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Conserved domains on  [gi|17864390|ref|NP_524779|]
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separation anxiety [Drosophila melanogaster]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10456837)

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
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
24-129 2.79e-18

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: 2.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864390    24 TVVFPVSYNDKFYVDVLEAGELAKLAYYNDIVVGAVCCRIDNTENqRRLYIMTLGCLSPYRRLGIGTVMFEHIMNFAEKD 103
Cdd:pfam00583  13 PEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEP-PVGEIEGLAVAPEYRGKGIGTALLQALLEWARER 91
                          90       100
                  ....*....|....*....|....*.
gi 17864390   104 GnFDSIFLHVQINNNGAIEFYKKFGF 129
Cdd:pfam00583  92 G-CERIFLEVAADNLAAIALYEKLGF 116
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
24-129 2.79e-18

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: 2.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864390    24 TVVFPVSYNDKFYVDVLEAGELAKLAYYNDIVVGAVCCRIDNTENqRRLYIMTLGCLSPYRRLGIGTVMFEHIMNFAEKD 103
Cdd:pfam00583  13 PEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEP-PVGEIEGLAVAPEYRGKGIGTALLQALLEWARER 91
                          90       100
                  ....*....|....*....|....*.
gi 17864390   104 GnFDSIFLHVQINNNGAIEFYKKFGF 129
Cdd:pfam00583  92 G-CERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
57-155 6.25e-18

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 74.69  E-value: 6.25e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864390  57 GAVCCRIDntENQRRLYIMTLGCLSPYRRLGIGTVMFEHIMNFAEKDGnFDSIFLHVQINNNGAIEFYKKFGFEIVDTKE 136
Cdd:COG0456   1 GFALLGLV--DGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERG-ARRLRLEVREDNEAAIALYEKLGFEEVGERP 77
                        90
                ....*....|....*....
gi 17864390 137 QYYkriePADAHVLQKTLR 155
Cdd:COG0456  78 NYY----GDDALVMEKELA 92
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
26-140 1.85e-11

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: 58.49  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864390    26 VFPVSYNDKFYVDVLEAGELA-KLAYYNDIVVGAVCCRIDNTENQrrlyIMTLGCLSPYRRLGIGTVMFEHIMNFAEKDG 104
Cdd:TIGR01575  12 AFAFPWTEAQFAEELANYHLCyLLARIGGKVVGYAGVQIVLDEAH----ILNIAVKPEYQGQGIGRALLRELIDEAKGRG 87
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 17864390   105 nFDSIFLHVQINNNGAIEFYKKFGFEIVDTKEQYYK 140
Cdd:TIGR01575  88 -VNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYP 122
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
48-112 3.09e-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: 48.43  E-value: 3.09e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17864390  48 LAYYNDIVVGAVCCRIDNTENqRRLYIMTLGCLSPYRRLGIGTVMFEHIMNFAEKDGnFDSIFLH 112
Cdd:cd04301   3 VAEDDGEIVGFASLSPDGSGG-DTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERG-AKRLRLE 65
PRK10140 PRK10140
N-acetyltransferase;
48-153 7.48e-07

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 46.90  E-value: 7.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864390   48 LAYYNDIVVGAVCcrIDNTENQRRLYIMTLG-CL-SPYRRLGIGTVMFEHIMNFAEKDGNFDSIFLHVQINNNGAIEFYK 125
Cdd:PRK10140  55 VACIDGDVVGHLT--IDVQQRPRRSHVADFGiCVdSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYK 132
                         90       100
                 ....*....|....*....|....*....
gi 17864390  126 KFGFEIVDTKEQYYKRI-EPADAHVLQKT 153
Cdd:PRK10140 133 KYGFEIEGTGKKYALRNgEYVDAYYMARV 161
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
24-129 2.79e-18

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: 2.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864390    24 TVVFPVSYNDKFYVDVLEAGELAKLAYYNDIVVGAVCCRIDNTENqRRLYIMTLGCLSPYRRLGIGTVMFEHIMNFAEKD 103
Cdd:pfam00583  13 PEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEP-PVGEIEGLAVAPEYRGKGIGTALLQALLEWARER 91
                          90       100
                  ....*....|....*....|....*.
gi 17864390   104 GnFDSIFLHVQINNNGAIEFYKKFGF 129
Cdd:pfam00583  92 G-CERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
57-155 6.25e-18

