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Conserved domains on  [gi|21312874|ref|NP_083366|]
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N-alpha-acetyltransferase 60 isoform 1 [Mus musculus]

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 4.00e-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: 4.00e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312874  92 DTQVAYILSLGVVKEFRKHGIGSLLLESLKDHIsttAQDHCKAIYLHVLTTNNTAINFYENRDFRQHHYLPYYYSIRGVL 171
Cdd:COG0456  10 GGDEAEIEDLAVDPEYRGRGIGRALLEAALERA---RERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDALV 86
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 23-155 8.47e-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: 62.92  E-value: 8.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312874    23 IDTVKHLCGDWFPIEYPDSWYR---DITSNKKFFSLAATYRGAIVGMIVAEIKNRTKIHkedgdilassfsvdtqvAYIL 99
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDlleDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPV-----------------GEIE 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 21312874   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 4.00e-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: 4.00e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312874  92 DTQVAYILSLGVVKEFRKHGIGSLLLESLKDHIsttAQDHCKAIYLHVLTTNNTAINFYENRDFRQHHYLPYYYSIRGVL 171
Cdd:COG0456  10 GGDEAEIEDLAVDPEYRGRGIGRALLEAALERA---RERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDALV 86
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 23-155 8.47e-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: 62.92  E-value: 8.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312874    23 IDTVKHLCGDWFPIEYPDSWYR---DITSNKKFFSLAATYRGAIVGMIVAEIKNRTKIHkedgdilassfsvdtqvAYIL 99
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDlleDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPV-----------------GEIE 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 21312874   100 SLGVVKEFRKHGIGSLLLESLKDHIsttAQDHCKAIYLHVLTTNNTAINFYENRDF 155
Cdd:pfam00583  64 GLAVAPEYRGKGIGTALLQALLEWA---RERGCERIFLEVAADNLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
15-156 2.18e-10

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 57.02  E-value: 2.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312874  15 LRLLCHDDIDTVKHLCGDWFPIEYPDSWYRDITSNKKF-FSLAATYRGAIVGMIVAEIknrtkihkedgdilaSSFSVDT 93
Cdd:COG3153   1 IRPATPEDAEAIAALLRAAFGPGREAELVDRLREDPAAgLSLVAEDDGEIVGHVALSP---------------VDIDGEG 65

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21312874  94 QVAYILSLGVVKEFRKHGIGSLLLESLKDHistTAQDHCKAIYLHvltTNNTAINFYENRDFR 156
Cdd:COG3153  66 PALLLGPLAVDPEYRGQGIGRALMRAALEA---ARERGARAVVLL---GDPSLLPFYERFGFR 122
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 55-157 1.18e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 50.92  E-value: 1.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312874    55 LAATYRGAIVGMIVAEIKNrtkihkedgdilassfsvDTQVAYILSLGVVKEFRKHGIGSLLLESLKDHIsttaqdHCKA 134
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLD------------------DEGALAELRLAVHPEYRGQGIGRALLEAAEAAA------KEGG 61

                          90       100
                  ....*....|....*....|...
gi 21312874   135 IYLHVLTTNNTAINFYENRDFRQ 157
Cdd:pfam13508  62 IKLLELETTNRAAAFYEKLGFEE 84
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 96-166 8.64e-08

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: 49.63  E-value: 8.64e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21312874    96 AYILSLGVVKEFRKHGIGSLLLESLKDHISTTAqdhCKAIYLHVLTTNNTAINFYENRDFRQHHYLPYYYS 166
Cdd:TIGR01575  55 AHILNIAVKPEYQGQGIGRALLRELIDEAKGRG---VNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYP 122
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 54-138 3.89e-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: 3.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312874  54 SLAATYRGAIVGMIVAEIKNRTKihkedgdilassfsvdtQVAYILSLGVVKEFRKHGIGSLLLESLKDHIsttAQDHCK 133
Cdd:cd04301   1 FLVAEDDGEIVGFASLSPDGSGG-----------------DTAYIGDLAVLPEYRGKGIGSALLEAAEEEA---RERGAK 60


