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Conserved domains on  [gi|2221283947|gb|UON17376|]
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homoserine kinase [Neisseria meningitidis]

Protein Classification

protein kinase family protein; serine/threonine-protein kinase( domain architecture ID 10795607)

protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to substrates such as serine/threonine and/or tyrosine residues on proteins, or may be a pseudokinase; serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
thrB_alt TIGR00938
homoserine kinase, Neisseria type; Homoserine kinase is required in the biosynthesis of ...
1-303 0e+00

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: 525.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947   1 MSVYTSVSDDEMRGFLSGYDLGEFVSLQGIAQGITNSNYFLTTTSGRYVLTVFEVL-KQEELPFFLELNRHLSMKGVAVA 79
Cdd:TIGR00938   1 MAVYTSVSDEEMSSFLDGYDLGELLSLKGIAEGVENSNYLLTTDVGRYILTLYEKRvKAEELPFFLALTTHLAARGLPVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947  80 APVARKDGRLDSVLAGKPACLVACLKGSDTALPTAEQCFHTGAMLAKMHLAAADFPLEMEN-PRYNAWWTEACAR--LLP 156
Cdd:TIGR00938  81 KPVKSRDGRQLSTLAGKPACLVEFLQGLSVGRPTAMHCRPVGEVLAWMHLAGAHFPENRKNsLRLEAWHILAEKCfeAAP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947 157 VLSQDDAALLCSEIDALKDNLGNHLPSGIIHADLFKDNVLLDGGQVSGFIDFYYACRGNFMYDLAIAVNDWARTADNKLD 236
Cdd:TIGR00938 161 QLEAHMGAELDKELDYLDKFWPRDLPRGVIHADLFPDNVLFDGDSVKGVIDFYFACTDARAYDLAITVNAWCFDADDHFD 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2221283947 237 EALKKAFIGGYEGVRPLSAEEKAYFPTAQRAGCIRFWVSRLLDFHFPQAGEMTFIKDPNAFRNLLLS 303
Cdd:TIGR00938 241 ADHAKALIKGYHQSRPLTEEEKAAFPVLLRGAAMRFLLTRLWDWVFTPAGALVVPKDPRDFERRLRF 307
 
Name Accession Description Interval E-value
thrB_alt TIGR00938
homoserine kinase, Neisseria type; Homoserine kinase is required in the biosynthesis of ...
1-303 0e+00

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: 525.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947   1 MSVYTSVSDDEMRGFLSGYDLGEFVSLQGIAQGITNSNYFLTTTSGRYVLTVFEVL-KQEELPFFLELNRHLSMKGVAVA 79
Cdd:TIGR00938   1 MAVYTSVSDEEMSSFLDGYDLGELLSLKGIAEGVENSNYLLTTDVGRYILTLYEKRvKAEELPFFLALTTHLAARGLPVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947  80 APVARKDGRLDSVLAGKPACLVACLKGSDTALPTAEQCFHTGAMLAKMHLAAADFPLEMEN-PRYNAWWTEACAR--LLP 156
Cdd:TIGR00938  81 KPVKSRDGRQLSTLAGKPACLVEFLQGLSVGRPTAMHCRPVGEVLAWMHLAGAHFPENRKNsLRLEAWHILAEKCfeAAP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947 157 VLSQDDAALLCSEIDALKDNLGNHLPSGIIHADLFKDNVLLDGGQVSGFIDFYYACRGNFMYDLAIAVNDWARTADNKLD 236
Cdd:TIGR00938 161 QLEAHMGAELDKELDYLDKFWPRDLPRGVIHADLFPDNVLFDGDSVKGVIDFYFACTDARAYDLAITVNAWCFDADDHFD 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2221283947 237 EALKKAFIGGYEGVRPLSAEEKAYFPTAQRAGCIRFWVSRLLDFHFPQAGEMTFIKDPNAFRNLLLS 303
Cdd:TIGR00938 241 ADHAKALIKGYHQSRPLTEEEKAAFPVLLRGAAMRFLLTRLWDWVFTPAGALVVPKDPRDFERRLRF 307
PRK05231 PRK05231
homoserine kinase; Provisional
1-301 4.76e-165

