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Conserved domains on  [gi|333773040|gb|EGL49824|]
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acetyltransferase, GNAT family [Streptococcus dysgalactiae subsp. equisimilis SK1249]

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
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];
4-138 1.70e-18

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


:

Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 76.28  E-value: 1.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333773040   4 LRPLSKADCPSLKEINDKALGYCVSLDLVESQFERLidDGHHYFLAYDDEdthQLVGYVHAECYETLYTDKGLNVLALAV 83
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPGREAELVDRLREDP--AAGLSLVAEDDG---EIVGHVALSPVDIDGEGPALLLGPLAV 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 333773040  84 LPDYQGKGIGRSLVAGLEALAKEEEFAFIRLNSASHRteaHGFYRKLNYVDDKTQ 138
Cdd:COG3153   76 DPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSL---LPFYERFGFRPAGEL 127
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
4-138 1.70e-18

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 76.28  E-value: 1.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333773040   4 LRPLSKADCPSLKEINDKALGYCVSLDLVESQFERLidDGHHYFLAYDDEdthQLVGYVHAECYETLYTDKGLNVLALAV 83
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPGREAELVDRLREDP--AAGLSLVAEDDG---EIVGHVALSPVDIDGEGPALLLGPLAV 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 333773040  84 LPDYQGKGIGRSLVAGLEALAKEEEFAFIRLNSASHRteaHGFYRKLNYVDDKTQ 138
Cdd:COG3153   76 DPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSL---LPFYERFGFRPAGEL 127
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
13-132 3.24e-15

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: 67.16  E-value: 3.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333773040   13 PSLKEINDKALGYCVSLDLVESQFERLIDDGHHYFLAYDDEdthQLVGYVhaECYETLYTDKGLNVLALAVLPDYQGKGI 92
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDG---ELVGFA--SLSIIDDEPPVGEIEGLAVAPEYRGKGI 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 333773040   93 GRSLVAGLEALAKEEEFAFIRLNSASHRTEAHGFYRKLNY 132
Cdd:pfam00583  77 GTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
46-115 3.25e-10

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: 52.66  E-value: 3.25e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333773040  46 YFLAYDDEdthQLVGYVHAECYEtlYTDKGLNVLALAVLPDYQGKGIGRSLVAGLEALAKEEEFAFIRLN 115
Cdd:cd04301    1 FLVAEDDG---EIVGFASLSPDG--SGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PRK07757 PRK07757
N-acetyltransferase;
46-139 2.88e-07

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 46.73  E-value: 2.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333773040  46 YFLAYDDEdthQLVGYvhaeCYETLYTDKGLNVLALAVLPDYQGKGIGRSLVAGLEALAKEEE----FAFirlnsashrT 121
Cdd:PRK07757  43 FYVAEEEG---EIVGC----CALHILWEDLAEIRSLAVSEDYRGQGIGRMLVEACLEEARELGvkrvFAL---------T 106
                         90
                 ....*....|....*....
gi 333773040 122 EAHGFYRKLNYVD-DKTQL 139
Cdd:PRK07757 107 YQPEFFEKLGFREvDKEAL 125
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
33-132 8.37e-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: 45.40  E-value: 8.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333773040   33 ESQFER-LIDDGHHYFLAYDDEdthQLVGYvhAECYETLYTDKglnVLALAVLPDYQGKGIGRSLVAGLEALAKEEEFAF 111
Cdd:TIGR01575  19 EAQFAEeLANYHLCYLLARIGG---KVVGY--AGVQIVLDEAH---ILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNE 90
                          90       100
                  ....*....|....*....|.
gi 333773040  112 IRLNSASHRTEAHGFYRKLNY 132
Cdd:TIGR01575  91 IFLEVRVSNIAAQALYKKLGF 111
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
4-138 1.70e-18

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 76.28  E-value: 1.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333773040   4 LRPLSKADCPSLKEINDKALGYCVSLDLVESQFERLidDGHHYFLAYDDEdthQLVGYVHAECYETLYTDKGLNVLALAV 83
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPGREAELVDRLREDP--AAGLSLVAEDDG---EIVGHVALSPVDIDGEGPALLLGPLAV 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 333773040  84 LPDYQGKGIGRSLVAGLEALAKEEEFAFIRLNSASHRteaHGFYRKLNYVDDKTQ 138
Cdd:COG3153   76 DPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSL---LPFYERFGFRPAGEL 127
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-145 4.19e-18

