NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1029682427|emb|SAO72957|]
View 

acetyltransferase (GNAT) family protein [Staphylococcus aureus]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10006981)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-142 8.38e-22

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


:

Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 85.52  E-value: 8.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427   3 LRKVIMQDLDQIIALENIGFSPEEAATPEAlKLRIVQIQETFIVAEKNDEVIGYIngpvikeRYISDDLFKNVPAnnseg 82
Cdd:COG3153     1 IRPATPEDAEAIAALLRAAFGPGREAELVD-RLREDPAAGLSLVAEDDGEIVGHV-------ALSPVDIDGEGPA----- 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427  83 GYISvlGLVVAPNYQGQGIAGRLLNYFENLAKNQHRHGVTLTCRESLISFYEKYGYRNEG 142
Cdd:COG3153    68 LLLG--PLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRPAG 125
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-142 8.38e-22

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 85.52  E-value: 8.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427   3 LRKVIMQDLDQIIALENIGFSPEEAATPEAlKLRIVQIQETFIVAEKNDEVIGYIngpvikeRYISDDLFKNVPAnnseg 82
Cdd:COG3153     1 IRPATPEDAEAIAALLRAAFGPGREAELVD-RLREDPAAGLSLVAEDDGEIVGHV-------ALSPVDIDGEGPA----- 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427  83 GYISvlGLVVAPNYQGQGIAGRLLNYFENLAKNQHRHGVTLTCRESLISFYEKYGYRNEG 142
Cdd:COG3153    68 LLLG--PLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRPAG 125
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 42-139 1.49e-15

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 67.48  E-value: 1.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427  42 ETFIVAEKNDEVIGYINGpvikeryisddlfknvpANNSEGGYISVLGLVVAPNYQGQGIAGRLLNYFENLAKNQHRHGV 121
Cdd:pfam13508   3 GRFFVAEDDGKIVGFAAL-----------------LPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLL 65

                          90
                  ....*....|....*...
gi 1029682427 122 TLTCRESLISFYEKYGYR 139
Cdd:pfam13508  66 ELETTNRAAAFYEKLGFE 83
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 10-143 3.16e-11

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: 57.72  E-value: 3.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427  10 DLDQIIALENIGFSpeEAATPEALKLRIVQIQETFIVAEKNDEVIGYINGPVikeryisdDLFknvpannsEGgyiSVLG 89
Cdd:TIGR01575   1 DLKAVLEIEAAAFA--FPWTEAQFAEELANYHLCYLLARIGGKVVGYAGVQI--------VLD--------EA---HILN 59

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1029682427  90 LVVAPNYQGQGIAGRLLNYFENLAKNQHRHGVTLTCRES---LISFYEKYGYRNEGV 143
Cdd:TIGR01575  60 IAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSniaAQALYKKLGFNEIAI 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 44-124 1.49e-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: 51.51  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427  44 FIVAEKNDEVIGYIngpVIKERYISDDlfknvpannseGGYISvlGLVVAPNYQGQGIAGRLLNYFENLAKNQHRHGVTL 123
Cdd:cd04301     1 FLVAEDDGEIVGFA---SLSPDGSGGD-----------TAYIG--DLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64


                  .
gi 1029682427 124 T 124
Cdd:cd04301    65 E 65
PTZ00330 PTZ00330
acetyltransferase; Provisional
 90-139 8.36e-06

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 43.29  E-value: 8.36e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1029682427  90 LVVAPNYQGQGIAGRLLNYFENLAKNQHRHGVTLTCRESLISFYEKYGYR 139
Cdd:PTZ00330   88 VVVDPSYRGQGLGRALISDLCEIARSSGCYKVILDCTEDMVAFYKKLGFR 137
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-142 8.38e-22

