NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15600688|ref|NP_254182|]
View 

homoserine kinase [Pseudomonas aeruginosa PAO1]

Protein Classification

homoserine kinase( domain architecture ID 10792412)

homoserine kinase catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK05231 PRK05231
homoserine kinase; Provisional
1-316 1.81e-152

homoserine kinase; Provisional


:

Pssm-ID: 235369 [Multi-domain]  Cd Length: 319  Bit Score: 429.99  E-value: 1.81e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688    1 MSVFTPLERSTLEAFLAPYDLGRLRDFRGIAEGSENSNFFVSLEHGEFVLTLVERGPVQDLPFFIELLDVLHEDGLPVPY 80
Cdd:PRK05231   1 MAVYTDVSDDELAAFLAPYDLGELLSLKGIAEGIENSNFFLTTTQGEYVLTLFERLTAEDLPFFLGLMQHLAARGVPVPA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688   81 ALRTRDGEALRRLEGKPALLQPRLAGRHERQPNAHHCQEVGDLLGHLHAATRGRILERPSDRGLPWMLEQGANLAPRLPE 160
Cdd:PRK05231  81 PVARRDGAALGELAGKPAAIVTFLEGKWPRAPTAAHCAEVGEMLARMHLAGRDFPLERPNLRGLAWWRELAPRLLPFLAD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688  161 QARALLAPALAEIAALDAER--PALPRANLHADLFRDNVLFDGPHLAGLIDFYNACSGWMLYDLAITLNDWCSNTDGSLD 238
Cdd:PRK05231 161 EQAALLEAELAAQLAFLASAawPALPRGVIHADLFRDNVLFEGDRLSGFIDFYFACNDKLLYDVAITLNDWCFEADGSLD 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600688  239 PARARALLAAYANRRPFTALEAEHWPSMLRVACVRFWLSRL-IAAEAFAGQDVLIHDPAEFEIRLAQRQNVEIHLPFAL 316
Cdd:PRK05231 241 ATKARALLAAYQSVRPLTAAERAALPVMLRGAALRFWLSRLyDWLLPRAGALVKPKDPLEFERKLRFRRAVVSALPYGL 319
 
Name Accession Description Interval E-value
PRK05231 PRK05231
homoserine kinase; Provisional
1-316 1.81e-152

homoserine kinase; Provisional


Pssm-ID: 235369 [Multi-domain]  Cd Length: 319  Bit Score: 429.99  E-value: 1.81e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688    1 MSVFTPLERSTLEAFLAPYDLGRLRDFRGIAEGSENSNFFVSLEHGEFVLTLVERGPVQDLPFFIELLDVLHEDGLPVPY 80
Cdd:PRK05231   1 MAVYTDVSDDELAAFLAPYDLGELLSLKGIAEGIENSNFFLTTTQGEYVLTLFERLTAEDLPFFLGLMQHLAARGVPVPA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688   81 ALRTRDGEALRRLEGKPALLQPRLAGRHERQPNAHHCQEVGDLLGHLHAATRGRILERPSDRGLPWMLEQGANLAPRLPE 160
Cdd:PRK05231  81 PVARRDGAALGELAGKPAAIVTFLEGKWPRAPTAAHCAEVGEMLARMHLAGRDFPLERPNLRGLAWWRELAPRLLPFLAD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688  161 QARALLAPALAEIAALDAER--PALPRANLHADLFRDNVLFDGPHLAGLIDFYNACSGWMLYDLAITLNDWCSNTDGSLD 238
Cdd:PRK05231 161 EQAALLEAELAAQLAFLASAawPALPRGVIHADLFRDNVLFEGDRLSGFIDFYFACNDKLLYDVAITLNDWCFEADGSLD 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600688  239 PARARALLAAYANRRPFTALEAEHWPSMLRVACVRFWLSRL-IAAEAFAGQDVLIHDPAEFEIRLAQRQNVEIHLPFAL 316
Cdd:PRK05231 241 ATKARALLAAYQSVRPLTAAERAALPVMLRGAALRFWLSRLyDWLLPRAGALVKPKDPLEFERKLRFRRAVVSALPYGL 319
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
9-305 6.32e-102

