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Conserved domains on  [gi|568988767|ref|XP_006519605|]
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N-alpha-acetyltransferase 30 isoform X1 [Mus musculus]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10456837)

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
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
237-351 5.79e-21

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: 87.19  E-value: 5.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988767  237 MPDIMRLITKDLSEPYSIYTYRYFIHNWPQ---LCFLAMVGEECVGAIVCKLDMHKkmFRRGYIAMLAVDSKYRRNGIGT 313
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDaseGFFVAEEDGELVGFASLSIIDDE--PPVGEIEGLAVAPEYRGKGIGT 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568988767  314 NLVKKAIYAMVEGDCDEVVLETEITNKSALKLYENLGF 351
Cdd:pfam00583  79 ALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
237-351 5.79e-21

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: 87.19  E-value: 5.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988767  237 MPDIMRLITKDLSEPYSIYTYRYFIHNWPQ---LCFLAMVGEECVGAIVCKLDMHKkmFRRGYIAMLAVDSKYRRNGIGT 313
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDaseGFFVAEEDGELVGFASLSIIDDE--PPVGEIEGLAVAPEYRGKGIGT 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568988767  314 NLVKKAIYAMVEGDCDEVVLETEITNKSALKLYENLGF 351
Cdd:pfam00583  79 ALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
293-372 8.20e-17

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 74.69  E-value: 8.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988767 293 RRGYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLETEITNKSALKLYENLGFVRDKRLFRYYLNGVDALRLKL 372
Cdd:COG0456   12 DEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDALVMEKEL 91
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
238-368 5.55e-12

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: 5.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988767  238 PDIMRLITKDLSEPYSIYTYRYFIHNwPQLCFL-AMVGEECVGAIVCKLDMHKkmfrrGYIAMLAVDSKYRRNGIGTNLV 316
Cdd:TIGR01575   3 KAVLEIEAAAFAFPWTEAQFAEELAN-YHLCYLlARIGGKVVGYAGVQIVLDE-----AHILNIAVKPEYQGQGIGRALL 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568988767  317 KKAIYAMVEGDCDEVVLETEITNKSALKLYENLGFVRDKRLFRYYLNGV-DAL 368
Cdd:TIGR01575  77 RELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGeDAI 129
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
268-334 6.67e-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: 51.89  E-value: 6.67e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568988767 268 CFLAMVGEECVGAIVCKLDMHKKmfRRGYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLE 334
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGG--DTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PRK03624 PRK03624
putative acetyltransferase; Provisional
265-357 1.77e-06

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 46.85  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988767 265 PQLCFLAMVGEECVGAIVCKLDMHkkmfrRGYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLETEITNKSALK 344
Cdd:PRK03624  44 PSLFLVAEVGGEVVGTVMGGYDGH-----RGWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLG 118
                         90
                 ....*....|...
gi 568988767 345 LYENLGFVRDKRL 357
Cdd:PRK03624 119 FYEALGYEEQDRI 131
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
237-351 5.79e-21

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: 87.19  E-value: 5.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988767  237 MPDIMRLITKDLSEPYSIYTYRYFIHNWPQ---LCFLAMVGEECVGAIVCKLDMHKkmFRRGYIAMLAVDSKYRRNGIGT 313
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDaseGFFVAEEDGELVGFASLSIIDDE--PPVGEIEGLAVAPEYRGKGIGT 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568988767  314 NLVKKAIYAMVEGDCDEVVLETEITNKSALKLYENLGF 351
Cdd:pfam00583  79 ALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
293-372 8.20e-17

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 74.69  E-value: 8.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988767 293 RRGYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLETEITNKSALKLYENLGFVRDKRLFRYYLNGVDALRLKL 372
Cdd:COG0456   12 DEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDALVMEKEL 91
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
229-372 5.49e-13

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 65.88  E-value: 5.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988767 229 VRYESELQMPDIMRLITKDLSEPYSIYT-YRYFIHNWPQLCFLAMVGEECVGAIVCKLDMHKKMFRRGYIAMLAVDSKYR 307
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPGREAELvDRLREDPAAGLSLVAEDDGEIVGHVALSPVDIDGEGPALLLGPLAVDPEYR 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568988767 308 RNGIGTNLVKKAIYAMVEGDCDEVVLEteiTNKSALKLYENLGFVRDKRLFRYYLNGVDALRLKL 372
Cdd:COG3153   81 GQGIGRALMRAALEAARERGARAVVLL---GDPSLLPFYERFGFRPAGELGLTLGPDEVFLAKEL 142
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
238-368 5.55e-12

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: 5.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988767  238 PDIMRLITKDLSEPYSIYTYRYFIHNwPQLCFL-AMVGEECVGAIVCKLDMHKkmfrrGYIAMLAVDSKYRRNGIGTNLV 316
Cdd:TIGR01575   3 KAVLEIEAAAFAFPWTEAQFAEELAN-YHLCYLlARIGGKVVGYAGVQIVLDE-----AHILNIAVKPEYQGQGIGRALL 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568988767  317 KKAIYAMVEGDCDEVVLETEITNKSALKLYENLGFVRDKRLFRYYLNGV-DAL 368
Cdd:TIGR01575  77 RELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGeDAI 129
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
268-353 8.53e-12

