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Conserved domains on  [gi|974005250|ref|NP_001305692|]
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alpha-tubulin N-acetyltransferase 1 isoform 6 [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 ...
 10-190 1.09e-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: 303.72  E-value: 1.09e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005250   10 LFPERITVLDQHLRPPARRPGtttpaRVDLQQQIMTIIDELGKASAKAQNLSAPITSASRMQSNRHVVYILKDSSARpaG 89
Cdd:pfam05301   3 LFPDEITKLDNTLLPEGFCRE-----RQDLQRKLSEVIDEMGKASAKAQGLKTPITSAEKLQNSDHTLYLLKDGEAN--G 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005250   90 KGAIIGFIKVGYKKLFVLDDREAHNEVEPLCILDFYIHESVQRHGHGRELFQYMLQKERVEPHQLAIDRPSQKLLKFLNK 169
Cdd:pfam05301  76 KGAVVGLLKVGYKKLFLFDEQGQHHEMEPLCVLDFYVHESRQRHGLGKKLFDYMLKDENVEPYQLAIDRPSPKLLSFLKK 155

                         170       180
                  ....*....|....*....|.
gi 974005250  170 HYNLETTVPQVNNFVIFEGFF 190
Cdd:pfam05301 156 HYGLKKTVPQVNNFVVFEGFF 176
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
191-312 3.61e-03

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK14951:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 618  Bit Score: 38.93  E-value: 3.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005250 191 AHQHRPPAPSLRATRHSRAAAVDPTPAAPARKLPPKRAEGDIKPYSSSDReflkVAVEPPWPLNRAPRRATPPAHPPPRS 270
Cdd:PRK14951 395 AQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAA----VALAPAPPAQAAPETVAIPVRVAPEP 470

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 974005250 271 SslgnSPERGPLRPFVPEQELLRSLRLCPP-HPTARLLLAADP 312
Cdd:PRK14951 471 A----VASAAPAPAAAPAAARLTPTEEGDVwHATVQQLAAAEA 509
 
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 1.09e-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: 303.72  E-value: 1.09e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005250   10 LFPERITVLDQHLRPPARRPGtttpaRVDLQQQIMTIIDELGKASAKAQNLSAPITSASRMQSNRHVVYILKDSSARpaG 89
Cdd:pfam05301   3 LFPDEITKLDNTLLPEGFCRE-----RQDLQRKLSEVIDEMGKASAKAQGLKTPITSAEKLQNSDHTLYLLKDGEAN--G 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005250   90 KGAIIGFIKVGYKKLFVLDDREAHNEVEPLCILDFYIHESVQRHGHGRELFQYMLQKERVEPHQLAIDRPSQKLLKFLNK 169
Cdd:pfam05301  76 KGAVVGLLKVGYKKLFLFDEQGQHHEMEPLCVLDFYVHESRQRHGLGKKLFDYMLKDENVEPYQLAIDRPSPKLLSFLKK 155

                         170       180
                  ....*....|....*....|.
gi 974005250  170 HYNLETTVPQVNNFVIFEGFF 190
Cdd:pfam05301 156 HYGLKKTVPQVNNFVVFEGFF 176
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 91-148 3.33e-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: 3.33e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 974005250  91 GAIIGFIkvgykklFVLDDREAHNEVEplcILDFYIHESVQRHGHGRELFQYMLQKER 148
Cdd:cd04301    8 GEIVGFA-------SLSPDGSGGDTAY---IGDLAVLPEYRGKGIGSALLEAAEEEAR 55
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 191-312 3.61e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 38.93  E-value: 3.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005250 191 AHQHRPPAPSLRATRHSRAAAVDPTPAAPARKLPPKRAEGDIKPYSSSDReflkVAVEPPWPLNRAPRRATPPAHPPPRS 270
Cdd:PRK14951 395 AQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAA----VALAPAPPAQAAPETVAIPVRVAPEP 470

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 974005250 271 SslgnSPERGPLRPFVPEQELLRSLRLCPP-HPTARLLLAADP 312
Cdd:PRK14951 471 A----VASAAPAPAAAPAAARLTPTEEGDVwHATVQQLAAAEA 509
 
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 1.09e-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: 303.72  E-value: 1.09e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005250   10 LFPERITVLDQHLRPPARRPGtttpaRVDLQQQIMTIIDELGKASAKAQNLSAPITSASRMQSNRHVVYILKDSSARpaG 89
Cdd:pfam05301   3 LFPDEITKLDNTLLPEGFCRE-----RQDLQRKLSEVIDEMGKASAKAQGLKTPITSAEKLQNSDHTLYLLKDGEAN--G 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005250   90 KGAIIGFIKVGYKKLFVLDDREAHNEVEPLCILDFYIHESVQRHGHGRELFQYMLQKERVEPHQLAIDRPSQKLLKFLNK 169
Cdd:pfam05301  76 KGAVVGLLKVGYKKLFLFDEQGQHHEMEPLCVLDFYVHESRQRHGLGKKLFDYMLKDENVEPYQLAIDRPSPKLLSFLKK 155

                         170       180
                  ....*....|....*....|.
gi 974005250  170 HYNLETTVPQVNNFVIFEGFF 190
Cdd:pfam05301 156 HYGLKKTVPQVNNFVVFEGFF 176
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 91-148 3.33e-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: 3.33e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 974005250  91 GAIIGFIkvgykklFVLDDREAHNEVEplcILDFYIHESVQRHGHGRELFQYMLQKER 148
Cdd:cd04301    8 GEIVGFA-------SLSPDGSGGDTAY---IGDLAVLPEYRGKGIGSALLEAAEEEAR 55
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 191-312 3.61e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 38.93  E-value: 3.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005250 191 AHQHRPPAPSLRATRHSRAAAVDPTPAAPARKLPPKRAEGDIKPYSSSDReflkVAVEPPWPLNRAPRRATPPAHPPPRS 270
Cdd:PRK14951 395 AQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAA----VALAPAPPAQAAPETVAIPVRVAPEP 470

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 974005250 271 SslgnSPERGPLRPFVPEQELLRSLRLCPP-HPTARLLLAADP 312
Cdd:PRK14951 471 A----VASAAPAPAAAPAAARLTPTEEGDVwHATVQQLAAAEA 509
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 91-170 4.61e-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: 4.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005250   91 GAIIGFIKvgykkLFVLDDREAHNEveplcILDFYIHESVQRHGHGRELFQYMLQ---KERVEPHQLAIDRPSQKLLKFL 167
Cdd:pfam00583  42 GELVGFAS-----LSIIDDEPPVGE-----IEGLAVAPEYRGKGIGTALLQALLEwarERGCERIFLEVAADNLAAIALY 111


                  ...
gi 974005250  168 NKH 170
Cdd:pfam00583 112 EKL 114
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 73-166 4.93e-03

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 35.51  E-value: 4.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005250   73 NRHVVYILKDssarpagKGAIIGFIKVGYkklfvlddreaHNEVEPLCILDFYIHESVQRHGHGRELFQYMLQKERVEPH 152
Cdd:pfam13508   1 PGGRFFVAED-------DGKIVGFAALLP-----------LDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGI 62

                          90
                  ....*....|....
gi 974005250  153 QLAIDRPSQKLLKF 166
Cdd:pfam13508  63 KLLELETTNRAAAF 76
PHA03378 PHA03378
EBNA-3B; Provisional
 196-323 7.31e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 38.12  E-value: 7.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005250 196 PPAPSLRATRHSRAAAVDPTP-AAPARKLPPKRAEGDIKPYSSSDREFLKVAVEP--PWPLNRAPRRATPpaHPPPRSSS 272
Cdd:PHA03378 707 PAAPPGRAQRPAAATGRARPPaAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPgrARPPAAAPGAPTP--QPPPQAPP 784

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 974005250 273 LGNSPERGPLRPFVPEQELLRSLRLCPPHPTA----------RLLLAADPGGSPAQRRRTR 323
Cdd:PHA03378 785 APQQRPRGAPTPQPPPQAGPTSMQLMPRAAPGqqgptkqilrQLLTGGVKRGRPSLKKPAA 845
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 197-320 9.07e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 37.84  E-value: 9.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005250  197 PAPSLRATRHSRAAAVDPTPAAPARKLPPKRAEGDIKPYSSSDREFLKVAVEPPWPlnraPRRATPPAHPPPRSSSLGNS 276
Cdd:PHA03307  780 PQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAASRTASKRKSRSHTPDGGSESSGP----ARPPGAAARPPPARSSESSK 855

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 974005250  277 PERGPLRPFVPEQELLRSLRlcPPHPTARLLLAADPGGSPAQRR 320
Cdd:PHA03307  856 SKPAAAGGRARGKNGRRRPR--PPEPRARPGAAAPPKAAAAAPP 897
PHA03247 PHA03247
large tegument protein UL36; Provisional
 195-323 9.09e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 38.00  E-value: 9.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974005250  195 RPPAPSLRATRHSRAAAVDPTPAAPARKLPPKRA---EGDIKPYSSSDREFLKVAVEPPWPLNRAPRRATPPAHPPPRSS 271
Cdd:PHA03247 2756 RPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVAslsESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQ 2835

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 974005250  272 SLGNSPERGPLRPFVPEQEllrslRLCPPHPTARLLLAADPGGSPAQRRRTR 323
Cdd:PHA03247 2836 PTAPPPPPGPPPPSLPLGG-----SVAPGGDVRRRPPSRSPAAKPAAPARPP 2882
 
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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