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MULTISPECIES: GNAT family N-acetyltransferase [Bacillus]

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];
7-165 5.88e-54

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 168.25  E-value: 5.88e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495618766   7 RMATEDDLKEIVDIYNSTIASREVTADTEPVTVEDRRQWFLNH-SEKRPLYVKtDEEGNIYGWLSFETFYGRPAYNGTVE 85
Cdd:COG1247    5 RPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAIlAPGRPVLVA-EEDGEVVGFASLGPFRPRPAYRGTAE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495618766  86 MSIYLNQNYRGKGLGSLFLQEALELAPSLGIRTLLAFIFGHNEASIKLFKKHGFETWGHLPRIAEMDGNRYDLDILGKEL 165
Cdd:COG1247   84 ESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQKRL 163
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
7-165 5.88e-54

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 168.25  E-value: 5.88e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495618766   7 RMATEDDLKEIVDIYNSTIASREVTADTEPVTVEDRRQWFLNH-SEKRPLYVKtDEEGNIYGWLSFETFYGRPAYNGTVE 85
Cdd:COG1247    5 RPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAIlAPGRPVLVA-EEDGEVVGFASLGPFRPRPAYRGTAE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495618766  86 MSIYLNQNYRGKGLGSLFLQEALELAPSLGIRTLLAFIFGHNEASIKLFKKHGFETWGHLPRIAEMDGNRYDLDILGKEL 165
Cdd:COG1247   84 ESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQKRL 163
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 17-139 9.66e-13

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: 61.38  E-value: 9.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495618766   17 IVDIYNSTIASREVTADTEPVtveDRRQWFLNHSEKRPLYVKtdEEGNIYGWLSFETFYGRPAYngTVEMSIYLNQNYRG 96
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPL---DLLEDWDEDASEGFFVAE--EDGELVGFASLSIIDDEPPV--GEIEGLAVAPEYRG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 495618766   97 KGLGSLFLQEALELAPSLGIRTLLAFIFGHNEASIKLFKKHGF 139
Cdd:pfam00583  74 KGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 60-119 5.32e-05

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: 39.18  E-value: 5.32e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495618766  60 DEEGNIYGWLSFeTFYGRPAYNGTVEMsIYLNQNYRGKGLGSLFLQEALELAPSLGIRTL 119
Cdd:cd04301    5 EDDGEIVGFASL-SPDGSGGDTAYIGD-LAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 87-140 5.14e-04

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: 38.08  E-value: 5.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 495618766   87 SIYLNQNYRGKGLGSLFLQEALELAPSLGIRTLLAFIFGHNEASIKLFKKHGFE 140
Cdd:TIGR01575  59 NIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFN 112
PRK10140 PRK10140
N-acetyltransferase;
62-157 6.77e-04

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 38.04  E-value: 6.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495618766  62 EGNIYGWLSFETfYGRPAYNGTVEMSIYLNQNYRGKGLGSLFLQEALELAPS-LGIRTLLAFIFGHNEASIKLFKKHGFE 140
Cdd:PRK10140  59 DGDVVGHLTIDV-QQRPRRSHVADFGICVDSRWKNRGVASALMREMIEMCDNwLRVDRIELTVFVDNAPAIKVYKKYGFE 137

                         90
                 ....*....|....*..
gi 495618766 141 TWGHLPRIAEMDGNRYD 157
Cdd:PRK10140 138 IEGTGKKYALRNGEYVD 154
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
7-165 5.88e-54

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 168.25  E-value: 5.88e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495618766   7 RMATEDDLKEIVDIYNSTIASREVTADTEPVTVEDRRQWFLNH-SEKRPLYVKtDEEGNIYGWLSFETFYGRPAYNGTVE 85
Cdd:COG1247    5 RPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAIlAPGRPVLVA-EEDGEVVGFASLGPFRPRPAYRGTAE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495618766  86 MSIYLNQNYRGKGLGSLFLQEALELAPSLGIRTLLAFIFGHNEASIKLFKKHGFETWGHLPRIAEMDGNRYDLDILGKEL 165
Cdd:COG1247   84 ESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQKRL 163
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 7-162 6.85e-19

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: 78.50  E-value: 6.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495618766   7 RMATEDDLKEIVDIYNStiasREVTA--DTEPVTVEDRRQWFLNHSEKR------PLYVKTDEEGNIYGWLSFetfYGRP 78
Cdd:COG1670   11 RPLRPEDAEALAELLND----PEVARylPGPPYSLEEARAWLERLLADWadggalPFAIEDKEDGELIGVVGL---YDID 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495618766  79 AYNGTVEMSIYLNQNYRGKGLGSLFLQEALELAPS-LGIRTLLAFIFGHNEASIKLFKKHGFETWGHLPRIAEMDGNRYD 157
Cdd:COG1670   84 RANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEeLGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRD 163


