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Conserved domains on  [gi|6322233|ref|NP_012308|]
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uncharacterized protein YIR042C [Saccharomyces cerevisiae S288C]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11447364)

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
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
27-201 5.54e-40

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: 135.51  E-value: 5.54e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322233   27 VVLKGNTCRLEPLDRErHGSELFSAYSEAgqKLWTYLPAGPFT--NLEEYLEFIKELNETKDTVPFAIINKETERAVGTL 104
Cdd:COG1670   1 PTLETERLRLRPLRPE-DAEALAELLNDP--EVARYLPGPPYSleEARAWLERLLADWADGGALPFAIEDKEDGELIGVV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322233  105 CLIRIDEANGSLEVGYVVfSPELQKTIIATEAQFLLMKYVFDDLQYRRYEWKCDSLNGPSRRAAMRLGFKYEGTFRQVVV 184
Cdd:COG1670  78 GLYDIDRANRSAEIGYWL-APAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALV 156
                       170
                ....*....|....*..
gi 6322233  185 YKGRTRDTQWFSIIDKE 201
Cdd:COG1670 157 IDGRYRDHVLYSLLREE 173
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
27-201 5.54e-40

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: 135.51  E-value: 5.54e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322233   27 VVLKGNTCRLEPLDRErHGSELFSAYSEAgqKLWTYLPAGPFT--NLEEYLEFIKELNETKDTVPFAIINKETERAVGTL 104
Cdd:COG1670   1 PTLETERLRLRPLRPE-DAEALAELLNDP--EVARYLPGPPYSleEARAWLERLLADWADGGALPFAIEDKEDGELIGVV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322233  105 CLIRIDEANGSLEVGYVVfSPELQKTIIATEAQFLLMKYVFDDLQYRRYEWKCDSLNGPSRRAAMRLGFKYEGTFRQVVV 184
Cdd:COG1670  78 GLYDIDRANRSAEIGYWL-APAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALV 156
                       170
                ....*....|....*..
gi 6322233  185 YKGRTRDTQWFSIIDKE 201
Cdd:COG1670 157 IDGRYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
35-174 1.01e-15

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 71.22  E-value: 1.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322233     35 RLEPLDRErhgsELFSAYSEAgqKLWTYLPAGPFT--NLEEYLEFIKELNETKDTVPFAIINKETeRAVGTLCLIRIDEA 112
Cdd:pfam13302   6 PLTEEDAE----ALFELLSDP--EVMRYGVPWPLTleEAREWLARIWAADEAERGYGWAIELKDT-GFIGSIGLYDIDGE 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6322233    113 NGSLEVGYVVFSPELQKTIiATEAQFLLMKYVFDDLQYRRYEWKCDSLNGPSRRAAMRLGFK 174
Cdd:pfam13302  79 PERAELGYWLGPDYWGKGY-ATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
98-199 3.67e-03

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 37.05  E-value: 3.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322233    98 ERAVGTLCLIRIDEANGSLEVGYVVFSPELQKTIIATEAQFLLMKYVfDDLQYRRYEWKCDSLNGPSRRAAMRLGFKYEG 177
Cdd:PRK10151  76 DELIGVLSFNRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYA-QSGELRRFVIKCRVDNPASNQVALRNGFTLEG 154
                         90       100
                 ....*....|....*....|...
gi 6322233   178 TFRQVVVYKGRTRDTQWFS-IID 199
Cdd:PRK10151 155 CLKQAEYLNGAYDDVNLYArIID 177
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
27-201 5.54e-40

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: 135.51  E-value: 5.54e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322233   27 VVLKGNTCRLEPLDRErHGSELFSAYSEAgqKLWTYLPAGPFT--NLEEYLEFIKELNETKDTVPFAIINKETERAVGTL 104
Cdd:COG1670   1 PTLETERLRLRPLRPE-DAEALAELLNDP--EVARYLPGPPYSleEARAWLERLLADWADGGALPFAIEDKEDGELIGVV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322233  105 CLIRIDEANGSLEVGYVVfSPELQKTIIATEAQFLLMKYVFDDLQYRRYEWKCDSLNGPSRRAAMRLGFKYEGTFRQVVV 184
Cdd:COG1670  78 GLYDIDRANRSAEIGYWL-APAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALV 156
                       170
                ....*....|....*..
gi 6322233  185 YKGRTRDTQWFSIIDKE 201
Cdd:COG1670 157 IDGRYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
35-174 1.01e-15

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 71.22  E-value: 1.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322233     35 RLEPLDRErhgsELFSAYSEAgqKLWTYLPAGPFT--NLEEYLEFIKELNETKDTVPFAIINKETeRAVGTLCLIRIDEA 112
Cdd:pfam13302   6 PLTEEDAE----ALFELLSDP--EVMRYGVPWPLTleEAREWLARIWAADEAERGYGWAIELKDT-GFIGSIGLYDIDGE 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6322233    113 NGSLEVGYVVFSPELQKTIiATEAQFLLMKYVFDDLQYRRYEWKCDSLNGPSRRAAMRLGFK 174
Cdd:pfam13302  79 PERAELGYWLGPDYWGKGY-ATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
67-173 8.30e-05

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: 40.96  E-value: 8.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322233     67 PFTNLEEYLEFIKELNETKDTVPFAIINKETERAVGTLCLIRIDEANGSLEVGYVVFSPELQKTIIATEaqflLMKYVFD 146
Cdd:pfam00583  11 EFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTA----LLQALLE 86
                          90       100       110
                  ....*....|....*....|....*....|
gi 6322233    147 ---DLQYRRYEWKCDSLNGPSRRAAMRLGF 173
Cdd:pfam00583  87 warERGCERIFLEVAADNLAAIALYEKLGF 116
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
98-199 3.67e-03

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 37.05  E-value: 3.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322233    98 ERAVGTLCLIRIDEANGSLEVGYVVFSPELQKTIIATEAQFLLMKYVfDDLQYRRYEWKCDSLNGPSRRAAMRLGFKYEG 177
Cdd:PRK10151  76 DELIGVLSFNRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYA-QSGELRRFVIKCRVDNPASNQVALRNGFTLEG 154
                         90       100
                 ....*....|....*....|...
gi 6322233   178 TFRQVVVYKGRTRDTQWFS-IID 199
Cdd:PRK10151 155 CLKQAEYLNGAYDDVNLYArIID 177
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
47-195 6.94e-03

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 36.13  E-value: 6.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322233   47 ELFSAYSEAGQKLWTYLPAGPftnlEEYLEFIKELNETKDTVPFAIINketERAVGTLCLIRIDEANGSLEVGY--VVFS 124
Cdd:COG1247  17 AIYNEAIAEGTATFETEPPSE----EEREAWFAAILAPGRPVLVAEED---GEVVGFASLGPFRPRPAYRGTAEesIYVD 89
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322233  125 PELQKTIIATeaqfLLMKYVFDDLQ---YRRYEWKCDSLNGPSRRAAMRLGFKYEGTFRQVVVYKGRTRDTQWF 195
Cdd:COG1247  90 PDARGRGIGR----ALLEALIERARargYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLM 159
 
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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