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 75.80  E-value: 4.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333773040   3 MLRPLSKADCPSLKEI-NDKALGYC-------VSLDLVESQFERLIDDGHHYFLAyddEDTHQLVGYVHAECYETLYTDK 74
Cdd:COG1247    3 TIRPATPEDAPAIAAIyNEAIAEGTatfetepPSEEEREAWFAAILAPGRPVLVA---EEDGEVVGFASLGPFRPRPAYR 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333773040  75 GLNVLALAVLPDYQGKGIGRSLVAGLEALAKEEEFAFIRLNSASHRTEAHGFYRKLNYVDDKTQLRFIKKL 145
Cdd:COG1247   80 GTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKF 150
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
13-132 3.24e-15

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: 67.16  E-value: 3.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333773040   13 PSLKEINDKALGYCVSLDLVESQFERLIDDGHHYFLAYDDEdthQLVGYVhaECYETLYTDKGLNVLALAVLPDYQGKGI 92
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDG---ELVGFA--SLSIIDDEPPVGEIEGLAVAPEYRGKGI 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 333773040   93 GRSLVAGLEALAKEEEFAFIRLNSASHRTEAHGFYRKLNY 132
Cdd:pfam00583  77 GTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
42-133 1.27e-14

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 64.78  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333773040   42 DGHHYFLAYDDEdthQLVGYVHAECYETLYTdkgLNVLALAVLPDYQGKGIGRSLVAGLEALAKEEEFAFIRLNSashRT 121
Cdd:pfam13508   1 PGGRFFVAEDDG---KIVGFAALLPLDDEGA---LAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TN 71
                          90
                  ....*....|..
gi 333773040  122 EAHGFYRKLNYV 133
Cdd:pfam13508  72 RAAAFYEKLGFE 83
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
36-145 2.23e-14

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 65.46  E-value: 2.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333773040  36 FERLIDDGHHYFLAYDDEDthQLVGYVHAecyeTLYTDKGLNVLALAVLPDYQGKGIGRSLVAGLEALAKEEEFAFIRLN 115
Cdd:COG0454   25 KAMEGSLAGAEFIAVDDKG--EPIGFAGL----RRLDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELD 98
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 333773040 116 SASHRTEAHGFYRKLNYVD-----DKTQLRFIKKL 145
Cdd:COG0454   99 TLDGNPAAIRFYERLGFKEieryvAYVGGEFEKEL 133
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
60-141 1.23e-13

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 62.37  E-value: 1.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333773040  60 GYVhaeCYETLYTDKGLNVLALAVLPDYQGKGIGRSLVAGLEALAKEEEFAFIRLNSASHRTEAHGFYRKLNYVDDKTQL 139
Cdd:COG0456    1 GFA---LLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                 ..
gi 333773040 140 RF 141
Cdd:COG0456   78 NY 79
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
3-133 5.85e-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: 61.55  E-value: 5.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333773040   3 MLRPLSKADCPSLKEINDKALgycvsldlvesqferLIDDGHHYFLAYDDEdthQLVGYVHAECYEtlytDKGLNVLALA 82
Cdd:COG1246    2 TIRPATPDDVPAILELIRPYA---------------LEEEIGEFWVAEEDG---EIVGCAALHPLD----EDLAELRSLA 59
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 333773040  83 VLPDYQGKGIGRSLVAGLEALAKEEEFAFIRLNSashRTEAHGFYRKLNYV 133
Cdd:COG1246   60 VHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT---TSAAIHFYEKLGFE 107
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
41-133 5.82e-12

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 59.04  E-value: 5.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333773040  41 DDGHHYFLAYDDEdthQLVGYVHaecyetlYTDKGLNVLAL---AVLPDYQGKGIGRSLVAGLEALAKEEEFAFIRLNSa 117
Cdd:COG2153   31 DEDARHLLAYDDG---ELVATAR-------LLPPGDGEAKIgrvAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSA- 99
                         90
                 ....*....|....*.
gi 333773040 118 shRTEAHGFYRKLNYV 133
Cdd:COG2153  100 --QAHAVGFYEKLGFV 113
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
35-134 9.21e-12

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: 58.44  E-value: 9.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333773040   35 QFERLIDDGHHYFLAYDDEDthQLVGYVhaecyeTLYTDKGLNVLAlaVLPDYQGKGIGRSLVAGLEALAKEEEFAFIRL 114
Cdd:pfam13673  21 ALRERIDQGEYFFFVAFEGG--QIVGVI------ALRDRGHISLLF--VDPDYQGQGIGKALLEAVEDYAEKDGIKLSEL 90
                          90       100
                  ....*....|....*....|..
gi 333773040  115 --NSASHrteAHGFYRKLNYVD 134
Cdd:pfam13673  91 tvNASPY---AVPFYEKLGFRA 109
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
46-115 3.25e-10

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: 52.66  E-value: 3.25e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333773040  46 YFLAYDDEdthQLVGYVHAECYEtlYTDKGLNVLALAVLPDYQGKGIGRSLVAGLEALAKEEEFAFIRLN 115
Cdd:cd04301    1 FLVAEDDG---EIVGFASLSPDG--SGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
78-134 2.99e-09