homoserine kinase; Provisional


Pssm-ID: 235369 [Multi-domain]  Cd Length: 319  Bit Score: 461.19  E-value: 4.76e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947   1 MSVYTSVSDDEMRGFLSGYDLGEFVSLQGIAQGITNSNYFLTTTSGRYVLTVFEVLKQEELPFFLELNRHLSMKGVAVAA 80
Cdd:PRK05231    1 MAVYTDVSDDELAAFLAPYDLGELLSLKGIAEGIENSNFFLTTTQGEYVLTLFERLTAEDLPFFLGLMQHLAARGVPVPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947  81 PVARKDGRLDSVLAGKPACLVACLKGSDTALPTAEQCFHTGAMLAKMHLAAADFPLEMENPRYNAWWTEACARLLPVLSQ 160
Cdd:PRK05231   81 PVARRDGAALGELAGKPAAIVTFLEGKWPRAPTAAHCAEVGEMLARMHLAGRDFPLERPNLRGLAWWRELAPRLLPFLAD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947 161 DDAALLCSEIDALKDNLGNH----LPSGIIHADLFKDNVLLDGGQVSGFIDFYYACRGNFMYDLAIAVNDWARTADNKLD 236
Cdd:PRK05231  161 EQAALLEAELAAQLAFLASAawpaLPRGVIHADLFRDNVLFEGDRLSGFIDFYFACNDKLLYDVAITLNDWCFEADGSLD 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2221283947 237 EALKKAFIGGYEGVRPLSAEEKAYFPTAQRAGCIRFWVSRLLDFHFPQAGEMTFIKDPNAFRNLL 301
Cdd:PRK05231  241 ATKARALLAAYQSVRPLTAAERAALPVMLRGAALRFWLSRLYDWLLPRAGALVKPKDPLEFERKL 305
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
9-302 4.55e-132

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: 376.98  E-value: 4.55e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947   9 DDEMRGFLSGYDLGEFVSLQGIAQGITNSNYFLTTTSGRYVLTVFEVLKQ-EELPFFLELNRHLSMKGVAVAAPVARKDG 87
Cdd:cd05153     1 DEELAEFLAHYDLGELLSFEGIAAGIENTNYFVTTTDGRYVLTLFEKRRSaAELPFELELLDHLAQAGLPVPRPLADKDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947  88 RLDSVLAGKPACLVACLKGSDTALPTAEQCFHTGAMLAKMHLAAADFPLEMENPRYNAWWTEACARLLPVL---SQDDAA 164
Cdd:cd05153    81 ELLGELNGKPAALFPFLPGESLTTPTPEQCRAIGAALARLHLALAGFPPPRPNPRGLAWWKPLAERLKARLdllAADDRA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947 165 LLCSEIDALKDNLGNHLPSGIIHADLFKDNVLLDGGQVSGFIDFYYACRGNFMYDLAIAVNDWARTADNKLDEALKKAFI 244
Cdd:cd05153   161 LLEDELARLQALAPSDLPRGVIHADLFRDNVLFDGDRLSGIIDFYDACYDPLLYDLAIALNDWCFDDDGKLDPERAKALL 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2221283947 245 GGYEGVRPLSAEEKAYFPTAQRAGCIRFWVSRLLDFHFPQAGEMTFIKDPNAFRNLLL 302
Cdd:cd05153   241 AGYQSVRPLTEEEKAALPLLLRAAALRFWLSRLYDFHLPREGALVTPKDPDEFLRRLR 298
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
10-281 6.86e-87

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: 262.17  E-value: 6.86e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947  10 DEMRGFLSGYDLGEFVSLQGIAQGItNSNYFLTTTSG-RYVLTVFE--VLKQEELPFFLELNRHLSMKGVAVAAPVARKD 86
Cdd:COG2334     1 DELAAALERYGLGPLSSLKPLNSGE-NRNYRVETEDGrRYVLKLYRpgRWSPEEIPFELALLAHLAAAGLPVPAPVPTRD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947  87 GRLDSVLAGKPACLVACLKGSDTALPTAEQCFHTGAMLAKMHLAAADFPleMENPRYNAWWTEACARLLP--VLSQDDAA 164
Cdd:COG2334    80 GETLLELEGRPAALFPFLPGRSPEEPSPEQLEELGRLLARLHRALADFP--RPNARDLAWWDELLERLLGplLPDPEDRA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947 165 LLCSEIDALKDNLG---NHLPSGIIHADLFKDNVLLDGGQVSGFIDFYYACRGNFMYDLAIAVNDWartADNKLDEALKK 241
Cdd:COG2334   158 LLEELLDRLEARLApllGALPRGVIHGDLHPDNVLFDGDGVSGLIDFDDAGYGPRLYDLAIALNGW---ADGPLDPARLA 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2221283947 242 AFIGGYEGVRPLSAEEKAYFPTAQRAGCIRFWVSRLLDFH 281
Cdd:COG2334   235 ALLEGYRAVRPLTEAELAALPPLLRLRALRFLAWRLRRVR 274
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
26-253 2.69e-38

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: 135.32  E-value: 2.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947  26 SLQGIAQGITNSNYFLTTTSGRYVLTVFE-VLKQEELPFFLELNRHLSMKGV-AVAAPVArkdGRLDSVLAGKPACLVAC 103
Cdd:pfam01636   1 TLRPISSGASNRTYLVTTGDGRYVLRLPPpGRAAEELRRELALLRHLAAAGVpPVPRVLA---GCTDAELLGLPFLLMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947 104 LKGSD-----TALPTAEQCFHTGAMLAKMH-LAAADFPLEMENPR--YNAWWTEA-CARLLPVLSQDD-AALLCSEIDAL 173
Cdd:pfam01636  78 LPGEVlarplLPEERGALLEALGRALARLHaVDPAALPLAGRLARllELLRQLEAaLARLLAAELLDRlEELEERLLAAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947 174 KDNLGNHLPSGIIHADLFKDNVLLD-GGQVSGFIDFYYACRGNFMYDLAIAVNDWARTADNKLDEALKKAFI-GGYEGVR 251
Cdd:pfam01636 158 LALLPAELPPVLVHGDLHPGNLLVDpGGRVSGVIDFEDAGLGDPAYDLAILLNSWGRELGAELLAAYLAAYGaFGYARLR 237

                  ..
gi 2221283947 252 PL 253
Cdd:pfam01636 238 EL 239
 
Name Accession Description Interval E-value
thrB_alt TIGR00938
homoserine kinase, Neisseria type; Homoserine kinase is required in the biosynthesis of ...
1-303 0e+00

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: 525.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947   1 MSVYTSVSDDEMRGFLSGYDLGEFVSLQGIAQGITNSNYFLTTTSGRYVLTVFEVL-KQEELPFFLELNRHLSMKGVAVA 79
Cdd:TIGR00938   1 MAVYTSVSDEEMSSFLDGYDLGELLSLKGIAEGVENSNYLLTTDVGRYILTLYEKRvKAEELPFFLALTTHLAARGLPVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947  80 APVARKDGRLDSVLAGKPACLVACLKGSDTALPTAEQCFHTGAMLAKMHLAAADFPLEMEN-PRYNAWWTEACAR--LLP 156
Cdd:TIGR00938  81 KPVKSRDGRQLSTLAGKPACLVEFLQGLSVGRPTAMHCRPVGEVLAWMHLAGAHFPENRKNsLRLEAWHILAEKCfeAAP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947 157 VLSQDDAALLCSEIDALKDNLGNHLPSGIIHADLFKDNVLLDGGQVSGFIDFYYACRGNFMYDLAIAVNDWARTADNKLD 236
Cdd:TIGR00938 161 QLEAHMGAELDKELDYLDKFWPRDLPRGVIHADLFPDNVLFDGDSVKGVIDFYFACTDARAYDLAITVNAWCFDADDHFD 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2221283947 237 EALKKAFIGGYEGVRPLSAEEKAYFPTAQRAGCIRFWVSRLLDFHFPQAGEMTFIKDPNAFRNLLLS 303
Cdd:TIGR00938 241 ADHAKALIKGYHQSRPLTEEEKAAFPVLLRGAAMRFLLTRLWDWVFTPAGALVVPKDPRDFERRLRF 307
PRK05231 PRK05231
homoserine kinase; Provisional
1-301 4.76e-165

