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Conserved domains on  [gi|84374836|gb|EAP91775|]
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3-oxoacyl-(acyl carrier protein) synthase [Vibrio splendidus 12B01]

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];
1-146 6.10e-16

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


:

Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 69.73  E-value: 6.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84374836   1 MKKADLDGAALVHQAAFvRQQNSREWLQCNLSASPRFLNFVAESEGEIVGYIIWVQKSGFRPEAVLELEQLAVLPSAQGQ 80
Cdd:COG3153   4 ATPEDAEAIAALLRAAF-GPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVDIDGEGPALLLGPLAVDPEYRGQ 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 84374836  81 GLGRKLILDSLpqvkQQLAQQGsalkHVLVTTRADNFAQKLYQStLGAEVETTISNLYSADEVLMI 146
Cdd:COG3153  83 GIGRALMRAAL----EAARERG----ARAVVLLGDPSLLPFYER-FGFRPAGELGLTLGPDEVFLA 139
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
1-146 6.10e-16

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 69.73  E-value: 6.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84374836   1 MKKADLDGAALVHQAAFvRQQNSREWLQCNLSASPRFLNFVAESEGEIVGYIIWVQKSGFRPEAVLELEQLAVLPSAQGQ 80
Cdd:COG3153   4 ATPEDAEAIAALLRAAF-GPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVDIDGEGPALLLGPLAVDPEYRGQ 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 84374836  81 GLGRKLILDSLpqvkQQLAQQGsalkHVLVTTRADNFAQKLYQStLGAEVETTISNLYSADEVLMI 146
Cdd:COG3153  83 GIGRALMRAAL----EAARERG----ARAVVLLGDPSLLPFYER-FGFRPAGELGLTLGPDEVFLA 139
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 40-124 2.26e-12

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 59.01  E-value: 2.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84374836    40 FVAESEGEIVGYIIWVQKSGfrpEAVLELEQLAVLPSAQGQGLGRKLIldslpqvkQQLAQQGSALKHVLVTTRADNFAQ 119
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLDD---EGALAELRLAVHPEYRGQGIGRALL--------EAAEAAAKEGGIKLLELETTNRAA 74


                  ....*
gi 84374836   120 KLYQS 124
Cdd:pfam13508  75 AFYEK 79
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 40-87 1.12e-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: 1.12e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 84374836  40 FVAESEGEIVGYIIWVQKSGFRPEAvlELEQLAVLPSAQGQGLGRKLI 87
Cdd:cd04301   2 LVAEDDGEIVGFASLSPDGSGGDTA--YIGDLAVLPEYRGKGIGSALL 47
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 5-145 1.23e-06

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: 45.01  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84374836     5 DLDGAALVHQAAFVRQQNsREWLQCNLSAspRFLNF-VAESEGEIVGYIIwVQKSGFrpEAvlELEQLAVLPSAQGQGLG 83
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPWT-EAQFAEELAN--YHLCYlLARIGGKVVGYAG-VQIVLD--EA--HILNIAVKPEYQGQGIG 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 84374836    84 RKLiLDSLPQVkqqlaQQGSALKHVLVTTRADN-FAQKLYQStLGAEVETTISNLYSA---DEVLM 145
Cdd:TIGR01575  73 RAL-LRELIDE-----AKGRGVNEIFLEVRVSNiAAQALYKK-LGFNEIAIRRNYYPDpgeDAIVM 131
PRK07757 PRK07757
N-acetyltransferase;
40-87 1.61e-06

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 45.19  E-value: 1.61e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 84374836   40 FVAESEGEIVGY----IIWvqksgfrpEAVLELEQLAVLPSAQGQGLGRKLI 87
Cdd:PRK07757  44 YVAEEEGEIVGCcalhILW--------EDLAEIRSLAVSEDYRGQGIGRMLV 87
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
1-146 6.10e-16

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 69.73  E-value: 6.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84374836   1 MKKADLDGAALVHQAAFvRQQNSREWLQCNLSASPRFLNFVAESEGEIVGYIIWVQKSGFRPEAVLELEQLAVLPSAQGQ 80
Cdd:COG3153   4 ATPEDAEAIAALLRAAF-GPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVDIDGEGPALLLGPLAVDPEYRGQ 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 84374836  81 GLGRKLILDSLpqvkQQLAQQGsalkHVLVTTRADNFAQKLYQStLGAEVETTISNLYSADEVLMI 146
Cdd:COG3153  83 GIGRALMRAAL----EAARERG----ARAVVLLGDPSLLPFYER-FGFRPAGELGLTLGPDEVFLA 139
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 50-145 1.16e-13

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 62.75  E-value: 1.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84374836  50 GYIIWVQKsgfRPEAVLELEQLAVLPSAQGQGLGRKLILdslpQVKQQLAQQGsaLKHVLVTTRADNF-AQKLYQStLGA 128
Cdd:COG0456   1 GFALLGLV---DGGDEAEIEDLAVDPEYRGRGIGRALLE----AALERARERG--ARRLRLEVREDNEaAIALYEK-LGF 70

