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Conserved domains on  [gi|1321392096]
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Chain A, Aminoglycoside-(3)-N-acetyltransferase

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 ...
 40-161 3.37e-16

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: 70.62  E-value: 3.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321392096  40 MRAALDLFGREFgdvaTYSQHQPDSDYLGNLLRSKTFIALAAFDQEAVVGALAAYVLPKFEQprsEIYIYDLAVSGEHRR 119
Cdd:pfam00583   1 LEALYELLSEEF----PEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPP---VGEIEGLAVAPEYRG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1321392096 120 QGIATALINLLKHEANALGAYVIYVQADYGDDPAVALYTKLG 161
Cdd:pfam00583  74 KGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLG 115
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 40-161 3.37e-16

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: 70.62  E-value: 3.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321392096  40 MRAALDLFGREFgdvaTYSQHQPDSDYLGNLLRSKTFIALAAFDQEAVVGALAAYVLPKFEQprsEIYIYDLAVSGEHRR 119
Cdd:pfam00583   1 LEALYELLSEEF----PEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPP---VGEIEGLAVAPEYRG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1321392096 120 QGIATALINLLKHEANALGAYVIYVQADYGDDPAVALYTKLG 161
Cdd:pfam00583  74 KGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLG 115
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 93-173 7.26e-14

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 63.91  E-value: 7.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321392096  93 AYVLPKFEQPRSEIYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYVQADYGDDPAVALYTKLG--IREEVMHFD 170
Cdd:COG0456     1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGfeEVGERPNYY 80


                  ...
gi 1321392096 171 IDP 173
Cdd:COG0456    81 GDD 83
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 79-144 3.14e-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: 50.74  E-value: 3.14e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1321392096  79 LAAFDQEAVVGALAAYvlpKFEQPRSEIYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYV 144
Cdd:cd04301     2 LVAEDDGEIVGFASLS---PDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
PRK03624 PRK03624
putative acetyltransferase; Provisional
 108-165 8.58e-07

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 46.08  E-value: 8.58e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1321392096 108 IYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYVQADYGDDPAVALYTKLGIREE 165
Cdd:PRK03624   71 AYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQ 128
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 89-165 7.50e-06

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: 43.47  E-value: 7.50e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1321392096  89 GALAAYVLPKFeqPRSEIYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYVQADYGDDPAVALYTKLGIREE 165
Cdd:TIGR01575  40 GKVVGYAGVQI--VLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEI 114
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 40-161 3.37e-16

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: 70.62  E-value: 3.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321392096  40 MRAALDLFGREFgdvaTYSQHQPDSDYLGNLLRSKTFIALAAFDQEAVVGALAAYVLPKFEQprsEIYIYDLAVSGEHRR 119
Cdd:pfam00583   1 LEALYELLSEEF----PEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPP---VGEIEGLAVAPEYRG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1321392096 120 QGIATALINLLKHEANALGAYVIYVQADYGDDPAVALYTKLG 161
Cdd:pfam00583  74 KGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLG 115
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 93-173 7.26e-14

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 63.91  E-value: 7.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321392096  93 AYVLPKFEQPRSEIYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYVQADYGDDPAVALYTKLG--IREEVMHFD 170
Cdd:COG0456     1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGfeEVGERPNYY 80


                  ...
gi 1321392096 171 IDP 173
Cdd:COG0456    81 GDD 83
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
77-161 1.92e-11

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 58.56  E-value: 1.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321392096  77 IALAAFDQEAVVGALAAYVLPkFEQPRSEIYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYVqadYGDDPAVAL 156
Cdd:COG3153    40 LSLVAEDDGEIVGHVALSPVD-IDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVL---LGDPSLLPF 115


                  ....*
gi 1321392096 157 YTKLG 161
Cdd:COG3153   116 YERFG 120
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 79-161 7.40e-10

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 53.23  E-value: 7.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321392096  79 LAAFDQEAVVGALAAYVLPkfeqPRSEIYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYVQAdygDDPAVALYT 158
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLD----DEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRAAAFYE 78


                  ...
gi 1321392096 159 KLG 161
Cdd:pfam13508  79 KLG 81
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 57-161 1.00e-09

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: 53.81  E-value: 1.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321392096  57 YSQHQPDSdyLGNLLRSKTFIALAAFDQEAVVGALAAyvlpkfeqpRSEIYIYDLAVSGEHRRQGIATALINLLKHEANA 136
Cdd:pfam13673  14 YEFISPEA--LRERIDQGEYFFFVAFEGGQIVGVIAL---------RDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEK 82

                          90       100
                  ....*....|....*....|....*
gi 1321392096 137 LGAYVIYVQADyGDDPAVALYTKLG 161
Cdd:pfam13673  83 DGIKLSELTVN-ASPYAVPFYEKLG 106
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 79-144 3.14e-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: 50.74  E-value: 3.14e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1321392096  79 LAAFDQEAVVGALAAYvlpKFEQPRSEIYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYV 144
Cdd:cd04301     2 LVAEDDGEIVGFASLS---PDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
55-161 7.22e-09