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: 301.10  E-value: 6.32e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688   9 RSTLEAFLAPYDLGRLRDFRGIAEGSENSNFFVSLEHGEFVLTLVERG-PVQDLPFFIELLDVLHEDGLPVPYALRTRDG 87
Cdd:cd05153   1 DEELAEFLAHYDLGELLSFEGIAAGIENTNYFVTTTDGRYVLTLFEKRrSAAELPFELELLDHLAQAGLPVPRPLADKDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688  88 EALRRLEGKPALLQPRLAGRHERQPNAHHCQEVGDLLGHLHAATRGRILERPSDRGLPWMLEQGANLAPRLPEQARALLA 167
Cdd:cd05153  81 ELLGELNGKPAALFPFLPGESLTTPTPEQCRAIGAALARLHLALAGFPPPRPNPRGLAWWKPLAERLKARLDLLAADDRA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688 168 PALAEIAALDA-ERPALPRANLHADLFRDNVLFDGPHLAGLIDFYNACSGWMLYDLAITLNDWCSNTDGSLDPARARALL 246
Cdd:cd05153 161 LLEDELARLQAlAPSDLPRGVIHADLFRDNVLFDGDRLSGIIDFYDACYDPLLYDLAIALNDWCFDDDGKLDPERAKALL 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688 247 AAYANRRPFTALEAEHWPSMLRVACVRFWLSRLIAAEAF-AGQDVLIHDPAEFEIRLAQR 305
Cdd:cd05153 241 AGYQSVRPLTEEEKAALPLLLRAAALRFWLSRLYDFHLPrEGALVTPKDPDEFLRRLRQR 300
thrB_alt TIGR00938
homoserine kinase, Neisseria type; Homoserine kinase is required in the biosynthesis of ...
1-303 1.58e-81

homoserine kinase, Neisseria type; Homoserine kinase is required in the biosynthesis of threonine from aspartate.The member of this family from Pseudomonas aeruginosa was shown by direct assay and complementation to act specifically as a homoserine kinase. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273351 [Multi-domain]  Cd Length: 307  Bit Score: 249.33  E-value: 1.58e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688     1 MSVFTPLERSTLEAFLAPYDLGRLRDFRGIAEGSENSNFFVSLEHGEFVLTLVE-RGPVQDLPFFIELLDVLHEDGLPVP 79
Cdd:TIGR00938   1 MAVYTSVSDEEMSSFLDGYDLGELLSLKGIAEGVENSNYLLTTDVGRYILTLYEkRVKAEELPFFLALTTHLAARGLPVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688    80 YALRTRDGEALRRLEGKPALLQPRLAGRHERQPNAHHCQEVGDLLGHLHAATRGRILERPSD-RGLPWMLEQGA--NLAP 156
Cdd:TIGR00938  81 KPVKSRDGRQLSTLAGKPACLVEFLQGLSVGRPTAMHCRPVGEVLAWMHLAGAHFPENRKNSlRLEAWHILAEKcfEAAP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688   157 RLPEQARALLAPALAEIAALDAERpaLPRANLHADLFRDNVLFDGPHLAGLIDFYNACSGWMLYDLAITLNDWCSNTDGS 236
Cdd:TIGR00938 161 QLEAHMGAELDKELDYLDKFWPRD--LPRGVIHADLFPDNVLFDGDSVKGVIDFYFACTDARAYDLAITVNAWCFDADDH 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600688   237 LDPARARALLAAYANRRPFTALEAEHWPSMLRVACVRFWLSRLIA-AEAFAGQDVLIHDPAEFEIRLA 303
Cdd:TIGR00938 239 FDADHAKALIKGYHQSRPLTEEEKAAFPVLLRGAAMRFLLTRLWDwVFTPAGALVVPKDPRDFERRLR 306
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
11-312 1.50e-68

