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Conserved domains on  [gi|2785670006|gb|XDY92856|]
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GNAT family N-acetyltransferase (plasmid) [Cronobacter sakazakii]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10456837)

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:  15581578|10940244|9175471|27367672|26818562
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 50-124 8.40e-12

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: 58.30  E-value: 8.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785670006  50 VCSRDGEVVGFCIFKEYER-----YIEIVALNALKLRKGIGCMLINEVRRYAESQGKFQIRLTTTNENLAAIAFYEKMGF 124
Cdd:pfam00583  37 VAEEDGELVGFASLSIIDDeppvgEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 50-124 8.40e-12

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: 58.30  E-value: 8.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785670006  50 VCSRDGEVVGFCIFKEYER-----YIEIVALNALKLRKGIGCMLINEVRRYAESQGKFQIRLTTTNENLAAIAFYEKMGF 124
Cdd:pfam00583  37 VAEEDGELVGFASLSIIDDeppvgEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
46-133 2.16e-11

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 58.08  E-value: 2.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785670006  46 LPISVCSRDGEVVGFC---IFKEYERYiEIVALNALKL-----RKGIGCMLINEVRRYAESQGKFQIRLTTTNENLAAIA 117
Cdd:COG1247    52 RPVLVAEEDGEVVGFAslgPFRPRPAY-RGTAEESIYVdpdarGRGIGRALLEALIERARARGYRRLVAVVLADNEASIA 130

                          90
                  ....*....|....*.
gi 2785670006 118 FYEKMGFTLYAVDKDA 133
Cdd:COG1247   131 LYEKLGFEEVGTLPEV 146
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 39-124 1.55e-08

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: 50.02  E-value: 1.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785670006  39 EEYILYSLPISVCSRDGEVVGFCI----FKEYEryIEIVALNALKLRKGIGCMLINEVRRYAESQGKFQIRLTTTNENLA 114
Cdd:TIGR01575  24 EELANYHLCYLLARIGGKVVGYAGvqivLDEAH--ILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIA 101

                          90
                  ....*....|
gi 2785670006 115 AIAFYEKMGF 124
Cdd:TIGR01575 102 AQALYKKLGF 111
PRK10562 PRK10562
putative acetyltransferase; Provisional
 54-125 2.26e-04

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 38.90  E-value: 2.26e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2785670006  54 DGEVVGFCIFKEyERYIE--IVALNALklRKGIGCMLINEV-RRYAesqgkfQIRLTTTNENLAAIAFYEKMGFT 125
Cdd:PRK10562   56 DGKLLGFVSVLE-GRFVGalFVAPKAV--RRGIGKALMQHVqQRYP------HLSLEVYQKNQRAVNFYHAQGFR 121
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 50-107 2.97e-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: 36.87  E-value: 2.97e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2785670006  50 VCSRDGEVVGFCIFKEYER-----YIEIVALNALKLRKGIGCMLINEVRRYAESQGKFQIRLT 107
Cdd:cd04301     3 VAEDDGEIVGFASLSPDGSggdtaYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 50-124 8.40e-12

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: 58.30  E-value: 8.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785670006  50 VCSRDGEVVGFCIFKEYER-----YIEIVALNALKLRKGIGCMLINEVRRYAESQGKFQIRLTTTNENLAAIAFYEKMGF 124
Cdd:pfam00583  37 VAEEDGELVGFASLSIIDDeppvgEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
46-133 2.16e-11

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 58.08  E-value: 2.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785670006  46 LPISVCSRDGEVVGFC---IFKEYERYiEIVALNALKL-----RKGIGCMLINEVRRYAESQGKFQIRLTTTNENLAAIA 117
Cdd:COG1247    52 RPVLVAEEDGEVVGFAslgPFRPRPAY-RGTAEESIYVdpdarGRGIGRALLEALIERARARGYRRLVAVVLADNEASIA 130

                          90
                  ....*....|....*.
gi 2785670006 118 FYEKMGFTLYAVDKDA 133
Cdd:COG1247   131 LYEKLGFEEVGTLPEV 146
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 81-140 3.36e-11

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 55.82  E-value: 3.36e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785670006  81 RKGIGCMLINEVRRYAESQGKFQIRLTTTNENLAAIAFYEKMGFTLYAVDKDAVTRARLL 140
Cdd:COG0456    27 GRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDALV 86
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 34-125 2.38e-09

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 51.98  E-value: 2.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785670006  34 MVVHGEEYILYSLpisvcsrDGEVVGFCIFKEYER---YIEIVALNALKLRKGIGCMLINEVRRYAESQGKFQIRLTTTN 110
Cdd:COG0454    29 GSLAGAEFIAVDD-------KGEPIGFAGLRRLDDkvlELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLD 101

                          90
                  ....*....|....*
gi 2785670006 111 ENLAAIAFYEKMGFT 125
Cdd:COG0454   102 GNPAAIRFYERLGFK 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 39-124 1.55e-08

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: 50.02  E-value: 1.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785670006  39 EEYILYSLPISVCSRDGEVVGFCI----FKEYEryIEIVALNALKLRKGIGCMLINEVRRYAESQGKFQIRLTTTNENLA 114
Cdd:TIGR01575  24 EELANYHLCYLLARIGGKVVGYAGvqivLDEAH--ILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIA 101

