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Conserved domains on  [gi|1194007197|gb|OTY09431|]
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S-methyl-5-thioribose kinase [Bacillus thuringiensis serovar muju]

Protein Classification

S-methyl-5-thioribose kinase( domain architecture ID 10008887)

S-methyl-5-thioribose kinase catalyzes the phosphorylation of methylthioribose to form methylthioribose-1-phosphate and is involved in the methionine salvage pathway

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MthN COG4857
5-Methylthioribose/5-deoxyribose kinase, methionine salvage pathway [Amino acid transport and ...
4-408 0e+00

5-Methylthioribose/5-deoxyribose kinase, methionine salvage pathway [Amino acid transport and metabolism];


:

Pssm-ID: 443885  Cd Length: 404  Bit Score: 584.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197   4 FTKYFLMEANDVIVYVKEKLSKFEHVKGLKCKEIGDGNLNYVFRVWDEKENISVIVKQAGDTARISDE-FKLSTNRIRIE 82
Cdd:COG4857     1 MSEYFPLTEEDVIAYLKEKAGLFGPDALLTVREIGDGNLNLVFRVSDEGTGKSVIVKQALPYVRVVGEsWPLTLDRARIE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197  83 SDVLQLEEELAPGLVPKVYFFDSVMNCCVMEDLSDHTILRTALINHQMFPKLADDLTTFLVNTLLLTSDVVMNHKEKKEL 162
Cdd:COG4857    81 AEALRLQAELAPGLVPKVYHFDEELALIVMEDLSDHKILRKELIAGKKFPGFAEHIGTFLARTLFYTSDLYLDPKEKKAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 163 VKNYINPELCEITEDLVYAEPFTNHnKRNELFPLNEgWIRERIYSDKELRMEVAKLKFSFMTNAQALLHGDLHTGSVFVR 242
Cdd:COG4857   161 VAKFINPELCKITEDLVFTDPYFDH-ERNNWTPELD-PVVEALRSDEALKLEVAKLKYRFMTKAEALLHGDLHTGSIFVN 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 243 DDSTKVIDPEFAFYGPMGYDIGNVMANLMFAWVNADATMSAGAEKDTYMDWLQSTMVEVIDLFKKKFLDAWDIHVTEIMA 322
Cdd:COG4857   239 EDSTKVIDPEFAFYGPIGFDIGNLIANLLLNYASQPGHDSDEEERADYRAWLLDTIEEIWETFEAEFRELWREEAKDPYA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 323 KEEGFNEIYLQSVLEDTAAVTGLELIRRIVGLAKVQDITCIENEEARARAERICLQVAKKFILRANQYKTGTSFVGTLKE 402
Cdd:COG4857   319 AAEGYLEAYLDRILQDALGFAGCELIRRIIGLAHVADLDSIEDPEKRAAAERLALELGRALILNREEIKSIDDLTALIRE 398

                  ....*.
gi 1194007197 403 QSMHYA 408
Cdd:COG4857   399 IAKEFQ 404
 
Name Accession Description Interval E-value
MthN COG4857
5-Methylthioribose/5-deoxyribose kinase, methionine salvage pathway [Amino acid transport and ...
4-408 0e+00

5-Methylthioribose/5-deoxyribose kinase, methionine salvage pathway [Amino acid transport and metabolism];


Pssm-ID: 443885  Cd Length: 404  Bit Score: 584.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197   4 FTKYFLMEANDVIVYVKEKLSKFEHVKGLKCKEIGDGNLNYVFRVWDEKENISVIVKQAGDTARISDE-FKLSTNRIRIE 82
Cdd:COG4857     1 MSEYFPLTEEDVIAYLKEKAGLFGPDALLTVREIGDGNLNLVFRVSDEGTGKSVIVKQALPYVRVVGEsWPLTLDRARIE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197  83 SDVLQLEEELAPGLVPKVYFFDSVMNCCVMEDLSDHTILRTALINHQMFPKLADDLTTFLVNTLLLTSDVVMNHKEKKEL 162
Cdd:COG4857    81 AEALRLQAELAPGLVPKVYHFDEELALIVMEDLSDHKILRKELIAGKKFPGFAEHIGTFLARTLFYTSDLYLDPKEKKAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 163 VKNYINPELCEITEDLVYAEPFTNHnKRNELFPLNEgWIRERIYSDKELRMEVAKLKFSFMTNAQALLHGDLHTGSVFVR 242
Cdd:COG4857   161 VAKFINPELCKITEDLVFTDPYFDH-ERNNWTPELD-PVVEALRSDEALKLEVAKLKYRFMTKAEALLHGDLHTGSIFVN 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 243 DDSTKVIDPEFAFYGPMGYDIGNVMANLMFAWVNADATMSAGAEKDTYMDWLQSTMVEVIDLFKKKFLDAWDIHVTEIMA 322
Cdd:COG4857   239 EDSTKVIDPEFAFYGPIGFDIGNLIANLLLNYASQPGHDSDEEERADYRAWLLDTIEEIWETFEAEFRELWREEAKDPYA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 323 KEEGFNEIYLQSVLEDTAAVTGLELIRRIVGLAKVQDITCIENEEARARAERICLQVAKKFILRANQYKTGTSFVGTLKE 402
Cdd:COG4857   319 AAEGYLEAYLDRILQDALGFAGCELIRRIIGLAHVADLDSIEDPEKRAAAERLALELGRALILNREEIKSIDDLTALIRE 398

