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Conserved domains on  [gi|117209782|gb|ABK32774|]
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BastaR [Silencing vector p3UTR12850S]

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
PPT_acetyltrans super family cl47276
phosphinothricin N-acetyltransferase; Phosphinothricin N-acetyltransferase (PAT) provides ...
 1-168 1.02e-122

phosphinothricin N-acetyltransferase; Phosphinothricin N-acetyltransferase (PAT) provides resistance to producers of the natural product phosphinothricin, non-proteinogenic amino acid antibiotic.


The actual alignment was detected with superfamily member NF040502:

Pssm-ID: 439723  Cd Length: 183  Bit Score: 343.51  E-value: 1.02e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117209782   1 MSPERRPADIRRATEADMPAVCTIVNHYIETSTVNFRTS-RRKQEWTDDLVRLRERYPWLVAEVDGEVAGIAYAGPWKAR 79
Cdd:NF040502   1 MSPERRPEGIRLATAADMPAVCEIVNHYIETSTVNFRTEpQLPQEWEDDLARLRERYPWLVAEVGGEVAGIAYAGPWKAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117209782  80 NAYDWTAESTVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRGMLRAAGFKHGNWHD 159
Cdd:NF040502  81 NAYDWTTESTVYVSDRHQRRGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRLHEALGYESRGRLRAAGHKHGGWHD 160


                 ....*....
gi 117209782 160 VGFWQLDFS 168
Cdd:NF040502 161 VGFWQRDFV 169
 
Name Accession Description Interval E-value
PPT_acetyltrans NF040502
phosphinothricin N-acetyltransferase; Phosphinothricin N-acetyltransferase (PAT) provides ...
 1-168 1.02e-122

phosphinothricin N-acetyltransferase; Phosphinothricin N-acetyltransferase (PAT) provides resistance to producers of the natural product phosphinothricin, non-proteinogenic amino acid antibiotic.


Pssm-ID: 439723  Cd Length: 183  Bit Score: 343.51  E-value: 1.02e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117209782   1 MSPERRPADIRRATEADMPAVCTIVNHYIETSTVNFRTS-RRKQEWTDDLVRLRERYPWLVAEVDGEVAGIAYAGPWKAR 79
Cdd:NF040502   1 MSPERRPEGIRLATAADMPAVCEIVNHYIETSTVNFRTEpQLPQEWEDDLARLRERYPWLVAEVGGEVAGIAYAGPWKAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117209782  80 NAYDWTAESTVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRGMLRAAGFKHGNWHD 159
Cdd:NF040502  81 NAYDWTTESTVYVSDRHQRRGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRLHEALGYESRGRLRAAGHKHGGWHD 160


                 ....*....
gi 117209782 160 VGFWQLDFS 168
Cdd:NF040502 161 VGFWQRDFV 169
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
10-166 8.83e-51

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 160.55  E-value: 8.83e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117209782  10 IRRATEADMPAVCTIVNHYIETSTVNF----RTSRRKQEWTDDlvRLRERYPWLVAEVDGEVAGIAYAGPWKARNAYDWT 85
Cdd:COG1247    4 IRPATPEDAPAIAAIYNEAIAEGTATFetepPSEEEREAWFAA--ILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117209782  86 AESTVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRGMLRAAGFKHGNWHDVGFWQL 165
Cdd:COG1247   82 AEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQK 161


                 .
gi 117209782 166 D 166
Cdd:COG1247  162 R 162
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 52-141 6.17e-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: 67.54  E-value: 6.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117209782   52 LRERYPWLVAEVDGEVAGiaYAGPWKARNAYDWTAESTVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDP 131
Cdd:pfam00583  29 EDASEGFFVAEEDGELVG--FASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLA 106

                          90
                  ....*....|
gi 117209782  132 SVRMHEALGY 141
Cdd:pfam00583 107 AIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 58-122 1.38e-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: 46.50  E-value: 1.38e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117209782  58 WLVAEVDGEVAGIAYAGPWkarNAYDWTAE-STVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVV 122
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPD---GSGGDTAYiGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
PRK03624 PRK03624
putative acetyltransferase; Provisional
 59-141 1.05e-06

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 46.08  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117209782  59 LVAEVDGEVAGIAYAGpwkarnaYD----WtaestVY---VSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDP 131
Cdd:PRK03624  48 LVAEVGGEVVGTVMGG-------YDghrgW-----AYylaVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDA 115

                         90
                 ....*....|
gi 117209782 132 SVRMHEALGY 141
Cdd:PRK03624 116 VLGFYEALGY 125
 
Name Accession Description Interval E-value
PPT_acetyltrans NF040502
phosphinothricin N-acetyltransferase; Phosphinothricin N-acetyltransferase (PAT) provides ...
 1-168 1.02e-122

phosphinothricin N-acetyltransferase; Phosphinothricin N-acetyltransferase (PAT) provides resistance to producers of the natural product phosphinothricin, non-proteinogenic amino acid antibiotic.