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 85.52  E-value: 8.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427   3 LRKVIMQDLDQIIALENIGFSPEEAATPEAlKLRIVQIQETFIVAEKNDEVIGYIngpvikeRYISDDLFKNVPAnnseg 82
Cdd:COG3153     1 IRPATPEDAEAIAALLRAAFGPGREAELVD-RLREDPAAGLSLVAEDDGEIVGHV-------ALSPVDIDGEGPA----- 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427  83 GYISvlGLVVAPNYQGQGIAGRLLNYFENLAKNQHRHGVTLTCRESLISFYEKYGYRNEG 142
Cdd:COG3153    68 LLLG--PLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRPAG 125
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 1-139 1.09e-15

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: 69.25  E-value: 1.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427   1 MVLRKVIMQDLDQIIALENigfspeeaatPEALKLRIvqiqETFIVAEKNDEVIGYINGPVIKERYisddlfknvpanns 80
Cdd:COG1246     1 MTIRPATPDDVPAILELIR----------PYALEEEI----GEFWVAEEDGEIVGCAALHPLDEDL-------------- 52

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1029682427  81 egGYISvlGLVVAPNYQGQGIAGRLLNYFENLAKNQHRHGVTLTCRESLISFYEKYGYR 139
Cdd:COG1246    53 --AELR--SLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSAAIHFYEKLGFE 107
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 42-139 1.49e-15

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 67.48  E-value: 1.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427  42 ETFIVAEKNDEVIGYINGpvikeryisddlfknvpANNSEGGYISVLGLVVAPNYQGQGIAGRLLNYFENLAKNQHRHGV 121
Cdd:pfam13508   3 GRFFVAEDDGKIVGFAAL-----------------LPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLL 65

                          90
                  ....*....|....*...
gi 1029682427 122 TLTCRESLISFYEKYGYR 139
Cdd:pfam13508  66 ELETTNRAAAFYEKLGFE 83
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 22-153 2.71e-15

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: 68.07  E-value: 2.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427  22 FSPEEAAT------PEALKLRIVQIQETFIVAEKNDEVIGYINgpvikeryISDdlfknvpannseGGYISvlGLVVAPN 95
Cdd:pfam13673   5 YSEEGIETfyefisPEALRERIDQGEYFFFVAFEGGQIVGVIA--------LRD------------RGHIS--LLFVDPD 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427  96 YQGQGIAGRLLNYFENLAKNQHRHGVTLTCRES--LISFYEKYGYRNEGvSESCHGGIKW 153
Cdd:pfam13673  63 YQGQGIGKALLEAVEDYAEKDGIKLSELTVNASpyAVPFYEKLGFRATG-PEQEFNGIRF 121
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-157 1.39e-14

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 67.33  E-value: 1.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427   1 MVLRKVIMQDLDQIIALENIGFS------PEEAATPEALKLRIVQIQE---TFIVAEKNDEVIGYIngpvikerYISDdl 71
Cdd:COG1247     2 MTIRPATPEDAPAIAAIYNEAIAegtatfETEPPSEEEREAWFAAILApgrPVLVAEEDGEVVGFA--------SLGP-- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427  72 FKNVPANnsegGYISVLGLVVAPNYQGQGIAGRLLNYFENLAKNQHRHGVTLTCRES---LISFYEKYGYRNEGVSESC- 147
Cdd:COG1247    72 FRPRPAY----RGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADneaSIALYEKLGFEEVGTLPEVg 147

                         170
                  ....*....|
gi 1029682427 148 HGGIKWYNLV 157
Cdd:COG1247   148 FKFGRWLDLV 157
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 79-145 6.28e-14

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 63.52  E-value: 6.28e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427  79 NSEGGYISVLGLVVAPNYQGQGIAGRLLNYFENLAKNQHRHGVTLTCRES---LISFYEKYGYRNEGVSE 145
Cdd:COG0456     8 VDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDneaAIALYEKLGFEEVGERP 77
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 11-138 1.61e-12

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: 60.61  E-value: 1.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427  11 LDQIIALENIGFSPEEAATPEALKLRIVQIQ-ETFIVAEKNDEVIGYINGPVIkeryisddlfknvpanNSEGGYISVLG 89
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDAsEGFFVAEEDGELVGFASLSII----------------DDEPPVGEIEG 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1029682427  90 LVVAPNYQGQGIAGRLLNYFENLAKNQHRHGVTLTCRES---LISFYEKYGY 138
Cdd:pfam00583  65 LAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADnlaAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 10-143 3.16e-11

