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Conserved domains on  [gi|489855740|ref|WP_003759402|]
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GNAT family N-acetyltransferase [Neisseria sicca]

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, ...
8-177 4.75e-38

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: 128.96  E-value: 4.75e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489855740   8 PVLSFDRVRLEPLTAAHEAGLREAVCDGEIWKLNVTTAPEPDQVADYIRTATQ-----TRLAFAVIDEDTGKIVGSTSLY 82
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLAdwadgGALPFAIEDKEDGELIGVVGLY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489855740  83 HIDPAIPRLYIGFtWYALSARRTRINTACKIMLLDYVFDTLNCRCACWQTDNLNTASQRAIERLGAHQDGILRCHkLRKD 162
Cdd:COG1670   81 DIDRANRSAEIGY-WLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDA-LVID 158
                        170
                 ....*....|....*
gi 489855740 163 GSVRDTVEYSLLREE 177
Cdd:COG1670  159 GRYRDHVLYSLLREE 173
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
8-177 4.75e-38

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: 128.96  E-value: 4.75e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489855740   8 PVLSFDRVRLEPLTAAHEAGLREAVCDGEIWKLNVTTAPEPDQVADYIRTATQ-----TRLAFAVIDEDTGKIVGSTSLY 82
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLAdwadgGALPFAIEDKEDGELIGVVGLY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489855740  83 HIDPAIPRLYIGFtWYALSARRTRINTACKIMLLDYVFDTLNCRCACWQTDNLNTASQRAIERLGAHQDGILRCHkLRKD 162
Cdd:COG1670   81 DIDRANRSAEIGY-WLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDA-LVID 158
                        170
                 ....*....|....*
gi 489855740 163 GSVRDTVEYSLLREE 177
Cdd:COG1670  159 GRYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
14-149 6.50e-20

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 81.24  E-value: 6.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489855740   14 RVRLEPLTAAHEAGLREAVCDGEIWKLNVTTAPEPDQVADYIRTA-----TQTRLAFAVIDEDTGkIVGSTSLYHIDPAI 88
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEEAREWLARIwaadeAERGYGWAIELKDTG-FIGSIGLYDIDGEP 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489855740   89 PRLYIGFTWYAlSARRTRINTACKIMLLDYVFDTLNCRCACWQTDNLNTASQRAIERLGAH 149
Cdd:pfam13302  80 ERAELGYWLGP-DYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
8-177 4.75e-38

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: 128.96  E-value: 4.75e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489855740   8 PVLSFDRVRLEPLTAAHEAGLREAVCDGEIWKLNVTTAPEPDQVADYIRTATQ-----TRLAFAVIDEDTGKIVGSTSLY 82
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLAdwadgGALPFAIEDKEDGELIGVVGLY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489855740  83 HIDPAIPRLYIGFtWYALSARRTRINTACKIMLLDYVFDTLNCRCACWQTDNLNTASQRAIERLGAHQDGILRCHkLRKD 162
Cdd:COG1670   81 DIDRANRSAEIGY-WLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDA-LVID 158
                        170
                 ....*....|....*
gi 489855740 163 GSVRDTVEYSLLREE 177
Cdd:COG1670  159 GRYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
14-149 6.50e-20

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 81.24  E-value: 6.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489855740   14 RVRLEPLTAAHEAGLREAVCDGEIWKLNVTTAPEPDQVADYIRTA-----TQTRLAFAVIDEDTGkIVGSTSLYHIDPAI 88
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEEAREWLARIwaadeAERGYGWAIELKDTG-FIGSIGLYDIDGEP 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489855740   89 PRLYIGFTWYAlSARRTRINTACKIMLLDYVFDTLNCRCACWQTDNLNTASQRAIERLGAH 149
Cdd:pfam13302  80 ERAELGYWLGP-DYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
15-174 2.91e-05

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 42.67  E-value: 2.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489855740  15 VRLEPLTAAHEAGLREAVCDGeIWKLNVT---TAPEPDQVADYIRTATQTRLAFAVIDEDtGKIVGSTSLYHIDPAIPRL 91
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEA-IAEGTATfetEPPSEEEREAWFAAILAPGRPVLVAEED-GEVVGFASLGPFRPRPAYR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489855740  92 YIGFTWYALS--ARRTRINTAckimLLDYVFD---TLNCRCACWQTDNLNTASQRAIERLGAHQDGILRCHkLRKDGSVR 166
Cdd:COG1247   80 GTAEESIYVDpdARGRGIGRA----LLEALIErarARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEV-GFKFGRWL 154

                 ....*...
gi 489855740 167 DTVEYSLL 174
Cdd:COG1247  155 DLVLMQKR 162
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
44-147 5.85e-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: 5.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489855740   44 TAPEPDQVADYIRTATQTRLAFAVIDEDTGKIVGSTSLYHIDPAIPRLYIGFTWYALSARRTRINTACKIMLLDYVFDtL 123
Cdd:pfam00583  13 PEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARE-R 91
                          90       100
                  ....*....|....*....|....
gi 489855740  124 NCRCACWQTDNLNTASQRAIERLG 147
Cdd:pfam00583  92 GCERIFLEVAADNLAAIALYEKLG 115
 
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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