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Conserved domains on  [gi|446328145|ref|WP_000406000|]
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MULTISPECIES: GNAT family acetyltransferase [Enterobacteriaceae]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11480005)

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

EC:  2.3.1.-
Gene Ontology:  GO:0008080
PubMed:  10940244

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK03624 PRK03624
putative acetyltransferase; Provisional
 1-138 4.40e-94

putative acetyltransferase; Provisional


:

Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 267.56  E-value: 4.40e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328145   1 MEIRVFRQEDFEEVITLWERCDLLRPWNDPEMDIERKMNHDVSLFLVAEVNGEVVGTVMGGYDGHRGSAYYLGVHPEFRG 80
Cdd:PRK03624   3 MEIRVFRQADFEAVIALWERCDLTRPWNDPEMDIERKLNHDPSLFLVAEVGGEVVGTVMGGYDGHRGWAYYLAVHPDFRG 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446328145  81 RGIANALLNRLEKKLIARGCPKIQINVPEDNDMVLGMYERLGYEHADVLSLGKRLIED 138
Cdd:PRK03624  83 RGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQDRISLGKRLIED 140
 
Name Accession Description Interval E-value
PRK03624 PRK03624
putative acetyltransferase; Provisional
 1-138 4.40e-94

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 267.56  E-value: 4.40e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328145   1 MEIRVFRQEDFEEVITLWERCDLLRPWNDPEMDIERKMNHDVSLFLVAEVNGEVVGTVMGGYDGHRGSAYYLGVHPEFRG 80
Cdd:PRK03624   3 MEIRVFRQADFEAVIALWERCDLTRPWNDPEMDIERKLNHDPSLFLVAEVGGEVVGTVMGGYDGHRGWAYYLAVHPDFRG 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446328145  81 RGIANALLNRLEKKLIARGCPKIQINVPEDNDMVLGMYERLGYEHADVLSLGKRLIED 138
Cdd:PRK03624  83 RGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQDRISLGKRLIED 140
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-129 1.01e-20

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 82.35  E-value: 1.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328145   1 MEIRVFRQEDFEEVITLWERCDLLRP--WNDPEMDIE------RKMNHDVSLFLVAEVNGEVVGTVMGG----YDGHRGS 68
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAIAEGTatFETEPPSEEereawfAAILAPGRPVLVAEEDGEVVGFASLGpfrpRPAYRGT 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446328145  69 AYY-LGVHPEFRGRGIANALLNRLEKKLIARGCPKIQINVPEDNDMVLGMYERLGYEHADVL 129
Cdd:COG1247   82 AEEsIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTL 143
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 18-123 2.06e-20

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: 80.25  E-value: 2.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328145   18 WERCDLLRPWNDPEMDIERKMNHDVS-LFLVAEVNGEVVGTVMGGYDGHRGSAYYLG---VHPEFRGRGIANALLNRLEK 93
Cdd:pfam00583   7 LLSEEFPEPWPDEPLDLLEDWDEDASeGFFVAEEDGELVGFASLSIIDDEPPVGEIEglaVAPEYRGKGIGTALLQALLE 86

                          90       100       110
                  ....*....|....*....|....*....|
gi 446328145   94 KLIARGCPKIQINVPEDNDMVLGMYERLGY 123
Cdd:pfam00583  87 WARERGCERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 26-130 1.06e-14

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: 65.81  E-value: 1.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328145   26 PWNdpEMDIERKMNHDVSLFLVAEVNGEVVGTVMGGYDGHRGSAYYLGVHPEFRGRGIANALLNRLEKKLIARGCPKIQI 105
Cdd:TIGR01575  16 PWT--EAQFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFL 93

                          90       100
                  ....*....|....*....|....*
gi 446328145  106 NVPEDNDMVLGMYERLGYEHADVLS 130
Cdd:TIGR01575  94 EVRVSNIAAQALYKKLGFNEIAIRR 118
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 45-106 1.05e-12

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: 58.83  E-value: 1.05e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446328145  45 FLVAEVNGEVVGTVMGGYDGHRGSAYY---LGVHPEFRGRGIANALLNRLEKKLIARGCPKIQIN 106
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDTAYigdLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
 
Name Accession Description Interval E-value
PRK03624 PRK03624
putative acetyltransferase; Provisional
 1-138 4.40e-94

