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Conserved domains on  [gi|492400740|ref|WP_005832381|]
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MULTISPECIES: GNAT family N-acetyltransferase [Bacteroidales]

Protein Classification

GNAT family protein( domain architecture ID 106742)

GNAT (Gcn5-related N-acetyltransferase) family protein similar to N-acetyltransferases that catalyze the transfer of an acetyl group from acetyl-CoA to a substrate

PubMed:  15581578

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NAT_SF super family cl17182
N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of ...
 2-138 4.84e-42

N-Acyltransferase superfamily: Various enyzmes that characteristicly 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, 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 mechanism is an ordered Bi-Bi ternary complex kinetic mechanism for most GNATs: 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 then 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/ph enylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


The actual alignment was detected with superfamily member PRK10514:

Pssm-ID: 473072 [Multi-domain]  Cd Length: 145  Bit Score: 136.29  E-value: 4.84e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400740   2 IRKIKVTDYPRLIEIWESAVLSTHDFLKEEDCLYYKEQLPVYFQYVTL-FGFEQEGILIGFMGIAEGNLEMLFIDNNYRG 80
Cdd:PRK10514   4 IRRSRHEEGERLVAIWRRSVDATHDFLSAEDRAEIEELVRSFLPEAPLwVAVDERDQPVGFMLLSGGHMEALFVDPDVRG 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 492400740  81 TGIGKKLVTYAIN-HLQVTkVDVNEQNIQAVGFYKYIGFNVYKRSDLDGEGKEYPILHM 138
Cdd:PRK10514  84 CGVGRMLVEHALSlHPELT-TDVNEQNEQAVGFYKKMGFKVTGRSEVDDQGRPYPLLHL 141
 
Name Accession Description Interval E-value
PRK10514 PRK10514
putative acetyltransferase; Provisional
 2-138 4.84e-42

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 136.29  E-value: 4.84e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400740   2 IRKIKVTDYPRLIEIWESAVLSTHDFLKEEDCLYYKEQLPVYFQYVTL-FGFEQEGILIGFMGIAEGNLEMLFIDNNYRG 80
Cdd:PRK10514   4 IRRSRHEEGERLVAIWRRSVDATHDFLSAEDRAEIEELVRSFLPEAPLwVAVDERDQPVGFMLLSGGHMEALFVDPDVRG 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 492400740  81 TGIGKKLVTYAIN-HLQVTkVDVNEQNIQAVGFYKYIGFNVYKRSDLDGEGKEYPILHM 138
Cdd:PRK10514  84 CGVGRMLVEHALSlHPELT-TDVNEQNEQAVGFYKKMGFKVTGRSEVDDQGRPYPLLHL 141
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 45-118 3.61e-13

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: 61.90  E-value: 3.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400740   45 QYVTLFGFEQEGILIGFMGIAEGN-LEMLFIDNNYRGTGIGKKLVTYAINH-----LQVTKVDVNEQNiQAVGFYKYIGF 118
Cdd:pfam13673  29 GEYFFFVAFEGGQIVGVIALRDRGhISLLFVDPDYQGQGIGKALLEAVEDYaekdgIKLSELTVNASP-YAVPFYEKLGF 107
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-118 6.24e-11

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 56.93  E-value: 6.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400740   1 MIRKIKVTDYPRLIEIWESAVLSTH-DFLKEEDCLyykEQLPVYFQYVTLFGF-----EQEGILIGFM------------ 62
Cdd:COG1247    3 TIRPATPEDAPAIAAIYNEAIAEGTaTFETEPPSE---EEREAWFAAILAPGRpvlvaEEDGEVVGFAslgpfrprpayr 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492400740  63 GIAEgnlEMLFIDNNYRGTGIGKKLVTYAINHLQ---VTKV--DVNEQNIQAVGFYKYIGF 118
Cdd:COG1247   80 GTAE---ESIYVDPDARGRGIGRALLEALIERARargYRRLvaVVLADNEASIALYEKLGF 137
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 49-96 8.22e-06

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: 41.11  E-value: 8.22e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 492400740  49 LFGFEQEGILIGFMGIA-------EGNLEMLFIDNNYRGTGIGKKLVTYAINHLQ 96
Cdd:cd04301    1 FLVAEDDGEIVGFASLSpdgsggdTAYIGDLAVLPEYRGKGIGSALLEAAEEEAR 55
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 45-123 2.95e-04

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: 38.08  E-value: 2.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400740   45 QYVTLFGFEQEGILIGFMGIA----EGNLEMLFIDNNYRGTGIGKKLVTYAINHL---QVTKV--DVNEQNIQAVGFYKY 115
Cdd:TIGR01575  29 YHLCYLLARIGGKVVGYAGVQivldEAHILNIAVKPEYQGQGIGRALLRELIDEAkgrGVNEIflEVRVSNIAAQALYKK 108


