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Conserved domains on  [gi|6651448|gb|AAF22304|]
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putative N-acetyltransferase CML3, partial [Rattus norvegicus]

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

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List of domain hits

 Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
92-192 1.61e-17

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


:

Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 75.89  E-value: 1.61e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6651448   92 SSHYSCFWVAESRGQMVGIIAVLPVKDPLlQRKQLQLRHLSVSLEHRREGIGRAMVRTALQFAEMQGFSEVVLVTSMlqy 171
Cdd:COG3153  35 DPAAGLSLVAEDDGEIVGHVALSPVDIDG-EGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDP--- 110

                        90       100
                ....*....|....*....|.
gi 6651448  172 AALALYQSMGFQKTGEFFYTF 192
Cdd:COG3153 111 SLLPFYERFGFRPAGELGLTL 131
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
92-192 1.61e-17

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 75.89  E-value: 1.61e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6651448   92 SSHYSCFWVAESRGQMVGIIAVLPVKDPLlQRKQLQLRHLSVSLEHRREGIGRAMVRTALQFAEMQGFSEVVLVTSMlqy 171
Cdd:COG3153  35 DPAAGLSLVAEDDGEIVGHVALSPVDIDG-EGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDP--- 110

                        90       100
                ....*....|....*....|.
gi 6651448  172 AALALYQSMGFQKTGEFFYTF 192
Cdd:COG3153 111 SLLPFYERFGFRPAGELGLTL 131
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 96-184 3.09e-14

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 65.55  E-value: 3.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6651448     96 SCFWVAESRGQMVGIIAVLPVKDpllqRKQLQLRHLSVSLEHRREGIGRAMVRTALQFAEMQGFSEVVLVTsmlQYAALA 175
Cdd:pfam13508   3 GRFFVAEDDGKIVGFAALLPLDD----EGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRAAA 75


                  ....*....
gi 6651448    176 LYQSMGFQK 184
Cdd:pfam13508  76 FYEKLGFEE 84
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 91-187 2.93e-10

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: 56.18  E-value: 2.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6651448     91 LSSHYSCFWVAESRGQMVGIIAVLPVKDpllqrkQLQLRHLSVSLEHRREGIGRAMVRTALQFAEMQGFSEVVLVTSMLQ 170
Cdd:TIGR01575  26 LANYHLCYLLARIGGKVVGYAGVQIVLD------EAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSN 99

                          90
                  ....*....|....*..
gi 6651448    171 YAALALYQSMGFQKTGE 187
Cdd:TIGR01575 100 IAAQALYKKLGFNEIAI 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 98-164 3.28e-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: 3.28e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6651448   98 FWVAESRGQMVGIIAVLPVKDPllqRKQLQLRHLSVSLEHRREGIGRAMVRTALQFAEMQGFSEVVL 164
Cdd:cd04301   1 FLVAEDDGEIVGFASLSPDGSG---GDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
PRK07757 PRK07757
N-acetyltransferase;
87-195 3.22e-04

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 39.79  E-value: 3.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6651448    87 PRTY--LSSHYSCFWVAESRGQMVGIIAVlpvkdPLLQRKQLQLRHLSVSLEHRREGIGRAMVRTALQFAEMQGFSEVVL 164
Cdd:PRK07757  30 PRSLdeLYENIRDFYVAEEEGEIVGCCAL-----HILWEDLAEIRSLAVSEDYRGQGIGRMLVEACLEEARELGVKRVFA 104

                         90       100       110
                 ....*....|....*....|....*....|.
gi 6651448   165 VTsmlqyaalalYQSMGFQKTGeffYTFVSR 195
Cdd:PRK07757 105 LT----------YQPEFFEKLG---FREVDK 122
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
92-192 1.61e-17

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 75.89  E-value: 1.61e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6651448   92 SSHYSCFWVAESRGQMVGIIAVLPVKDPLlQRKQLQLRHLSVSLEHRREGIGRAMVRTALQFAEMQGFSEVVLVTSMlqy 171
Cdd:COG3153  35 DPAAGLSLVAEDDGEIVGHVALSPVDIDG-EGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDP--- 110

                        90       100
                ....*....|....*....|.
gi 6651448  172 AALALYQSMGFQKTGEFFYTF 192
Cdd:COG3153 111 SLLPFYERFGFRPAGELGLTL 131
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 97-187 1.32e-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: 70.41  E-value: 1.32e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6651448   97 CFWVAESRGQMVGIIAVLPVKDPLLQrkqlqLRHLSVSLEHRREGIGRAMVRTALQFAEMQGFSEVVLVTSmlqYAALAL 176
Cdd:COG1246  29 EFWVAEEDGEIVGCAALHPLDEDLAE-----LRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTT---SAAIHF 100

