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Conserved domains on  [gi|515722280|ref|WP_017154880|]
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MULTISPECIES: phosphinothricin N-acetyltransferase [Bacteria]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PPT_acetyltrans NF040502
phosphinothricin N-acetyltransferase; Phosphinothricin N-acetyltransferase (PAT) provides ...
 1-169 4.38e-128

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: 357.38  E-value: 4.38e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722280   1 MSPERRPADIRRATEADMPAVCTIVNHYIETSTVNFRTEPQEPQEWTDDLVRLRERYPWLVAEVDGEVAGIAYAGPWKAR 80
Cdd:NF040502   1 MSPERRPEGIRLATAADMPAVCEIVNHYIETSTVNFRTEPQLPQEWEDDLARLRERYPWLVAEVGGEVAGIAYAGPWKAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722280  81 NAYDWTAESTVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRGMLRAAGFKHGNWHD 160
Cdd:NF040502  81 NAYDWTTESTVYVSDRHQRRGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRLHEALGYESRGRLRAAGHKHGGWHD 160


                 ....*....
gi 515722280 161 VGFWQLDFS 169
Cdd:NF040502 161 VGFWQRDFV 169
 
Name Accession Description Interval E-value
PPT_acetyltrans NF040502
phosphinothricin N-acetyltransferase; Phosphinothricin N-acetyltransferase (PAT) provides ...
 1-169 4.38e-128

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: 357.38  E-value: 4.38e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722280   1 MSPERRPADIRRATEADMPAVCTIVNHYIETSTVNFRTEPQEPQEWTDDLVRLRERYPWLVAEVDGEVAGIAYAGPWKAR 80
Cdd:NF040502   1 MSPERRPEGIRLATAADMPAVCEIVNHYIETSTVNFRTEPQLPQEWEDDLARLRERYPWLVAEVGGEVAGIAYAGPWKAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722280  81 NAYDWTAESTVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRGMLRAAGFKHGNWHD 160
Cdd:NF040502  81 NAYDWTTESTVYVSDRHQRRGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRLHEALGYESRGRLRAAGHKHGGWHD 160


                 ....*....
gi 515722280 161 VGFWQLDFS 169
Cdd:NF040502 161 VGFWQRDFV 169
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
10-167 4.41e-55

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 171.72  E-value: 4.41e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722280  10 IRRATEADMPAVCTIVNHYIETSTVNFRTEPQEPQEWTDDLV-RLRERYPWLVAEVDGEVAGIAYAGPWKARNAYDWTAE 88
Cdd:COG1247    4 IRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAaILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRGTAE 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515722280  89 STVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRGMLRAAGFKHGNWHDVGFWQLD 167
Cdd:COG1247   84 ESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQKR 162
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 24-142 1.44e-16

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: 71.78  E-value: 1.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722280   24 IVNHYIETSTVNFRTEPQEPQEWTDDlvrlRERYPWLVAEVDGEVAGiaYAGPWKARNAYDWTAESTVYVSPRHQRTGLG 103
Cdd:pfam00583   4 LYELLSEEFPEPWPDEPLDLLEDWDE----DASEGFFVAEEDGELVG--FASLSIIDDEPPVGEIEGLAVAPEYRGKGIG 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 515722280  104 STLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGY 142
Cdd:pfam00583  78 TALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 59-123 7.84e-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: 47.27  E-value: 7.84e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515722280  59 WLVAEVDGEVAGIAYAGPWkarNAYDWTAE-STVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVV 123
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPD---GSGGDTAYiGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
PRK03624 PRK03624
putative acetyltransferase; Provisional
 60-142 7.86e-07

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 46.46  E-value: 7.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722280  60 LVAEVDGEVAGIAYAGpwkarnaYD----WtaestVY---VSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDP 132
Cdd:PRK03624  48 LVAEVGGEVVGTVMGG-------YDghrgW-----AYylaVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDA 115

