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Conserved domains on  [gi|17566320|ref|NP_505053|]
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N-alpha-acetyltransferase 20 [Caenorhabditis elegans]

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
PubMed:  27367672|26818562|15581578|10940244
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 ...
 55-152 6.37e-17

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 71.61  E-value: 6.37e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566320  55 AYVMGKIEGRDTnwHGHVTALSVAPNFRRLGLAAYMMEFLERTSEARRAYFVDLFVRVSNKIAIELYKKLGYVVYRQIIG 134
Cdd:COG0456   1 GFALLGLVDGGD--EAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPN 78

                        90
                ....*....|....*...
gi 17566320 135 YYtgdrDEDAFDMRKSLS 152
Cdd:COG0456  79 YY----GDDALVMEKELA 92
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 55-152 6.37e-17

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 71.61  E-value: 6.37e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566320  55 AYVMGKIEGRDTnwHGHVTALSVAPNFRRLGLAAYMMEFLERTSEARRAYFVDLFVRVSNKIAIELYKKLGYVVYRQIIG 134
Cdd:COG0456   1 GFALLGLVDGGD--EAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPN 78

                        90
                ....*....|....*...
gi 17566320 135 YYtgdrDEDAFDMRKSLS 152
Cdd:COG0456  79 YY----GDDALVMEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 25-126 3.04e-15

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: 67.93  E-value: 3.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566320    25 ETYGFQFYLHYMMNYPEYYQVAEHpNGEIMAYVMGKIEGrDTNWHGHVTALSVAPNFRRLGLAAYMMEFLERTSEARRAY 104
Cdd:pfam00583  17 PDEPLDLLEDWDEDASEGFFVAEE-DGELVGFASLSIID-DEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCE 94

                          90       100
                  ....*....|....*....|..
gi 17566320   105 FVDLFVRVSNKIAIELYKKLGY 126
Cdd:pfam00583  95 RIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 38-147 6.77e-14

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: 64.66  E-value: 6.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566320    38 NYPEYYQVAEHpNGEIMAYVMGKIegrdTNWHGHVTALSVAPNFRRLGLAAYMMEFLERTSEARRAYFVDLFVRVSNKIA 117
Cdd:TIGR01575  28 NYHLCYLLARI-GGKVVGYAGVQI----VLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAA 102

                          90       100       110
                  ....*....|....*....|....*....|
gi 17566320   118 IELYKKLGYVVYRQIIGYYTgDRDEDAFDM 147
Cdd:TIGR01575 103 QALYKKLGFNEIAIRRNYYP-DPGEDAIVM 131
PRK03624 PRK03624
putative acetyltransferase; Provisional
 40-126 1.78e-07

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 48.00  E-value: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566320   40 PEYYQVAEHpNGEIMAYVMGKIEGrdtnwH-GHVTALSVAPNFRRLGLAAYMMEFLERTSEARRAYFVDLFVRVSNKIAI 118
Cdd:PRK03624  44 PSLFLVAEV-GGEVVGTVMGGYDG-----HrGWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVL 117


                 ....*...
gi 17566320  119 ELYKKLGY 126
Cdd:PRK03624 118 GFYEALGY 125
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 45-108 1.59e-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: 43.42  E-value: 1.59e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17566320  45 VAEHpNGEIMAYVMGKIEGRDTNwHGHVTALSVAPNFRRLGLAAYMMEFLERTSEARRAYFVDL 108
Cdd:cd04301   3 VAED-DGEIVGFASLSPDGSGGD-TAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 55-152 6.37e-17

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 71.61  E-value: 6.37e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566320  55 AYVMGKIEGRDTnwHGHVTALSVAPNFRRLGLAAYMMEFLERTSEARRAYFVDLFVRVSNKIAIELYKKLGYVVYRQIIG 134
Cdd:COG0456   1 GFALLGLVDGGD--EAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPN 78

                        90
                ....*....|....*...
gi 17566320 135 YYtgdrDEDAFDMRKSLS 152
Cdd:COG0456  79 YY----GDDALVMEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 25-126 3.04e-15

