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Conserved domains on  [gi|16077321|ref|NP_388134|]
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putative phosphotransferase [Bacillus subtilis subsp. subtilis str. 168]

Protein Classification

macrolide 2'-phosphotransferase( domain architecture ID 10142354)

macrolide 2'-phosphotransferase is an aminoglycoside phosphotransferase family protein that 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPH2' cd05152
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ...
 14-289 1.14e-147

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: 415.49  E-value: 1.14e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321  14 VGLARSQGLTVHSENAQLNETGMDFQVVFAKDDTGMPWVLRKPRRSDVVERASAEGITLAFLRANLTADVPDWRIHTPEL 93
Cdd:cd05152   1 LALAAKHGLDLKPATLRLNESGLDFQVAFARDTEGRRWVLRIPRRPDVSERLEAEKKVLDLVTPHLPFAVPDWRIHTPEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321  94 IAYPMLKGTPAAGIDLEQKQYVWNMDHQPPSDDFVRTLADILAELHGTDQISAGQSGIEVIRPEDFRQMTADSMVDVKNK 173
Cdd:cd05152  81 IAYPLLPGVPAATIDPEIQNYVWNWDPLAPPPVFARSLGKALAALHSIPADLAAAAGLPVYTAEEVRARMAARMDRVKET 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321 174 LGVSTTLWERWQKWVDDDAYWPGFSSLIHGDLHPPHILIDQNGRVTGLLDWTEAKVADPAKDFVLYQTIFGEKETARLLE 253
Cdd:cd05152 161 FGVPPALLARWQAWLADDSLWPFHTVLVHGDLHPGHILVDEDGRVTGLIDWTEAKVGDPADDFAWHYAAFGEEALERLLD 240

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 16077321 254 YYDQAGGRIWAKMQEHISEMQAAYPVEIAKLALQTQ 289
Cdd:cd05152 241 AYEKAGGEVWPRMLEHIIELAAAYPLTIALFALDSG 276
 
Name Accession Description Interval E-value
MPH2' cd05152
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ...
 14-289 1.14e-147

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: 415.49  E-value: 1.14e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321  14 VGLARSQGLTVHSENAQLNETGMDFQVVFAKDDTGMPWVLRKPRRSDVVERASAEGITLAFLRANLTADVPDWRIHTPEL 93
Cdd:cd05152   1 LALAAKHGLDLKPATLRLNESGLDFQVAFARDTEGRRWVLRIPRRPDVSERLEAEKKVLDLVTPHLPFAVPDWRIHTPEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321  94 IAYPMLKGTPAAGIDLEQKQYVWNMDHQPPSDDFVRTLADILAELHGTDQISAGQSGIEVIRPEDFRQMTADSMVDVKNK 173
Cdd:cd05152  81 IAYPLLPGVPAATIDPEIQNYVWNWDPLAPPPVFARSLGKALAALHSIPADLAAAAGLPVYTAEEVRARMAARMDRVKET 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321 174 LGVSTTLWERWQKWVDDDAYWPGFSSLIHGDLHPPHILIDQNGRVTGLLDWTEAKVADPAKDFVLYQTIFGEKETARLLE 253
Cdd:cd05152 161 FGVPPALLARWQAWLADDSLWPFHTVLVHGDLHPGHILVDEDGRVTGLIDWTEAKVGDPADDFAWHYAAFGEEALERLLD 240

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 16077321 254 YYDQAGGRIWAKMQEHISEMQAAYPVEIAKLALQTQ 289
Cdd:cd05152 241 AYEKAGGEVWPRMLEHIIELAAAYPLTIALFALDSG 276
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 35-269 1.54e-35

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: 128.39  E-value: 1.54e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321    35 GMDFQVVFAKDDTGmPWVLRKPRRSDVVERASAEGITLAFLRANLtaDVPDWRIHTPELIAYpmLKGTPAAGIDLEQKQY 114
Cdd:pfam01636   8 GASNRTYLVTTGDG-RYVLRLPPPGRAAEELRRELALLRHLAAAG--VPPVPRVLAGCTDAE--LLGLPFLLMEYLPGEV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321   115 VWNMDHQPPSDDFVRTLADILAELHGTDQISAGQSGIEVIRPEDFRQMTADSMVDVKNKLGVS-TTLWERWQKWVDDDAY 193
Cdd:pfam01636  83 LARPLLPEERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAAELLDRlEELEERLLAALLALLP 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16077321   194 WPGFSSLIHGDLHPPHILIDQNGRVTGLLDWTEAKVADPAKDFVLYQTIFGEKETARLLEYYDQAGGRI-WAKMQEH 269
Cdd:pfam01636 163 AELPPVLVHGDLHPGNLLVDPGGRVSGVIDFEDAGLGDPAYDLAILLNSWGRELGAELLAAYLAAYGAFgYARLREL 239
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 16-262 5.80e-23

