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Conserved domains on  [gi|19112093|ref|NP_595301|]
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GCN5-related N-acetyltransferase [Schizosaccharomyces pombe]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11447457)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

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 ...
129-196 7.77e-08

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: 49.05  E-value: 7.77e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112093   129 EVHIVGELELMIAEPQNRRKGYGTKIVDAFLHYvessgiAKNKQILKYRVKVGSQNKPSIRLFKKLGF 196
Cdd:pfam00583  55 DEPPVGEIEGLAVAPEYRGKGIGTALLQALLEW------ARERGCERIFLEVAADNLAAIALYEKLGF 116
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
14-215 3.27e-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: 48.46  E-value: 3.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112093  14 LILVPYQKCHVLKYHNWMKNEELQELTCSEPLTLDEEYQMQASWSTD---EDKLTFIVLLNENDEakkpsildhvkahsv 90
Cdd:COG1670   8 LRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLADwadGGALPFAIEDKEDGE--------------- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112093  91 esMIGDVNMFlteeyadGIEEFDDSpsdanatnatkesevhivGELELMIAePQNRRKGYGTKIVDAFLHYvessgiAKN 170
Cdd:COG1670  73 --LIGVVGLY-------DIDRANRS------------------AEIGYWLA-PAYWGKGYATEALRALLDY------AFE 118
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19112093 171 KQILKyRV--KVGSQNKPSIRLFKKLGFSQVKY--------NAYFDHVELELMRT 215
Cdd:COG1670 119 ELGLH-RVeaEVDPDNTASIRVLEKLGFRLEGTlrdalvidGRYRDHVLYSLLRE 172
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
129-196 7.77e-08

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: 49.05  E-value: 7.77e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112093   129 EVHIVGELELMIAEPQNRRKGYGTKIVDAFLHYvessgiAKNKQILKYRVKVGSQNKPSIRLFKKLGF 196
Cdd:pfam00583  55 DEPPVGEIEGLAVAPEYRGKGIGTALLQALLEW------ARERGCERIFLEVAADNLAAIALYEKLGF 116
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
14-215 3.27e-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: 48.46  E-value: 3.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112093  14 LILVPYQKCHVLKYHNWMKNEELQELTCSEPLTLDEEYQMQASWSTD---EDKLTFIVLLNENDEakkpsildhvkahsv 90
Cdd:COG1670   8 LRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLADwadGGALPFAIEDKEDGE--------------- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112093  91 esMIGDVNMFlteeyadGIEEFDDSpsdanatnatkesevhivGELELMIAePQNRRKGYGTKIVDAFLHYvessgiAKN 170
Cdd:COG1670  73 --LIGVVGLY-------DIDRANRS------------------AEIGYWLA-PAYWGKGYATEALRALLDY------AFE 118
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19112093 171 KQILKyRV--KVGSQNKPSIRLFKKLGFSQVKY--------NAYFDHVELELMRT 215
Cdd:COG1670 119 ELGLH-RVeaEVDPDNTASIRVLEKLGFRLEGTlrdalvidGRYRDHVLYSLLRE 172
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
133-214 5.11e-07

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 46.19  E-value: 5.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112093 133 VGELELMIAEPQNRRKGYGTKIVDAFLHYvessgiAKNKQILKYRVKVGSQNKPSIRLFKKLGFSQVKYNAYFDHVELEL 212
Cdd:COG0456  13 EAEIEDLAVDPEYRGRGIGRALLEAALER------ARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDALV 86

                ..
gi 19112093 213 MR 214
Cdd:COG0456  87 ME 88
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
60-201 9.72e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 36.95  E-value: 9.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112093     60 DEDKLTFIVLLNE-----NDEAKKPSILDHVKAHSVESMIG-------DVNMFLTEEYADGIEEFDD-SPSDANATNATK 126
Cdd:TIGR01612 1784 DEIKNTRINAQNEflkiiEIEKKSKSYLDDIEAKEFDRIINhfkkkldHVNDKFTKEYSKINEGFDDiSKSIENVKNSTD 1863
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112093    127 ESevhivgeleLMIAEPQNRRKGYGTKIVDAFLHY-VESSGIAKNKQILKYRVKVGSQNKPSIRLFKKLGFSQVKY 201
Cdd:TIGR01612 1864 EN---------LLFDILNKTKDAYAGIIGKKYYSYkDEAEKIFINISKLANSINIQIQNNSGIDLFDNINIAILSS 1930
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
129-196 7.77e-08

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: 49.05  E-value: 7.77e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112093   129 EVHIVGELELMIAEPQNRRKGYGTKIVDAFLHYvessgiAKNKQILKYRVKVGSQNKPSIRLFKKLGF 196
Cdd:pfam00583  55 DEPPVGEIEGLAVAPEYRGKGIGTALLQALLEW------ARERGCERIFLEVAADNLAAIALYEKLGF 116
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
14-196 1.61e-07

