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Conserved domains on  [gi|190341107|ref|NP_001011713|]
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N-alpha-acetyltransferase 30 [Homo sapiens]

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
PubMed:  15581578|10940244|9175471|27367672|26818562
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 ...
 224-338 3.21e-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: 87.57  E-value: 3.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190341107  224 MPDIMRLITKDLSEPYSIYTYRYFIHNWPQ---LCFLAMVGEECVGAIVCKLDMHKkmFRRGYIAMLAVDSKYRRNGIGT 300
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDaseGFFVAEEDGELVGFASLSIIDDE--PPVGEIEGLAVAPEYRGKGIGT 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 190341107  301 NLVKKAIYAMVEGDCDEVVLETEITNKSALKLYENLGF 338
Cdd:pfam00583  79 ALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 224-338 3.21e-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: 87.57  E-value: 3.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190341107  224 MPDIMRLITKDLSEPYSIYTYRYFIHNWPQ---LCFLAMVGEECVGAIVCKLDMHKkmFRRGYIAMLAVDSKYRRNGIGT 300
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDaseGFFVAEEDGELVGFASLSIIDDE--PPVGEIEGLAVAPEYRGKGIGT 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 190341107  301 NLVKKAIYAMVEGDCDEVVLETEITNKSALKLYENLGF 338
Cdd:pfam00583  79 ALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 280-359 4.09e-17

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 75.46  E-value: 4.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190341107 280 RRGYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLETEITNKSALKLYENLGFVRDKRLFRYYLNGVDALRLKL 359
Cdd:COG0456   12 DEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDALVMEKEL 91
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 225-355 5.23e-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: 5.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190341107  225 PDIMRLITKDLSEPYSIYTYRYFIHNwPQLCFL-AMVGEECVGAIVCKLDMHKkmfrrGYIAMLAVDSKYRRNGIGTNLV 303
Cdd:TIGR01575   3 KAVLEIEAAAFAFPWTEAQFAEELAN-YHLCYLlARIGGKVVGYAGVQIVLDE-----AHILNIAVKPEYQGQGIGRALL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 190341107  304 KKAIYAMVEGDCDEVVLETEITNKSALKLYENLGFVRDKRLFRYYLNGV-DAL 355
Cdd:TIGR01575  77 RELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGeDAI 129
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 255-321 3.93e-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: 52.28  E-value: 3.93e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 190341107 255 CFLAMVGEECVGAIVCKLDMHKKmfRRGYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLE 321
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGG--DTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PRK03624 PRK03624
putative acetyltransferase; Provisional
 252-344 1.70e-06

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 46.85  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190341107 252 PQLCFLAMVGEECVGAIVCKLDMHkkmfrRGYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLETEITNKSALK 331
Cdd:PRK03624  44 PSLFLVAEVGGEVVGTVMGGYDGH-----RGWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLG 118

                         90
                 ....*....|...
gi 190341107 332 LYENLGFVRDKRL 344
Cdd:PRK03624 119 FYEALGYEEQDRI 131
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 224-338 3.21e-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: 87.57  E-value: 3.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190341107  224 MPDIMRLITKDLSEPYSIYTYRYFIHNWPQ---LCFLAMVGEECVGAIVCKLDMHKkmFRRGYIAMLAVDSKYRRNGIGT 300
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDaseGFFVAEEDGELVGFASLSIIDDE--PPVGEIEGLAVAPEYRGKGIGT 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 190341107  301 NLVKKAIYAMVEGDCDEVVLETEITNKSALKLYENLGF 338
Cdd:pfam00583  79 ALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 280-359 4.09e-17

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 75.46  E-value: 4.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190341107 280 RRGYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLETEITNKSALKLYENLGFVRDKRLFRYYLNGVDALRLKL 359
Cdd:COG0456   12 DEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDALVMEKEL 91
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
216-359 6.12e-13

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 65.49  E-value: 6.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190341107 216 VRYESELQMPDIMRLITKDLSEPYSIYT-YRYFIHNWPQLCFLAMVGEECVGAIVCKLDMHKKMFRRGYIAMLAVDSKYR 294
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPGREAELvDRLREDPAAGLSLVAEDDGEIVGHVALSPVDIDGEGPALLLGPLAVDPEYR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190341107 295 RNGIGTNLVKKAIYAMVEGDCDEVVLEteiTNKSALKLYENLGFVRDKRLFRYYLNGVDALRLKL 359
Cdd:COG3153   81 GQGIGRALMRAALEAARERGARAVVLL---GDPSLLPFYERFGFRPAGELGLTLGPDEVFLAKEL 142
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 255-340 4.07e-12

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 61.32  E-value: 4.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190341107  255 CFLAMVGEECVGAIVCKLDMHKKMFrrgYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLETEITnksALKLYE 334
Cdd:pfam13508   5 FFVAEDDGKIVGFAALLPLDDEGAL---AELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNR---AAAFYE 78


