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Conserved domains on  [gi|505180206|ref|WP_015367308|]
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MULTISPECIES: GNAT family N-acetyltransferase [Klebsiella]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11441181)

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
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
2-153 3.43e-32

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 112.40  E-value: 3.43e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180206   2 SITIRQARPDDASAIYNMIYE-----LAVYEKAPQEVvttpdEIRETLFGD--DSKTEALICEIDGKTAGYAvFFTSYST 74
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEaiaegTATFETEPPSE-----EEREAWFAAilAPGRPVLVAEEDGEVVGFA-SLGPFRP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180206  75 WLGRNGIYMEDLYISPDYRGQGAGRALLKTIARYAVARRCGRLEWSVLDWNQPAIDFYLSIGAAAQSEWIR-YRLDGEAL 153
Cdd:COG1247   75 RPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEvGFKFGRWL 154
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
2-153 3.43e-32

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 112.40  E-value: 3.43e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180206   2 SITIRQARPDDASAIYNMIYE-----LAVYEKAPQEVvttpdEIRETLFGD--DSKTEALICEIDGKTAGYAvFFTSYST 74
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEaiaegTATFETEPPSE-----EEREAWFAAilAPGRPVLVAEEDGEVVGFA-SLGPFRP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180206  75 WLGRNGIYMEDLYISPDYRGQGAGRALLKTIARYAVARRCGRLEWSVLDWNQPAIDFYLSIGAAAQSEWIR-YRLDGEAL 153
Cdd:COG1247   75 RPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEvGFKFGRWL 154
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 17-136 8.69e-19

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: 76.79  E-value: 8.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180206   17 YNMIYELavYEKAPQEVVTTPDEIRETLFGDDSKTEALICEIDGKTAGYAVFFTSYSTWlgrNGIYMEDLYISPDYRGQG 96
Cdd:pfam00583   1 LEALYEL--LSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEP---PVGEIEGLAVAPEYRGKG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 505180206   97 AGRALLKTIARYAVARRCGRLEWSVLDWNQPAIDFYLSIG 136
Cdd:pfam00583  76 IGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLG 115
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 54-118 1.08e-10

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: 54.20  E-value: 1.08e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505180206  54 LICEIDGKTAGYAVFftsYSTWLGRNGIYMEDLYISPDYRGQGAGRALLKTIARYAVARRCGRLE 118
Cdd:cd04301    2 LVAEDDGEIVGFASL---SPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 51-136 3.76e-07

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: 46.55  E-value: 3.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180206   51 TEALICEIDGKTAGYAVfftsysTWLGRNGIYMEDLYISPDYRGQGAGRALLKTIARYAVARRCGRLEWSVLDWNQPAID 130
Cdd:TIGR01575  31 LCYLLARIGGKVVGYAG------VQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQA 104


                  ....*.
gi 505180206  131 FYLSIG 136
Cdd:TIGR01575 105 LYKKLG 110
PTZ00330 PTZ00330
acetyltransferase; Provisional
 77-148 8.06e-07

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 45.99  E-value: 8.06e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505180206  77 GRNGIYMEDLYISPDYRGQGAGRALLKTIARYAVARRCGRLewsVLDWNQPAIDFYLSIGAAAQSEWIRYRL 148
Cdd:PTZ00330  79 GKCVGHIEDVVVDPSYRGQGLGRALISDLCEIARSSGCYKV---ILDCTEDMVAFYKKLGFRACERQMRLDL 147
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
2-153 3.43e-32

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 112.40  E-value: 3.43e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180206   2 SITIRQARPDDASAIYNMIYE-----LAVYEKAPQEVvttpdEIRETLFGD--DSKTEALICEIDGKTAGYAvFFTSYST 74
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEaiaegTATFETEPPSE-----EEREAWFAAilAPGRPVLVAEEDGEVVGFA-SLGPFRP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180206  75 WLGRNGIYMEDLYISPDYRGQGAGRALLKTIARYAVARRCGRLEWSVLDWNQPAIDFYLSIGAAAQSEWIR-YRLDGEAL 153
Cdd:COG1247   75 RPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEvGFKFGRWL 154
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 3-150 1.78e-23

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 89.34  E-value: 1.78e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180206   3 ITIRQARPDDASAIynmiyelavyekapqevvTTPDEIRETLF---GDDSKTEALICEIDGKTAGYAVFFTsystwLGRN 79
Cdd:COG0454    1 MSIRKATPEDINFI------------------LLIEALDAELKameGSLAGAEFIAVDDKGEPIGFAGLRR-----LDDK 57

