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Conserved domains on  [gi|394480163|emb|CCI85668|]
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Kanamycin kinase [Lactobacillus pasteurii DSM 23907 = CRBIP 24.76]

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 cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
 23-259 5.92e-90

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: 265.98  E-value: 5.92e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163  23 QAKTYDSSSSPEARTYFIKRDR-GYFLKVAA---TDSLKDEATMDDYFYKKKIGPEVVEYLSL-DQDYLLTRQVPGYDCV 97
Cdd:cd05150    1 YRWEPDTIGESGARVYRLDGGGpVLYLKTAPagyAYELAREAERLRWLAGKLPVPEVLDYGSDdGGDWLLTTALPGRDAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163  98 QAEYLDQPERLVKLLAENLAWLHQLDFQGCPIT-RTSNYLEKALDNFEKGHYD-SNFLAESSFSDIESAHDYILAHRDWL 175
Cdd:cd05150   81 SLEPLLDPERLVDLLAEALRALHSLPIADCPFDrRLDARLAEARARVEAGLVDeDDFDEERQGRTAEELLAELEATRPAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163 176 KADILIHGDFCQPNIILDNWNFSGYIDLDCAGVGDRHVDIYWALHSLKFNFKTDKYASLFIDTYGRDKVDFKRLKLIDAI 255
Cdd:cd05150  161 EDLVVTHGDACLPNIILDPGRFSGFIDLGRLGVADRYQDLALAVRSLRENLGGEEYAERFLDAYGIDAPDPERLAYYRLL 240


                 ....
gi 394480163 256 EIFG 259
Cdd:cd05150  241 DEFF 244
 
Name Accession Description Interval E-value
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
 23-259 5.92e-90

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: 265.98  E-value: 5.92e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163  23 QAKTYDSSSSPEARTYFIKRDR-GYFLKVAA---TDSLKDEATMDDYFYKKKIGPEVVEYLSL-DQDYLLTRQVPGYDCV 97
Cdd:cd05150    1 YRWEPDTIGESGARVYRLDGGGpVLYLKTAPagyAYELAREAERLRWLAGKLPVPEVLDYGSDdGGDWLLTTALPGRDAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163  98 QAEYLDQPERLVKLLAENLAWLHQLDFQGCPIT-RTSNYLEKALDNFEKGHYD-SNFLAESSFSDIESAHDYILAHRDWL 175
Cdd:cd05150   81 SLEPLLDPERLVDLLAEALRALHSLPIADCPFDrRLDARLAEARARVEAGLVDeDDFDEERQGRTAEELLAELEATRPAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163 176 KADILIHGDFCQPNIILDNWNFSGYIDLDCAGVGDRHVDIYWALHSLKFNFKTDKYASLFIDTYGRDKVDFKRLKLIDAI 255
Cdd:cd05150  161 EDLVVTHGDACLPNIILDPGRFSGFIDLGRLGVADRYQDLALAVRSLRENLGGEEYAERFLDAYGIDAPDPERLAYYRLL 240


                 ....
gi 394480163 256 EIFG 259
Cdd:cd05150  241 DEFF 244
Aph COG3231
Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];
46-249 1.91e-34

Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442463 [Multi-domain]  Cd Length: 258  Bit Score: 124.26  E-value: 1.91e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163  46 YFLKVA---ATDSLKDEATMDDYFYKKKI-GPEVVEYLSLD-QDYLLTRQVPGYDCVQAEYLDQPERLVKLLAENLAWLH 120
Cdd:COG3231   40 LYLKIEpagPAAELEDEADRLRWLAGQGLpVPEVLDFGEDDgGAWLLTTAVPGRPAASVSEALDPERAVELLAEALRRLH 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163 121 QLDFQGCPIT-RTSNYLEKALDNFEKGHYD-SNFLAESSFSDIESAHDYILAHRDwlKADILI--HGDFCQPNIILDNWN 196
Cdd:COG3231  120 ALPVADCPFDrRLERRLAEARARVAAGLVDpDDFDEERRGRPPEELLAELLAERP--AEEDLVvtHGDACLPNILVDPGT 197

