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Conserved domains on  [gi|19424126|ref|NP_597998|]
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thialysine N-epsilon-acetyltransferase isoform 3 [Homo sapiens]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11441181)

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

CATH:  3.40.630.30
EC:  2.3.-.-
Gene Ontology:  GO:0016746|GO:0008080
PubMed:  27367672|26818562|15581578|10940244
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-153 1.16e-26

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 98.53  E-value: 1.16e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19424126   3 SVRIREAKEGDCGDILRLIRE-----LAEFEKLSDqvkisEEALRADGFGD--NPFYHCLVAEilpAPGKllgpcVVGYg 75
Cdd:COG1247   1 EMTIRPATPEDAPAIAAIYNEaiaegTATFETEPP-----SEEEREAWFAAilAPGRPVLVAE---EDGE-----VVGF- 66

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19424126  76 IYYFIYSTWKG-RTIYLEDIYVMPEYRGQGIGSKIIKKVAEVALDKGCSQFRLAVLDWNQRAMDLYKALGAQDLTEAEG 153
Cdd:COG1247  67 ASLGPFRPRPAyRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPE 145
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-153 1.16e-26

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 98.53  E-value: 1.16e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19424126   3 SVRIREAKEGDCGDILRLIRE-----LAEFEKLSDqvkisEEALRADGFGD--NPFYHCLVAEilpAPGKllgpcVVGYg 75
Cdd:COG1247   1 EMTIRPATPEDAPAIAAIYNEaiaegTATFETEPP-----SEEEREAWFAAilAPGRPVLVAE---EDGE-----VVGF- 66

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19424126  76 IYYFIYSTWKG-RTIYLEDIYVMPEYRGQGIGSKIIKKVAEVALDKGCSQFRLAVLDWNQRAMDLYKALGAQDLTEAEG 153
Cdd:COG1247  67 ASLGPFRPRPAyRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPE 145
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 48-144 2.60e-17

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: 73.32  E-value: 2.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19424126    48 DNPFYHCLVAEIlpapgkllGPCVVGYGIYYFIYSTWKgrTIYLEDIYVMPEYRGQGIGSKIIKKVAEVALDKGCSQFRL 127
Cdd:pfam00583  29 EDASEGFFVAEE--------DGELVGFASLSIIDDEPP--VGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFL 98

                          90
                  ....*....|....*..
gi 19424126   128 AVLDWNQRAMDLYKALG 144
Cdd:pfam00583  99 EVAADNLAAIALYEKLG 115
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 71-127 2.92e-10

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: 53.43  E-value: 2.92e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19424126  71 VVGYGIYYFIYstWKGRTIYLEDIYVMPEYRGQGIGSKIIKKVAEVALDKGCSQFRL 127
Cdd:cd04301  10 IVGFASLSPDG--SGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
PTZ00330 PTZ00330
acetyltransferase; Provisional
 3-144 1.99e-09

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 53.31  E-value: 1.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19424126    3 SVRIREAKEGDCGDILRLIRELAEFEKLSdQVKISE--EALRADGFGDNPFYHCLVAEILPAPGKLLGPCVvgygiyyfi 80
Cdd:PTZ00330   6 SLELRDLEEGDLGSVLELLSHLTSAPALS-QEELEQiaARRRLAGVVTRVFVHSPTQRIVGTASLFVEPKF--------- 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19424126   81 ysTWKGRTI-YLEDIYVMPEYRGQGIGSKIIKKVAEVALDKGCSQfrlAVLDWNQRAMDLYKALG 144
Cdd:PTZ00330  76 --TRGGKCVgHIEDVVVDPSYRGQGLGRALISDLCEIARSSGCYK---VILDCTEDMVAFYKKLG 135
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 23-150 4.21e-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: 49.25  E-value: 4.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19424126    23 ELAEFEKLSDQVKISEEALRADgFGdNPFYHCLVAEIlpapgkllGPCVVGYGIYYFIYSTWKgrtiyLEDIYVMPEYRG 102
Cdd:TIGR01575   4 AVLEIEAAAFAFPWTEAQFAEE-LA-NYHLCYLLARI--------GGKVVGYAGVQIVLDEAH-----ILNIAVKPEYQG 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 19424126   103 QGIGSKIIKKVAEVALDKGCSQFRLAVLDWNQRAMDLYKALGAQDLTE 150
Cdd:TIGR01575  69 QGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAI 116
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-153 1.16e-26

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 98.53  E-value: 1.16e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19424126   3 SVRIREAKEGDCGDILRLIRE-----LAEFEKLSDqvkisEEALRADGFGD--NPFYHCLVAEilpAPGKllgpcVVGYg 75
Cdd:COG1247   1 EMTIRPATPEDAPAIAAIYNEaiaegTATFETEPP-----SEEEREAWFAAilAPGRPVLVAE---EDGE-----VVGF- 66

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19424126  76 IYYFIYSTWKG-RTIYLEDIYVMPEYRGQGIGSKIIKKVAEVALDKGCSQFRLAVLDWNQRAMDLYKALGAQDLTEAEG 153
Cdd:COG1247  67 ASLGPFRPRPAyRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPE 145
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 25-160 4.20e-18

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 75.86  E-value: 4.20e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19424126  25 AEFEKLSDQVKISEEALRADGFGDNpfYHCLVAEIlpaPGKLlgpcvVGYGIYYFIystwKGRTIYLEDIYVMPEYRGQG 104
Cdd:COG0454   9 EDINFILLIEALDAELKAMEGSLAG--AEFIAVDD---KGEP-----IGFAGLRRL----DDKVLELKRLYVLPEYRGKG 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 19424126 105 IGSKIIKKVAEVALDKGCSQFRLAVLDWNQRAMDLYKALGAQDLTEAEGWHFFCFQ 160
Cdd:COG0454  75 IGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIERYVAYVGGEFE 130
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 73-155 1.75e-17

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 72.77  E-value: 1.75e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19424126  73 GYGIYYFIYStwkGRTIYLEDIYVMPEYRGQGIGSKIIKKVAEVALDKGCSQFRLAVLDWNQRAMDLYKALGAQDLTEAE 152
Cdd:COG0456   1 GFALLGLVDG---GDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERP 77


                ...
gi 19424126 153 GWH 155
Cdd:COG0456  78 NYY 80
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 48-144 2.60e-17

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: 73.32  E-value: 2.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19424126    48 DNPFYHCLVAEIlpapgkllGPCVVGYGIYYFIYSTWKgrTIYLEDIYVMPEYRGQGIGSKIIKKVAEVALDKGCSQFRL 127
Cdd:pfam00583  29 EDASEGFFVAEE--------DGELVGFASLSIIDDEPP--VGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFL 98

                          90
                  ....*....|....*..
gi 19424126   128 AVLDWNQRAMDLYKALG 144
Cdd:pfam00583  99 EVAADNLAAIALYEKLG 115
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
6-156 3.43e-16

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 70.88  E-value: 3.43e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19424126   6 IREAKEGDCGDILRLIRELAEFEKLSDQVkiseEALRADGfgdnPFYHCLVAEIlpapgkllGPCVVGYGIYYFIYSTWK 85
Cdd:COG3153   1 IRPATPEDAEAIAALLRAAFGPGREAELV----DRLREDP----AAGLSLVAED--------DGEIVGHVALSPVDIDGE 64

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19424126  86 GRTIYLEDIYVMPEYRGQGIGSKIIKKVAEVALDKGCsqfRLAVLDWNQRAMDLYKALGAQDLTEAEGWHF 156
Cdd:COG3153  65 GPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGA---RAVVLLGDPSLLPFYERFGFRPAGELGLTLG 132
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
86-160 4.60e-12

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 58.77  E-value: 4.60e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19424126  86 GRTIYLEDIYVMPEYRGQGIGSKIIKKVAEVALDKGCSQFRLAVLDWNQRAMDLYKALGAQDLTEaegWHFFCFQ 160
Cdd:COG3393  13 PGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGE---YATVLFR 84
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 4-144 5.06e-12

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: 59.62  E-value: 5.06e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19424126   4 VRIREAKEGDCGDILRLIRELAEFEKLSdqvkiseealradgfgdnpfyHCLVAEIlpaPGKllgpcVVGYGIYYFIyst 83
Cdd:COG1246   1 MTIRPATPDDVPAILELIRPYALEEEIG---------------------EFWVAEE---DGE-----IVGCAALHPL--- 48

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19424126  84 wKGRTIYLEDIYVMPEYRGQGIGSKIIKKVAEVALDKGCSQFRLAVldwNQRAMDLYKALG 144
Cdd:COG1246  49 -DEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT---TSAAIHFYEKLG 105
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 71-127 2.92e-10

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: 53.43  E-value: 2.92e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19424126  71 VVGYGIYYFIYstWKGRTIYLEDIYVMPEYRGQGIGSKIIKKVAEVALDKGCSQFRL 127
Cdd:cd04301  10 IVGFASLSPDG--SGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 50-144 7.48e-10

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 52.84  E-value: 7.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19424126    50 PFYHCLVAEIlpapgkllGPCVVGYGIYYFIystWKGRTIYLEDIYVMPEYRGQGIGSKIIKKVAEVALDKGCSQFRLAV 129
Cdd:pfam13508   1 PGGRFFVAED--------DGKIVGFAALLPL---DDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET 69

                          90
                  ....*....|....*
gi 19424126   130 ldwNQRAMDLYKALG 144
Cdd:pfam13508  70 ---TNRAAAFYEKLG 81
PTZ00330 PTZ00330
acetyltransferase; Provisional
 3-144 1.99e-09

