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Conserved domains on  [gi|161076800|ref|NP_001033883|]
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glycine N-acyltransferase [Drosophila melanogaster]

Protein Classification

GNAT family protein( domain architecture ID 106742)

GNAT (Gcn5-related N-acetyltransferase) family protein similar to N-acetyltransferases that catalyze the transfer of an acetyl group from acetyl-CoA to a substrate

PubMed:  15581578

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NAT_SF super family cl17182
N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of ...
 189-272 3.10e-18

N-Acyltransferase superfamily: Various enyzmes that characteristicly 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, 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 mechanism is an ordered Bi-Bi ternary complex kinetic mechanism for most GNATs: 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 then 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/ph enylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


The actual alignment was detected with superfamily member pfam08445:

Pssm-ID: 473072 [Multi-domain]  Cd Length: 86  Bit Score: 77.37  E-value: 3.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076800  189 VGVFDNQ-GEPLAWCLRSPHGSLSNLHVLSSHRRMGLGSLAVRFMANEIKLKGSEVLATVVPENEGSQKMFEKLGFNNIN 267
Cdd:pfam08445   2 LGIYRGDtGELAAWCLRLPGGELGALQTLPEHRRRGLGSRLVAALARGIAERGITPFAVVVAGNTPSRRLYEKLGFRKID 81


                  ....*
gi 161076800  268 KLYWA 272
Cdd:pfam08445  82 ETYWV 86
 
Name Accession Description Interval E-value
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 189-272 3.10e-18

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: 77.37  E-value: 3.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076800  189 VGVFDNQ-GEPLAWCLRSPHGSLSNLHVLSSHRRMGLGSLAVRFMANEIKLKGSEVLATVVPENEGSQKMFEKLGFNNIN 267
Cdd:pfam08445   2 LGIYRGDtGELAAWCLRLPGGELGALQTLPEHRRRGLGSRLVAALARGIAERGITPFAVVVAGNTPSRRLYEKLGFRKID 81


                  ....*
gi 161076800  268 KLYWA 272
Cdd:pfam08445  82 ETYWV 86
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 199-263 1.40e-07

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 48.50  E-value: 1.40e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161076800 199 LAWCLRSPHGSLSNLHVLSSHRRMGLGSLAVRFMANEIKLKG-SEVLATVVPENEGSQKMFEKLGF 263
Cdd:COG0456    5 LGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGaRRLRLEVREDNEAAIALYEKLGF 70
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 191-244 2.17e-03

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: 35.71  E-value: 2.17e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076800 191 VFDNQGEPLAWCL------RSPHGSLSNLHVLSSHRRMGLGSLAVRFMANEIKLKGSEVL 244
Cdd:cd04301    3 VAEDDGEIVGFASlspdgsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
 
Name Accession Description Interval E-value
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 189-272 3.10e-18

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: 77.37  E-value: 3.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076800  189 VGVFDNQ-GEPLAWCLRSPHGSLSNLHVLSSHRRMGLGSLAVRFMANEIKLKGSEVLATVVPENEGSQKMFEKLGFNNIN 267
Cdd:pfam08445   2 LGIYRGDtGELAAWCLRLPGGELGALQTLPEHRRRGLGSRLVAALARGIAERGITPFAVVVAGNTPSRRLYEKLGFRKID 81


                  ....*
gi 161076800  268 KLYWA 272
Cdd:pfam08445  82 ETYWV 86
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 199-263 1.40e-07

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 48.50  E-value: 1.40e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161076800 199 LAWCLRSPHGSLSNLHVLSSHRRMGLGSLAVRFMANEIKLKG-SEVLATVVPENEGSQKMFEKLGF 263
Cdd:COG0456    5 LGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGaRRLRLEVREDNEAAIALYEKLGF 70
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 196-263 1.85e-07

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: 48.67  E-value: 1.85e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161076800  196 GEPLAWCL------RSPHGSLSNLHVLSSHRRMGLGSLAVRFMANEIKLKGSEVL-ATVVPENEGSQKMFEKLGF 263
Cdd:pfam00583  42 GELVGFASlsiiddEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIfLEVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
179-263 6.89e-07

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 48.07  E-value: 6.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076800 179 IRGFMENNLAVGVFDNQGEPLAWCLRSPHGSLS--------NLHVLSSHRRMGLGSLAVRFMANEIKLKG-SEVLATVVP 249
Cdd:COG1247   44 FAAILAPGRPVLVAEEDGEVVGFASLGPFRPRPayrgtaeeSIYVDPDARGRGIGRALLEALIERARARGyRRLVAVVLA 123

                         90
                 ....*....|....
gi 161076800 250 ENEGSQKMFEKLGF 263
Cdd:COG1247  124 DNEASIALYEKLGF 137
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 214-263 4.76e-05

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: 43.06  E-value: 4.76e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 161076800 214 HVLSSHRRMGLGSLAVRFMANEI--KLKGSEVLATVVPENEGSQKMFEKLGF 263
Cdd:COG1670   94 WLAPAYWGKGYATEALRALLDYAfeELGLHRVEAEVDPDNTASIRVLEKLGF 145
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 168-263 9.31e-05

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 41.56  E-value: 9.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076800  168 WAYRSADSITMIRGFMENNLAV-----GVFDNQGEPLAWC-LRSPHGSLSNLHV----LSSHRRMGLGSLAVR----FMA 233
Cdd:pfam13302  31 WPLTLEEAREWLARIWAADEAErgygwAIELKDTGFIGSIgLYDIDGEPERAELgywlGPDYWGKGYATEAVRalleYAF 110

                          90       100       110
                  ....*....|....*....|....*....|
gi 161076800  234 NEIKLKgsEVLATVVPENEGSQKMFEKLGF 263
Cdd:pfam13302 111 EELGLP--RLVARIDPENTASRRVLEKLGF 138
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
210-263 1.40e-04

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 39.89  E-value: 1.40e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 161076800 210 LSNLHVLSSHRRMGLGSLAVRFMANEIKLKGSEVLA-TVVPENEGSQKMFEKLGF 263
Cdd:COG3393   18 ISGVYTHPEYRGRGLASALVAALAREALARGARTPFlYVDADNPAARRLYERLGF 72
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
154-263 2.14e-03

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 37.76  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076800 154 AYITSNHAELVDkhwAYRSADSITMIRGFMENNLAVGVFdnQGEPLAWCLRSPHGSLSNLHVLSSHRRMGLGSLAVRFMA 233
Cdd:COG3153   19 AFGPGREAELVD---RLREDPAAGLSLVAEDDGEIVGHV--ALSPVDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAAL 93

                         90       100       110
                 ....*....|....*....|....*....|
gi 161076800 234 NEIKLKGSEVLATVVpeNEGSQKMFEKLGF 263
Cdd:COG3153   94 EAARERGARAVVLLG--DPSLLPFYERFGF 121
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 191-244 2.17e-03

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: 35.71  E-value: 2.17e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076800 191 VFDNQGEPLAWCL------RSPHGSLSNLHVLSSHRRMGLGSLAVRFMANEIKLKGSEVL 244
Cdd:cd04301    3 VAEDDGEIVGFASlspdgsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
 
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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