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Conserved domains on  [gi|1405942272|gb|PZX82089|]
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GNAT family N-acetyltransferase [Klebsiella variicola]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10006981)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
4-134 1.16e-16

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


:

Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 71.27  E-value: 1.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942272   4 IRAAESKDIPSLKTLFLQ-LGYQTETAIIEQRITAPQSMMSaLVAETENAVCGVIVINFIlPVHENRLWALISALVIEES 82
Cdd:COG3153     1 IRPATPEDAEAIAALLRAaFGPGREAELVDRLREDPAAGLS-LVAEDDGEIVGHVALSPV-DIDGEGPALLLGPLAVDPE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1405942272  83 SRGSGIGQQLLHAAERLARDKQCAQIELSSSEkriRAHQFYENNGYKEVRKR 134
Cdd:COG3153    79 YRGQGIGRALMRAALEAARERGARAVVLLGDP---SLLPFYERFGFRPAGEL 127
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
4-134 1.16e-16

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 71.27  E-value: 1.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942272   4 IRAAESKDIPSLKTLFLQ-LGYQTETAIIEQRITAPQSMMSaLVAETENAVCGVIVINFIlPVHENRLWALISALVIEES 82
Cdd:COG3153     1 IRPATPEDAEAIAALLRAaFGPGREAELVDRLREDPAAGLS-LVAEDDGEIVGHVALSPV-DIDGEGPALLLGPLAVDPE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1405942272  83 SRGSGIGQQLLHAAERLARDKQCAQIELSSSEkriRAHQFYENNGYKEVRKR 134
Cdd:COG3153    79 YRGQGIGRALMRAALEAARERGARAVVLLGDP---SLLPFYERFGFRPAGEL 127
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 45-130 1.61e-12

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 59.01  E-value: 1.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942272  45 LVAETENAVCGVIVINfilpVHENRLWALISALVIEESSRGSGIGQQLLHAAERLARDKQCAQIELSSSEkriRAHQFYE 124
Cdd:pfam13508   6 FVAEDDGKIVGFAALL----PLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTN---RAAAFYE 78


                  ....*.
gi 1405942272 125 NNGYKE 130
Cdd:pfam13508  79 KLGFEE 84
PRK10146 PRK10146
aminoalkylphosphonate N-acetyltransferase;
46-139 6.55e-11

aminoalkylphosphonate N-acetyltransferase;


Pssm-ID: 182266 [Multi-domain]  Cd Length: 144  Bit Score: 56.46  E-value: 6.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942272  46 VAETENAVCGVIVINFILPVHENRLWALISALVIEESSRGSGIGQQLLHAAERLARDKQCAQIELSSSEKRIRAHQFYEN 125
Cdd:PRK10146   51 LALLDGEVVGMIGLHLQFHLHHVNWIGEIQELVVMPQARGLNVGSKLLAWAEEEARQAGAEMTELSTNVKRHDAHRFYLR 130

                          90
                  ....*....|....
gi 1405942272 126 NGYKEVRKRFVKHL 139
Cdd:PRK10146  131 EGYEQSHFRFTKAL 144
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 45-111 4.62e-08

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: 46.89  E-value: 4.62e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942272  45 LVAETENAVCGVIVInfiLPVHENRLWALISALVIEESSRGSGIGQQLLHAAERLARDKQCAQIELS 111
Cdd:cd04301     2 LVAEDDGEIVGFASL---SPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 45-135 4.86e-07

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: 45.78  E-value: 4.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942272  45 LVAETENAVCGVIVINFILpvHEnrlwALISALVIEESSRGSGIGQQLLHAAERLARDKQCAQIELSSSEKRIRAHQFYE 124
Cdd:TIGR01575  34 LLARIGGKVVGYAGVQIVL--DE----AHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYK 107

                          90
                  ....*....|...
gi 1405942272 125 NNGYKEV--RKRF 135
Cdd:TIGR01575 108 KLGFNEIaiRRNY 120
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
4-134 1.16e-16

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 71.27  E-value: 1.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942272   4 IRAAESKDIPSLKTLFLQ-LGYQTETAIIEQRITAPQSMMSaLVAETENAVCGVIVINFIlPVHENRLWALISALVIEES 82
Cdd:COG3153     1 IRPATPEDAEAIAALLRAaFGPGREAELVDRLREDPAAGLS-LVAEDDGEIVGHVALSPV-DIDGEGPALLLGPLAVDPE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1405942272  83 SRGSGIGQQLLHAAERLARDKQCAQIELSSSEkriRAHQFYENNGYKEVRKR 134
Cdd:COG3153    79 YRGQGIGRALMRAALEAARERGARAVVLLGDP---SLLPFYERFGFRPAGEL 127
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 4-140 2.90e-14

