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Conserved domains on  [gi|489201878|ref|WP_003111044|]
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MULTISPECIES: N-acetyltransferase [Pseudomonas]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11418877)

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
SCOP:  3000403

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
67-146 3.87e-19

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 76.62  E-value: 3.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201878  67 GYIAtcncYSIEFRGIEVWIDEFYIDEQCRGQGFGSEILEKVKSFLKSQGAAIVHLEVDENNPKAVSFYKKSGFEFRERF 146
Cdd:COG0456    1 GFAL----LGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGER 76
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
67-146 3.87e-19

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 76.62  E-value: 3.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201878  67 GYIAtcncYSIEFRGIEVWIDEFYIDEQCRGQGFGSEILEKVKSFLKSQGAAIVHLEVDENNPKAVSFYKKSGFEFRERF 146
Cdd:COG0456    1 GFAL----LGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGER 76
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
57-140 7.84e-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: 69.08  E-value: 7.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201878   57 WIICLGSKQIGYIAtcnCYSIEFRGIEVWIDEFYIDEQCRGQGFGSEILEKVKSFLKSQGAAIVHLEVDENNPKAVSFYK 136
Cdd:pfam00583  36 FVAEEDGELVGFAS---LSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYE 112

                  ....
gi 489201878  137 KSGF 140
Cdd:pfam00583 113 KLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
62-141 7.47e-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: 53.49  E-value: 7.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201878   62 GSKQIGYIAtcncysiefrgieVWIDEF-------YIDEQCRGQGFGSEILEKVKSFLKSQGAAIVHLEVDENNPKAVSF 134
Cdd:TIGR01575  39 GGKVVGYAG-------------VQIVLDeahilniAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQAL 105

                  ....*..
gi 489201878  135 YKKSGFE 141
Cdd:TIGR01575 106 YKKLGFN 112
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
56-123 2.39e-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: 50.74  E-value: 2.39e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489201878  56 VWIICLGSKQIGYIAtcnCYSIEFRGIEVWIDEFYIDEQCRGQGFGSEILEKVKSFLKSQGAAIVHLE 123
Cdd:cd04301    1 FLVAEDDGEIVGFAS---LSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PRK03624 PRK03624
putative acetyltransferase; Provisional
80-148 1.14e-06

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 45.30  E-value: 1.14e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489201878  80 RGievWIDEFYIDEQCRGQGFGSEILEKVKSFLKSQGAAIVHLEVDENNPKAVSFYKKSGFEFRERFVM 148
Cdd:PRK03624  68 RG---WAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQDRISL 133
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
67-146 3.87e-19

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 76.62  E-value: 3.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201878  67 GYIAtcncYSIEFRGIEVWIDEFYIDEQCRGQGFGSEILEKVKSFLKSQGAAIVHLEVDENNPKAVSFYKKSGFEFRERF 146
Cdd:COG0456    1 GFAL----LGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGER 76
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
57-140 7.84e-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: 69.08  E-value: 7.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201878   57 WIICLGSKQIGYIAtcnCYSIEFRGIEVWIDEFYIDEQCRGQGFGSEILEKVKSFLKSQGAAIVHLEVDENNPKAVSFYK 136
Cdd:pfam00583  36 FVAEEDGELVGFAS---LSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYE 112

                  ....
gi 489201878  137 KSGF 140
Cdd:pfam00583 113 KLGF 116
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
33-147 4.20e-14

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 65.07  E-value: 4.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201878  33 IEMTDEDrlaaLRPLLSSSEKGNVWIICLGSKQIGYIATCncySIEFRGIEVwiDEFYIDEQCRGQGFGSEILEKVKSFL 112
Cdd:COG0454   17 IEALDAE----LKAMEGSLAGAEFIAVDDKGEPIGFAGLR---RLDDKVLEL--KRLYVLPEYRGKGIGKALLEALLEWA 87
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489201878 113 KSQGAAIVHLEVDENNPKAVSFYKKSGFEFRERFV 147
Cdd:COG0454   88 RERGCTALELDTLDGNPAAIRFYERLGFKEIERYV 122
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
52-141 3.96e-13

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 60.93  E-value: 3.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201878   52 EKGNVWIICLGSKQIGYIAtcncYSIEFRGIEVWIDEFYIDEQCRGQGFGSEILEKVKSFLKSQGAAIVHLevdENNPKA 131
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAA----LLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLEL---ETTNRA 73
                          90
                  ....*....|
gi 489201878  132 VSFYKKSGFE 141
Cdd:pfam13508  74 AAFYEKLGFE 83
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
6-141 3.23e-12

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 60.39  E-value: 3.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201878   6 NIKLISASIDDELLLVELMKKYHL-----YDGIEMTDEDRLAALRPLLSSSEKgnVWIICLGSKQIGYiatcnCYSIEFR 80
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEAIAegtatFETEPPSEEEREAWFAAILAPGRP--VLVAEEDGEVVGF-----ASLGPFR 73
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489201878  81 GIE----VWIDEFYIDEQCRGQGFGSEILEKVKSFLKSQGAAIVHLEVDENNPKAVSFYKKSGFE 141
Cdd:COG1247   74 PRPayrgTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFE 138
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
7-145 8.28e-12

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 58.85  E-value: 8.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201878   7 IKLISASIDDELLLVELMKKYHLYDGIemtdedrlaalrpllsssekGNVWIICLGSKQIGYIAtcncysIEFRGIEV-W 85
Cdd:COG1246    1 MTIRPATPDDVPAILELIRPYALEEEI--------------------GEFWVAEEDGEIVGCAA------LHPLDEDLaE 54
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201878  86 IDEFYIDEQCRGQGFGSEILEKVKSFLKSQGAAIVHLEVdenNPKAVSFYKKSGFEFRER 145
Cdd:COG1246   55 LRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT---TSAAIHFYEKLGFEEIDK 111
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
84-148 1.89e-11