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: 215.56  E-value: 1.50e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688  11 TLEAFLAPYDLGRLRDFRGIAEGsENSNFFVSLEHG-EFVLTLVE--RGPVQDLPFFIELLDVLHEDGLPVPYALRTRDG 87
Cdd:COG2334   2 ELAAALERYGLGPLSSLKPLNSG-ENRNYRVETEDGrRYVLKLYRpgRWSPEEIPFELALLAHLAAAGLPVPAPVPTRDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688  88 EALRRLEGKPALLQPRLAGRHERQPNAHHCQEVGDLLGHLHAATRGriLERPSDRGLPWMLEQGANLAPRL---PEQARA 164
Cdd:COG2334  81 ETLLELEGRPAALFPFLPGRSPEEPSPEQLEELGRLLARLHRALAD--FPRPNARDLAWWDELLERLLGPLlpdPEDRAL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688 165 LLAPALAEIAALDAERPALPRANLHADLFRDNVLFDGPHLAGLIDFYNACSGWMLYDLAITLNDWcsnTDGSLDPARARA 244
Cdd:COG2334 159 LEELLDRLEARLAPLLGALPRGVIHGDLHPDNVLFDGDGVSGLIDFDDAGYGPRLYDLAIALNGW---ADGPLDPARLAA 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600688 245 LLAAYANRRPFTALEAEHWPSMLRVACVRFWLSRLiaaeafagQDVLIHDPAEFEIRLAQRQNVEIHL 312
Cdd:COG2334 236 LLEGYRAVRPLTEAELAALPPLLRLRALRFLAWRL--------RRVRAKDPAFERYLRRQIALAWAAL 295
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
26-238 2.82e-32

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: 119.91  E-value: 2.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688    26 DFRGIAEGSENSNFFVSLEHGEFVLTLVERG-PVQDLPFFIELLDVLHEDGlpVPYALRTRDGEALRRLEGKPALLQPRL 104
Cdd:pfam01636   1 TLRPISSGASNRTYLVTTGDGRYVLRLPPPGrAAEELRRELALLRHLAAAG--VPPVPRVLAGCTDAELLGLPFLLMEYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688   105 AGRHERQPNAHHCQE-----VGDLLGHLHAAtrgrileRPSDRGLPWMLEQGANLAPRLPEQARALLAPALAEIAALDAE 179
Cdd:pfam01636  79 PGEVLARPLLPEERGalleaLGRALARLHAV-------DPAALPLAGRLARLLELLRQLEAALARLLAAELLDRLEELEE 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688   180 R----------PALPRANLHADLFRDNVLFD-GPHLAGLIDFYNACSGWMLYDLAITLNDWCSNTDGSLD 238
Cdd:pfam01636 152 RllaallallpAELPPVLVHGDLHPGNLLVDpGGRVSGVIDFEDAGLGDPAYDLAILLNSWGRELGAELL 221
 
Name Accession Description Interval E-value
PRK05231 PRK05231
homoserine kinase; Provisional
1-316 1.81e-152

homoserine kinase; Provisional


Pssm-ID: 235369 [Multi-domain]  Cd Length: 319  Bit Score: 429.99  E-value: 1.81e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688    1 MSVFTPLERSTLEAFLAPYDLGRLRDFRGIAEGSENSNFFVSLEHGEFVLTLVERGPVQDLPFFIELLDVLHEDGLPVPY 80
Cdd:PRK05231   1 MAVYTDVSDDELAAFLAPYDLGELLSLKGIAEGIENSNFFLTTTQGEYVLTLFERLTAEDLPFFLGLMQHLAARGVPVPA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688   81 ALRTRDGEALRRLEGKPALLQPRLAGRHERQPNAHHCQEVGDLLGHLHAATRGRILERPSDRGLPWMLEQGANLAPRLPE 160
Cdd:PRK05231  81 PVARRDGAALGELAGKPAAIVTFLEGKWPRAPTAAHCAEVGEMLARMHLAGRDFPLERPNLRGLAWWRELAPRLLPFLAD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688  161 QARALLAPALAEIAALDAER--PALPRANLHADLFRDNVLFDGPHLAGLIDFYNACSGWMLYDLAITLNDWCSNTDGSLD 238
Cdd:PRK05231 161 EQAALLEAELAAQLAFLASAawPALPRGVIHADLFRDNVLFEGDRLSGFIDFYFACNDKLLYDVAITLNDWCFEADGSLD 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600688  239 PARARALLAAYANRRPFTALEAEHWPSMLRVACVRFWLSRL-IAAEAFAGQDVLIHDPAEFEIRLAQRQNVEIHLPFAL 316
Cdd:PRK05231 241 ATKARALLAAYQSVRPLTAAERAALPVMLRGAALRFWLSRLyDWLLPRAGALVKPKDPLEFERKLRFRRAVVSALPYGL 319
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
9-305 6.32e-102