                ....*
gi 21312874 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 4.00e-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: 4.00e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312874  92 DTQVAYILSLGVVKEFRKHGIGSLLLESLKDHIsttAQDHCKAIYLHVLTTNNTAINFYENRDFRQHHYLPYYYSIRGVL 171
Cdd:COG0456  10 GGDEAEIEDLAVDPEYRGRGIGRALLEAALERA---RERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDALV 86
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 23-155 8.47e-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: 62.92  E-value: 8.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312874    23 IDTVKHLCGDWFPIEYPDSWYR---DITSNKKFFSLAATYRGAIVGMIVAEIKNRTKIHkedgdilassfsvdtqvAYIL 99
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDlleDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPV-----------------GEIE 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 21312874   100 SLGVVKEFRKHGIGSLLLESLKDHIsttAQDHCKAIYLHVLTTNNTAINFYENRDF 155
Cdd:pfam00583  64 GLAVAPEYRGKGIGTALLQALLEWA---RERGCERIFLEVAADNLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
15-156 2.18e-10

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 57.02  E-value: 2.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312874  15 LRLLCHDDIDTVKHLCGDWFPIEYPDSWYRDITSNKKF-FSLAATYRGAIVGMIVAEIknrtkihkedgdilaSSFSVDT 93
Cdd:COG3153   1 IRPATPEDAEAIAALLRAAFGPGREAELVDRLREDPAAgLSLVAEDDGEIVGHVALSP---------------VDIDGEG 65

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21312874  94 QVAYILSLGVVKEFRKHGIGSLLLESLKDHistTAQDHCKAIYLHvltTNNTAINFYENRDFR 156
Cdd:COG3153  66 PALLLGPLAVDPEYRGQGIGRALMRAALEA---ARERGARAVVLL---GDPSLLPFYERFGFR 122
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
12-173 3.43e-10

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 56.93  E-value: 3.43e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312874  12 EVSLRLLCHDDIDTVKHLCGDW-------FPIEYPD-----SWYRDITSNKkFFSLAATYRGAIVGMIVAEIknrtkihk 79
Cdd:COG1247   1 EMTIRPATPEDAPAIAAIYNEAiaegtatFETEPPSeeereAWFAAILAPG-RPVLVAEEDGEVVGFASLGP-------- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312874  80 edgdilASSFSVDTQVAYIlSLGVVKEFRKHGIGSLLLESLKDHistTAQDHCKAIYLHVLTTNNTAINFYENRDFRQHH 159
Cdd:COG1247  72 ------FRPRPAYRGTAEE-SIYVDPDARGRGIGRALLEALIER---ARARGYRRLVAVVLADNEASIALYEKLGFEEVG 141

                       170
                ....*....|....
gi 21312874 160 YLPYYYSIRGVLKD 173
Cdd:COG1247 142 TLPEVGFKFGRWLD 155
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 55-157 1.18e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 50.92  E-value: 1.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312874    55 LAATYRGAIVGMIVAEIKNrtkihkedgdilassfsvDTQVAYILSLGVVKEFRKHGIGSLLLESLKDHIsttaqdHCKA 134
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLD------------------DEGALAELRLAVHPEYRGQGIGRALLEAAEAAA------KEGG 61

                          90       100
                  ....*....|....*....|...
gi 21312874   135 IYLHVLTTNNTAINFYENRDFRQ 157
Cdd:pfam13508  62 IKLLELETTNRAAAFYEKLGFEE 84
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 13-163 2.92e-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: 51.15  E-value: 2.92e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312874  13 VSLRLLCHDDIDTVKHLCGDWFPIEypdswyrditSNKKFFslAATYRGAIVGMIVaeiknrtkIHKEDGDilassfsvd 92
Cdd:COG1246   1 MTIRPATPDDVPAILELIRPYALEE----------EIGEFW--VAEEDGEIVGCAA--------LHPLDED--------- 51

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21312874  93 tqVAYILSLGVVKEFRKHGIGSLLLESLKDHisttAQDH-CKAIYLHvltTNNTAINFYENRDFRQ--HHYLPY 163
Cdd:COG1246  52 --LAELRSLAVHPDYRGRGIGRRLLEALLAE----ARELgLKRLFLL---TTSAAIHFYEKLGFEEidKEDLPY 116
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 35-164 6.82e-08

