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Conserved domains on  [gi|1806852151|gb|QHX00529|]
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fluoroquinolone-acetylating aminoglycoside 6'-N-acetyltransferase AAC(6')-Ib-cr5 (plasmid) [Klebsiella variicola]

Protein Classification

N-acetyltransferase( domain architecture ID 11500359)

N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
N6_acetyl_AAC6 TIGR04431
aminoglycoside N(6')-acetyltransferase, AacA4 family; Members of this family are the aacA4 ...
 1-184 9.76e-142

aminoglycoside N(6')-acetyltransferase, AacA4 family; Members of this family are the aacA4 type of aminoglycoside N(6')-acetyltransferase (EC 2.3.1.82), an enzyme that modifies and inactivates aminoglycoside antibiotics such as kanamycin, neomycin, tobramycin, and amikacin. Members are regularly spread among pathogens into integron, transposon, and plasmid loci, with recombination often happening within the protein-coding region. Most of the region amino-terminal to the recombination site or sites was removed from this model. [Cellular processes, Toxin production and resistance]


:

Pssm-ID: 275224  Cd Length: 184  Bit Score: 391.55  E-value: 9.76e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806852151   1 MTNSNDSVTLRLMTEHDLAMLYEWLNRSHIVEWWGGEEARPTLADVQEQYLPSVLAQESVTPYIAMLNGEPIGYAQSYVA 80
Cdd:TIGR04431   1 MSNSNDPVTLRLMTEHDLPMLHEWLNRPHIVEWWGGEEERPTLADVQEHYLPRVLAEESVTPYIAMLGEEPIGYAQSYVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806852151  81 LGSGDGRWEEETDPGVRGIDQLLANASQLGKGLGTKLVRALVELLFNDPEVTKIQTDPSPSNLRAIRCYEKAGFERQGTV 160
Cdd:TIGR04431  81 LGSGDGWWEDETDPGVRGIDQSLANPSQLGKGLGTKLVRALVELLFNDPEVTKIQTDPSPNNHRAIRCYEKAGFVRQKTI 160

                         170       180
                  ....*....|....*....|....
gi 1806852151 161 TTPYGPAVYMVQTRQAFERTRSDA 184
Cdd:TIGR04431 161 TTPDGPAVYMVQTRQAFERARSAA 184
 
Name Accession Description Interval E-value
N6_acetyl_AAC6 TIGR04431
aminoglycoside N(6')-acetyltransferase, AacA4 family; Members of this family are the aacA4 ...
 1-184 9.76e-142

aminoglycoside N(6')-acetyltransferase, AacA4 family; Members of this family are the aacA4 type of aminoglycoside N(6')-acetyltransferase (EC 2.3.1.82), an enzyme that modifies and inactivates aminoglycoside antibiotics such as kanamycin, neomycin, tobramycin, and amikacin. Members are regularly spread among pathogens into integron, transposon, and plasmid loci, with recombination often happening within the protein-coding region. Most of the region amino-terminal to the recombination site or sites was removed from this model. [Cellular processes, Toxin production and resistance]


Pssm-ID: 275224  Cd Length: 184  Bit Score: 391.55  E-value: 9.76e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806852151   1 MTNSNDSVTLRLMTEHDLAMLYEWLNRSHIVEWWGGEEARPTLADVQEQYLPSVLAQESVTPYIAMLNGEPIGYAQSYVA 80
Cdd:TIGR04431   1 MSNSNDPVTLRLMTEHDLPMLHEWLNRPHIVEWWGGEEERPTLADVQEHYLPRVLAEESVTPYIAMLGEEPIGYAQSYVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806852151  81 LGSGDGRWEEETDPGVRGIDQLLANASQLGKGLGTKLVRALVELLFNDPEVTKIQTDPSPSNLRAIRCYEKAGFERQGTV 160
Cdd:TIGR04431  81 LGSGDGWWEDETDPGVRGIDQSLANPSQLGKGLGTKLVRALVELLFNDPEVTKIQTDPSPNNHRAIRCYEKAGFVRQKTI 160