                  ....*.
gi 1194007197 403 QSMHYA 408
Cdd:COG4857   399 IAKEFQ 404
MTRK TIGR01767
S-methyl-5-thioribose kinase; This enzyme, S-methyl-5-thioribose kinase (MtnK) is involved in ...
35-401 2.65e-102

S-methyl-5-thioribose kinase; This enzyme, S-methyl-5-thioribose kinase (MtnK) is involved in the methionine salvage pathway in certain bacteria.


Pssm-ID: 130828  Cd Length: 370  Bit Score: 307.97  E-value: 2.65e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197  35 KEIGDGNLNYVFRVWDEKENISVIVKQAGDTAR-ISDEFKLSTNRIRIESDVLQLEEELAPGLVPKVYFFDSVMNCCVME 113
Cdd:TIGR01767   1 QEVGDGNLNLVFHVYDQEGDRAAIVKQALPYVRvVGESWPLTLDRARIESSALIRQGEHVPHLVPRIFHFDTEMAVTVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 114 DLSDHTILRTALINHQMFPKLADDLTTFLVNTLLLTSDVVMNHKEKKELVKNYINPELCEITEDLVYAEPFTNHnKRNEL 193
Cdd:TIGR01767  81 DLSHHKIARKGLIEGENYPHLARHIGEFLAKTLFYSSDYALEPKVKKALVAQFTNPELCDITERLVFTDPYFDH-DTNDF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 194 FPLNEGWIrERIYSDKELRMEVAKLKFSFMTNAQALLHGDLHTGSVFVRDDSTKVIDPEFAFYGPMGYDIGNVMANLMFA 273
Cdd:TIGR01767 160 EEELRPFV-AKLRNDDSLKIEAAKLKHSFLASAETLLHGDLHSGSIFVSEHETKVIDPEFAFYGPIGFDIGQFIANLFLN 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 274 WVNADATMSAGaEKDTYMDWLQSTMVEVIDLFKKKFLDAWDIHVTEIM-AKEEGFNEIYLQSVLEDTAAVTGLELIRRIV 352
Cdd:TIGR01767 239 ALSRDGADQKG-KRDAMREPLLEHVNQVWETFEETFSELWQKDSLDMVyANIDGYLTDTLSHIWEDAIGFAGCELIRRTI 317
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1194007197 353 GLAKVQDITCIENEEARARAERICLQVAKKFILRANQYKTGTSFVGTLK 401
Cdd:TIGR01767 318 GLAHVADLDTIVDFAKRIGCKRLALETGRAFIVKRSEIKSIDEVIELFA 366
PLN02756 PLN02756
S-methyl-5-thioribose kinase
31-404 5.52e-78