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 48.88  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112093    14 LILVPYQKCHVLKYHNWMKNEELQELTCSEPLTLDEEYQ-MQASWSTDEDKLTFIVLLNENDEAkkpsildhvkahsves 92
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEEAREwLARIWAADEAERGYGWAIELKDTG---------------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112093    93 MIGDVnmflteeyadGIEEFDDSPSDAnatnatkesevhivgELELMIAePQNRRKGYGTKIVDAFLHYVessgiAKNKQ 172
Cdd:pfam13302  66 FIGSI----------GLYDIDGEPERA---------------ELGYWLG-PDYWGKGYATEAVRALLEYA-----FEELG 114
                         170       180
                  ....*....|....*....|....
gi 19112093   173 ILKYRVKVGSQNKPSIRLFKKLGF 196
Cdd:pfam13302 115 LPRLVARIDPENTASRRVLEKLGF 138
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
14-215 3.27e-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: 48.46  E-value: 3.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112093  14 LILVPYQKCHVLKYHNWMKNEELQELTCSEPLTLDEEYQMQASWSTD---EDKLTFIVLLNENDEakkpsildhvkahsv 90
Cdd:COG1670   8 LRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLADwadGGALPFAIEDKEDGE--------------- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112093  91 esMIGDVNMFlteeyadGIEEFDDSpsdanatnatkesevhivGELELMIAePQNRRKGYGTKIVDAFLHYvessgiAKN 170
Cdd:COG1670  73 --LIGVVGLY-------DIDRANRS------------------AEIGYWLA-PAYWGKGYATEALRALLDY------AFE 118
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19112093 171 KQILKyRV--KVGSQNKPSIRLFKKLGFSQVKY--------NAYFDHVELELMRT 215
Cdd:COG1670 119 ELGLH-RVeaEVDPDNTASIRVLEKLGFRLEGTlrdalvidGRYRDHVLYSLLRE 172
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
133-214 5.11e-07

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 46.19  E-value: 5.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112093 133 VGELELMIAEPQNRRKGYGTKIVDAFLHYvessgiAKNKQILKYRVKVGSQNKPSIRLFKKLGFSQVKYNAYFDHVELEL 212
Cdd:COG0456  13 EAEIEDLAVDPEYRGRGIGRALLEAALER------ARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDALV 86

                ..
gi 19112093 213 MR 214
Cdd:COG0456  87 ME 88
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
133-212 1.47e-06

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 46.53  E-value: 1.47e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112093 133 VGELELMIAePQNRRKGYGTKIVDAFLHYVESSGIaknKQIlkyRVKVGSQNKPSIRLFKKLGFSQV--------KYNAY 204
Cdd:COG1247  81 TAEESIYVD-PDARGRGIGRALLEALIERARARGY---RRL---VAVVLADNEASIALYEKLGFEEVgtlpevgfKFGRW 153

                ....*...
gi 19112093 205 FDHVELEL 212
Cdd:COG1247 154 LDLVLMQK 161
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
133-215 2.00e-06

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 45.81  E-value: 2.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112093 133 VGELELMIAEPQNRRKGYGTKIVDAFLHYVESSGIAknkqilKYRVKVGSQNKPSIRLFKKLGFSQVkyNAYFDHVELEL 212
Cdd:COG0454  58 VLELKRLYVLPEYRGKGIGKALLEALLEWARERGCT------ALELDTLDGNPAAIRFYERLGFKEI--ERYVAYVGGEF 129

                ...
gi 19112093 213 MRT 215
Cdd:COG0454 130 EKE 132
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
133-196 2.00e-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: 41.55  E-value: 2.00e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112093   133 VGELELMIAEPQNRRKGYGTKIVDAFLHyvessGIAKNKQILKyrVKVGSQNKPSIRLFKKLGF 196
Cdd:pfam08445  21 GGELGALQTLPEHRRRGLGSRLVAALAR-----GIAERGITPF--AVVVAGNTPSRRLYEKLGF 77
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
133-200 2.13e-05

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: 42.67  E-value: 2.13e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112093 133 VGELELMIAEPQNRRKGYGTKIVDAFLHYVESSGIAknkqilkyRVKVGSqNKPSIRLFKKLGFSQVK 200
Cdd:COG1246  52 LAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLK--------RLFLLT-TSAAIHFYEKLGFEEID 110
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
124-196 1.29e-03

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 36.66  E-value: 1.29e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112093   124 ATKESEVHIVGELELMIAePQNRRKGYGTKIVDAFLHyvessgIAKNKQILKYRVKVgsqNKPSIRLFKKLGF 196
Cdd:pfam13508  20 LLPLDDEGALAELRLAVH-PEYRGQGIGRALLEAAEA------AAKEGGIKLLELET---TNRAAAFYEKLGF 82
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
133-199 3.53e-03

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 35.27  E-value: 3.53e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19112093 133 VGELELMIAEPQNRRKGYGTKIVDAFLHYVESSGIAknkqILKYRvkVGSQNKPSIRLFKKLGFSQV 199
Cdd:COG3393  15 VAEISGVYTHPEYRGRGLASALVAALAREALARGAR----TPFLY--VDADNPAARRLYERLGFRPV 75
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
60-201 9.72e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 36.95  E-value: 9.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112093     60 DEDKLTFIVLLNE-----NDEAKKPSILDHVKAHSVESMIG-------DVNMFLTEEYADGIEEFDD-SPSDANATNATK 126
Cdd:TIGR01612 1784 DEIKNTRINAQNEflkiiEIEKKSKSYLDDIEAKEFDRIINhfkkkldHVNDKFTKEYSKINEGFDDiSKSIENVKNSTD 1863
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112093    127 ESevhivgeleLMIAEPQNRRKGYGTKIVDAFLHY-VESSGIAKNKQILKYRVKVGSQNKPSIRLFKKLGFSQVKY 201
Cdd:TIGR01612 1864 EN---------LLFDILNKTKDAYAGIIGKKYYSYkDEAEKIFINISKLANSINIQIQNNSGIDLFDNINIAILSS 1930
 
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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