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 74.69  E-value: 6.25e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864390  57 GAVCCRIDntENQRRLYIMTLGCLSPYRRLGIGTVMFEHIMNFAEKDGnFDSIFLHVQINNNGAIEFYKKFGFEIVDTKE 136
Cdd:COG0456   1 GFALLGLV--DGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERG-ARRLRLEVREDNEAAIALYEKLGFEEVGERP 77
                        90
                ....*....|....*....
gi 17864390 137 QYYkriePADAHVLQKTLR 155
Cdd:COG0456  78 NYY----GDDALVMEKELA 92
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
48-155 7.67e-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: 67.71  E-value: 7.67e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864390  48 LAYYNDIVVGavCCRIDNTENqRRLYIMTLGCLSPYRRLGIGTVMFEHIMNFAEKDGnFDSIFLHVqinNNGAIEFYKKF 127
Cdd:COG1246  32 VAEEDGEIVG--CAALHPLDE-DLAELRSLAVHPDYRGRGIGRRLLEALLAEARELG-LKRLFLLT---TSAAIHFYEKL 104
                        90       100
                ....*....|....*....|....*...
gi 17864390 128 GFEIVDTKEQYYKRIEPADAHVLQKTLR 155
Cdd:COG1246 105 GFEEIDKEDLPYAKVWQRDSVVMEKDLE 132
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
12-154 1.66e-13

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 64.34  E-value: 1.66e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864390  12 TPHNIKQLKKLNTVVFPVSYNDKFyVDVLEAGELAKL---AYYNDIVVGAVCC-RIDNTENQRRLYIMTLGCLSPYRRLG 87
Cdd:COG3153   5 TPEDAEAIAALLRAAFGPGREAEL-VDRLREDPAAGLslvAEDDGEIVGHVALsPVDIDGEGPALLLGPLAVDPEYRGQG 83
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17864390  88 IGTVMFEHIMNFAEKDGnFDSIFLHVqinNNGAIEFYKKFGFEIVDTkeqyYKRIEPADAHVLQKTL 154
Cdd:COG3153  84 IGRALMRAALEAARERG-ARAVVLLG---DPSLLPFYERFGFRPAGE----LGLTLGPDEVFLAKEL 142
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
83-154 2.85e-12

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 61.55  E-value: 2.85e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17864390  83 YRRLGIGTVMFEHIMNFAEKDGnFDSIFLHVQINNNGAIEFYKKFGFEIVDT-KEQYYKRIEPADAHVLQKTL 154
Cdd:COG1247  92 ARGRGIGRALLEALIERARARG-YRRLVAVVLADNEASIALYEKLGFEEVGTlPEVGFKFGRWLDLVLMQKRL 163
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
40-157 4.53e-12

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 60.45  E-value: 4.53e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864390  40 LEAGELAKLAYYNDIVVGAVCCRIdntENQRRLYIMTLGCLSPYRRLGIGTVMFEHIMNFAEKDGnFDSIFLHVQINNNG 119
Cdd:COG0454  30 SLAGAEFIAVDDKGEPIGFAGLRR---LDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERG-CTALELDTLDGNPA 105
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 17864390 120 AIEFYKKFGFEIVDtkeqyykRIEPADAHVLQKTLRRT 157
Cdd:COG0454 106 AIRFYERLGFKEIE-------RYVAYVGGEFEKELSLS 136
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
26-140 1.85e-11

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: 58.49  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864390    26 VFPVSYNDKFYVDVLEAGELA-KLAYYNDIVVGAVCCRIDNTENQrrlyIMTLGCLSPYRRLGIGTVMFEHIMNFAEKDG 104
Cdd:TIGR01575  12 AFAFPWTEAQFAEELANYHLCyLLARIGGKVVGYAGVQIVLDEAH----ILNIAVKPEYQGQGIGRALLRELIDEAKGRG 87
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 17864390   105 nFDSIFLHVQINNNGAIEFYKKFGFEIVDTKEQYYK 140
Cdd:TIGR01575  88 -VNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYP 122
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
48-131 6.95e-11

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 55.92  E-value: 6.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864390    48 LAYYNDIVVGavCCRIDNTENQRRLYIMTLGCLSPYRRLGIGTVMFEHIMnFAEKDGNFDSIFLHvqiNNNGAIEFYKKF 127
Cdd:pfam13508   7 VAEDDGKIVG--FAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAE-AAAKEGGIKLLELE---TTNRAAAFYEKL 80

                  ....
gi 17864390   128 GFEI 131
Cdd:pfam13508  81 GFEE 84
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
48-132 3.77e-10

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 55.19  E-value: 3.77e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864390  48 LAYYNDIVVGavCCRIDNTENQ----RRLYImtlgcLSPYRRLGIGTVMFEHIMNFAEKDGnFDSIFLHVQINnngAIEF 123
Cdd:COG2153  38 LAYDDGELVA--TARLLPPGDGeakiGRVAV-----LPEYRGQGLGRALMEAAIEEARERG-ARRIVLSAQAH---AVGF 106

