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Conserved domains on  [gi|742381234|ref|WP_038860361|]
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GNAT family N-acetyltransferase [Cronobacter sakazakii]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10006981)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

CATH:  3.40.630.30
EC:  2.3.-.-
Gene Ontology:  GO:0016746|GO:0008080
PubMed:  27367672|26818562|15581578|10940244
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
10-121 3.76e-12

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


:

Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 59.71  E-value: 3.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742381234  10 ETP-DWQALATLIERAGLGARDPHEVERcYRNS---TFCWYGFHEGKLVATAHA----ISDLTWSSYVADIVVDPDYQGR 81
Cdd:COG3153    4 ATPeDAEAIAALLRAAFGPGREAELVDR-LREDpaaGLSLVAEDDGEIVGHVALspvdIDGEGPALLLGPLAVDPEYRGQ 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 742381234  82 GFGNQLMDEILETL--LPFGKVFIYAVLDKVAFYKKYQFREL 121
Cdd:COG3153   83 GIGRALMRAALEAAreRGARAVVLLGDPSLLPFYERFGFRPA 124
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
10-121 3.76e-12

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 59.71  E-value: 3.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742381234  10 ETP-DWQALATLIERAGLGARDPHEVERcYRNS---TFCWYGFHEGKLVATAHA----ISDLTWSSYVADIVVDPDYQGR 81
Cdd:COG3153    4 ATPeDAEAIAALLRAAFGPGREAELVDR-LREDpaaGLSLVAEDDGEIVGHVALspvdIDGEGPALLLGPLAVDPEYRGQ 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 742381234  82 GFGNQLMDEILETL--LPFGKVFIYAVLDKVAFYKKYQFREL 121
Cdd:COG3153   83 GIGRALMRAALEAAreRGARAVVLLGDPSLLPFYERFGFRPA 124
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 14-115 4.68e-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: 50.98  E-value: 4.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742381234   14 WQALATLIERAGLGARDPHEV----ERCYRNSTFCWYGFHEGKLVATA--HAISDLTWSSYVADIVVDPDYQGRGFGNQL 87
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLdlleDWDEDASEGFFVAEEDGELVGFAslSIIDDEPPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 742381234   88 MDEILETLLPFGKVFIYAVLDK-----VAFYKK 115
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAAdnlaaIALYEK 113
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 13-122 2.89e-08

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: 49.25  E-value: 2.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742381234   13 DWQALATLIERAGLGARDPHEVERCYRNSTFCWYGFHEGKLVAtAHAISDLTWSSY-VADIVVDPDYQGRGFGNQLMDEI 91
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPWTEAQFAEELANYHLCYLLARIGGKVV-GYAGVQIVLDEAhILNIAVKPEYQGQGIGRALLREL 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 742381234   92 LETLLPFGKVFIYavLD-------KVAFYKKYQFRELT 122
Cdd:TIGR01575  80 IDEAKGRGVNEIF--LEvrvsniaAQALYKKLGFNEIA 115
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 44-93 1.57e-06

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: 43.03  E-value: 1.57e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 742381234  44 CWYGFHEGKLVATA--HAISDLTWSSYVADIVVDPDYQGRGFGNQLMDEILE 93
Cdd:cd04301    1 FLVAEDDGEIVGFAslSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEE 52
PTZ00330 PTZ00330
acetyltransferase; Provisional
 68-125 6.76e-06

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 42.91  E-value: 6.76e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 742381234  68 YVADIVVDPDYQGRGFGNQLMDEILETLLPFG--KVFIYAVLDKVAFYKKYQFRELTSGM 125
Cdd:PTZ00330  84 HIEDVVVDPSYRGQGLGRALISDLCEIARSSGcyKVILDCTEDMVAFYKKLGFRACERQM 143
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
10-121 3.76e-12

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 59.71  E-value: 3.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742381234  10 ETP-DWQALATLIERAGLGARDPHEVERcYRNS---TFCWYGFHEGKLVATAHA----ISDLTWSSYVADIVVDPDYQGR 81
Cdd:COG3153    4 ATPeDAEAIAALLRAAFGPGREAELVDR-LREDpaaGLSLVAEDDGEIVGHVALspvdIDGEGPALLLGPLAVDPEYRGQ 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 742381234  82 GFGNQLMDEILETL--LPFGKVFIYAVLDKVAFYKKYQFREL 121
Cdd:COG3153   83 GIGRALMRAALEAAreRGARAVVLLGDPSLLPFYERFGFRPA 124
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 10-121 5.63e-11

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: 5.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742381234  10 ETPDWQALATLIERAGLgardphevercYRNSTFCWYGFHEGKLVATAHAISDLTWSSYVADIVVDPDYQGRGFGNQLMD 89
Cdd:COG1246    7 TPDDVPAILELIRPYAL-----------EEEIGEFWVAEEDGEIVGCAALHPLDEDLAELRSLAVHPDYRGRGIGRRLLE 75

                         90       100       110
                 ....*....|....*....|....*....|....
gi 742381234  90 EILETLLPFG--KVFIYAVLDKVAFYKKYQFREL 121
Cdd:COG1246   76 ALLAEARELGlkRLFLLTTSAAIHFYEKLGFEEI 109
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 14-115 4.68e-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: 50.98  E-value: 4.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742381234   14 WQALATLIERAGLGARDPHEV----ERCYRNSTFCWYGFHEGKLVATA--HAISDLTWSSYVADIVVDPDYQGRGFGNQL 87
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLdlleDWDEDASEGFFVAEEDGELVGFAslSIIDDEPPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 742381234   88 MDEILETLLPFGKVFIYAVLDK-----VAFYKK 115
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAAdnlaaIALYEK 113
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 40-120 5.75e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 49.76  E-value: 5.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742381234   40 NSTFCWYGFHEGKLVATAHA-ISDLTWSSYVADIVVDPDYQGRGFGNQLMDEILETL--LPFGKVFIYAVLDKVAFYKKY 116
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALlPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAkeGGIKLLELETTNRAAAFYEKL 80


                  ....
gi 742381234  117 QFRE 120
Cdd:pfam13508  81 GFEE 84
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 13-122 2.89e-08

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: 49.25  E-value: 2.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742381234   13 DWQALATLIERAGLGARDPHEVERCYRNSTFCWYGFHEGKLVAtAHAISDLTWSSY-VADIVVDPDYQGRGFGNQLMDEI 91
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPWTEAQFAEELANYHLCYLLARIGGKVV-GYAGVQIVLDEAhILNIAVKPEYQGQGIGRALLREL 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 742381234   92 LETLLPFGKVFIYavLD-------KVAFYKKYQFRELT 122
Cdd:TIGR01575  80 IDEAKGRGVNEIF--LEvrvsniaAQALYKKLGFNEIA 115
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 13-119 4.84e-08

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 48.34  E-value: 4.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742381234   13 DWQALATLIERAgLGARDPHEVERCYRN---STFCWYGFHEGKLVATAHAIsDLTWS--------SYVADIVVDPDYQGR 81
Cdd:pfam13527   8 EFDEVLRLLEYA-FQDEDSPELREYFRPlleEGRVLGAFDDGELVSTLALY-PFELNvpgktlpaAGITGVATYPEYRGR 85

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 742381234   82 GFGNQLMDEILETLLPFGKVFIYAVLDKVAFYKKYQFR 119
Cdd:pfam13527  86 GVMSRLLRRSLEEMRERGVPLSFLYPSSYPIYRRFGYE 123
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 68-120 2.77e-07

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 45.80  E-value: 2.77e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 742381234  68 YVADIVVDPDYQGRGFGNQLMDEILETLLPFGKVFIYAVLDK-----VAFYKKYQFRE 120
Cdd:COG0456   15 EIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREdneaaIALYEKLGFEE 72
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
13-121 4.97e-07

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 46.53  E-value: 4.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742381234  13 DWQALATLIERA--------GLGARDPHEVER----CYRNSTFCWYGFHEGKLVATAHAISDLTWSSY----VADIVVDP 76
Cdd:COG1247   11 DAPAIAAIYNEAiaegtatfETEPPSEEEREAwfaaILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYrgtaEESIYVDP 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 742381234  77 DYQGRGFGNQLMDEILETLLPFGKVFIYAVLDK-----VAFYKKYQFREL 121
Cdd:COG1247   91 DARGRGIGRALLEALIERARARGYRRLVAVVLAdneasIALYEKLGFEEV 140
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
47-120 5.45e-07

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 45.56  E-value: 5.45e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742381234  47 GFHEGKLVATAHAISDLTWSSYVADIVVDPDYQGRGFGNQLMDEILETL--LPFGKVFIYAVLDKVAFYKKYQFRE 120
Cdd:COG2153   39 AYDDGELVATARLLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEAreRGARRIVLSAQAHAVGFYEKLGFVP 114
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 35-123 1.40e-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: 44.57  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742381234   35 ERCYRNSTFCWYGFHEGKLVATAhAISDltwSSYVADIVVDPDYQGRGFGNQLMDEILETLLP----FGKVFIYAVLDKV 110
Cdd:pfam13673  24 ERIDQGEYFFFVAFEGGQIVGVI-ALRD---RGHISLLFVDPDYQGQGIGKALLEAVEDYAEKdgikLSELTVNASPYAV 99

                          90
                  ....*....|...
gi 742381234  111 AFYKKYQFRELTS 123
Cdd:pfam13673 100 PFYEKLGFRATGP 112
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 44-93 1.57e-06

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: 43.03  E-value: 1.57e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 742381234  44 CWYGFHEGKLVATA--HAISDLTWSSYVADIVVDPDYQGRGFGNQLMDEILE 93
Cdd:cd04301    1 FLVAEDDGEIVGFAslSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEE 52
Eis COG4552
Predicted acetyltransferase [General function prediction only];
13-95 4.25e-06

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 44.89  E-value: 4.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742381234  13 DWQALATLIERAGLGARDPHEVER---CYRNSTFcwYG-FHEGKLVATAHAIS-DLTW------SSYVADIVVDPDYQGR 81
Cdd:COG4552   10 DLDAFARLLAYAFGPEPDDEELEAyrpLLEPGRV--LGvFDDGELVGTLALYPfTLNVggarvpMAGITGVAVAPEHRRR 87

                         90
                 ....*....|....
gi 742381234  82 GFGNQLMDEILETL 95
Cdd:COG4552   88 GVARALLREALAEL 101
PTZ00330 PTZ00330
acetyltransferase; Provisional
 68-125 6.76e-06

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 42.91  E-value: 6.76e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 742381234  68 YVADIVVDPDYQGRGFGNQLMDEILETLLPFG--KVFIYAVLDKVAFYKKYQFRELTSGM 125
Cdd:PTZ00330  84 HIEDVVVDPSYRGQGLGRALISDLCEIARSSGcyKVILDCTEDMVAFYKKLGFRACERQM 143
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 49-121 2.71e-05

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 41.19  E-value: 2.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742381234  49 HEGKLV--ATAHAISDltWSSYVADIVVDPDYQGRGFGNQLMDEILETLLPFG----KVFIYAVLDK-VAFYKKYQFREL 121
Cdd:COG0454   41 DKGEPIgfAGLRRLDD--KVLELKRLYVLPEYRGKGIGKALLEALLEWARERGctalELDTLDGNPAaIRFYERLGFKEI 118
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
52-120 5.73e-05

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 39.51  E-value: 5.73e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 742381234  52 KLVATAHAISDLTWSSYVADIVVDPDYQGRGFGNQLMDEILETLLPFGK--VFIYAVLDK---VAFYKKYQFRE 120
Cdd:COG3393    1 ELVAMAGVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGArtPFLYVDADNpaaRRLYERLGFRP 74
PRK03624 PRK03624
putative acetyltransferase; Provisional
 13-89 9.43e-05

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 39.91  E-value: 9.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742381234  13 DWQALATLIERAGL--GARDPH---EVERCYRNSTFcWYGFHEGKLVATAHAISD--LTWSSYVAdivVDPDYQGRGFGN 85
Cdd:PRK03624  12 DFEAVIALWERCDLtrPWNDPEmdiERKLNHDPSLF-LVAEVGGEVVGTVMGGYDghRGWAYYLA---VHPDFRGRGIGR 87


                 ....
gi 742381234  86 QLMD 89
Cdd:PRK03624  88 ALVA 91
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 72-95 7.99e-04

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 37.22  E-value: 7.99e-04
                         10        20
                 ....*....|....*....|....
gi 742381234  72 IVVDPDYQGRGFGNQLMDEILETL 95
Cdd:PRK09491  69 IAVDPDYQRQGLGRALLEHLIDEL 92
Citrate_lyase_ligase cd02169
Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is ...
 72-134 3.59e-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: 3.59e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742381234  72 IVVDPDYQGRGFGNQLMDEILETLLPFGK--VFIYAVLDKVAFYKKYQFRELtsgmVCATDEKLF 134
Cdd:cd02169   31 VAVCPKYQGEGLALKIVSELINKAYEEGIfhLFLFTKPKNAKFFRGLGFKEL----ANASDEAVL 91
 
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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