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Conserved domains on  [gi|402294530|gb|AFQ55242|]
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Sm resistance protein B [Expression vector pJRD215]

Protein Classification

aminoglycoside phosphotransferase family protein( domain architecture ID 10519870)

aminoglycoside phosphotransferase family protein inactivates its antibiotic substrate by phosphorylation, similar to streptomycin 6-kinase that catalyzes the phosphorylation of streptomycin to form streptomycin 6-phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
APH_6_hur pfam04655
Aminoglycoside/hydroxyurea antibiotic resistance kinase; The aminoglycoside ...
 10-256 5.56e-130

Aminoglycoside/hydroxyurea antibiotic resistance kinase; The aminoglycoside phosphotransferases achieve inactivation of their antibiotic substrates by phosphorylation utilizing ATP. Likewise hydroxyurea is inactivated by phosphorylation of the hydroxy group in the hydroxylamine moiety.


:

Pssm-ID: 398368 [Multi-domain]  Cd Length: 250  Bit Score: 368.86  E-value: 5.56e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402294530   10 HWHVSQPVLIADTFSSLVWKVSLPDGTPAIVKGLKPIEDIADELRGADYLVWRNGRGAVRLLGR--ENNLMLLEYA-GER 86
Cdd:pfam04655   1 RWHLVPDVEPPGTHSSLVLPVRTAEGAPAMLKLAPRRARPEEERRGADLLVWWGGRGAVRVLAEgdEEGALLLERAhGDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402294530   87 MLSHIVAEHGDYQATEIAAELMAKLYAASEEPLPSaLLPIRDRFAALFQRARDDQNAGCQTDYVHAAIIADQMMSNASEL 166
Cdd:pfam04655  81 SLRSLVAEGGDDEATRIAAGALARLHAPRPGPLPS-LLPLEDWFERLFAQARMRAGAVAQPLYVAAAAAARQLLGGPSEQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402294530  167 RGLHGDLHHENIMFSS-RGWLVIDPVGLVGEVGFGAANMFYDPADRDDLCLDPRRIAQMADAFSRALDVDPRRLLDQAYA 245
Cdd:pfam04655 160 RPLHGDLHHSNVLDGGrRGWLAIDPKGLVGERGFDLANLFRDPDEDTIQALGPGRTERQLKRLAEALEVDPRRLLGWTLA 239

                         250
                  ....*....|.
gi 402294530  246 YGCLSAAWNAD 256
Cdd:pfam04655 240 YTGLSAAWARE 250
 
Name Accession Description Interval E-value
APH_6_hur pfam04655
Aminoglycoside/hydroxyurea antibiotic resistance kinase; The aminoglycoside ...
 10-256 5.56e-130

Aminoglycoside/hydroxyurea antibiotic resistance kinase; The aminoglycoside phosphotransferases achieve inactivation of their antibiotic substrates by phosphorylation utilizing ATP. Likewise hydroxyurea is inactivated by phosphorylation of the hydroxy group in the hydroxylamine moiety.


Pssm-ID: 398368 [Multi-domain]  Cd Length: 250  Bit Score: 368.86  E-value: 5.56e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402294530   10 HWHVSQPVLIADTFSSLVWKVSLPDGTPAIVKGLKPIEDIADELRGADYLVWRNGRGAVRLLGR--ENNLMLLEYA-GER 86
Cdd:pfam04655   1 RWHLVPDVEPPGTHSSLVLPVRTAEGAPAMLKLAPRRARPEEERRGADLLVWWGGRGAVRVLAEgdEEGALLLERAhGDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402294530   87 MLSHIVAEHGDYQATEIAAELMAKLYAASEEPLPSaLLPIRDRFAALFQRARDDQNAGCQTDYVHAAIIADQMMSNASEL 166
Cdd:pfam04655  81 SLRSLVAEGGDDEATRIAAGALARLHAPRPGPLPS-LLPLEDWFERLFAQARMRAGAVAQPLYVAAAAAARQLLGGPSEQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402294530  167 RGLHGDLHHENIMFSS-RGWLVIDPVGLVGEVGFGAANMFYDPADRDDLCLDPRRIAQMADAFSRALDVDPRRLLDQAYA 245
Cdd:pfam04655 160 RPLHGDLHHSNVLDGGrRGWLAIDPKGLVGERGFDLANLFRDPDEDTIQALGPGRTERQLKRLAEALEVDPRRLLGWTLA 239

                         250
                  ....*....|.
gi 402294530  246 YGCLSAAWNAD 256
Cdd:pfam04655 240 YTGLSAAWARE 250
StrB COG3570
Streptomycin 6-kinase [Defense mechanisms];
3-274 9.53e-76

Streptomycin 6-kinase [Defense mechanisms];


Pssm-ID: 442791 [Multi-domain]  Cd Length: 301  Bit Score: 232.94  E-value: 9.53e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402294530   3 MPPVFPAHWHVSQPVLIADTFSSLVWKVSLPDGTPAIVKGLKPIEDIAdelRGADYLVWRNGRGAVRLLGRENNL--MLL 80
Cdd:COG3570   29 LLEELLDRWGLTPDGPPAHGSSSLVLPVRRADGTPAVLKLSPPDEEAA---REARALRWWDGRGAVRLLAADPDRgaLLL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402294530  81 EYA-GERMLSHIVAEhgDYQATEIAAELMAKLYAaseePLPSALLPIRDRFAALFQRARDDQNAGCQTD---YVHAAIIA 156
Cdd:COG3570  106 ERLdPGRSLADLPRR--DDEATRILADLLRRLHV----PAPPGLPPLADWFARLFAAAPARWRLADPVPrrlLARAAALA 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402294530 157 DQMMSNASELRGLHGDLHHENIM-FSSRGWLVIDPVGLVGEVGFGAANMFYDPADRDDLCLDPRRIAQMADAFSRALDVD 235
Cdd:COG3570  180 RELLASPAEDVLLHGDLHHGNVLaAGRRGWLAIDPKGLIGDPAFDLANLLRNPLDELPLATDPARLRRRVDLLAEAAGLD 259