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 394480163 197 FSGYIDLDCAGVGDRHVDIYWALHSLKFNFkTDKYASLFIDTYGRD----KVDFKRL 249
Cdd:COG3231  198 FSGFIDLGRLGVADRYQDLALAARSLRENL-GEGWVEPFLDAYGIApdpeRLAFYRL 253
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 34-222 6.35e-22

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: 91.02  E-value: 6.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163   34 EARTYFIKRDRG-YFLKVA----ATDSLKDEATMDDYFYKKKIG--PEVVEYLSLDQD----YLLTRQVPGYDCVQAEYL 102
Cdd:pfam01636  10 SNRTYLVTTGDGrYVLRLPppgrAAEELRRELALLRHLAAAGVPpvPRVLAGCTDAELlglpFLLMEYLPGEVLARPLLP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163  103 DQPERLVKLLAENLAWLHQLDFQGCP---ITRTSNYLEKALDNFEKGHYDSNfLAESSFSDIESAHDYILAHRDWLKADI 179
Cdd:pfam01636  90 EERGALLEALGRALARLHAVDPAALPlagRLARLLELLRQLEAALARLLAAE-LLDRLEELEERLLAALLALLPAELPPV 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 394480163  180 LIHGDFCQPNIILD-NWNFSGYIDLDCAGVGDRHVDIYWALHSL 222
Cdd:pfam01636 169 LVHGDLHPGNLLVDpGGRVSGVIDFEDAGLGDPAYDLAILLNSW 212
 
Name Accession Description Interval E-value
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
 23-259 5.92e-90

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: 265.98  E-value: 5.92e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163  23 QAKTYDSSSSPEARTYFIKRDR-GYFLKVAA---TDSLKDEATMDDYFYKKKIGPEVVEYLSL-DQDYLLTRQVPGYDCV 97
Cdd:cd05150    1 YRWEPDTIGESGARVYRLDGGGpVLYLKTAPagyAYELAREAERLRWLAGKLPVPEVLDYGSDdGGDWLLTTALPGRDAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163  98 QAEYLDQPERLVKLLAENLAWLHQLDFQGCPIT-RTSNYLEKALDNFEKGHYD-SNFLAESSFSDIESAHDYILAHRDWL 175
Cdd:cd05150   81 SLEPLLDPERLVDLLAEALRALHSLPIADCPFDrRLDARLAEARARVEAGLVDeDDFDEERQGRTAEELLAELEATRPAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163 176 KADILIHGDFCQPNIILDNWNFSGYIDLDCAGVGDRHVDIYWALHSLKFNFKTDKYASLFIDTYGRDKVDFKRLKLIDAI 255
Cdd:cd05150  161 EDLVVTHGDACLPNIILDPGRFSGFIDLGRLGVADRYQDLALAVRSLRENLGGEEYAERFLDAYGIDAPDPERLAYYRLL 240


                 ....
gi 394480163 256 EIFG 259
Cdd:cd05150  241 DEFF 244
Aph COG3231
Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];
46-249 1.91e-34

Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442463 [Multi-domain]  Cd Length: 258  Bit Score: 124.26  E-value: 1.91e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163  46 YFLKVA---ATDSLKDEATMDDYFYKKKI-GPEVVEYLSLD-QDYLLTRQVPGYDCVQAEYLDQPERLVKLLAENLAWLH 120
Cdd:COG3231   40 LYLKIEpagPAAELEDEADRLRWLAGQGLpVPEVLDFGEDDgGAWLLTTAVPGRPAASVSEALDPERAVELLAEALRRLH 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163 121 QLDFQGCPIT-RTSNYLEKALDNFEKGHYD-SNFLAESSFSDIESAHDYILAHRDwlKADILI--HGDFCQPNIILDNWN 196
Cdd:COG3231  120 ALPVADCPFDrRLERRLAEARARVAAGLVDpDDFDEERRGRPPEELLAELLAERP--AEEDLVvtHGDACLPNILVDPGT 197

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 394480163 197 FSGYIDLDCAGVGDRHVDIYWALHSLKFNFkTDKYASLFIDTYGRD----KVDFKRL 249
Cdd:COG3231  198 FSGFIDLGRLGVADRYQDLALAARSLRENL-GEGWVEPFLDAYGIApdpeRLAFYRL 253
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 34-222 6.35e-22