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 50.68  E-value: 2.99e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 333773040  78 VLALAVLPDYQGKGIGRSLVAGLEALAKEEEFAFIRLNSASHRTEAHGFYRKLNYVD 134
Cdd:COG3393   18 ISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRP 74
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
4-133 1.57e-07

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: 48.07  E-value: 1.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333773040   4 LRPLSKADCPSLKEI-NDKAL-----GYCVSLDLVESQFERLIDD---GHHYFLAYDDEDTHQLVGYVhaECYETLYTDK 74
Cdd:COG1670   10 LRPLRPEDAEALAELlNDPEVarylpGPPYSLEEARAWLERLLADwadGGALPFAIEDKEDGELIGVV--GLYDIDRANR 87
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333773040  75 GLNvLALAVLPDYQGKGIGRSLVAGLEALAKeEEFAFIRL-------NSASHRteahgFYRKLNYV 133
Cdd:COG1670   88 SAE-IGYWLAPAYWGKGYATEALRALLDYAF-EELGLHRVeaevdpdNTASIR-----VLEKLGFR 146
PRK07757 PRK07757
N-acetyltransferase;
46-139 2.88e-07

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 46.73  E-value: 2.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333773040  46 YFLAYDDEdthQLVGYvhaeCYETLYTDKGLNVLALAVLPDYQGKGIGRSLVAGLEALAKEEE----FAFirlnsashrT 121
Cdd:PRK07757  43 FYVAEEEG---EIVGC----CALHILWEDLAEIRSLAVSEDYRGQGIGRMLVEACLEEARELGvkrvFAL---------T 106
                         90
                 ....*....|....*....
gi 333773040 122 EAHGFYRKLNYVD-DKTQL 139
Cdd:PRK07757 107 YQPEFFEKLGFREvDKEAL 125
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
33-132 8.37e-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: 45.40  E-value: 8.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333773040   33 ESQFER-LIDDGHHYFLAYDDEdthQLVGYvhAECYETLYTDKglnVLALAVLPDYQGKGIGRSLVAGLEALAKEEEFAF 111
Cdd:TIGR01575  19 EAQFAEeLANYHLCYLLARIGG---KVVGY--AGVQIVLDEAH---ILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNE 90
                          90       100
                  ....*....|....*....|.
gi 333773040  112 IRLNSASHRTEAHGFYRKLNY 132
Cdd:TIGR01575  91 IFLEVRVSNIAAQALYKKLGF 111
Eis COG4552
Predicted acetyltransferase [General function prediction only];
4-132 9.78e-06

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 43.73  E-value: 9.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333773040   4 LRPLSKADCPSLKEINDKALGYCVSLDLVESQFERLidDGHHYFLAYDDEdthQLVG---------YVHAECYETLYtdk 74
Cdd:COG4552    3 IRPLTEDDLDAFARLLAYAFGPEPDDEELEAYRPLL--EPGRVLGVFDDG---ELVGtlalypftlNVGGARVPMAG--- 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 333773040  75 glnVLALAVLPDYQGKGIGRSLVAGLEALAKEEEFAFirlnSASHRTEAhGFYRKLNY 132
Cdd:COG4552   75 ---ITGVAVAPEHRRRGVARALLREALAELRERGQPL----SALYPFEP-GFYRRFGY 124
PRK03624 PRK03624
putative acetyltransferase; Provisional
81-132 3.78e-05

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 41.07  E-value: 3.78e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 333773040  81 LAVLPDYQGKGIGRSLVAGLEALAKEEEFAFIRLNSASHRTEAHGFYRKLNY 132
Cdd:PRK03624  74 LAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGY 125
PRK13688 PRK13688
N-acetyltransferase;
81-138 6.37e-05

N-acetyltransferase;


Pssm-ID: 237470  Cd Length: 156  Bit Score: 40.38  E-value: 6.37e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 333773040  81 LAVLPDYQGKGIGRSLVagleALAKEEEFAfIRLNSashRTEAHGFYRKLNYVDDKTQ 138
Cdd:PRK13688  85 LEVLPKYQNRGYGEMLV----DFAKSFQLP-IKTIA---RNKSKDFWLKLGFTPVEYK 134
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
80-132 7.05e-04

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: 36.54  E-value: 7.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 333773040   80 ALAVLPDYQGKGIGRSLVAGL-EALAKEEE--FAFIRLNSashrTEAHGFYRKLNY 132
Cdd:pfam08445  26 ALQTLPEHRRRGLGSRLVAALaRGIAERGItpFAVVVAGN----TPSRRLYEKLGF 77
 
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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