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: 301.10  E-value: 6.32e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688   9 RSTLEAFLAPYDLGRLRDFRGIAEGSENSNFFVSLEHGEFVLTLVERG-PVQDLPFFIELLDVLHEDGLPVPYALRTRDG 87
Cdd:cd05153   1 DEELAEFLAHYDLGELLSFEGIAAGIENTNYFVTTTDGRYVLTLFEKRrSAAELPFELELLDHLAQAGLPVPRPLADKDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688  88 EALRRLEGKPALLQPRLAGRHERQPNAHHCQEVGDLLGHLHAATRGRILERPSDRGLPWMLEQGANLAPRLPEQARALLA 167
Cdd:cd05153  81 ELLGELNGKPAALFPFLPGESLTTPTPEQCRAIGAALARLHLALAGFPPPRPNPRGLAWWKPLAERLKARLDLLAADDRA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688 168 PALAEIAALDA-ERPALPRANLHADLFRDNVLFDGPHLAGLIDFYNACSGWMLYDLAITLNDWCSNTDGSLDPARARALL 246
Cdd:cd05153 161 LLEDELARLQAlAPSDLPRGVIHADLFRDNVLFDGDRLSGIIDFYDACYDPLLYDLAIALNDWCFDDDGKLDPERAKALL 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688 247 AAYANRRPFTALEAEHWPSMLRVACVRFWLSRLIAAEAF-AGQDVLIHDPAEFEIRLAQR 305
Cdd:cd05153 241 AGYQSVRPLTEEEKAALPLLLRAAALRFWLSRLYDFHLPrEGALVTPKDPDEFLRRLRQR 300
thrB_alt TIGR00938
homoserine kinase, Neisseria type; Homoserine kinase is required in the biosynthesis of ...
1-303 1.58e-81

homoserine kinase, Neisseria type; Homoserine kinase is required in the biosynthesis of threonine from aspartate.The member of this family from Pseudomonas aeruginosa was shown by direct assay and complementation to act specifically as a homoserine kinase. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273351 [Multi-domain]  Cd Length: 307  Bit Score: 249.33  E-value: 1.58e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688     1 MSVFTPLERSTLEAFLAPYDLGRLRDFRGIAEGSENSNFFVSLEHGEFVLTLVE-RGPVQDLPFFIELLDVLHEDGLPVP 79
Cdd:TIGR00938   1 MAVYTSVSDEEMSSFLDGYDLGELLSLKGIAEGVENSNYLLTTDVGRYILTLYEkRVKAEELPFFLALTTHLAARGLPVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688    80 YALRTRDGEALRRLEGKPALLQPRLAGRHERQPNAHHCQEVGDLLGHLHAATRGRILERPSD-RGLPWMLEQGA--NLAP 156
Cdd:TIGR00938  81 KPVKSRDGRQLSTLAGKPACLVEFLQGLSVGRPTAMHCRPVGEVLAWMHLAGAHFPENRKNSlRLEAWHILAEKcfEAAP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688   157 RLPEQARALLAPALAEIAALDAERpaLPRANLHADLFRDNVLFDGPHLAGLIDFYNACSGWMLYDLAITLNDWCSNTDGS 236
Cdd:TIGR00938 161 QLEAHMGAELDKELDYLDKFWPRD--LPRGVIHADLFPDNVLFDGDSVKGVIDFYFACTDARAYDLAITVNAWCFDADDH 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600688   237 LDPARARALLAAYANRRPFTALEAEHWPSMLRVACVRFWLSRLIA-AEAFAGQDVLIHDPAEFEIRLA 303
Cdd:TIGR00938 239 FDADHAKALIKGYHQSRPLTEEEKAAFPVLLRGAAMRFLLTRLWDwVFTPAGALVVPKDPRDFERRLR 306
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
11-312 1.50e-68

