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Conserved domains on  [gi|6325307|ref|NP_015376|]
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peptide alpha-N-acetyltransferase MAK3 [Saccharomyces cerevisiae S288C]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10456837)

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:  15581578|10940244|9175471|27367672|26818562
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 16-135 1.52e-19

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: 79.10  E-value: 1.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325307     16 FASIKKLIDADLSEPYSIYVYRYFLNQW---PELTYIAVDNksgtpNIPIGCIVCKMDPHRNvrLRGYIGMLAVESTYRG 92
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDedaSEGFFVAEED-----GELVGFASLSIIDDEP--PVGEIEGLAVAPEYRG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 6325307     93 HGIAKKLVEIAIDKMQREHCDEIMLETEVENSAALNLYEGMGF 135
Cdd:pfam00583  74 KGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 16-135 1.52e-19

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: 79.10  E-value: 1.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325307     16 FASIKKLIDADLSEPYSIYVYRYFLNQW---PELTYIAVDNksgtpNIPIGCIVCKMDPHRNvrLRGYIGMLAVESTYRG 92
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDedaSEGFFVAEED-----GELVGFASLSIIDDEP--PVGEIEGLAVAPEYRG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 6325307     93 HGIAKKLVEIAIDKMQREHCDEIMLETEVENSAALNLYEGMGF 135
Cdd:pfam00583  74 KGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 63-159 1.84e-19

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 78.16  E-value: 1.84e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325307   63 GCIVCKMDPHRNVrlrGYIGMLAVESTYRGHGIAKKLVEIAIDKMQREHCDEIMLETEVENSAALNLYEGMGFIRMKRMF 142
Cdd:COG0456   1 GFALLGLVDGGDE---AEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                        90
                ....*....|....*..
gi 6325307  143 RYYLNegDAFKLILPLT 159
Cdd:COG0456  78 NYYGD--DALVMEKELA 92
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 48-118 2.72e-09

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: 51.12  E-value: 2.72e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6325307   48 YIAVDNksgtpNIPIGCIVCKMDPHRNvrLRGYIGMLAVESTYRGHGIAKKLVEIAIDKMQREHCDEIMLE 118
Cdd:cd04301   2 LVAEDD-----GEIVGFASLSPDGSGG--DTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 76-152 3.47e-09

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: 52.33  E-value: 3.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325307     76 RLRGYIGM-----------LAVESTYRGHGIAKKLVEIAIDKMQREHCDEIMLETEVENSAALNLYEGMGFIRMKRMFRY 144
Cdd:TIGR01575  41 KVVGYAGVqivldeahilnIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNY 120


                  ....*....
gi 6325307    145 YLNEG-DAF 152
Cdd:TIGR01575 121 YPDPGeDAI 129
PRK03624 PRK03624
putative acetyltransferase; Provisional
 78-135 7.94e-07

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 46.08  E-value: 7.94e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6325307    78 RGYIGMLAVESTYRGHGIAKKLVEIAIDKMQREHCDEIMLETEVENSAALNLYEGMGF 135
Cdd:PRK03624  68 RGWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGY 125
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 16-135 1.52e-19

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: 79.10  E-value: 1.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325307     16 FASIKKLIDADLSEPYSIYVYRYFLNQW---PELTYIAVDNksgtpNIPIGCIVCKMDPHRNvrLRGYIGMLAVESTYRG 92
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDedaSEGFFVAEED-----GELVGFASLSIIDDEP--PVGEIEGLAVAPEYRG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 6325307     93 HGIAKKLVEIAIDKMQREHCDEIMLETEVENSAALNLYEGMGF 135
Cdd:pfam00583  74 KGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 63-159 1.84e-19

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 78.16  E-value: 1.84e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325307   63 GCIVCKMDPHRNVrlrGYIGMLAVESTYRGHGIAKKLVEIAIDKMQREHCDEIMLETEVENSAALNLYEGMGFIRMKRMF 142
Cdd:COG0456   1 GFALLGLVDGGDE---AEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                        90
                ....*....|....*..
gi 6325307  143 RYYLNegDAFKLILPLT 159
Cdd:COG0456  78 NYYGD--DALVMEKELA 92
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
10-158 1.46e-14

