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Conserved domains on  [gi|299758426|ref|NP_001177653|]
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alpha-tubulin N-acetyltransferase 1 isoform 3 [Homo sapiens]

Protein Classification

alpha-tubulin N-acetyltransferase( domain architecture ID 10526333)

alpha-tubulin N-acetyltransferase (TAT) acetylates Lys-40 of alpha-tubulin in the microtubule lumen

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Acetyltransf_16 pfam05301
GNAT acetyltransferase, Mec-17; Mec-17 is the protein product of one of the 18 genes required ...
 10-178 1.20e-98

GNAT acetyltransferase, Mec-17; Mec-17 is the protein product of one of the 18 genes required for the development and function of the touch receptor neuron for gentle touch. Mec-17 is specifically required for maintaining the differentiation of the touch receptor. The family shares all the residue-motifs characteriztic of Gcn5-related acetyl-transferases, though the exact unction is still unknown.


:

Pssm-ID: 461616  Cd Length: 176  Bit Score: 286.77  E-value: 1.20e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758426   10 LTITLREEGVCHlESVDLQQQIMTIIDELGKASAKAQNLSAPITSASRMQSNRHVVYILKDSSARpaGKGAIIGFIKVGY 89
Cdd:pfam05301  11 LDNTLLPEGFCR-ERQDLQRKLSEVIDEMGKASAKAQGLKTPITSAEKLQNSDHTLYLLKDGEAN--GKGAVVGLLKVGY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758426   90 KKLFVLDDREAHNEVEPLCILDFYIHESVQRHGHGRELFQYMLQKERVEPHQLAIDRPSQKLLKFLNKHYNLETTVPQVN 169
Cdd:pfam05301  88 KKLFLFDEQGQHHEMEPLCVLDFYVHESRQRHGLGKKLFDYMLKDENVEPYQLAIDRPSPKLLSFLKKHYGLKKTVPQVN 167


                  ....*....
gi 299758426  170 NFVIFEGFF 178
Cdd:pfam05301 168 NFVVFEGFF 176
 
Name Accession Description Interval E-value
Acetyltransf_16 pfam05301
GNAT acetyltransferase, Mec-17; Mec-17 is the protein product of one of the 18 genes required ...
 10-178 1.20e-98

GNAT acetyltransferase, Mec-17; Mec-17 is the protein product of one of the 18 genes required for the development and function of the touch receptor neuron for gentle touch. Mec-17 is specifically required for maintaining the differentiation of the touch receptor. The family shares all the residue-motifs characteriztic of Gcn5-related acetyl-transferases, though the exact unction is still unknown.


Pssm-ID: 461616  Cd Length: 176  Bit Score: 286.77  E-value: 1.20e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758426   10 LTITLREEGVCHlESVDLQQQIMTIIDELGKASAKAQNLSAPITSASRMQSNRHVVYILKDSSARpaGKGAIIGFIKVGY 89
Cdd:pfam05301  11 LDNTLLPEGFCR-ERQDLQRKLSEVIDEMGKASAKAQGLKTPITSAEKLQNSDHTLYLLKDGEAN--GKGAVVGLLKVGY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758426   90 KKLFVLDDREAHNEVEPLCILDFYIHESVQRHGHGRELFQYMLQKERVEPHQLAIDRPSQKLLKFLNKHYNLETTVPQVN 169
Cdd:pfam05301  88 KKLFLFDEQGQHHEMEPLCVLDFYVHESRQRHGLGKKLFDYMLKDENVEPYQLAIDRPSPKLLSFLKKHYGLKKTVPQVN 167


                  ....*....
gi 299758426  170 NFVIFEGFF 178
Cdd:pfam05301 168 NFVVFEGFF 176
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 79-136 2.95e-03

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: 35.33  E-value: 2.95e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 299758426  79 GAIIGFIkvgykklFVLDDREAHNEVEplcILDFYIHESVQRHGHGRELFQYMLQKER 136
Cdd:cd04301    8 GEIVGFA-------SLSPDGSGGDTAY---IGDLAVLPEYRGKGIGSALLEAAEEEAR 55
 
Name Accession Description Interval E-value
Acetyltransf_16 pfam05301
GNAT acetyltransferase, Mec-17; Mec-17 is the protein product of one of the 18 genes required ...
 10-178 1.20e-98

GNAT acetyltransferase, Mec-17; Mec-17 is the protein product of one of the 18 genes required for the development and function of the touch receptor neuron for gentle touch. Mec-17 is specifically required for maintaining the differentiation of the touch receptor. The family shares all the residue-motifs characteriztic of Gcn5-related acetyl-transferases, though the exact unction is still unknown.


Pssm-ID: 461616  Cd Length: 176  Bit Score: 286.77  E-value: 1.20e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758426   10 LTITLREEGVCHlESVDLQQQIMTIIDELGKASAKAQNLSAPITSASRMQSNRHVVYILKDSSARpaGKGAIIGFIKVGY 89
Cdd:pfam05301  11 LDNTLLPEGFCR-ERQDLQRKLSEVIDEMGKASAKAQGLKTPITSAEKLQNSDHTLYLLKDGEAN--GKGAVVGLLKVGY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758426   90 KKLFVLDDREAHNEVEPLCILDFYIHESVQRHGHGRELFQYMLQKERVEPHQLAIDRPSQKLLKFLNKHYNLETTVPQVN 169
Cdd:pfam05301  88 KKLFLFDEQGQHHEMEPLCVLDFYVHESRQRHGLGKKLFDYMLKDENVEPYQLAIDRPSPKLLSFLKKHYGLKKTVPQVN 167


                  ....*....
gi 299758426  170 NFVIFEGFF 178
Cdd:pfam05301 168 NFVVFEGFF 176
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 79-136 2.95e-03

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: 35.33  E-value: 2.95e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 299758426  79 GAIIGFIkvgykklFVLDDREAHNEVEplcILDFYIHESVQRHGHGRELFQYMLQKER 136
Cdd:cd04301    8 GEIVGFA-------SLSPDGSGGDTAY---IGDLAVLPEYRGKGIGSALLEAAEEEAR 55
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 79-158 4.20e-03

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: 36.34  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758426   79 GAIIGFIKvgykkLFVLDDREAHNEveplcILDFYIHESVQRHGHGRELFQYMLQ---KERVEPHQLAIDRPSQKLLKFL 155
Cdd:pfam00583  42 GELVGFAS-----LSIIDDEPPVGE-----IEGLAVAPEYRGKGIGTALLQALLEwarERGCERIFLEVAADNLAAIALY 111


                  ...
gi 299758426  156 NKH 158
Cdd:pfam00583 112 EKL 114
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 61-154 4.34e-03

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 35.51  E-value: 4.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299758426   61 NRHVVYILKDssarpagKGAIIGFIKVGYkklfvlddreaHNEVEPLCILDFYIHESVQRHGHGRELFQYMLQKERVEPH 140
Cdd:pfam13508   1 PGGRFFVAED-------DGKIVGFAALLP-----------LDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGI 62

                          90
                  ....*....|....
gi 299758426  141 QLAIDRPSQKLLKF 154
Cdd:pfam13508  63 KLLELETTNRAAAF 76
 
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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