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Conserved domains on  [gi|1907126334|ref|XP_036016698|]
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alpha-tubulin N-acetyltransferase 1 isoform X2 [Mus musculus]

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 ...
 10-190 2.08e-104

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: 301.79  E-value: 2.08e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126334  10 LFPERITVLDQHLRPPARRPGtttpaRVDLQQQIMTIVDELGKASAKAQHLPAPITSALRMQSNRHVIYILKDTSARpaG 89
Cdd:pfam05301   3 LFPDEITKLDNTLLPEGFCRE-----RQDLQRKLSEVIDEMGKASAKAQGLKTPITSAEKLQNSDHTLYLLKDGEAN--G 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126334  90 KGAIIGFLKVGYKKLFVLDDREAHNEVEPLCILDFYIHESVQRHGHGRELFQHMLQKERVEPHQLAIDRPSPKLLKFLNK 169
Cdd:pfam05301  76 KGAVVGLLKVGYKKLFLFDEQGQHHEMEPLCVLDFYVHESRQRHGLGKKLFDYMLKDENVEPYQLAIDRPSPKLLSFLKK 155

                         170       180
                  ....*....|....*....|.
gi 1907126334 170 HYNLETTVPQVNNFVIFEGFF 190
Cdd:pfam05301 156 HYGLKKTVPQVNNFVVFEGFF 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 ...
 10-190 2.08e-104

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: 301.79  E-value: 2.08e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126334  10 LFPERITVLDQHLRPPARRPGtttpaRVDLQQQIMTIVDELGKASAKAQHLPAPITSALRMQSNRHVIYILKDTSARpaG 89
Cdd:pfam05301   3 LFPDEITKLDNTLLPEGFCRE-----RQDLQRKLSEVIDEMGKASAKAQGLKTPITSAEKLQNSDHTLYLLKDGEAN--G 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126334  90 KGAIIGFLKVGYKKLFVLDDREAHNEVEPLCILDFYIHESVQRHGHGRELFQHMLQKERVEPHQLAIDRPSPKLLKFLNK 169
Cdd:pfam05301  76 KGAVVGLLKVGYKKLFLFDEQGQHHEMEPLCVLDFYVHESRQRHGLGKKLFDYMLKDENVEPYQLAIDRPSPKLLSFLKK 155

                         170       180
                  ....*....|....*....|.
gi 1907126334 170 HYNLETTVPQVNNFVIFEGFF 190
Cdd:pfam05301 156 HYGLKKTVPQVNNFVVFEGFF 176
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 91-148 2.71e-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: 35.71  E-value: 2.71e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907126334  91 GAIIGFLkvgykklFVLDDREAHNEVEplcILDFYIHESVQRHGHGRELFQHMLQKER 148
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 ...
 10-190 2.08e-104

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: 301.79  E-value: 2.08e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126334  10 LFPERITVLDQHLRPPARRPGtttpaRVDLQQQIMTIVDELGKASAKAQHLPAPITSALRMQSNRHVIYILKDTSARpaG 89
Cdd:pfam05301   3 LFPDEITKLDNTLLPEGFCRE-----RQDLQRKLSEVIDEMGKASAKAQGLKTPITSAEKLQNSDHTLYLLKDGEAN--G 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126334  90 KGAIIGFLKVGYKKLFVLDDREAHNEVEPLCILDFYIHESVQRHGHGRELFQHMLQKERVEPHQLAIDRPSPKLLKFLNK 169
Cdd:pfam05301  76 KGAVVGLLKVGYKKLFLFDEQGQHHEMEPLCVLDFYVHESRQRHGLGKKLFDYMLKDENVEPYQLAIDRPSPKLLSFLKK 155

                         170       180
                  ....*....|....*....|.
gi 1907126334 170 HYNLETTVPQVNNFVIFEGFF 190
Cdd:pfam05301 156 HYGLKKTVPQVNNFVVFEGFF 176
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 91-148 2.71e-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: 35.71  E-value: 2.71e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907126334  91 GAIIGFLkvgykklFVLDDREAHNEVEplcILDFYIHESVQRHGHGRELFQHMLQKER 148
Cdd:cd04301     8 GEIVGFA-------SLSPDGSGGDTAY---IGDLAVLPEYRGKGIGSALLEAAEEEAR 55
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 99-170 9.03e-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: 35.57  E-value: 9.03e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907126334  99 VGYKKLFVLDDREAHNEveplcILDFYIHESVQRHGHGRELFQHMLQ---KERVEPHQLAIDRPSPKLLKFLNKH 170
Cdd:pfam00583  45 VGFASLSIIDDEPPVGE-----IEGLAVAPEYRGKGIGTALLQALLEwarERGCERIFLEVAADNLAAIALYEKL 114
 
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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