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 60.55  E-value: 8.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988767  268 CFLAMVGEECVGAIVCKLDMHKkmfRRGYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLETEITnksALKLYE 347
Cdd:pfam13508   5 FFVAEDDGKIVGFAALLPLDDE---GALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNR---AAAFYE 78

                  ....*.
gi 568988767  348 NLGFVR 353
Cdd:pfam13508  79 KLGFEE 84
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
267-372 5.88e-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: 56.51  E-value: 5.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988767  267 LCFLAMVGEECVGAIvckldmhkKMFRRGYIAMLAVDSKYRRNGIGTNLVKKaiyamVEGDCDEVVLET-EIT---NKSA 342
Cdd:pfam13673  32 FFFVAFEGGQIVGVI--------ALRDRGHISLLFVDPDYQGQGIGKALLEA-----VEDYAEKDGIKLsELTvnaSPYA 98
                          90       100       110
                  ....*....|....*....|....*....|
gi 568988767  343 LKLYENLGFVRDKRLFryYLNGVDALRLKL 372
Cdd:pfam13673  99 VPFYEKLGFRATGPEQ--EFNGIRFVPMEK 126
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
267-364 6.09e-10

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 56.99  E-value: 6.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988767 267 LCFLAMVGEECVG-AIVCKLDmHKkmfrRGYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLETEITNKSALKL 345
Cdd:COG0454   35 EFIAVDDKGEPIGfAGLRRLD-DK----VLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRF 109
                         90
                 ....*....|....*....
gi 568988767 346 YENLGFVRDKRLFRYYLNG 364
Cdd:COG0454  110 YERLGFKEIERYVAYVGGE 128
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
268-334 6.67e-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: 51.89  E-value: 6.67e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568988767 268 CFLAMVGEECVGAIVCKLDMHKKmfRRGYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLE 334
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGG--DTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
281-362 1.21e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 51.83  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988767 281 IVCKLDMHKKMFRRGYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLETEITNKSALKLYENLGFVRDKRLFRY 360
Cdd:COG3393    2 LVAMAGVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEYATV 81

                 ..
gi 568988767 361 YL 362
Cdd:COG3393   82 LF 83
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
237-353 4.50e-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: 51.53  E-value: 4.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988767 237 MPDIMRLITkdlsepysiytyRYFIHNWPQLCFLAMVGEECVGaiVCKLDMHKKmfRRGYIAMLAVDSKYRRNGIGTNLV 316
Cdd:COG1246   11 VPAILELIR------------PYALEEEIGEFWVAEEDGEIVG--CAALHPLDE--DLAELRSLAVHPDYRGRGIGRRLL 74
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568988767 317 KKAIYAMVEGDCDEVVLEteiTNKSALKLYENLGFVR 353
Cdd:COG1246   75 EALLAEARELGLKRLFLL---TTSAAIHFYEKLGFEE 108
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
238-362 1.92e-07

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: 50.38  E-value: 1.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988767 238 PDIMRLITkdlSEPYSIYTYRYFIHNW------PQLCFLAMV---GEECVGaiVCKLDMHKKMFRRGYIAMlAVDSKYRR 308
Cdd:COG1670   28 PEVARYLP---GPPYSLEEARAWLERLladwadGGALPFAIEdkeDGELIG--VVGLYDIDRANRSAEIGY-WLAPAYWG 101
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568988767 309 NGIGTNLVKKAI-YAMVEGDCDEVVLETEITNKSALKLYENLGFVRDKRLFRYYL 362
Cdd:COG1670  102 KGYATEALRALLdYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALV 156
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
268-373 3.08e-07

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 49.61  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988767 268 CFLAMVGEECVGAIVCKLDMHKKMFRRGYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLETEITNKSALKLYE 347
Cdd:COG1247   54 VLVAEEDGEVVGFASLGPFRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYE 133
                         90       100
                 ....*....|....*....|....*.
gi 568988767 348 NLGFVRDKRLFRYYLNGVDALRLKLW 373
Cdd:COG1247  134 KLGFEEVGTLPEVGFKFGRWLDLVLM 159
PRK03624 PRK03624
putative acetyltransferase; Provisional
265-357 1.77e-06

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 46.85  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988767 265 PQLCFLAMVGEECVGAIVCKLDMHkkmfrRGYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLETEITNKSALK 344
Cdd:PRK03624  44 PSLFLVAEVGGEVVGTVMGGYDGH-----RGWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLG 118
                         90
                 ....*....|...
gi 568988767 345 LYENLGFVRDKRL 357
Cdd:PRK03624 119 FYEALGYEEQDRI 131
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
300-351 5.70e-04

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 39.91  E-value: 5.70e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568988767 300 LAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLETEITNKSALKLYENLGF 351
Cdd:PRK09491  69 IAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF 120
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
295-353 7.96e-04

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 39.01  E-value: 7.96e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568988767 295 GYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLETEITnksALKLYENLGFVR 353
Cdd:COG2153   59 AKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH---AVGFYEKLGFVP 114
 
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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