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Conserved domains on  [gi|24662097|ref|NP_729584|]
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variable nurse cells, isoform E [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 ...
 54-154 1.91e-16

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 70.84  E-value: 1.91e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662097  54 GYVLAKmeepePNEESRHGHITSLAVKRSYRRLGLAQKLMNQASQAMVECfNAQYVSLHVRKSNRAALNLYTnALKFKII 133
Cdd:COG0456   1 GFALLG-----LVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARER-GARRLRLEVREDNEAAIALYE-KLGFEEV 73

                        90       100
                ....*....|....*....|.
gi 24662097 134 EVEPKYYADgeDAYAMRRDLS 154
Cdd:COG0456  74 GERPNYYGD--DALVMEKELA 92
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 54-154 1.91e-16

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 70.84  E-value: 1.91e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662097  54 GYVLAKmeepePNEESRHGHITSLAVKRSYRRLGLAQKLMNQASQAMVECfNAQYVSLHVRKSNRAALNLYTnALKFKII 133
Cdd:COG0456   1 GFALLG-----LVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARER-GARRLRLEVREDNEAAIALYE-KLGFEEV 73

                        90       100
                ....*....|....*....|.
gi 24662097 134 EVEPKYYADgeDAYAMRRDLS 154
Cdd:COG0456  74 GERPNYYGD--DALVMEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 28-124 1.31e-14

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: 66.77  E-value: 1.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662097    28 MKYYFYHGLTWPQLSYVAVDDKGAIVGYVLAKMEepepNEESRHGHITSLAVKRSYRRLGLAQKLMNQASQAMVEcFNAQ 107
Cdd:pfam00583  20 PLDLLEDWDEDASEGFFVAEEDGELVGFASLSII----DDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARE-RGCE 94

                          90
                  ....*....|....*..
gi 24662097   108 YVSLHVRKSNRAALNLY 124
Cdd:pfam00583  95 RIFLEVAADNLAAIALY 111
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 42-112 1.29e-08

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: 49.58  E-value: 1.29e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24662097  42 SYVAVDDkGAIVGYVLAKMEEPEPneesRHGHITSLAVKRSYRRLGLAQKLMNQASQAMVEcFNAQYVSLH 112
Cdd:cd04301   1 FLVAEDD-GEIVGFASLSPDGSGG----DTAYIGDLAVLPEYRGKGIGSALLEAAEEEARE-RGAKRLRLE 65
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
44-125 1.66e-06

dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;


Pssm-ID: 182877  Cd Length: 194  Bit Score: 46.46  E-value: 1.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662097   44 VAVDDKGAIVGYV-LAKMEEPEpneesrhGHITSLAVKRSYRRLGLAQKLMnQASQAmvECFNAQYVSLHV--RKSNRAA 120
Cdd:PRK10975 105 LLRDASGQIQGFVtLRELNDTD-------ARIGLLAVFPGAQGRGIGARLM-QAALN--WCQARGLTRLRVatQMGNLAA 174


                 ....*
gi 24662097  121 LNLYT 125
Cdd:PRK10975 175 LRLYI 179
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 54-154 1.91e-16

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 70.84  E-value: 1.91e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662097  54 GYVLAKmeepePNEESRHGHITSLAVKRSYRRLGLAQKLMNQASQAMVECfNAQYVSLHVRKSNRAALNLYTnALKFKII 133
Cdd:COG0456   1 GFALLG-----LVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARER-GARRLRLEVREDNEAAIALYE-KLGFEEV 73

                        90       100
                ....*....|....*....|.
gi 24662097 134 EVEPKYYADgeDAYAMRRDLS 154
Cdd:COG0456  74 GERPNYYGD--DALVMEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 28-124 1.31e-14