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: 67.93  E-value: 3.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566320    25 ETYGFQFYLHYMMNYPEYYQVAEHpNGEIMAYVMGKIEGrDTNWHGHVTALSVAPNFRRLGLAAYMMEFLERTSEARRAY 104
Cdd:pfam00583  17 PDEPLDLLEDWDEDASEGFFVAEE-DGELVGFASLSIID-DEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCE 94

                          90       100
                  ....*....|....*....|..
gi 17566320   105 FVDLFVRVSNKIAIELYKKLGY 126
Cdd:pfam00583  95 RIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 38-147 6.77e-14

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: 64.66  E-value: 6.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566320    38 NYPEYYQVAEHpNGEIMAYVMGKIegrdTNWHGHVTALSVAPNFRRLGLAAYMMEFLERTSEARRAYFVDLFVRVSNKIA 117
Cdd:TIGR01575  28 NYHLCYLLARI-GGKVVGYAGVQI----VLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAA 102

                          90       100       110
                  ....*....|....*....|....*....|
gi 17566320   118 IELYKKLGYVVYRQIIGYYTgDRDEDAFDM 147
Cdd:TIGR01575 103 QALYKKLGFNEIAIRRNYYP-DPGEDAIVM 131
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
62-132 9.51e-10

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 52.60  E-value: 9.51e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17566320  62 EGRDTNWHGHVTALSVAPNFRRLGLAAYMMEFLERTSEARRAYFVDLFVRVSNKIAIELYKKLGYVVYRQI 132
Cdd:COG3393   8 VRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEY 78
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
45-151 2.83e-09

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 53.07  E-value: 2.83e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566320  45 VAEHpNGEIMAYV-MGKIEGRDTNWHGHVTALSVAPNFRRLGLAAYMMEFLERTSEARRAYFVDLFVRVSNKIAIELYKK 123
Cdd:COG1247  56 VAEE-DGEVVGFAsLGPFRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEK 134

                        90       100
                ....*....|....*....|....*....
gi 17566320 124 LGY-VVYRQIIGYYTGDRDEDAFDMRKSL 151
Cdd:COG1247 135 LGFeEVGTLPEVGFKFGRWLDLVLMQKRL 163
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 45-128 3.59e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 51.30  E-value: 3.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566320    45 VAEHpNGEIMAYVMGKIEGRDTNWHGHvtALSVAPNFRRLGLAAYMMEFLErtsEARRAYFVDLFVRVSNKIAIELYKKL 124
Cdd:pfam13508   7 VAED-DGKIVGFAALLPLDDEGALAEL--RLAVHPEYRGQGIGRALLEAAE---AAAKEGGIKLLELETTNRAAAFYEKL 80


                  ....
gi 17566320   125 GYVV 128
Cdd:pfam13508  81 GFEE 84
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
45-151 1.39e-08

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 50.85  E-value: 1.39e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566320  45 VAEHpNGEIMAYVMG-KIEGRDTNWHGHVTALSVAPNFRRLGLAAYMMEFLERTSEARRAYFVDLfvrVSNKIAIELYKK 123
Cdd:COG3153  43 VAED-DGEIVGHVALsPVDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVL---LGDPSLLPFYER 118

                        90       100
                ....*....|....*....|....*...
gi 17566320 124 LGYVVyrqiIGYYTGDRDEDAFDMRKSL 151
Cdd:COG3153 119 FGFRP----AGELGLTLGPDEVFLAKEL 142
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 43-152 2.52e-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: 49.99  E-value: 2.52e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566320  43 YQVAEHpNGEIMAYVMGKIEGRDTnwhGHVTALSVAPNFRRLGLAAYMMEFLERtsEARRAYFVDLFVrVSNKIAIELYK 122
Cdd:COG1246  30 FWVAEE-DGEIVGCAALHPLDEDL---AELRSLAVHPDYRGRGIGRRLLEALLA--EARELGLKRLFL-LTTSAAIHFYE 102

