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Conserved domains on  [gi|388772247|gb|AFK77929|]
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aminoglycoside-3'-phosphotransferase, partial [Cloning vector pVK101]

Protein Classification

aminoglycoside 3'-phosphotransferase( domain architecture ID 10142347)

aminoglycoside 3'-phosphotransferase phosphorylates and inactives antibiotic substrates such as kanamycin, streptomycin, neomycin, and gentamicin, among others

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Aph super family cl43814
Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];
12-185 1.31e-68

Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG3231:

Pssm-ID: 442463 [Multi-domain]  Cd Length: 258  Bit Score: 209.39  E-value: 1.31e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388772247  12 RPRLNSNMDADLYGYKWARDNVGQSGATIYRLYGkPDAPELFLKHGKGSVANDVTDEMVRLNWLTEF-MPLPTIKHFIRT 90
Cdd:COG3231    1 GPRLPPALRELLGGYRWEPVTIGESGAKVFRLAD-GGRPTLYLKIEPAGPAAELEDEADRLRWLAGQgLPVPEVLDFGED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388772247  91 PDDAWLLTTAIPGKTAFQVleEYPDSGENIVDALAVFLRRLHSIPVCNCPFNSDRVFRLAQAQSRMNNGLVDASDFDDER 170
Cdd:COG3231   80 DGGAWLLTTAVPGRPAASV--SEALDPERAVELLAEALRRLHALPVADCPFDRRLERRLAEARARVAAGLVDPDDFDEER 157

                        170
                 ....*....|....*
gi 388772247 171 NGWPVEQVWKEMHKL 185
Cdd:COG3231  158 RGRPPEELLAELLAE 172
 
Name Accession Description Interval E-value
Aph COG3231
Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];
12-185 1.31e-68

Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442463 [Multi-domain]  Cd Length: 258  Bit Score: 209.39  E-value: 1.31e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388772247  12 RPRLNSNMDADLYGYKWARDNVGQSGATIYRLYGkPDAPELFLKHGKGSVANDVTDEMVRLNWLTEF-MPLPTIKHFIRT 90
Cdd:COG3231    1 GPRLPPALRELLGGYRWEPVTIGESGAKVFRLAD-GGRPTLYLKIEPAGPAAELEDEADRLRWLAGQgLPVPEVLDFGED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388772247  91 PDDAWLLTTAIPGKTAFQVleEYPDSGENIVDALAVFLRRLHSIPVCNCPFNSDRVFRLAQAQSRMNNGLVDASDFDDER 170
Cdd:COG3231   80 DGGAWLLTTAVPGRPAASV--SEALDPERAVELLAEALRRLHALPVADCPFDRRLERRLAEARARVAAGLVDPDDFDEER 157

                        170
                 ....*....|....*
gi 388772247 171 NGWPVEQVWKEMHKL 185
Cdd:COG3231  158 RGRPPEELLAELLAE 172
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
 26-185 1.66e-57

Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group from ATP to aminoglycoside antibiotics such as kanamycin, streptomycin, neomycin, and gentamicin, among others. The aminoglycoside antibiotics target the 30S ribosome and promote miscoding, leading to the production of defective proteins which insert into the bacterial membrane, resulting in membrane damage and the ultimate demise of the bacterium. Phosphorylation of the aminoglycoside antibiotics results in their inactivation, leading to bacterial antibiotic resistance. The APH gene is found on transposons and plasmids and is thought to have originated as a self-defense mechanism used by microorganisms that produce the antibiotics. The APH subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270699 [Multi-domain]  Cd Length: 244  Bit Score: 180.47  E-value: 1.66e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388772247  26 YKWARDNVGQSGATIYRLYGKPdaPELFLKHGKGSVANDVTDEMVRLNWLTEFMPLPTIKHFIRTPDDAWLLTTAIPGKT 105
Cdd:cd05150    1 YRWEPDTIGESGARVYRLDGGG--PVLYLKTAPAGYAYELAREAERLRWLAGKLPVPEVLDYGSDDGGDWLLTTALPGRD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388772247 106 AFQvlEEYPDSGENIVDALAVFLRRLHSIPVCNCPFNSDRVFRLAQAQSRMNNGLVDASDFDDERNGWPVEQVWKEMHKL 185
Cdd:cd05150   79 AAS--LEPLLDPERLVDLLAEALRALHSLPIADCPFDRRLDARLAEARARVEAGLVDEDDFDEERQGRTAEELLAELEAT 156
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 27-185 4.79e-05

Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.


