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Conserved domains on  [gi|24584063|ref|NP_723798|]
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N(alpha)-acetyltransferase 20 B, isoform A [Drosophila melanogaster]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11418877)

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
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 55-159 1.48e-16

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 71.61  E-value: 1.48e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584063  55 GFILGTRVEDAtesfgdaktmtwNHGHISALAVAQDYRKLGLGTRLLTTVRDMMDRQKDFYIDLFVREKNTIAIGLYESL 134
Cdd:COG0456   1 GFALLGLVDGG------------DEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKL 68

                        90       100
                ....*....|....*....|....*
gi 24584063 135 GYVKYRWIPKFYADDHgYEMRLPLS 159
Cdd:COG0456  69 GFEEVGERPNYYGDDA-LVMEKELA 92
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 55-159 1.48e-16

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 71.61  E-value: 1.48e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584063  55 GFILGTRVEDAtesfgdaktmtwNHGHISALAVAQDYRKLGLGTRLLTTVRDMMDRQKDFYIDLFVREKNTIAIGLYESL 134
Cdd:COG0456   1 GFALLGLVDGG------------DEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKL 68

                        90       100
                ....*....|....*....|....*
gi 24584063 135 GYVKYRWIPKFYADDHgYEMRLPLS 159
Cdd:COG0456  69 GFEEVGERPNYYGDDA-LVMEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 9-136 1.67e-12

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 61.38  E-value: 1.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584063     9 LEDLFKFNNIVMDPLAEVYSLPFLLPKILEHPELVLAADApDNSLMGFILGTRVEDatesfgdaktmTWNHGHISALAVA 88
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEE-DGELVGFASLSIIDD-----------EPPVGEIEGLAVA 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 24584063    89 QDYRKLGLGTRLLTTVRDMMDRQKDFYIDLFVREKNTIAIGLYESLGY 136
Cdd:pfam00583  69 PEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 75-148 1.32e-11

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: 59.65  E-value: 1.32e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24584063    75 MTWNHGHISALAVAQDYRKLGLGTRLLttvRDMMDRQKDF---YIDLFVREKNTIAIGLYESLGYVKYRWIPKFYAD 148
Cdd:TIGR01575  50 IVLDEAHILNIAVKPEYQGQGIGRALL---RELIDEAKGRgvnEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPD 123
PRK03624 PRK03624
putative acetyltransferase; Provisional
 40-136 1.39e-06

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 46.08  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584063   40 PELVLAADAPDN---SLMGFILGTRvedatesfgdaktmtwnhGHISALAVAQDYRKLGLGTRLLTTVRDMMDRQKDFYI 116
Cdd:PRK03624  44 PSLFLVAEVGGEvvgTVMGGYDGHR------------------GWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKI 105

                         90       100
                 ....*....|....*....|
gi 24584063  117 DLFVREKNTIAIGLYESLGY 136
Cdd:PRK03624 106 NLQVREDNDAVLGFYEALGY 125
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 50-118 7.88e-04

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 36.48  E-value: 7.88e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24584063  50 DNSLMGFILGTRVEDatesfgdaktmTWNHGHISALAVAQDYRKLGLGTRLLTTVRDMMDRQKDFYIDL 118
Cdd:cd04301   7 DGEIVGFASLSPDGS-----------GGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 55-159 1.48e-16

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 71.61  E-value: 1.48e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584063  55 GFILGTRVEDAtesfgdaktmtwNHGHISALAVAQDYRKLGLGTRLLTTVRDMMDRQKDFYIDLFVREKNTIAIGLYESL 134
Cdd:COG0456   1 GFALLGLVDGG------------DEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKL 68

                        90       100
                ....*....|....*....|....*
gi 24584063 135 GYVKYRWIPKFYADDHgYEMRLPLS 159
Cdd:COG0456  69 GFEEVGERPNYYGDDA-LVMEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 9-136 1.67e-12