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 267.56  E-value: 4.40e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328145   1 MEIRVFRQEDFEEVITLWERCDLLRPWNDPEMDIERKMNHDVSLFLVAEVNGEVVGTVMGGYDGHRGSAYYLGVHPEFRG 80
Cdd:PRK03624   3 MEIRVFRQADFEAVIALWERCDLTRPWNDPEMDIERKLNHDPSLFLVAEVGGEVVGTVMGGYDGHRGWAYYLAVHPDFRG 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446328145  81 RGIANALLNRLEKKLIARGCPKIQINVPEDNDMVLGMYERLGYEHADVLSLGKRLIED 138
Cdd:PRK03624  83 RGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQDRISLGKRLIED 140
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-129 1.01e-20

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 82.35  E-value: 1.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328145   1 MEIRVFRQEDFEEVITLWERCDLLRP--WNDPEMDIE------RKMNHDVSLFLVAEVNGEVVGTVMGG----YDGHRGS 68
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAIAEGTatFETEPPSEEereawfAAILAPGRPVLVAEEDGEVVGFASLGpfrpRPAYRGT 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446328145  69 AYY-LGVHPEFRGRGIANALLNRLEKKLIARGCPKIQINVPEDNDMVLGMYERLGYEHADVL 129
Cdd:COG1247   82 AEEsIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTL 143
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 18-123 2.06e-20

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: 80.25  E-value: 2.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328145   18 WERCDLLRPWNDPEMDIERKMNHDVS-LFLVAEVNGEVVGTVMGGYDGHRGSAYYLG---VHPEFRGRGIANALLNRLEK 93
Cdd:pfam00583   7 LLSEEFPEPWPDEPLDLLEDWDEDASeGFFVAEEDGELVGFASLSIIDDEPPVGEIEglaVAPEYRGKGIGTALLQALLE 86

                          90       100       110
                  ....*....|....*....|....*....|
gi 446328145   94 KLIARGCPKIQINVPEDNDMVLGMYERLGY 123
Cdd:pfam00583  87 WARERGCERIFLEVAADNLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-127 5.24e-20

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 79.74  E-value: 5.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328145   3 IRVFRQEDFEEVITLWERCdllrpWNDP-EMDIERKMNHD--VSLFLVAEVNGEVVGTVMG--GYDGHRGSAYYLG---V 74
Cdd:COG3153    1 IRPATPEDAEAIAALLRAA-----FGPGrEAELVDRLREDpaAGLSLVAEDDGEIVGHVALspVDIDGEGPALLLGplaV 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446328145  75 HPEFRGRGIANALLNRLEKKLIARGCPKIQINVPEDNdmvLGMYERLGYEHAD 127
Cdd:COG3153   76 DPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSL---LPFYERFGFRPAG 125
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 1-131 1.20e-16

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: 70.79  E-value: 1.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328145   1 MEIRVFRQEDFEEVITLWERCDLLRPWNDpemdierkmnhdvslFLVAEVNGEVVGTvmGGYDGHRGSAYYLG---VHPE 77
Cdd:COG1246    1 MTIRPATPDDVPAILELIRPYALEEEIGE---------------FWVAEEDGEIVGC--AALHPLDEDLAELRslaVHPD 63

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446328145  78 FRGRGIANALLNRLEKKLIARGCPKIQINVpedNDMVLGMYERLGYEHADVLSL 131
Cdd:COG1246   64 YRGRGIGRRLLEALLAEARELGLKRLFLLT---TSAAIHFYEKLGFEEIDKEDL 114
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 56-128 1.54e-16

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 69.68  E-value: 1.54e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446328145  56 GTVMGGYDGHRGSAY--YLGVHPEFRGRGIANALLNRLEKKLIARGCPKIQINVPEDNDMVLGMYERLGYEHADV 128
Cdd:COG0456    1 GFALLGLVDGGDEAEieDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGE 75
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 43-124 2.08e-15

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 66.32  E-value: 2.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328145   43 SLFLVAEVNGEVVGTVMGGYDGHRGSAYYLG--VHPEFRGRGIANALLNRLEKKLIARGCPKIQINVPEDNdmvLGMYER 120
Cdd:pfam13508   3 GRFFVAEDDGKIVGFAALLPLDDEGALAELRlaVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRA---AAFYEK 79


                  ....
gi 446328145  121 LGYE 124
Cdd:pfam13508  80 LGFE 83
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 26-130 1.06e-14

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: 65.81  E-value: 1.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328145   26 PWNdpEMDIERKMNHDVSLFLVAEVNGEVVGTVMGGYDGHRGSAYYLGVHPEFRGRGIANALLNRLEKKLIARGCPKIQI 105
Cdd:TIGR01575  16 PWT--EAQFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFL 93