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: 91.02  E-value: 6.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163   34 EARTYFIKRDRG-YFLKVA----ATDSLKDEATMDDYFYKKKIG--PEVVEYLSLDQD----YLLTRQVPGYDCVQAEYL 102
Cdd:pfam01636  10 SNRTYLVTTGDGrYVLRLPppgrAAEELRRELALLRHLAAAGVPpvPRVLAGCTDAELlglpFLLMEYLPGEVLARPLLP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163  103 DQPERLVKLLAENLAWLHQLDFQGCP---ITRTSNYLEKALDNFEKGHYDSNfLAESSFSDIESAHDYILAHRDWLKADI 179
Cdd:pfam01636  90 EERGALLEALGRALARLHAVDPAALPlagRLARLLELLRQLEAALARLLAAE-LLDRLEELEERLLAALLALLPAELPPV 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 394480163  180 LIHGDFCQPNIILD-NWNFSGYIDLDCAGVGDRHVDIYWALHSL 222
Cdd:pfam01636 169 LVHGDLHPGNLLVDpGGRVSGVIDFEDAGLGDPAYDLAILLNSW 212
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 73-241 4.77e-11

Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction only];


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 61.67  E-value: 4.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163  73 PEVVEYLS----LDQDYLLTRQVPG---YDCVQAEYLDQPERLVKLLAENLAWLHQLDFQGC-PITRTSNYLEKALDNFE 144
Cdd:COG3173   79 PRPLALGEdgevIGAPFYVMEWVEGetlEDALPDLSPAERRALARALGEFLAALHAVDPAAAgLADGRPEGLERQLARWR 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163 145 KgHYDSNFLAESSFSDI-ESAHDYILAHRDWLKADILIHGDFCQPNIILD--NWNFSGYIDLDCAGVGDRHVDIYWALHS 221
Cdd:COG3173  159 A-QLRRALARTDDLPALrERLAAWLAANLPEWGPPVLVHGDLRPGNLLVDpdDGRLTAVIDWELATLGDPAADLAYLLLY 237

                        170       180
                 ....*....|....*....|
gi 394480163 222 LKFNFKTDKYASLFIDTYGR 241
Cdd:COG3173  238 WRLPDDLLGPRAAFLAAYEE 257
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
 73-219 5.22e-07

N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This subfamily is composed of the N-terminal domains of vertebrate ACAD10 and ACAD11, and similar uncharacterized bacterial and eukaryotic proteins. ACADs are a family of flavoproteins that are involved in the beta-oxidation of fatty acyl-CoA derivatives. ACAD deficiency can cause metabolic disorders including muscle fatigue, hypoglycemia, and hepatic lipidosis. There are at least 11 distinct ACADs, some of which show distinct substrate specificities to either straight-chain or branched-chain fatty acids. ACAD10 is widely expressed in human tissues and highly expressed in liver, kidney, pancreas, and spleen. ACAD10 and ACAD11 are both significantly expressed in human brain tissues. They contain a long N-terminal domain with similarity to phosphotransferases with a Protein Kinase fold, which is absent in other ACADs. They may exhibit multiple functions in acyl-CoA oxidation pathways. ACAD11 utilizes substrates with carbon chain lengths of 20 to 26, with optimal activity towards C22CoA. ACAD10 may be associated with an increased risk in type II diabetes. The ACAD10/11-like 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: 270703 [Multi-domain]  Cd Length: 254  Bit Score: 49.54  E-value: 5.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163  73 PEVVEYLS----LDQDYLLTRQVPG---YDCVQAEYLDQPER--LVKLLAENLAWLHQLDFQGCP---ITRTSNYLEKAL 140
Cdd:cd05154   63 PRVLALCEdpsvLGAPFYVMERVDGrvlPDPLPRPDLSPEERraLARSLVDALAALHSVDPAALGladLGRPEGYLERQV 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163 141 DNFEKghydsnfLAESSFSDIESAHDYILahrDWLKADI-------LIHGDFCQPNIILDNWN-FSGYIDLDCAGVGDRH 212
Cdd:cd05154  143 DRWRR-------QLEAAATDPPPALEEAL---RWLRANLpadgrpvLVHGDFRLGNLLFDPDGrVTAVLDWELATLGDPL 212


                 ....*..
gi 394480163 213 VDIYWAL 219
Cdd:cd05154  213 EDLAWLL 219
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 34-215 8.31e-07

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: 47.68  E-value: 8.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163  34 EARTYFIKRDRGYFLKV---AATDSLKDEATMDDYFYKKKI--GPEVVE-YLSLDQDYLLTRQVPGYDCVQAEYL---DQ 104
Cdd:cd05120   11 DNKVYLLGDPREYVLKIgppRLKKDLEKEAAMLQLLAGKLSlpVPKVYGfGESDGWEYLLMERIEGETLSEVWPRlseEE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163 105 PERLVKLLAENLAWLHQLDFQGcpitrtsnylekaldnfekghydsnflaessfsdiesahdyilahrdwlkadiLIHGD 184
Cdd:cd05120   91 KEKIADQLAEILAALHRIDSSV-----------------------------------------------------LTHGD 117

                        170       180       190
                 ....*....|....*....|....*....|..
gi 394480163 185 FCQPNIILDN-WNFSGYIDLDCAGVGDRHVDI 215
Cdd:cd05120  118 LHPGNILVKPdGKLSGIIDWEFAGYGPPAFDY 149
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
 102-221 6.17e-05

Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and Choline kinase; This subfamily is composed of uncharacterized bacterial proteins with similarity to APH and ChoK. Other APH/ChoK-like proteins include 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). These proteins 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-like 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: 270704 [Multi-domain]  Cd Length: 234  Bit Score: 42.99  E-value: 6.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163 102 LDQPERLVKLLAENLAWLHQLD-------FQGCPITRTSNYLEKALDNFEK--GHYDSNFLAESsfsdIESAhdyiLAHR 172
Cdd:cd05155   86 LADPAAAAEDLARFLAALHAIDpagppnpGRGNPLRGRDLAVRDAEEALAAlaGLLDVAAARAL----WERA----LAAP 157

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 394480163 173 DWLKADILIHGDFCQPNIILDNWNFSGYIDLDCAGVGDRHVD--IYWALHS 221
Cdd:cd05155  158 AWAGPPVWLHGDLHPGNLLVRDGRLSAVIDFGDLGVGDPACDlaIAWTLFD 208
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
 34-223 2.76e-04

Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal transduction mechanisms]; Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist is part of the Pathway/BioSystem: Threonine biosynthesis


Pssm-ID: 441905 [Multi-domain]  Cd Length: 297  Bit Score: 41.45  E-value: 2.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163  34 EARTYFIKRDRG--YFLKVAATDSLKDEATMD-----DYFYKKKIG-PEVV-----EYLSLDQDY---LLTRqVPGydcv 97
Cdd:COG2334   25 ENRNYRVETEDGrrYVLKLYRPGRWSPEEIPFelallAHLAAAGLPvPAPVptrdgETLLELEGRpaaLFPF-LPG---- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163  98 QAEYLDQPERLvKLLAENLAWLHQL--DFQGcPITRTSNYLEKALDNFEKGH-YDSNFLAEssfsdIESAHDYILAHRDW 174
Cdd:COG2334  100 RSPEEPSPEQL-EELGRLLARLHRAlaDFPR-PNARDLAWWDELLERLLGPLlPDPEDRAL-----LEELLDRLEARLAP 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 394480163 175 LKAD---ILIHGDfCQP-NIILDNWNFSGYIDLDCAGVGDRHVDIYWALHSLK 223
Cdd:COG2334  173 LLGAlprGVIHGD-LHPdNVLFDGDGVSGLIDFDDAGYGPRLYDLAIALNGWA 224
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
 106-215 6.76e-03

Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase 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: 270702 [Multi-domain]  Cd Length: 300  Bit Score: 37.24  E-value: 6.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394480163 106 ERLVKLLAENLAWLHQLDfQGCPITRTSNYLEkaldNFEKGHYDS--NFLAESSFSDIESAHDYILAHRDWLKADI---L 180
Cdd:cd05153  107 PEQCRAIGAALARLHLAL-AGFPPPRPNPRGL----AWWKPLAERlkARLDLLAADDRALLEDELARLQALAPSDLprgV 181

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 394480163 181 IHGDFCQPNIILDNWNFSGYIDLDCAGVGDRHVDI 215
Cdd:cd05153  182 IHADLFRDNVLFDGDRLSGIIDFYDACYDPLLYDL 216
 
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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