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 95.95  E-value: 5.80e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321  16 LARSQGLTVHSENAQLNETGMDFQVVFAkdDTGMPWVLR-KPRRSDVVERASAEGITLAFLRANLtaDVPdwrihTPELI 94
Cdd:COG3173  12 LAAQLPGLAGLPEVEPLSGGWSNLTYRL--DTGDRLVLRrPPRGLASAHDVRREARVLRALAPRL--GVP-----VPRPL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321  95 AYpmlkGTPAAGIDLEQKQYVW----NMDHQPPSDD------FVRTLADILAELHGTDQISAGQSGIeviRPEDF-RQMT 163
Cdd:COG3173  83 AL----GEDGEVIGAPFYVMEWvegeTLEDALPDLSpaerraLARALGEFLAALHAVDPAAAGLADG---RPEGLeRQLA 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321 164 --ADSMVDVKNKLGVSTTLWERWQKWVDDDAYWPGFSSLIHGDLHPPHILID-QNGRVTGLLDWTEAKVADPAKDFV--- 237
Cdd:COG3173 156 rwRAQLRRALARTDDLPALRERLAAWLAANLPEWGPPVLVHGDLRPGNLLVDpDDGRLTAVIDWELATLGDPAADLAyll 235

                       250       260
                ....*....|....*....|....*..
gi 16077321 238 LYQTIFGE--KETARLLEYYDQAGGRI 262
Cdd:COG3173 236 LYWRLPDDllGPRAAFLAAYEEATGDL 262
 
Name Accession Description Interval E-value
MPH2' cd05152
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ...
 14-289 1.14e-147

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: 415.49  E-value: 1.14e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321  14 VGLARSQGLTVHSENAQLNETGMDFQVVFAKDDTGMPWVLRKPRRSDVVERASAEGITLAFLRANLTADVPDWRIHTPEL 93
Cdd:cd05152   1 LALAAKHGLDLKPATLRLNESGLDFQVAFARDTEGRRWVLRIPRRPDVSERLEAEKKVLDLVTPHLPFAVPDWRIHTPEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321  94 IAYPMLKGTPAAGIDLEQKQYVWNMDHQPPSDDFVRTLADILAELHGTDQISAGQSGIEVIRPEDFRQMTADSMVDVKNK 173
Cdd:cd05152  81 IAYPLLPGVPAATIDPEIQNYVWNWDPLAPPPVFARSLGKALAALHSIPADLAAAAGLPVYTAEEVRARMAARMDRVKET 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321 174 LGVSTTLWERWQKWVDDDAYWPGFSSLIHGDLHPPHILIDQNGRVTGLLDWTEAKVADPAKDFVLYQTIFGEKETARLLE 253
Cdd:cd05152 161 FGVPPALLARWQAWLADDSLWPFHTVLVHGDLHPGHILVDEDGRVTGLIDWTEAKVGDPADDFAWHYAAFGEEALERLLD 240

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 16077321 254 YYDQAGGRIWAKMQEHISEMQAAYPVEIAKLALQTQ 289
Cdd:cd05152 241 AYEKAGGEVWPRMLEHIIELAAAYPLTIALFALDSG 276
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 35-269 1.54e-35

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: 128.39  E-value: 1.54e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321    35 GMDFQVVFAKDDTGmPWVLRKPRRSDVVERASAEGITLAFLRANLtaDVPDWRIHTPELIAYpmLKGTPAAGIDLEQKQY 114
Cdd:pfam01636   8 GASNRTYLVTTGDG-RYVLRLPPPGRAAEELRRELALLRHLAAAG--VPPVPRVLAGCTDAE--LLGLPFLLMEYLPGEV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321   115 VWNMDHQPPSDDFVRTLADILAELHGTDQISAGQSGIEVIRPEDFRQMTADSMVDVKNKLGVS-TTLWERWQKWVDDDAY 193
Cdd:pfam01636  83 LARPLLPEERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAAELLDRlEELEERLLAALLALLP 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16077321   194 WPGFSSLIHGDLHPPHILIDQNGRVTGLLDWTEAKVADPAKDFVLYQTIFGEKETARLLEYYDQAGGRI-WAKMQEH 269
Cdd:pfam01636 163 AELPPVLVHGDLHPGNLLVDPGGRVSGVIDFEDAGLGDPAYDLAILLNSWGRELGAELLAAYLAAYGAFgYARLREL 239
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 16-262 5.80e-23