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: 215.56  E-value: 1.50e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688  11 TLEAFLAPYDLGRLRDFRGIAEGsENSNFFVSLEHG-EFVLTLVE--RGPVQDLPFFIELLDVLHEDGLPVPYALRTRDG 87
Cdd:COG2334   2 ELAAALERYGLGPLSSLKPLNSG-ENRNYRVETEDGrRYVLKLYRpgRWSPEEIPFELALLAHLAAAGLPVPAPVPTRDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688  88 EALRRLEGKPALLQPRLAGRHERQPNAHHCQEVGDLLGHLHAATRGriLERPSDRGLPWMLEQGANLAPRL---PEQARA 164
Cdd:COG2334  81 ETLLELEGRPAALFPFLPGRSPEEPSPEQLEELGRLLARLHRALAD--FPRPNARDLAWWDELLERLLGPLlpdPEDRAL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688 165 LLAPALAEIAALDAERPALPRANLHADLFRDNVLFDGPHLAGLIDFYNACSGWMLYDLAITLNDWcsnTDGSLDPARARA 244
Cdd:COG2334 159 LEELLDRLEARLAPLLGALPRGVIHGDLHPDNVLFDGDGVSGLIDFDDAGYGPRLYDLAIALNGW---ADGPLDPARLAA 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600688 245 LLAAYANRRPFTALEAEHWPSMLRVACVRFWLSRLiaaeafagQDVLIHDPAEFEIRLAQRQNVEIHL 312
Cdd:COG2334 236 LLEGYRAVRPLTEAELAALPPLLRLRALRFLAWRL--------RRVRAKDPAFERYLRRQIALAWAAL 295
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
26-238 2.82e-32

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: 119.91  E-value: 2.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688    26 DFRGIAEGSENSNFFVSLEHGEFVLTLVERG-PVQDLPFFIELLDVLHEDGlpVPYALRTRDGEALRRLEGKPALLQPRL 104
Cdd:pfam01636   1 TLRPISSGASNRTYLVTTGDGRYVLRLPPPGrAAEELRRELALLRHLAAAG--VPPVPRVLAGCTDAELLGLPFLLMEYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688   105 AGRHERQPNAHHCQE-----VGDLLGHLHAAtrgrileRPSDRGLPWMLEQGANLAPRLPEQARALLAPALAEIAALDAE 179
Cdd:pfam01636  79 PGEVLARPLLPEERGalleaLGRALARLHAV-------DPAALPLAGRLARLLELLRQLEAALARLLAAELLDRLEELEE 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688   180 R----------PALPRANLHADLFRDNVLFD-GPHLAGLIDFYNACSGWMLYDLAITLNDWCSNTDGSLD 238
Cdd:pfam01636 152 RllaallallpAELPPVLVHGDLHPGNLLVDpGGRVSGVIDFEDAGLGDPAYDLAILLNSWGRELGAELL 221
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
30-230 4.00e-08

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: 51.92  E-value: 4.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688  30 IAEGSENSNFFVSLEhGEFVLTLVERGPVQDLPFFIELLDVLHED-GLPVPYALrtrdgeALRRLEGKPALLQPRLAGR- 107
Cdd:cd05120   6 IKEGGDNKVYLLGDP-REYVLKIGPPRLKKDLEKEAAMLQLLAGKlSLPVPKVY------GFGESDGWEYLLMERIEGEt 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688 108 -------HERQPNAHHCQEVGDLLGHLHAATrgrilerpsdrglpwmleqganlaprlpeqarallapalaeiaaldaer 180
Cdd:cd05120  79 lsevwprLSEEEKEKIADQLAEILAALHRID------------------------------------------------- 109
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15600688 181 palPRANLHADLFRDNVLFDG-PHLAGLIDFYNACSGWMLYDLAITLNDWC 230
Cdd:cd05120 110 ---SSVLTHGDLHPGNILVKPdGKLSGIIDWEFAGYGPPAFDYAAALRDWT 157
PRK06149 PRK06149
aminotransferase;
72-225 2.33e-07

aminotransferase;


