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Conserved domains on  [gi|2787363762|ref|WP_370450811|]
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MULTISPECIES: GNAT family N-acetyltransferase [Parabacteroides]

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 ...
 5-142 5.03e-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 PRK10514:

Pssm-ID: 473072 [Multi-domain]  Cd Length: 145  Bit Score: 128.97  E-value: 5.03e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787363762   5 ITRPSFEDFNELLLLWEASVRSTHHFLKEEDILFYKELVPGYFPLVELYIIRNERGKIAAFMGLSDELIEMLFVHPEEQG 84
Cdd:PRK10514    4 IRRSRHEEGERLVAIWRRSVDATHDFLSAEDRAEIEELVRSFLPEAPLWVAVDERDQPVGFMLLSGGHMEALFVDPDVRG 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2787363762  85 KGLGKRLIQFALQETPIRKVDVNEQNTTALHFYQHLGFQVIGRDETDSSHKPFPILHL 142
Cdd:PRK10514   84 CGVGRMLVEHALSLHPELTTDVNEQNEQAVGFYKKMGFKVTGRSEVDDQGRPYPLLHL 141
 
Name Accession Description Interval E-value
PRK10514 PRK10514
putative acetyltransferase; Provisional
 5-142 5.03e-39

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 128.97  E-value: 5.03e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787363762   5 ITRPSFEDFNELLLLWEASVRSTHHFLKEEDILFYKELVPGYFPLVELYIIRNERGKIAAFMGLSDELIEMLFVHPEEQG 84
Cdd:PRK10514    4 IRRSRHEEGERLVAIWRRSVDATHDFLSAEDRAEIEELVRSFLPEAPLWVAVDERDQPVGFMLLSGGHMEALFVDPDVRG 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2787363762  85 KGLGKRLIQFALQETPIRKVDVNEQNTTALHFYQHLGFQVIGRDETDSSHKPFPILHL 142
Cdd:PRK10514   84 CGVGRMLVEHALSLHPELTTDVNEQNEQAVGFYKKMGFKVTGRSEVDDQGRPYPLLHL 141
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 51-127 6.14e-16

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 69.31  E-value: 6.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787363762  51 ELYIIRNERGKIAAFMGLS----DEL-IEMLFVHPEEQGKGLGKRLIQFALQE------TPIRkVDVNEQNTTALHFYQH 119
Cdd:COG0454    34 AEFIAVDDKGEPIGFAGLRrlddKVLeLKRLYVLPEYRGKGIGKALLEALLEWarergcTALE-LDTLDGNPAAIRFYER 112


                  ....*...
gi 2787363762 120 LGFQVIGR 127
Cdd:COG0454   113 LGFKEIER 120
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 24-127 5.96e-13

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: 61.52  E-value: 5.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787363762  24 VRSTHHFLKEEDIlfYKELVPGYFPLVELYiirnERGKIAAFMGLSDEL-IEMLFVHPEEQGKGLGKRLIQFALQETP-- 100
Cdd:pfam13673  10 IETFYEFISPEAL--RERIDQGEYFFFVAF----EGGQIVGVIALRDRGhISLLFVDPDYQGQGIGKALLEAVEDYAEkd 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 2787363762 101 ---IRKVDVNEQNtTALHFYQHLGFQVIGR 127
Cdd:pfam13673  84 gikLSELTVNASP-YAVPFYEKLGFRATGP 112
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 52-98 2.26e-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: 45.34  E-value: 2.26e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2787363762  52 LYIIRNErGKIAAFMGLSDE-------LIEMLFVHPEEQGKGLGKRLIQFALQE 98
Cdd:cd04301     1 FLVAEDD-GEIVGFASLSPDgsggdtaYIGDLAVLPEYRGKGIGSALLEAAEEE 53
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 53-127 6.75e-06

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: 42.70  E-value: 6.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787363762  53 YIIRNERGKIAAFMGLSDELIEM----LFVHPEEQGKGLGKRLIQFALQETPIRKV-----DVNEQNTTALHFYQHLGFQ 123
Cdd:TIGR01575  33 YLLARIGGKVVGYAGVQIVLDEAhilnIAVKPEYQGQGIGRALLRELIDEAKGRGVneiflEVRVSNIAAQALYKKLGFN 112


                  ....
gi 2787363762 124 VIGR 127
Cdd:TIGR01575 113 EIAI 116
 
Name Accession Description Interval E-value
PRK10514 PRK10514
putative acetyltransferase; Provisional
 5-142 5.03e-39