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 52.30  E-value: 7.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321392096  55 ATYSQHQPDSDYLGNLLRSKT---FIALAAFDQEAVVGALAAYVLPKFEQPRsEIYIYDLAVSGEHRRQGIATALINLLK 131
Cdd:COG1247    28 ATFETEPPSEEEREAWFAAILapgRPVLVAEEDGEVVGFASLGPFRPRPAYR-GTAEESIYVDPDARGRGIGRALLEALI 106

                          90       100       110
                  ....*....|....*....|....*....|
gi 1321392096 132 HEANALGAYVIYVQADYGDDPAVALYTKLG 161
Cdd:COG1247   107 ERARARGYRRLVAVVLADNEASIALYEKLG 136
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
106-161 1.20e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 49.91  E-value: 1.20e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1321392096 106 IYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYVQADYGDDPAVALYTKLG 161
Cdd:COG3393    16 AEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLG 71
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 70-161 2.68e-08

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 50.05  E-value: 2.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321392096  70 LLRSKTFIAlaAFDQEAVVGALAAYVLPKfeqprSEIYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYVQADYG 149
Cdd:COG0454    30 SLAGAEFIA--VDDKGEPIGFAGLRRLDD-----KVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDG 102

                          90
                  ....*....|..
gi 1321392096 150 DDPAVALYTKLG 161
Cdd:COG0454   103 NPAAIRFYERLG 114
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 81-161 1.86e-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: 47.68  E-value: 1.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321392096  81 AFDQEAVVGALAAYVLPKfeqprSEIYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYVQAdygDDPAVALYTKL 160
Cdd:COG1246    33 AEEDGEIVGCAALHPLDE-----DLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT---TSAAIHFYEKL 104


                  .
gi 1321392096 161 G 161
Cdd:COG1246   105 G 105
PRK03624 PRK03624
putative acetyltransferase; Provisional
 108-165 8.58e-07

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 46.08  E-value: 8.58e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1321392096 108 IYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYVQADYGDDPAVALYTKLGIREE 165
Cdd:PRK03624   71 AYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQ 128
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 89-165 7.50e-06

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: 43.47  E-value: 7.50e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1321392096  89 GALAAYVLPKFeqPRSEIYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYVQADYGDDPAVALYTKLGIREE 165
Cdd:TIGR01575  40 GKVVGYAGVQI--VLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEI 114
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 53-165 4.45e-04

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: 38.83  E-value: 4.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321392096  53 DVATYSQHQPDS-----DYLGNLLR---SKTFIALAAFDQE--AVVGALAAYVLPKfEQPRSEIYIYdlaVSGEHRRQGI 122
Cdd:COG1670    29 EVARYLPGPPYSleearAWLERLLAdwaDGGALPFAIEDKEdgELIGVVGLYDIDR-ANRSAEIGYW---LAPAYWGKGY 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1321392096 123 ATALINLLKHEA-NALGAYVIYVQADYGDDPAVALYTKLGIREE 165
Cdd:COG1670   105 ATEALRALLDYAfEELGLHRVEAEVDPDNTASIRVLEKLGFRLE 148
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
79-161 5.15e-04

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 38.24  E-value: 5.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321392096  79 LAAFDQEAVVGALAAyvlpkFEQPRSEIYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYVQADYgddPAVALYT 158
Cdd:COG2153    37 LLAYDDGELVATARL-----LPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQA---HAVGFYE 108


                  ...
gi 1321392096 159 KLG 161
Cdd:COG2153   109 KLG 111
Eis COG4552
Predicted acetyltransferase [General function prediction only];
40-141 1.25e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 38.34  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321392096  40 MRAALDLFGREFGDVATYSQHQPDSDYLGNllrsktFIALAAFDQEAVVGALAAYvlpKFEQP-RSEIY----IYDLAVS 114
Cdd:COG4552    11 LDAFARLLAYAFGPEPDDEELEAYRPLLEP------GRVLGVFDDGELVGTLALY---PFTLNvGGARVpmagITGVAVA 81

                          90       100
                  ....*....|....*....|....*..
gi 1321392096 115 GEHRRQGIATALINLLKHEANALGAYV 141
Cdd:COG4552    82 PEHRRRGVARALLREALAELRERGQPL 108
PTZ00330 PTZ00330
acetyltransferase; Provisional
 87-171 1.68e-03

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 37.13  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1321392096  87 VVGALAAYVLPKFEQP-RSEIYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYVQAdygDDPAVALYTKLGIR-- 163
Cdd:PTZ00330   63 IVGTASLFVEPKFTRGgKCVGHIEDVVVDPSYRGQGLGRALISDLCEIARSSGCYKVILDC---TEDMVAFYKKLGFRac 139


                  ....*...
gi 1321392096 164 EEVMHFDI 171
Cdd:PTZ00330  140 ERQMRLDL 147
 
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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