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 61.38  E-value: 1.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584063     9 LEDLFKFNNIVMDPLAEVYSLPFLLPKILEHPELVLAADApDNSLMGFILGTRVEDatesfgdaktmTWNHGHISALAVA 88
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEE-DGELVGFASLSIIDD-----------EPPVGEIEGLAVA 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 24584063    89 QDYRKLGLGTRLLTTVRDMMDRQKDFYIDLFVREKNTIAIGLYESLGY 136
Cdd:pfam00583  69 PEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 75-148 1.32e-11

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: 59.65  E-value: 1.32e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24584063    75 MTWNHGHISALAVAQDYRKLGLGTRLLttvRDMMDRQKDF---YIDLFVREKNTIAIGLYESLGYVKYRWIPKFYAD 148
Cdd:TIGR01575  50 IVLDEAHILNIAVKPEYQGQGIGRALL---RELIDEAKGRgvnEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPD 123
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
68-142 1.39e-09

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 52.99  E-value: 1.39e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24584063  68 SFGDAKTMTWNHGHISALAVAQDYRKLGLGTRLLTTVRDMMDRQKDFYIDLFVREKNTIAIGLYESLGYVKYRWI 142
Cdd:COG3393   4 AMAGVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEY 78
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 37-159 1.87e-08

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 51.21  E-value: 1.87e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584063  37 LEHPELVLAADApDNSLMGFILGTRVEDatesfgdaktmtwNHGHISALAVAQDYRKLGLGTRLLTTVRDMMdRQKDF-Y 115
Cdd:COG0454  30 SLAGAEFIAVDD-KGEPIGFAGLRRLDD-------------KVLELKRLYVLPEYRGKGIGKALLEALLEWA-RERGCtA 94

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 24584063 116 IDLFVREKNTIAIGLYESLGYVKyrwIPKFYADD-HGYEMRLPLS 159
Cdd:COG0454  95 LELDTLDGNPAAIRFYERLGFKE---IERYVAYVgGEFEKELSLS 136
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 78-137 3.49e-08

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: 49.96  E-value: 3.49e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584063    78 NHGHISALAVAQDYRKLGLGTRLLTTVRDMMDRQKDFYIDLFVREKNTiAIGLYESLGYV 137
Cdd:pfam13673  50 DRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNASPY-AVPFYEKLGFR 108
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
78-159 1.64e-07

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 48.26  E-value: 1.64e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584063  78 NHGHISALAVAQDYRKLGLGTRLLTTVRDMMDRQKDFYIDLFVReknTIAIGLYESLGYVKYRwiPKFyaDDHG---YEM 154
Cdd:COG2153  57 GEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQ---AHAVGFYEKLGFVPVG--EEF--LEAGiphIDM 129


                ....*
gi 24584063 155 RLPLS 159
Cdd:COG2153 130 RKPLS 134
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 50-138 2.92e-07

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 46.68  E-value: 2.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584063    50 DNSLMGFILGTRVEDATesfgdaktmtwnHGHISALAVAQDYRKLGLGTRLLTTVRDMMDRQKDFYIDLFVREKntiAIG 129
Cdd:pfam13508  11 DGKIVGFAALLPLDDEG------------ALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNR---AAA 75


                  ....*....
gi 24584063   130 LYESLGYVK 138
Cdd:pfam13508  76 FYEKLGFEE 84
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
39-158 9.83e-07

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 46.62  E-value: 9.83e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584063  39 HPELVLAADApDNSLMGFILGTRVEDATESfgdaktmtwNHGHISALAVAQDYRKLGLGTRLLTTVRDMMDRQKDFYIDL 118
Cdd:COG3153  37 AAGLSLVAED-DGEIVGHVALSPVDIDGEG---------PALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVL 106