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 128.97  E-value: 5.03e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787363762   5 ITRPSFEDFNELLLLWEASVRSTHHFLKEEDILFYKELVPGYFPLVELYIIRNERGKIAAFMGLSDELIEMLFVHPEEQG 84
Cdd:PRK10514    4 IRRSRHEEGERLVAIWRRSVDATHDFLSAEDRAEIEELVRSFLPEAPLWVAVDERDQPVGFMLLSGGHMEALFVDPDVRG 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2787363762  85 KGLGKRLIQFALQETPIRKVDVNEQNTTALHFYQHLGFQVIGRDETDSSHKPFPILHL 142
Cdd:PRK10514   84 CGVGRMLVEHALSLHPELTTDVNEQNEQAVGFYKKMGFKVTGRSEVDDQGRPYPLLHL 141
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 51-127 6.14e-16

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 69.31  E-value: 6.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787363762  51 ELYIIRNERGKIAAFMGLS----DEL-IEMLFVHPEEQGKGLGKRLIQFALQE------TPIRkVDVNEQNTTALHFYQH 119
Cdd:COG0454    34 AEFIAVDDKGEPIGFAGLRrlddKVLeLKRLYVLPEYRGKGIGKALLEALLEWarergcTALE-LDTLDGNPAAIRFYER 112


                  ....*...
gi 2787363762 120 LGFQVIGR 127
Cdd:COG0454   113 LGFKEIER 120
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 73-130 1.24e-15

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 67.37  E-value: 1.24e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2787363762  73 IEMLFVHPEEQGKGLGKRLIQFALQETPIRKV-----DVNEQNTTALHFYQHLGFQVIGRDET 130
Cdd:COG0456    16 IEDLAVDPEYRGRGIGRALLEAALERARERGArrlrlEVREDNEAAIALYEKLGFEEVGERPN 78
PRK10562 PRK10562
putative acetyltransferase; Provisional
 11-144 4.19e-15

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 67.40  E-value: 4.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787363762  11 EDFNELLLLWEASVRSTHHFLKEEdilFYKELVP----GYFPLVELYIIRnERGKIAAFMG-LSDELIEMLFVHPEEQGK 85
Cdd:PRK10562    8 SDLPAILQLWLESTIWAHPFIKEQ---YWRESAPlvrdVYLPAAQTWVWE-EDGKLLGFVSvLEGRFVGALFVAPKAVRR 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2787363762  86 GLGKRLIQFALQETPIRKVDVNEQNTTALHFYQHLGFQVIGRDETDSSHKPFPILHLQV 144
Cdd:PRK10562   84 GIGKALMQHVQQRYPHLSLEVYQKNQRAVNFYHAQGFRIVDSAWQEETQHPTWIMSWQA 142
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 24-127 5.96e-13

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: 61.52  E-value: 5.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787363762  24 VRSTHHFLKEEDIlfYKELVPGYFPLVELYiirnERGKIAAFMGLSDEL-IEMLFVHPEEQGKGLGKRLIQFALQETP-- 100
Cdd:pfam13673  10 IETFYEFISPEAL--RERIDQGEYFFFVAF----EGGQIVGVIALRDRGhISLLFVDPDYQGQGIGKALLEAVEDYAEkd 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 2787363762 101 ---IRKVDVNEQNtTALHFYQHLGFQVIGR 127
Cdd:pfam13673  84 gikLSELTVNASP-YAVPFYEKLGFRATGP 112
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 51-124 3.52e-12

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 58.23  E-value: 3.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787363762  51 ELYIIRNErGKIAAFMGLS------DELIEMLFVHPEEQGKGLGKRLIQF---ALQETPIRKVDVNEQNtTALHFYQHLG 121
Cdd:pfam13508   4 RFFVAEDD-GKIVGFAALLplddegALAELRLAVHPEYRGQGIGRALLEAaeaAAKEGGIKLLELETTN-RAAAFYEKLG 81


                  ...
gi 2787363762 122 FQV 124
Cdd:pfam13508  82 FEE 84
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
11-129 1.06e-11

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 58.85  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787363762  11 EDFNELLLLWEASVRSTH-------HFLKEEDILFYKELVPGYFPLV-ElyiirnERGKIAAFMGLSDE---------LI 73
Cdd:COG1247    10 EDAPAIAAIYNEAIAEGTatfetepPSEEEREAWFAAILAPGRPVLVaE------EDGEVVGFASLGPFrprpayrgtAE 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2787363762  74 EMLFVHPEEQGKGLGKRLIQFALQETP---IRKV--DVNEQNTTALHFYQHLGFQVIGRDE 129
Cdd:COG1247    84 ESIYVDPDARGRGIGRALLEALIERARargYRRLvaVVLADNEASIALYEKLGFEEVGTLP 144
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 32-129 1.32e-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: 58.08  E-value: 1.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787363762  32 KEEDILFYKELVPGYF---PLVELYIIRNErGKIAAFMGLSDE-----LIEMLFVHPEEQGKGLGKRLIQFALQ---ETP 100
Cdd:COG1246     7 TPDDVPAILELIRPYAleeEIGEFWVAEED-GEIVGCAALHPLdedlaELRSLAVHPDYRGRGIGRRLLEALLAearELG 85

