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Conserved domains on  [gi|1831008666|ref|WP_168297524|]
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aminoglycoside phosphotransferase family protein [Rhizobium binae]

Protein Classification

aminoglycoside phosphotransferase family protein( domain architecture ID 10007572)

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
StrB COG3570
Streptomycin 6-kinase [Defense mechanisms];
1-264 1.53e-89

Streptomycin 6-kinase [Defense mechanisms];


:

Pssm-ID: 442791 [Multi-domain]  Cd Length: 301  Bit Score: 267.61  E-value: 1.53e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831008666   1 MFAPYLDRWSLISDGEPILTHSSRLLPVLWQE-RPAMLKVATDKTE-RYGALLMQWWDGDGAAHVYAHEGD--AVLLERA 76
Cdd:COG3570    29 LLEELLDRWGLTPDGPPAHGSSSLVLPVRRADgTPAVLKLSPPDEEaAREARALRWWDGRGAVRLLAADPDrgALLLERL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831008666  77 TGKRSLLAMAmkDEDDEASRILCRTAARLHAPrqkPLPDPIPLTRWFRELAPTADKV--------GGTFADCSTVANALL 148
Cdd:COG3570   109 DPGRSLADLP--RRDDEATRILADLLRRLHVP---APPGLPPLADWFARLFAAAPARwrladpvpRRLLARAAALARELL 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831008666 149 SDPRDVTILHGDIHHGNILDFETRGWLAIDPKRLHGERGFDFANIFANQ--ELPVITDLTRFRRQLPIVSMEARLEPKRL 226
Cdd:COG3570   184 ASPAEDVLLHGDLHHGNVLAAGRRGWLAIDPKGLIGDPAFDLANLLRNPldELPLATDPARLRRRVDLLAEAAGLDRDRL 263
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1831008666 227 LQWIAAYSGLSAAWFFGDANTPQVETALTVARLALSEL 264
Cdd:COG3570   264 LAWALARAVLSALWALEDGEAEDAERALAVAEALAALL 301
 
Name Accession Description Interval E-value
StrB COG3570
Streptomycin 6-kinase [Defense mechanisms];
1-264 1.53e-89

Streptomycin 6-kinase [Defense mechanisms];


Pssm-ID: 442791 [Multi-domain]  Cd Length: 301  Bit Score: 267.61  E-value: 1.53e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831008666   1 MFAPYLDRWSLISDGEPILTHSSRLLPVLWQE-RPAMLKVATDKTE-RYGALLMQWWDGDGAAHVYAHEGD--AVLLERA 76
Cdd:COG3570    29 LLEELLDRWGLTPDGPPAHGSSSLVLPVRRADgTPAVLKLSPPDEEaAREARALRWWDGRGAVRLLAADPDrgALLLERL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831008666  77 TGKRSLLAMAmkDEDDEASRILCRTAARLHAPrqkPLPDPIPLTRWFRELAPTADKV--------GGTFADCSTVANALL 148
Cdd:COG3570   109 DPGRSLADLP--RRDDEATRILADLLRRLHVP---APPGLPPLADWFARLFAAAPARwrladpvpRRLLARAAALARELL 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831008666 149 SDPRDVTILHGDIHHGNILDFETRGWLAIDPKRLHGERGFDFANIFANQ--ELPVITDLTRFRRQLPIVSMEARLEPKRL 226
Cdd:COG3570   184 ASPAEDVLLHGDLHHGNVLAAGRRGWLAIDPKGLIGDPAFDLANLLRNPldELPLATDPARLRRRVDLLAEAAGLDRDRL 263
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1831008666 227 LQWIAAYSGLSAAWFFGDANTPQVETALTVARLALSEL 264
Cdd:COG3570   264 LAWALARAVLSALWALEDGEAEDAERALAVAEALAALL 301
APH_6_hur pfam04655
Aminoglycoside/hydroxyurea antibiotic resistance kinase; The aminoglycoside ...
8-241 1.68e-76

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: 232.50  E-value: 1.68e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831008666   8 RWSLISDGEPILTHSSRLLPVLWQE-RPAMLKVATDKT----ERYGALLMQWWDGDGAAHV--YAHEGDAVLLERATGKR 80
Cdd:pfam04655   1 RWHLVPDVEPPGTHSSLVLPVRTAEgAPAMLKLAPRRArpeeERRGADLLVWWGGRGAVRVlaEGDEEGALLLERAHGDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831008666  81 SLLAMAMKDEDDEASRILCRTAARLHAPRQKPLPDPIPLTRWFRELAPTADKVGGTFA-----DCSTVANALLSDPRDVT 155
Cdd:pfam04655  81 SLRSLVAEGGDDEATRIAAGALARLHAPRPGPLPSLLPLEDWFERLFAQARMRAGAVAqplyvAAAAAARQLLGGPSEQR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831008666 156 ILHGDIHHGNILDFETRGWLAIDPKRLHGERGFDFANIFAN--QELPVITDLTRFRRQLPIVSMEARLEPKRLLQWIAAY 233
Cdd:pfam04655 161 PLHGDLHHSNVLDGGRRGWLAIDPKGLVGERGFDLANLFRDpdEDTIQALGPGRTERQLKRLAEALEVDPRRLLGWTLAY 240

                  ....*...
gi 1831008666 234 SGLSAAWF 241
Cdd:pfam04655 241 TGLSAAWA 248
 
Name Accession Description Interval E-value
StrB COG3570
Streptomycin 6-kinase [Defense mechanisms];
1-264 1.53e-89

Streptomycin 6-kinase [Defense mechanisms];


Pssm-ID: 442791 [Multi-domain]  Cd Length: 301  Bit Score: 267.61  E-value: 1.53e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831008666   1 MFAPYLDRWSLISDGEPILTHSSRLLPVLWQE-RPAMLKVATDKTE-RYGALLMQWWDGDGAAHVYAHEGD--AVLLERA 76
Cdd:COG3570    29 LLEELLDRWGLTPDGPPAHGSSSLVLPVRRADgTPAVLKLSPPDEEaAREARALRWWDGRGAVRLLAADPDrgALLLERL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831008666  77 TGKRSLLAMAmkDEDDEASRILCRTAARLHAPrqkPLPDPIPLTRWFRELAPTADKV--------GGTFADCSTVANALL 148
Cdd:COG3570   109 DPGRSLADLP--RRDDEATRILADLLRRLHVP---APPGLPPLADWFARLFAAAPARwrladpvpRRLLARAAALARELL 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831008666 149 SDPRDVTILHGDIHHGNILDFETRGWLAIDPKRLHGERGFDFANIFANQ--ELPVITDLTRFRRQLPIVSMEARLEPKRL 226
Cdd:COG3570   184 ASPAEDVLLHGDLHHGNVLAAGRRGWLAIDPKGLIGDPAFDLANLLRNPldELPLATDPARLRRRVDLLAEAAGLDRDRL 263
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1831008666 227 LQWIAAYSGLSAAWFFGDANTPQVETALTVARLALSEL 264
Cdd:COG3570   264 LAWALARAVLSALWALEDGEAEDAERALAVAEALAALL 301
APH_6_hur pfam04655
Aminoglycoside/hydroxyurea antibiotic resistance kinase; The aminoglycoside ...
8-241 1.68e-76

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: 232.50  E-value: 1.68e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831008666   8 RWSLISDGEPILTHSSRLLPVLWQE-RPAMLKVATDKT----ERYGALLMQWWDGDGAAHV--YAHEGDAVLLERATGKR 80
Cdd:pfam04655   1 RWHLVPDVEPPGTHSSLVLPVRTAEgAPAMLKLAPRRArpeeERRGADLLVWWGGRGAVRVlaEGDEEGALLLERAHGDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831008666  81 SLLAMAMKDEDDEASRILCRTAARLHAPRQKPLPDPIPLTRWFRELAPTADKVGGTFA-----DCSTVANALLSDPRDVT 155
Cdd:pfam04655  81 SLRSLVAEGGDDEATRIAAGALARLHAPRPGPLPSLLPLEDWFERLFAQARMRAGAVAqplyvAAAAAARQLLGGPSEQR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831008666 156 ILHGDIHHGNILDFETRGWLAIDPKRLHGERGFDFANIFAN--QELPVITDLTRFRRQLPIVSMEARLEPKRLLQWIAAY 233
Cdd:pfam04655 161 PLHGDLHHSNVLDGGRRGWLAIDPKGLVGERGFDLANLFRDpdEDTIQALGPGRTERQLKRLAEALEVDPRRLLGWTLAY 240

                  ....*...
gi 1831008666 234 SGLSAAWF 241
Cdd:pfam04655 241 TGLSAAWA 248
 
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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