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 402294530 236 PRRLLDQAYAYGCLSAAWNA---DGEEEQRDLAIAAAIKQVR 274
Cdd:COG3570  260 RDRLLAWALARAVLSALWALedgEAEDAERALAVAEALAALL 301
 
Name Accession Description Interval E-value
APH_6_hur pfam04655
Aminoglycoside/hydroxyurea antibiotic resistance kinase; The aminoglycoside ...
 10-256 5.56e-130

Aminoglycoside/hydroxyurea antibiotic resistance kinase; The aminoglycoside phosphotransferases achieve inactivation of their antibiotic substrates by phosphorylation utilizing ATP. Likewise hydroxyurea is inactivated by phosphorylation of the hydroxy group in the hydroxylamine moiety.


Pssm-ID: 398368 [Multi-domain]  Cd Length: 250  Bit Score: 368.86  E-value: 5.56e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402294530   10 HWHVSQPVLIADTFSSLVWKVSLPDGTPAIVKGLKPIEDIADELRGADYLVWRNGRGAVRLLGR--ENNLMLLEYA-GER 86
Cdd:pfam04655   1 RWHLVPDVEPPGTHSSLVLPVRTAEGAPAMLKLAPRRARPEEERRGADLLVWWGGRGAVRVLAEgdEEGALLLERAhGDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402294530   87 MLSHIVAEHGDYQATEIAAELMAKLYAASEEPLPSaLLPIRDRFAALFQRARDDQNAGCQTDYVHAAIIADQMMSNASEL 166
Cdd:pfam04655  81 SLRSLVAEGGDDEATRIAAGALARLHAPRPGPLPS-LLPLEDWFERLFAQARMRAGAVAQPLYVAAAAAARQLLGGPSEQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402294530  167 RGLHGDLHHENIMFSS-RGWLVIDPVGLVGEVGFGAANMFYDPADRDDLCLDPRRIAQMADAFSRALDVDPRRLLDQAYA 245
Cdd:pfam04655 160 RPLHGDLHHSNVLDGGrRGWLAIDPKGLVGERGFDLANLFRDPDEDTIQALGPGRTERQLKRLAEALEVDPRRLLGWTLA 239

                         250
                  ....*....|.
gi 402294530  246 YGCLSAAWNAD 256
Cdd:pfam04655 240 YTGLSAAWARE 250
StrB COG3570
Streptomycin 6-kinase [Defense mechanisms];
3-274 9.53e-76

Streptomycin 6-kinase [Defense mechanisms];


Pssm-ID: 442791 [Multi-domain]  Cd Length: 301  Bit Score: 232.94  E-value: 9.53e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402294530   3 MPPVFPAHWHVSQPVLIADTFSSLVWKVSLPDGTPAIVKGLKPIEDIAdelRGADYLVWRNGRGAVRLLGRENNL--MLL 80
Cdd:COG3570   29 LLEELLDRWGLTPDGPPAHGSSSLVLPVRRADGTPAVLKLSPPDEEAA---REARALRWWDGRGAVRLLAADPDRgaLLL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402294530  81 EYA-GERMLSHIVAEhgDYQATEIAAELMAKLYAaseePLPSALLPIRDRFAALFQRARDDQNAGCQTD---YVHAAIIA 156
Cdd:COG3570  106 ERLdPGRSLADLPRR--DDEATRILADLLRRLHV----PAPPGLPPLADWFARLFAAAPARWRLADPVPrrlLARAAALA 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402294530 157 DQMMSNASELRGLHGDLHHENIM-FSSRGWLVIDPVGLVGEVGFGAANMFYDPADRDDLCLDPRRIAQMADAFSRALDVD 235
Cdd:COG3570  180 RELLASPAEDVLLHGDLHHGNVLaAGRRGWLAIDPKGLIGDPAFDLANLLRNPLDELPLATDPARLRRRVDLLAEAAGLD 259

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 402294530 236 PRRLLDQAYAYGCLSAAWNA---DGEEEQRDLAIAAAIKQVR 274
Cdd:COG3570  260 RDRLLAWALARAVLSALWALedgEAEDAERALAVAEALAALL 301
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 19-189 6.70e-04

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: 40.18  E-value: 6.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402294530   19 IADTFSSLVWKVSLPDGtPAIVK---GLKPIEDIADELRGADYLVWRNGRGAVRLLGRENN-------LMLLEYAGERML 88
Cdd:pfam01636   5 ISSGASNRTYLVTTGDG-RYVLRlppPGRAAEELRRELALLRHLAAAGVPPVPRVLAGCTDaellglpFLLMEYLPGEVL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402294530   89 SHIVAEHGDYQATEIAAELMAKLYAASEEPLPSALLPIRDRFAALFQRARDDQNAGCQTDYVHAAIIA------DQMMSN 162
Cdd:pfam01636  84 ARPLLPEERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAAELLDRLEELEErllaalLALLPA 163

                         170       180
                  ....*....|....*....|....*....
gi 402294530  163 ASELRGLHGDLHHENIMFSSRGWL--VID 189
Cdd:pfam01636 164 ELPPVLVHGDLHPGNLLVDPGGRVsgVID 192
 
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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