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 24584063 119 FVREKNtiaIGLYESLGYVKYRWIPKFYADDHGYeMRLPL 158
Cdd:COG3153 107 LGDPSL---LPFYERFGFRPAGELGLTLGPDEVF-LAKEL 142
PRK03624 PRK03624
putative acetyltransferase; Provisional
 40-136 1.39e-06

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 46.08  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584063   40 PELVLAADAPDN---SLMGFILGTRvedatesfgdaktmtwnhGHISALAVAQDYRKLGLGTRLLTTVRDMMDRQKDFYI 116
Cdd:PRK03624  44 PSLFLVAEVGGEvvgTVMGGYDGHR------------------GWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKI 105

                         90       100
                 ....*....|....*....|
gi 24584063  117 DLFVREKNTIAIGLYESLGY 136
Cdd:PRK03624 106 NLQVREDNDAVLGFYEALGY 125
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 80-140 1.80e-06

FR47-like protein; The members of this family are similar to the C-terminal region of the D. melanogaster hypothetical protein FR47. This protein has been found to consist of two N-acyltransferase-like domains swapped with the C-terminal strands.


Pssm-ID: 117022 [Multi-domain]  Cd Length: 86  Bit Score: 44.63  E-value: 1.80e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24584063    80 GHISALAVAQDYRKLGLGTRLLTTV-RDMMDRQKDfyIDLFVREKNTIAIGLYESLGYVKYR 140
Cdd:pfam08445  22 GELGALQTLPEHRRRGLGSRLVAALaRGIAERGIT--PFAVVVAGNTPSRRLYEKLGFRKID 81
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 85-158 2.53e-06

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 45.31  E-value: 2.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584063   85 LAVAQDYRKLGLGTRLLTTVRDMMDRQKDFYIDLFVREKNTIAIGLYESLGY--VKYRwiPKFYADDHGYE----MRLPL 158
Cdd:PRK09491  69 IAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFneVTIR--RNYYPTADGREdaiiMALPL 146
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
84-158 4.12e-05

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 42.29  E-value: 4.12e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584063  84 ALAVAQDYRKLGLGTRLLTTVRDMMdRQKDF-YIDLFVREKNTIAIGLYESLGYVKYRWIPKFYADDHGYE----MRLPL 158
Cdd:COG1247  85 SIYVDPDARGRGIGRALLEALIERA-RARGYrRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLdlvlMQKRL 163
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 78-137 1.54e-04

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: 39.98  E-value: 1.54e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24584063  78 NHGHISALAVAQDYRKLGLGTRLLTTVrdmMDRQKDFYID-LFVrEKNTIAIGLYESLGYV 137
Cdd:COG1246  51 DLAELRSLAVHPDYRGRGIGRRLLEAL---LAEARELGLKrLFL-LTTSAAIHFYEKLGFE 107
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 50-118 7.88e-04

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 36.48  E-value: 7.88e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24584063  50 DNSLMGFILGTRVEDatesfgdaktmTWNHGHISALAVAQDYRKLGLGTRLLTTVRDMMDRQKDFYIDL 118
Cdd:cd04301   7 DGEIVGFASLSPDGS-----------GGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
PRK10514 PRK10514
putative acetyltransferase; Provisional
 75-136 1.86e-03

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 37.29  E-value: 1.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24584063   75 MTWNHGHISALAVAQDYRKLGLGTRLlttVRDMMDRQKDFYIDlfVREKNTIAIGLYESLGY 136
Cdd:PRK10514  65 MLLSGGHMEALFVDPDVRGCGVGRML---VEHALSLHPELTTD--VNEQNEQAVGFYKKMGF 121
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 77-153 2.49e-03

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: 37.29  E-value: 2.49e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24584063  77 WNHGHIsALAVAQDYRKLGLGTRLLTTVRDMMDRQKDF-YIDLFVREKNTIAIGLYESLGYVKYRWIPKFYADDHGYE 153
Cdd:COG1670  86 NRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEELGLhRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYR 162
 
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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