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 67.03  E-value: 1.46e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325307   10 IRNEEQ--FASIKKLIDADLSEPY-SIYVYRYFLNQWPELTYIAVDNksgtpNIPIGCIVCKMDPHRNVRLRGYIGMLAV 86
Cdd:COG3153   1 IRPATPedAEAIAALLRAAFGPGReAELVDRLREDPAAGLSLVAEDD-----GEIVGHVALSPVDIDGEGPALLLGPLAV 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325307   87 ESTYRGHGIAKKLVEIAIDKMQREHCDEIMLETeveNSAALNLYEGMGFIRMKRmFRYYLNEGDAFkLILPL 158
Cdd:COG3153  76 DPEYRGQGIGRALMRAALEAARERGARAVVLLG---DPSLLPFYERFGFRPAGE-LGLTLGPDEVF-LAKEL 142
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 11-148 1.20e-12

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 61.61  E-value: 1.20e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325307   11 RNEEQFASIKKLIDADLSEPYSIYVYRYFlnqwpeltyIAVDnksgTPNIPIGCIVCKM--DPHrnvrlrGYIGMLAVES 88
Cdd:COG0454   8 PEDINFILLIEALDAELKAMEGSLAGAEF---------IAVD----DKGEPIGFAGLRRldDKV------LELKRLYVLP 68

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325307   89 TYRGHGIAKKLVEIAIDKMQREHCDEIMLETEVENSAALNLYEGMGFIRMKRMFRYYLNE 148
Cdd:COG0454  69 EYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIERYVAYVGGE 128
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
65-146 2.85e-11

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 56.84  E-value: 2.85e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325307   65 IVCKMDPHRNVRLRGYIGMLAVESTYRGHGIAKKLVEIAIDKMQREHCDEIMLETEVENSAALNLYEGMGFIRMKRMFRY 144
Cdd:COG3393   2 LVAMAGVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEYATV 81


                ..
gi 6325307  145 YL 146
Cdd:COG3393  82 LF 83
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 61-140 2.24e-10

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: 55.77  E-value: 2.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325307   61 PIGCIVCKMDPHRNvrlrGYIGMLAVESTYRGHGIAKKLVEIAIDKMQREHCDEIMLETeveNSAALNLYEGMGFIRMKR 140
Cdd:COG1246  39 IVGCAALHPLDEDL----AELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT---TSAAIHFYEKLGFEEIDK 111
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 45-137 1.03e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 52.46  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325307     45 ELTYIAVDNksgtpNIPIGCIVCKMDPHRNVRLRGyigMLAVESTYRGHGIAKKLVEIAIDKMQREHCDEIMLETEVEns 124
Cdd:pfam13508   3 GRFFVAEDD-----GKIVGFAALLPLDDEGALAEL---RLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNR-- 72

                          90
                  ....*....|...
gi 6325307    125 aALNLYEGMGFIR 137
Cdd:pfam13508  73 -AAAFYEKLGFEE 84
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 48-118 2.72e-09

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: 51.12  E-value: 2.72e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6325307   48 YIAVDNksgtpNIPIGCIVCKMDPHRNvrLRGYIGMLAVESTYRGHGIAKKLVEIAIDKMQREHCDEIMLE 118
Cdd:cd04301   2 LVAEDD-----GEIVGFASLSPDGSGG--DTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 76-152 3.47e-09

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: 52.33  E-value: 3.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325307     76 RLRGYIGM-----------LAVESTYRGHGIAKKLVEIAIDKMQREHCDEIMLETEVENSAALNLYEGMGFIRMKRMFRY 144
Cdd:TIGR01575  41 KVVGYAGVqivldeahilnIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNY 120


                  ....*....
gi 6325307    145 YLNEG-DAF 152
Cdd:TIGR01575 121 YPDPGeDAI 129
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
84-156 3.92e-09