                         170       180
                  ....*....|....*....|....
gi 1806852151 161 TTPYGPAVYMVQTRQAFERTRSDA 184
Cdd:TIGR04431 161 TTPDGPAVYMVQTRQAFERARSAA 184
Acetyltransf_8 pfam13523
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 15-162 6.19e-47

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


Pssm-ID: 433280  Cd Length: 145  Bit Score: 150.36  E-value: 6.19e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806852151  15 EHDLAMLYEWLNRSHIVEWWGGEearPTLADVQEqYLPSVLAQESVTPYIAMLNGEPIGYAQSYVALGSGDGRwEEETDP 94
Cdd:pfam13523   3 EADLELLHRWMNDPRVAFWWMLA---GPLEQVRE-YLARLAADPHSHPYIGLLDGEPFGYFEIYWAKEDRLGE-YYDARP 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1806852151  95 GVRGIDQLLANASQLGKGLGTKLVRALVELLFNDPEVTKIQTDPSPSNLRAIRCYEKAGFERQGTVTT 162
Cdd:pfam13523  78 GDRGIHLLIGEPAFRGRGFTTALLRALVHYLFADPRTRRVVVEPDVRNERAIRLLERAGFRKVKEIDL 145
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 6-160 1.00e-21

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: 86.59  E-value: 1.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806852151   6 DSVTLRLMTEHDLAMLYEWLNRSHIVEWWGG-----EEARPTLADVQEQYlpsvlAQESVTPYIAML--NGEPIGYAqsy 78
Cdd:COG1670     6 ERLRLRPLRPEDAEALAELLNDPEVARYLPGppyslEEARAWLERLLADW-----ADGGALPFAIEDkeDGELIGVV--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806852151  79 valgsgdGRWEEETDPGVRGIDQLLANASQlGKGLGTKLVRALVELLFNDPEVTKIQTDPSPSNLRAIRCYEKAGFERQG 158
Cdd:COG1670    78 -------GLYDIDRANRSAEIGYWLAPAYW-GKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEG 149


                  ..
gi 1806852151 159 TV 160
Cdd:COG1670   150 TL 151
AlcB smart01006
Siderophore biosynthesis protein domain; AlcB is the conserved 45 residue region of one of the ...
 15-58 1.68e-04

Siderophore biosynthesis protein domain; AlcB is the conserved 45 residue region of one of the proteins of a complex which mediates alcaligin biosynthesis in Bordetella and aerobactin biosynthesis in E. coli and other bacteria. The protein appears to catalyse N-acylation of the hydroxylamine group in N-hydroxyputrescine with succinyl CoA - an activated mono-thioester derivative of succinic acid that is an intermediate in the Krebs cycle.


Pssm-ID: 198074  Cd Length: 48  Bit Score: 37.93  E-value: 1.68e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1806852151   15 EHDLAMLYEWLNRSHIVEWWGGEEarpTLADVqEQYLPSVLAQE 58
Cdd:smart01006   6 EQDLPLLHRWMNRPHVAAFWGMGG---PLEEV-RAYLRAQLADP 45
 
Name Accession Description Interval E-value
N6_acetyl_AAC6 TIGR04431
aminoglycoside N(6')-acetyltransferase, AacA4 family; Members of this family are the aacA4 ...
 1-184 9.76e-142

aminoglycoside N(6')-acetyltransferase, AacA4 family; Members of this family are the aacA4 type of aminoglycoside N(6')-acetyltransferase (EC 2.3.1.82), an enzyme that modifies and inactivates aminoglycoside antibiotics such as kanamycin, neomycin, tobramycin, and amikacin. Members are regularly spread among pathogens into integron, transposon, and plasmid loci, with recombination often happening within the protein-coding region. Most of the region amino-terminal to the recombination site or sites was removed from this model. [Cellular processes, Toxin production and resistance]


