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Conserved domains on  [gi|14318503|ref|NP_116637|]
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glucosamine 6-phosphate N-acetyltransferase [Saccharomyces cerevisiae S288C]

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 ...
 5-155 1.14e-39

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 PLN02706:

Pssm-ID: 473072 [Multi-domain]  Cd Length: 150  Bit Score: 130.98  E-value: 1.14e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318503    5 DGFYIRRMEEGDLEQ-VTETLKVLTTVGTITPESFSKLIKYwneatVWNDNEDKKIMqynpmVIVDKRTETVAATGNIII 83
Cdd:PLN02706   5 EKFKVRRLEISDKSKgFLELLQQLTVVGDVTEEEFEARFQE-----LASLGDDHLIC-----VIEDAASGRIIATGSVFV 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14318503   84 ERKIIHELGLCGHIEDIAVNSKYQGQGLGKLLIDQLVTIGFDYGCYKIILDCDEKNVKFYEKCGFSNAGVEM 155
Cdd:PLN02706  75 ERKFIRNCGKVGHIEDVVVDSAARGKGLGKKIIEALTEHARSAGCYKVILDCSEENKAFYEKCGYVRKEIQM 146
 
Name Accession Description Interval E-value
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
 5-155 1.14e-39

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 130.98  E-value: 1.14e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318503    5 DGFYIRRMEEGDLEQ-VTETLKVLTTVGTITPESFSKLIKYwneatVWNDNEDKKIMqynpmVIVDKRTETVAATGNIII 83
Cdd:PLN02706   5 EKFKVRRLEISDKSKgFLELLQQLTVVGDVTEEEFEARFQE-----LASLGDDHLIC-----VIEDAASGRIIATGSVFV 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14318503   84 ERKIIHELGLCGHIEDIAVNSKYQGQGLGKLLIDQLVTIGFDYGCYKIILDCDEKNVKFYEKCGFSNAGVEM 155
Cdd:PLN02706  75 ERKFIRNCGKVGHIEDVVVDSAARGKGLGKKIIEALTEHARSAGCYKVILDCSEENKAFYEKCGYVRKEIQM 146
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 63-148 2.12e-18

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: 75.63  E-value: 2.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318503    63 NPMVIVDKRTETVAATGNIiierKIIHELGLCGHIEDIAVNSKYQGQGLGKLLIDQLVTIGFDYGCYKIILDCDEKN--- 139
Cdd:pfam00583  32 SEGFFVAEEDGELVGFASL----SIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNlaa 107


                  ....*....
gi 14318503   140 VKFYEKCGF 148
Cdd:pfam00583 108 IALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 95-153 5.21e-15

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 66.22  E-value: 5.21e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14318503  95 GHIEDIAVNSKYQGQGLGKLLIDQLVTIGFDYGCYKIILDCDEKN---VKFYEKCGFSNAGV 153
Cdd:COG0456  14 AEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNeaaIALYEKLGFEEVGE 75
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 95-153 3.16e-10

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 54.64  E-value: 3.16e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14318503    95 GHIEDIAVNSKYQGQGLGKLLIDQLVTIGFDYGCYKIILDCDEKNV---KFYEKCGFSNAGV 153
Cdd:TIGR01575  55 AHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIaaqALYKKLGFNEIAI 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 94-134 3.48e-07

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: 44.96  E-value: 3.48e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 14318503  94 CGHIEDIAVNSKYQGQGLGKLLIDQLVTIGFDYGCYKIILD 134
Cdd:cd04301  25 TAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
 
Name Accession Description Interval E-value
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
 5-155 1.14e-39

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 130.98  E-value: 1.14e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318503    5 DGFYIRRMEEGDLEQ-VTETLKVLTTVGTITPESFSKLIKYwneatVWNDNEDKKIMqynpmVIVDKRTETVAATGNIII 83
Cdd:PLN02706   5 EKFKVRRLEISDKSKgFLELLQQLTVVGDVTEEEFEARFQE-----LASLGDDHLIC-----VIEDAASGRIIATGSVFV 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14318503   84 ERKIIHELGLCGHIEDIAVNSKYQGQGLGKLLIDQLVTIGFDYGCYKIILDCDEKNVKFYEKCGFSNAGVEM 155
Cdd:PLN02706  75 ERKFIRNCGKVGHIEDVVVDSAARGKGLGKKIIEALTEHARSAGCYKVILDCSEENKAFYEKCGYVRKEIQM 146
PTZ00330 PTZ00330
acetyltransferase; Provisional
 9-158 2.91e-23

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 89.13  E-value: 2.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318503    9 IRRMEEGDLEQVTETLKVLTTVGTITPESFSKLikywneatvwndNEDKKIMQYNPMVIVDKRTETVAATGNIIIERKII 88
Cdd:PTZ00330   9 LRDLEEGDLGSVLELLSHLTSAPALSQEELEQI------------AARRRLAGVVTRVFVHSPTQRIVGTASLFVEPKFT 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318503   89 HELGLCGHIEDIAVNSKYQGQGLGKLLIDQLVTIGFDYGCYKIILDCDEKNVKFYEKCGFSNAgvEMQIR 158
Cdd:PTZ00330  77 RGGKCVGHIEDVVVDPSYRGQGLGRALISDLCEIARSSGCYKVILDCTEDMVAFYKKLGFRAC--ERQMR 144
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 63-148 2.12e-18

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: 75.63  E-value: 2.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318503    63 NPMVIVDKRTETVAATGNIiierKIIHELGLCGHIEDIAVNSKYQGQGLGKLLIDQLVTIGFDYGCYKIILDCDEKN--- 139
Cdd:pfam00583  32 SEGFFVAEEDGELVGFASL----SIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNlaa 107


                  ....*....
gi 14318503   140 VKFYEKCGF 148
Cdd:pfam00583 108 IALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 95-153 5.21e-15

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 66.22  E-value: 5.21e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14318503  95 GHIEDIAVNSKYQGQGLGKLLIDQLVTIGFDYGCYKIILDCDEKN---VKFYEKCGFSNAGV 153
Cdd:COG0456  14 AEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNeaaIALYEKLGFEEVGE 75
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
79-152 1.37e-12

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 61.25  E-value: 1.37e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14318503  79 GNIIIERKIIHELGLCGHIEDIAVNSKYQGQGLGKLLIDQLVTIGFDYGCYKIILDCDEKNVKFYEKCGFSNAG 152
Cdd:COG3153  52 GHVALSPVDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRPAG 125
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 75-148 6.74e-12

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 57.85  E-value: 6.74e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14318503    75 VAATGNIII--ERKIIHELGLCGHIEDIAVNSKYQGQGLGKLLIDQLVTIGFDYGCYKIILDCDEKNVKFYEKCGF 148
Cdd:pfam13508   7 VAEDDGKIVgfAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGF 82
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
95-148 7.48e-11

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 56.35  E-value: 7.48e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 14318503  95 GHIEDIAVNSKYQGQGLGKLLIDQLVTIGFDYGCYKIILDCDEKNVKFYEKCGF 148
Cdd:COG2153  59 AKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAHAVGFYEKLGF 112
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 95-154 1.01e-10

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: 56.15  E-value: 1.01e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318503  95 GHIEDIAVNSKYQGQGLGKLLIDQLVTIGFDYGCYKIILDCDEKNVKFYEKCGFSNAGVE 154
Cdd:COG1246  53 AELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSAAIHFYEKLGFEEIDKE 112
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 95-148 2.25e-10

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 55.44  E-value: 2.25e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 14318503  95 GHIEDIAVNSKYQGQGLGKLLIDQLVTIGFDYGCYKIILDC---DEKNVKFYEKCGF 148
Cdd:COG0454  59 LELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTldgNPAAIRFYERLGF 115
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 95-153 3.16e-10

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 54.64  E-value: 3.16e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14318503    95 GHIEDIAVNSKYQGQGLGKLLIDQLVTIGFDYGCYKIILDCDEKNV---KFYEKCGFSNAGV 153
Cdd:TIGR01575  55 AHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIaaqALYKKLGFNEIAI 116
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 5-156 1.44e-08

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 51.15  E-value: 1.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318503   5 DGFYIRRMEEGDLEQVTE-----TLKVLTTVGTITPESFSKLIKYWNEAtvWNDNEdkkimqYNPMVIVDKRTETVAATG 79
Cdd:COG1670   6 ERLRLRPLRPEDAEALAEllndpEVARYLPGPPYSLEEARAWLERLLAD--WADGG------ALPFAIEDKEDGELIGVV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318503  80 NIIIERKIIHELGLcghieDIAVNSKYQGQGLGKLLIDQLVTIGFD-YGCYKIILDCDEKNV---KFYEKCGFSNAGVEM 155
Cdd:COG1670  78 GLYDIDRANRSAEI-----GYWLAPAYWGKGYATEALRALLDYAFEeLGLHRVEAEVDPDNTasiRVLEKLGFRLEGTLR 152


                .
gi 14318503 156 Q 156
Cdd:COG1670 153 D 153
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
98-159 9.70e-08

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 48.84  E-value: 9.70e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14318503  98 EDIAVNSKYQGQGLGKLLIDQLVTIGFDYGCYKIILDCDEKN---VKFYEKCGFSNAGVEMQIRK 159
Cdd:COG1247  84 ESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNeasIALYEKLGFEEVGTLPEVGF 148
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 94-134 3.48e-07

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: 44.96  E-value: 3.48e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 14318503  94 CGHIEDIAVNSKYQGQGLGKLLIDQLVTIGFDYGCYKIILD 134
Cdd:cd04301  25 TAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
87-148 2.20e-06

Predicted acetyltransferase, GNAT family [General function prediction only];


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 43.36  E-value: 2.20e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14318503  87 IIHELGLCGHIEDIAVNSKYQGQGLGKLLIDQLVTIGFDYGCYKIILDCDEKN---VKFYEKCGF 148
Cdd:COG3393   8 VRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNpaaRRLYERLGF 72
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 94-154 2.46e-06

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: 44.18  E-value: 2.46e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318503    94 CGHIEDIAVNSKYQGQGLGKLLIDQLVTIGFDYGCYKIILDCDEKN--VKFYEKCGFSNAGVE 154
Cdd:pfam13673  51 RGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNASPyaVPFYEKLGFRATGPE 113
PRK07757 PRK07757
N-acetyltransferase;
91-149 9.96e-05

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 40.18  E-value: 9.96e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14318503   91 LGLCG-HI--EDIA------VNSKYQGQGLGKLLIDQLVTIGFDYGCYKIIldCDEKNVKFYEKCGFS 149
Cdd:PRK07757  53 VGCCAlHIlwEDLAeirslaVSEDYRGQGIGRMLVEACLEEARELGVKRVF--ALTYQPEFFEKLGFR 118
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 100-159 1.82e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 36.45  E-value: 1.82e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14318503  100 IAVNSKYQGQGLGKLLIDQLVTIGFDYGCYKIILDCDEKNV---KFYEKCGFSnagvEMQIRK 159
Cdd:PRK09491  69 IAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAaaiALYESLGFN----EVTIRR 127
Citrate_lyase_ligase cd02169
Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is ...
 81-150 5.75e-03

Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is responsible for acetylation of the (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) prosthetic group of the gamma subunit of citrate lyase, converting the inactive thiol form of this enzyme to the active form. The acetylation of 1 molecule of deacetyl-citrate lyase to enzymatically active citrate lyase requires 6 molecules of ATP. The Adenylylyltranferase activity of the enzyme involves the formation of AMP and and pyrophosphate in the acetylation reaction.


Pssm-ID: 173920 [Multi-domain]  Cd Length: 297  Bit Score: 36.09  E-value: 5.75e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318503  81 IIIERKIIHELGLCGH-IEDIAVNSKYQGQGLGKLLIDQLVTIGFDYGCYKIILDCDEKNVKFYEKCGFSN 150
Cdd:cd02169  11 FDDAGELIATGSIAGNvLKCVAVCPKYQGEGLALKIVSELINKAYEEGIFHLFLFTKPKNAKFFRGLGFKE 81
PRK10514 PRK10514
putative acetyltransferase; Provisional
 95-152 5.90e-03

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 35.36  E-value: 5.90e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318503   95 GHIEDIAVNSKYQGQGLGKLLIDQLVTIGFDygcykIILDCDEKN---VKFYEKCGFSNAG 152
Cdd:PRK10514  70 GHMEALFVDPDVRGCGVGRMLVEHALSLHPE-----LTTDVNEQNeqaVGFYKKMGFKVTG 125
 
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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