                        90
                ....*....|....*..
gi 84374836 129 EVETTISNLYSADEVLM 145
Cdd:COG0456  71 EEVGERPNYYGDDALVM 87
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 40-124 2.26e-12

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 59.01  E-value: 2.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84374836    40 FVAESEGEIVGYIIWVQKSGfrpEAVLELEQLAVLPSAQGQGLGRKLIldslpqvkQQLAQQGSALKHVLVTTRADNFAQ 119
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLDD---EGALAELRLAVHPEYRGQGIGRALL--------EAAEAAAKEGGIKLLELETTNRAA 74


                  ....*
gi 84374836   120 KLYQS 124
Cdd:pfam13508  75 AFYEK 79
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 23-123 6.35e-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: 58.68  E-value: 6.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84374836    23 SREWLQCNLSASPRFLNFVAESEGEIVGYIIWVQKSGFRPEAvlELEQLAVLPSAQGQGLGRKLILdslpQVKQQLAQQG 102
Cdd:pfam00583  19 EPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVG--EIEGLAVAPEYRGKGIGTALLQ----ALLEWARERG 92

                          90       100
                  ....*....|....*....|..
gi 84374836   103 saLKHVLVTTRADNF-AQKLYQ 123
Cdd:pfam00583  93 --CERIFLEVAADNLaAIALYE 112
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
24-145 6.86e-12

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 59.62  E-value: 6.86e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84374836  24 REWLQCNLSasPRFLNFVAESEGEIVGYIIWVQKSGFRPEAVLELEQLAVLPSAQGQGLGRKLildsLPQVKQQLAQQGs 103
Cdd:COG1247  41 EAWFAAILA--PGRPVLVAEEDGEVVGFASLGPFRPRPAYRGTAEESIYVDPDARGRGIGRAL----LEALIERARARG- 113

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 84374836 104 aLKHVLVTTRADN-FAQKLYQStLGAEVETTISNLYS-----ADEVLM 145
Cdd:COG1247 114 -YRRLVAVVLADNeASIALYEK-LGFEEVGTLPEVGFkfgrwLDLVLM 159
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 40-146 1.59e-11

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: 58.08  E-value: 1.59e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84374836  40 FVAESEGEIVGYIIWVqksgFRPEAVLELEQLAVLPSAQGQGLGRKLILdslpQVKQQLAQQGsaLKHVLVTTRADnfAQ 119
Cdd:COG1246  31 WVAEEDGEIVGCAALH----PLDEDLAELRSLAVHPDYRGRGIGRRLLE----ALLAEARELG--LKRLFLLTTSA--AI 98

                        90       100       110
                ....*....|....*....|....*....|
gi 84374836 120 KLYQS---TLGAEVETTISNLYSADEVLMI 146
Cdd:COG1246  99 HFYEKlgfEEIDKEDLPYAKVWQRDSVVME 128
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 34-124 1.70e-10

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: 55.35  E-value: 1.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84374836    34 SPRFLNFVAESEGEIVGYIiwvqksGFRPEAVLELeqLAVLPSAQGQGLGRKLILDslpqVKQQLAQQGSALKHVLVttR 113
Cdd:pfam13673  28 QGEYFFFVAFEGGQIVGVI------ALRDRGHISL--LFVDPDYQGQGIGKALLEA----VEDYAEKDGIKLSELTV--N 93

                          90
                  ....*....|.
gi 84374836   114 ADNFAQKLYQS 124
Cdd:pfam13673  94 ASPYAVPFYEK 104
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 40-87 1.12e-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: 1.12e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 84374836  40 FVAESEGEIVGYIIWVQKSGFRPEAvlELEQLAVLPSAQGQGLGRKLI 87
Cdd:cd04301   2 LVAEDDGEIVGFASLSPDGSGGDTA--YIGDLAVLPEYRGKGIGSALL 47
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 40-124 1.25e-08

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 50.44  E-value: 1.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84374836  40 FVAESEGEIVGYIiwvqksGFRP--EAVLELEQLAVLPSAQGQGLGRKLILDSLpqvkQQLAQQGsaLKHVLVTT-RADN 116
Cdd:COG0454  37 IAVDDKGEPIGFA------GLRRldDKVLELKRLYVLPEYRGKGIGKALLEALL----EWARERG--CTALELDTlDGNP 104


                ....*...
gi 84374836 117 FAQKLYQS 124
Cdd:COG0454 105 AAIRFYER 112
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 5-145 1.23e-06

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: 45.01  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84374836     5 DLDGAALVHQAAFVRQQNsREWLQCNLSAspRFLNF-VAESEGEIVGYIIwVQKSGFrpEAvlELEQLAVLPSAQGQGLG 83
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPWT-EAQFAEELAN--YHLCYlLARIGGKVVGYAG-VQIVLD--EA--HILNIAVKPEYQGQGIG 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 84374836    84 RKLiLDSLPQVkqqlaQQGSALKHVLVTTRADN-FAQKLYQStLGAEVETTISNLYSA---DEVLM 145
Cdd:TIGR01575  73 RAL-LRELIDE-----AKGRGVNEIFLEVRVSNiAAQALYKK-LGFNEIAIRRNYYPDpgeDAIVM 131
PRK07757 PRK07757
N-acetyltransferase;
40-87 1.61e-06