homoserine kinase; Provisional


Pssm-ID: 235369 [Multi-domain]  Cd Length: 319  Bit Score: 461.19  E-value: 4.76e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947   1 MSVYTSVSDDEMRGFLSGYDLGEFVSLQGIAQGITNSNYFLTTTSGRYVLTVFEVLKQEELPFFLELNRHLSMKGVAVAA 80
Cdd:PRK05231    1 MAVYTDVSDDELAAFLAPYDLGELLSLKGIAEGIENSNFFLTTTQGEYVLTLFERLTAEDLPFFLGLMQHLAARGVPVPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947  81 PVARKDGRLDSVLAGKPACLVACLKGSDTALPTAEQCFHTGAMLAKMHLAAADFPLEMENPRYNAWWTEACARLLPVLSQ 160
Cdd:PRK05231   81 PVARRDGAALGELAGKPAAIVTFLEGKWPRAPTAAHCAEVGEMLARMHLAGRDFPLERPNLRGLAWWRELAPRLLPFLAD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947 161 DDAALLCSEIDALKDNLGNH----LPSGIIHADLFKDNVLLDGGQVSGFIDFYYACRGNFMYDLAIAVNDWARTADNKLD 236
Cdd:PRK05231  161 EQAALLEAELAAQLAFLASAawpaLPRGVIHADLFRDNVLFEGDRLSGFIDFYFACNDKLLYDVAITLNDWCFEADGSLD 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2221283947 237 EALKKAFIGGYEGVRPLSAEEKAYFPTAQRAGCIRFWVSRLLDFHFPQAGEMTFIKDPNAFRNLL 301
Cdd:PRK05231  241 ATKARALLAAYQSVRPLTAAERAALPVMLRGAALRFWLSRLYDWLLPRAGALVKPKDPLEFERKL 305
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
9-302 4.55e-132

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: 376.98  E-value: 4.55e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947   9 DDEMRGFLSGYDLGEFVSLQGIAQGITNSNYFLTTTSGRYVLTVFEVLKQ-EELPFFLELNRHLSMKGVAVAAPVARKDG 87
Cdd:cd05153     1 DEELAEFLAHYDLGELLSFEGIAAGIENTNYFVTTTDGRYVLTLFEKRRSaAELPFELELLDHLAQAGLPVPRPLADKDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947  88 RLDSVLAGKPACLVACLKGSDTALPTAEQCFHTGAMLAKMHLAAADFPLEMENPRYNAWWTEACARLLPVL---SQDDAA 164
Cdd:cd05153    81 ELLGELNGKPAALFPFLPGESLTTPTPEQCRAIGAALARLHLALAGFPPPRPNPRGLAWWKPLAERLKARLdllAADDRA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947 165 LLCSEIDALKDNLGNHLPSGIIHADLFKDNVLLDGGQVSGFIDFYYACRGNFMYDLAIAVNDWARTADNKLDEALKKAFI 244
Cdd:cd05153   161 LLEDELARLQALAPSDLPRGVIHADLFRDNVLFDGDRLSGIIDFYDACYDPLLYDLAIALNDWCFDDDGKLDPERAKALL 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2221283947 245 GGYEGVRPLSAEEKAYFPTAQRAGCIRFWVSRLLDFHFPQAGEMTFIKDPNAFRNLLL 302
Cdd:cd05153   241 AGYQSVRPLTEEEKAALPLLLRAAALRFWLSRLYDFHLPREGALVTPKDPDEFLRRLR 298
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
10-281 6.86e-87

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: 262.17  E-value: 6.86e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947  10 DEMRGFLSGYDLGEFVSLQGIAQGItNSNYFLTTTSG-RYVLTVFE--VLKQEELPFFLELNRHLSMKGVAVAAPVARKD 86
Cdd:COG2334     1 DELAAALERYGLGPLSSLKPLNSGE-NRNYRVETEDGrRYVLKLYRpgRWSPEEIPFELALLAHLAAAGLPVPAPVPTRD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947  87 GRLDSVLAGKPACLVACLKGSDTALPTAEQCFHTGAMLAKMHLAAADFPleMENPRYNAWWTEACARLLP--VLSQDDAA 164
Cdd:COG2334    80 GETLLELEGRPAALFPFLPGRSPEEPSPEQLEELGRLLARLHRALADFP--RPNARDLAWWDELLERLLGplLPDPEDRA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947 165 LLCSEIDALKDNLG---NHLPSGIIHADLFKDNVLLDGGQVSGFIDFYYACRGNFMYDLAIAVNDWartADNKLDEALKK 241
Cdd:COG2334   158 LLEELLDRLEARLApllGALPRGVIHGDLHPDNVLFDGDGVSGLIDFDDAGYGPRLYDLAIALNGW---ADGPLDPARLA 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2221283947 242 AFIGGYEGVRPLSAEEKAYFPTAQRAGCIRFWVSRLLDFH 281
Cdd:COG2334   235 ALLEGYRAVRPLTEAELAALPPLLRLRALRFLAWRLRRVR 274
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
26-253 2.69e-38

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: 135.32  E-value: 2.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947  26 SLQGIAQGITNSNYFLTTTSGRYVLTVFE-VLKQEELPFFLELNRHLSMKGV-AVAAPVArkdGRLDSVLAGKPACLVAC 103
Cdd:pfam01636   1 TLRPISSGASNRTYLVTTGDGRYVLRLPPpGRAAEELRRELALLRHLAAAGVpPVPRVLA---GCTDAELLGLPFLLMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947 104 LKGSD-----TALPTAEQCFHTGAMLAKMH-LAAADFPLEMENPR--YNAWWTEA-CARLLPVLSQDD-AALLCSEIDAL 173
Cdd:pfam01636  78 LPGEVlarplLPEERGALLEALGRALARLHaVDPAALPLAGRLARllELLRQLEAaLARLLAAELLDRlEELEERLLAAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947 174 KDNLGNHLPSGIIHADLFKDNVLLD-GGQVSGFIDFYYACRGNFMYDLAIAVNDWARTADNKLDEALKKAFI-GGYEGVR 251
Cdd:pfam01636 158 LALLPAELPPVLVHGDLHPGNLLVDpGGRVSGVIDFEDAGLGDPAYDLAILLNSWGRELGAELLAAYLAAYGaFGYARLR 237

                  ..
gi 2221283947 252 PL 253
Cdd:pfam01636 238 EL 239
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
6-251 1.26e-09

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 57.82  E-value: 1.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947   6 SVSDDEMRGFLS--GYDLGEFVSLQGIAQGITNSNYFLTTtSGRYVLTV--------------FEVLKQeelpffleLNR 69
Cdd:COG3173     2 ELDEAALRALLAaqLPGLAGLPEVEPLSGGWSNLTYRLDT-GDRLVLRRpprglasahdvrreARVLRA--------LAP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947  70 HLsmkGVAVAAPVARKDgrlDSVLAGKPACLVACLKGS--DTALPTAEQ------CFHTGAMLAKMH-LAAADFPLEMEN 140
Cdd:COG3173    73 RL---GVPVPRPLALGE---DGEVIGAPFYVMEWVEGEtlEDALPDLSPaerralARALGEFLAALHaVDPAAAGLADGR 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947 141 P--------RYNAWWTEACARLLPVLSQDDAAllcseIDALKDNLGNHLPSGIIHADLFKDNVLLDG--GQVSGFIDFYY 210
Cdd:COG3173   147 PeglerqlaRWRAQLRRALARTDDLPALRERL-----AAWLAANLPEWGPPVLVHGDLRPGNLLVDPddGRLTAVIDWEL 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2221283947 211 ACRGNFMYDLAIAVNDWARTADnkLDEALkKAFIGGYEGVR 251
Cdd:COG3173   222 ATLGDPAADLAYLLLYWRLPDD--LLGPR-AAFLAAYEEAT 259
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
158-227 5.99e-09

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: 54.23  E-value: 5.99e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2221283947 158 LSQDDAALLCSEIDALKDNLGNHL-------PSGIIHADLFKDNVLLDG-GQVSGFIDFYYACRGNFMYDLAIAVNDW 227
Cdd:cd05120    79 LSEVWPRLSEEEKEKIADQLAEILaalhridSSVLTHGDLHPGNILVKPdGKLSGIIDWEFAGYGPPAFDYAAALRDW 156
PRK06148 PRK06148
hypothetical protein; Provisional
38-257 5.22e-08

