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Conserved domains on  [gi|13376261|ref|NP_079121|]
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N-alpha-acetyltransferase 60 isoform a [Homo sapiens]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 12001312)

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

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 ...
92-171 4.73e-15

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 68.53  E-value: 4.73e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376261  92 DTQVAYILSLGVVKEFRKHGIGSLLLESLKDHIsttAQDHCKAIYLHVLTTNNTAINFYENRDFKQHHYLPYYYSIRGVL 171
Cdd:COG0456  10 GGDEAEIEDLAVDPEYRGRGIGRALLEAALERA---RERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDALV 86
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
23-155 6.76e-13

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: 63.31  E-value: 6.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376261    23 IDTVKHLCGDWFPIEYPDSWYR---DITSNKKFFSLAATYRGAIVGMIVAEIKNRTKIHkedgdilasnfsvdtqvAYIL 99
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDlleDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPV-----------------GEIE 63
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 13376261   100 SLGVVKEFRKHGIGSLLLESLKDHIsttAQDHCKAIYLHVLTTNNTAINFYENRDF 155
Cdd:pfam00583  64 GLAVAPEYRGKGIGTALLQALLEWA---RERGCERIFLEVAADNLAAIALYEKLGF 116
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
92-171 4.73e-15

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 68.53  E-value: 4.73e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376261  92 DTQVAYILSLGVVKEFRKHGIGSLLLESLKDHIsttAQDHCKAIYLHVLTTNNTAINFYENRDFKQHHYLPYYYSIRGVL 171
Cdd:COG0456  10 GGDEAEIEDLAVDPEYRGRGIGRALLEAALERA---RERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDALV 86
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
23-155 6.76e-13

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: 63.31  E-value: 6.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376261    23 IDTVKHLCGDWFPIEYPDSWYR---DITSNKKFFSLAATYRGAIVGMIVAEIKNRTKIHkedgdilasnfsvdtqvAYIL 99
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDlleDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPV-----------------GEIE 63
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 13376261   100 SLGVVKEFRKHGIGSLLLESLKDHIsttAQDHCKAIYLHVLTTNNTAINFYENRDF 155
Cdd:pfam00583  64 GLAVAPEYRGKGIGTALLQALLEWA---RERGCERIFLEVAADNLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
15-156 4.20e-10

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 56.25  E-value: 4.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376261  15 LRLLCHDDIDTVKHLCGDWFPIEYPDSWYRDITSNKKF-FSLAATYRGAIVGMIVAEIknrtkihkedgdilaSNFSVDT 93
Cdd:COG3153   1 IRPATPEDAEAIAALLRAAFGPGREAELVDRLREDPAAgLSLVAEDDGEIVGHVALSP---------------VDIDGEG 65
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13376261  94 QVAYILSLGVVKEFRKHGIGSLLLESLKDHistTAQDHCKAIYLHvltTNNTAINFYENRDFK 156
Cdd:COG3153  66 PALLLGPLAVDPEYRGQGIGRALMRAALEA---ARERGARAVVLL---GDPSLLPFYERFGFR 122
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
55-157 8.31e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 51.30  E-value: 8.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376261    55 LAATYRGAIVGMIVAEIKNrtkihkedgdilasnfsvDTQVAYILSLGVVKEFRKHGIGSLLLESLKDHIsttaqdHCKA 134
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLD------------------DEGALAELRLAVHPEYRGQGIGRALLEAAEAAA------KEGG 61
                          90       100
                  ....*....|....*....|...
gi 13376261   135 IYLHVLTTNNTAINFYENRDFKQ 157
Cdd:pfam13508  62 IKLLELETTNRAAAFYEKLGFEE 84
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
96-166 1.54e-07

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: 48.86  E-value: 1.54e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13376261    96 AYILSLGVVKEFRKHGIGSLLLESLKDHISTTAqdhCKAIYLHVLTTNNTAINFYENRDFKQHHYLPYYYS 166
Cdd:TIGR01575  55 AHILNIAVKPEYQGQGIGRALLRELIDEAKGRG---VNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYP 122
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
54-138 3.19e-05

