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Conserved domains on  [gi|1079631251|emb|SCW51676|]
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Acetyltransferase (GNAT) family protein [Ruminococcaceae bacterium YRB3002]

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 ...
63-155 5.72e-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: 5.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631251  63 GFIYYMTKGVfGSYPYLHIIAVKEEYRSHGIGKQLMRFFEDNASDQPRARYFLTVDDFNPGARKLYENLGYKCVGELPDF 142
Cdd:COG0456     1 GFALLGLVDG-GDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNY 79
                          90
                  ....*....|...
gi 1079631251 143 YKQGinCYLMMKT 155
Cdd:COG0456    80 YGDD--ALVMEKE 90
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
63-155 5.72e-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: 5.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631251  63 GFIYYMTKGVfGSYPYLHIIAVKEEYRSHGIGKQLMRFFEDNASDQPRARYFLTVDDFNPGARKLYENLGYKCVGELPDF 142
Cdd:COG0456     1 GFALLGLVDG-GDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNY 79
                          90
                  ....*....|...
gi 1079631251 143 YKQGinCYLMMKT 155
Cdd:COG0456    80 YGDD--ALVMEKE 90
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
48-152 5.26e-13

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: 62.35  E-value: 5.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631251  48 QNNVYVALDEHGKCLGFIYYMTkgVFGSYpYLHIIAVKEEYRSHGIGKQLMRFFEDNASDQPRARYFLTVDDFNPGARKL 127
Cdd:TIGR01575  29 YHLCYLLARIGGKVVGYAGVQI--VLDEA-HILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQAL 105
                          90       100
                  ....*....|....*....|....*.
gi 1079631251 128 YENLGYKCVGELPDFYK-QGINCYLM 152
Cdd:TIGR01575 106 YKKLGFNEIAIRRNYYPdPGEDAIVM 131
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
35-133 5.36e-13

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: 61.76  E-value: 5.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631251  35 HKKATDMLSYAVAQNNVYVALDEHGKCLGFIYYMTKGVFGSYPYLHIIAVKEEYRSHGIGKQLMRFFEDNASDQPRARYF 114
Cdd:pfam00583  18 DEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIF 97
                          90
                  ....*....|....*....
gi 1079631251 115 LTVDDFNPGARKLYENLGY 133
Cdd:pfam00583  98 LEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
51-116 1.19e-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: 54.20  E-value: 1.19e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1079631251  51 VYVALDEhGKCLGFIYYMTKGVFGSYPYLHIIAVKEEYRSHGIGKQLMRFFEDNASDQPRARYFLT 116
Cdd:cd04301     1 FLVAEDD-GEIVGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
82-143 9.67e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 34.52  E-value: 9.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1079631251  82 IAVKEEYRSHGIGKQLMRFFednaSDQPRARYFLT----VDDFNPGARKLYENLGYKCVGELPDFY 143
Cdd:PRK09491   69 IAVDPDYQRQGLGRALLEHL----IDELEKRGVATlwleVRASNAAAIALYESLGFNEVTIRRNYY 130
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
63-155 5.72e-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: 5.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631251  63 GFIYYMTKGVfGSYPYLHIIAVKEEYRSHGIGKQLMRFFEDNASDQPRARYFLTVDDFNPGARKLYENLGYKCVGELPDF 142
Cdd:COG0456     1 GFALLGLVDG-GDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNY 79
                          90
                  ....*....|...
gi 1079631251 143 YKQGinCYLMMKT 155
Cdd:COG0456    80 YGDD--ALVMEKE 90
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
5-144 2.08e-17

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 74.65  E-value: 2.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631251   5 IAIRLADMTYIDSCVEILQDSVLGKA--YFSDHKKATDMLSYAVAQNN----VYVAlDEHGKCLGFIYYMTKGVFGSYP- 77
Cdd:COG1247     2 MTIRPATPEDAPAIAAIYNEAIAEGTatFETEPPSEEEREAWFAAILApgrpVLVA-EEDGEVVGFASLGPFRPRPAYRg 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1079631251  78 -YLHIIAVKEEYRSHGIGKQLMRFFEDNASDQPRARYFLTVDDFNPGARKLYENLGYKCVGELPDFYK 144
Cdd:COG1247    81 tAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGF 148
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
7-139 9.58e-15

