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Conserved domains on  [gi|985494695|ref|WP_060792668|]
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MULTISPECIES: GNAT family N-acetyltransferase [Enterococcus]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 20260227)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

CATH:  3.40.630.30
EC:  2.3.1.-
Gene Ontology:  GO:0016746|GO:0008080
PubMed:  9175471|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 ...
 74-146 5.64e-20

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 79.31  E-value: 5.64e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 985494695  74 GYM--KVNDEKDTIEIQRLYLLKDYQNKGLGQRLLDEANRYAKTKQKRYLRLTVYEKNHAGIRFYERHGFKKIGI 146
Cdd:COG0456    1 GFAllGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGE 75
Spm_actase_Thplmales super family cl46108
spermidine N(1)-acetyltransferase;
5-114 1.21e-05

spermidine N(1)-acetyltransferase;


The actual alignment was detected with superfamily member NF041158:

Pssm-ID: 469070  Cd Length: 115  Bit Score: 42.22  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494695   5 ITLAYLDYDDLDALQVVSVVSFYESFIDGADPLDMQGYLQTQLTTEILAVELAQSTSK----FIGIKDHQILIGYMKVND 80
Cdd:NF041158   2 ITIRKLSAEDVDALIEVARESWKWTYRDIYSNEFIESWISEKYSKEKLLNEIIRSQSNldiiFLGAFVNSALIGFIELKI 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 985494695  81 EKDTIEIQRLYLLKDYQNKGLGQRLLDEANRYAK 114
Cdd:NF041158  82 IADKAELLRLYLKPEYTHRGIGKLLLSEAEKIMK 115
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 74-146 5.64e-20

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 79.31  E-value: 5.64e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 985494695  74 GYM--KVNDEKDTIEIQRLYLLKDYQNKGLGQRLLDEANRYAKTKQKRYLRLTVYEKNHAGIRFYERHGFKKIGI 146
Cdd:COG0456    1 GFAllGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGE 75
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 63-141 2.16e-15

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: 67.93  E-value: 2.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494695   63 FIGIKDHQILIGYM---KVNDEKDTIEIQRLYLLKDYQNKGLGQRLLDEANRYAKTKQKRYLRLTVYEKNHAGIRFYERH 139
Cdd:pfam00583  35 FFVAEEDGELVGFAslsIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKL 114


                  ..
gi 985494695  140 GF 141
Cdd:pfam00583 115 GF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 48-157 2.23e-14

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: 65.81  E-value: 2.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494695   48 TTEILAVELAQSTSKFIGIKDHQILIGYMKVNDEKDTIEIQRLYLLKDYQNKGLGQRLLDEANRYAKTKQKRYLRLTVYE 127
Cdd:TIGR01575  18 TEAQFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRV 97

                          90       100       110
                  ....*....|....*....|....*....|..
gi 985494695  128 KNHAGIRFYERHGFKKIGI--KHFPLGKQDRI 157
Cdd:TIGR01575  98 SNIAAQALYKKLGFNEIAIrrNYYPDPGEDAI 129
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 63-124 2.94e-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: 48.04  E-value: 2.94e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 985494695  63 FIGIKDHQILIGYM---KVNDEKDTIEIQRLYLLKDYQNKGLGQRLLDEANRYAKTKQKRYLRLT 124
Cdd:cd04301    1 FLVAEDDGEIVGFAslsPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
Spm_actase_Thplmales NF041158
spermidine N(1)-acetyltransferase;
5-114 1.21e-05

spermidine N(1)-acetyltransferase;


Pssm-ID: 469070  Cd Length: 115  Bit Score: 42.22  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494695   5 ITLAYLDYDDLDALQVVSVVSFYESFIDGADPLDMQGYLQTQLTTEILAVELAQSTSK----FIGIKDHQILIGYMKVND 80
Cdd:NF041158   2 ITIRKLSAEDVDALIEVARESWKWTYRDIYSNEFIESWISEKYSKEKLLNEIIRSQSNldiiFLGAFVNSALIGFIELKI 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 985494695  81 EKDTIEIQRLYLLKDYQNKGLGQRLLDEANRYAK 114
Cdd:NF041158  82 IADKAELLRLYLKPEYTHRGIGKLLLSEAEKIMK 115
PRK10562 PRK10562
putative acetyltransferase; Provisional
 72-145 1.37e-04