                        90
                ....*....|.
gi 6651448  177 YQSMGFQKTGE 187
Cdd:COG1246 101 YEKLGFEEIDK 111
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 96-184 3.09e-14

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 65.55  E-value: 3.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6651448     96 SCFWVAESRGQMVGIIAVLPVKDpllqRKQLQLRHLSVSLEHRREGIGRAMVRTALQFAEMQGFSEVVLVTsmlQYAALA 175
Cdd:pfam13508   3 GRFFVAEDDGKIVGFAALLPLDD----EGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRAAA 75


                  ....*....
gi 6651448    176 LYQSMGFQK 184
Cdd:pfam13508  76 FYEKLGFEE 84
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
98-188 1.22e-13

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 65.79  E-value: 1.22e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6651448   98 FWVAESRGQMVGIIAVLPVKDPLLQRKQLQLrHLSVSLEHRREGIGRAMVRTALQFAEMQGFSEVVLVTSMLQYAALALY 177
Cdd:COG1247  54 VLVAEEDGEVVGFASLGPFRPRPAYRGTAEE-SIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALY 132

                        90
                ....*....|.
gi 6651448  178 QSMGFQKTGEF 188
Cdd:COG1247 133 EKLGFEEVGTL 143
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 84-199 2.41e-13

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 64.69  E-value: 2.41e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6651448   84 ADIPRTYLSSHYSCFWVAESRGQMVGIIAVLPVKDpllqrKQLQLRHLSVSLEHRREGIGRAMVRTALQFAEMQGFSEVV 163
Cdd:COG0454  22 AELKAMEGSLAGAEFIAVDDKGEPIGFAGLRRLDD-----KVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALE 96

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 6651448  164 LVTSMLQYAALALYQSMGFQKTGEF----FYTFVSRLRNS 199
Cdd:COG0454  97 LDTLDGNPAAIRFYERLGFKEIERYvayvGGEFEKELSLS 136
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 109-188 2.72e-12

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 60.44  E-value: 2.72e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6651448  109 GIIAVLPVKDPllqrKQLQLRHLSVSLEHRREGIGRAMVRTALQFAEMQGFSEVVLVTSMLQYAALALYQSMGFQKTGEF 188
Cdd:COG0456   1 GFALLGLVDGG----DEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGER 76
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 71-182 3.21e-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: 60.99  E-value: 3.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6651448     71 WEKYTAMCLHSDMADIpRTYLSSHYSCFWVAESRGQMVGIIAVLPVKDPllqRKQLQLRHLSVSLEHRREGIGRAMVRTA 150
Cdd:pfam00583   9 SEEFPEPWPDEPLDLL-EDWDEDASEGFFVAEEDGELVGFASLSIIDDE---PPVGEIEGLAVAPEYRGKGIGTALLQAL 84

                          90       100       110
                  ....*....|....*....|....*....|..
gi 6651448    151 LQFAEMQGFSEVVLVTSMLQYAALALYQSMGF 182
Cdd:pfam00583  85 LEWARERGCERIFLEVAADNLAAIALYEKLGF 116
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
100-189 2.59e-11

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 59.04  E-value: 2.59e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6651448  100 VAESRGQMVGIIAVLPVKDPllqrkQLQLRHLSVSLEHRREGIGRAMVRTALQFAEMQGFSEVVLVTsmlQYAALALYQS 179
Cdd:COG2153  38 LAYDDGELVATARLLPPGDG-----EAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSA---QAHAVGFYEK 109

                        90
                ....*....|
gi 6651448  180 MGFQKTGEFF 189
Cdd:COG2153 110 LGFVPVGEEF 119
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 91-187 2.93e-10

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: 56.18  E-value: 2.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6651448     91 LSSHYSCFWVAESRGQMVGIIAVLPVKDpllqrkQLQLRHLSVSLEHRREGIGRAMVRTALQFAEMQGFSEVVLVTSMLQ 170
Cdd:TIGR01575  26 LANYHLCYLLARIGGKVVGYAGVQIVLD------EAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSN 99

                          90
                  ....*....|....*..
gi 6651448    171 YAALALYQSMGFQKTGE 187
Cdd:TIGR01575 100 IAAQALYKKLGFNEIAI 116
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 98-190 2.75e-09

