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Conserved domains on  [gi|1520954928|gb|RPN81787|]
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ribosomal-protein-alanine acetyltransferase [Pseudomonas aeruginosa]

Protein Classification

GNAT family N-acetyltransferase/peptidase C39 family protein( domain architecture ID 11418992)

GNAT family N-acetyltransferase/peptidase C39 family protein may catalyze the transfer of an acetyl group from acetyl-CoA to a substrate and/or function as a cysteine peptidase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DUF3335 pfam11814
Peptidase_C39 like family;
159-362 2.03e-129

Peptidase_C39 like family;


:

Pssm-ID: 432095  Cd Length: 206  Bit Score: 369.20  E-value: 2.03e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928 159 VPFYRQTTDFTCGPACLLMAMGALQPERQLTRREELRLWREATTIYMTAGHGGCSPQGLALAAWRRGFRVKLVLSASGPL 238
Cdd:pfam11814   1 VPYYRQTTEFTCGPAALMMAMAALDPEYALDREEELRLWREATTIFMTSGHGGCGPHGLALAARRRGFRVEVYVNTDGPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928 239 FLDGVRNEDKKAVMRLVHEDFCEELDASGVEQKRS--TRLDIPRQLARGGQPLVLISSYRLTRSKAPHWVLVTHYDEDFV 316
Cdd:pfam11814  81 FLDSVRSEEKKEVMRLVHEDFREEAAAAGVPVHYRdlSLDDLRAALAAGAVVLVLISTYRMDGEKAPHWVLVTGADDDFV 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1520954928 317 YLHDPDVDHSQHRQPLDCQHIPVSHAEFDKMSRFGRSKLRAAVILF 362
Cdd:pfam11814 161 YIHDPDVDAELGESPLDCQYLPIPRAEFDRMSRYGRARLRAAVLIR 206
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
56-149 2.58e-23

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 92.41  E-value: 2.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928  56 GYALVLFHEGTSLARLYSIAIDPRARGIGLGQKLLEAAEQAARDNDRAYMRLEVRPDNRGAIALYERNGYRPFATVRDYY 135
Cdd:COG0456     1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80
                          90
                  ....*....|....
gi 1520954928 136 EDHseALRFEKRIR 149
Cdd:COG0456    81 GDD--ALVMEKELA 92
PLN02825 super family cl33573
amino-acid N-acetyltransferase
6-97 8.25e-03

amino-acid N-acetyltransferase


The actual alignment was detected with superfamily member PLN02825:

Pssm-ID: 215441 [Multi-domain]  Cd Length: 515  Bit Score: 38.22  E-value: 8.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928   6 RPAGTDDLSALVELENRCFDYDRLSRRNFQWMLtRAHASLTVAEGDGGVLG-YALVLFHEGTSlARLYSIAIDPRARGIG 84
Cdd:PLN02825  371 RMARVEDLAGIRQIIRPLEESGILVRRTDEELL-RALDSFVVVEREGSIIAcAALFPFFEEKC-GEVAAIAVSPECRGQG 448
                          90
                  ....*....|...
gi 1520954928  85 LGQKLLEAAEQAA 97
Cdd:PLN02825  449 QGDKLLDYIEKKA 461
 
Name Accession Description Interval E-value
DUF3335 pfam11814
Peptidase_C39 like family;
159-362 2.03e-129

Peptidase_C39 like family;


Pssm-ID: 432095  Cd Length: 206  Bit Score: 369.20  E-value: 2.03e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928 159 VPFYRQTTDFTCGPACLLMAMGALQPERQLTRREELRLWREATTIYMTAGHGGCSPQGLALAAWRRGFRVKLVLSASGPL 238
Cdd:pfam11814   1 VPYYRQTTEFTCGPAALMMAMAALDPEYALDREEELRLWREATTIFMTSGHGGCGPHGLALAARRRGFRVEVYVNTDGPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928 239 FLDGVRNEDKKAVMRLVHEDFCEELDASGVEQKRS--TRLDIPRQLARGGQPLVLISSYRLTRSKAPHWVLVTHYDEDFV 316
Cdd:pfam11814  81 FLDSVRSEEKKEVMRLVHEDFREEAAAAGVPVHYRdlSLDDLRAALAAGAVVLVLISTYRMDGEKAPHWVLVTGADDDFV 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1520954928 317 YLHDPDVDHSQHRQPLDCQHIPVSHAEFDKMSRFGRSKLRAAVILF 362
Cdd:pfam11814 161 YIHDPDVDAELGESPLDCQYLPIPRAEFDRMSRYGRARLRAAVLIR 206
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
56-149 2.58e-23

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 92.41  E-value: 2.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928  56 GYALVLFHEGTSLARLYSIAIDPRARGIGLGQKLLEAAEQAARDNDRAYMRLEVRPDNRGAIALYERNGYRPFATVRDYY 135
Cdd:COG0456     1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80
                          90
                  ....*....|....
gi 1520954928 136 EDHseALRFEKRIR 149
Cdd:COG0456    81 GDD--ALVMEKELA 92
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
12-140 3.68e-20

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: 85.07  E-value: 3.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928  12 DLSALVELENRCFDYDRlSRRNFQWMLTRAHASLTVAEGDGGVLGYALV--LFHEGTslarLYSIAIDPRARGIGLGQKL 89
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPW-TEAQFAEELANYHLCYLLARIGGKVVGYAGVqiVLDEAH----ILNIAVKPEYQGQGIGRAL 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1520954928  90 LEAAEQAARDNDRAYMRLEVRPDNRGAIALYERNGYRPFATVRDYYEDHSE 140
Cdd:TIGR01575  76 LRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGE 126
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
13-125 5.00e-17

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: 76.02  E-value: 5.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928  13 LSALVELENRCF--DYDRLSRRNFQWMLTRAHASLTVAEGDGGVLGYA-LVLFHEGTSLARLYSIAIDPRARGIGLGQKL 89
Cdd:pfam00583   1 LEALYELLSEEFpePWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFAsLSIIDDEPPVGEIEGLAVAPEYRGKGIGTAL 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1520954928  90 LEAAEQAARDNDRAYMRLEVRPDNRGAIALYERNGY 125
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
PRK03624 PRK03624
putative acetyltransferase; Provisional
1-126 3.08e-11

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 60.71  E-value: 3.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928   1 MNLTLRPAGTDDLSALVELENRCFdydrLSR------RNFQWMLTRAHASLTVAEGDGGVLGYALVLF--HEGTslarLY 72
Cdd:PRK03624    1 DAMEIRVFRQADFEAVIALWERCD----LTRpwndpeMDIERKLNHDPSLFLVAEVGGEVVGTVMGGYdgHRGW----AY 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1520954928  73 SIAIDPRARGIGLGQKLLEAAEQAARDNDRAYMRLEVRPDNRGAIALYERNGYR 126
Cdd:PRK03624   73 YLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYE 126
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
47-108 5.81e-09

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: 51.89  E-value: 5.81e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1520954928  47 VAEGDGGVLGYALVLFHEGTS-LARLYSIAIDPRARGIGLGQKLLEAAEQAARDNDRAYMRLE 108
Cdd:cd04301     3 VAEDDGEIVGFASLSPDGSGGdTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
156-346 1.17e-04

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 44.05  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928 156 RRHVPFYRQTTDFTCGPACLLMAMGALQPERQLTR-REELRLWREattiymtaghgGCSPQGLALAAWRRGFRVKLVlsa 234
Cdd:COG2274     1 RRKVPFVLQMEAADCGLACLAMIARYYGRPVSLEElREALGVSRD-----------GLSLLGLLRAARRLGLRARGV--- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928 235 sgplfldgvrnedkkavmrlvhedfceeldasgveqkrstRLDIpRQLARGGQPLVLissyrltRSKAPHWVLVTHYDED 314
Cdd:COG2274    67 ----------------------------------------RLDL-EELAELPLPAIL-------HWDGNHFVVLEGVDGD 98
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1520954928 315 FVYLHDPDVDhsqhrqpldcqHIPVSHAEFDK 346
Cdd:COG2274    99 KVTIADPATG-----------RRKLSLEEFAE 119
PLN02825 PLN02825
amino-acid N-acetyltransferase
6-97 8.25e-03

amino-acid N-acetyltransferase


Pssm-ID: 215441 [Multi-domain]  Cd Length: 515  Bit Score: 38.22  E-value: 8.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928   6 RPAGTDDLSALVELENRCFDYDRLSRRNFQWMLtRAHASLTVAEGDGGVLG-YALVLFHEGTSlARLYSIAIDPRARGIG 84
Cdd:PLN02825  371 RMARVEDLAGIRQIIRPLEESGILVRRTDEELL-RALDSFVVVEREGSIIAcAALFPFFEEKC-GEVAAIAVSPECRGQG 448
                          90
                  ....*....|...
gi 1520954928  85 LGQKLLEAAEQAA 97
Cdd:PLN02825  449 QGDKLLDYIEKKA 461
 
Name Accession Description Interval E-value
DUF3335 pfam11814
Peptidase_C39 like family;
159-362 2.03e-129

Peptidase_C39 like family;


Pssm-ID: 432095  Cd Length: 206  Bit Score: 369.20  E-value: 2.03e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928 159 VPFYRQTTDFTCGPACLLMAMGALQPERQLTRREELRLWREATTIYMTAGHGGCSPQGLALAAWRRGFRVKLVLSASGPL 238
Cdd:pfam11814   1 VPYYRQTTEFTCGPAALMMAMAALDPEYALDREEELRLWREATTIFMTSGHGGCGPHGLALAARRRGFRVEVYVNTDGPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928 239 FLDGVRNEDKKAVMRLVHEDFCEELDASGVEQKRS--TRLDIPRQLARGGQPLVLISSYRLTRSKAPHWVLVTHYDEDFV 316
Cdd:pfam11814  81 FLDSVRSEEKKEVMRLVHEDFREEAAAAGVPVHYRdlSLDDLRAALAAGAVVLVLISTYRMDGEKAPHWVLVTGADDDFV 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1520954928 317 YLHDPDVDHSQHRQPLDCQHIPVSHAEFDKMSRFGRSKLRAAVILF 362
Cdd:pfam11814 161 YIHDPDVDAELGESPLDCQYLPIPRAEFDRMSRYGRARLRAAVLIR 206
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
56-149 2.58e-23

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 92.41  E-value: 2.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928  56 GYALVLFHEGTSLARLYSIAIDPRARGIGLGQKLLEAAEQAARDNDRAYMRLEVRPDNRGAIALYERNGYRPFATVRDYY 135
Cdd:COG0456     1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80
                          90
                  ....*....|....
gi 1520954928 136 EDHseALRFEKRIR 149
Cdd:COG0456    81 GDD--ALVMEKELA 92
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
2-148 1.59e-21

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 90.05  E-value: 1.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928   2 NLTLRPAGTDDLSALVELENRC-------FDYDRLSRRNFQWMLTRAHAS---LTVAEGDGGVLGYA-LVLFHEGTSLAR 70
Cdd:COG1247     1 EMTIRPATPEDAPAIAAIYNEAiaegtatFETEPPSEEEREAWFAAILAPgrpVLVAEEDGEVVGFAsLGPFRPRPAYRG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928  71 LY--SIAIDPRARGIGLGQKLLEAAEQAARDNDRAYMRLEVRPDNRGAIALYERNGYRPFATVRDYYEDHSEAL---RFE 145
Cdd:COG1247    81 TAeeSIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLdlvLMQ 160

                  ...
gi 1520954928 146 KRI 148
Cdd:COG1247   161 KRL 163
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
12-140 3.68e-20

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: 85.07  E-value: 3.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928  12 DLSALVELENRCFDYDRlSRRNFQWMLTRAHASLTVAEGDGGVLGYALV--LFHEGTslarLYSIAIDPRARGIGLGQKL 89
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPW-TEAQFAEELANYHLCYLLARIGGKVVGYAGVqiVLDEAH----ILNIAVKPEYQGQGIGRAL 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1520954928  90 LEAAEQAARDNDRAYMRLEVRPDNRGAIALYERNGYRPFATVRDYYEDHSE 140
Cdd:TIGR01575  76 LRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGE 126
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
13-125 5.00e-17

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: 76.02  E-value: 5.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928  13 LSALVELENRCF--DYDRLSRRNFQWMLTRAHASLTVAEGDGGVLGYA-LVLFHEGTSLARLYSIAIDPRARGIGLGQKL 89
Cdd:pfam00583   1 LEALYELLSEEFpePWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFAsLSIIDDEPPVGEIEGLAVAPEYRGKGIGTAL 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1520954928  90 LEAAEQAARDNDRAYMRLEVRPDNRGAIALYERNGY 125
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
5-145 2.27e-16

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 75.12  E-value: 2.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928   5 LRPAGTDDLSALVELENRCFDYDRLSRRNFQWMLTRAHASLTVAEGDGGVLGYAL---VLFHEGTSLARLYSIAIDPRAR 81
Cdd:COG3153     1 IRPATPEDAEAIAALLRAAFGPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVAlspVDIDGEGPALLLGPLAVDPEYR 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1520954928  82 GIGLGQKLLEAAEQAARDNDRAYMRLEVRPDNRgaiALYERNGYRPFATVRDYYEDHSEALRFE 145
Cdd:COG3153    81 GQGIGRALMRAALEAARERGARAVVLLGDPSLL---PFYERFGFRPAGELGLTLGPDEVFLAKE 141
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
3-149 1.23e-15

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: 72.72  E-value: 1.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928   3 LTLRPAGTDDLSALVELENrcfdydrlsrrnfQWMLTRAHASLTVAEGDGGVLGYALVLFHEGTsLARLYSIAIDPRARG 82
Cdd:COG1246     1 MTIRPATPDDVPAILELIR-------------PYALEEEIGEFWVAEEDGEIVGCAALHPLDED-LAELRSLAVHPDYRG 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1520954928  83 IGLGQKLLEAAEQAARDNDRAYMRLEVRPDnrgAIALYERNGYRPFATVRDYYED--HSEALRFEKRIR 149
Cdd:COG1246    67 RGIGRRLLEALLAEARELGLKRLFLLTTSA---AIHFYEKLGFEEIDKEDLPYAKvwQRDSVVMEKDLE 132
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
47-127 1.08e-14

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 68.64  E-value: 1.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928  47 VAEGDGGVLGYALVLFHEGTSLARLYSIAIDPRARGIGLGQKLLEAAEQAARDNDRAYMRLEVRPDnrgAIALYERNGYR 126
Cdd:pfam13508   7 VAEDDGKIVGFAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNR---AAAFYEKLGFE 83

                  .
gi 1520954928 127 P 127
Cdd:pfam13508  84 E 84
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
47-151 1.84e-14

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 69.70  E-value: 1.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928  47 VAEGDGGVLGYALV--LFHEGTSLARLYsiaIDPRARGIGLGQKLLEAAEQAARDNDRAYMRLEVRPDNRGAIALYERNG 124
Cdd:COG0454    38 AVDDKGEPIGFAGLrrLDDKVLELKRLY---VLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLG 114
                          90       100
                  ....*....|....*....|....*..
gi 1520954928 125 YRPFATVRDYyedhsEALRFEKRIRNP 151
Cdd:COG0454   115 FKEIERYVAY-----VGGEFEKELSLS 136
PRK03624 PRK03624
putative acetyltransferase; Provisional
1-126 3.08e-11

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 60.71  E-value: 3.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928   1 MNLTLRPAGTDDLSALVELENRCFdydrLSR------RNFQWMLTRAHASLTVAEGDGGVLGYALVLF--HEGTslarLY 72
Cdd:PRK03624    1 DAMEIRVFRQADFEAVIALWERCD----LTRpwndpeMDIERKLNHDPSLFLVAEVGGEVVGTVMGGYdgHRGW----AY 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1520954928  73 SIAIDPRARGIGLGQKLLEAAEQAARDNDRAYMRLEVRPDNRGAIALYERNGYR 126
Cdd:PRK03624   73 YLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYE 126
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
69-134 6.09e-11

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 58.00  E-value: 6.09e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1520954928  69 ARLYSIAIDPRARGIGLGQKLLEAAEQAARDNDRAYMRLEVRPDNRGAIALYERNGYRPFATVRDY 134
Cdd:COG3393    16 AEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEYATV 81
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
1-135 1.20e-09

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: 56.93  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928   1 MNLTLRPAGTDDLSALVELEN-----RCFDYDRLSRRNFQWMLTRAHAsltvAEGDGGVLGYALVLFHEGTSL--ARLYS 73
Cdd:COG1670     6 ERLRLRPLRPEDAEALAELLNdpevaRYLPGPPYSLEEARAWLERLLA----DWADGGALPFAIEDKEDGELIgvVGLYD 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1520954928  74 I-----------AIDPRARGIGLGQKLLEAAEQAARDNDRA-YMRLEVRPDNRGAIALYERNGYRPFATVRDYY 135
Cdd:COG1670    82 IdranrsaeigyWLAPAYWGKGYATEALRALLDYAFEELGLhRVEAEVDPDNTASIRVLEKLGFRLEGTLRDAL 155
COG3818 COG3818
Predicted N-acetyltransferase, GNAT superfamily [General function prediction only];
3-126 1.34e-09

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


Pssm-ID: 443030 [Multi-domain]  Cd Length: 168  Bit Score: 56.48  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928   3 LTLRPAGTDDLSALVELENRCFDY-DRLSRRNFQWMLTRAHASLtVAEGDGGVLGYaLVLFHEGTSLAR----------- 70
Cdd:COG3818     5 IVIRDAREHDLDAVLALNNAAVPAvSPLDAARLARLHEQAAYAR-VAEVDGEVAGF-LLAFGPGADYDSpnyrwfaeryd 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1520954928  71 --LY--SIAIDPRARGIGLGQKLLEAAEQAARDNDRAYMRLEV--RPDNRGAIALYERNGYR 126
Cdd:COG3818    83 nfLYidRIVVAPSARGRGLGRALYADVFSYARARGVPRVTCEVnlEPPNPGSLAFHARLGFR 144
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
69-135 4.60e-09

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 54.55  E-value: 4.60e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1520954928  69 ARLYSIAIDPRARGIGLGQKLLEAAEQAARDNDRAYMRLEVRPDNRGAIALYERNGYRPFATVRDYY 135
Cdd:PRK09491   64 ATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYY 130
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
47-108 5.81e-09

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: 51.89  E-value: 5.81e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1520954928  47 VAEGDGGVLGYALVLFHEGTS-LARLYSIAIDPRARGIGLGQKLLEAAEQAARDNDRAYMRLE 108
Cdd:cd04301     3 VAEDDGEIVGFASLSPDGSGGdTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
47-128 9.81e-09

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 53.26  E-value: 9.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928  47 VAEGDGGVLGYALvLFHEGTSLARLYSIAIDPRARGIGLGQKLLEAAEQAARDNDRAYMRLEVRPDnrgAIALYERNGYR 126
Cdd:COG2153    38 LAYDDGELVATAR-LLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH---AVGFYEKLGFV 113

                  ..
gi 1520954928 127 PF 128
Cdd:COG2153   114 PV 115
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
13-148 2.01e-08

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


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 52.27  E-value: 2.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928  13 LSALVELENRCFdYDRLSRRNFQWMLTRAHASLTVAEGDGGVLGYALVlfhegTSLARLYSIAIDPRARGIGLGQKLLEA 92
Cdd:pfam13673   2 APDYSEEGIETF-YEFISPEALRERIDQGEYFFFVAFEGGQIVGVIAL-----RDRGHISLLFVDPDYQGQGIGKALLEA 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1520954928  93 AEQAARDNDRAYMRLEVRPDNrGAIALYERNGYRpfATVRDYYEDHSEALRFEKRI 148
Cdd:pfam13673  76 VEDYAEKDGIKLSELTVNASP-YAVPFYEKLGFR--ATGPEQEFNGIRFVPMEKEL 128
PRK07757 PRK07757
N-acetyltransferase;
37-99 1.94e-06

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 47.11  E-value: 1.94e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928  37 MLTRAHASL-------TVAEGDGGVLGYALVLFHeGTSLARLYSIAIDPRARGIGLGQKLLEAAEQAARD 99
Cdd:PRK07757   28 MLPRSLDELyenirdfYVAEEEGEIVGCCALHIL-WEDLAEIRSLAVSEDYRGQGIGRMLVEACLEEARE 96
ectoine_EctA TIGR02406
diaminobutyrate acetyltransferase; This enzyme family is the EctA of ectoine biosynthesis. ...
5-122 2.50e-05

diaminobutyrate acetyltransferase; This enzyme family is the EctA of ectoine biosynthesis. Ectoine is a compatible solute, analagous to trehalose, betaines, etc., found often in halotolerant organisms. EctA is L-2,4-diaminobutyric acid acetyltransferase, also called DABA acetyltransferase. [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 131459  Cd Length: 157  Bit Score: 43.94  E-value: 2.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928   5 LRPAGTDDLSALVELENRCFDYDRLSRRNFQWMLTRAHASLTVAEGDGG-----VLGYAL-----VLFhegtslarLYSI 74
Cdd:TIGR02406   1 FRPPRIEDGAGIWELVKDCPPLDLNSSYAYLLLCTDFADTSIVAESEGGeivgfVSGYLRpdrpdVLF--------VWQV 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1520954928  75 AIDPRARGIGLGQKLLEAAEQAARDNDRAYMRLEVRPDNRGAIALYER 122
Cdd:TIGR02406  73 AVDPRARGKGLARRLLEALLERVACERVRHLETTITPDNQASRALFKA 120
PRK10146 PRK10146
aminoalkylphosphonate N-acetyltransferase;
4-125 5.77e-05

aminoalkylphosphonate N-acetyltransferase;


Pssm-ID: 182266 [Multi-domain]  Cd Length: 144  Bit Score: 42.60  E-value: 5.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928   4 TLRPAGTDDLSA----LVELENRCFDYDRLsRRNFQWMLTRAHASLTVAEGDGGVLG----YALVLFHEGTSLARLYSIA 75
Cdd:PRK10146    5 ELRPATQYDTDAvyalICELKQAEFDHQAF-RVGFNANLRDPNMRYHLALLDGEVVGmiglHLQFHLHHVNWIGEIQELV 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1520954928  76 IDPRARGIGLGQKLLEAAEQAARDNDRAYMRLEVRPDNRGAIALYERNGY 125
Cdd:PRK10146   84 VMPQARGLNVGSKLLAWAEEEARQAGAEMTELSTNVKRHDAHRFYLREGY 133
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
156-346 1.17e-04

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 44.05  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928 156 RRHVPFYRQTTDFTCGPACLLMAMGALQPERQLTR-REELRLWREattiymtaghgGCSPQGLALAAWRRGFRVKLVlsa 234
Cdd:COG2274     1 RRKVPFVLQMEAADCGLACLAMIARYYGRPVSLEElREALGVSRD-----------GLSLLGLLRAARRLGLRARGV--- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928 235 sgplfldgvrnedkkavmrlvhedfceeldasgveqkrstRLDIpRQLARGGQPLVLissyrltRSKAPHWVLVTHYDED 314
Cdd:COG2274    67 ----------------------------------------RLDL-EELAELPLPAIL-------HWDGNHFVVLEGVDGD 98
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1520954928 315 FVYLHDPDVDhsqhrqpldcqHIPVSHAEFDK 346
Cdd:COG2274    99 KVTIADPATG-----------RRKLSLEEFAE 119
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
3-126 6.18e-04

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 39.64  E-value: 6.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928   3 LTLRPAGTDDLSALVELEN-----RCFDYDRLSRRNFQ-WMLTRAHASLT-------VAEGDGGVLGYA-LVLFHEGTSL 68
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSdpevmRYGVPWPLTLEEAReWLARIWAADEAergygwaIELKDTGFIGSIgLYDIDGEPER 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1520954928  69 ARLySIAIDPRARGIGLGQKLLEAA-EQAARDNDRAYMRLEVRPDNRGAIALYERNGYR 126
Cdd:pfam13302  82 AEL-GYWLGPDYWGKGYATEAVRALlEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
74-126 1.29e-03

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 38.92  E-value: 1.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1520954928  74 IAIDPRARGIGLGQKLLEAAEQAARDNDRAYMRLEVRPDNRgaiALYERNGYR 126
Cdd:PLN02706   91 VVVDSAARGKGLGKKIIEALTEHARSAGCYKVILDCSEENK---AFYEKCGYV 140
PLN02825 PLN02825
amino-acid N-acetyltransferase
6-97 8.25e-03

amino-acid N-acetyltransferase


Pssm-ID: 215441 [Multi-domain]  Cd Length: 515  Bit Score: 38.22  E-value: 8.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520954928   6 RPAGTDDLSALVELENRCFDYDRLSRRNFQWMLtRAHASLTVAEGDGGVLG-YALVLFHEGTSlARLYSIAIDPRARGIG 84
Cdd:PLN02825  371 RMARVEDLAGIRQIIRPLEESGILVRRTDEELL-RALDSFVVVEREGSIIAcAALFPFFEEKC-GEVAAIAVSPECRGQG 448
                          90
                  ....*....|...
gi 1520954928  85 LGQKLLEAAEQAA 97
Cdd:PLN02825  449 QGDKLLDYIEKKA 461
 
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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