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 53.31  E-value: 1.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19424126    3 SVRIREAKEGDCGDILRLIRELAEFEKLSdQVKISE--EALRADGFGDNPFYHCLVAEILPAPGKLLGPCVvgygiyyfi 80
Cdd:PTZ00330   6 SLELRDLEEGDLGSVLELLSHLTSAPALS-QEELEQiaARRRLAGVVTRVFVHSPTQRIVGTASLFVEPKF--------- 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19424126   81 ysTWKGRTI-YLEDIYVMPEYRGQGIGSKIIKKVAEVALDKGCSQfrlAVLDWNQRAMDLYKALG 144
Cdd:PTZ00330  76 --TRGGKCVgHIEDVVVDPSYRGQGLGRALISDLCEIARSSGCYK---VILDCTEDMVAFYKKLG 135
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 23-150 4.21e-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: 49.25  E-value: 4.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19424126    23 ELAEFEKLSDQVKISEEALRADgFGdNPFYHCLVAEIlpapgkllGPCVVGYGIYYFIYSTWKgrtiyLEDIYVMPEYRG 102
Cdd:TIGR01575   4 AVLEIEAAAFAFPWTEAQFAEE-LA-NYHLCYLLARI--------GGKVVGYAGVQIVLDEAH-----ILNIAVKPEYQG 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 19424126   103 QGIGSKIIKKVAEVALDKGCSQFRLAVLDWNQRAMDLYKALGAQDLTE 150
Cdd:TIGR01575  69 QGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAI 116
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 4-157 1.21e-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: 48.84  E-value: 1.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19424126   4 VRIREAKEGDCGDILRLIRElAEFEKLSDQVKISEEALRA------DGFGDNPFYHCLVaeILPAPGKLLGpcVVGygiy 77
Cdd:COG1670   8 LRLRPLRPEDAEALAELLND-PEVARYLPGPPYSLEEARAwlerllADWADGGALPFAI--EDKEDGELIG--VVG---- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19424126  78 yFIYSTWKGRTIYLeDIYVMPEYRGQGIGSKIIKKVAEVALDK-GCSQFRLAVLDWNQRAMDLYKALGAQDLTEAEGWHF 156
Cdd:COG1670  79 -LYDIDRANRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALV 156


                .
gi 19424126 157 F 157
Cdd:COG1670 157 I 157
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
71-144 1.46e-04

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 39.78  E-value: 1.46e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19424126  71 VVGYG-IYYFIYSTWKgrtiyLEDIYVMPEYRGQGIGSKIIKKVAEVALDKGCSQFRLAVldwnQ-RAMDLYKALG 144
Cdd:COG2153  45 LVATArLLPPGDGEAK-----IGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSA----QaHAVGFYEKLG 111
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
 86-122 6.38e-04

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 38.15  E-value: 6.38e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 19424126   86 GRTIYLEDIYVMPEYRGQGIGSKIIKKVAEVALDKGC 122
Cdd:PLN02706  83 GKVGHIEDVVVDSAARGKGLGKKIIEALTEHARSAGC 119
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
 85-121 7.72e-04

GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both CoA and acetyl-CoA. They are characterized by highly conserved glycine, a cysteine residue in the acetyl-CoA binding site near the acetyl group, their small size compared with other GNATs and a lack of of an obvious substrate-binding site. It is proposed that they transfer an acetyl group from acetyl-CoA to one or more unidentified aliphatic amines via an acetyl (cysteine) enzyme intermediate. The substrate might be another macromolecule.


Pssm-ID: 434030 [Multi-domain]  Cd Length: 79  Bit Score: 36.73  E-value: 7.72e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 19424126    85 KGRTIYLEDIYVMPEYRGQGIGSKIIKKVAEVALDKG 121
Cdd:pfam14542  20 GDGVLIITHTEVPPALRGQGIASKLVKAALDDAREEG 56
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
48-121 9.61e-04

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 36.67  E-value: 9.61e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19424126  48 DNPFYHCLVAEIlpaPGKLLGpcvvgygiyyFIYSTWKGRTIYLEDIYVMPEYRGQGIGSKIIKKVAEVALDKG 121
Cdd:COG2388   5 HNEEKGRFELEV---DGELAG----------ELTYRLEGGVIIITHTEVPPALRGQGIASALVEAALDDARERG 65
PRK03624 PRK03624
putative acetyltransferase; Provisional
 55-144 1.67e-03

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 36.83  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19424126   55 LVAEilpAPGKLLGPCVVGYG-----IYYFIystwkgrtiylediyVMPEYRGQGIGSKIIKKvAEVAL-DKGCSQFRLA 128
Cdd:PRK03624  48 LVAE---VGGEVVGTVMGGYDghrgwAYYLA---------------VHPDFRGRGIGRALVAR-LEKKLiARGCPKINLQ 108

                         90
                 ....*....|....*.
gi 19424126  129 VLDWNQRAMDLYKALG 144
Cdd:PRK03624 109 VREDNDAVLGFYEALG 124
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 87-121 4.44e-03

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: 35.32  E-value: 4.44e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 19424126    87 RTIYLEDIYVMPEYRGQGIGSKIIKKVAEVALDKG 121
Cdd:pfam13673  50 DRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDG 84
 
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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