                          90       100
                  ....*....|....*....|....*
gi 446328145  106 NVPEDNDMVLGMYERLGYEHADVLS 130
Cdd:TIGR01575  94 EVRVSNIAAQALYKKLGFNEIAIRR 118
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
53-125 6.92e-14

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 62.62  E-value: 6.92e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446328145  53 EVVGtvMGGYDGHRGSAYYLG---VHPEFRGRGIANALLNRLEKKLIARGCPKIQINVPEDNDMVLGMYERLGYEH 125
Cdd:COG3393    1 ELVA--MAGVRAESPGVAEISgvyTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRP 74
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 45-106 1.05e-12

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: 58.83  E-value: 1.05e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446328145  45 FLVAEVNGEVVGTVMGGYDGHRGSAYY---LGVHPEFRGRGIANALLNRLEKKLIARGCPKIQIN 106
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDTAYigdLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 41-127 3.04e-11

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 56.99  E-value: 3.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328145  41 DVSLFLVAEVNGEVVGTV-MGGYDGHRGSAYYLGVHPEFRGRGIANALLNRLEKKLIARGCPKIQINVPEDNDMVLGMYE 119
Cdd:COG0454   32 AGAEFIAVDDKGEPIGFAgLRRLDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYE 111


                 ....*...
gi 446328145 120 RLGYEHAD 127
Cdd:COG0454  112 RLGFKEIE 119
Eis COG4552
Predicted acetyltransferase [General function prediction only];
1-126 8.85e-11

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 57.99  E-value: 8.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328145   1 MEIRVFRQEDFEEVITLWERCdLLRPWNDPEMDIERKMNHDVSlFLVAEVNGEVVGTvMGGYDGH---RGSAY------Y 71
Cdd:COG4552    1 MEIRPLTEDDLDAFARLLAYA-FGPEPDDEELEAYRPLLEPGR-VLGVFDDGELVGT-LALYPFTlnvGGARVpmagitG 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446328145  72 LGVHPEFRGRGIANALLNRLEKKLIARGCPkiqinvpedndMVL------GMYERLGYEHA 126
Cdd:COG4552   78 VAVAPEHRRRGVARALLREALAELRERGQP-----------LSAlypfepGFYRRFGYELA 127
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
41-124 9.64e-10

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 52.88  E-value: 9.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328145  41 DVSLFLVAEVNGEVVGTV----MGGYDGHrgsayyLG---VHPEFRGRGIANALLNRLEKKLIARGCPKIQINVPEDndm 113
Cdd:COG2153   32 EDARHLLAYDDGELVATArllpPGDGEAK------IGrvaVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH--- 102

                         90
                 ....*....|.
gi 446328145 114 VLGMYERLGYE 124
Cdd:COG2153  103 AVGFYEKLGFV 113
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 34-124 7.58e-09

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: 50.35  E-value: 7.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328145   34 IERKMNHDVSLFLVAEVNGEVVGTVMGGYDGHrgsAYYLGVHPEFRGRGIANALLNRLEKKLIARGCPKIQINVPEDNDM 113
Cdd:pfam13673  22 LRERIDQGEYFFFVAFEGGQIVGVIALRDRGH---ISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNASPYA 98

                          90
                  ....*....|.
gi 446328145  114 VlGMYERLGYE 124
Cdd:pfam13673  99 V-PFYEKLGFR 108
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-129 2.02e-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: 50.38  E-value: 2.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328145   1 MEIRVFRQEDFEEVITLWERCDLLRPWNDPEMDIE------------RKMNHDVSLFLVAEVNGEVVGTV-MGGYDGHRG 67
Cdd:COG1670    8 LRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEearawlerlladWADGGALPFAIEDKEDGELIGVVgLYDIDRANR 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446328145  68 SAYY-LGVHPEFRGRGIANALLNRLEKKLIAR-GCPKIQINVPEDNDMVLGMYERLGYEHADVL 129
Cdd:COG1670   88 SAEIgYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGFRLEGTL 151
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 3-125 3.34e-08

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 48.72  E-value: 3.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328145    3 IRVFRQEDFEEVITLWERCDLLRPwnDPEMDIERKMNHDVSLFLVAEVNGEVVGTVMGgYD------GHRGSAYYLG--- 73
Cdd:pfam13527   1 IRPLTEDEFDEVLRLLEYAFQDED--SPELREYFRPLLEEGRVLGAFDDGELVSTLAL-YPfelnvpGKTLPAAGITgva 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446328145   74 VHPEFRGRGIANALLNRLEKKLIARGCPkIQINVPEDndmvLGMYERLGYEH 125
Cdd:pfam13527  78 TYPEYRGRGVMSRLLRRSLEEMRERGVP-LSFLYPSS----YPIYRRFGYEI 124
PRK12308 PRK12308
argininosuccinate lyase;
22-140 1.52e-05

argininosuccinate lyase;