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: 57.72  E-value: 3.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427  10 DLDQIIALENIGFSpeEAATPEALKLRIVQIQETFIVAEKNDEVIGYINGPVikeryisdDLFknvpannsEGgyiSVLG 89
Cdd:TIGR01575   1 DLKAVLEIEAAAFA--FPWTEAQFAEELANYHLCYLLARIGGKVVGYAGVQI--------VLD--------EA---HILN 59

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1029682427  90 LVVAPNYQGQGIAGRLLNYFENLAKNQHRHGVTLTCRES---LISFYEKYGYRNEGV 143
Cdd:TIGR01575  60 IAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSniaAQALYKKLGFNEIAI 116
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
45-142 2.39e-10

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 55.19  E-value: 2.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427  45 IVAEKNDEVIGYIngpvikeRYISDDLfknvpannsEGGYISvlGLVVAPNYQGQGIAGRLLNYFENLAKNQHRHGVTLT 124
Cdd:COG2153    37 LLAYDDGELVATA-------RLLPPGD---------GEAKIG--RVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLS 98

                          90
                  ....*....|....*...
gi 1029682427 125 CRESLISFYEKYGYRNEG 142
Cdd:COG2153    99 AQAHAVGFYEKLGFVPVG 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 44-124 1.49e-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: 51.51  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427  44 FIVAEKNDEVIGYIngpVIKERYISDDlfknvpannseGGYISvlGLVVAPNYQGQGIAGRLLNYFENLAKNQHRHGVTL 123
Cdd:cd04301     1 FLVAEDDGEIVGFA---SLSPDGSGGD-----------TAYIG--DLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64


                  .
gi 1029682427 124 T 124
Cdd:cd04301    65 E 65
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 13-139 4.68e-09

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 51.98  E-value: 4.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427  13 QIIALENIGF-SPEEAATPEALKLRIVQIQETFIVAEKNDEVIGYINGpvikeRYISDDlfknvpannseGGYISvlGLV 91
Cdd:COG0454     4 RKATPEDINFiLLIEALDAELKAMEGSLAGAEFIAVDDKGEPIGFAGL-----RRLDDK-----------VLELK--RLY 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1029682427  92 VAPNYQGQGIAGRLLNYFENLAKNQHRHGVTLTCRESL---ISFYEKYGYR 139
Cdd:COG0454    66 VLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNpaaIRFYERLGFK 116
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-147 9.84e-09

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: 51.92  E-value: 9.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427   1 MVLRKVIMQDLDQIIALEN----IGFSPEEAATPEALKLRIVQIQE--------TFIVAEK-NDEVIGYINgpvikeryi 67
Cdd:COG1670     8 LRLRPLRPEDAEALAELLNdpevARYLPGPPYSLEEARAWLERLLAdwadggalPFAIEDKeDGELIGVVG--------- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427  68 sddlFKNVPANNSEGGyisvLGLVVAPNYQGQGIAGRLLNYFENLAKNQHR-HGVTLTCRE----SlISFYEKYGYRNEG 142
Cdd:COG1670    79 ----LYDIDRANRSAE----IGYWLAPAYWGKGYATEALRALLDYAFEELGlHRVEAEVDPdntaS-IRVLEKLGFRLEG 149


                  ....*
gi 1029682427 143 VSESC 147
Cdd:COG1670   150 TLRDA 154
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
82-139 2.77e-07

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 46.06  E-value: 2.77e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1029682427  82 GGYISVLGLVVAPNYQGQGIAGRLLNYFENLAKNQHRHGVTLTCRES---LISFYEKYGYR 139
Cdd:COG3393    13 PGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADnpaARRLYERLGFR 73
Eis COG4552
Predicted acetyltransferase [General function prediction only];
1-138 3.00e-07

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 48.74  E-value: 3.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427   1 MVLRKVIMQDLDQIIALENIGFSPEEAATPEALKLRIVQIQETFIVAEkNDEVIGYIngpvikeRYISDDLF---KNVPA 77
Cdd:COG4552     1 MEIRPLTEDDLDAFARLLAYAFGPEPDDEELEAYRPLLEPGRVLGVFD-DGELVGTL-------ALYPFTLNvggARVPM 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1029682427  78 nnsegGYISvlGLVVAPNYQGQGIAGRLLNYFENLAknqHRHGVTLTCresL----ISFYEKYGY 138
Cdd:COG4552    73 -----AGIT--GVAVAPEHRRRGVARALLREALAEL---RERGQPLSA---LypfePGFYRRFGY 124
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 10-139 3.21e-07

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 46.80  E-value: 3.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427  10 DLDQIIALENIGFSPEEAATPEALKLRIVQIQETfIVAEKNDEVIGyingpviKERYISDDLfkNVPANNSEGGYISvlG 89
Cdd:pfam13527   8 EFDEVLRLLEYAFQDEDSPELREYFRPLLEEGRV-LGAFDDGELVS-------TLALYPFEL--NVPGKTLPAAGIT--G 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1029682427  90 LVVAPNYQGQGIAGRLLNY-FENLAKNqhrhGVTLTCRE-SLISFYEKYGYR 139
Cdd:pfam13527  76 VATYPEYRGRGVMSRLLRRsLEEMRER----GVPLSFLYpSSYPIYRRFGYE 123
PTZ00330 PTZ00330
acetyltransferase; Provisional
 90-139 8.36e-06

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 43.29  E-value: 8.36e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1029682427  90 LVVAPNYQGQGIAGRLLNYFENLAKNQHRHGVTLTCRESLISFYEKYGYR 139
Cdd:PTZ00330   88 VVVDPSYRGQGLGRALISDLCEIARSSGCYKVILDCTEDMVAFYKKLGFR 137
PRK07757 PRK07757
N-acetyltransferase;
1-139 3.08e-05

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 41.72  E-value: 3.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427   1 MVLRKVIMQDLDQIIALENigfspEEAATPEALKLRIVQIQET---FIVAEKNDEVIGY----IngpvikeryISDDLfk 73
Cdd:PRK07757    2 MEIRKARLSDVKAIHALIN-----VYAKKGLMLPRSLDELYENirdFYVAEEEGEIVGCcalhI---------LWEDL-- 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427  74 nvpannSEggyisVLGLVVAPNYQGQGIAGRLLNYFENLAKNQhrhGV----TLTCREsliSFYEKYGYR 139
Cdd:PRK07757   66 ------AE-----IRSLAVSEDYRGQGIGRMLVEACLEEAREL---GVkrvfALTYQP---EFFEKLGFR 118
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
 91-143 4.86e-04

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 38.53  E-value: 4.86e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1029682427  91 VVAPNYQGQGIAGRLLNYFENLAKNQHRHGVTLTCRESLISFYEKYGYRNEGV 143
Cdd:PLN02706   92 VVDSAARGKGLGKKIIEALTEHARSAGCYKVILDCSEENKAFYEKCGYVRKEI 144
PRK03624 PRK03624
putative acetyltransferase; Provisional
 1-141 8.62e-04

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 37.60  E-value: 8.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029682427   1 MVLRKVIMQDLDQIIAL-ENIGFSPEEAaTPEA---LKLRivQIQETFIVAEKNDEVIGYIngpvikeryisddlfknvp 76
Cdd:PRK03624    3 MEIRVFRQADFEAVIALwERCDLTRPWN-DPEMdieRKLN--HDPSLFLVAEVGGEVVGTV------------------- 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1029682427  77 annsEGGYI----SVLGLVVAPNYQGQGIAGRLLNYFEnlAKNQHRhG---VTLTCRE---SLISFYEKYGYRNE 141
Cdd:PRK03624   61 ----MGGYDghrgWAYYLAVHPDFRGRGIGRALVARLE--KKLIAR-GcpkINLQVREdndAVLGFYEALGYEEQ 128
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH