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Conserved domains on  [gi|8346635|emb|CAB93900|]
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gentamycin acetyltransferase [Artificial vector pLoxGen4]

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 4.35e-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: 70.24  E-value: 4.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8346635     40 MRAALDLFGREFgdvaTYSQHQPDSDYLGNLLRSKTFIALAAFDQEAVVGALAAYVLPRFEQprsEIYIYDLAVSGEHRR 119
Cdd:pfam00583   1 LEALYELLSEEF----PEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPP---VGEIEGLAVAPEYRG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 8346635    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 4.35e-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: 70.24  E-value: 4.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8346635     40 MRAALDLFGREFgdvaTYSQHQPDSDYLGNLLRSKTFIALAAFDQEAVVGALAAYVLPRFEQprsEIYIYDLAVSGEHRR 119
Cdd:pfam00583   1 LEALYELLSEEF----PEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPP---VGEIEGLAVAPEYRG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 8346635    120 QGIATALINLLKHEANALGAYVIYVQADYGDDPAVALYTKLG 161
Cdd:pfam00583  74 KGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLG 115
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 93-173 7.11e-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: 7.11e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8346635   93 AYVLPRFEQPRSEIYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYVQADYGDDPAVALYTKLG--IREEVMHFD 170
Cdd:COG0456   1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGfeEVGERPNYY 80


                ...
gi 8346635  171 IDP 173
Cdd:COG0456  81 GDD 83
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 79-144 2.42e-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: 51.12  E-value: 2.42e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8346635   79 LAAFDQEAVVGALAAYvlpRFEQPRSEIYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYV 144
Cdd:cd04301   2 LVAEDDGEIVGFASLS---PDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
PRK03624 PRK03624
putative acetyltransferase; Provisional
 108-165 1.07e-06

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 45.69  E-value: 1.07e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 8346635   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 2.99e-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: 44.63  E-value: 2.99e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8346635     89 GALAAYVLPRFeqPRSEIYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYVQADYGDDPAVALYTKLGIREE 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 4.35e-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: 70.24  E-value: 4.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8346635     40 MRAALDLFGREFgdvaTYSQHQPDSDYLGNLLRSKTFIALAAFDQEAVVGALAAYVLPRFEQprsEIYIYDLAVSGEHRR 119
Cdd:pfam00583   1 LEALYELLSEEF----PEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPP---VGEIEGLAVAPEYRG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 8346635    120 QGIATALINLLKHEANALGAYVIYVQADYGDDPAVALYTKLG 161
Cdd:pfam00583  74 KGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLG 115
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 93-173 7.11e-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: 7.11e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8346635   93 AYVLPRFEQPRSEIYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYVQADYGDDPAVALYTKLG--IREEVMHFD 170
Cdd:COG0456   1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGfeEVGERPNYY 80


                ...
gi 8346635  171 IDP 173
Cdd:COG0456  81 GDD 83
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
77-161 2.29e-11

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 58.56  E-value: 2.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8346635   77 IALAAFDQEAVVGAlAAYVLPRFEQPRSEIYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYVqadYGDDPAVAL 156
Cdd:COG3153  40 LSLVAEDDGEIVGH-VALSPVDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVL---LGDPSLLPF 115


                ....*
gi 8346635  157 YTKLG 161
Cdd:COG3153 116 YERFG 120
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 79-161 5.93e-10

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 53.23  E-value: 5.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8346635     79 LAAFDQEAVVGALAAYVLPRfeqpRSEIYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYVQAdygDDPAVALYT 158
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLDD----EGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRAAAFYE 78


                  ...
gi 8346635    159 KLG 161
Cdd:pfam13508  79 KLG 81
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 57-161 1.06e-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: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8346635     57 YSQHQPDSdyLGNLLRSKTFIALAAFDQEAVVGALAAyvlprfeqpRSEIYIYDLAVSGEHRRQGIATALINLLKHEANA 136
Cdd:pfam13673  14 YEFISPEA--LRERIDQGEYFFFVAFEGGQIVGVIAL---------RDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEK 82

                          90       100
                  ....*....|....*....|....*
gi 8346635    137 LGAYVIYVQADyGDDPAVALYTKLG 161
Cdd:pfam13673  83 DGIKLSELTVN-ASPYAVPFYEKLG 106
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 79-144 2.42e-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: 51.12  E-value: 2.42e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8346635   79 LAAFDQEAVVGALAAYvlpRFEQPRSEIYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYV 144
Cdd:cd04301   2 LVAEDDGEIVGFASLS---PDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
55-161 4.20e-09

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 52.69  E-value: 4.20e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8346635   55 ATYSQHQPDSDYLGNLLRSKT---FIALAAFDQEAVVGaLAAYVLPRFEQPRSEIYIYDLAVSGEHRRQGIATALINLLK 131
Cdd:COG1247  28 ATFETEPPSEEEREAWFAAILapgRPVLVAEEDGEVVG-FASLGPFRPRPAYRGTAEESIYVDPDARGRGIGRALLEALI 106