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: 66.77  E-value: 1.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662097    28 MKYYFYHGLTWPQLSYVAVDDKGAIVGYVLAKMEepepNEESRHGHITSLAVKRSYRRLGLAQKLMNQASQAMVEcFNAQ 107
Cdd:pfam00583  20 PLDLLEDWDEDASEGFFVAEEDGELVGFASLSII----DDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARE-RGCE 94

                          90
                  ....*....|....*..
gi 24662097   108 YVSLHVRKSNRAALNLY 124
Cdd:pfam00583  95 RIFLEVAADNLAAIALY 111
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-153 6.03e-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: 6.03e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662097   1 MNIRCAKPEDLMTMQHCNLLCLPENY-----------QMKYYFYHGLTWPQLSYVAVDDkGAIVGYvlAKMEEPEPNEES 69
Cdd:COG1247   2 MTIRPATPEDAPAIAAIYNEAIAEGTatfeteppseeEREAWFAAILAPGRPVLVAEED-GEVVGF--ASLGPFRPRPAY 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662097  70 RHGHITSLAVKRSYRRLGLAQKLMnQASQAMVECFNAQYVSLHVRKSNRAALNLYTnALKFKIIEVEPK-YYADGE--DA 146
Cdd:COG1247  79 RGTAEESIYVDPDARGRGIGRALL-EALIERARARGYRRLVAVVLADNEASIALYE-KLGFEEVGTLPEvGFKFGRwlDL 156


                ....*..
gi 24662097 147 YAMRRDL 153
Cdd:COG1247 157 VLMQKRL 163
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-153 1.05e-08

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 51.62  E-value: 1.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662097   3 IRCAKPEDLMTMQHCNLLCLPENY--QMKYYFYHGLTwPQLSYVAVDDkGAIVGYVLakMEEPEPNEESRHGHITSLAVK 80
Cdd:COG3153   1 IRPATPEDAEAIAALLRAAFGPGReaELVDRLREDPA-AGLSLVAEDD-GEIVGHVA--LSPVDIDGEGPALLLGPLAVD 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24662097  81 RSYRRLGLAQKLMNQASQAMVEcFNAQYVSLHvrkSNRAALNLYTNaLKFKIIEVEPkyYADGEDAYAMRRDL 153
Cdd:COG3153  77 PEYRGQGIGRALMRAALEAARE-RGARAVVLL---GDPSLLPFYER-FGFRPAGELG--LTLGPDEVFLAKEL 142
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 42-112 1.29e-08

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: 49.58  E-value: 1.29e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24662097  42 SYVAVDDkGAIVGYVLAKMEEPEPneesRHGHITSLAVKRSYRRLGLAQKLMNQASQAMVEcFNAQYVSLH 112
Cdd:cd04301   1 FLVAEDD-GEIVGFASLSPDGSGG----DTAYIGDLAVLPEYRGKGIGSALLEAAEEEARE-RGAKRLRLE 65
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 1-154 1.01e-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: 48.83  E-value: 1.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662097   1 MNIRCAKPEDLMTMQHcnlLCLPENYQMKYYFYhgltwpqlsYVAVDDkGAIVGYV-LAKMEEpepneesRHGHITSLAV 79
Cdd:COG1246   1 MTIRPATPDDVPAILE---LIRPYALEEEIGEF---------WVAEED-GEIVGCAaLHPLDE-------DLAELRSLAV 60

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24662097  80 KRSYRRLGLAQKLMNQASQAMVEcFNAQYVSLHvrkSNRAALNLYTnALKFKIIEVE--PKYYADGEDAYAMRRDLS 154
Cdd:COG1246  61 HPDYRGRGIGRRLLEALLAEARE-LGLKRLFLL---TTSAAIHFYE-KLGFEEIDKEdlPYAKVWQRDSVVMEKDLE 132
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 43-124 1.29e-06

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 44.75  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662097    43 YVAVDDkGAIVGYVLAkmeepEPNEESRHGHITSLAVKRSYRRLGLAQKLMNQASQAMvecfNAQYVSLHVRKSNRAALN 122
Cdd:pfam13508   6 FVAEDD-GKIVGFAAL-----LPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAA----KEGGIKLLELETTNRAAA 75