                  ....*...
gi 492400740  116 IGFNVYKR 123
Cdd:TIGR01575 109 LGFNEIAI 116
 
Name Accession Description Interval E-value
PRK10514 PRK10514
putative acetyltransferase; Provisional
 2-138 4.84e-42

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 136.29  E-value: 4.84e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400740   2 IRKIKVTDYPRLIEIWESAVLSTHDFLKEEDCLYYKEQLPVYFQYVTL-FGFEQEGILIGFMGIAEGNLEMLFIDNNYRG 80
Cdd:PRK10514   4 IRRSRHEEGERLVAIWRRSVDATHDFLSAEDRAEIEELVRSFLPEAPLwVAVDERDQPVGFMLLSGGHMEALFVDPDVRG 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 492400740  81 TGIGKKLVTYAIN-HLQVTkVDVNEQNIQAVGFYKYIGFNVYKRSDLDGEGKEYPILHM 138
Cdd:PRK10514  84 CGVGRMLVEHALSlHPELT-TDVNEQNEQAVGFYKKMGFKVTGRSEVDDQGRPYPLLHL 141
PRK10562 PRK10562
putative acetyltransferase; Provisional
 1-120 4.74e-16

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 69.71  E-value: 4.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400740   1 MIRKIKVTDYPRLIEIWESAVLSTHDFLKEEdclYYKEQLP----VYFQYVTLFGFEQEGILIGFMGIAEGN-LEMLFID 75
Cdd:PRK10562   1 MIREYQPSDLPAILQLWLESTIWAHPFIKEQ---YWRESAPlvrdVYLPAAQTWVWEEDGKLLGFVSVLEGRfVGALFVA 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 492400740  76 NNYRGTGIGKKLVTYAINHLQVTKVDVNEQNIQAVGFYKYIGFNV 120
Cdd:PRK10562  78 PKAVRRGIGKALMQHVQQRYPHLSLEVYQKNQRAVNFYHAQGFRI 122
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 45-118 3.61e-13

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: 61.90  E-value: 3.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400740   45 QYVTLFGFEQEGILIGFMGIAEGN-LEMLFIDNNYRGTGIGKKLVTYAINH-----LQVTKVDVNEQNiQAVGFYKYIGF 118
Cdd:pfam13673  29 GEYFFFVAFEGGQIVGVIALRDRGhISLLFVDPDYQGQGIGKALLEAVEDYaekdgIKLSELTVNASP-YAVPFYEKLGF 107
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-118 6.24e-11

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 56.93  E-value: 6.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400740   1 MIRKIKVTDYPRLIEIWESAVLSTH-DFLKEEDCLyykEQLPVYFQYVTLFGF-----EQEGILIGFM------------ 62
Cdd:COG1247    3 TIRPATPEDAPAIAAIYNEAIAEGTaTFETEPPSE---EEREAWFAAILAPGRpvlvaEEDGEVVGFAslgpfrprpayr 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492400740  63 GIAEgnlEMLFIDNNYRGTGIGKKLVTYAINHLQ---VTKV--DVNEQNIQAVGFYKYIGF 118
Cdd:COG1247   80 GTAE---ESIYVDPDARGRGIGRALLEALIERARargYRRLvaVVLADNEASIALYEKLGF 137
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 66-125 5.71e-09

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 50.04  E-value: 5.71e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492400740  66 EGNLEMLFIDNNYRGTGIGKKLVTYAINHLQ---VTKV--DVNEQNIQAVGFYKYIGFNVYKRSD 125
Cdd:COG0456   13 EAEIEDLAVDPEYRGRGIGRALLEAALERARergARRLrlEVREDNEAAIALYEKLGFEEVGERP 77
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 1-134 1.73e-08

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: 49.61  E-value: 1.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400740   1 MIRKIKVTDYPRLIEIWESAVLSTHDflkeedclyykeqlpvyfqyVTLFGFEQEGILIGFMGIA-----EGNLEMLFID 75
Cdd:COG1246    2 TIRPATPDDVPAILELIRPYALEEEI--------------------GEFWVAEEDGEIVGCAALHpldedLAELRSLAVH 61

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492400740  76 NNYRGTGIGKKLVTYAINH---LQVTKVDVnEQNIQAVGFYKYIGFNVYKRSDLDGEGKEYP 134
Cdd:COG1246   62 PDYRGRGIGRRLLEALLAEareLGLKRLFL-LTTSAAIHFYEKLGFEEIDKEDLPYAKVWQR 122
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
2-133 1.04e-07

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 47.77  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400740   2 IRKIKVTDYPRLIEIWESAvlstHDFLKEEDCLyykEQLPVYFQYVTLFGFEQEGILIGFMGIAEGN---------LEML 72
Cdd:COG3153    1 IRPATPEDAEAIAALLRAA----FGPGREAELV---DRLREDPAAGLSLVAEDDGEIVGHVALSPVDidgegpallLGPL 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492400740  73 FIDNNYRGTGIGKKLVTYAINHLQ---VTKVdVNEQNIQAVGFYKYIGFNVYKRSDLDGEGKEY 133
Cdd:COG3153   74 AVDPEYRGQGIGRALMRAALEAARergARAV-VLLGDPSLLPFYERFGFRPAGELGLTLGPDEV 136
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 48-118 1.66e-07

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: 46.74  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400740   48 TLFGFEQEGILIGFMGIAEGN-------LEMLFIDNNYRGTGIGKKLVTYAINHL-----QVTKVDVNEQNIQAVGFYKY 115
Cdd:pfam00583  34 GFFVAEEDGELVGFASLSIIDdeppvgeIEGLAVAPEYRGKGIGTALLQALLEWArergcERIFLEVAADNLAAIALYEK 113


                  ...
gi 492400740  116 IGF 118
Cdd:pfam00583 114 LGF 116
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 12-120 2.47e-07

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 46.59  E-value: 2.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400740  12 RLIEIWESAVLSTHDFLKEEdclyYKEQLPVYFQYvTLFGFEQEGILIGFMGIAEGN-----LEMLFIDNNYRGTGIGKK 86
Cdd:COG0454    4 RKATPEDINFILLIEALDAE----LKAMEGSLAGA-EFIAVDDKGEPIGFAGLRRLDdkvleLKRLYVLPEYRGKGIGKA 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 492400740  87 LVTYAI-----NHLQVTKVDVNEQNIQAVGFYKYIGFNV 120
Cdd:COG0454   79 LLEALLewareRGCTALELDTLDGNPAAIRFYERLGFKE 117
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 48-118 7.12e-07

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 44.37  E-value: 7.12e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492400740   48 TLFGFEQEGILIGFMGIAEGNLE------MLFIDNNYRGTGIGKKLVTYAINHLQVTKVDV--NEQNIQAVGFYKYIGF 118
Cdd:pfam13508   4 RFFVAEDDGKIVGFAALLPLDDEgalaelRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLleLETTNRAAAFYEKLGF 82
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 49-96 8.22e-06

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: 41.11  E-value: 8.22e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 492400740  49 LFGFEQEGILIGFMGIA-------EGNLEMLFIDNNYRGTGIGKKLVTYAINHLQ 96
Cdd:cd04301    1 FLVAEDDGEIVGFASLSpdgsggdTAYIGDLAVLPEYRGKGIGSALLEAAEEEAR 55
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
50-121 3.75e-05

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 40.55  E-value: 3.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400740  50 FGFEQEGILIG-----FMGIAEGNLEMLFIDNNYRGTGIGKKLVTYAINHLQ---VTKVDVNEQnIQAVGFYKYIGFNVY 121
Cdd:COG2153   37 LLAYDDGELVAtarllPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARergARRIVLSAQ-AHAVGFYEKLGFVPV 115
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 2-140 9.21e-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: 39.98  E-value: 9.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400740   2 IRKIKVTDYPRLIEIWESAVLSTHDFLKEEDclyyKEQLPVYFQYVT---------LFGFE--QEGILIGFMGI-----A 65
Cdd:COG1670   10 LRPLRPEDAEALAELLNDPEVARYLPGPPYS----LEEARAWLERLLadwadggalPFAIEdkEDGELIGVVGLydidrA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400740  66 EGNLEM-LFIDNNYRGTGIG----KKLVTYAINHLQVTKV--DVNEQNIQAVGFYKYIGFNV--YKRSDLDGEGKEYPIL 136
Cdd:COG1670   86 NRSAEIgYWLAPAYWGKGYAtealRALLDYAFEELGLHRVeaEVDPDNTASIRVLEKLGFRLegTLRDALVIDGRYRDHV 165


                 ....
gi 492400740 137 HMQL 140
Cdd:COG1670  166 LYSL 169
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 45-123 2.95e-04

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: 38.08  E-value: 2.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400740   45 QYVTLFGFEQEGILIGFMGIA----EGNLEMLFIDNNYRGTGIGKKLVTYAINHL---QVTKV--DVNEQNIQAVGFYKY 115
Cdd:TIGR01575  29 YHLCYLLARIGGKVVGYAGVQivldEAHILNIAVKPEYQGQGIGRALLRELIDEAkgrGVNEIflEVRVSNIAAQALYKK 108


                  ....*...
gi 492400740  116 IGFNVYKR 123
Cdd:TIGR01575 109 LGFNEIAI 116
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
63-118 3.64e-03

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 34.50  E-value: 3.64e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492400740  63 GIAEgnLEMLFIDNNYRGTGIGKKLVTYAINHLQ---VTKV--DVNEQNIQAVGFYKYIGF 118
Cdd:COG3393   14 GVAE--ISGVYTHPEYRGRGLASALVAALAREALargARTPflYVDADNPAARRLYERLGF 72
 
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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