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Conserved domains on  [gi|1115239731|gb|APM87886|]
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BAR [Cloning vector pAL004(Ubi-nos)mDII]

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 4.61e-129

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: 359.69  E-value: 4.61e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1115239731   1 MSPERRPADIRRATEADMPAVCTIVNHYIETSTVNFRTEPQEPQEWTDDLVRLRERYPWLVAEVDGEVAGIAYAGPWKAR 80
Cdd:NF040502    1 MSPERRPEGIRLATAADMPAVCEIVNHYIETSTVNFRTEPQLPQEWEDDLARLRERYPWLVAEVGGEVAGIAYAGPWKAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1115239731  81 NAYDWTAESTVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRGMLRAAGFKHGNWHD 160
Cdd:NF040502   81 NAYDWTTESTVYVSDRHQRRGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRLHEALGYESRGRLRAAGHKHGGWHD 160


                  ....*....
gi 1115239731 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 4.61e-129

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: 359.69  E-value: 4.61e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1115239731   1 MSPERRPADIRRATEADMPAVCTIVNHYIETSTVNFRTEPQEPQEWTDDLVRLRERYPWLVAEVDGEVAGIAYAGPWKAR 80
Cdd:NF040502    1 MSPERRPEGIRLATAADMPAVCEIVNHYIETSTVNFRTEPQLPQEWEDDLARLRERYPWLVAEVGGEVAGIAYAGPWKAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1115239731  81 NAYDWTAESTVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRGMLRAAGFKHGNWHD 160
Cdd:NF040502   81 NAYDWTTESTVYVSDRHQRRGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRLHEALGYESRGRLRAAGHKHGGWHD 160


                  ....*....
gi 1115239731 161 VGFWQLDFS 169
Cdd:NF040502  161 VGFWQRDFV 169
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
10-167 1.17e-55

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 173.26  E-value: 1.17e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1115239731  10 IRRATEADMPAVCTIVNHYIETSTVNFRTEPQEPQEWTDDLV-RLRERYPWLVAEVDGEVAGIAYAGPWKARNAYDWTAE 88
Cdd:COG1247     4 IRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAaILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRGTAE 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1115239731  89 STVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRGMLRAAGFKHGNWHDVGFWQLD 167
Cdd:COG1247    84 ESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQKR 162
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 24-142 8.47e-17

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: 72.55  E-value: 8.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1115239731  24 IVNHYIETSTVNFRTEPQEPQEWTDDlvrlRERYPWLVAEVDGEVAGiaYAGPWKARNAYDWTAESTVYVSPRHQRTGLG 103
Cdd:pfam00583   4 LYELLSEEFPEPWPDEPLDLLEDWDE----DASEGFFVAEEDGELVG--FASLSIIDDEPPVGEIEGLAVAPEYRGKGIG 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1115239731 104 STLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGY 142
Cdd:pfam00583  78 TALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 59-123 6.23e-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: 47.66  E-value: 6.23e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1115239731  59 WLVAEVDGEVAGIAYAGPWkarNAYDWTAE-STVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVV 123
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPD---GSGGDTAYiGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
PRK03624 PRK03624
putative acetyltransferase; Provisional
 60-142 5.75e-07

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 46.85  E-value: 5.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1115239731  60 LVAEVDGEVAGIAYAGpwkarnaYD----WtaestVY---VSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDP 132
Cdd:PRK03624   48 LVAEVGGEVVGTVMGG-------YDghrgW-----AYylaVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDA 115

                          90
                  ....*....|
gi 1115239731 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 4.61e-129

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: 359.69  E-value: 4.61e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1115239731   1 MSPERRPADIRRATEADMPAVCTIVNHYIETSTVNFRTEPQEPQEWTDDLVRLRERYPWLVAEVDGEVAGIAYAGPWKAR 80
Cdd:NF040502    1 MSPERRPEGIRLATAADMPAVCEIVNHYIETSTVNFRTEPQLPQEWEDDLARLRERYPWLVAEVGGEVAGIAYAGPWKAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1115239731  81 NAYDWTAESTVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRGMLRAAGFKHGNWHD 160
Cdd:NF040502   81 NAYDWTTESTVYVSDRHQRRGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRLHEALGYESRGRLRAAGHKHGGWHD 160


                  ....*....
gi 1115239731 161 VGFWQLDFS 169
Cdd:NF040502  161 VGFWQRDFV 169
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
10-167 1.17e-55

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 173.26  E-value: 1.17e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1115239731  10 IRRATEADMPAVCTIVNHYIETSTVNFRTEPQEPQEWTDDLV-RLRERYPWLVAEVDGEVAGIAYAGPWKARNAYDWTAE 88
Cdd:COG1247     4 IRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAaILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRGTAE 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1115239731  89 STVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRGMLRAAGFKHGNWHDVGFWQLD 167
Cdd:COG1247    84 ESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQKR 162
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 24-142 8.47e-17

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: 72.55  E-value: 8.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1115239731  24 IVNHYIETSTVNFRTEPQEPQEWTDDlvrlRERYPWLVAEVDGEVAGiaYAGPWKARNAYDWTAESTVYVSPRHQRTGLG 103
Cdd:pfam00583   4 LYELLSEEFPEPWPDEPLDLLEDWDE----DASEGFFVAEEDGELVG--FASLSIIDDEPPVGEIEGLAVAPEYRGKGIG 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1115239731 104 STLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGY 142
Cdd:pfam00583  78 TALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
10-149 1.31e-14

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 67.42  E-value: 1.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1115239731  10 IRRATEADMPAVCTIVNHYIetstvnfrtepqePQEWTDDLV-RLRERYP---WLVAEVDGEVAGIAYAGPWKARNAYDW 85
Cdd:COG3153     1 IRPATPEDAEAIAALLRAAF-------------GPGREAELVdRLREDPAaglSLVAEDDGEIVGHVALSPVDIDGEGPA 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1115239731  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 1.27e-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: 61.93  E-value: 1.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1115239731  10 IRRATEADMPAVCTIVNHYIetstvnfrtepqepqewtddLVRLRERYpwLVAEVDGEVAGIAYAGPWKARnaydwTAE- 88
Cdd:COG1246     3 IRPATPDDVPAILELIRPYA--------------------LEEEIGEF--WVAEEDGEIVGCAALHPLDED-----LAEl 55

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1115239731  89 STVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAvigLPNDPSVRMHEALGYAP 144
Cdd:COG1246    56 RSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFL---LTTSAAIHFYEKLGFEE 108
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 10-166 1.64e-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: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1115239731  10 IRRATEADMPAVCTIVNH-YIETSTVNFRTEPQEPQEWTDDLVRL---RERYPWLVAE-VDGEVAGIAYAGPWkarNAYD 84
Cdd:COG1670    10 LRPLRPEDAEALAELLNDpEVARYLPGPPYSLEEARAWLERLLADwadGGALPFAIEDkEDGELIGVVGLYDI---DRAN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1115239731  85 WTAESTVYVSPRHQRTGLGSTLYTHLLK-SLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRGMLRAAGFKHGNWHDVGF 163
Cdd:COG1670    87 RSAEIGYWLAPAYWGKGYATEALRALLDyAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHVL 166


                  ...
gi 1115239731 164 WQL 166
Cdd:COG1670   167 YSL 169
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
10-160 3.60e-10

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 55.84  E-value: 3.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1115239731  10 IRRATEADMPAVCTIVNHYIETSTVNFRT-EPQepQEWTDDLVRLR---ERYPWLVAEvDGEVAGIAYAGPWKARnaYDW 85
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAEDRVNPAFTQEYaHSS--IEEFETFLAAYlspGEIVFGVAE-SDRLIGYATLRQFDYV--KTH 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1115239731  86 TAESTVYVSpRHQRTGLGSTLYTHLLKSLEA-QGFKSVVAVIGLPNDPSVRMHEALGYAPRGMLRAAGFKHGNWHD 160
Cdd:pfam13420  76 KAELSFYVV-KNNDEGINRELINAIIQYARKnQNIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKKNGRWID 150
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 10-144 1.85e-09

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 53.52  E-value: 1.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1115239731  10 IRRATEADMPAVCTIvnhyietstvnfrtEPQEPQ-EWTDDLVRLRErypWLVAEVDGEVAGIAYAGPWKarnayDWTAE 88
Cdd:COG0454     3 IRKATPEDINFILLI--------------EALDAElKAMEGSLAGAE---FIAVDDKGEPIGFAGLRRLD-----DKVLE 60

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1115239731  89 -STVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAP 144
Cdd:COG0454    61 lKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKE 117
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
67-154 3.49e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 48.75  E-value: 3.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1115239731  67 EVAGIAYAGPWkarnAYDWTAESTVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRG 146
Cdd:COG3393     1 ELVAMAGVRAE----SPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVG 76


                  ....*...
gi 1115239731 147 MLRAAGFK 154
Cdd:COG3393    77 EYATVLFR 84
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 59-123 6.23e-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: 47.66  E-value: 6.23e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1115239731  59 WLVAEVDGEVAGIAYAGPWkarNAYDWTAE-STVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVV 123
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPD---GSGGDTAYiGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 90-146 1.51e-07

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 47.34  E-value: 1.51e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1115239731  90 TVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRMHEALGYAPRG 146
Cdd:COG0456    18 DLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVG 74
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 55-142 2.34e-07

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 46.68  E-value: 2.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1115239731  55 ERYPWLVAEVDGEVAGIAYAGPwkaRNAYDWTAESTVYVSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAvigLPNDPSV 134
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLP---LDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLEL---ETTNRAA 74


                  ....*...
gi 1115239731 135 RMHEALGY 142
Cdd:pfam13508  75 AFYEKLGF 82
PRK03624 PRK03624
putative acetyltransferase; Provisional
 60-142 5.75e-07

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 46.85  E-value: 5.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1115239731  60 LVAEVDGEVAGIAYAGpwkarnaYD----WtaestVY---VSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDP 132
Cdd:PRK03624   48 LVAEVGGEVVGTVMGG-------YDghrgW-----AYylaVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDA 115

                          90
                  ....*....|
gi 1115239731 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 5.48e-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: 5.48e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1115239731  89 STVYVSPRHQRTGLGSTLYTHLLKSLEAQGfKSVVAVIGLPNDPSVRMHEALGY 142
Cdd:pfam08445  25 GALQTLPEHRRRGLGSRLVAALARGIAERG-ITPFAVVVAGNTPSRRLYEKLGF 77
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 55-142 9.86e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 34.90  E-value: 9.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1115239731  55 ERYPWLVAEVDGEVAGIAYAgpwkaRNAYDwtaESTVY---VSPRHQRTGLGSTLYTHLLKSLEAQGFKSVVAVIGLPND 131
Cdd:PRK09491   38 ERYLNLKLTVNGQMAAFAIT-----QVVLD---EATLFniaVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNA 109

                          90
                  ....*....|.
gi 1115239731 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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