                          90       100
                  ....*....|....*....|....*....
gi 2787363762 101 IRKVDVnEQNTTALHFYQHLGFQVIGRDE 129
Cdd:COG1246    86 LKRLFL-LTTSAAIHFYEKLGFEEIDKED 113
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
61-127 6.24e-11

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 55.30  E-value: 6.24e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2787363762  61 KIAAFMGLSDEL-----IEMLFVHPEEQGKGLGKRLIQFALQE-------TPIrkVDVNEQNTTALHFYQHLGFQVIGR 127
Cdd:COG3393     1 ELVAMAGVRAESpgvaeISGVYTHPEYRGRGLASALVAALAREalargarTPF--LYVDADNPAARRLYERLGFRPVGE 77
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 51-122 8.57e-11

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: 55.60  E-value: 8.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787363762  51 ELYIIRNERGKIAAFMGLSDEL-------IEMLFVHPEEQGKGLGKRLIQFALQ---ETPIRKV--DVNEQNTTALHFYQ 118
Cdd:pfam00583  33 EGFFVAEEDGELVGFASLSIIDdeppvgeIEGLAVAPEYRGKGIGTALLQALLEwarERGCERIflEVAADNLAAIALYE 112


                  ....
gi 2787363762 119 HLGF 122
Cdd:pfam00583 113 KLGF 116
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
73-126 5.95e-10

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 53.65  E-value: 5.95e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2787363762  73 IEMLFVHPEEQGKGLGKRLIQFAL---QETPIRKVDVNEQnTTALHFYQHLGFQVIG 126
Cdd:COG2153    61 IGRVAVLPEYRGQGLGRALMEAAIeeaRERGARRIVLSAQ-AHAVGFYEKLGFVPVG 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
60-127 8.10e-10

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 53.55  E-value: 8.10e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2787363762  60 GKIAAFMGLSDE---------LIEMLFVHPEEQGKGLGKRLIQFALQETPIRKVD--VNEQNTTALHFYQHLGFQVIGR 127
Cdd:COG3153    48 GEIVGHVALSPVdidgegpalLLGPLAVDPEYRGQGIGRALMRAALEAARERGARavVLLGDPSLLPFYERFGFRPAGE 126
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 52-98 2.26e-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: 45.34  E-value: 2.26e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2787363762  52 LYIIRNErGKIAAFMGLSDE-------LIEMLFVHPEEQGKGLGKRLIQFALQE 98
Cdd:cd04301     1 FLVAEDD-GEIVGFASLSPDgsggdtaYIGDLAVLPEYRGKGIGSALLEAAEEE 53
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 11-127 1.53e-06

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: 45.38  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787363762  11 EDFNELLLLWEASVRSTHHFLKEEDILFYKelvPGYFPLVelyIIRNERGKIAAFMGLSDELIEM------LFVHPEEQG 84
Cdd:COG1670    28 PEVARYLPGPPYSLEEARAWLERLLADWAD---GGALPFA---IEDKEDGELIGVVGLYDIDRANrsaeigYWLAPAYWG 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2787363762  85 KGLGKR----LIQFALQETPIRKV--DVNEQNTTALHFYQHLGFQVIGR 127
Cdd:COG1670   102 KGYATEalraLLDYAFEELGLHRVeaEVDPDNTASIRVLEKLGFRLEGT 150
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 53-127 6.75e-06

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: 42.70  E-value: 6.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787363762  53 YIIRNERGKIAAFMGLSDELIEM----LFVHPEEQGKGLGKRLIQFALQETPIRKV-----DVNEQNTTALHFYQHLGFQ 123
Cdd:TIGR01575  33 YLLARIGGKVVGYAGVQIVLDEAhilnIAVKPEYQGQGIGRALLRELIDEAKGRGVneiflEVRVSNIAAQALYKKLGFN 112


                  ....
gi 2787363762 124 VIGR 127
Cdd:TIGR01575 113 EIAI 116
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 76-122 1.08e-05

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 42.61  E-value: 1.08e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2787363762  76 LF---VHPEEQGKGLGKRLIQFALQETPIRKV-----DVNEQNTTALHFYQHLGF 122
Cdd:PRK09491   66 LFniaVDPDYQRQGLGRALLEHLIDELEKRGVatlwlEVRASNAAAIALYESLGF 120
PRK03624 PRK03624
putative acetyltransferase; Provisional
 76-124 2.16e-05