Pssm-ID: 439723  Cd Length: 183  Bit Score: 343.51  E-value: 1.02e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117209782   1 MSPERRPADIRRATEADMPAVCTIVNHYIETSTVNFRTS-RRKQEWTDDLVRLRERYPWLVAEVDGEVAGIAYAGPWKAR 79
Cdd:NF040502   1 MSPERRPEGIRLATAADMPAVCEIVNHYIETSTVNFRTEpQLPQEWEDDLARLRERYPWLVAEVGGEVAGIAYAGPWKAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117209782  80 NAYDWTAESTVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRGMLRAAGFKHGNWHD 159
Cdd:NF040502  81 NAYDWTTESTVYVSDRHQRRGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRLHEALGYESRGRLRAAGHKHGGWHD 160


                 ....*....
gi 117209782 160 VGFWQLDFS 168
Cdd:NF040502 161 VGFWQRDFV 169
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
10-166 8.83e-51

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 160.55  E-value: 8.83e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117209782  10 IRRATEADMPAVCTIVNHYIETSTVNF----RTSRRKQEWTDDlvRLRERYPWLVAEVDGEVAGIAYAGPWKARNAYDWT 85
Cdd:COG1247    4 IRPATPEDAPAIAAIYNEAIAEGTATFetepPSEEEREAWFAA--ILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117209782  86 AESTVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRGMLRAAGFKHGNWHDVGFWQL 165
Cdd:COG1247   82 AEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQK 161


                 .
gi 117209782 166 D 166
Cdd:COG1247  162 R 162
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 52-141 6.17e-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: 67.54  E-value: 6.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117209782   52 LRERYPWLVAEVDGEVAGiaYAGPWKARNAYDWTAESTVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDP 131
Cdd:pfam00583  29 EDASEGFFVAEEDGELVG--FASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLA 106

                          90
                  ....*....|
gi 117209782  132 SVRMHEALGY 141
Cdd:pfam00583 107 AIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
10-148 1.55e-14

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 67.03  E-value: 1.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117209782  10 IRRATEADMPAVCTIvnhyietstvnFRTSRRKQEWTDDLVRLRERYP---WLVAEVDGEVAGIAYAGPWKARNAYDWTA 86
Cdd:COG3153    1 IRPATPEDAEAIAAL-----------LRAAFGPGREAELVDRLREDPAaglSLVAEDDGEIVGHVALSPVDIDGEGPALL 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 117209782  87 ESTVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAViglPNDPSVRMHEALGYAPRGMLR 148
Cdd:COG3153   70 LGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLL---GDPSLLPFYERFGFRPAGELG 128
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 10-143 2.29e-12

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: 61.16  E-value: 2.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117209782  10 IRRATEADMPAVCTIVNHYIetstvnfrtsrrkqewtddLVRLRERYpwLVAEVDGEVAGIAYAGPWKARnaydwTAE-S 88
Cdd:COG1246    3 IRPATPDDVPAILELIRPYA-------------------LEEEIGEF--WVAEEDGEIVGCAALHPLDED-----LAElR 56

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 117209782  89 TVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAvigLPNDPSVRMHEALGYAP 143
Cdd:COG1246   57 SLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFL---LTTSAAIHFYEKLGFEE 108
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
10-159 6.34e-11

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 57.76  E-value: 6.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117209782   10 IRRATEADMPAVCTIVNHYIETSTVNFRTSRRKQEWTDDLVRLR---ERYPWLVAEvDGEVAGIAYAGPWKARnaYDWTA 86
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAEDRVNPAFTQEYAHSSIEEFETFLAAYlspGEIVFGVAE-SDRLIGYATLRQFDYV--KTHKA 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 117209782   87 ESTVYVSpRHQRTGLGSTLYTHLLKSLEA-QGFKSVVAVIGLPNDPSVRMHEALGYAPRGMLRAAGFKHGNWHD 159
Cdd:pfam13420  78 ELSFYVV-KNNDEGINRELINAIIQYARKnQNIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKKNGRWID 150
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 10-165 1.58e-10