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 54.26  E-value: 5.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947   38 NYFLTTTSGR-YVLTVFEVLKQE-ELPFFLELNRHLSMKGVAVAAP-------------VARKDG-----RLDSVLAGKP 97
Cdd:PRK06148    40 NFRLTTDDGAdYILKIVNPSEPRvESDFQTAALDHLAAVAPDLPVPrlipslsgaslasAQDPDGeprllRLLSWLPGTP 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947   98 ACLVAclKGSDTALPTaeqcfhTGAMLAKMHLAAADF--PLEMENPRYN---AWWteACARLLPVLSQDDAALLCSEIDA 172
Cdd:PRK06148   120 LAEAA--PRTEALLDN------LGRALGRLDRALQGFmhPGALRDLDWDlrhAGR--ARDRLHFIDDPEDRALVERFLAR 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947  173 LKDNLG---NHLPSGIIHADLFKDNVLLDGG---QVSGFIDFYYACRGNFMYDLAIAvndwarTADNKLD----EALKKA 242
Cdd:PRK06148   190 FERNVAprlAALPAQVIHNDANDYNILVDADdgeRISGLIDFGDAVHAPRICEVAIA------AAYAILDhpdpIGAAAA 263
                          250
                   ....*....|....*
gi 2221283947  243 FIGGYEGVRPLSAEE 257
Cdd:PRK06148   264 LVAGYHAVYPLQAQE 278
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
25-229 1.79e-06

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: 48.38  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947  25 VSLQGIAQGITNSNYFLTTTSG----RYVLTV----------------FEVLkqeelpfflelnRHLSMKGVAVAAPVAR 84
Cdd:cd05154     1 LAVRRLSGGASNETYLVDAGGDgggrRLVLRRpppggllpsahdlereYRVL------------RALAGTGVPVPRVLAL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947  85 KDGrlDSVLaGKPACLVACLKG------SDTALPTAEQ----CFHTGAMLAKMH-LAAADFPLEMENP----------RY 143
Cdd:cd05154    69 CED--PSVL-GAPFYVMERVDGrvlpdpLPRPDLSPEErralARSLVDALAALHsVDPAALGLADLGRpegylerqvdRW 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947 144 NAWWTEACARLLPVLsqdDAALlcseiDALKDNLGNHLPSGIIHADlFK-DNVLLDG-GQVSGFIDFYYACRGNFMYDLA 221
Cdd:cd05154   146 RRQLEAAATDPPPAL---EEAL-----RWLRANLPADGRPVLVHGD-FRlGNLLFDPdGRVTAVLDWELATLGDPLEDLA 216

                  ....*...
gi 2221283947 222 IAVNDWAR 229
Cdd:cd05154   217 WLLARWWR 224
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
158-256 1.17e-05

Thiamine kinase or a related kinase [Coenzyme transport and metabolism];


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 44.77  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947 158 LSQDDAALLCSEIDALKDNLGNH-LPSGIIHADLFKDNVLLDGGQVSGFIDFYYACRGNFMYDLAIAVndwartADNKLD 236
Cdd:COG0510    23 LGPRDLPELLRRLEELERALAARpLPLVLCHGDLHPGNFLVTDDGRLYLIDWEYAGLGDPAFDLAALL------VEYGLS 96
                          90       100
                  ....*....|....*....|
gi 2221283947 237 EALKKAFIGGYEGVRPLSAE 256
Cdd:COG0510    97 PEQAEELLEAYGFGRPTEEL 116
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
183-255 1.19e-04

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 41.87  E-value: 1.19e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2221283947 183 SGIIHADLFKDNVLLDGGQVsGFIDF---YYACRGNFM-YDLAIAVNDWARTADNKLDEaLKKAFIGGYEGVRPLSA 255
Cdd:COG3642    70 AGIVHGDLTTSNILVDDGGV-YLIDFglaRYSDPLEDKaVDLAVLKRSLESTHPDPAEE-LWEAFLEGYREVGPAEE 144
PRK14879 PRK14879
Kae1-associated kinase Bud32;
184-257 3.53e-04

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 41.05  E-value: 3.53e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2221283947 184 GIIHADLFKDNVLLDGGQVSgFIDFYYACRGNFMYDLAIAVNDWARTADN---KLDEALKKAFIGGYEGVRPLSAEE 257
Cdd:PRK14879  115 GIIHGDLTTSNMILSGGKIY-LIDFGLAEFSKDLEDRAVDLHVLLRSLESthpDWAEELFEAFLEGYREVMGEKAEE 190
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
186-252 5.14e-04

