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Conserved domains on  [gi|2360777647|emb|CAI4457892|]
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ALH_1c_G0017960.mRNA.1.CDS.1 [Saccharomyces cerevisiae]

Protein Classification

GNAT family protein( domain architecture ID 106742)

GNAT (Gcn5-related N-acetyltransferase) family protein similar to N-acetyltransferases that catalyze the transfer of an acetyl group from acetyl-CoA to a substrate

PubMed:  15581578

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NAT_SF super family cl17182
N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of ...
 10-142 2.69e-26

N-Acyltransferase superfamily: Various enyzmes that characteristicly 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, 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 mechanism is an ordered Bi-Bi ternary complex kinetic mechanism for most GNATs: 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 then 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/ph enylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


The actual alignment was detected with superfamily member PRK10562:

Pssm-ID: 473072 [Multi-domain]  Cd Length: 145  Bit Score: 96.29  E-value: 2.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360777647  10 SEELVAILHIWLQANIDAHHFIPKEYWERNYEFVRST-LPKATLFTYCVGNEIVGFLGLM-GSYIAGIFVKKQWRSCGIG 87
Cdd:PRK10562    7 PSDLPAILQLWLESTIWAHPFIKEQYWRESAPLVRDVyLPAAQTWVWEEDGKLLGFVSVLeGRFVGALFVAPKAVRRGIG 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2360777647  88 RKLINTVKAEKMRLSLSVYDKNERAISFYLSEGFTLKEKKIESETNEIESILFWA 142
Cdd:PRK10562   87 KALMQHVQQRYPHLSLEVYQKNQRAVNFYHAQGFRIVDSAWQEETQHPTWIMSWQ 141
 
Name Accession Description Interval E-value
PRK10562 PRK10562
putative acetyltransferase; Provisional
 10-142 2.69e-26

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 96.29  E-value: 2.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360777647  10 SEELVAILHIWLQANIDAHHFIPKEYWERNYEFVRST-LPKATLFTYCVGNEIVGFLGLM-GSYIAGIFVKKQWRSCGIG 87
Cdd:PRK10562    7 PSDLPAILQLWLESTIWAHPFIKEQYWRESAPLVRDVyLPAAQTWVWEEDGKLLGFVSVLeGRFVGALFVAPKAVRRGIG 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2360777647  88 RKLINTVKAEKMRLSLSVYDKNERAISFYLSEGFTLKEKKIESETNEIESILFWA 142
Cdd:PRK10562   87 KALMQHVQQRYPHLSLEVYQKNQRAVNFYHAQGFRIVDSAWQEETQHPTWIMSWQ 141
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 71-122 7.90e-11

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 55.05  E-value: 7.90e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2360777647  71 YIAGIFVKKQWRSCGIGRKLINTVKAE-----KMRLSLSVYDKNERAISFYLSEGFT 122
Cdd:COG0456    15 EIEDLAVDPEYRGRGIGRALLEAALERarergARRLRLEVREDNEAAIALYEKLGFE 71
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 48-122 1.35e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 51.69  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360777647  48 PKATLFTYCVGNEIVGFLGLM------GSYIAGIFVKKQWRSCGIGRKLINTVK--AEKMRLSLSVYDKNERAISFYLSE 119
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLplddegALAELRLAVHPEYRGQGIGRALLEAAEaaAKEGGIKLLELETTNRAAAFYEKL 80


                  ...
gi 2360777647 120 GFT 122
Cdd:pfam13508  81 GFE 83
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 52-97 3.14e-05

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: 39.57  E-value: 3.14e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2360777647  52 LFTYCVGNEIVGFLGLMGS-------YIAGIFVKKQWRSCGIGRKLINTVKAE 97
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPDgsggdtaYIGDLAVLPEYRGKGIGSALLEAAEEE 53
 
Name Accession Description Interval E-value
PRK10562 PRK10562
putative acetyltransferase; Provisional
 10-142 2.69e-26

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 96.29  E-value: 2.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360777647  10 SEELVAILHIWLQANIDAHHFIPKEYWERNYEFVRST-LPKATLFTYCVGNEIVGFLGLM-GSYIAGIFVKKQWRSCGIG 87
Cdd:PRK10562    7 PSDLPAILQLWLESTIWAHPFIKEQYWRESAPLVRDVyLPAAQTWVWEEDGKLLGFVSVLeGRFVGALFVAPKAVRRGIG 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2360777647  88 RKLINTVKAEKMRLSLSVYDKNERAISFYLSEGFTLKEKKIESETNEIESILFWA 142
Cdd:PRK10562   87 KALMQHVQQRYPHLSLEVYQKNQRAVNFYHAQGFRIVDSAWQEETQHPTWIMSWQ 141
PRK10514 PRK10514
putative acetyltransferase; Provisional
 1-121 1.06e-12

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 61.17  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360777647   1 MIKqITNVTSEELVAILHIWLQAnIDA-HHFIPKEYWERNYEFVRSTLPKATL-FTYCVGNEIVGFLGLMGSYIAGIFVK 78
Cdd:PRK10514    1 MIS-IRRSRHEEGERLVAIWRRS-VDAtHDFLSAEDRAEIEELVRSFLPEAPLwVAVDERDQPVGFMLLSGGHMEALFVD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2360777647  79 KQWRSCGIGRKLINTVKAEKMRLSLSVYDKNERAISFYLSEGF 121
Cdd:PRK10514   79 PDVRGCGVGRMLVEHALSLHPELTTDVNEQNEQAVGFYKKMGF 121
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 71-122 7.90e-11

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 55.05  E-value: 7.90e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2360777647  71 YIAGIFVKKQWRSCGIGRKLINTVKAE-----KMRLSLSVYDKNERAISFYLSEGFT 122
Cdd:COG0456    15 EIEDLAVDPEYRGRGIGRALLEAALERarergARRLRLEVREDNEAAIALYEKLGFE 71
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
4-122 1.88e-10

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 55.77  E-value: 1.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360777647   4 QITNVTSEELVAILHIWLQA---NIDAHHFIPKEYWERNYEFVRSTLPKATLFTYCVGNEIVGFLGLM---------GSY 71
Cdd:COG1247     3 TIRPATPEDAPAIAAIYNEAiaeGTATFETEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLGpfrprpayrGTA 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2360777647  72 IAGIFVKKQWRSCGIGRKLINTV--KAEKM---RLSLSVYDKNERAISFYLSEGFT 122
Cdd:COG1247    83 EESIYVDPDARGRGIGRALLEALieRARARgyrRLVAVVLADNEASIALYEKLGFE 138
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 48-122 1.35e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 51.69  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360777647  48 PKATLFTYCVGNEIVGFLGLM------GSYIAGIFVKKQWRSCGIGRKLINTVK--AEKMRLSLSVYDKNERAISFYLSE 119
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLplddegALAELRLAVHPEYRGQGIGRALLEAAEaaAKEGGIKLLELETTNRAAAFYEKL 80


                  ...
gi 2360777647 120 GFT 122
Cdd:pfam13508  81 GFE 83
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 45-122 1.58e-09

N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 52.75  E-value: 1.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360777647  45 STLPKATLFTYCVGNEIVGFLGLM-----GSYIAGIFVKKQWRSCGIGRKLINtvKAEKM-------RLSLSVYDKNERA 112
Cdd:COG0454    29 GSLAGAEFIAVDDKGEPIGFAGLRrlddkVLELKRLYVLPEYRGKGIGKALLE--ALLEWarergctALELDTLDGNPAA 106

                          90
                  ....*....|
gi 2360777647 113 ISFYLSEGFT 122
Cdd:COG0454   107 IRFYERLGFK 116
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 13-121 2.53e-09

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: 51.75  E-value: 2.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360777647  13 LVAILHIWLQANIDAHHFIPKEYWERNYEfvrstLPKATLFTYCVGNEIVGFLGLM-------GSYIAGIFVKKQWRSCG 85
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDE-----DASEGFFVAEEDGELVGFASLSiiddeppVGEIEGLAVAPEYRGKG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2360777647  86 IGRKLINTV--KAEKM---RLSLSVYDKNERAISFYLSEGF 121
Cdd:pfam00583  76 IGTALLQALleWARERgceRIFLEVAADNLAAIALYEKLGF 116
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 28-134 4.92e-08

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 48.42  E-value: 4.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360777647  28 HHFIPKEYWERnyefvRSTLPKATLFTYCVGNEIVGFLGLM-GSYIAGIFVKKQWRSCGIGRKLINTVKAE-------KM 99
Cdd:pfam13673  14 YEFISPEALRE-----RIDQGEYFFFVAFEGGQIVGVIALRdRGHISLLFVDPDYQGQGIGKALLEAVEDYaekdgikLS 88

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2360777647 100 RLSL--SVYdknerAISFYLSEGFtlkeKKIESETNE 134
Cdd:pfam13673  89 ELTVnaSPY-----AVPFYEKLGF----RATGPEQEF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
5-122 1.50e-07

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 47.39  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360777647   5 ITNVTSEELVAILHIWLQAnidahhFiPKEYWERNYEFVRSTLPKATLFTYCVGNEIVGFLGLMGS---------YIAGI 75
Cdd:COG3153     1 IRPATPEDAEAIAALLRAA------F-GPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVdidgegpalLLGPL 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2360777647  76 FVKKQWRSCGIGRKLINTV--KAEKMRLSLSVYDKNERAISFYLSEGFT 122
Cdd:COG3153    74 AVDPEYRGQGIGRALMRAAleAARERGARAVVLLGDPSLLPFYERFGFR 122
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 48-122 4.60e-06

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 43.44  E-value: 4.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360777647  48 PKATLFTYCVGNEIVGFLGLMGS-----YIAGIFVKKQWRSCGIGRKLINTV--KAEKM---RLSLSVYDkneRAISFYL 117
Cdd:COG1246    26 EIGEFWVAEEDGEIVGCAALHPLdedlaELRSLAVHPDYRGRGIGRRLLEALlaEARELglkRLFLLTTS---AAIHFYE 102


                  ....*
gi 2360777647 118 SEGFT 122
Cdd:COG1246   103 KLGFE 107
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 52-97 3.14e-05

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: 39.57  E-value: 3.14e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2360777647  52 LFTYCVGNEIVGFLGLMGS-------YIAGIFVKKQWRSCGIGRKLINTVKAE 97
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPDgsggdtaYIGDLAVLPEYRGKGIGSALLEAAEEE 53
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
48-122 9.12e-04

Predicted N-acyltransferase, GNAT family [General function prediction only];


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 37.09  E-value: 9.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360777647  48 PKATLFTYCVGNEIVG-----FLGLMGSYIAGIFVKKQWRSCGIGRKLINTV-------KAEKMRLSLSVYdknerAISF 115
Cdd:COG2153    32 EDARHLLAYDDGELVAtarllPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAieearerGARRIVLSAQAH-----AVGF 106


                  ....*..
gi 2360777647 116 YLSEGFT 122
Cdd:COG2153   107 YEKLGFV 113
PRK09831 PRK09831
GNAT family N-acetyltransferase;
4-129 3.85e-03

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 35.70  E-value: 3.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2360777647   4 QITNVTSEELVAILHIWLQA--NIDAHHFIPKEY--WERNYEFV-RSTLPKATLFTYCVGNEIVGFLGLMGSYIAGIFVK 78
Cdd:PRK09831    2 QIRNYQPGDFQQLCAIFIRAvtMTASQHYSPQQIaaWAQIDESRwKEKLAKSQVRVAVINAQPVGFITCIEHYIDMLFVD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2360777647  79 KQWRSCGIGRKLINTVKAEKMRLSLsvyDKNERAISFYLSEGF-TLKEKKIE 129
Cdd:PRK09831   82 PEYTRRGVASALLKPLIKSESELTV---DASITAKPFFERYGFqTVKQQRVE 130
 
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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