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: 40.72  E-value: 3.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376261  54 SLAATYRGAIVGMIVAEIKNRTKihkedgdilasnfsvdtQVAYILSLGVVKEFRKHGIGSLLLESLKDHIsttAQDHCK 133
Cdd:cd04301   1 FLVAEDDGEIVGFASLSPDGSGG-----------------DTAYIGDLAVLPEYRGKGIGSALLEAAEEEA---RERGAK 60

                ....*
gi 13376261 134 AIYLH 138
Cdd:cd04301  61 RLRLE 65
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
92-171 4.73e-15

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 68.53  E-value: 4.73e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376261  92 DTQVAYILSLGVVKEFRKHGIGSLLLESLKDHIsttAQDHCKAIYLHVLTTNNTAINFYENRDFKQHHYLPYYYSIRGVL 171
Cdd:COG0456  10 GGDEAEIEDLAVDPEYRGRGIGRALLEAALERA---RERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDALV 86
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
23-155 6.76e-13

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: 63.31  E-value: 6.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376261    23 IDTVKHLCGDWFPIEYPDSWYR---DITSNKKFFSLAATYRGAIVGMIVAEIKNRTKIHkedgdilasnfsvdtqvAYIL 99
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDlleDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPV-----------------GEIE 63
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 13376261   100 SLGVVKEFRKHGIGSLLLESLKDHIsttAQDHCKAIYLHVLTTNNTAINFYENRDF 155
Cdd:pfam00583  64 GLAVAPEYRGKGIGTALLQALLEWA---RERGCERIFLEVAADNLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
15-156 4.20e-10

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 56.25  E-value: 4.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376261  15 LRLLCHDDIDTVKHLCGDWFPIEYPDSWYRDITSNKKF-FSLAATYRGAIVGMIVAEIknrtkihkedgdilaSNFSVDT 93
Cdd:COG3153   1 IRPATPEDAEAIAALLRAAFGPGREAELVDRLREDPAAgLSLVAEDDGEIVGHVALSP---------------VDIDGEG 65
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13376261  94 QVAYILSLGVVKEFRKHGIGSLLLESLKDHistTAQDHCKAIYLHvltTNNTAINFYENRDFK 156
Cdd:COG3153  66 PALLLGPLAVDPEYRGQGIGRALMRAALEA---ARERGARAVVLL---GDPSLLPFYERFGFR 122
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
12-173 1.28e-09

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 55.39  E-value: 1.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376261  12 EVSLRLLCHDDIDTVKHLCGDW-------FPIEYPD-----SWYRDITSNKkFFSLAATYRGAIVGMIVAEIknrtkihk 79
Cdd:COG1247   1 EMTIRPATPEDAPAIAAIYNEAiaegtatFETEPPSeeereAWFAAILAPG-RPVLVAEEDGEVVGFASLGP-------- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376261  80 edgdilASNFSVDTQVAYIlSLGVVKEFRKHGIGSLLLESLKDHistTAQDHCKAIYLHVLTTNNTAINFYENRDFKQHH 159
Cdd:COG1247  72 ------FRPRPAYRGTAEE-SIYVDPDARGRGIGRALLEALIER---ARARGYRRLVAVVLADNEASIALYEKLGFEEVG 141
                       170
                ....*....|....
gi 13376261 160 YLPYYYSIRGVLKD 173
Cdd:COG1247 142 TLPEVGFKFGRWLD 155
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
55-157 8.31e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 51.30  E-value: 8.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376261    55 LAATYRGAIVGMIVAEIKNrtkihkedgdilasnfsvDTQVAYILSLGVVKEFRKHGIGSLLLESLKDHIsttaqdHCKA 134
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLD------------------DEGALAELRLAVHPEYRGQGIGRALLEAAEAAA------KEGG 61
                          90       100
                  ....*....|....*....|...
gi 13376261   135 IYLHVLTTNNTAINFYENRDFKQ 157
Cdd:pfam13508  62 IKLLELETTNRAAAFYEKLGFEE 84
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
13-163 3.23e-08

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: 50.76  E-value: 3.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376261  13 VSLRLLCHDDIDTVKHLCGDWFPIEypdswyrditSNKKFFslAATYRGAIVGMIVaeiknrtkIHKEDGDilasnfsvd 92
Cdd:COG1246   1 MTIRPATPDDVPAILELIRPYALEE----------EIGEFW--VAEEDGEIVGCAA--------LHPLDED--------- 51
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13376261  93 tqVAYILSLGVVKEFRKHGIGSLLLESLKDHisttAQDH-CKAIYLHvltTNNTAINFYENRDFKQ--HHYLPY 163
Cdd:COG1246  52 --LAELRSLAVHPDYRGRGIGRRLLEALLAE----ARELgLKRLFLL---TTSAAIHFYEKLGFEEidKEDLPY 116
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
35-164 4.03e-08

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 50.82  E-value: 4.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376261  35 PIEYPDSWYRDITSNKKFFSLAATYRGAIVgmIVAEIKNRTkihkedgdILASNFS-VDTQVAYILSLGVVKEFRKHGIG 113
Cdd:COG0454   7 TPEDINFILLIEALDAELKAMEGSLAGAEF--IAVDDKGEP--------IGFAGLRrLDDKVLELKRLYVLPEYRGKGIG 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 13376261 114 SLLLESLkdhISTTAQDHCKAIYLHVLTTNNTAINFYENRDFKQHHYLPYY 164
Cdd:COG0454  77 KALLEAL---LEWARERGCTALELDTLDGNPAAIRFYERLGFKEIERYVAY 124
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
33-158 1.07e-07

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: 49.19  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376261    33 WFPIEYPDSWYRDITSNKKFFsLAATYRGAIVGMIvaEIKNRTKIHkedgdilasnfsvdtqvayilSLGVVKEFRKHGI 112
Cdd:pfam13673  13 FYEFISPEALRERIDQGEYFF-FVAFEGGQIVGVI--ALRDRGHIS---------------------LLFVDPDYQGQGI 68
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 13376261   113 GSLLLESLKDHISttaQDHCKAIYLhVLTTNNTAINFYENRDFKQH 158
Cdd:pfam13673  69 GKALLEAVEDYAE---KDGIKLSEL-TVNASPYAVPFYEKLGFRAT 110
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
96-166 1.54e-07

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: 48.86  E-value: 1.54e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13376261    96 AYILSLGVVKEFRKHGIGSLLLESLKDHISTTAqdhCKAIYLHVLTTNNTAINFYENRDFKQHHYLPYYYS 166
Cdd:TIGR01575  55 AHILNIAVKPEYQGQGIGRALLRELIDEAKGRG---VNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYP 122
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
95-164 2.10e-06

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 44.51  E-value: 2.10e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376261  95 VAYILSLGVVKEFRKHGIGSLLLESLKDHIsttAQDHCKAIYLHVLTTNNTAINFYENRDFKQHHYLPYY 164
Cdd:COG3393  15 VAEISGVYTHPEYRGRGLASALVAALAREA---LARGARTPFLYVDADNPAARRLYERLGFRPVGEYATV 81
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
54-138 3.19e-05

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: 40.72  E-value: 3.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376261  54 SLAATYRGAIVGMIVAEIKNRTKihkedgdilasnfsvdtQVAYILSLGVVKEFRKHGIGSLLLESLKDHIsttAQDHCK 133
Cdd:cd04301   1 FLVAEDDGEIVGFASLSPDGSGG-----------------DTAYIGDLAVLPEYRGKGIGSALLEAAEEEA---RERGAK 60

                ....*
gi 13376261 134 AIYLH 138
Cdd:cd04301  61 RLRLE 65
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
94-151 3.05e-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: 38.46  E-value: 3.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 13376261    94 QVAYILSLGVVKEFRKHGIGSLLLESLKDHISTTAQDhckaIYLHVLTTNNTAINFYE 151
Cdd:pfam08445  20 PGGELGALQTLPEHRRRGLGSRLVAALARGIAERGIT----PFAVVVAGNTPSRRLYE 73
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
103-158 3.28e-04

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 39.40  E-value: 3.28e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 13376261 103 VVKEFRKHGIGSLLLESLKDHIsttAQDHCKAIYLHVLTtnnTAINFYENRDFKQH 158
Cdd:COG2153  66 VLPEYRGQGLGRALMEAAIEEA---RERGARRIVLSAQA---HAVGFYEKLGFVPV 115
 
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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