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 50.05  E-value: 6.82e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312874  35 PIEYPDSWYRDITSNKKFFSLAATYRGAIVgmIVAEIKNRTkihkedgdILASSFS-VDTQVAYILSLGVVKEFRKHGIG 113
Cdd:COG0454   7 TPEDINFILLIEALDAELKAMEGSLAGAEF--IAVDDKGEP--------IGFAGLRrLDDKVLELKRLYVLPEYRGKGIG 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 21312874 114 SLLLESLkdhISTTAQDHCKAIYLHVLTTNNTAINFYENRDFRQHHYLPYY 164
Cdd:COG0454  77 KALLEAL---LEWARERGCTALELDTLDGNPAAIRFYERLGFKEIERYVAY 124
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 96-166 8.64e-08

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: 49.63  E-value: 8.64e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21312874    96 AYILSLGVVKEFRKHGIGSLLLESLKDHISTTAqdhCKAIYLHVLTTNNTAINFYENRDFRQHHYLPYYYS 166
Cdd:TIGR01575  55 AHILNIAVKPEYQGQGIGRALLRELIDEAKGRG---VNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYP 122
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 33-158 8.76e-08

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: 49.58  E-value: 8.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312874    33 WFPIEYPDSWYRDITSNKKFFsLAATYRGAIVGMIvaEIKNRTKIHkedgdilassfsvdtqvayilSLGVVKEFRKHGI 112
Cdd:pfam13673  13 FYEFISPEALRERIDQGEYFF-FVAFEGGQIVGVI--ALRDRGHIS---------------------LLFVDPDYQGQGI 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 21312874   113 GSLLLESLKDHISttaQDHCKAIYLhVLTTNNTAINFYENRDFRQH 158
Cdd:pfam13673  69 GKALLEAVEDYAE---KDGIKLSEL-TVNASPYAVPFYEKLGFRAT 110
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
86-164 2.56e-07

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 47.21  E-value: 2.56e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21312874  86 ASSFSVDTQVAYILSLGVVKEFRKHGIGSLLLESLKDHIsttAQDHCKAIYLHVLTTNNTAINFYENRDFRQHHYLPYY 164
Cdd:COG3393   6 AGVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREA---LARGARTPFLYVDADNPAARRLYERLGFRPVGEYATV 81
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 54-138 3.89e-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: 3.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312874  54 SLAATYRGAIVGMIVAEIKNRTKihkedgdilassfsvdtQVAYILSLGVVKEFRKHGIGSLLLESLKDHIsttAQDHCK 133
Cdd:cd04301   1 FLVAEDDGEIVGFASLSPDGSGG-----------------DTAYIGDLAVLPEYRGKGIGSALLEAAEEEA---RERGAK 60


                ....*
gi 21312874 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. ...
 94-156 1.27e-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: 39.62  E-value: 1.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21312874    94 QVAYILSLGVVKEFRKHGIGSLLLESLKDHISTTAQDhckaIYLHVLTTNNTAINFYENRDFR 156
Cdd:pfam08445  20 PGGELGALQTLPEHRRRGLGSRLVAALARGIAERGIT----PFAVVVAGNTPSRRLYEKLGFR 78
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
103-158 3.22e-04

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 39.40  E-value: 3.22e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21312874 103 VVKEFRKHGIGSLLLESLKDHIsttAQDHCKAIYLHVLTtnnTAINFYENRDFRQH 158
Cdd:COG2153  66 VLPEYRGQGLGRALMEAAIEEA---RERGARRIVLSAQA---HAVGFYEKLGFVPV 115
MDH_FMN cd04736
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ...
 139-203 1.44e-03

Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of homologous FMN-dependent a-hydroxy acid oxidizing enzymes that oxidizes (S)-mandelate to phenylglyoxalate. MDH is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).


Pssm-ID: 240087  Cd Length: 361  Bit Score: 39.04  E-value: 1.44e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21312874 139 VLTTNnTAINFYENRDFRQHHYLPYYYSIRGVLkDGFTyvlyinggHPPWTiLDYIQHLGSALAN 203
Cdd:cd04736 146 VLTTD-VAVNGYRERDLRNGFAIPFRYTPRVLL-DGIL--------HPRWL-LRFLRNGMPQLAN 199
 
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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