                         90
                 ....*....|
gi 515722280 133 SVRMHEALGY 142
Cdd:PRK03624 116 VLGFYEALGY 125
 
Name Accession Description Interval E-value
PPT_acetyltrans NF040502
phosphinothricin N-acetyltransferase; Phosphinothricin N-acetyltransferase (PAT) provides ...
 1-169 4.38e-128

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: 357.38  E-value: 4.38e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722280   1 MSPERRPADIRRATEADMPAVCTIVNHYIETSTVNFRTEPQEPQEWTDDLVRLRERYPWLVAEVDGEVAGIAYAGPWKAR 80
Cdd:NF040502   1 MSPERRPEGIRLATAADMPAVCEIVNHYIETSTVNFRTEPQLPQEWEDDLARLRERYPWLVAEVGGEVAGIAYAGPWKAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722280  81 NAYDWTAESTVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRGMLRAAGFKHGNWHD 160
Cdd:NF040502  81 NAYDWTTESTVYVSDRHQRRGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRLHEALGYESRGRLRAAGHKHGGWHD 160


                 ....*....
gi 515722280 161 VGFWQLDFS 169
Cdd:NF040502 161 VGFWQRDFV 169
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
10-167 4.41e-55

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 171.72  E-value: 4.41e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722280  10 IRRATEADMPAVCTIVNHYIETSTVNFRTEPQEPQEWTDDLV-RLRERYPWLVAEVDGEVAGIAYAGPWKARNAYDWTAE 88
Cdd:COG1247    4 IRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAaILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRGTAE 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515722280  89 STVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRGMLRAAGFKHGNWHDVGFWQLD 167
Cdd:COG1247   84 ESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQKR 162
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 24-142 1.44e-16

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: 71.78  E-value: 1.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722280   24 IVNHYIETSTVNFRTEPQEPQEWTDDlvrlRERYPWLVAEVDGEVAGiaYAGPWKARNAYDWTAESTVYVSPRHQRTGLG 103
Cdd:pfam00583   4 LYELLSEEFPEPWPDEPLDLLEDWDE----DASEGFFVAEEDGELVG--FASLSIIDDEPPVGEIEGLAVAPEYRGKGIG 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 515722280  104 STLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGY 142
Cdd:pfam00583  78 TALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
10-149 2.53e-14

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 66.65  E-value: 2.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722280  10 IRRATEADMPAVCTIVNHYIetstvnfrtepqePQEWTDDLV-RLRERYP---WLVAEVDGEVAGIAYAGPWKARNAYDW 85
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAF-------------GPGREAELVdRLREDPAaglSLVAEDDGEIVGHVALSPVDIDGEGPA 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515722280  86 TAESTVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAViglPNDPSVRMHEALGYAPRGMLR 149
Cdd:COG3153   68 LLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLL---GDPSLLPFYERFGFRPAGELG 128
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 10-144 1.80e-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: 1.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722280  10 IRRATEADMPAVCTIVNHYIetstvnfrtepqepqewtddLVRLRERYpwLVAEVDGEVAGIAYAGPWKARnaydwTAE- 88
Cdd:COG1246    3 IRPATPDDVPAILELIRPYA--------------------LEEEIGEF--WVAEEDGEIVGCAALHPLDED-----LAEl 55

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515722280  89 STVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAvigLPNDPSVRMHEALGYAP 144
Cdd:COG1246   56 RSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFL---LTTSAAIHFYEKLGFEE 108
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 10-166 3.22e-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: 56.16  E-value: 3.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722280  10 IRRATEADMPAVCTIVNH-YIETSTVNFRTEPQEPQEWTDDLVRL---RERYPWLVAE-VDGEVAGIAYAGPWkarNAYD 84
Cdd:COG1670   10 LRPLRPEDAEALAELLNDpEVARYLPGPPYSLEEARAWLERLLADwadGGALPFAIEDkEDGELIGVVGLYDI---DRAN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722280  85 WTAESTVYVSPRHQRTGLGSTLYTHLLK-SLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRGMLRAAGFKHGNWHDVGF 163
Cdd:COG1670   87 RSAEIGYWLAPAYWGKGYATEALRALLDyAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHVL 166


                 ...
gi 515722280 164 WQL 166
Cdd:COG1670  167 YSL 169
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
10-160 4.31e-10

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 55.45  E-value: 4.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722280   10 IRRATEADMPAVCTIVNHYIETSTVNFRT-EPQepQEWTDDLVRLR---ERYPWLVAEvDGEVAGIAYAGPWKARnaYDW 85
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAEDRVNPAFTQEYaHSS--IEEFETFLAAYlspGEIVFGVAE-SDRLIGYATLRQFDYV--KTH 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515722280   86 TAESTVYVSpRHQRTGLGSTLYTHLLKSLEA-QGFKSVVAVIGLPNDPSVRMHEALGYAPRGMLRAAGFKHGNWHD 160
Cdd:pfam13420  76 KAELSFYVV-KNNDEGINRELINAIIQYARKnQNIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKKNGRWID 150
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 10-144 2.76e-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: 2.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722280  10 IRRATEADMPAVCTIvnhyietstvnfrtEPQEPQ-EWTDDLVRLRErypWLVAEVDGEVAGIAYAGPWKarnayDWTAE 88
Cdd:COG0454    3 IRKATPEDINFILLI--------------EALDAElKAMEGSLAGAE---FIAVDDKGEPIGFAGLRRLD-----DKVLE 60

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515722280  89 -STVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAP 144
Cdd:COG0454   61 lKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKE 117
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
67-154 4.51e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 48.37  E-value: 4.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722280  67 EVAGIAYAGPWkarnAYDWTAESTVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRG 146
Cdd:COG3393    1 ELVAMAGVRAE----SPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVG 76


                 ....*...
gi 515722280 147 MLRAAGFK 154
Cdd:COG3393   77 EYATVLFR 84
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 59-123 7.84e-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: 47.27  E-value: 7.84e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515722280  59 WLVAEVDGEVAGIAYAGPWkarNAYDWTAE-STVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVV 123
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPD---GSGGDTAYiGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 90-146 2.11e-07

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 46.96  E-value: 2.11e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515722280  90 TVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRG 146
Cdd:COG0456   18 DLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVG 74
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 55-142 2.98e-07

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 46.29  E-value: 2.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722280   55 ERYPWLVAEVDGEVAGIAYAGPwkaRNAYDWTAESTVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAvigLPNDPSV 134
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLP---LDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLEL---ETTNRAA 74


                  ....*...
gi 515722280  135 RMHEALGY 142
Cdd:pfam13508  75 AFYEKLGF 82
PRK03624 PRK03624
putative acetyltransferase; Provisional
 60-142 7.86e-07

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 46.46  E-value: 7.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722280  60 LVAEVDGEVAGIAYAGpwkarnaYD----WtaestVY---VSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDP 132
Cdd:PRK03624  48 LVAEVGGEVVGTVMGG-------YDghrgW-----AYylaVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDA 115

                         90
                 ....*....|
gi 515722280 133 SVRMHEALGY 142
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. ...
 89-142 6.07e-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: 42.70  E-value: 6.07e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 515722280   89 STVYVSPRHQRTGLGSTLYTHLLKSLEAQGfKSVVAVIGLPNDPSVRMHEALGY 142
Cdd:pfam08445  25 GALQTLPEHRRRGLGSRLVAALARGIAERG-ITPFAVVVAGNTPSRRLYEKLGF 77
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 55-142 9.75e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 34.90  E-value: 9.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515722280  55 ERYPWLVAEVDGEVAGIAYAgpwkaRNAYDwtaESTVY---VSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPND 131
Cdd:PRK09491  38 ERYLNLKLTVNGQMAAFAIT-----QVVLD---EATLFniaVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNA 109

                         90
                 ....*....|.
gi 515722280 132 PSVRMHEALGY 142
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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