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 45.19  E-value: 1.61e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 84374836   40 FVAESEGEIVGY----IIWvqksgfrpEAVLELEQLAVLPSAQGQGLGRKLI 87
Cdd:PRK07757  44 YVAEEEGEIVGCcalhILW--------EDLAEIRSLAVSEDYRGQGIGRMLV 87
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
71-138 6.01e-05

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


Pssm-ID: 182877  Cd Length: 194  Bit Score: 41.07  E-value: 6.01e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 84374836   71 LAVLPSAQGQGLGRKLIldslpQVKQQLAQQGSaLKHVLVTTRADNF-AQKLYQsTLGAEVETTISNLY 138
Cdd:PRK10975 132 LAVFPGAQGRGIGARLM-----QAALNWCQARG-LTRLRVATQMGNLaALRLYI-RSGANIESTAYWLY 193
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
40-131 8.07e-05

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 40.17  E-value: 8.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84374836  40 FVAESEGEIVGYIIWVQKSGfrpeAVLELEQLAVLPSAQGQGLGRKLILDSLpqvkQQLAQQGsaLKHVLVTTRADnfAQ 119
Cdd:COG2153  37 LLAYDDGELVATARLLPPGD----GEAKIGRVAVLPEYRGQGLGRALMEAAI----EEARERG--ARRIVLSAQAH--AV 104

                        90
                ....*....|..
gi 84374836 120 KLYQStLGAEVE 131
Cdd:COG2153 105 GFYEK-LGFVPV 115
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 36-124 1.52e-04

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 39.53  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84374836   36 RFLNFVAESEGEIVGYIIwvqksgfrPEAVLE---LEQLAVLPSAQGQGLGRKLildsLPQVKQQLAQQGsalkhvlVTT 112
Cdd:PRK09491  39 RYLNLKLTVNGQMAAFAI--------TQVVLDeatLFNIAVDPDYQRQGLGRAL----LEHLIDELEKRG-------VAT 99

                         90
                 ....*....|....*...
gi 84374836  113 -----RADNF-AQKLYQS 124
Cdd:PRK09491 100 lwlevRASNAaAIALYES 117
PRK03624 PRK03624
putative acetyltransferase; Provisional
 40-135 2.39e-04

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 38.76  E-value: 2.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84374836   40 FVAESEGEIVGYIIwVQKSGFRPEAVleleQLAVLPSAQGQGLGRKLILdslpQVKQQLAQQGSALKHVLVttRADNFA- 118
Cdd:PRK03624  48 LVAEVGGEVVGTVM-GGYDGHRGWAY----YLAVHPDFRGRGIGRALVA----RLEKKLIARGCPKINLQV--REDNDAv 116

                         90
                 ....*....|....*..
gi 84374836  119 QKLYQsTLGAEVETTIS 135
Cdd:PRK03624 117 LGFYE-ALGYEEQDRIS 132
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 23-134 1.12e-03

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: 37.29  E-value: 1.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84374836  23 SREWLQ--CNLSASPRFLNFVAE--SEGEIVGYIIWVQKSGFRPEAvlELeQLAVLPSAQGQGLGR---KLILDslpqvk 95
Cdd:COG1670  44 ARAWLErlLADWADGGALPFAIEdkEDGELIGVVGLYDIDRANRSA--EI-GYWLAPAYWGKGYATealRALLD------ 114

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 84374836  96 qqLAQQGSALKHVLVTTRADNFA-QKLYQStLGAEVETTI 134
Cdd:COG1670 115 --YAFEELGLHRVEAEVDPDNTAsIRVLEK-LGFRLEGTL 151
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
40-118 1.63e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 36.81  E-value: 1.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84374836  40 FVAESEGEIVGYIiwvqksGFRPEAVLELEQL------AVLPSAQGQGLGRKLildsLPQVKQQLAQQGsaLKHVLVTTR 113
Cdd:COG3981  66 WLVDEDGRIVGAI------NLRHELNEFLLRVgghigyGVRPSERGKGYATEM----LRLALEEARELG--LDRVLITCD 133


                ....*
gi 84374836 114 ADNFA 118
Cdd:COG3981 134 KDNIA 138
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
61-127 4.92e-03

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 34.50  E-value: 4.92e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 84374836  61 RPEAVLELEQLAVLPSAQGQGLGRKLILdslpQVKQQLAQQGsaLKHVLVTTRADNF-AQKLYQStLG 127
Cdd:COG3393  11 ESPGVAEISGVYTHPEYRGRGLASALVA----ALAREALARG--ARTPFLYVDADNPaARRLYER-LG 71
 
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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