.89e-04

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 38.64  E-value: 3.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196865725  35 WIWKEKEKTIGIL-IYIVREKEFEIVNVAVEPSHQGKGIGGKLLETAFQKLSQLASsqTQIIVRTGSTssaalHLYQKMG 113
Cdd:PRK07757   44 YVAEEEGEIVGCCaLHILWEDLAEIRSLAVSEDYRGQGIGRMLVEACLEEARELGV--KRVFALTYQP-----EFFEKLG 116

                          90
                  ....*....|...
gi 1196865725 114 YVEIGrvKDYFIH 126
Cdd:PRK07757  117 FREVD--KEALPQ 127
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 57-117 5.22e-03

FR47-like protein; The members of this family are similar to the C-terminal region of the D. melanogaster hypothetical protein FR47. This protein has been found to consist of two N-acyltransferase-like domains swapped with the C-terminal strands.


Pssm-ID: 117022 [Multi-domain]  Cd Length: 86  Bit Score: 34.23  E-value: 5.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1196865725  57 EIVNVAVEPSHQGKGIGGKLLETAFQKLSQLassQTQIIVRTGSTSSAALHLYQKMGYVEI 117
Cdd:pfam08445  23 ELGALQTLPEHRRRGLGSRLVAALARGIAER---GITPFAVVVAGNTPSRRLYEKLGFRKI 80
PRK10562 PRK10562
putative acetyltransferase; Provisional
 27-119 8.91e-03

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 34.66  E-value: 8.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196865725  27 VYVSKGNGWIWKEKEKTIGiliYI-VREKEFeIVNVAVEPSHQGKGIGGKLLETAFQKLSQLASSQTQIIVRtgstssaA 105
Cdd:PRK10562   43 VYLPAAQTWVWEEDGKLLG---FVsVLEGRF-VGALFVAPKAVRRGIGKALMQHVQQRYPHLSLEVYQKNQR-------A 111

                          90
                  ....*....|....
gi 1196865725 106 LHLYQKMGYVEIGR 119
Cdd:PRK10562  112 VNFYHAQGFRIVDS 125
 
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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