S-methyl-5-thioribose kinase


Pssm-ID: 166397 [Multi-domain]  Cd Length: 418  Bit Score: 247.09  E-value: 5.52e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197  31 GLKCKEIGDGNLNYVFRVWDEKEniSVIVKQAGDTAR-ISDEFKLSTNRIRIESDVLQLEEELAPGLVPKVYFFDSVMNC 109
Cdd:PLN02756   34 DLKIKEVGDGNLNFVYIVVSSSG--SFVIKQALPYIRcIGESWPMTKERAYFEATALREHGRLCPDHVPEVYHFDRTMAL 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 110 CVMEDLSD-HTILRTALINHQMFPKLADDLTTFLVNTLLLTSDVVMNHKEKKELVKNYI-NPELCEITEDLVYAEPF--T 185
Cdd:PLN02756  112 IGMRYLEPpHIILRKGLIAGIEYPLLAEHMSDYMAKTLFFTSLLYHDTTEHKRAVAEFCgNVELCRLTEQVVFSDPYkvS 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 186 NHNKRNELFPLNEGwirERIYSDKELRMEVAKLKFSFMTNAQALLHGDLHTGSVFVRDDSTKVIDPEFAFYGPMGYDIGN 265
Cdd:PLN02756  192 QYNRWTSPYLDRDA---EAVREDNILKLEIAELKSMFCERAQALVHGDLHTGSVMVTPDSTQVIDPEFAFYGPMGFDIGA 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 266 VMANLMFAWVNADATMSAGAEKDTYMDWLQSTMVEVIDLFKKKFLDAWDIH--------VTEIMAKEEGF---NEIYLQS 334
Cdd:PLN02756  269 FLGNLILAYFAQDGHADQANDRKTYKEWILKTIEQTWNLFHKKFTALWDEHkdgsgeayLPEIYNNPELLqlvQKKYMQD 348
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 335 VLEDTAAVTGLELIRRIVGLAKVQDITCIENEEARARAERICLQVAKKFILRANQYKTGTSFVGTLKEQS 404
Cdd:PLN02756  349 LLHDTLGFGAAKMIRRIVGVAHVEDFESIEDASKRANCERQALDFAKMLLKERRKFQSIGEVVSAIQQLQ 418
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
33-290 8.94e-09

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: 55.59  E-value: 8.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197  33 KCKEIGDGNLNYVFRVWDEKEniSVIVKQAgdtarisdEFKLSTNRIRIESDVLQLEEELAPGLVPKVYFFDSV-----M 107
Cdd:pfam01636   1 TLRPISSGASNRTYLVTTGDG--RYVLRLP--------PPGRAAEELRRELALLRHLAAAGVPPVPRVLAGCTDaellgL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 108 NCCVMEDLsDHTILRTALINHQmfpklADDLTTFLVNTLLLTSDVvmnhkekkelvkNYINPELCEITEDLVYAEPFTNH 187
Cdd:pfam01636  71 PFLLMEYL-PGEVLARPLLPEE-----RGALLEALGRALARLHAV------------DPAALPLAGRLARLLELLRQLEA 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 188 NKRNELFPLNEGWIRERIysDKELRMEVAKLKFSFmtnAQALLHGDLHTGSVFVRDDS--TKVIDPEFAFYGPMGYDIGN 265
Cdd:pfam01636 133 ALARLLAAELLDRLEELE--ERLLAALLALLPAEL---PPVLVHGDLHPGNLLVDPGGrvSGVIDFEDAGLGDPAYDLAI 207
                         250       260
                  ....*....|....*....|....*.
gi 1194007197 266 VMANLMFA-WVNADATMSAGAEKDTY 290
Cdd:pfam01636 208 LLNSWGRElGAELLAAYLAAYGAFGY 233
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
228-268 3.69e-06

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: 46.53  E-value: 3.69e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1194007197 228 ALLHGDLHTGSVFVRDDS--TKVIDPEFAFYGPMGYDIGNVMA 268
Cdd:cd05120   112 VLTHGDLHPGNILVKPDGklSGIIDWEFAGYGPPAFDYAAALR 154
 
Name Accession Description Interval E-value
MthN COG4857
5-Methylthioribose/5-deoxyribose kinase, methionine salvage pathway [Amino acid transport and ...
4-408 0e+00

5-Methylthioribose/5-deoxyribose kinase, methionine salvage pathway [Amino acid transport and metabolism];


Pssm-ID: 443885  Cd Length: 404  Bit Score: 584.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197   4 FTKYFLMEANDVIVYVKEKLSKFEHVKGLKCKEIGDGNLNYVFRVWDEKENISVIVKQAGDTARISDE-FKLSTNRIRIE 82
Cdd:COG4857     1 MSEYFPLTEEDVIAYLKEKAGLFGPDALLTVREIGDGNLNLVFRVSDEGTGKSVIVKQALPYVRVVGEsWPLTLDRARIE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197  83 SDVLQLEEELAPGLVPKVYFFDSVMNCCVMEDLSDHTILRTALINHQMFPKLADDLTTFLVNTLLLTSDVVMNHKEKKEL 162
Cdd:COG4857    81 AEALRLQAELAPGLVPKVYHFDEELALIVMEDLSDHKILRKELIAGKKFPGFAEHIGTFLARTLFYTSDLYLDPKEKKAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 163 VKNYINPELCEITEDLVYAEPFTNHnKRNELFPLNEgWIRERIYSDKELRMEVAKLKFSFMTNAQALLHGDLHTGSVFVR 242
Cdd:COG4857   161 VAKFINPELCKITEDLVFTDPYFDH-ERNNWTPELD-PVVEALRSDEALKLEVAKLKYRFMTKAEALLHGDLHTGSIFVN 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 243 DDSTKVIDPEFAFYGPMGYDIGNVMANLMFAWVNADATMSAGAEKDTYMDWLQSTMVEVIDLFKKKFLDAWDIHVTEIMA 322
Cdd:COG4857   239 EDSTKVIDPEFAFYGPIGFDIGNLIANLLLNYASQPGHDSDEEERADYRAWLLDTIEEIWETFEAEFRELWREEAKDPYA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 323 KEEGFNEIYLQSVLEDTAAVTGLELIRRIVGLAKVQDITCIENEEARARAERICLQVAKKFILRANQYKTGTSFVGTLKE 402
Cdd:COG4857   319 AAEGYLEAYLDRILQDALGFAGCELIRRIIGLAHVADLDSIEDPEKRAAAERLALELGRALILNREEIKSIDDLTALIRE 398

                  ....*.
gi 1194007197 403 QSMHYA 408
Cdd:COG4857   399 IAKEFQ 404
MTRK TIGR01767
S-methyl-5-thioribose kinase; This enzyme, S-methyl-5-thioribose kinase (MtnK) is involved in ...
35-401 2.65e-102

S-methyl-5-thioribose kinase; This enzyme, S-methyl-5-thioribose kinase (MtnK) is involved in the methionine salvage pathway in certain bacteria.


Pssm-ID: 130828  Cd Length: 370  Bit Score: 307.97  E-value: 2.65e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197  35 KEIGDGNLNYVFRVWDEKENISVIVKQAGDTAR-ISDEFKLSTNRIRIESDVLQLEEELAPGLVPKVYFFDSVMNCCVME 113
Cdd:TIGR01767   1 QEVGDGNLNLVFHVYDQEGDRAAIVKQALPYVRvVGESWPLTLDRARIESSALIRQGEHVPHLVPRIFHFDTEMAVTVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 114 DLSDHTILRTALINHQMFPKLADDLTTFLVNTLLLTSDVVMNHKEKKELVKNYINPELCEITEDLVYAEPFTNHnKRNEL 193
Cdd:TIGR01767  81 DLSHHKIARKGLIEGENYPHLARHIGEFLAKTLFYSSDYALEPKVKKALVAQFTNPELCDITERLVFTDPYFDH-DTNDF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 194 FPLNEGWIrERIYSDKELRMEVAKLKFSFMTNAQALLHGDLHTGSVFVRDDSTKVIDPEFAFYGPMGYDIGNVMANLMFA 273
Cdd:TIGR01767 160 EEELRPFV-AKLRNDDSLKIEAAKLKHSFLASAETLLHGDLHSGSIFVSEHETKVIDPEFAFYGPIGFDIGQFIANLFLN 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 274 WVNADATMSAGaEKDTYMDWLQSTMVEVIDLFKKKFLDAWDIHVTEIM-AKEEGFNEIYLQSVLEDTAAVTGLELIRRIV 352
Cdd:TIGR01767 239 ALSRDGADQKG-KRDAMREPLLEHVNQVWETFEETFSELWQKDSLDMVyANIDGYLTDTLSHIWEDAIGFAGCELIRRTI 317
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1194007197 353 GLAKVQDITCIENEEARARAERICLQVAKKFILRANQYKTGTSFVGTLK 401
Cdd:TIGR01767 318 GLAHVADLDTIVDFAKRIGCKRLALETGRAFIVKRSEIKSIDEVIELFA 366
PLN02756 PLN02756
S-methyl-5-thioribose kinase
31-404 5.52e-78

S-methyl-5-thioribose kinase


Pssm-ID: 166397 [Multi-domain]  Cd Length: 418  Bit Score: 247.09  E-value: 5.52e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197  31 GLKCKEIGDGNLNYVFRVWDEKEniSVIVKQAGDTAR-ISDEFKLSTNRIRIESDVLQLEEELAPGLVPKVYFFDSVMNC 109
Cdd:PLN02756   34 DLKIKEVGDGNLNFVYIVVSSSG--SFVIKQALPYIRcIGESWPMTKERAYFEATALREHGRLCPDHVPEVYHFDRTMAL 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 110 CVMEDLSD-HTILRTALINHQMFPKLADDLTTFLVNTLLLTSDVVMNHKEKKELVKNYI-NPELCEITEDLVYAEPF--T 185
Cdd:PLN02756  112 IGMRYLEPpHIILRKGLIAGIEYPLLAEHMSDYMAKTLFFTSLLYHDTTEHKRAVAEFCgNVELCRLTEQVVFSDPYkvS 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 186 NHNKRNELFPLNEGwirERIYSDKELRMEVAKLKFSFMTNAQALLHGDLHTGSVFVRDDSTKVIDPEFAFYGPMGYDIGN 265
Cdd:PLN02756  192 QYNRWTSPYLDRDA---EAVREDNILKLEIAELKSMFCERAQALVHGDLHTGSVMVTPDSTQVIDPEFAFYGPMGFDIGA 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 266 VMANLMFAWVNADATMSAGAEKDTYMDWLQSTMVEVIDLFKKKFLDAWDIH--------VTEIMAKEEGF---NEIYLQS 334
Cdd:PLN02756  269 FLGNLILAYFAQDGHADQANDRKTYKEWILKTIEQTWNLFHKKFTALWDEHkdgsgeayLPEIYNNPELLqlvQKKYMQD 348
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 335 VLEDTAAVTGLELIRRIVGLAKVQDITCIENEEARARAERICLQVAKKFILRANQYKTGTSFVGTLKEQS 404
Cdd:PLN02756  349 LLHDTLGFGAAKMIRRIVGVAHVEDFESIEDASKRANCERQALDFAKMLLKERRKFQSIGEVVSAIQQLQ 418
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
33-290 8.94e-09

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: 55.59  E-value: 8.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197  33 KCKEIGDGNLNYVFRVWDEKEniSVIVKQAgdtarisdEFKLSTNRIRIESDVLQLEEELAPGLVPKVYFFDSV-----M 107
Cdd:pfam01636   1 TLRPISSGASNRTYLVTTGDG--RYVLRLP--------PPGRAAEELRRELALLRHLAAAGVPPVPRVLAGCTDaellgL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 108 NCCVMEDLsDHTILRTALINHQmfpklADDLTTFLVNTLLLTSDVvmnhkekkelvkNYINPELCEITEDLVYAEPFTNH 187
Cdd:pfam01636  71 PFLLMEYL-PGEVLARPLLPEE-----RGALLEALGRALARLHAV------------DPAALPLAGRLARLLELLRQLEA 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194007197 188 NKRNELFPLNEGWIRERIysDKELRMEVAKLKFSFmtnAQALLHGDLHTGSVFVRDDS--TKVIDPEFAFYGPMGYDIGN 265
Cdd:pfam01636 133 ALARLLAAELLDRLEELE--ERLLAALLALLPAEL---PPVLVHGDLHPGNLLVDPGGrvSGVIDFEDAGLGDPAYDLAI 207
                         250       260
                  ....*....|....*....|....*.
gi 1194007197 266 VMANLMFA-WVNADATMSAGAEKDTY 290
Cdd:pfam01636 208 LLNSWGRElGAELLAAYLAAYGAFGY 233
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
228-268 3.69e-06

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: 46.53  E-value: 3.69e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1194007197 228 ALLHGDLHTGSVFVRDDS--TKVIDPEFAFYGPMGYDIGNVMA 268
Cdd:cd05120   112 VLTHGDLHPGNILVKPDGklSGIIDWEFAGYGPPAFDYAAALR 154
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
226-279 1.97e-03

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 39.71  E-value: 1.97e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1194007197 226 AQALLHGDLHTGSVFVRDDSTK---VIDPEFAFYGPMGYDIgnvmANLMFAWVNADA 279
Cdd:COG3173   191 PPVLVHGDLRPGNLLVDPDDGRltaVIDWELATLGDPAADL----AYLLLYWRLPDD 243
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
227-269 2.98e-03

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: 39.14  E-value: 2.98e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1194007197 227 QALLHGDLHTGSVFVRDDS-TKVIDPEFAFYGPMGYDIGnVMAN 269
Cdd:COG2334   179 RGVIHGDLHPDNVLFDGDGvSGLIDFDDAGYGPRLYDLA-IALN 221
StrB COG3570
Streptomycin 6-kinase [Defense mechanisms];
226-269 4.08e-03

Streptomycin 6-kinase [Defense mechanisms];


Pssm-ID: 442791 [Multi-domain]  Cd Length: 301  Bit Score: 38.80  E-value: 4.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1194007197 226 AQALLHGDLHTGSVFVRDDST-KVIDPEfAFYGPMGYDIGNVMAN 269
Cdd:COG3570   188 EDVLLHGDLHHGNVLAAGRRGwLAIDPK-GLIGDPAFDLANLLRN 231
 
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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