                  ..
gi 24662097   123 LY 124
Cdd:pfam13508  76 FY 77
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
44-125 1.66e-06

dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;


Pssm-ID: 182877  Cd Length: 194  Bit Score: 46.46  E-value: 1.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662097   44 VAVDDKGAIVGYV-LAKMEEPEpneesrhGHITSLAVKRSYRRLGLAQKLMnQASQAmvECFNAQYVSLHV--RKSNRAA 120
Cdd:PRK10975 105 LLRDASGQIQGFVtLRELNDTD-------ARIGLLAVFPGAQGRGIGARLM-QAALN--WCQARGLTRLRVatQMGNLAA 174


                 ....*
gi 24662097  121 LNLYT 125
Cdd:PRK10975 175 LRLYI 179
PRK03624 PRK03624
putative acetyltransferase; Provisional
 39-124 1.03e-05

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 43.38  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662097   39 PQLSYVAVDDkGAIVGYVLAkmeepepNEESRHGHITSLAVKRSYRRLGLAQKLMNQASQAMVE--CfnaQYVSLHVRKS 116
Cdd:PRK03624  44 PSLFLVAEVG-GEVVGTVMG-------GYDGHRGWAYYLAVHPDFRGRGIGRALVARLEKKLIArgC---PKINLQVRED 112


                 ....*...
gi 24662097  117 NRAALNLY 124
Cdd:PRK03624 113 NDAVLGFY 120
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
67-124 2.24e-05

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 41.43  E-value: 2.24e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24662097  67 EESRHGHITSLAVKRSYRRLGLAQKLMNQASQAMVECfNAQYVSLHVRKSNRAALNLY 124
Cdd:COG3393  11 ESPGVAEISGVYTHPEYRGRGLASALVAALAREALAR-GARTPFLYVDADNPAARRLY 67
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 43-153 4.30e-05

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: 41.49  E-value: 4.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662097    43 YVAVDDKGAIVGYVLAKmeepepneesRHGHITSLAVKRSYRRLGLAQKLMNQASQAMVECF-NAQYVSLHvrkSNRAAL 121
Cdd:pfam13673  33 FFVAFEGGQIVGVIALR----------DRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGiKLSELTVN---ASPYAV 99

                          90       100       110
                  ....*....|....*....|....*....|..
gi 24662097   122 NLYtnaLKFKIIEVEPKYYADGEDAYAMRRDL 153
Cdd:pfam13673 100 PFY---EKLGFRATGPEQEFNGIRFVPMEKEL 128
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 77-149 8.79e-05

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 41.07  E-value: 8.79e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24662097   77 LAVKRSYRRLGLAQKLMNQASQAMVEcFNAQYVSLHVRKSNRAALNLYtNALKFKIIEVEPKYY--ADG-EDAYAM 149
Cdd:PRK09491  69 IAVDPDYQRQGLGRALLEHLIDELEK-RGVATLWLEVRASNAAAIALY-ESLGFNEVTIRRNYYptADGrEDAIIM 142
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
43-154 4.05e-04

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 39.01  E-value: 4.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662097  43 YVAVDDkGAIVGYVLAKMEEPEpneesrHGHITSLAVKRSYRRLGLAQKLMnQASQAMVECFNAQYVSLHVRKSnraALN 122
Cdd:COG2153  37 LLAYDD-GELVATARLLPPGDG------EAKIGRVAVLPEYRGQGLGRALM-EAAIEEARERGARRIVLSAQAH---AVG 105

                        90       100       110
                ....*....|....*....|....*....|..
gi 24662097 123 LYTnALKFKIieVEPKYYADGEDAYAMRRDLS 154
Cdd:COG2153 106 FYE-KLGFVP--VGEEFLEAGIPHIDMRKPLS 134
 
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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