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 53.07  E-value: 3.92e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6325307   84 LAVESTYRGHGIAKKLVEIAIDKMQREHCDEIMLETEVENSAALNLYEGMGFIRMKRMFRYYLNEGDAFKLIL 156
Cdd:COG1247  86 IYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVL 158
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 30-149 2.00e-07

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: 48.46  E-value: 2.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325307   30 PYSIYVYRYFLNQW-------PELTYIAVDNKSGTPnipIGCI-VCKMDPHRNvrlRGYIGMlAVESTYRGHGIAKKLVE 101
Cdd:COG1670  38 PYSLEEARAWLERLladwadgGALPFAIEDKEDGEL---IGVVgLYDIDRANR---SAEIGY-WLAPAYWGKGYATEALR 110

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 6325307  102 IAIDKMQRE-HCDEIMLETEVENSAALNLYEGMGFIRMKRMFRYYLNEG 149
Cdd:COG1670 111 ALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDG 159
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
79-137 2.16e-07

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 47.49  E-value: 2.16e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6325307   79 GYIGMLAVESTYRGHGIAKKLVEIAIDKMQREHCDEIMLETEVEnsaALNLYEGMGFIR 137
Cdd:COG2153  59 AKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH---AVGFYEKLGFVP 114
PRK03624 PRK03624
putative acetyltransferase; Provisional
 78-135 7.94e-07

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 46.08  E-value: 7.94e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6325307    78 RGYIGMLAVESTYRGHGIAKKLVEIAIDKMQREHCDEIMLETEVENSAALNLYEGMGF 135
Cdd:PRK03624  68 RGWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGY 125
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 75-142 9.08e-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: 45.72  E-value: 9.08e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6325307     75 VRLRGYIGMLAVESTYRGHGIAKKLVEIAIDKMQREHCDEImlETEVENS-AALNLYEGMGFIRMKRMF 142
Cdd:pfam13673  48 LRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLS--ELTVNASpYAVPFYEKLGFRATGPEQ 114
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
 44-145 1.42e-05

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 42.77  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325307    44 PELTYIAVDNKSGTPnIPIGCIVCKMDPHRNVRLRGYIGMLAVESTYRGHGIAKKLVEIAIDKMQREHCDEIMLETEVEN 123
Cdd:PLN02706  52 DHLICVIEDAASGRI-IATGSVFVERKFIRNCGKVGHIEDVVVDSAARGKGLGKKIIEALTEHARSAGCYKVILDCSEEN 130

                         90       100
                 ....*....|....*....|...
gi 6325307   124 SAalnLYEGMGFIRMK-RMFRYY 145
Cdd:PLN02706 131 KA---FYEKCGYVRKEiQMVKYF 150
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
81-135 1.08e-04

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


Pssm-ID: 182877  Cd Length: 194  Bit Score: 41.07  E-value: 1.08e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6325307    81 IGMLAVESTYRGHGIAKKLVEIAIDKMQREHCDEIMLETEVENSAALNLYEGMGF 135
Cdd:PRK10975 129 IGLLAVFPGAQGRGIGARLMQAALNWCQARGLTRLRVATQMGNLAALRLYIRSGA 183
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 84-135 4.93e-04

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 38.37  E-value: 4.93e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 6325307    84 LAVESTYRGHGIAKKLVEIAIDKMQREHCDEIMLETEVENSAALNLYEGMGF 135
Cdd:PRK09491  69 IAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF 120
PRK10562 PRK10562
putative acetyltransferase; Provisional
 80-135 2.06e-03

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 36.58  E-value: 2.06e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6325307    80 YIGMLAVESTYRGHGIAKKLveiaIDKMQREHcDEIMLETEVENSAALNLYEGMGF 135
Cdd:PRK10562  70 FVGALFVAPKAVRRGIGKAL----MQHVQQRY-PHLSLEVYQKNQRAVNFYHAQGF 120
 
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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