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Conserved domains on  [gi|504295173|ref|WP_014482275|]
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MULTISPECIES: phosphotransferase [Bifidobacterium]

Protein Classification

protein kinase family protein( domain architecture ID 229378)

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

CATH:  1.10.510.10
PubMed:  16244704
SCOP:  4003661

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
 115-259 2.59e-19

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd05152:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 276  Bit Score: 87.69  E-value: 2.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504295173 115 SFGTALGAIHRLRQNFITDAHYPVFTTGQIHAQLTAWIKRLRQAGHVPQEITSRWGGIMETEGLWSFSTRPVHGGFSDGD 194
Cdd:cd05152  117 SLGKALAALHSIPADLAAAAGLPVYTAEEVRARMAARMDRVKETFGVPPALLARWQAWLADDSLWPFHTVLVHGDLHPGH 196

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504295173 195 -LIYSGSSITAITNWQDMQINDPARDLAWVFAKLDETHRNAVITAY----GRVLGNRLDDLIMLRANLWV 259
Cdd:cd05152  197 iLVDEDGRVTGLIDWTEAKVGDPADDFAWHYAAFGEEALERLLDAYekagGEVWPRMLEHIIELAAAYPL 266
 
Name Accession Description Interval E-value
MPH2' cd05152
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ...
 115-259 2.59e-19

Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group from ATP to the 2'-hydroxyl of macrolide antibiotics such as erythromycin, clarithromycin, and azithromycin, among others. Macrolides penetrate the bacterial cell and bind to ribosomes, where it interrupts protein elongation, leading ultimately to the demise of the bacterium. Phosphorylation of macrolides leads to their inactivation. Based on substrate specificity and amino acid sequence, MPH2' is divided into types I and II, encoded by mphA and mphB genes, respectively. MPH2'I inactivates 14-membered ring macrolides while MPH2'II inactivates both 14- and 16-membered ring macrolides. Enzymatic inactivation of macrolides has been reported as a mechanism for bacterial resistance in clinical samples. MPH2' 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: 270701 [Multi-domain]  Cd Length: 276  Bit Score: 87.69  E-value: 2.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504295173 115 SFGTALGAIHRLRQNFITDAHYPVFTTGQIHAQLTAWIKRLRQAGHVPQEITSRWGGIMETEGLWSFSTRPVHGGFSDGD 194
Cdd:cd05152  117 SLGKALAALHSIPADLAAAAGLPVYTAEEVRARMAARMDRVKETFGVPPALLARWQAWLADDSLWPFHTVLVHGDLHPGH 196

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504295173 195 -LIYSGSSITAITNWQDMQINDPARDLAWVFAKLDETHRNAVITAY----GRVLGNRLDDLIMLRANLWV 259
Cdd:cd05152  197 iLVDEDGRVTGLIDWTEAKVGDPADDFAWHYAAFGEEALERLLDAYekagGEVWPRMLEHIIELAAAYPL 266
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 44-250 3.04e-06

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 48.96  E-value: 3.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504295173  44 DPRGKKRLHARGRAAAVVDRSREFagLGFGTEHVLAFHAGKEGpEDASVLITTHPDGV--ARSLELLTIDD----CSSFG 117
Cdd:COG3173   50 PPRGLASAHDVRREARVLRALAPR--LGVPVPRPLALGEDGEV-IGAPFYVMEWVEGEtlEDALPDLSPAErralARALG 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504295173 118 TALGAIHRLRqnfITDAHYPVFTTGQIHAQLTAWIKRLRQAGHVPQ---EITSRWGGIMETEGLWSFSTRPVHGGFSDGD 194
Cdd:COG3173  127 EFLAALHAVD---PAAAGLADGRPEGLERQLARWRAQLRRALARTDdlpALRERLAAWLAANLPEWGPPVLVHGDLRPGN 203

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504295173 195 LIYSGSS--ITAITNWQDMQINDPARDLAWVFAKLDETH-----RNAVITAYGRVLGnRLDDL 250
Cdd:COG3173  204 LLVDPDDgrLTAVIDWELATLGDPAADLAYLLLYWRLPDdllgpRAAFLAAYEEATG-DLDDL 265
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 34-246 3.85e-06

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: 48.27  E-value: 3.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504295173   34 GRLFNVYAAYDPRGKK--RLHARGRAAAVVDR----SREFAGLGFGteHVLAFHAGKEGPEDASVLITTHPDGVARSLEL 107
Cdd:pfam01636   8 GASNRTYLVTTGDGRYvlRLPPPGRAAEELRRelalLRHLAAAGVP--PVPRVLAGCTDAELLGLPFLLMEYLPGEVLAR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504295173  108 LTIDDCS-----SFGTALGAIHRLRQNFITDAHYPVFTTGQIhAQLTAWIKRLRQAGH--VPQEITSRWGGIMETEGLWS 180
Cdd:pfam01636  86 PLLPEERgalleALGRALARLHAVDPAALPLAGRLARLLELL-RQLEAALARLLAAELldRLEELEERLLAALLALLPAE 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504295173  181 FSTRPVHGGFSDGDLIYS-GSSITAITNWQDMQINDPARDLAWVFAKLDETHRNAVITAYGRVLGNR 246
Cdd:pfam01636 165 LPPVLVHGDLHPGNLLVDpGGRVSGVIDFEDAGLGDPAYDLAILLNSWGRELGAELLAAYLAAYGAF 231
 