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 56.93  E-value: 1.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117209782  10 IRRATEADMPAVCTIVNH-----YIETSTVNFRTSRRKQEWTDDLVRLRERYPWLVAE-VDGEVAGIAYAGPWkarNAYD 83
Cdd:COG1670   10 LRPLRPEDAEALAELLNDpevarYLPGPPYSLEEARAWLERLLADWADGGALPFAIEDkEDGELIGVVGLYDI---DRAN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117209782  84 WTAESTVYVSPRHQRTGLGSTLYTHLLK-SLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRGMLRAAGFKHGNWHDVGF 162
Cdd:COG1670   87 RSAEIGYWLAPAYWGKGYATEALRALLDyAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHVL 166


                 ...
gi 117209782 163 WQL 165
Cdd:COG1670  167 YSL 169
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 10-143 3.40e-09

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 52.75  E-value: 3.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117209782  10 IRRATEADMPAVCTIvnhyietstvnfRTSRRKQEWTDDLVRLRErypWLVAEVDGEVAGIAYAGPWKarnayDWTAE-S 88
Cdd:COG0454    3 IRKATPEDINFILLI------------EALDAELKAMEGSLAGAE---FIAVDDKGEPIGFAGLRRLD-----DKVLElK 62

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 117209782  89 TVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAP 143
Cdd:COG0454   63 RLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKE 117
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
66-153 8.53e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 47.60  E-value: 8.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117209782  66 EVAGIAYAGPWkarnAYDWTAESTVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRG 145
Cdd:COG3393    1 ELVAMAGVRAE----SPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVG 76


                 ....*...
gi 117209782 146 MLRAAGFK 153
Cdd:COG3393   77 EYATVLFR 84
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 58-122 1.38e-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: 46.50  E-value: 1.38e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117209782  58 WLVAEVDGEVAGIAYAGPWkarNAYDWTAE-STVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVV 122
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPD---GSGGDTAYiGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 89-145 3.33e-07

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 46.19  E-value: 3.33e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 117209782  89 TVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRG 145
Cdd:COG0456   18 DLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVG 74
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 54-141 4.77e-07

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 45.52  E-value: 4.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117209782   54 ERYPWLVAEVDGEVAGIAYAGPwkaRNAYDWTAESTVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAvigLPNDPSV 133
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLP---LDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLEL---ETTNRAA 74


                  ....*...
gi 117209782  134 RMHEALGY 141
Cdd:pfam13508  75 AFYEKLGF 82
PRK03624 PRK03624
putative acetyltransferase; Provisional
 59-141 1.05e-06

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 46.08  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117209782  59 LVAEVDGEVAGIAYAGpwkarnaYD----WtaestVY---VSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDP 131
Cdd:PRK03624  48 LVAEVGGEVVGTVMGG-------YDghrgW-----AYylaVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDA 115

                         90
                 ....*....|
gi 117209782 132 SVRMHEALGY 141
Cdd:PRK03624 116 VLGFYEALGY 125
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 88-141 9.98e-06

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: 41.93  E-value: 9.98e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 117209782   88 STVYVSPRHQRTGLGSTLYTHLLKSLEAQGfKSVVAVIGLPNDPSVRMHEALGY 141
Cdd:pfam08445  25 GALQTLPEHRRRGLGSRLVAALARGIAERG-ITPFAVVVAGNTPSRRLYEKLGF 77
PRK12308 PRK12308
argininosuccinate lyase;
10-128 7.71e-03

argininosuccinate lyase;


Pssm-ID: 183425 [Multi-domain]  Cd Length: 614  Bit Score: 36.30  E-value: 7.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117209782  10 IRRATEADMPAVCTIVNHYIETSTvNFRTSRrkqewtDDLVRLRERYPwlVAEVDGEVAGIAyagpwkARNAYD-WTAE- 87
Cdd:PRK12308 466 VRPARLTDIDAIEGMVAYWAGLGE-NLPRSR------NELVRDIGSFA--VAEHHGEVTGCA------SLYIYDsGLAEi 530

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 117209782  88 STVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLP 128
Cdd:PRK12308 531 RSLGVEAGWQVQGQGSALVQYLVEKARQMAIKKVFVLTRVP 571
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 54-141 9.55e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 34.90  E-value: 9.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117209782  54 ERYPWLVAEVDGEVAGIAYAgpwkaRNAYDwtaESTVY---VSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPND 130
Cdd:PRK09491  38 ERYLNLKLTVNGQMAAFAIT-----QVVLD---EATLFniaVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNA 109

                         90
                 ....*....|.
gi 117209782 131 PSVRMHEALGY 141
Cdd:PRK09491 110 AAIALYESLGF 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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