                          90
                  ....*....|
gi 2785670006 115 AIAFYEKMGF 124
Cdd:TIGR01575 102 AQALYKKLGF 111
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 50-125 2.89e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 48.22  E-value: 2.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785670006  50 VCSRDGEVVGFCIFKEYERYIEIVALNalkL-------RKGIGCMLINEVRRYAESQGKFQIRLTTTNEnlaAIAFYEKM 122
Cdd:pfam13508   7 VAEDDGKIVGFAALLPLDDEGALAELR---LavhpeyrGQGIGRALLEAAEAAAKEGGIKLLELETTNR---AAAFYEKL 80


                  ...
gi 2785670006 123 GFT 125
Cdd:pfam13508  81 GFE 83
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 50-125 1.68e-07

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: 47.29  E-value: 1.68e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2785670006  50 VCSRDGEVVGFCIFKEYER---YIEIVALNALKLRKGIGCMLINEVRRYAESQGKFQIRLTTTNenlAAIAFYEKMGFT 125
Cdd:COG1246    32 VAEEDGEIVGCAALHPLDEdlaELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTS---AAIHFYEKLGFE 107
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 50-124 8.82e-07

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: 44.95  E-value: 8.82e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2785670006  50 VCSRDGEVVGFCIFKEyERYIEIVALNALKLRKGIGCMLINEVRRYAESQGkFQIRLTTTNENLAAIAFYEKMGF 124
Cdd:pfam13673  35 VAFEGGQIVGVIALRD-RGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDG-IKLSELTVNASPYAVPFYEKLGF 107
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 54-134 1.57e-06

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: 45.38  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785670006  54 DGEVVGFCIFKEYERY---IEI-VALNALKLRKGIGCMLINEVRRYAESQGKFQ-IRLTTTNENLAAIAFYEKMGFTLYA 128
Cdd:COG1670    70 DGELIGVVGLYDIDRAnrsAEIgYWLAPAYWGKGYATEALRALLDYAFEELGLHrVEAEVDPDNTASIRVLEKLGFRLEG 149


                  ....*.
gi 2785670006 129 VDKDAV 134
Cdd:COG1670   150 TLRDAL 155
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
50-125 6.98e-06

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 43.15  E-value: 6.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785670006  50 VCSRDGEVVGFCIFKEYERYIEIVALNALKL-------RKGIGCMLINEVRRYAESQGKFQIRLTTTNENlaaIAFYEKM 122
Cdd:COG3153    43 VAEDDGEIVGHVALSPVDIDGEGPALLLGPLavdpeyrGQGIGRALMRAALEAARERGARAVVLLGDPSL---LPFYERF 119


                  ...
gi 2785670006 123 GFT 125
Cdd:COG3153   120 GFR 122
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
81-128 2.51e-05

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 40.28  E-value: 2.51e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2785670006  81 RKGIGCMLINEVRRYAESQGKFQIRLTTTNENLAAIAFYEKMGFTLYA 128
Cdd:COG3393    29 GRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVG 76
PRK10562 PRK10562
putative acetyltransferase; Provisional
 54-125 2.26e-04

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 38.90  E-value: 2.26e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2785670006  54 DGEVVGFCIFKEyERYIE--IVALNALklRKGIGCMLINEV-RRYAesqgkfQIRLTTTNENLAAIAFYEKMGFT 125
Cdd:PRK10562   56 DGKLLGFVSVLE-GRFVGalFVAPKAV--RRGIGKALMQHVqQRYP------HLSLEVYQKNQRAVNFYHAQGFR 121
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 50-107 2.97e-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: 36.87  E-value: 2.97e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2785670006  50 VCSRDGEVVGFCIFKEYER-----YIEIVALNALKLRKGIGCMLINEVRRYAESQGKFQIRLT 107
Cdd:cd04301     3 VAEDDGEIVGFASLSPDGSggdtaYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
70-126 3.99e-04

dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;


Pssm-ID: 182877  Cd Length: 194  Bit Score: 38.76  E-value: 3.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2785670006  70 IEIVALNALKLRKGIGCMLINEVRRYAESQGKFQIRLTTTNENLAAIAFYEKMGFTL 126
Cdd:PRK10975  129 IGLLAVFPGAQGRGIGARLMQAALNWCQARGLTRLRVATQMGNLAALRLYIRSGANI 185
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 78-132 1.09e-03

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this family are members of the pfam00583 (GNAT) superfamily of acetyltransferases and are proposed to perform a N-acetylation step in the process of pseudaminic acid biosynthesis in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci. Significantly, many genomes containing other components of this pathway lack this gene, indicating that some other N-acetyl transferases may be incolved and/or the step is optional, resulting in a non-acetylated pseudaminic acid variant sugar.


Pssm-ID: 274661 [Multi-domain]  Cd Length: 152  Bit Score: 36.95  E-value: 1.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2785670006  78 LKLRKGIGCMLINEVRRYAESQ-GKFQIRLTTTNENLAAIAFYEKMGFTLYAVDKD 132
Cdd:TIGR03585  86 PFCKPGVGSVLEEAALEYAFEHlGLHKLSLEVLESNNKALKLYEKFGFEREGVFRQ 141
PRK13688 PRK13688
N-acetyltransferase;
63-132 7.00e-03

N-acetyltransferase;


Pssm-ID: 237470  Cd Length: 156  Bit Score: 34.99  E-value: 7.00e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2785670006  63 FKEYERYIEIVALNALK--LRKGIGCMLINevrrYAESQGkFQIRlttTNENLAAIAFYEKMGFTLYAVDKD 132
Cdd:PRK13688   73 FEDTQDYLELWKLEVLPkyQNRGYGEMLVD----FAKSFQ-LPIK---TIARNKSKDFWLKLGFTPVEYKND 136
 
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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