                  ....*.
gi 190341107  335 NLGFVR 340
Cdd:pfam13508  79 KLGFEE 84
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 225-355 5.23e-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: 5.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190341107  225 PDIMRLITKDLSEPYSIYTYRYFIHNwPQLCFL-AMVGEECVGAIVCKLDMHKkmfrrGYIAMLAVDSKYRRNGIGTNLV 303
Cdd:TIGR01575   3 KAVLEIEAAAFAFPWTEAQFAEELAN-YHLCYLlARIGGKVVGYAGVQIVLDE-----AHILNIAVKPEYQGQGIGRALL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 190341107  304 KKAIYAMVEGDCDEVVLETEITNKSALKLYENLGFVRDKRLFRYYLNGV-DAL 355
Cdd:TIGR01575  77 RELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGeDAI 129
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 254-359 4.98e-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: 56.90  E-value: 4.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190341107  254 LCFLAMVGEECVGAIvckldmhkKMFRRGYIAMLAVDSKYRRNGIGTNLVKKaiyamVEGDCDEVVLET-EIT---NKSA 329
Cdd:pfam13673  32 FFFVAFEGGQIVGVI--------ALRDRGHISLLFVDPDYQGQGIGKALLEA-----VEDYAEKDGIKLsELTvnaSPYA 98

                          90       100       110
                  ....*....|....*....|....*....|
gi 190341107  330 LKLYENLGFVRDKRLFryYLNGVDALRLKL 359
Cdd:pfam13673  99 VPFYEKLGFRATGPEQ--EFNGIRFVPMEK 126
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 254-351 5.79e-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: 5.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190341107 254 LCFLAMVGEECVG-AIVCKLDmHKkmfrRGYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLETEITNKSALKL 332
Cdd:COG0454   35 EFIAVDDKGEPIGfAGLRRLD-DK----VLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRF 109

                         90
                 ....*....|....*....
gi 190341107 333 YENLGFVRDKRLFRYYLNG 351
Cdd:COG0454  110 YERLGFKEIERYVAYVGGE 128
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 255-321 3.93e-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: 52.28  E-value: 3.93e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 190341107 255 CFLAMVGEECVGAIVCKLDMHKKmfRRGYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLE 321
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGG--DTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
268-349 1.20e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 51.83  E-value: 1.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190341107 268 IVCKLDMHKKMFRRGYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLETEITNKSALKLYENLGFVRDKRLFRY 347
Cdd:COG3393    2 LVAMAGVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEYATV 81


                 ..
gi 190341107 348 YL 349
Cdd:COG3393   82 LF 83
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 224-340 3.58e-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: 3.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190341107 224 MPDIMRLITkdlsepysiytyRYFIHNWPQLCFLAMVGEECVGaiVCKLDMHKKmfRRGYIAMLAVDSKYRRNGIGTNLV 303
Cdd:COG1246   11 VPAILELIR------------PYALEEEIGEFWVAEEDGEIVG--CAALHPLDE--DLAELRSLAVHPDYRGRGIGRRLL 74

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 190341107 304 KKAIYAMVEGDCDEVVLEteiTNKSALKLYENLGFVR 340
Cdd:COG1246   75 EALLAEARELGLKRLFLL---TTSAAIHFYEKLGFEE 108
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 225-349 1.73e-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: 1.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190341107 225 PDIMRLITkdlSEPYSIYTYRYFIHNW------PQLCFLAMV---GEECVGaiVCKLDMHKKMFRRGYIAMlAVDSKYRR 295
Cdd:COG1670   28 PEVARYLP---GPPYSLEEARAWLERLladwadGGALPFAIEdkeDGELIG--VVGLYDIDRANRSAEIGY-WLAPAYWG 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 190341107 296 NGIGTNLVKKAI-YAMVEGDCDEVVLETEITNKSALKLYENLGFVRDKRLFRYYL 349
Cdd:COG1670  102 KGYATEALRALLdYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALV 156
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
255-360 3.69e-07

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 49.22  E-value: 3.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190341107 255 CFLAMVGEECVGAIVCKLDMHKKMFRRGYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLETEITNKSALKLYE 334
Cdd:COG1247   54 VLVAEEDGEVVGFASLGPFRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYE 133

                         90       100
                 ....*....|....*....|....*.
gi 190341107 335 NLGFVRDKRLFRYYLNGVDALRLKLW 360
Cdd:COG1247  134 KLGFEEVGTLPEVGFKFGRWLDLVLM 159
PRK03624 PRK03624
putative acetyltransferase; Provisional
 252-344 1.70e-06

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 46.85  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190341107 252 PQLCFLAMVGEECVGAIVCKLDMHkkmfrRGYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLETEITNKSALK 331
Cdd:PRK03624  44 PSLFLVAEVGGEVVGTVMGGYDGH-----RGWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLG 118

                         90
                 ....*....|...
gi 190341107 332 LYENLGFVRDKRL 344
Cdd:PRK03624 119 FYEALGYEEQDRI 131
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 287-338 5.45e-04

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 39.91  E-value: 5.45e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 190341107 287 LAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLETEITNKSALKLYENLGF 338
Cdd:PRK09491  69 IAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF 120
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
282-340 8.15e-04

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 39.01  E-value: 8.15e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 190341107 282 GYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLETEITnksALKLYENLGFVR 340
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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