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505180206  80 GIYMEDLYISPDYRGQGAGRALLKTIARYAVARRCGRLEWSVLDWNQPAIDFYLSIGAAAQSEWIRYRLDG 150
Cdd:COG0454   58 VLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIERYVAYVGGE 128
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 17-136 8.69e-19

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: 76.79  E-value: 8.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180206   17 YNMIYELavYEKAPQEVVTTPDEIRETLFGDDSKTEALICEIDGKTAGYAVFFTSYSTWlgrNGIYMEDLYISPDYRGQG 96
Cdd:pfam00583   1 LEALYEL--LSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEP---PVGEIEGLAVAPEYRGKG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 505180206   97 AGRALLKTIARYAVARRCGRLEWSVLDWNQPAIDFYLSIG 136
Cdd:pfam00583  76 IGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLG 115
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 64-151 2.29e-17

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 72.38  E-value: 2.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180206  64 GYAVFFTSYstwlGRNGIYMEDLYISPDYRGQGAGRALLKTIARYAVARRCGRLEWSVLDWNQPAIDFYLSIGAAAQSEW 143
Cdd:COG0456    1 GFALLGLVD----GGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGER 76


                 ....*...
gi 505180206 144 IRYRLDGE 151
Cdd:COG0456   77 PNYYGDDA 84
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
5-153 1.43e-15

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 68.96  E-value: 1.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180206   5 IRQARPDDASAIYNmIYELAVYEKAPQEVVttpDEIREtlfgDDSKTEALICEIDGKTAGYaVFFTSYSTWLGRNGIYME 84
Cdd:COG3153    1 IRPATPEDAEAIAA-LLRAAFGPGREAELV---DRLRE----DPAAGLSLVAEDDGEIVGH-VALSPVDIDGEGPALLLG 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505180206  85 DLYISPDYRGQGAGRALLKTIARYAVARRCGRLewsVLDWNQPAIDFYLSIGAAAQSEWIRYRLDGEAL 153
Cdd:COG3153   72 PLAVDPEYRGQGIGRALMRAALEAARERGARAV---VLLGDPSLLPFYERFGFRPAGELGLTLGPDEVF 137
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 3-136 6.13e-15

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: 66.94  E-value: 6.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180206   3 ITIRQARPDDASAIYNMIYELAVYEKApqevvttpdeiretlfgddskTEALICEIDGKTAGYAVFFTsYSTWLGrngiY 82
Cdd:COG1246    1 MTIRPATPDDVPAILELIRPYALEEEI---------------------GEFWVAEEDGEIVGCAALHP-LDEDLA----E 54

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 505180206  83 MEDLYISPDYRGQGAGRALLKTIARYAVARRCGRLEwsvLDWNQPAIDFYLSIG 136
Cdd:COG1246   55 LRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLF---LLTTSAAIHFYEKLG 105
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 54-136 1.79e-11

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 56.69  E-value: 1.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180206   54 LICEIDGKTAGYAVFFTSYstwlGRNGIYMEDLYISPDYRGQGAGRALLKTIARYAVARRCGRLEwsvLDWNQPAIDFYL 133
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLD----DEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLE---LETTNRAAAFYE 78


                  ...
gi 505180206  134 SIG 136
Cdd:pfam13508  79 KLG 81
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
67-149 5.42e-11

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 55.69  E-value: 5.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180206  67 VFFTSYSTWLGRNGiYMEDLYISPDYRGQGAGRALLKTIARYAVARRCGRLEWSVLDWNQPAIDFYLSIGAAAQSEWIRY 146
Cdd:COG3393    3 VAMAGVRAESPGVA-EISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEYATV 81


                 ...
gi 505180206 147 RLD 149
Cdd:COG3393   82 LFR 84
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 54-118 1.08e-10

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: 54.20  E-value: 1.08e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505180206  54 LICEIDGKTAGYAVFftsYSTWLGRNGIYMEDLYISPDYRGQGAGRALLKTIARYAVARRCGRLE 118
Cdd:cd04301    2 LVAEDDGEIVGFASL---SPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 36-146 6.73e-10

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: 6.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180206   36 TPDEIRETLFGDDSKTeaLICEIDGKTAGYAVFftsystwlgRNGIYMEDLYISPDYRGQGAGRALLKTIARYAVARRCG 115
Cdd:pfam13673  18 SPEALRERIDQGEYFF--FVAFEGGQIVGVIAL---------RDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIK 86

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 505180206  116 RLEWSVldwN-QP-AIDFYLSIGAAAQSE-----WIRY 146
Cdd:pfam13673  87 LSELTV---NaSPyAVPFYEKLGFRATGPeqefnGIRF 121
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 3-136 5.52e-09

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: 52.31  E-value: 5.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180206   3 ITIRQARPDDASAIYNMIYELAVYEKAPqEVVTTPDEIRETLfgddskTEALICEIDGKTAGYAVFFTSYSTWLGRNGIY 82
Cdd:COG1670    8 LRLRPLRPEDAEALAELLNDPEVARYLP-GPPYSLEEARAWL------ERLLADWADGGALPFAIEDKEDGELIGVVGLY 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505180206  83 MED---------LYISPDYRGQGAGRALLKTIARYAVAR-RCGRLEWSVLDWNQPAIDFYLSIG 136
Cdd:COG1670   81 DIDranrsaeigYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLG 144
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
46-142 6.52e-08

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 48.64  E-value: 6.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180206  46 GDDSKTEALICEIDGKTAGYA-VFFTSYSTW-LGRngiymedLYISPDYRGQGAGRALLKTIARYAVARRCGRLewsVLD 123
Cdd:COG2153   29 GKDEDARHLLAYDDGELVATArLLPPGDGEAkIGR-------VAVLPEYRGQGLGRALMEAAIEEARERGARRI---VLS 98

                         90
                 ....*....|....*....
gi 505180206 124 WNQPAIDFYLSIGAAAQSE 142
Cdd:COG2153   99 AQAHAVGFYEKLGFVPVGE 117
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 51-136 3.76e-07

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: 46.55  E-value: 3.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180206   51 TEALICEIDGKTAGYAVfftsysTWLGRNGIYMEDLYISPDYRGQGAGRALLKTIARYAVARRCGRLEWSVLDWNQPAID 130
Cdd:TIGR01575  31 LCYLLARIGGKVVGYAG------VQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQA 104


                  ....*.
gi 505180206  131 FYLSIG 136
Cdd:TIGR01575 105 LYKKLG 110
PTZ00330 PTZ00330
acetyltransferase; Provisional
 77-148 8.06e-07

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 45.99  E-value: 8.06e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505180206  77 GRNGIYMEDLYISPDYRGQGAGRALLKTIARYAVARRCGRLewsVLDWNQPAIDFYLSIGAAAQSEWIRYRL 148
Cdd:PTZ00330  79 GKCVGHIEDVVVDPSYRGQGLGRALISDLCEIARSSGCYKV---ILDCTEDMVAFYKKLGFRACERQMRLDL 147
PRK10514 PRK10514
putative acetyltransferase; Provisional
 3-136 1.39e-04

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 39.60  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180206   3 ITIRQARPDDASAIYNmIYELAVyekapqevvttpDEIRETLFGDDSKtealicEIDGKTAGyavFFTSYSTWLGRN--- 79
Cdd:PRK10514   2 ISIRRSRHEEGERLVA-IWRRSV------------DATHDFLSAEDRA------EIEELVRS---FLPEAPLWVAVDerd 59

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505180206  80 ---------GIYMEDLYISPDYRGQGAGRALLktiaRYAVARRcGRLEWSVLDWNQPAIDFYLSIG 136
Cdd:PRK10514  60 qpvgfmllsGGHMEALFVDPDVRGCGVGRMLV----EHALSLH-PELTTDVNEQNEQAVGFYKKMG 120
PRK07757 PRK07757
N-acetyltransferase;
3-111 4.68e-04

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 38.25  E-value: 4.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180206   3 ITIRQARPDDASAIYNMIyelAVYEKAPQEVVTTPDEIRETL--FgddskteaLICEIDGKTAGYAVFFtsystwlgrng 80
Cdd:PRK07757   2 MEIRKARLSDVKAIHALI---NVYAKKGLMLPRSLDELYENIrdF--------YVAEEEGEIVGCCALH----------- 59

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 505180206  81 IYMEDL------YISPDYRGQGAGRALLKTIARYAVA 111
Cdd:PRK07757  60 ILWEDLaeirslAVSEDYRGQGIGRMLVEACLEEARE 96
PRK03624 PRK03624
putative acetyltransferase; Provisional
 86-140 7.42e-04

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 37.60  E-value: 7.42e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 505180206  86 LYISPDYRGQGAGRALLKTIARYAVARRCGRLEWSVLDWNQPAIDFYLSIGAAAQ 140
Cdd:PRK03624  74 LAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQ 128
 
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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