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 40.05  E-value: 1.37e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 985494695  72 LIGYMKVNDEKdtiEIQRLYLLKDYQNKGLGQRLLDEAnryaktkQKRY--LRLTVYEKNHAGIRFYERHGFKKIG 145
Cdd:PRK10562  59 LLGFVSVLEGR---FVGALFVAPKAVRRGIGKALMQHV-------QQRYphLSLEVYQKNQRAVNFYHAQGFRIVD 124
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 74-146 5.64e-20

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 79.31  E-value: 5.64e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 985494695  74 GYM--KVNDEKDTIEIQRLYLLKDYQNKGLGQRLLDEANRYAKTKQKRYLRLTVYEKNHAGIRFYERHGFKKIGI 146
Cdd:COG0456    1 GFAllGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGE 75
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 43-145 1.32e-19

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 79.71  E-value: 1.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494695  43 LQTQLTTEILAVELAQ-----STSKFIGIKDHQILIGYMKVND-EKDTIEIQRLYLLKDYQNKGLGQRLLDEANRYAKTK 116
Cdd:COG0454   11 INFILLIEALDAELKAmegslAGAEFIAVDDKGEPIGFAGLRRlDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARER 90

                         90       100
                 ....*....|....*....|....*....
gi 985494695 117 QKRYLRLTVYEKNHAGIRFYERHGFKKIG 145
Cdd:COG0454   91 GCTALELDTLDGNPAAIRFYERLGFKEIE 119
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 63-141 2.16e-15

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: 67.93  E-value: 2.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494695   63 FIGIKDHQILIGYM---KVNDEKDTIEIQRLYLLKDYQNKGLGQRLLDEANRYAKTKQKRYLRLTVYEKNHAGIRFYERH 139
Cdd:pfam00583  35 FFVAEEDGELVGFAslsIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKL 114


                  ..
gi 985494695  140 GF 141
Cdd:pfam00583 115 GF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 48-157 2.23e-14

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: 65.81  E-value: 2.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494695   48 TTEILAVELAQSTSKFIGIKDHQILIGYMKVNDEKDTIEIQRLYLLKDYQNKGLGQRLLDEANRYAKTKQKRYLRLTVYE 127
Cdd:TIGR01575  18 TEAQFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRV 97

                          90       100       110
                  ....*....|....*....|....*....|..
gi 985494695  128 KNHAGIRFYERHGFKKIGI--KHFPLGKQDRI 157
Cdd:TIGR01575  98 SNIAAQALYKKLGFNEIAIrrNYYPDPGEDAI 129
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 45-150 8.18e-14

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: 64.21  E-value: 8.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494695   45 TQLTTEILAVELAQSTSKFIGIKDHQILIGYMKVndeKDTIEIQRLYLLKDYQNKGLGQRLLDEANRYAKTKQKRYLRLT 124
Cdd:pfam13673  15 EFISPEALRERIDQGEYFFFVAFEGGQIVGVIAL---RDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELT 91

                          90       100       110
                  ....*....|....*....|....*....|...
gi 985494695  125 VYEKNHAgIRFYERHGFKKI-------GIKHFP 150
Cdd:pfam13673  92 VNASPYA-VPFYEKLGFRATgpeqefnGIRFVP 123
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
90-156 3.38e-13

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 63.48  E-value: 3.38e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 985494695  90 LYLLKDYQNKGLGQRLLDEANRYAKTKQKRYLRLTVYEKNHAGIRFYERHGFKKIGIKHFPLGKQDR 156
Cdd:COG1247   86 IYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGR 152
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 51-165 4.07e-13

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: 62.70  E-value: 4.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494695  51 ILAVELAQSTSKFIGIKDHQILIGY--MKVNDEkDTIEIQRLYLLKDYQNKGLGQRLLDEANRYAKTKQKRYLRLTVYek 128
Cdd:COG1246   18 IRPYALEEEIGEFWVAEEDGEIVGCaaLHPLDE-DLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTT-- 94

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 985494695 129 nHAGIRFYERHGFKKIGIKHFPLGKQDRICPI-LEKEI 165
Cdd:COG1246   95 -SAAIHFYEKLGFEEIDKEDLPYAKVWQRDSVvMEKDL 131
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 61-143 1.27e-12