Pssm-ID: 275224  Cd Length: 184  Bit Score: 391.55  E-value: 9.76e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806852151   1 MTNSNDSVTLRLMTEHDLAMLYEWLNRSHIVEWWGGEEARPTLADVQEQYLPSVLAQESVTPYIAMLNGEPIGYAQSYVA 80
Cdd:TIGR04431   1 MSNSNDPVTLRLMTEHDLPMLHEWLNRPHIVEWWGGEEERPTLADVQEHYLPRVLAEESVTPYIAMLGEEPIGYAQSYVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806852151  81 LGSGDGRWEEETDPGVRGIDQLLANASQLGKGLGTKLVRALVELLFNDPEVTKIQTDPSPSNLRAIRCYEKAGFERQGTV 160
Cdd:TIGR04431  81 LGSGDGWWEDETDPGVRGIDQSLANPSQLGKGLGTKLVRALVELLFNDPEVTKIQTDPSPNNHRAIRCYEKAGFVRQKTI 160

                         170       180
                  ....*....|....*....|....
gi 1806852151 161 TTPYGPAVYMVQTRQAFERTRSDA 184
Cdd:TIGR04431 161 TTPDGPAVYMVQTRQAFERARSAA 184
Acetyltransf_8 pfam13523
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 15-162 6.19e-47

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


Pssm-ID: 433280  Cd Length: 145  Bit Score: 150.36  E-value: 6.19e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806852151  15 EHDLAMLYEWLNRSHIVEWWGGEearPTLADVQEqYLPSVLAQESVTPYIAMLNGEPIGYAQSYVALGSGDGRwEEETDP 94
Cdd:pfam13523   3 EADLELLHRWMNDPRVAFWWMLA---GPLEQVRE-YLARLAADPHSHPYIGLLDGEPFGYFEIYWAKEDRLGE-YYDARP 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1806852151  95 GVRGIDQLLANASQLGKGLGTKLVRALVELLFNDPEVTKIQTDPSPSNLRAIRCYEKAGFERQGTVTT 162
Cdd:pfam13523  78 GDRGIHLLIGEPAFRGRGFTTALLRALVHYLFADPRTRRVVVEPDVRNERAIRLLERAGFRKVKEIDL 145
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 6-160 1.00e-21

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: 86.59  E-value: 1.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806852151   6 DSVTLRLMTEHDLAMLYEWLNRSHIVEWWGG-----EEARPTLADVQEQYlpsvlAQESVTPYIAML--NGEPIGYAqsy 78
Cdd:COG1670     6 ERLRLRPLRPEDAEALAELLNDPEVARYLPGppyslEEARAWLERLLADW-----ADGGALPFAIEDkeDGELIGVV--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806852151  79 valgsgdGRWEEETDPGVRGIDQLLANASQlGKGLGTKLVRALVELLFNDPEVTKIQTDPSPSNLRAIRCYEKAGFERQG 158
Cdd:COG1670    78 -------GLYDIDRANRSAEIGYWLAPAYW-GKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEG 149


                  ..
gi 1806852151 159 TV 160
Cdd:COG1670   150 TL 151
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 18-154 2.48e-14

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: 66.00  E-value: 2.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806852151  18 LAMLYEWLNRSHIVEWwggeeaRPTLADVQEQYLPsvlaQESVTPYIAMLNGEPIGYAQSYValgsgdgRWEEetdPGVR 97
Cdd:pfam00583   1 LEALYELLSEEFPEPW------PDEPLDLLEDWDE----DASEGFFVAEEDGELVGFASLSI-------IDDE---PPVG 60

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1806852151  98 GIDQLLANASQLGKGLGTKLVRALVELLFNDpEVTKIQTDPSPSNLRAIRCYEKAGF 154
Cdd:pfam00583  61 EIEGLAVAPEYRGKGIGTALLQALLEWARER-GCERIFLEVAADNLAAIALYEKLGF 116
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 8-155 2.90e-14

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 66.22  E-value: 2.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806852151   8 VTLRLMTEHDLAMLYEWLNRSHIVEWWGGEEarPTLADVQEQYLPSVLAQESVTPY---IAMLNGEPIGYAqSYVALGSG 84
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSDPEVMRYGVPWP--LTLEEAREWLARIWAADEAERGYgwaIELKDTGFIGSI-GLYDIDGE 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1806852151  85 DGRWEeetdpgvrgIDQLLANASQlGKGLGTKLVRALVELLFNDPEVTKIQTDPSPSNLRAIRCYEKAGFE 155
Cdd:pfam13302  79 PERAE---------LGYWLGPDYW-GKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
7-160 2.45e-11