Name Accession Description Interval E-value
MPH2' cd05152
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ...
 115-259 2.59e-19

Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group from ATP to the 2'-hydroxyl of macrolide antibiotics such as erythromycin, clarithromycin, and azithromycin, among others. Macrolides penetrate the bacterial cell and bind to ribosomes, where it interrupts protein elongation, leading ultimately to the demise of the bacterium. Phosphorylation of macrolides leads to their inactivation. Based on substrate specificity and amino acid sequence, MPH2' is divided into types I and II, encoded by mphA and mphB genes, respectively. MPH2'I inactivates 14-membered ring macrolides while MPH2'II inactivates both 14- and 16-membered ring macrolides. Enzymatic inactivation of macrolides has been reported as a mechanism for bacterial resistance in clinical samples. MPH2' 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: 270701 [Multi-domain]  Cd Length: 276  Bit Score: 87.69  E-value: 2.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504295173 115 SFGTALGAIHRLRQNFITDAHYPVFTTGQIHAQLTAWIKRLRQAGHVPQEITSRWGGIMETEGLWSFSTRPVHGGFSDGD 194
Cdd:cd05152  117 SLGKALAALHSIPADLAAAAGLPVYTAEEVRARMAARMDRVKETFGVPPALLARWQAWLADDSLWPFHTVLVHGDLHPGH 196

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504295173 195 -LIYSGSSITAITNWQDMQINDPARDLAWVFAKLDETHRNAVITAY----GRVLGNRLDDLIMLRANLWV 259
Cdd:cd05152  197 iLVDEDGRVTGLIDWTEAKVGDPADDFAWHYAAFGEEALERLLDAYekagGEVWPRMLEHIIELAAAYPL 266
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 44-250 3.04e-06

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 48.96  E-value: 3.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504295173  44 DPRGKKRLHARGRAAAVVDRSREFagLGFGTEHVLAFHAGKEGpEDASVLITTHPDGV--ARSLELLTIDD----CSSFG 117
Cdd:COG3173   50 PPRGLASAHDVRREARVLRALAPR--LGVPVPRPLALGEDGEV-IGAPFYVMEWVEGEtlEDALPDLSPAErralARALG 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504295173 118 TALGAIHRLRqnfITDAHYPVFTTGQIHAQLTAWIKRLRQAGHVPQ---EITSRWGGIMETEGLWSFSTRPVHGGFSDGD 194
Cdd:COG3173  127 EFLAALHAVD---PAAAGLADGRPEGLERQLARWRAQLRRALARTDdlpALRERLAAWLAANLPEWGPPVLVHGDLRPGN 203

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504295173 195 LIYSGSS--ITAITNWQDMQINDPARDLAWVFAKLDETH-----RNAVITAYGRVLGnRLDDL 250
Cdd:COG3173  204 LLVDPDDgrLTAVIDWELATLGDPAADLAYLLLYWRLPDdllgpRAAFLAAYEEATG-DLDDL 265
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 34-246 3.85e-06

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: 48.27  E-value: 3.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504295173   34 GRLFNVYAAYDPRGKK--RLHARGRAAAVVDR----SREFAGLGFGteHVLAFHAGKEGPEDASVLITTHPDGVARSLEL 107
Cdd:pfam01636   8 GASNRTYLVTTGDGRYvlRLPPPGRAAEELRRelalLRHLAAAGVP--PVPRVLAGCTDAELLGLPFLLMEYLPGEVLAR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504295173  108 LTIDDCS-----SFGTALGAIHRLRQNFITDAHYPVFTTGQIhAQLTAWIKRLRQAGH--VPQEITSRWGGIMETEGLWS 180
Cdd:pfam01636  86 PLLPEERgalleALGRALARLHAVDPAALPLAGRLARLLELL-RQLEAALARLLAAELldRLEELEERLLAALLALLPAE 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504295173  181 FSTRPVHGGFSDGDLIYS-GSSITAITNWQDMQINDPARDLAWVFAKLDETHRNAVITAYGRVLGNR 246
Cdd:pfam01636 165 LPPVLVHGDLHPGNLLVDpGGRVSGVIDFEDAGLGDPAYDLAILLNSWGRELGAELLAAYLAAYGAF 231
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
 103-255 6.01e-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: 38.75  E-value: 6.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504295173 103 RSLELLTIDDCSSFGTALGAIHRLRQNFITDAHYPVFTTGQIHAQ-LTAWIKRLRQAGHVPQEIT---SRWGgimetEGL 178
Cdd:COG2334  100 RSPEEPSPEQLEELGRLLARLHRALADFPRPNARDLAWWDELLERlLGPLLPDPEDRALLEELLDrleARLA-----PLL 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504295173 179 WSFSTRPVHGGFSDGDLIYSGSSITAITNWQDMQINDPARDLA-----WVFAKLDETHRNAVITAYGRVlgNRLDD---- 249
Cdd:COG2334  175 GALPRGVIHGDLHPDNVLFDGDGVSGLIDFDDAGYGPRLYDLAialngWADGPLDPARLAALLEGYRAV--RPLTEaela 252

                        170
                 ....*....|
gi 504295173 250 ----LIMLRA 255
Cdd:COG2334  253 alppLLRLRA 262
 
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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