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 67.03  E-value: 9.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631251   7 IRLADMTYIDSCVEILQDSvlgkayFSDHKKAT--DMLSYAVAQNNVYVALDEhGKCLGFIYYMTKGVFGSYPYLHI--I 82
Cdd:COG3153     1 IRPATPEDAEAIAALLRAA------FGPGREAElvDRLREDPAAGLSLVAEDD-GEIVGHVALSPVDIDGEGPALLLgpL 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1079631251  83 AVKEEYRSHGIGKQLMRFFEDNASDQPRARYFLTVDdfnPGARKLYENLGYKCVGEL 139
Cdd:COG3153    74 AVDPEYRGQGIGRALMRAALEAARERGARAVVLLGD---PSLLPFYERFGFRPAGEL 127
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
74-139 1.96e-13

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 62.23  E-value: 1.96e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1079631251  74 GSYPYLHIIAVKEEYRSHGIGKQLMRFFEDNASDQPRARYFLTVDDFNPGARKLYENLGYKCVGEL 139
Cdd:COG3393    13 PGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEY 78
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
48-152 5.26e-13

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: 62.35  E-value: 5.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631251  48 QNNVYVALDEHGKCLGFIYYMTkgVFGSYpYLHIIAVKEEYRSHGIGKQLMRFFEDNASDQPRARYFLTVDDFNPGARKL 127
Cdd:TIGR01575  29 YHLCYLLARIGGKVVGYAGVQI--VLDEA-HILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQAL 105
                          90       100
                  ....*....|....*....|....*.
gi 1079631251 128 YENLGYKCVGELPDFYK-QGINCYLM 152
Cdd:TIGR01575 106 YKKLGFNEIAIRRNYYPdPGEDAIVM 131
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
35-133 5.36e-13

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: 61.76  E-value: 5.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631251  35 HKKATDMLSYAVAQNNVYVALDEHGKCLGFIYYMTKGVFGSYPYLHIIAVKEEYRSHGIGKQLMRFFEDNASDQPRARYF 114
Cdd:pfam00583  18 DEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIF 97
                          90
                  ....*....|....*....
gi 1079631251 115 LTVDDFNPGARKLYENLGY 133
Cdd:pfam00583  98 LEVAADNLAAIALYEKLGF 116
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
51-134 2.49e-11

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 56.69  E-value: 2.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631251  51 VYVALDEhGKCLGFIYYMTKGVFGSYPYLHIiAVKEEYRSHGIGKQLMRFFEDNASDQPRARYFLTVddfNPGARKLYEN 130
Cdd:pfam13508   5 FFVAEDD-GKIVGFAALLPLDDEGALAELRL-AVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRAAAFYEK 79

                  ....
gi 1079631251 131 LGYK 134
Cdd:pfam13508  80 LGFE 83
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
51-116 1.19e-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: 54.20  E-value: 1.19e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1079631251  51 VYVALDEhGKCLGFIYYMTKGVFGSYPYLHIIAVKEEYRSHGIGKQLMRFFEDNASDQPRARYFLT 116
Cdd:cd04301     1 FLVAEDD-GEIVGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
47-154 1.32e-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: 55.74  E-value: 1.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631251  47 AQNNVYVALDEHGKCLGFIYYMTKGvfgsypYLHIIAVKEEYRSHGIGKQLMRFFEDNASDQPRARYFLTVDDfNPGARK 126
Cdd:pfam13673  28 QGEYFFFVAFEGGQIVGVIALRDRG------HISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNA-SPYAVP 100
                          90       100
                  ....*....|....*....|....*...
gi 1079631251 127 LYENLGYKCVGelPDFYKQGInCYLMMK 154
Cdd:pfam13673 101 FYEKLGFRATG--PEQEFNGI-RFVPME 125
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
52-141 1.60e-10

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 55.83  E-value: 1.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631251  52 YVALDEHGKCLGF--IYYMTKGVFgsypYLHIIAVKEEYRSHGIGKQLMRFFEDNASDQPRARYFLTVDDFNPGARKLYE 129
Cdd:COG0454    36 FIAVDDKGEPIGFagLRRLDDKVL----ELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYE 111
                          90
                  ....*....|..
gi 1079631251 130 NLGYKCVGELPD 141
Cdd:COG0454   112 RLGFKEIERYVA 123
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
5-155 1.68e-10

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: 55.77  E-value: 1.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631251   5 IAIRLADMTYIDSCVEILQDSVLgkayfsdhkkatdmlsyAVAQNNVYVALDEhGKCLGFIYYMTKGvfGSYPYLHIIAV 84
Cdd:COG1246     1 MTIRPATPDDVPAILELIRPYAL-----------------EEEIGEFWVAEED-GEIVGCAALHPLD--EDLAELRSLAV 60
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1079631251  85 KEEYRSHGIGKQLMRFFEDNASDQPRARYFLTVddfNPGARKLYENLGYKCVG--ELPDFYKQGINCYLMMKT 155
Cdd:COG1246    61 HPDYRGRGIGRRLLEALLAEARELGLKRLFLLT---TSAAIHFYEKLGFEEIDkeDLPYAKVWQRDSVVMEKD 130
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
53-156 6.87e-10

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: 54.62  E-value: 6.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631251  53 VALDEHGKCLGFIYYMtkGVFGSYPYLHI-IAVKEEYRSHGIGKQLMRFFEDNASDQPRA-RYFLTVDDFNPGARKLYEN 130
Cdd:COG1670    65 IEDKEDGELIGVVGLY--DIDRANRSAEIgYWLAPAYWGKGYATEALRALLDYAFEELGLhRVEAEVDPDNTASIRVLEK 142
                          90       100
                  ....*....|....*....|....*....
gi 1079631251 131 LGYKCVGELPDFYK---QGINCYLMMKTR 156
Cdd:COG1670   143 LGFRLEGTLRDALVidgRYRDHVLYSLLR 171
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
82-155 9.33e-08

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 48.26  E-value: 9.33e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1079631251  82 IAVKEEYRSHGIGKQLMRFFEDNASDQPRARYFLTVDDfnpGARKLYENLGYKCVGElpDFYKQGINCYLMMKT 155
Cdd:COG2153    64 VAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQA---HAVGFYEKLGFVPVGE--EFLEAGIPHIDMRKP 132
COG3375 COG3375
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
1-162 7.47e-05

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


Pssm-ID: 442602 [Multi-domain]  Cd Length: 271  Bit Score: 41.47  E-value: 7.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631251   1 MSKKIAIR-LADMTYIDSCVEiLQDSVLGkayfSDHKKA--TDMLSyAVAQNNVYV--ALDEhGKCLGFIYymtkGVFGS 75
Cdd:COG3375     1 MAAGVEIReLTTPAELEAVQR-LQRSVWG----SPPNEPvpVHLLR-ALAHAGGYVlgAFDG-GELVGFSF----GFPGF 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079631251  76 YP---YL--HIIAVKEEYRSHGIGKQLMRFFEDNAsdqpRAR-YFL---TVDDFNpgARKLYEN---LGYKCVGELPDFY 143
Cdd:COG3375    70 RPgglYLhsHMAGVLPEYRGRGVGYALKLHQREWA----LERgVTLitwTFDPLQ--ARNAYFNlakLGAIAREYLPNFY 143
                         170       180
                  ....*....|....*....|..
gi 1079631251 144 KQ---GINcylmmktRGIENDR 162
Cdd:COG3375   144 GEmrdGIN-------RGLPTDR 158
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
82-143 9.67e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 34.52  E-value: 9.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1079631251  82 IAVKEEYRSHGIGKQLMRFFednaSDQPRARYFLT----VDDFNPGARKLYENLGYKCVGELPDFY 143
Cdd:PRK09491   69 IAVDPDYQRQGLGRALLEHL----IDELEKRGVATlwleVRASNAAAIALYESLGFNEVTIRRNYY 130
 
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.
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