Pssm-ID: 183425 [Multi-domain]  Cd Length: 614  Bit Score: 43.23  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328145  22 DLLRPWNDPEMDIERKMN---HDVSLFLVAEVNGEVVGTV-MGGYDGHRGSAYYLGVHPEFRGRGIANALLNRLEKKliA 97
Cdd:PRK12308 479 GMVAYWAGLGENLPRSRNelvRDIGSFAVAEHHGEVTGCAsLYIYDSGLAEIRSLGVEAGWQVQGQGSALVQYLVEK--A 556

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446328145  98 RgcpKIQIN-------VPEdndmvlgMYERLGYEHADVLSLGKRLIEDEE 140
Cdd:PRK12308 557 R---QMAIKkvfvltrVPE-------FFMKQGFSPTSKSLLPEKVLKDCD 596
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 74-128 1.89e-05

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 41.84  E-value: 1.89e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446328145  74 VHPEFRGRGIANALLNRLEKKLIARGCPKIQINVPEDNDMVLGMYERLGYEHADV 128
Cdd:PRK09491  71 VDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTI 125
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 67-128 4.07e-05

FR47-like protein; The members of this family are similar to the C-terminal region of the D. melanogaster hypothetical protein FR47. This protein has been found to consist of two N-acyltransferase-like domains swapped with the C-terminal strands.


Pssm-ID: 117022 [Multi-domain]  Cd Length: 86  Bit Score: 39.62  E-value: 4.07e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446328145   67 GSAYYLGVHPEFRGRGIANALLNRLEKKLIARGcpkIQINVP--EDNDMVLGMYERLGYEHADV 128
Cdd:pfam08445  22 GELGALQTLPEHRRRGLGSRLVAALARGIAERG---ITPFAVvvAGNTPSRRLYEKLGFRKIDE 82
Acetyltransf_6 pfam13480
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 45-100 1.06e-04

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


Pssm-ID: 433244 [Multi-domain]  Cd Length: 143  Bit Score: 39.57  E-value: 1.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446328145   45 FLVAEVNGEVVGTVMGGYDGHRGSAYYLGVHPEFRGRGIANALLNRLEKKLIARGC 100
Cdd:pfam13480  74 LYVLRLDGRPVAALLGLRSGDRLYYWFGGYDPEYARLSPGLLLLWELIEHAAEEGL 129
COG3375 COG3375
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
33-87 1.13e-04

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


Pssm-ID: 442602 [Multi-domain]  Cd Length: 271  Bit Score: 40.31  E-value: 1.13e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446328145  33 DIERKMNHDVSLFLVAEVNGEVVGTVMG--GYDGHRGSAY--YLGVHPEFRGRGIANAL 87
Cdd:COG3375   38 HLLRALAHAGGYVLGAFDGGELVGFSFGfpGFRPGGLYLHshMAGVLPEYRGRGVGYAL 96
PRK10514 PRK10514
putative acetyltransferase; Provisional
 2-125 2.43e-04

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 38.83  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446328145   2 EIRVFRQEDFEEVITLWERC-----DLLRPWNDPEMDIE-RKMNHDVSLFLVAEVNGEVVGtVMGGYDGHRGSayyLGVH 75
Cdd:PRK10514   3 SIRRSRHEEGERLVAIWRRSvdathDFLSAEDRAEIEELvRSFLPEAPLWVAVDERDQPVG-FMLLSGGHMEA---LFVD 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446328145  76 PEFRGRGIANALLnRLEKKLIargcPKIQINVPEDNDMVLGMYERLGYEH 125
Cdd:PRK10514  79 PDVRGCGVGRMLV-EHALSLH----PELTTDVNEQNEQAVGFYKKMGFKV 123
PTZ00330 PTZ00330
acetyltransferase; Provisional
 74-124 4.60e-04

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 37.90  E-value: 4.60e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446328145  74 VHPEFRGRGIANALLNRLEKKLIARGCPKIQINVPEDndmVLGMYERLGYE 124
Cdd:PTZ00330  90 VDPSYRGQGLGRALISDLCEIARSSGCYKVILDCTED---MVAFYKKLGFR 137
 
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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