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Conserved domains on  [gi|1958659528|ref|XP_038942245|]
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thialysine N-epsilon-acetyltransferase isoform X1 [Rattus norvegicus]

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];
3-165 1.68e-22

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 88.51  E-value: 1.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659528   3 STRIREAKESDCGDIMRMIRElaefeklshqvkISEEGSrpspppsAFFVIPPISVALRADGFGE--NPFFHCLVAEiip 80
Cdd:COG1247     1 EMTIRPATPEDAPAIAAIYNE------------AIAEGT-------ATFETEPPSEEEREAWFAAilAPGRPVLVAE--- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659528  81 APGEpqgslVVGYgLYYFIYSTWTG-RNIYLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRLAVLNWNKKAVNLY 159
Cdd:COG1247    59 EDGE-----VVGF-ASLGPFRPRPAyRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALY 132


                  ....*.
gi 1958659528 160 KFLGAQ 165
Cdd:COG1247   133 EKLGFE 138
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-165 1.68e-22

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 88.51  E-value: 1.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659528   3 STRIREAKESDCGDIMRMIRElaefeklshqvkISEEGSrpspppsAFFVIPPISVALRADGFGE--NPFFHCLVAEiip 80
Cdd:COG1247     1 EMTIRPATPEDAPAIAAIYNE------------AIAEGT-------ATFETEPPSEEEREAWFAAilAPGRPVLVAE--- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659528  81 APGEpqgslVVGYgLYYFIYSTWTG-RNIYLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRLAVLNWNKKAVNLY 159
Cdd:COG1247    59 EDGE-----VVGF-ASLGPFRPRPAyRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALY 132


                  ....*.
gi 1958659528 160 KFLGAQ 165
Cdd:COG1247   133 EKLGFE 138
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 90-163 2.57e-16

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: 71.01  E-value: 2.57e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958659528  90 VVGYGLYYFIYSTWtgRNIYLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRLAVLNWNKKAVNLYKFLG 163
Cdd:pfam00583  44 LVGFASLSIIDDEP--PVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLG 115
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 90-146 2.44e-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: 53.82  E-value: 2.44e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958659528  90 VVGYGLYYFIYstWTGRNIYLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRL 146
Cdd:cd04301    10 IVGFASLSPDG--SGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
PTZ00330 PTZ00330
acetyltransferase; Provisional
 109-163 2.20e-06

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 45.22  E-value: 2.20e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958659528 109 YLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQfrlAVLNWNKKAVNLYKFLG 163
Cdd:PTZ00330   84 HIEDVVVDPSYRGQGLGRALISDLCEIARSSGCYK---VILDCTEDMVAFYKKLG 135
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 86-169 1.78e-05

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: 42.70  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659528  86 QGSLVVGYGLYYFIYSTWTgrniyLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRLAVLNWNKKAVNLYKFLGAQ 165
Cdd:TIGR01575  38 IGGKVVGYAGVQIVLDEAH-----ILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFN 112


                  ....
gi 1958659528 166 DLTE 169
Cdd:TIGR01575 113 EIAI 116
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-165 1.68e-22

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 88.51  E-value: 1.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659528   3 STRIREAKESDCGDIMRMIRElaefeklshqvkISEEGSrpspppsAFFVIPPISVALRADGFGE--NPFFHCLVAEiip 80
Cdd:COG1247     1 EMTIRPATPEDAPAIAAIYNE------------AIAEGT-------ATFETEPPSEEEREAWFAAilAPGRPVLVAE--- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659528  81 APGEpqgslVVGYgLYYFIYSTWTG-RNIYLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRLAVLNWNKKAVNLY 159
Cdd:COG1247    59 EDGE-----VVGF-ASLGPFRPRPAyRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALY 132


                  ....*.
gi 1958659528 160 KFLGAQ 165
Cdd:COG1247   133 EKLGFE 138
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 90-179 1.05e-16