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 60.16  E-value: 1.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494695   61 SKFIGIKDHQILIGY--MKVNDEKDTIEIQRLYLLKDYQNKGLGQRLLDEANRYAKTKQKRYLRLTVyekNHAGIRFYER 138
Cdd:pfam13508   3 GRFFVAEDDGKIVGFaaLLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRAAAFYEK 79


                  ....*
gi 985494695  139 HGFKK 143
Cdd:pfam13508  80 LGFEE 84
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 51-146 2.18e-11

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: 58.86  E-value: 2.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494695  51 ILAVELaQSTSKFIGikdhqiLIGYMKVNDEKDTIEIqRLYLLKDYQNKGLGQRLLDEANRYAKTKQK-RYLRLTVYEKN 129
Cdd:COG1670   62 PFAIED-KEDGELIG------VVGLYDIDRANRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEELGlHRVEAEVDPDN 133

                         90
                 ....*....|....*..
gi 985494695 130 HAGIRFYERHGFKKIGI 146
Cdd:COG1670  134 TASIRVLEKLGFRLEGT 150
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
63-165 2.53e-11

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 58.17  E-value: 2.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494695  63 FIGIKDHQIlIGY-----MKVNDEKDTIEIQRLYLLKDYQNKGLGQRLLDEANRYAKTKQKRYLRLTVyekNHAGIRFYE 137
Cdd:COG3153   42 LVAEDDGEI-VGHvalspVDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLG---DPSLLPFYE 117

                         90       100
                 ....*....|....*....|....*...
gi 985494695 138 RHGFKKIGIKHFPLGKQDRicpILEKEI 165
Cdd:COG3153  118 RFGFRPAGELGLTLGPDEV---FLAKEL 142
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
83-145 3.58e-11

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 56.07  E-value: 3.58e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 985494695  83 DTIEIQRLYLLKDYQNKGLGQRLLDEANRYAKTKQKRYLRLTVYEKNHAGIRFYERHGFKKIG 145
Cdd:COG3393   14 GVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVG 76
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
64-150 7.86e-10

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 54.03  E-value: 7.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494695  64 IGIKDHQILIGYMKV-NDEKDTIEIQRLYLLKDYQNKGLGQRLLDEANRYAKTKQKRYLRLTVYEknHAgIRFYERHGFK 142
Cdd:COG2153   37 LLAYDDGELVATARLlPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQA--HA-VGFYEKLGFV 113

                         90
                 ....*....|....*
gi 985494695 143 KI-------GIKHFP 150
Cdd:COG2153  114 PVgeefleaGIPHID 128
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 63-124 2.94e-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: 48.04  E-value: 2.94e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 985494695  63 FIGIKDHQILIGYM---KVNDEKDTIEIQRLYLLKDYQNKGLGQRLLDEANRYAKTKQKRYLRLT 124
Cdd:cd04301    1 FLVAEDDGEIVGFAslsPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
Spm_actase_Thplmales NF041158
spermidine N(1)-acetyltransferase;
5-114 1.21e-05

spermidine N(1)-acetyltransferase;


Pssm-ID: 469070  Cd Length: 115  Bit Score: 42.22  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494695   5 ITLAYLDYDDLDALQVVSVVSFYESFIDGADPLDMQGYLQTQLTTEILAVELAQSTSK----FIGIKDHQILIGYMKVND 80
Cdd:NF041158   2 ITIRKLSAEDVDALIEVARESWKWTYRDIYSNEFIESWISEKYSKEKLLNEIIRSQSNldiiFLGAFVNSALIGFIELKI 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 985494695  81 EKDTIEIQRLYLLKDYQNKGLGQRLLDEANRYAK 114
Cdd:NF041158  82 IADKAELLRLYLKPEYTHRGIGKLLLSEAEKIMK 115
PRK10562 PRK10562
putative acetyltransferase; Provisional
 72-145 1.37e-04

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 40.05  E-value: 1.37e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 985494695  72 LIGYMKVNDEKdtiEIQRLYLLKDYQNKGLGQRLLDEAnryaktkQKRY--LRLTVYEKNHAGIRFYERHGFKKIG 145
Cdd:PRK10562  59 LLGFVSVLEGR---FVGALFVAPKAVRRGIGKALMQHV-------QQRYphLSLEVYQKNQRAVNFYHAQGFRIVD 124
PRK13688 PRK13688
N-acetyltransferase;
57-144 1.52e-04

N-acetyltransferase;


Pssm-ID: 237470  Cd Length: 156  Bit Score: 40.00  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494695  57 AQSTSKFIGIKDHQILIGYM---KVNDEKDT--------IEIQRLYLLKDYQNKGLGQRLLDeanrYAKTKQkryLRLTV 125
Cdd:PRK13688  41 NDSESPFYGIYYGDSLVARMslyKKGGVEEPyfedtqdyLELWKLEVLPKYQNRGYGEMLVD----FAKSFQ---LPIKT 113

                         90
                 ....*....|....*....
gi 985494695 126 YEKNHAGiRFYERHGFKKI 144
Cdd:PRK13688 114 IARNKSK-DFWLKLGFTPV 131
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 95-157 1.81e-04

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 39.53  E-value: 1.81e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 985494695  95 DYQNKGLGQRLLDEANRYAKTKQKRYLRLTVYEKNHAGIRFYERHGFKKIGI-KHF---PLGKQDRI 157
Cdd:PRK09491  74 DYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIrRNYyptADGREDAI 140
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 86-144 2.64e-04

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: 38.08  E-value: 2.64e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 985494695   86 EIQRLYLLKDYQNKGLGQRLLDEANRYAKTKQKRYLRLTVyEKNHAGIRFYERHGFKKI 144
Cdd:pfam08445  23 ELGALQTLPEHRRRGLGSRLVAALARGIAERGITPFAVVV-AGNTPSRRLYEKLGFRKI 80
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
68-142 6.94e-04

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


Pssm-ID: 182877  Cd Length: 194  Bit Score: 38.37  E-value: 6.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494695  68 DHQILIgymkVNDEKDTIE--------------IQRLYLLKDYQNKGLGQRLLDEANRYAKTKQKRYLRLTVYEKNHAGI 133
Cdd:PRK10975 100 DHQCLL----LRDASGQIQgfvtlrelndtdarIGLLAVFPGAQGRGIGARLMQAALNWCQARGLTRLRVATQMGNLAAL 175


                 ....*....
gi 985494695 134 RFYERHGFK 142
Cdd:PRK10975 176 RLYIRSGAN 184
PRK10514 PRK10514
putative acetyltransferase; Provisional
 73-161 9.43e-04

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 37.67  E-value: 9.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494695  73 IGYMKVNDEkdtiEIQRLYLLKDYQNKGLGQRLLDEAnryaktkQKRYLRLT--VYEKNHAGIRFYERHGFKKIGikHFP 150
Cdd:PRK10514  62 VGFMLLSGG----HMEALFVDPDVRGCGVGRMLVEHA-------LSLHPELTtdVNEQNEQAVGFYKKMGFKVTG--RSE 128

                         90
                 ....*....|.
gi 985494695 151 LGKQDRICPIL 161
Cdd:PRK10514 129 VDDQGRPYPLL 139
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 52-142 1.82e-03

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 36.56  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985494695   52 LAVELAQStsKFIGikdhqiLIGYMKVNDEKDTIEIqRLYLLKDYQNKGLG----QRLLDEANRyakTKQKRYLRLTVYE 127
Cdd:pfam13302  57 WAIELKDT--GFIG------SIGLYDIDGEPERAEL-GYWLGPDYWGKGYAteavRALLEYAFE---ELGLPRLVARIDP 124

                          90
                  ....*....|....*
gi 985494695  128 KNHAGIRFYERHGFK 142
Cdd:pfam13302 125 ENTASRRVLEKLGFK 139
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 99-148 5.21e-03

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this family are members of the pfam00583 (GNAT) superfamily of acetyltransferases and are proposed to perform a N-acetylation step in the process of pseudaminic acid biosynthesis in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci. Significantly, many genomes containing other components of this pathway lack this gene, indicating that some other N-acetyl transferases may be incolved and/or the step is optional, resulting in a non-acetylated pseudaminic acid variant sugar.


Pssm-ID: 274661 [Multi-domain]  Cd Length: 152  Bit Score: 35.41  E-value: 5.21e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 985494695   99 KGLGQRLLDEANRYAKTK-QKRYLRLTVYEKNHAGIRFYERHGFKKIGIKH 148
Cdd:TIGR03585  90 PGVGSVLEEAALEYAFEHlGLHKLSLEVLESNNKALKLYEKFGFEREGVFR 140
 
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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