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: 53.43  E-value: 2.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6651448     98 FWVAESRGQMVGIIAVLpvkdpllqrkqlQLRHLS---VSLEHRREGIGRAMVRTALQFAEMQGFSEV-VLVTSMLqyAA 173
Cdd:pfam13673  33 FFVAFEGGQIVGVIALR------------DRGHISllfVDPDYQGQGIGKALLEAVEDYAEKDGIKLSeLTVNASP--YA 98

                          90
                  ....*....|....*..
gi 6651448    174 LALYQSMGFQKTGEFFY 190
Cdd:pfam13673  99 VPFYEKLGFRATGPEQE 115
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 98-164 3.28e-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: 3.28e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6651448   98 FWVAESRGQMVGIIAVLPVKDPllqRKQLQLRHLSVSLEHRREGIGRAMVRTALQFAEMQGFSEVVL 164
Cdd:cd04301   1 FLVAEDDGEIVGFASLSPDGSG---GDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
136-195 8.06e-09

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 51.06  E-value: 8.06e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6651448  136 EHRREGIGRAMVRTALQFAEMQGFSEVVLVTSMLQYAALALYQSMGFQKTGEFFYTFVSR 195
Cdd:COG3393  26 EYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEYATVLFRK 85
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 92-188 4.49e-05

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: 42.29  E-value: 4.49e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6651448   92 SSHYSCFWVAESR--GQMVGIIAVLPVkDPLLQRKQLqlrHLSVSLEHRREGIGRAMVRTALQFA-EMQGFSEVVLVTSM 168
Cdd:COG1670  56 ADGGALPFAIEDKedGELIGVVGLYDI-DRANRSAEI---GYWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDP 131

                        90       100
                ....*....|....*....|
gi 6651448  169 LQYAALALYQSMGFQKTGEF 188
Cdd:COG1670 132 DNTASIRVLEKLGFRLEGTL 151
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
70-166 3.15e-04

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 39.89  E-value: 3.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6651448   70 PWEKYTAMCL-HSDMADIPRTYLSSHYscFWVAESRGQMVGIIAVlpvkdpllqRKQLQ--LRHL------SVSLEHRRE 140
Cdd:COG3981  38 DFEAWLERLLdEEKGEELPEGWVPATT--YWLVDEDGRIVGAINL---------RHELNefLLRVgghigyGVRPSERGK 106

                        90       100
                ....*....|....*....|....*.
gi 6651448  141 GIGRAMVRTALQFAEMQGFSEvVLVT 166
Cdd:COG3981 107 GYATEMLRLALEEARELGLDR-VLIT 131
PRK07757 PRK07757
N-acetyltransferase;
87-195 3.22e-04

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 39.79  E-value: 3.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6651448    87 PRTY--LSSHYSCFWVAESRGQMVGIIAVlpvkdPLLQRKQLQLRHLSVSLEHRREGIGRAMVRTALQFAEMQGFSEVVL 164
Cdd:PRK07757  30 PRSLdeLYENIRDFYVAEEEGEIVGCCAL-----HILWEDLAEIRSLAVSEDYRGQGIGRMLVEACLEEARELGVKRVFA 104

                         90       100       110
                 ....*....|....*....|....*....|.
gi 6651448   165 VTsmlqyaalalYQSMGFQKTGeffYTFVSR 195
Cdd:PRK07757 105 LT----------YQPEFFEKLG---FREVDK 122
Eis COG4552
Predicted acetyltransferase [General function prediction only];
98-182 5.57e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 37.19  E-value: 5.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6651448   98 FWVAESRGQMVGIIAVLPVkdpllqrkQLQLR----------HLSVSLEHRREGIGRAMVRTALqfAEMQGFSEVVlvtS 167
Cdd:COG4552  43 VLGVFDDGELVGTLALYPF--------TLNVGgarvpmagitGVAVAPEHRRRGVARALLREAL--AELRERGQPL---S 109

                        90
                ....*....|....*
gi 6651448  168 MLQYAALALYQSMGF 182
Cdd:COG4552 110 ALYPFEPGFYRRFGY 124
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
131-183 5.66e-03

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


Pssm-ID: 182877  Cd Length: 194  Bit Score: 36.45  E-value: 5.66e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6651448   131 LSVSLEHRREGIGRAMVRTALQFAEMQGFSEVVLVTSMLQYAALALYQSMGFQ 183
Cdd:PRK10975 132 LAVFPGAQGRGIGARLMQAALNWCQARGLTRLRVATQMGNLAALRLYIRSGAN 184
 
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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