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: 40.64  E-value: 5.14e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2221283947 186 IHADLFKDNVLLDGGQVSGFIDFYYACRGNFMYDLAIAVNDwarTADNKLDEALKKAFIGGYEGVRP 252
Cdd:cd05150   166 THGDACLPNIILDPGRFSGFIDLGRLGVADRYQDLALAVRS---LRENLGGEEYAERFLDAYGIDAP 229
PRK06149 PRK06149
aminotransferase;
38-262 6.37e-04

aminotransferase;


Pssm-ID: 235716 [Multi-domain]  Cd Length: 972  Bit Score: 41.52  E-value: 6.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947  38 NYFLTTTSGRYVLTV----FEvlkQEELPFFLELNRHLSMK--GVAVAAPVARKDG---------------RLDSVLAGK 96
Cdd:PRK06149   46 NFRVDSDGGRFVLKIchaaYA---AVELEAQHAALRHLAERepALRVPVVIPALDGeelltldvrgqglrvRLLDYLPGQ 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947  97 P--------ACLVACLkgsdtalptaeqcfhtGAMLAKMHLAAADF--P-LEME---NPRYNAwwtEACARLLPVLSQDD 162
Cdd:PRK06149  123 PltrlghlaPASVAGL----------------GALCARVARALADFdhPgLDRTlqwDLRHAG---PVVAHLLSHITDPA 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947 163 --AALLCSEIDALK--DNLGNHLPSGIIHADLFKDNVLLD---GGQVS--GFIDFYYACRGNFMYDLAIavndwarTADN 233
Cdd:PRK06149  184 qrARIAEATRDAARrlQPLAPALPLQAVHLDITDDNVVGSrdaDGRWQpdGVIDFGDLVRTWRVADLAV-------TCAS 256
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2221283947 234 KLDEALKKAF-----IGGYEGVRPLSAEE-KAYFP 262
Cdd:PRK06149  257 LLHHAGGDPFsilpaVRAYHAVRPLSEAElKALWP 291
TCAD9 pfam19974
Ternary complex associated domain 9; Novel uncharacterized protein domain found associated ...
142-221 3.74e-03

Ternary complex associated domain 9; Novel uncharacterized protein domain found associated with the vWA-MoxR-VMAP ternary systems. This domain is likely a phosphotransferase enzyme.


Pssm-ID: 466244 [Multi-domain]  Cd Length: 428  Bit Score: 38.66  E-value: 3.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947 142 RYNAWWTEACARLLPVLSQDDAALLCSEIDALKDNLGNHLP---SGIIHADLFKDNVLLDGGQVsGFIDFYYACRGN-FM 217
Cdd:pfam19974 252 RGARRWELLRELLSDTILEIDGLRLPHPFAALRDALTEAREgrvTSSVHGDLNPRNILLDGDNV-YLIDYARTRPGHpLL 330

                  ....
gi 2221283947 218 YDLA 221
Cdd:pfam19974 331 SDFA 334
FN3K COG3001
Fructosamine-3-kinase [Carbohydrate transport and metabolism];
112-255 9.77e-03

Fructosamine-3-kinase [Carbohydrate transport and metabolism];


Pssm-ID: 442239 [Multi-domain]  Cd Length: 287  Bit Score: 37.10  E-value: 9.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947 112 PTAEQCFhtGAMLAKMHLAAAD-FPLEMEN-----PRYNAW---WTE--------------ACARLLPVLSQDDAALLCS 168
Cdd:COG3001    99 AGAWERL--GRQLAALHQATAPrFGWDRDNfigstPQPNTWtddWAEffaeqrlgpqlqlaAEKGLLFAADRERIERLVE 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221283947 169 EIDALkdnLGNH--LPSgIIHADLFKDNVLLDGGQVSGFID--FYYACRgnfMYDLAIAvndwartadnKLDEALKKAFI 244
Cdd:COG3001   177 RLPEL---LAPHepQPS-LLHGDLWSGNVLFTADGEPVLIDpaVYYGDR---EVDLAMT----------ELFGGFPDAFY 239
                         170
                  ....*....|.
gi 2221283947 245 GGYEGVRPLSA 255
Cdd:COG3001   240 DAYQEVWPLDP 250
 
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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