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 56.84  E-value: 1.89e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489201878  84 VWIDEFYIDEQCRGQGFGSEILEKVKSFLKSQGAAIVHLEVDENNPKAVSFYKKSGFEFRERFVM 148
Cdd:COG3393   16 AEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEYAT 80
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
38-141 2.15e-10

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 55.48  E-value: 2.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201878  38 EDRLAALRpllSSSEKGNVWIICLGSKQIGYIATCNCySIEFRGIEVWIDEFYIDEQCRGQGFGSEILEKVKSFLKSQGA 117
Cdd:COG3153   26 AELVDRLR---EDPAAGLSLVAEDDGEIVGHVALSPV-DIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGA 101
                         90       100
                 ....*....|....*....|....
gi 489201878 118 AIVHLEVDennPKAVSFYKKSGFE 141
Cdd:COG3153  102 RAVVLLGD---PSLLPFYERFGFR 122
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
62-141 7.47e-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: 53.49  E-value: 7.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201878   62 GSKQIGYIAtcncysiefrgieVWIDEF-------YIDEQCRGQGFGSEILEKVKSFLKSQGAAIVHLEVDENNPKAVSF 134
Cdd:TIGR01575  39 GGKVVGYAG-------------VQIVLDeahilniAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQAL 105

                  ....*..
gi 489201878  135 YKKSGFE 141
Cdd:TIGR01575 106 YKKLGFN 112
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
56-123 2.39e-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: 50.74  E-value: 2.39e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489201878  56 VWIICLGSKQIGYIAtcnCYSIEFRGIEVWIDEFYIDEQCRGQGFGSEILEKVKSFLKSQGAAIVHLE 123
Cdd:cd04301    1 FLVAEDDGEIVGFAS---LSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
86-141 2.89e-08

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: 49.19  E-value: 2.89e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 489201878   86 IDEFYIDEQCRGQGFGSEILEKVKSFLKSQGAAIVHLEVDEnNPKAVSFYKKSGFE 141
Cdd:pfam13673  54 ISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNA-SPYAVPFYEKLGFR 108
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
38-146 3.20e-08

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: 50.00  E-value: 3.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201878  38 EDRLAALRPLLSSSEKGNVWIICLGSKQIgyIATCNCYSIEFRGIEVWIDeFYIDEQCRGQGFGSEILEKVKSFLKSQ-G 116
Cdd:COG1670   45 RAWLERLLADWADGGALPFAIEDKEDGEL--IGVVGLYDIDRANRSAEIG-YWLAPAYWGKGYATEALRALLDYAFEElG 121
                         90       100       110
                 ....*....|....*....|....*....|
gi 489201878 117 AAIVHLEVDENNPKAVSFYKKSGFEFRERF 146
Cdd:COG1670  122 LHRVEAEVDPDNTASIRVLEKLGFRLEGTL 151
PRK03624 PRK03624
putative acetyltransferase; Provisional
80-148 1.14e-06

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 45.30  E-value: 1.14e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489201878  80 RGievWIDEFYIDEQCRGQGFGSEILEKVKSFLKSQGAAIVHLEVDENNPKAVSFYKKSGFEFRERFVM 148
Cdd:PRK03624  68 RG---WAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQDRISL 133
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
36-141 1.86e-06

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 44.64  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201878   36 TDEDRLAALRPLLSSS--EKGNVWIICL-GSKQIGYIaTCNCYSIEFRGIEVwidEFYIDEQCRGQGFGSEILEKVKSFL 112
Cdd:pfam13302  34 TLEEAREWLARIWAADeaERGYGWAIELkDTGFIGSI-GLYDIDGEPERAEL---GYWLGPDYWGKGYATEAVRALLEYA 109
                          90       100       110
                  ....*....|....*....|....*....|
gi 489201878  113 KSQ-GAAIVHLEVDENNPKAVSFYKKSGFE 141
Cdd:pfam13302 110 FEElGLPRLVARIDPENTASRRVLEKLGFK 139
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
83-141 1.32e-05

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 42.09  E-value: 1.32e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489201878  83 EVWIDEFYIDEQCRGQGFGSEILEKVKSFLKSQGAAIVHLEVDENnpkAVSFYKKSGFE 141
Cdd:COG2153   58 EAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH---AVGFYEKLGFV 113
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
91-140 1.22e-04

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 39.91  E-value: 1.22e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 489201878  91 IDEQCRGQGFGSEILEKVKSFLKSQGAAIVHLEVDENNPKAVSFYKKSGF 140
Cdd:PRK09491  71 VDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF 120
PTZ00330 PTZ00330
acetyltransferase; Provisional
86-145 1.33e-04

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 39.83  E-value: 1.33e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489201878  86 IDEFYIDEQCRGQGFGSEILEKVKSFLKSQGAAIVHLEVDEnnpKAVSFYKKSGFEFRER 145
Cdd:PTZ00330  85 IEDVVVDPSYRGQGLGRALISDLCEIARSSGCYKVILDCTE---DMVAFYKKLGFRACER 141
PRK10514 PRK10514
putative acetyltransferase; Provisional
86-145 2.82e-04

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 38.83  E-value: 2.82e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489201878  86 IDEFYIDEQCRGQGFGSEILEKvksflksqgAAIVH----LEVDENNPKAVSFYKKSGFEFRER 145
Cdd:PRK10514  72 MEALFVDPDVRGCGVGRMLVEH---------ALSLHpeltTDVNEQNEQAVGFYKKMGFKVTGR 126
 
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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