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Conserved domains on  [gi|22137720|gb|AAH28847|]
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2610110G12Rik protein [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

CATH:  3.40.630.30
EC:  2.3.1.108
Gene Ontology:  GO:0019799|GO:0004468|GO:0071929
PubMed:  23105108
SCOP:  3000403

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 8.98e-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: 304.88  E-value: 8.98e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22137720    10 LFPERITVLDQHLRPPARRPGtttpaRVDLQQQIMTIVDELGKASAKAQHLPAPITSALRMQSNRHVIYILKDTSARpaG 89
Cdd:pfam05301   3 LFPDEITKLDNTLLPEGFCRE-----RQDLQRKLSEVIDEMGKASAKAQGLKTPITSAEKLQNSDHTLYLLKDGEAN--G 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22137720    90 KGAIIGFLKVGYKKLFVLDDREAHNEVEPLCILDFYIHESVQRHGHGRELFQHMLQKERVEPHQLAIDRPSPKLLKFLNK 169
Cdd:pfam05301  76 KGAVVGLLKVGYKKLFLFDEQGQHHEMEPLCVLDFYVHESRQRHGLGKKLFDYMLKDENVEPYQLAIDRPSPKLLSFLKK 155

                         170       180
                  ....*....|....*....|.
gi 22137720   170 HYNLETTVPQVNNFVIFEGFF 190
Cdd:pfam05301 156 HYGLKKTVPQVNNFVVFEGFF 176
PHA03378 super family cl33729
EBNA-3B; Provisional
 209-326 4.37e-03

EBNA-3B; Provisional


The actual alignment was detected with superfamily member PHA03378:

Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.67  E-value: 4.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22137720  209 AAVADPIPAAPARKLPPKRAEGDIKPYSSsdreflkvavePPWPLNRaPRRATPPAHPPPRSSSLGNSPDRGPLRPFVPE 288
Cdd:PHA03378 681 ANTMLPIQWAPGTMQPPPRAPTPMRPPAA-----------PPGRAQR-PAAATGRARPPAAAPGRARPPAAAPGRARPPA 748

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 22137720  289 QELLRSLRLCPPHPTARLLLATD--------PGGSPAQRRRTRGTP 326
Cdd:PHA03378 749 AAPGRARPPAAAPGRARPPAAAPgaptpqppPQAPPAPQQRPRGAP 794
 
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 8.98e-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: 304.88  E-value: 8.98e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22137720    10 LFPERITVLDQHLRPPARRPGtttpaRVDLQQQIMTIVDELGKASAKAQHLPAPITSALRMQSNRHVIYILKDTSARpaG 89
Cdd:pfam05301   3 LFPDEITKLDNTLLPEGFCRE-----RQDLQRKLSEVIDEMGKASAKAQGLKTPITSAEKLQNSDHTLYLLKDGEAN--G 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22137720    90 KGAIIGFLKVGYKKLFVLDDREAHNEVEPLCILDFYIHESVQRHGHGRELFQHMLQKERVEPHQLAIDRPSPKLLKFLNK 169
Cdd:pfam05301  76 KGAVVGLLKVGYKKLFLFDEQGQHHEMEPLCVLDFYVHESRQRHGLGKKLFDYMLKDENVEPYQLAIDRPSPKLLSFLKK 155

                         170       180
                  ....*....|....*....|.
gi 22137720   170 HYNLETTVPQVNNFVIFEGFF 190
Cdd:pfam05301 156 HYGLKKTVPQVNNFVVFEGFF 176
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 91-148 3.88e-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: 3.88e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 22137720  91 GAIIGFLkvgykklFVLDDREAHNEVEplcILDFYIHESVQRHGHGRELFQHMLQKER 148
Cdd:cd04301   8 GEIVGFA-------SLSPDGSGGDTAY---IGDLAVLPEYRGKGIGSALLEAAEEEAR 55
PHA03378 PHA03378
EBNA-3B; Provisional
 209-326 4.37e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.67  E-value: 4.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22137720  209 AAVADPIPAAPARKLPPKRAEGDIKPYSSsdreflkvavePPWPLNRaPRRATPPAHPPPRSSSLGNSPDRGPLRPFVPE 288
Cdd:PHA03378 681 ANTMLPIQWAPGTMQPPPRAPTPMRPPAA-----------PPGRAQR-PAAATGRARPPAAAPGRARPPAAAPGRARPPA 748

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 22137720  289 QELLRSLRLCPPHPTARLLLATD--------PGGSPAQRRRTRGTP 326
Cdd:PHA03378 749 AAPGRARPPAAAPGRARPPAAAPgaptpqppPQAPPAPQQRPRGAP 794
 
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 8.98e-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: 304.88  E-value: 8.98e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22137720    10 LFPERITVLDQHLRPPARRPGtttpaRVDLQQQIMTIVDELGKASAKAQHLPAPITSALRMQSNRHVIYILKDTSARpaG 89
Cdd:pfam05301   3 LFPDEITKLDNTLLPEGFCRE-----RQDLQRKLSEVIDEMGKASAKAQGLKTPITSAEKLQNSDHTLYLLKDGEAN--G 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22137720    90 KGAIIGFLKVGYKKLFVLDDREAHNEVEPLCILDFYIHESVQRHGHGRELFQHMLQKERVEPHQLAIDRPSPKLLKFLNK 169
Cdd:pfam05301  76 KGAVVGLLKVGYKKLFLFDEQGQHHEMEPLCVLDFYVHESRQRHGLGKKLFDYMLKDENVEPYQLAIDRPSPKLLSFLKK 155

                         170       180
                  ....*....|....*....|.
gi 22137720   170 HYNLETTVPQVNNFVIFEGFF 190
Cdd:pfam05301 156 HYGLKKTVPQVNNFVVFEGFF 176
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 91-148 3.88e-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: 3.88e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 22137720  91 GAIIGFLkvgykklFVLDDREAHNEVEplcILDFYIHESVQRHGHGRELFQHMLQKER 148
Cdd:cd04301   8 GEIVGFA-------SLSPDGSGGDTAY---IGDLAVLPEYRGKGIGSALLEAAEEEAR 55
PHA03378 PHA03378
EBNA-3B; Provisional
 209-326 4.37e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.67  E-value: 4.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22137720  209 AAVADPIPAAPARKLPPKRAEGDIKPYSSsdreflkvavePPWPLNRaPRRATPPAHPPPRSSSLGNSPDRGPLRPFVPE 288
Cdd:PHA03378 681 ANTMLPIQWAPGTMQPPPRAPTPMRPPAA-----------PPGRAQR-PAAATGRARPPAAAPGRARPPAAAPGRARPPA 748

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 22137720  289 QELLRSLRLCPPHPTARLLLATD--------PGGSPAQRRRTRGTP 326
Cdd:PHA03378 749 AAPGRARPPAAAPGRARPPAAAPgaptpqppPQAPPAPQQRPRGAP 794
PHA03378 PHA03378
EBNA-3B; Provisional
 195-324 4.37e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.67  E-value: 4.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22137720  195 RPPTSSLRATRHSRAAV--ADPIPAAPARKLPPKRAEGDIKPYSSSDREFLKVAVEP--PWPLNRAPRRATPpaHPPPRS 270
Cdd:PHA03378 705 RPPAAPPGRAQRPAAATgrARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPgrARPPAAAPGAPTP--QPPPQA 782

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22137720  271 SSLGNSPDRGPLRPFVPEQELLRSLRLCPPHPTA----------RLLLATDPGGSPAQRRRTRG 324
Cdd:PHA03378 783 PPAPQQRPRGAPTPQPPPQAGPTSMQLMPRAAPGqqgptkqilrQLLTGGVKRGRPSLKKPAAL 846
 
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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