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Conserved domains on  [gi|530391402|ref|XP_005252184|]
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N-alpha-acetyltransferase 35, NatC auxiliary subunit isoform X1 [Homo sapiens]

Protein Classification

N-alpha-acetyltransferase 35, NatC auxiliary subunit( domain architecture ID 10513778)

N-alpha-acetyltransferase 35, NatC auxiliary subunit is a component of the N-terminal acetyltransferase C (NatC) complex which catalyzes the acetylation of N-terminal methionine residues

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Mak10 pfam04112
Mak10 subunit, NatC N(alpha)-terminal acetyltransferase; NatC N(alpha)-terminal ...
46-181 1.33e-42

Mak10 subunit, NatC N(alpha)-terminal acetyltransferase; NatC N(alpha)-terminal acetyltransferases contains Mak10p, Mak31p and Mak3p subunits. All three subunits are associated with each other to form the active complex.


:

Pssm-ID: 461179  Cd Length: 162  Bit Score: 151.55  E-value: 1.33e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530391402   46 GELLHDKLFGLFEAMSAIEMMDPKMDAGMIGNQVNRKVLNFEqaikdgtiKIKDLTLPELIGIMDTCFCCLITWLEGHSL 125
Cdd:pfam04112   2 GELVKDPGFTLFEATSALEIMDPKMDSGLIAPELEEEELDFD--------PSRPLLPEEVLGIMDRLLRSEMAWHNGSPL 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530391402  126 AQTVFTCLYIHN-----PDFI------------EDPAM----KAFALGILKICDIAREKVNKAAVFEEEDFQSMTYG 181
Cdd:pfam04112  74 SQTVLTCLYVEHlllpsPKSLkeasfdsdklstGLELVdkvlRAYVLGLLKFCDFVLRELSSGVLYEEEDFVTNTYG 150
 
Name Accession Description Interval E-value
Mak10 pfam04112
Mak10 subunit, NatC N(alpha)-terminal acetyltransferase; NatC N(alpha)-terminal ...
46-181 1.33e-42

Mak10 subunit, NatC N(alpha)-terminal acetyltransferase; NatC N(alpha)-terminal acetyltransferases contains Mak10p, Mak31p and Mak3p subunits. All three subunits are associated with each other to form the active complex.


Pssm-ID: 461179  Cd Length: 162  Bit Score: 151.55  E-value: 1.33e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530391402   46 GELLHDKLFGLFEAMSAIEMMDPKMDAGMIGNQVNRKVLNFEqaikdgtiKIKDLTLPELIGIMDTCFCCLITWLEGHSL 125
Cdd:pfam04112   2 GELVKDPGFTLFEATSALEIMDPKMDSGLIAPELEEEELDFD--------PSRPLLPEEVLGIMDRLLRSEMAWHNGSPL 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530391402  126 AQTVFTCLYIHN-----PDFI------------EDPAM----KAFALGILKICDIAREKVNKAAVFEEEDFQSMTYG 181
Cdd:pfam04112  74 SQTVLTCLYVEHlllpsPKSLkeasfdsdklstGLELVdkvlRAYVLGLLKFCDFVLRELSSGVLYEEEDFVTNTYG 150
 
Name Accession Description Interval E-value
Mak10 pfam04112
Mak10 subunit, NatC N(alpha)-terminal acetyltransferase; NatC N(alpha)-terminal ...
46-181 1.33e-42

Mak10 subunit, NatC N(alpha)-terminal acetyltransferase; NatC N(alpha)-terminal acetyltransferases contains Mak10p, Mak31p and Mak3p subunits. All three subunits are associated with each other to form the active complex.


Pssm-ID: 461179  Cd Length: 162  Bit Score: 151.55  E-value: 1.33e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530391402   46 GELLHDKLFGLFEAMSAIEMMDPKMDAGMIGNQVNRKVLNFEqaikdgtiKIKDLTLPELIGIMDTCFCCLITWLEGHSL 125
Cdd:pfam04112   2 GELVKDPGFTLFEATSALEIMDPKMDSGLIAPELEEEELDFD--------PSRPLLPEEVLGIMDRLLRSEMAWHNGSPL 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530391402  126 AQTVFTCLYIHN-----PDFI------------EDPAM----KAFALGILKICDIAREKVNKAAVFEEEDFQSMTYG 181
Cdd:pfam04112  74 SQTVLTCLYVEHlllpsPKSLkeasfdsdklstGLELVdkvlRAYVLGLLKFCDFVLRELSSGVLYEEEDFVTNTYG 150
 
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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