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 41.45  E-value: 2.16e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2787363762  76 LFVHPEEQGKGLGKRLIQFA---LQETPIRKVD--VNEQNTTALHFYQHLGFQV 124
Cdd:PRK03624   74 LAVHPDFRGRGIGRALVARLekkLIARGCPKINlqVREDNDAVLGFYEALGYEE 127
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 54-125 3.96e-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: 40.01  E-value: 3.96e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2787363762  54 IIRNERGKIAAFM-GLSDELIEMLFVHPEEQGKGLGKRLIQfALQETPIRK-----VDVNEQNTTALHFYQHLGFQVI 125
Cdd:pfam08445   4 IYRGDTGELAAWClRLPGGELGALQTLPEHRRRGLGSRLVA-ALARGIAERgitpfAVVVAGNTPSRRLYEKLGFRKI 80
TmcA COG1444
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
 78-125 1.07e-04

tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA(Met) C34 N-acetyltransferase TmcA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441053 [Multi-domain]  Cd Length: 703  Bit Score: 40.97  E-value: 1.07e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2787363762  78 VHPEEQGKGLGKRLIQFALQETPIRKVD-------VNEQnttALHFYQHLGFQVI 125
Cdd:COG1444   493 VHPALQRRGLGSRLLAEIREEAKEEGLDwlgvsfgATPE---LLRFWQRNGFVPV 544
PRK07757 PRK07757
N-acetyltransferase;
48-129 1.71e-04

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 39.41  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787363762  48 PLVELY-IIRN-----ERGKIAAFMGL---SDELIEM--LFVHPEEQGKGLGKRLIQFALQETpiRKVDVNEQNTTAL-- 114
Cdd:PRK07757   32 SLDELYeNIRDfyvaeEEGEIVGCCALhilWEDLAEIrsLAVSEDYRGQGIGRMLVEACLEEA--RELGVKRVFALTYqp 109

                          90
                  ....*....|....*
gi 2787363762 115 HFYQHLGFQVIGRDE 129
Cdd:PRK07757  110 EFFEKLGFREVDKEA 124
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
54-124 3.98e-04

dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;


Pssm-ID: 182877  Cd Length: 194  Bit Score: 38.76  E-value: 3.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787363762  54 IIRNERGKIAAFMGL-----SDELIEMLFVHPEEQGKGLGKRLIQFAL---QETPIRKVDVNEQ--NTTALHFYQHLGFQ 123
Cdd:PRK10975  105 LLRDASGQIQGFVTLrelndTDARIGLLAVFPGAQGRGIGARLMQAALnwcQARGLTRLRVATQmgNLAALRLYIRSGAN 184


                  .
gi 2787363762 124 V 124
Cdd:PRK10975  185 I 185
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
 53-99 6.62e-04

GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both CoA and acetyl-CoA. They are characterized by highly conserved glycine, a cysteine residue in the acetyl-CoA binding site near the acetyl group, their small size compared with other GNATs and a lack of of an obvious substrate-binding site. It is proposed that they transfer an acetyl group from acetyl-CoA to one or more unidentified aliphatic amines via an acetyl (cysteine) enzyme intermediate. The substrate might be another macromolecule.


Pssm-ID: 434030 [Multi-domain]  Cd Length: 79  Bit Score: 36.34  E-value: 6.62e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2787363762  53 YIIRNERGKIAAFMGLSDELIEMLFVH----PEEQGKGLGKRLIQFALQET 99
Cdd:pfam14542   2 FEIRVDGGAEVAFLTYRRGDGVLIITHtevpPALRGQGIASKLVKAALDDA 52
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
4-98 2.27e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 36.43  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787363762   4 AITRPSFEDFNELLLLWEASVRSTHhfLKEEdilfykeLVPGYFplvelYIIRNERGKIAAFMGLSDELIEMLF------ 77
Cdd:COG3981    30 SGYLVSFEDFEAWLERLLDEEKGEE--LPEG-------WVPATT-----YWLVDEDGRIVGAINLRHELNEFLLrvgghi 95

                          90       100
                  ....*....|....*....|....
gi 2787363762  78 ---VHPEEQGKGLGKRLIQFALQE 98
Cdd:COG3981    96 gygVRPSERGKGYATEMLRLALEE 119
PRK09831 PRK09831
GNAT family N-acetyltransferase;
73-125 4.94e-03

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 35.32  E-value: 4.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2787363762  73 IEMLFVHPEEQGKGLGKRLIQFALQETPIRKVDVneqNTTALHFYQHLGFQVI 125
Cdd:PRK09831   75 IDMLFVDPEYTRRGVASALLKPLIKSESELTVDA---SITAKPFFERYGFQTV 124
 
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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