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 65.07  E-value: 2.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942272   4 IRAAESKDIPSLktlflqLGYQTETAIIEQRItAPQSMMSALVAETENAVCGVIVINFI-LPVHEnrlwalISALVIEES 82
Cdd:COG0454     3 IRKATPEDINFI------LLIEALDAELKAME-GSLAGAEFIAVDDKGEPIGFAGLRRLdDKVLE------LKRLYVLPE 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1405942272  83 SRGSGIGQQLLHAAERLARDKQCAQIELSSSEKRIRAHQFYENNGYKE-------VRKRFVKHLS 140
Cdd:COG0454    70 YRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEieryvayVGGEFEKELS 134
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 4-131 1.48e-13

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: 63.09  E-value: 1.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942272   4 IRAAESKDIPSLKTLFLQLGYQTETAIIeqritapqsmmsaLVAETENAVCGVIVINfilpVHENRLwALISALVIEESS 83
Cdd:COG1246     3 IRPATPDDVPAILELIRPYALEEEIGEF-------------WVAEEDGEIVGCAALH----PLDEDL-AELRSLAVHPDY 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1405942272  84 RGSGIGQQLLHAAERLARDKQCAQIELSSsekRIRAHQFYENNGYKEV 131
Cdd:COG1246    65 RGRGIGRRLLEALLAEARELGLKRLFLLT---TSAAIHFYEKLGFEEI 109
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 62-134 2.70e-13

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 61.21  E-value: 2.70e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1405942272  62 ILPVHENRLWALISALVIEESSRGSGIGQQLLHAAERLARDKQCAQIELSSSEKRIRAHQFYENNGYKEVRKR 134
Cdd:COG0456     4 LLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGER 76
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-131 4.43e-13

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 62.32  E-value: 4.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942272   1 MVFIRAAESKDIPSLKTLFLQLGYQT---------ETAIIEQRITAPQS-MMSALVAETENAVCGVIVINFILPVHENRL 70
Cdd:COG1247     1 EMTIRPATPEDAPAIAAIYNEAIAEGtatfeteppSEEEREAWFAAILApGRPVLVAEEDGEVVGFASLGPFRPRPAYRG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1405942272  71 WALISaLVIEESSRGSGIGQQLLHAAERLARDKQCAQIELSSSEKRIRAHQFYENNGYKEV 131
Cdd:COG1247    81 TAEES-IYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEV 140
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 45-130 1.61e-12

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 59.01  E-value: 1.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942272  45 LVAETENAVCGVIVINfilpVHENRLWALISALVIEESSRGSGIGQQLLHAAERLARDKQCAQIELSSSEkriRAHQFYE 124
Cdd:pfam13508   6 FVAEDDGKIVGFAALL----PLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTN---RAAAFYE 78


                  ....*.
gi 1405942272 125 NNGYKE 130
Cdd:pfam13508  79 KLGFEE 84
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 45-128 2.50e-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: 56.76  E-value: 2.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942272  45 LVAETENAVCGVIVINfilPVHENRLWALISALVIEESSRGSGIGQQLLHAAERLARDKQCAQIELSSSEKRIRAHQFYE 124
Cdd:pfam00583  36 FVAEEDGELVGFASLS---IIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYE 112


                  ....
gi 1405942272 125 NNGY 128
Cdd:pfam00583 113 KLGF 116
PRK10146 PRK10146
aminoalkylphosphonate N-acetyltransferase;
46-139 6.55e-11

aminoalkylphosphonate N-acetyltransferase;


Pssm-ID: 182266 [Multi-domain]  Cd Length: 144  Bit Score: 56.46  E-value: 6.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942272  46 VAETENAVCGVIVINFILPVHENRLWALISALVIEESSRGSGIGQQLLHAAERLARDKQCAQIELSSSEKRIRAHQFYEN 125
Cdd:PRK10146   51 LALLDGEVVGMIGLHLQFHLHHVNWIGEIQELVVMPQARGLNVGSKLLAWAEEEARQAGAEMTELSTNVKRHDAHRFYLR 130

                          90
                  ....*....|....
gi 1405942272 126 NGYKEVRKRFVKHL 139
Cdd:PRK10146  131 EGYEQSHFRFTKAL 144
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
71-131 9.96e-09

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 50.18  E-value: 9.96e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1405942272  71 WALISALVIEESSRGSGIGQQLLHAAERLARDKQCAQIELSSsekRIRAHQFYENNGYKEV 131
Cdd:COG2153    58 EAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSA---QAHAVGFYEKLGFVPV 115
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 45-111 4.62e-08

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: 46.89  E-value: 4.62e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1405942272  45 LVAETENAVCGVIVInfiLPVHENRLWALISALVIEESSRGSGIGQQLLHAAERLARDKQCAQIELS 111
Cdd:cd04301     2 LVAEDDGEIVGFASL---SPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 45-135 4.86e-07

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: 45.78  E-value: 4.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942272  45 LVAETENAVCGVIVINFILpvHEnrlwALISALVIEESSRGSGIGQQLLHAAERLARDKQCAQIELSSSEKRIRAHQFYE 124
Cdd:TIGR01575  34 LLARIGGKVVGYAGVQIVL--DE----AHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYK 107

                          90
                  ....*....|...
gi 1405942272 125 NNGYKEV--RKRF 135
Cdd:TIGR01575 108 KLGFNEIaiRRNY 120
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
71-132 3.70e-06

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 42.59  E-value: 3.70e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1405942272  71 WALISALVIEESSRGSGIGQQLLHAAERLARDKQCAQIELSSSEKRIRAHQFYENNGYKEVR 132
Cdd:COG3393    15 VAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVG 76
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
 74-139 5.66e-04

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 37.76  E-value: 5.66e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942272  74 ISALVIEESSRGSGIGQQLLHAAERLARDKQCAQIELSSSEKRIrahQFYENNGYKEVRKRFVKHL 139
Cdd:PLN02706   88 IEDVVVDSAARGKGLGKKIIEALTEHARSAGCYKVILDCSEENK---AFYEKCGYVRKEIQMVKYF 150
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 31-138 6.99e-04

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: 37.25  E-value: 6.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942272  31 IEQRITAPQSMMsaLVAETENAVCGVI-VINfilpvhENRlwalISALVIEESSRGSGIGQQLLHAAERLARDKQ--CAQ 107
Cdd:pfam13673  22 LRERIDQGEYFF--FVAFEGGQIVGVIaLRD------RGH----ISLLFVDPDYQGQGIGKALLEAVEDYAEKDGikLSE 89

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1405942272 108 IELSSSekrIRAHQFYENNGYKEVRKRFVKH 138
Cdd:pfam13673  90 LTVNAS---PYAVPFYEKLGFRATGPEQEFN 117
PHA00673 PHA00673
acetyltransferase domain containing protein
 7-139 5.62e-03

acetyltransferase domain containing protein


Pssm-ID: 106981  Cd Length: 154  Bit Score: 35.08  E-value: 5.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942272   7 AESKDIPSLKTLFLQLGYQTETAIIEQRIT---APQSMMSALVAETENAVCGVIVINFI------LPVHENRLWALISAL 77
Cdd:PHA00673   12 AELADAPTFASLCAEYAHESANADLAGRAPdhhAYAGMEAAGVAHFLGVFRGEELVGFAcllvtpVPHFKGQLIGTTESI 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1405942272  78 VIEESSRGSGIGQQLLHAAERLARDKQCAQIELSSSEKRiRAHQFYENNGYKEVRKRFVKHL 139
Cdd:PHA00673   92 FVAAAHRPGGAGMALLRATEALARDLGATGLYVSGPTEG-RLVQLLPAAGYRETNRTFYRGL 152
PTZ00330 PTZ00330
acetyltransferase; Provisional
 74-129 7.30e-03

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 34.82  E-value: 7.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1405942272  74 ISALVIEESSRGSGIGQQLLHAAERLARDKQCAQIELSSSEKRIrahQFYENNGYK 129
Cdd:PTZ00330   85 IEDVVVDPSYRGQGLGRALISDLCEIARSSGCYKVILDCTEDMV---AFYKKLGFR 137
PRK07757 PRK07757
N-acetyltransferase;
1-133 8.18e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 34.40  E-value: 8.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405942272   1 MVFIRAAESKDIPSLKTLflqLGYQTETAIIEQRitAPQSMMSAL----VAETENAVCGVIVINFILPvhenRLwALISA 76
Cdd:PRK07757    1 MMEIRKARLSDVKAIHAL---INVYAKKGLMLPR--SLDELYENIrdfyVAEEEGEIVGCCALHILWE----DL-AEIRS 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1405942272  77 LVIEESSRGSGIGQQLLHAAERLARDkqcaqIELssseKRIRA----HQFYENNGYKEVRK 133
Cdd:PRK07757   71 LAVSEDYRGQGIGRMLVEACLEEARE-----LGV----KRVFAltyqPEFFEKLGFREVDK 122
 
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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