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Conserved domains on  [gi|489012768|ref|WP_002923294|]
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MULTISPECIES: GNAT family N-acetyltransferase [Klebsiella]

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
Acetyltransf_10 super family cl48219
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
42-140 2.01e-15

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


The actual alignment was detected with superfamily member pfam13673:

Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 68.07  E-value: 2.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489012768   42 KNRFNAPGETLLGAFVNHQLVGVCGInsdpfspqPRAGRIRHLYISERYRRRGIGQQLLVSVITHSSAWFDFLNT---HA 118
Cdd:pfam13673  23 RERIDQGEYFFFVAFEGGQIVGVIAL--------RDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSEltvNA 94
                          90       100
                  ....*....|....*....|..
gi 489012768  119 PAQAWPFYERLGFRPVyDEPRV 140
Cdd:pfam13673  95 SPYAVPFYEKLGFRAT-GPEQE 115
 
Name Accession Description Interval E-value
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
42-140 2.01e-15

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: 68.07  E-value: 2.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489012768   42 KNRFNAPGETLLGAFVNHQLVGVCGInsdpfspqPRAGRIRHLYISERYRRRGIGQQLLVSVITHSSAWFDFLNT---HA 118
Cdd:pfam13673  23 RERIDQGEYFFFVAFEGGQIVGVIAL--------RDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSEltvNA 94
                          90       100
                  ....*....|....*....|..
gi 489012768  119 PAQAWPFYERLGFRPVyDEPRV 140
Cdd:pfam13673  95 SPYAVPFYEKLGFRAT-GPEQE 115
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
5-137 8.52e-12

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 58.94  E-value: 8.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489012768   5 LIAATTPDAPGFAALRIESLEQHF--NMLRRLAENWQSGknrfnapgeTLLGAFVNHQLVGVCGINSDPFSPQPRAGRIR 82
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPGReaELVDRLREDPAAG---------LSLVAEDDGEIVGHVALSPVDIDGEGPALLLG 71
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489012768  83 HLYISERYRRRGIGQQLLVSVITHSSAW-FDFLNTHAPAQAWPFYERLGFRPVYDE 137
Cdd:COG3153   72 PLAVDPEYRGQGIGRALMRAALEAARERgARAVVLLGDPSLLPFYERFGFRPAGEL 127
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
52-106 2.01e-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: 2.01e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489012768  52 LLGAFVNHQLVGVCGInsDPFSPQPRAGRIRHLYISERYRRRGIGQQLLVSVITH 106
Cdd:cd04301    1 FLVAEDDGEIVGFASL--SPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEE 53
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
52-132 1.47e-04

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: 39.23  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489012768   52 LLGAFVNHQLVGVCGINSDPFSpqpraGRIRHLYISERYRRRGIGQQLLVSVITHS------SAWFDFLNTHAPAQAwpF 125
Cdd:TIGR01575  33 YLLARIGGKVVGYAGVQIVLDE-----AHILNIAVKPEYQGQGIGRALLRELIDEAkgrgvnEIFLEVRVSNIAAQA--L 105

                  ....*..
gi 489012768  126 YERLGFR 132
Cdd:TIGR01575 106 YKKLGFN 112
PRK09831 PRK09831
GNAT family N-acetyltransferase;
62-143 1.57e-04

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 39.56  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489012768  62 VGVCGINSDPFSPQPRAGR-IRHLYISERYRRRGIGQQLLVSVITHSSAwfdfLNTHAPAQAWPFYERLGFRPVyDEPRV 140
Cdd:PRK09831  55 VRVAVINAQPVGFITCIEHyIDMLFVDPEYTRRGVASALLKPLIKSESE----LTVDASITAKPFFERYGFQTV-KQQRV 129

                 ...
gi 489012768 141 THR 143
Cdd:PRK09831 130 ECR 132
 
Name Accession Description Interval E-value
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
42-140 2.01e-15

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: 68.07  E-value: 2.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489012768   42 KNRFNAPGETLLGAFVNHQLVGVCGInsdpfspqPRAGRIRHLYISERYRRRGIGQQLLVSVITHSSAWFDFLNT---HA 118
Cdd:pfam13673  23 RERIDQGEYFFFVAFEGGQIVGVIAL--------RDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSEltvNA 94
                          90       100
                  ....*....|....*....|..
gi 489012768  119 PAQAWPFYERLGFRPVyDEPRV 140
Cdd:pfam13673  95 SPYAVPFYEKLGFRAT-GPEQE 115
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
5-137 8.52e-12

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 58.94  E-value: 8.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489012768   5 LIAATTPDAPGFAALRIESLEQHF--NMLRRLAENWQSGknrfnapgeTLLGAFVNHQLVGVCGINSDPFSPQPRAGRIR 82
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPGReaELVDRLREDPAAG---------LSLVAEDDGEIVGHVALSPVDIDGEGPALLLG 71
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489012768  83 HLYISERYRRRGIGQQLLVSVITHSSAW-FDFLNTHAPAQAWPFYERLGFRPVYDE 137
Cdd:COG3153   72 PLAVDPEYRGQGIGRALMRAALEAARERgARAVVLLGDPSLLPFYERFGFRPAGEL 127
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
48-134 1.60e-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: 57.69  E-value: 1.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489012768  48 PGETLLGAFVNHQLVGVCGINSDPfspqPRAGRIRHLYISERYRRRGIGQQLLVSVITHSSAW-FD--FLNTHAPAQawP 124
Cdd:COG1246   26 EIGEFWVAEEDGEIVGCAALHPLD----EDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELgLKrlFLLTTSAAI--H 99
                         90
                 ....*....|
gi 489012768 125 FYERLGFRPV 134
Cdd:COG1246  100 FYEKLGFEEI 109
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
48-133 5.57e-11

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 55.15  E-value: 5.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489012768   48 PGETLLGAFVNHQLVGVCGINsdpFSPQPRAGRIRHLYISERYRRRGIGQQLL---VSVITHSSAWFDFLNTHAPAQAwp 124
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALL---PLDDEGALAELRLAVHPEYRGQGIGRALLeaaEAAAKEGGIKLLELETTNRAAA-- 75

                  ....*....
gi 489012768  125 FYERLGFRP 133
Cdd:pfam13508  76 FYEKLGFEE 84
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
8-144 5.78e-10

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 54.23  E-value: 5.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489012768   8 ATTPDAPGFAALR---IESLEQHFNMLRRLAENWQSGKNRFNAPGETLLGAFVNHQLVGVCGInsDPFSPQPRAGRIRH- 83
Cdd:COG1247    7 ATPEDAPAIAAIYneaIAEGTATFETEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFASL--GPFRPRPAYRGTAEe 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489012768  84 -LYISERYRRRGIGQQLLVSVITHSSAW-FDFLNTHAPAQ---AWPFYERLGFRPVYDEPRVTHRL 144
Cdd:COG1247   85 sIYVDPDARGRGIGRALLEALIERARARgYRRLVAVVLADneaSIALYEKLGFEEVGTLPEVGFKF 150
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
42-131 8.24e-10

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: 52.91  E-value: 8.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489012768   42 KNRFNAPGETLLGAFVNHQLVGVCGINSDPFspQPRAGRIRHLYISERYRRRGIGQQLLVSVITHSSAW---FDFLNTHA 118
Cdd:pfam00583  25 EDWDEDASEGFFVAEEDGELVGFASLSIIDD--EPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERgceRIFLEVAA 102
                          90
                  ....*....|....
gi 489012768  119 P-AQAWPFYERLGF 131
Cdd:pfam00583 103 DnLAAIALYEKLGF 116
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
53-143 1.47e-09

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 52.88  E-value: 1.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489012768  53 LGAFVNHQLVGVCGInsdpFSPQPRAGRIRHLYISERYRRRGIGQQLLVSVITH------SSAWFdflntHAPAQAWPFY 126
Cdd:COG2153   37 LLAYDDGELVATARL----LPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEarergaRRIVL-----SAQAHAVGFY 107
                         90       100
                 ....*....|....*....|
gi 489012768 127 ERLGFRPV---YDEPRVTHR 143
Cdd:COG2153  108 EKLGFVPVgeeFLEAGIPHI 127
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
72-139 2.36e-09

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 51.19  E-value: 2.36e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489012768  72 FSPQPRAGRIRHLYISERYRRRGIGQQLLVSVITHSSAW---FDFLNTHAP-AQAWPFYERLGFRPVYDEPR 139
Cdd:COG0456    7 LVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERgarRLRLEVREDnEAAIALYEKLGFEEVGERPN 78
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
52-106 2.01e-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: 2.01e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489012768  52 LLGAFVNHQLVGVCGInsDPFSPQPRAGRIRHLYISERYRRRGIGQQLLVSVITH 106
Cdd:cd04301    1 FLVAEDDGEIVGFASL--SPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEE 53
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
16-134 1.66e-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: 1.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489012768  16 FAALRIESLEQHFNMLRRLAENWQSGknrfnapGETLLGAF--VNHQLVGVCGINsdPFSPQPRAGRIrHLYISERYRRR 93
Cdd:COG1670   33 YLPGPPYSLEEARAWLERLLADWADG-------GALPFAIEdkEDGELIGVVGLY--DIDRANRSAEI-GYWLAPAYWGK 102
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 489012768  94 GIGQQLLVSVITHSSAWFDF----LNTHA---PAQAwpFYERLGFRPV 134
Cdd:COG1670  103 GYATEALRALLDYAFEELGLhrveAEVDPdntASIR--VLEKLGFRLE 148
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
60-136 6.85e-06

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 41.82  E-value: 6.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489012768  60 QLVGVCGINSDPfspqPRAGRIRHLYISERYRRRGIGQQLLVSVITHSSA------WFDFLNTHAPAQAwpFYERLGFRP 133
Cdd:COG3393    1 ELVAMAGVRAES----PGVAEISGVYTHPEYRGRGLASALVAALAREALArgartpFLYVDADNPAARR--LYERLGFRP 74

                 ...
gi 489012768 134 VYD 136
Cdd:COG3393   75 VGE 77
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
4-145 9.75e-06

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 42.73  E-value: 9.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489012768   4 LLIAATTPDAPGFAALRIESLEQHFNMLRRLAenwqsgknrfnapGETLLGAFVNHQLVGVCGINSDPfspqPRAGRIRH 83
Cdd:COG0454    1 MSIRKATPEDINFILLIEALDAELKAMEGSLA-------------GAEFIAVDDKGEPIGFAGLRRLD----DKVLELKR 63
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489012768  84 LYISERYRRRGIGQQLLvsviTHSSAWFD-------FLNTHAP-AQAWPFYERLGFRPVYDEPRVTHRLF 145
Cdd:COG0454   64 LYVLPEYRGKGIGKALL----EALLEWARergctalELDTLDGnPAAIRFYERLGFKEIERYVAYVGGEF 129
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
52-132 1.47e-04

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: 39.23  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489012768   52 LLGAFVNHQLVGVCGINSDPFSpqpraGRIRHLYISERYRRRGIGQQLLVSVITHS------SAWFDFLNTHAPAQAwpF 125
Cdd:TIGR01575  33 YLLARIGGKVVGYAGVQIVLDE-----AHILNIAVKPEYQGQGIGRALLRELIDEAkgrgvnEIFLEVRVSNIAAQA--L 105

                  ....*..
gi 489012768  126 YERLGFR 132
Cdd:TIGR01575 106 YKKLGFN 112
PRK09831 PRK09831
GNAT family N-acetyltransferase;
62-143 1.57e-04

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 39.56  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489012768  62 VGVCGINSDPFSPQPRAGR-IRHLYISERYRRRGIGQQLLVSVITHSSAwfdfLNTHAPAQAWPFYERLGFRPVyDEPRV 140
Cdd:PRK09831  55 VRVAVINAQPVGFITCIEHyIDMLFVDPEYTRRGVASALLKPLIKSESE----LTVDASITAKPFFERYGFQTV-KQQRV 129

                 ...
gi 489012768 141 THR 143
Cdd:PRK09831 130 ECR 132
PRK07757 PRK07757
N-acetyltransferase;
60-134 4.59e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 35.17  E-value: 4.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489012768  60 QLVGVCG--INSdpfspqPRAGRIRHLYISERYRRRGIGQQLLVSVIthSSAWFD-----FLNTHAPAqawpFYERLGFR 132
Cdd:PRK07757  51 EIVGCCAlhILW------EDLAEIRSLAVSEDYRGQGIGRMLVEACL--EEARELgvkrvFALTYQPE----FFEKLGFR 118

                 ..
gi 489012768 133 PV 134
Cdd:PRK07757 119 EV 120
 
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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