                        90       100       110
                ....*....|....*....|....*....|
gi 17566320 123 KLGYVVYRQIIGYYTGDRDEDAFDMRKSLS 152
Cdd:COG1246 103 KLGFEEIDKEDLPYAKVWQRDSVVMEKDLE 132
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 39-154 4.91e-08

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 49.28  E-value: 4.91e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566320  39 YPEYYQVAEHPNGEIMAYVMGKIEGRDtnwHGHVTALSVAPNFRRLGLAAYMMEFLERTSEARRAYFVDLFVRVSNKIAI 118
Cdd:COG0454  31 LAGAEFIAVDDKGEPIGFAGLRRLDDK---VLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAI 107

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 17566320 119 ELYKKLGYVVYRQIIGYytgdrdeDAFDMRKSLSRD 154
Cdd:COG0454 108 RFYERLGFKEIERYVAY-------VGGEFEKELSLS 136
PRK03624 PRK03624
putative acetyltransferase; Provisional
 40-126 1.78e-07

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 48.00  E-value: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566320   40 PEYYQVAEHpNGEIMAYVMGKIEGrdtnwH-GHVTALSVAPNFRRLGLAAYMMEFLERTSEARRAYFVDLFVRVSNKIAI 118
Cdd:PRK03624  44 PSLFLVAEV-GGEVVGTVMGGYDG-----HrGWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVL 117


                 ....*...
gi 17566320  119 ELYKKLGY 126
Cdd:PRK03624 118 GFYEALGY 125
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 45-108 1.59e-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: 43.42  E-value: 1.59e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17566320  45 VAEHpNGEIMAYVMGKIEGRDTNwHGHVTALSVAPNFRRLGLAAYMMEFLERTSEARRAYFVDL 108
Cdd:cd04301   3 VAED-DGEIVGFASLSPDGSGGD-TAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
50-152 3.41e-06

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 44.40  E-value: 3.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566320  50 NGEIMAYVMGKIEGRDTnwhGHVTALSVAPNFRRLGLAAYMMEFLERTSEARRAYFVDLFVRVSnkiAIELYKKLGYVVy 129
Cdd:COG2153  42 DGELVATARLLPPGDGE---AKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH---AVGFYEKLGFVP- 114

                        90       100
                ....*....|....*....|....*..
gi 17566320 130 rqiigyyTGDRDEDA----FDMRKSLS 152
Cdd:COG2153 115 -------VGEEFLEAgiphIDMRKPLS 134
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 70-131 4.64e-05

FR47-like protein; The members of this family are similar to the C-terminal region of the D. melanogaster hypothetical protein FR47. This protein has been found to consist of two N-acyltransferase-like domains swapped with the C-terminal strands.


Pssm-ID: 117022 [Multi-domain]  Cd Length: 86  Bit Score: 40.01  E-value: 4.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17566320    70 GHVTALSVAPNFRRLGLAAYMMEFLERTSeARRAYFVDLFVRVSNKIAIELYKKLGYVVYRQ 131
Cdd:pfam08445  22 GELGALQTLPEHRRRGLGSRLVAALARGI-AERGITPFAVVVAGNTPSRRLYEKLGFRKIDE 82
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 55-128 6.62e-05

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: 40.72  E-value: 6.62e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17566320    55 AYVMGKIEG----RDTNwhgHVTALSVAPNFRRLGLAAYMMEFLERTSEARRAYFVDLFVRVSNKiAIELYKKLGYVV 128
Cdd:pfam13673  36 AFEGGQIVGvialRDRG---HISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNASPY-AVPFYEKLGFRA 109
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 75-147 1.24e-04

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 40.30  E-value: 1.24e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17566320   75 LSVAPNFRRLGLAAYMMEFLERTSEARRAYFVDLFVRVSNKIAIELYKKLGY--VVYRQiiGYY-TGDRDEDAFDM 147
Cdd:PRK09491  69 IAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFneVTIRR--NYYpTADGREDAIIM 142
 
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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