Pssm-ID: 426359 [Multi-domain]  Cd Length: 239  Bit Score: 42.49  E-value: 4.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388772247   27 KWARDNVGQSGATIYRLYGKPdapELFLK-HGKGSVANDVTDEMVRLNWLTE--FMPLPTIKHFIRTPDD---AWLLTTA 100
Cdd:pfam01636   1 TLRPISSGASNRTYLVTTGDG---RYVLRlPPPGRAAEELRRELALLRHLAAagVPPVPRVLAGCTDAELlglPFLLMEY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388772247  101 IPGKTAFQVLEeyPDSGENIVDALAVFLRRLHSIPVCNCPFNSDRVFRLAQAQSRMN--NGLVDASDFDdeRNGWPVEQV 178
Cdd:pfam01636  78 LPGEVLARPLL--PEERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAalARLLAAELLD--RLEELEERL 153


                  ....*..
gi 388772247  179 WKEMHKL 185
Cdd:pfam01636 154 LAALLAL 160
 
Name Accession Description Interval E-value
Aph COG3231
Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];
12-185 1.31e-68

Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442463 [Multi-domain]  Cd Length: 258  Bit Score: 209.39  E-value: 1.31e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388772247  12 RPRLNSNMDADLYGYKWARDNVGQSGATIYRLYGkPDAPELFLKHGKGSVANDVTDEMVRLNWLTEF-MPLPTIKHFIRT 90
Cdd:COG3231    1 GPRLPPALRELLGGYRWEPVTIGESGAKVFRLAD-GGRPTLYLKIEPAGPAAELEDEADRLRWLAGQgLPVPEVLDFGED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388772247  91 PDDAWLLTTAIPGKTAFQVleEYPDSGENIVDALAVFLRRLHSIPVCNCPFNSDRVFRLAQAQSRMNNGLVDASDFDDER 170
Cdd:COG3231   80 DGGAWLLTTAVPGRPAASV--SEALDPERAVELLAEALRRLHALPVADCPFDRRLERRLAEARARVAAGLVDPDDFDEER 157

                        170
                 ....*....|....*
gi 388772247 171 NGWPVEQVWKEMHKL 185
Cdd:COG3231  158 RGRPPEELLAELLAE 172
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
 26-185 1.66e-57

Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group from ATP to aminoglycoside antibiotics such as kanamycin, streptomycin, neomycin, and gentamicin, among others. The aminoglycoside antibiotics target the 30S ribosome and promote miscoding, leading to the production of defective proteins which insert into the bacterial membrane, resulting in membrane damage and the ultimate demise of the bacterium. Phosphorylation of the aminoglycoside antibiotics results in their inactivation, leading to bacterial antibiotic resistance. The APH gene is found on transposons and plasmids and is thought to have originated as a self-defense mechanism used by microorganisms that produce the antibiotics. The APH subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270699 [Multi-domain]  Cd Length: 244  Bit Score: 180.47  E-value: 1.66e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388772247  26 YKWARDNVGQSGATIYRLYGKPdaPELFLKHGKGSVANDVTDEMVRLNWLTEFMPLPTIKHFIRTPDDAWLLTTAIPGKT 105
Cdd:cd05150    1 YRWEPDTIGESGARVYRLDGGG--PVLYLKTAPAGYAYELAREAERLRWLAGKLPVPEVLDYGSDDGGDWLLTTALPGRD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388772247 106 AFQvlEEYPDSGENIVDALAVFLRRLHSIPVCNCPFNSDRVFRLAQAQSRMNNGLVDASDFDDERNGWPVEQVWKEMHKL 185
Cdd:cd05150   79 AAS--LEPLLDPERLVDLLAEALRALHSLPIADCPFDRRLDARLAEARARVEAGLVDEDDFDEERQGRTAEELLAELEAT 156
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 27-185 4.79e-05

Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.


Pssm-ID: 426359 [Multi-domain]  Cd Length: 239  Bit Score: 42.49  E-value: 4.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388772247   27 KWARDNVGQSGATIYRLYGKPdapELFLK-HGKGSVANDVTDEMVRLNWLTE--FMPLPTIKHFIRTPDD---AWLLTTA 100
Cdd:pfam01636   1 TLRPISSGASNRTYLVTTGDG---RYVLRlPPPGRAAEELRRELALLRHLAAagVPPVPRVLAGCTDAELlglPFLLMEY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388772247  101 IPGKTAFQVLEeyPDSGENIVDALAVFLRRLHSIPVCNCPFNSDRVFRLAQAQSRMN--NGLVDASDFDdeRNGWPVEQV 178
Cdd:pfam01636  78 LPGEVLARPLL--PEERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAalARLLAAELLD--RLEELEERL 153


                  ....*..
gi 388772247  179 WKEMHKL 185
Cdd:pfam01636 154 LAALLAL 160
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 48-136 2.79e-03

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 36.51  E-value: 2.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388772247  48 DAPELFLKHGKGSVANDVTDEMVRLNWLTEFM--PLPTIKHFIRTPDDAWLLTTAIPGKTAFQV-LEEYPDSGENIVDAL 124
Cdd:cd05120   19 DPREYVLKIGPPRLKKDLEKEAAMLQLLAGKLslPVPKVYGFGESDGWEYLLMERIEGETLSEVwPRLSEEEKEKIADQL 98

                         90
                 ....*....|..
gi 388772247 125 AVFLRRLHSIPV 136
Cdd:cd05120   99 AEILAALHRIDS 110
 
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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