                ....*....
gi 17864390 124 YKKFGFEIV 132
Cdd:COG2153 107 YEKLGFVPV 115
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
48-112 3.09e-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: 48.43  E-value: 3.09e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17864390  48 LAYYNDIVVGAVCCRIDNTENqRRLYIMTLGCLSPYRRLGIGTVMFEHIMNFAEKDGnFDSIFLH 112
Cdd:cd04301   3 VAEDDGEIVGFASLSPDGSGG-DTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERG-AKRLRLE 65
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
52-141 1.15e-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: 49.23  E-value: 1.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864390  52 NDIVVGAVCCRIDNTENQRrlyiMTLG-CLSP-YRRLGIGTVMFEHIMNFAEKDGNFDSIFLHVQINNNGAIEFYKKFGF 129
Cdd:COG1670  70 DGELIGVVGLYDIDRANRS----AEIGyWLAPaYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGF 145
                        90
                ....*....|..
gi 17864390 130 EIVDTKEQYYKR 141
Cdd:COG1670 146 RLEGTLRDALVI 157
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
48-138 2.61e-07

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: 47.27  E-value: 2.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864390    48 LAYYNDIVVGAvcCRIDNTENQRRLYImtlgcLSPYRRLGIGTVMFEHIMNFAEKDG-NFDSIFLHVQINnngAIEFYKK 126
Cdd:pfam13673  35 VAFEGGQIVGV--IALRDRGHISLLFV-----DPDYQGQGIGKALLEAVEDYAEKDGiKLSELTVNASPY---AVPFYEK 104
                          90
                  ....*....|..
gi 17864390   127 FGFEIVDtKEQY 138
Cdd:pfam13673 105 LGFRATG-PEQE 115
PRK10140 PRK10140
N-acetyltransferase;
48-153 7.48e-07

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 46.90  E-value: 7.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864390   48 LAYYNDIVVGAVCcrIDNTENQRRLYIMTLG-CL-SPYRRLGIGTVMFEHIMNFAEKDGNFDSIFLHVQINNNGAIEFYK 125
Cdd:PRK10140  55 VACIDGDVVGHLT--IDVQQRPRRSHVADFGiCVdSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYK 132
                         90       100
                 ....*....|....*....|....*....
gi 17864390  126 KFGFEIVDTKEQYYKRI-EPADAHVLQKT 153
Cdd:PRK10140 133 KYGFEIEGTGKKYALRNgEYVDAYYMARV 161
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
83-134 1.55e-05

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 41.43  E-value: 1.55e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 17864390  83 YRRLGIGTVMFEHIMNFAEKDGnFDSIFLHVQINNNGAIEFYKKFGFEIVDT 134
Cdd:COG3393  27 YRGRGLASALVAALAREALARG-ARTPFLYVDADNPAARRLYERLGFRPVGE 77
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
87-149 8.79e-05

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 40.81  E-value: 8.79e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17864390    87 GIGTVMFEHIMNFAEKDGNFDSIFLHVQINNNGAIEFYKKFGFEIV-DTKEQYYKRIEPADAHV 149
Cdd:pfam13420  90 GINRELINAIIQYARKNQNIENLEACIASNNINAIVFLKAIGFEWLgIERNAIKKNGRWIDMMW 153
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
71-136 1.18e-03

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: 1.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17864390    71 RLYIMTLG--CLSP-YRRLGIGTV----MFEHImnfAEKDgnfDSIFLHVQINNNGAIEFYKKFGFEIVDTKE 136
Cdd:pfam08445  18 RLPGGELGalQTLPeHRRRGLGSRlvaaLARGI---AERG---ITPFAVVVAGNTPSRRLYEKLGFRKIDETY 84
COG5628 COG5628
Predicted acetyltransferase [General function prediction only];
80-149 2.60e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 444356  Cd Length: 163  Bit Score: 36.84  E-value: 2.60e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17864390  80 LSPYRRLGIGTVMFEHImnFAEKDGNFdsiFLHVQINNNGAIEFYKKfgfeIVD--TKEQYYKRIEPADAHV 149
Cdd:COG5628  90 LRKYRRKGIGKRAAHEL--FKRFPGRW---EVKQLEANVPAVAFWRK----VIGeyTGGAYTEEERYIDGRP 152
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
83-139 9.29e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 34.90  E-value: 9.29e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17864390   83 YRRLGIGTVMFEHIMNFAEKDGNFdSIFLHVQINNNGAIEFYKKFGFEIVDTKEQYY 139
Cdd:PRK09491  75 YQRQGLGRALLEHLIDELEKRGVA-TLWLEVRASNAAAIALYESLGFNEVTIRRNYY 130
 
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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