                        90       100       110
                ....*....|....*....|....*....|
gi 8346635  132 HEANALGAYVIYVQADYGDDPAVALYTKLG 161
Cdd:COG1247 107 ERARARGYRRLVAVVLADNEASIALYEKLG 136
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
106-161 1.69e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 49.52  E-value: 1.69e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 8346635  106 IYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYVQADYGDDPAVALYTKLG 161
Cdd:COG3393  16 AEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLG 71
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 70-161 3.33e-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: 3.33e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8346635   70 LLRSKTFIAlaAFDQEAVVGALAayvLPRFEQPRseIYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYVQADYG 149
Cdd:COG0454  30 SLAGAEFIA--VDDKGEPIGFAG---LRRLDDKV--LELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDG 102

                        90
                ....*....|..
gi 8346635  150 DDPAVALYTKLG 161
Cdd:COG0454 103 NPAAIRFYERLG 114
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 81-161 3.68e-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: 46.91  E-value: 3.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8346635   81 AFDQEAVVGALAAYVLPRfeqprSEIYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYVQAdygDDPAVALYTKL 160
Cdd:COG1246  33 AEEDGEIVGCAALHPLDE-----DLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT---TSAAIHFYEKL 104


                .
gi 8346635  161 G 161
Cdd:COG1246 105 G 105
PRK03624 PRK03624
putative acetyltransferase; Provisional
 108-165 1.07e-06

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 45.69  E-value: 1.07e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 8346635   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 2.99e-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: 44.63  E-value: 2.99e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8346635     89 GALAAYVLPRFeqPRSEIYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYVQADYGDDPAVALYTKLGIREE 165
Cdd:TIGR01575  40 GKVVGYAGVQI--VLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEI 114
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 53-165 2.17e-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: 39.98  E-value: 2.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8346635   53 DVATYSQHQPDS-----DYLGNLLR---SKTFIALAAFDQE--AVVGALAAYVLPRfEQPRSEIYIYdlaVSGEHRRQGI 122
Cdd:COG1670  29 EVARYLPGPPYSleearAWLERLLAdwaDGGALPFAIEDKEdgELIGVVGLYDIDR-ANRSAEIGYW---LAPAYWGKGY 104

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 8346635  123 ATALINLLKHEA-NALGAYVIYVQADYGDDPAVALYTKLGIREE 165
Cdd:COG1670 105 ATEALRALLDYAfEELGLHRVEAEVDPDNTASIRVLEKLGFRLE 148
Eis COG4552
Predicted acetyltransferase [General function prediction only];
40-141 4.41e-04

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 39.88  E-value: 4.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8346635   40 MRAALDLFGREFGDVATYSQHQPDSDYLGNllrsktFIALAAFDQEAVVGALAAYvlpRFEQP-RSEIY----IYDLAVS 114
Cdd:COG4552  11 LDAFARLLAYAFGPEPDDEELEAYRPLLEP------GRVLGVFDDGELVGTLALY---PFTLNvGGARVpmagITGVAVA 81

                        90       100
                ....*....|....*....|....*..
gi 8346635  115 GEHRRQGIATALINLLKHEANALGAYV 141
Cdd:COG4552  82 PEHRRRGVARALLREALAELRERGQPL 108
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
79-161 5.69e-04

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 38.24  E-value: 5.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8346635   79 LAAFDQEAVVGALaayvlpR-FEQPRSEIYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYVQADYgddPAVALY 157
Cdd:COG2153  37 LLAYDDGELVATA------RlLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQA---HAVGFY 107


                ....
gi 8346635  158 TKLG 161
Cdd:COG2153 108 EKLG 111
PTZ00330 PTZ00330
acetyltransferase; Provisional
 87-171 6.55e-03

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 35.20  E-value: 6.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8346635    87 VVGALAAYVLPRFEQP-RSEIYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYVQAdygDDPAVALYTKLGIR-- 163
Cdd:PTZ00330  63 IVGTASLFVEPKFTRGgKCVGHIEDVVVDPSYRGQGLGRALISDLCEIARSSGCYKVILDC---TEDMVAFYKKLGFRac 139


                 ....*...
gi 8346635   164 EEVMHFDI 171
Cdd:PTZ00330 140 ERQMRLDL 147
PRK07757 PRK07757
N-acetyltransferase;
81-138 7.94e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 35.17  E-value: 7.94e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 8346635    81 AFDQEAVVGALAAYVL-PRFEQPRSeiyiydLAVSGEHRRQGIATALINLLKHEANALG 138
Cdd:PRK07757  46 AEEEGEIVGCCALHILwEDLAEIRS------LAVSEDYRGQGIGRMLVEACLEEARELG 98
 
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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