Pssm-ID: 235716 [Multi-domain]  Cd Length: 972  Bit Score: 52.31  E-value: 2.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688   72 HEDGLPVPYALRTRDGEALRRLEGKPALLQPRLAGRHERQPNAH--HCQ-----EVGDLLGHLHAATRGriLERPS-DRG 143
Cdd:PRK06149  83 REPALRVPVVIPALDGEELLTLDVRGQGLRVRLLDYLPGQPLTRlgHLApasvaGLGALCARVARALAD--FDHPGlDRT 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688  144 LPWMLEQGANLAPRLPEQARALLAPALAEIAALDAER------PALPRANLHADLFRDNVLFD-----GPHLAGLIDFYN 212
Cdd:PRK06149 161 LQWDLRHAGPVVAHLLSHITDPAQRARIAEATRDAARrlqplaPALPLQAVHLDITDDNVVGSrdadgRWQPDGVIDFGD 240
                        170
                 ....*....|...
gi 15600688  213 ACSGWMLYDLAIT 225
Cdd:PRK06149 241 LVRTWRVADLAVT 253
PRK06148 PRK06148
hypothetical protein; Provisional
33-225 3.77e-06

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 48.48  E-value: 3.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688    33 GSENSNFFVSLEHG-EFVLTLVERG-PVQDLPFFIELLDVL--HEDGLPVPYALRTRDGEALRRLE---GKPAL--LQPR 103
Cdd:PRK06148   35 GERDLNFRLTTDDGaDYILKIVNPSePRVESDFQTAALDHLaaVAPDLPVPRLIPSLSGASLASAQdpdGEPRLlrLLSW 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688   104 LAGRH-----ERQPNAHHcqEVGDLLGHLHAATRGriLERPS-DRGLPWMLEQGANLAPRL-----PEQARALLAPALAE 172
Cdd:PRK06148  115 LPGTPlaeaaPRTEALLD--NLGRALGRLDRALQG--FMHPGaLRDLDWDLRHAGRARDRLhfiddPEDRALVERFLARF 190
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15600688   173 IAALDAERPALPRANLHADLFRDNVLFDG---PHLAGLIDFYNACSGWMLYDLAIT 225
Cdd:PRK06148  191 ERNVAPRLAALPAQVIHNDANDYNILVDAddgERISGLIDFGDAVHAPRICEVAIA 246
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
6-236 3.71e-05

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 44.72  E-value: 3.71e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688   6 PLERSTLEAFLAPY--DLGRLRDFRGIAEGSENSNFFVSLEhGEFVLTLVERGPVQDLPFFIE--LLDVLHED-GLPVPY 80
Cdd:COG3173   2 ELDEAALRALLAAQlpGLAGLPEVEPLSGGWSNLTYRLDTG-DRLVLRRPPRGLASAHDVRREarVLRALAPRlGVPVPR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688  81 ALRTRDGEA--------LRRLEGKPALLQPRLAGRHERqpnAHHCQEVGDLLGHLHAA-TRGRILERPSDRGLPWMLEQG 151
Cdd:COG3173  81 PLALGEDGEvigapfyvMEWVEGETLEDALPDLSPAER---RALARALGEFLAALHAVdPAAAGLADGRPEGLERQLARW 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600688 152 ANLAPRLPEQARALLAPALAEIAALDAERPALPRANL-HADLFRDNVLFDG--PHLAGLIDFYNACSGWMLYDLAITLND 228
Cdd:COG3173 158 RAQLRRALARTDDLPALRERLAAWLAANLPEWGPPVLvHGDLRPGNLLVDPddGRLTAVIDWELATLGDPAADLAYLLLY 237

                ....*...
gi 15600688 229 WCSNTDGS 236
Cdd:COG3173 238 WRLPDDLL 245
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH