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MULTISPECIES: GNAT family N-acetyltransferase [Caldilinea]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10006981)

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
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
5-146 9.32e-16

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


:

Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 69.73  E-value: 9.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504246677   5 IVRARPEHAVRLTQIAHAAKSYwGYPAQWIELWRNQLTITEAYIeanevyaAVDaDDVILGFYAL-----GGEGEKRTLE 79
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGP-GREAELVDRLREDPAAGLSLV-------AED-DGEIVGHVALspvdiDGEGPALLLG 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504246677  80 HLWVQPQSFGAGVGRQLFTHAVARAQTLGARVIEIESDPHAEGFYQRMGAETIGEVTYDMEGSPRRL 146
Cdd:COG3153   72 PLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRPAGELGLTLGPDEVFL 138
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
5-146 9.32e-16

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 69.73  E-value: 9.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504246677   5 IVRARPEHAVRLTQIAHAAKSYwGYPAQWIELWRNQLTITEAYIeanevyaAVDaDDVILGFYAL-----GGEGEKRTLE 79
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGP-GREAELVDRLREDPAAGLSLV-------AED-DGEIVGHVALspvdiDGEGPALLLG 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504246677  80 HLWVQPQSFGAGVGRQLFTHAVARAQTLGARVIEIESDPHAEGFYQRMGAETIGEVTYDMEGSPRRL 146
Cdd:COG3153   72 PLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRPAGELGLTLGPDEVFL 138
PRK10514 PRK10514
putative acetyltransferase; Provisional
 2-151 7.70e-12

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 59.63  E-value: 7.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504246677   2 TIRIVRARPEHAVRLTQIahaaksywgypaqwielWRNQLTITEAYIEAN-------EVYA---------AVDADDVILG 65
Cdd:PRK10514   1 MISIRRSRHEEGERLVAI-----------------WRRSVDATHDFLSAEdraeieeLVRSflpeaplwvAVDERDQPVG 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504246677  66 FYALGGEgekrTLEHLWVQPQSFGAGVGRQLFTHAVARAQTLGARVieIESDPHAEGFYQRMGAETIGEVTYDMEGSPRR 145
Cdd:PRK10514  64 FMLLSGG----HMEALFVDPDVRGCGVGRMLVEHALSLHPELTTDV--NEQNEQAVGFYKKMGFKVTGRSEVDDQGRPYP 137


                 ....*.
gi 504246677 146 LPLMAY 151
Cdd:PRK10514 138 LLHLAY 143
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 29-138 3.44e-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: 54.58  E-value: 3.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504246677   29 YPAQWIELWRNQLTITEAYIE----ANEVYAAVDaDDVILGFYALGGEGEkrtLEHLWVQPQSFGAGVGRQLFTHAVARA 104
Cdd:pfam13673   5 YSEEGIETFYEFISPEALRERidqgEYFFFVAFE-GGQIVGVIALRDRGH---ISLLFVDPDYQGQGIGKALLEAVEDYA 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 504246677  105 QTLGARVIEIE--SDPHAEGFYQRMGAETIGEVTYD 138
Cdd:pfam13673  81 EKDGIKLSELTvnASPYAVPFYEKLGFRATGPEQEF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 54-115 2.03e-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: 37.64  E-value: 2.03e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504246677  54 YAAVDADDVILGFYALGGEGEKRT---LEHLWVQPQSFGAGVGRQLFTHAVARAQTLGARVIEIE 115
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDtayIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
5-146 9.32e-16

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 69.73  E-value: 9.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504246677   5 IVRARPEHAVRLTQIAHAAKSYwGYPAQWIELWRNQLTITEAYIeanevyaAVDaDDVILGFYAL-----GGEGEKRTLE 79
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGP-GREAELVDRLREDPAAGLSLV-------AED-DGEIVGHVALspvdiDGEGPALLLG 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504246677  80 HLWVQPQSFGAGVGRQLFTHAVARAQTLGARVIEIESDPHAEGFYQRMGAETIGEVTYDMEGSPRRL 146
Cdd:COG3153   72 PLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRPAGELGLTLGPDEVFL 138
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
78-145 5.53e-13

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 62.12  E-value: 5.53e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504246677  78 LEHLWVQPQSFGAGVGRQLFTHAVARAQTLGARVIEIESDPHAEGFYQRMGAETIGEVtYDMEGSPRR 145
Cdd:COG2153   61 IGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAHAVGFYEKLGFVPVGEE-FLEAGIPHI 127
PRK10514 PRK10514
putative acetyltransferase; Provisional
 2-151 7.70e-12

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 59.63  E-value: 7.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504246677   2 TIRIVRARPEHAVRLTQIahaaksywgypaqwielWRNQLTITEAYIEAN-------EVYA---------AVDADDVILG 65
Cdd:PRK10514   1 MISIRRSRHEEGERLVAI-----------------WRRSVDATHDFLSAEdraeieeLVRSflpeaplwvAVDERDQPVG 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504246677  66 FYALGGEgekrTLEHLWVQPQSFGAGVGRQLFTHAVARAQTLGARVieIESDPHAEGFYQRMGAETIGEVTYDMEGSPRR 145
Cdd:PRK10514  64 FMLLSGG----HMEALFVDPDVRGCGVGRMLVEHALSLHPELTTDV--NEQNEQAVGFYKKMGFKVTGRSEVDDQGRPYP 137


                 ....*.
gi 504246677 146 LPLMAY 151
Cdd:PRK10514 138 LLHLAY 143
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-153 2.92e-11

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 58.47  E-value: 2.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504246677   1 MTIRivRARPEHAVRLTQIAHAAKSY----WGYPAQWIELWRNQltITEAYIEANEVYAAVDaDDVILGFYALG----GE 72
Cdd:COG1247    2 MTIR--PATPEDAPAIAAIYNEAIAEgtatFETEPPSEEEREAW--FAAILAPGRPVLVAEE-DGEVVGFASLGpfrpRP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504246677  73 GEKRTLEH-LWVQPQSFGAGVGRQLFTHAVARAQTLGARVIEIESDPH---AEGFYQRMGAETIG--EVTYDMEGSPRRL 146
Cdd:COG1247   77 AYRGTAEEsIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADneaSIALYEKLGFEEVGtlPEVGFKFGRWLDL 156


                 ....*..
gi 504246677 147 PLMAYML 153
Cdd:COG1247  157 VLMQKRL 163
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 46-145 3.26e-11

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: 57.69  E-value: 3.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504246677  46 AYIEANEVYAAVDADDVILGFYAL----GGEGEkrtLEHLWVQPQSFGAGVGRQLFTHAVARAQTLGARVIEIESDPHAE 121
Cdd:COG1246   22 ALEEEIGEFWVAEEDGEIVGCAALhpldEDLAE---LRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSAAI 98

                         90       100
                 ....*....|....*....|....
gi 504246677 122 GFYQRMGAETIGEVTYDMEGSPRR 145
Cdd:COG1246   99 HFYEKLGFEEIDKEDLPYAKVWQR 122
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 29-138 3.44e-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: 54.58  E-value: 3.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504246677   29 YPAQWIELWRNQLTITEAYIE----ANEVYAAVDaDDVILGFYALGGEGEkrtLEHLWVQPQSFGAGVGRQLFTHAVARA 104
Cdd:pfam13673   5 YSEEGIETFYEFISPEALRERidqgEYFFFVAFE-GGQIVGVIALRDRGH---ISLLFVDPDYQGQGIGKALLEAVEDYA 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 504246677  105 QTLGARVIEIE--SDPHAEGFYQRMGAETIGEVTYD 138
Cdd:pfam13673  81 EKDGIKLSELTvnASPYAVPFYEKLGFRATGPEQEF 116
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 49-128 2.29e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 51.69  E-value: 2.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504246677   49 EANEVYAAVDaDDVILGFYALGGEGEKRTLEH--LWVQPQSFGAGVGRQLFTHAVARAQTLGARVIEIESDPHAEGFYQR 126
Cdd:pfam13508   1 PGGRFFVAED-DGKIVGFAALLPLDDEGALAElrLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEK 79


                  ..
gi 504246677  127 MG 128
Cdd:pfam13508  80 LG 81
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 62-134 3.62e-09

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 51.19  E-value: 3.62e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504246677  62 VILGFYALGGEGEkrtLEHLWVQPQSFGAGVGRQLFTHAVARAQTLGARVIEIESDPH---AEGFYQRMGAETIGE 134
Cdd:COG0456    3 ALLGLVDGGDEAE---IEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDneaAIALYEKLGFEEVGE 75
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 3-138 9.85e-09

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: 9.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504246677   3 IRIVRARPEHAVRLTQIahaaksywgypaqwiELWRNQLTITEaYIEANEVYAAVDADDVILGFYALGGEGEKRT-LEHL 81
Cdd:COG0454    1 MSIRKATPEDINFILLI---------------EALDAELKAME-GSLAGAEFIAVDDKGEPIGFAGLRRLDDKVLeLKRL 64

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504246677  82 WVQPQSFGAGVGRQLFTHAVARAQTLGARVIEIE---SDPHAEGFYQRMGAETIGEVTYD 138
Cdd:COG0454   65 YVLPEYRGKGIGKALLEALLEWARERGCTALELDtldGNPAAIRFYERLGFKEIERYVAY 124
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 16-128 3.08e-06

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: 44.05  E-value: 3.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504246677   16 LTQIAHAAKSYWGYPAQWIELWRnqltITEAYIEANEVYAAVDADDVILGF---YALGGEGEKRTLEHLWVQPQSFGAGV 92
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDL----LEDWDEDASEGFFVAEEDGELVGFaslSIIDDEPPVGEIEGLAVAPEYRGKGI 76

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 504246677   93 GRQLFTHAVARAQTLGARVIEIE---SDPHAEGFYQRMG 128
Cdd:pfam00583  77 GTALLQALLEWARERGCERIFLEvaaDNLAAIALYEKLG 115
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 54-115 2.03e-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: 37.64  E-value: 2.03e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504246677  54 YAAVDADDVILGFYALGGEGEKRT---LEHLWVQPQSFGAGVGRQLFTHAVARAQTLGARVIEIE 115
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDtayIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PRK08186 PRK08186
allophanate hydrolase; Provisional
 84-121 3.64e-03

allophanate hydrolase; Provisional


Pssm-ID: 236177 [Multi-domain]  Cd Length: 600  Bit Score: 36.74  E-value: 3.64e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 504246677  84 QPQSFGAGVGRQLFTHAVARAQTLGARVIEIESDPHAE 121
Cdd:PRK08186 261 QLEFFGDAEAEAAFAAALARLEALGAELVEIDFSPFLE 298
 
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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