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 72.78  E-value: 1.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659528  90 VVGYGLYyFIYSTWTGrniYLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRLAVLNWNKKAVNLYKFLGAQDLTE 169
Cdd:COG0454    45 PIGFAGL-RRLDDKVL---ELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIER 120

                          90
                  ....*....|
gi 1958659528 170 SEGWLSFRFE 179
Cdd:COG0454   121 YVAYVGGEFE 130
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 90-163 2.57e-16

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: 71.01  E-value: 2.57e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958659528  90 VVGYGLYYFIYSTWtgRNIYLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRLAVLNWNKKAVNLYKFLG 163
Cdd:pfam00583  44 LVGFASLSIIDDEP--PVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLG 115
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 92-173 6.13e-16

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 69.30  E-value: 6.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659528  92 GYGLYYFIYstwTGRNIYLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRLAVLNWNKKAVNLYKFLGAQDLTESE 171
Cdd:COG0456     1 GFALLGLVD---GGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERP 77


                  ..
gi 1958659528 172 GW 173
Cdd:COG0456    78 NY 79
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
6-169 9.35e-11

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 57.02  E-value: 9.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659528   6 IREAKESDCGDIMRMIRElaEFeklshqvkiseegsrpSPPPSAFFVIppisvALRADGfgenPFFHCLVAEIipapgep 85
Cdd:COG3153     1 IRPATPEDAEAIAALLRA--AF----------------GPGREAELVD-----RLREDP----AAGLSLVAED------- 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659528  86 qGSLVVGYGLYYFIYSTWTGRNIYLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCsqfRLAVLNWNKKAVNLYKFLGAQ 165
Cdd:COG3153    47 -DGEIVGHVALSPVDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGA---RAVVLLGDPSLLPFYERFGFR 122


                  ....
gi 1958659528 166 DLTE 169
Cdd:COG3153   123 PAGE 126
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 90-146 2.44e-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: 53.82  E-value: 2.44e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958659528  90 VVGYGLYYFIYstWTGRNIYLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRL 146
Cdd:cd04301    10 IVGFASLSPDG--SGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 72-160 8.45e-10

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 53.23  E-value: 8.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659528  72 HCLVAEiipapgepQGSLVVGYGLYYFIYSTWTGRNIyleDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRLAVLNw 151
Cdd:pfam13508   4 RFFVAE--------DDGKIVGFAALLPLDDEGALAEL---RLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTN- 71


                  ....*....
gi 1958659528 152 nkKAVNLYK 160
Cdd:pfam13508  72 --RAAAFYE 78
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
100-179 1.43e-09

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 52.60  E-value: 1.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659528 100 YSTWTGRNIYLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRLAVLNWNKKAVNLYKFLGAQDLTEsegWLSFRFE 179
Cdd:COG3393     8 VRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGE---YATVLFR 84
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 5-163 3.63e-07

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: 47.29  E-value: 3.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659528   5 RIREAKESDCGDIMRMIRELAEFEKLSHqvkiseegsrpspppsaFFVIppisvalRADGfgenpffhclvaeiipapge 84
Cdd:COG1246     2 TIRPATPDDVPAILELIRPYALEEEIGE-----------------FWVA-------EEDG-------------------- 37

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958659528  85 pqgsLVVGYGLYYFIystwTGRNIYLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRLAVlnwNKKAVNLYKFLG 163
Cdd:COG1246    38 ----EIVGCAALHPL----DEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT---TSAAIHFYEKLG 105
PTZ00330 PTZ00330
acetyltransferase; Provisional
 109-163 2.20e-06

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 45.22  E-value: 2.20e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958659528 109 YLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQfrlAVLNWNKKAVNLYKFLG 163
Cdd:PTZ00330   84 HIEDVVVDPSYRGQGLGRALISDLCEIARSSGCYK---VILDCTEDMVAFYKKLG 135
PRK03624 PRK03624
putative acetyltransferase; Provisional
 74-163 1.43e-05

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 42.99  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659528  74 LVAEiipAPGEPQGSLVVGYG-----LYYFIystwtgrniylediyVMPKYRGQGIGTKIIKKvAEVALR-KGCSQFRLA 147
Cdd:PRK03624   48 LVAE---VGGEVVGTVMGGYDghrgwAYYLA---------------VHPDFRGRGIGRALVAR-LEKKLIaRGCPKINLQ 108

                          90
                  ....*....|....*.
gi 1958659528 148 VLNWNKKAVNLYKFLG 163
Cdd:PRK03624  109 VREDNDAVLGFYEALG 124
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 86-169 1.78e-05

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: 42.70  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659528  86 QGSLVVGYGLYYFIYSTWTgrniyLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRLAVLNWNKKAVNLYKFLGAQ 165
Cdd:TIGR01575  38 IGGKVVGYAGVQIVLDEAH-----ILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFN 112


                  ....
gi 1958659528 166 DLTE 169
Cdd:TIGR01575 113 EIAI 116
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 106-176 2.43e-05

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: 42.26  E-value: 2.43e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958659528 106 RNIYLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRLAVlNWNKKAVNLYKFLG--AQDLTESEGWLSF 176
Cdd:pfam13673  50 DRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTV-NASPYAVPFYEKLGfrATGPEQEFNGIRF 121
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 90-186 5.69e-04

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: 38.83  E-value: 5.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659528  90 VVGYGLYYFIysTWTGRNIYLeDIYVMPKYRGQGIGTKIIKKVAEVALRK-GCSQFRLAVLNWNKKAVNLYKFLGaqdlt 168
Cdd:COG1670    73 LIGVVGLYDI--DRANRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLG----- 144

                          90
                  ....*....|....*...
gi 1958659528 169 esegwlsFRFEGEAMREL 186
Cdd:COG1670   145 -------FRLEGTLRDAL 155
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
 109-141 6.94e-04

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 38.53  E-value: 6.94e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958659528 109 YLEDIYVMPKYRGQGIGTKIIKKVAEVALRKGC 141
Cdd:PLN02706   87 HIEDVVVDSAARGKGLGKKIIEALTEHARSAGC 119
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
110-146 1.71e-03

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 37.09  E-value: 1.71e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1958659528 110 LEDIYVMPKYRGQGIGTKIIKKVAEVALRKGCSQFRL 146
Cdd:COG2153    61 IGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVL 97
COG5628 COG5628
Predicted acetyltransferase [General function prediction only];
2-183 4.98e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 444356  Cd Length: 163  Bit Score: 36.06  E-value: 4.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659528   2 ASTRIREAKESDCGDIMRM----IRELAEFeklsHQVKISEEGSRPSPPPSAFFVIPPISvalradgfgenPFFhclvae 77
Cdd:COG5628     1 MKVSIERVTAEDKPILENLyqlyLHDLSEF----TGILPDADGLFEYEYLDTYWTDDDRH-----------PYL------ 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659528  78 iIPAPGEPQG-SLVVGYGlyyFIYSTWtgrniYLEDIYVMPKYRGQGIGTKIIKKVaeVALRKGcsQFRLAVLNWNKKAV 156
Cdd:COG5628    60 -IYVDGEPAGfALVRRLP---FLESDY-----EIAEFFVLRKYRRKGIGKRAAHEL--FKRFPG--RWEVKQLEANVPAV 126

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1958659528 157 ----NLYKFLGAQDLTESEG------WLSFRFEGEAM 183
Cdd:COG5628   127 afwrKVIGEYTGGAYTEEERyidgrpGLVQRFEVAGP 163
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
98-140 9.11e-03

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 33.98  E-value: 9.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1958659528  98 FIYSTWTGRNIYLEDIYVMPKYRGQGIGTKIIKKVAEVALRKG 140
Cdd:COG2388    23 ELTYRLEGGVIIITHTEVPPALRGQGIASALVEAALDDARERG 65
 
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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