                 ....*
gi 495618766 158 LDILG 162
Cdd:COG1670  164 HVLYS 168
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 17-139 9.66e-13

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: 61.38  E-value: 9.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495618766   17 IVDIYNSTIASREVTADTEPVtveDRRQWFLNHSEKRPLYVKtdEEGNIYGWLSFETFYGRPAYngTVEMSIYLNQNYRG 96
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPL---DLLEDWDEDASEGFFVAE--EDGELVGFASLSIIDDEPPV--GEIEGLAVAPEYRG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 495618766   97 KGLGSLFLQEALELAPSLGIRTLLAFIFGHNEASIKLFKKHGF 139
Cdd:pfam00583  74 KGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 7-140 1.62e-12

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 61.21  E-value: 1.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495618766    7 RMATEDDLKEIVDIYnstiASREVT--ADTEPVTVEDRRQWFLNHSEKRPL-----YVKTDEEGNIYGWLSFetfYGRPA 79
Cdd:pfam13302   5 RPLTEEDAEALFELL----SDPEVMryGVPWPLTLEEAREWLARIWAADEAergygWAIELKDTGFIGSIGL---YDIDG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495618766   80 YNGTVEMSIYLNQNYRGKGLGSLFLQEALELA-PSLGIRTLLAFIFGHNEASIKLFKKHGFE 140
Cdd:pfam13302  78 EPERAELGYWLGPDYWGKGYATEAVRALLEYAfEELGLPRLVARIDPENTASRRVLEKLGFK 139
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 87-147 7.41e-10

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 53.12  E-value: 7.41e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495618766  87 SIYLNQNYRGKGLGSLFLQEALELAPSLGIRTLLAFIFGHNEASIKLFKKHGFETWGHLPR 147
Cdd:COG0456   18 DLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPN 78
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 7-140 2.12e-09

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: 52.69  E-value: 2.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495618766   7 RMATEDDLKEIVDIYNSTIASrevtadtepvtvEDRRQWFLnhsekrplyvkTDEEGNIYGWLSFETFYGrpaynGTVEM 86
Cdd:COG1246    4 RPATPDDVPAILELIRPYALE------------EEIGEFWV-----------AEEDGEIVGCAALHPLDE-----DLAEL 55

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495618766  87 -SIYLNQNYRGKGLGSLFLQEALELAPSLGIRTLLAFIfghNEASIKLFKKHGFE 140
Cdd:COG1246   56 rSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT---TSAAIHFYEKLGFE 107
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 88-156 3.12e-09

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 52.36  E-value: 3.12e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495618766  88 IYLNQNYRGKGLGSLFLQEALELAPSLGIRTLLAFIFGHNEASIKLFKKHGFEtwgHLPRIAEMDGNRY 156
Cdd:COG0454   64 LYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFK---EIERYVAYVGGEF 129
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
7-157 2.13e-07

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 47.75  E-value: 2.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495618766    7 RMATEDDLKEIVDIYNSTIASREVTADTEPVTVEDRRQWFLNHSEKRPLYVKTDEEGNIYGWLSFETFygRPAYNGTVEM 86
Cdd:pfam13420   2 RALTQNDLKEIRRWYAEDRVNPAFTQEYAHSSIEEFETFLAAYLSPGEIVFGVAESDRLIGYATLRQF--DYVKTHKAEL 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495618766   87 SIYLNQNyRGKGLGSLFLQEALELAPS-LGIRTLLAFIFGHNEASIKLFKKHGFETWGHLPRIAEMDGNRYD 157
Cdd:pfam13420  80 SFYVVKN-NDEGINRELINAIIQYARKnQNIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKKNGRWID 150
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 60-140 1.43e-06

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 43.98  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495618766   60 DEEGNIYGWLSFETFYGRPAYngtVEMSIYLNQNYRGKGLGSLFLQEALELAPSLGIRTLLAFifgHNEASIKLFKKHGF 139
Cdd:pfam13508   9 EDDGKIVGFAALLPLDDEGAL---AELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELE---TTNRAAAFYEKLGF 82


                  .
gi 495618766  140 E 140
Cdd:pfam13508  83 E 83
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
75-143 6.84e-06

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 42.20  E-value: 6.84e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495618766  75 YGRPAYNGTVEMSIYLNQNYRGKGLGSLFLQEALELAPSLGIRTLLAFIFGHNEASIKLFKKHGFETWG 143
Cdd:COG3393    8 VRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVG 76
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
7-140 1.05e-05

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 42.77  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495618766   7 RMATEDDLKEIVDIYNSTIASrevtaDTEPVTVEDrrqwfLNHSEKRPLYVKTDEEGNIYGWLSFETFYGRPAYN-GTVE 85
Cdd:COG3153    2 RPATPEDAEAIAALLRAAFGP-----GREAELVDR-----LREDPAAGLSLVAEDDGEIVGHVALSPVDIDGEGPaLLLG 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495618766  86 MsIYLNQNYRGKGLGSLFLQEALELAPSLGIRTLlaFIFGHnEASIKLFKKHGFE 140
Cdd:COG3153   72 P-LAVDPEYRGQGIGRALMRAALEAARERGARAV--VLLGD-PSLLPFYERFGFR 122
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 60-119 5.32e-05

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: 39.18  E-value: 5.32e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495618766  60 DEEGNIYGWLSFeTFYGRPAYNGTVEMsIYLNQNYRGKGLGSLFLQEALELAPSLGIRTL 119
Cdd:cd04301    5 EDDGEIVGFASL-SPDGSGGDTAYIGD-LAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
GNAT_acetyltran pfam12746
GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance ...
 80-140 2.75e-04

GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance proteins, whereas others are listed as being GNAT acetyltransferases. The family has similarities to the GNAT acetyltransferase family.


Pssm-ID: 403833  Cd Length: 239  Bit Score: 39.95  E-value: 2.75e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495618766   80 YNGTVEMSIYLNQNYRGKGL----GSLFLQEALE--LAPSLGirtllafifGHNEASIKLFKKHGFE 140
Cdd:pfam12746 174 YEGGIEIEIDTHPDYRGKGLaticAAALILECLKrgLYPSWD---------AHNEASVALAEKLGYE 231
COG3818 COG3818
Predicted N-acetyltransferase, GNAT superfamily [General function prediction only];
1-140 3.73e-04

Predicted N-acetyltransferase, GNAT superfamily [General function prediction only];


Pssm-ID: 443030 [Multi-domain]  Cd Length: 168  Bit Score: 38.76  E-value: 3.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495618766   1 MVKTFN-RMATEDDLKEIVDIYNStiasrEVTAdTEPVTvEDRRQWFLNHSEkrpLYVKTDEEGNIYGWL-SFE--TFYG 76
Cdd:COG3818    1 MTNPIViRDAREHDLDAVLALNNA-----AVPA-VSPLD-AARLARLHEQAA---YARVAEVDGEVAGFLlAFGpgADYD 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495618766  77 RPAY---NGTVEMSIYLN-----QNYRGKGLGSLFLQEALELAPSLGIRTLLA--FIFGHNEASIKLFKKHGFE 140
Cdd:COG3818   71 SPNYrwfAERYDNFLYIDrivvaPSARGRGLGRALYADVFSYARARGVPRVTCevNLEPPNPGSLAFHARLGFR 144
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 87-140 5.14e-04

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: 38.08  E-value: 5.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 495618766   87 SIYLNQNYRGKGLGSLFLQEALELAPSLGIRTLLAFIFGHNEASIKLFKKHGFE 140
Cdd:TIGR01575  59 NIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFN 112
PRK10140 PRK10140
N-acetyltransferase;
62-157 6.77e-04

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 38.04  E-value: 6.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495618766  62 EGNIYGWLSFETfYGRPAYNGTVEMSIYLNQNYRGKGLGSLFLQEALELAPS-LGIRTLLAFIFGHNEASIKLFKKHGFE 140
Cdd:PRK10140  59 DGDVVGHLTIDV-QQRPRRSHVADFGICVDSRWKNRGVASALMREMIEMCDNwLRVDRIELTVFVDNAPAIKVYKKYGFE 137

                         90
                 ....*....|....*..
gi 495618766 141 TWGHLPRIAEMDGNRYD 157
Cdd:PRK10140 138 IEGTGKKYALRNGEYVD 154
PRK10514 PRK10514
putative acetyltransferase; Provisional
 7-163 3.13e-03

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 36.13  E-value: 3.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495618766   7 RMATEDDLKEIVDIYnstiaSREVTADTEPVTVEDRRQW------FLNHSekrPLYVKTDEEGNIYGWLSFEtfygrpay 80
Cdd:PRK10514   5 RRSRHEEGERLVAIW-----RRSVDATHDFLSAEDRAEIeelvrsFLPEA---PLWVAVDERDQPVGFMLLS-------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495618766  81 NGTVEmSIYLNQNYRGKGLGSLFLQEALELAPSLGIRtllafIFGHNEASIKLFKKHGFETWGhlpriaemdgnRYDLDI 160
Cdd:PRK10514  69 GGHME-ALFVDPDVRGCGVGRMLVEHALSLHPELTTD-----VNEQNEQAVGFYKKMGFKVTG-----------RSEVDD 131


                 ...
gi 495618766 161 LGK 163
Cdd:PRK10514 132 QGR 134
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
92-143 4.00e-03

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 35.55  E-value: 4.00e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495618766  92 QNYRGKGLGSLFLQEALELAPSLGIRTLlafIFGHNEASIKLFKKHGFETWG 143
Cdd:COG2153   68 PEYRGQGLGRALMEAAIEEARERGARRI---VLSAQAHAVGFYEKLGFVPVG 116
 
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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