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 58.85  E-value: 2.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806852151   7 SVTLRLMTEHD---LAMLYEWLNRSHIVEWwggEEARPTLADVQEQYlpSVLAQESVTPYIAMLNGEPIGYA--QSYVAL 81
Cdd:COG1247     1 EMTIRPATPEDapaIAAIYNEAIAEGTATF---ETEPPSEEEREAWF--AAILAPGRPVLVAEEDGEVVGFAslGPFRPR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806852151  82 GSGDGRWEEE--TDPGVRGidqllanasqlgKGLGTKLVRALVELLFNDPeVTKIQTDPSPSNLRAIRCYEKAGFERQGT 159
Cdd:COG1247    76 PAYRGTAEESiyVDPDARG------------RGIGRALLEALIERARARG-YRRLVAVVLADNEASIALYEKLGFEEVGT 142


                  .
gi 1806852151 160 V 160
Cdd:COG1247   143 L 143
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 110-171 3.41e-08

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 48.88  E-value: 3.41e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1806852151 110 GKGLGTKLVRALVELLFnDPEVTKIQTDPSPSNLRAIRCYEKAGFERQGTVTTPYG-PAVYMV 171
Cdd:COG0456    27 GRGIGRALLEAALERAR-ERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGdDALVME 88
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
10-171 1.06e-07

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 48.93  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806852151  10 LRLMTEHDLAMLYEWLNRShiveWWGGEEARpTLADVQEQYLPSVLaqesvtpYIAMLNGEPIGYAQSYVALGSGDGRWE 89
Cdd:COG3153     1 IRPATPEDAEAIAALLRAA----FGPGREAE-LVDRLREDPAAGLS-------LVAEDDGEIVGHVALSPVDIDGEGPAL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806852151  90 E----ETDPGVRGidqllanasqlgKGLGTKLVRALVELL--FNDPEVTkIQTDPSPSNLraircYEKAGFERQGTVTTP 163
Cdd:COG3153    69 LlgplAVDPEYRG------------QGIGRALMRAALEAAreRGARAVV-LLGDPSLLPF-----YERFGFRPAGELGLT 130


                  ....*....
gi 1806852151 164 YGP-AVYMV 171
Cdd:COG3153   131 LGPdEVFLA 139
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
110-162 1.42e-06

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 44.51  E-value: 1.42e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1806852151 110 GKGLGTKLVRALVELLFNDpEVTKIQTDPSPSNLRAIRCYEKAGFERQGTVTT 162
Cdd:COG3393    29 GRGLASALVAALAREALAR-GARTPFLYVDADNPAARRLYERLGFRPVGEYAT 80
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 63-156 1.10e-05

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 42.06  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806852151  63 YIAMLNGEPIGYAqSYVALGSGDGRWEEE--TDPGVRGidqllanasqlgKGLGTKLVRALVELLfNDPEVTKIQTDpsp 140
Cdd:pfam13508   6 FVAEDDGKIVGFA-ALLPLDDEGALAELRlaVHPEYRG------------QGIGRALLEAAEAAA-KEGGIKLLELE--- 68

                          90
                  ....*....|....*.
gi 1806852151 141 SNLRAIRCYEKAGFER 156
Cdd:pfam13508  69 TTNRAAAFYEKLGFEE 84
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
63-158 5.63e-05

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 40.94  E-value: 5.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806852151  63 YIAMLNGEPIGYAqsyvalgsgdgRWEEETDPGVRgIDQLLANASQLGKGLGTKLVRALVELLFNDPeVTKI----QTdp 138
Cdd:COG2153    37 LLAYDDGELVATA-----------RLLPPGDGEAK-IGRVAVLPEYRGQGLGRALMEAAIEEARERG-ARRIvlsaQA-- 101

                          90       100
                  ....*....|....*....|
gi 1806852151 139 spsnlRAIRCYEKAGFERQG 158
Cdd:COG2153   102 -----HAVGFYEKLGFVPVG 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 17-158 7.91e-05

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: 40.78  E-value: 7.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806852151  17 DLAMLYEWLNRSHIVEWwggeearptladvQEQYLPSVLAQESVTPYIAMLNGEPIGYAQSYVALGSGDgrweeetdpgv 96
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPW-------------TEAQFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAH----------- 56

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1806852151  97 rgIDQLLANASQLGKGLGTKLVRALVELLFNDpEVTKIQTDPSPSNLRAIRCYEKAGFERQG 158
Cdd:TIGR01575  57 --ILNIAVKPEYQGQGIGRALLRELIDEAKGR-GVNEIFLEVRVSNIAAQALYKKLGFNEIA 115
AlcB smart01006
Siderophore biosynthesis protein domain; AlcB is the conserved 45 residue region of one of the ...
 15-58 1.68e-04

Siderophore biosynthesis protein domain; AlcB is the conserved 45 residue region of one of the proteins of a complex which mediates alcaligin biosynthesis in Bordetella and aerobactin biosynthesis in E. coli and other bacteria. The protein appears to catalyse N-acylation of the hydroxylamine group in N-hydroxyputrescine with succinyl CoA - an activated mono-thioester derivative of succinic acid that is an intermediate in the Krebs cycle.


Pssm-ID: 198074  Cd Length: 48  Bit Score: 37.93  E-value: 1.68e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1806852151   15 EHDLAMLYEWLNRSHIVEWWGGEEarpTLADVqEQYLPSVLAQE 58
Cdd:smart01006   6 EQDLPLLHRWMNRPHVAAFWGMGG---PLEEV-RAYLRAQLADP 45
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 37-165 3.62e-04

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: 38.82  E-value: 3.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806852151  37 EEARPT-LADVQEQYLPSVLAQESVTPYIAMLNGEPIGYAqsyvALgsgdgrweEETDPGVRGIDQLLANASQLGKGLGT 115
Cdd:COG1246     4 RPATPDdVPAILELIRPYALEEEIGEFWVAEEDGEIVGCA----AL--------HPLDEDLAELRSLAVHPDYRGRGIGR 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1806852151 116 KLVRALVELLfNDPEVTKIQTDpspSNLRAIRCYEKAGFERQGTVTTPYG 165
Cdd:COG1246    72 RLLEALLAEA-RELGLKRLFLL---TTSAAIHFYEKLGFEEIDKEDLPYA 117
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 27-171 8.28e-04

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 37.73  E-value: 8.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806852151  27 RSHIVEWWGGEEARPTLADVQEQYLPSVLaqesvtpYIAMLNGEPIGYAqsyvalgsgdgrWEEETDPGVRGIDQLLANA 106
Cdd:COG0454     8 PEDINFILLIEALDAELKAMEGSLAGAEF-------IAVDDKGEPIGFA------------GLRRLDDKVLELKRLYVLP 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1806852151 107 SQLGKGLGTKLVRALVELLfNDPEVTKIQTDPSPSNLRAIRCYEKAGFERQGTVTTPYGPAVYMV 171
Cdd:COG0454    69 EYRGKGIGKALLEALLEWA-RERGCTALELDTLDGNPAAIRFYERLGFKEIERYVAYVGGEFEKE 132
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 30-158 1.35e-03

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: 37.25  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806852151  30 IVEWWGGEEARPTLADVQEQYLPSVLAQESVTPYIAMLNGEPIGYAqsyvALGSGdgrweeetdpgvRGIDQLLANASQL 109
Cdd:pfam13673   1 EAPDYSEEGIETFYEFISPEALRERIDQGEYFFFVAFEGGQIVGVI----ALRDR------------GHISLLFVDPDYQ 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1806852151 110 GKGLGTKLVRALVELLFND-PEVTKIQTDPSPSnlrAIRCYEKAGFERQG 158
Cdd:pfam13673  65 GQGIGKALLEAVEDYAEKDgIKLSELTVNASPY---AVPFYEKLGFRATG 111
 
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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