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 95.95  E-value: 5.80e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321  16 LARSQGLTVHSENAQLNETGMDFQVVFAkdDTGMPWVLR-KPRRSDVVERASAEGITLAFLRANLtaDVPdwrihTPELI 94
Cdd:COG3173  12 LAAQLPGLAGLPEVEPLSGGWSNLTYRL--DTGDRLVLRrPPRGLASAHDVRREARVLRALAPRL--GVP-----VPRPL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321  95 AYpmlkGTPAAGIDLEQKQYVW----NMDHQPPSDD------FVRTLADILAELHGTDQISAGQSGIeviRPEDF-RQMT 163
Cdd:COG3173  83 AL----GEDGEVIGAPFYVMEWvegeTLEDALPDLSpaerraLARALGEFLAALHAVDPAAAGLADG---RPEGLeRQLA 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321 164 --ADSMVDVKNKLGVSTTLWERWQKWVDDDAYWPGFSSLIHGDLHPPHILID-QNGRVTGLLDWTEAKVADPAKDFV--- 237
Cdd:COG3173 156 rwRAQLRRALARTDDLPALRERLAAWLAANLPEWGPPVLVHGDLRPGNLLVDpDDGRLTAVIDWELATLGDPAADLAyll 235

                       250       260
                ....*....|....*....|....*..
gi 16077321 238 LYQTIFGE--KETARLLEYYDQAGGRI 262
Cdd:COG3173 236 LYWRLPDDllGPRAAFLAAYEEATGDL 262
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 47-245 2.42e-10

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: 58.08  E-value: 2.42e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321  47 TGMPWVLRKPRRSdVVERASAEGITLAFLRANLTADVP----DWRIHTPELIAYPMLKGTPAAGIDLEqkqyvwnMDHQP 122
Cdd:cd05120  19 DPREYVLKIGPPR-LKKDLEKEAAMLQLLAGKLSLPVPkvygFGESDGWEYLLMERIEGETLSEVWPR-------LSEEE 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321 123 PsDDFVRTLADILAELHGTDqisagqsgievirpedfrqmtadsmvdvknklgvsttlwerwqkwvdddaywpgFSSLIH 202
Cdd:cd05120  91 K-EKIADQLAEILAALHRID------------------------------------------------------SSVLTH 115

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 16077321 203 GDLHPPHILIDQNGRVTGLLDWTEAKVADPAKDFVLYQTIFGE 245
Cdd:cd05120 116 GDLHPGNILVKPDGKLSGIIDWEFAGYGPPAFDYAAALRDWTE 158
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
 48-264 4.15e-10

Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and Choline kinase; This subfamily is composed of uncharacterized bacterial proteins with similarity to APH and ChoK. Other APH/ChoK-like proteins include ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). These proteins catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates, such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides, and macrolides leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270704 [Multi-domain]  Cd Length: 234  Bit Score: 58.79  E-value: 4.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321  48 GMPWVLRKPRRSDVVERASAEGITLAFLRANLtadvpdwRIHTPELIA-------YPM-------LKGTPAAGIDLEQkq 113
Cdd:cd05155  18 GDDLAVRLPRRAWAAELLEKEQRWLPRLAPRL-------PLPVPVPLAlgkpgagYPWpwsvyrwLEGETAADAPLAD-- 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321 114 yvwnmdhqppSDDFVRTLADILAELHGTDQISAGQSGIEV---IRPEDFR-----QMTADSMVDVknklGVSTTLWERWQ 185
Cdd:cd05155  89 ----------PAAAAEDLARFLAALHAIDPAGPPNPGRGNplrGRDLAVRdaeeaLAALAGLLDV----AAARALWERAL 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321 186 --KWVDDDAYWpgfsslIHGDLHPPHILIDqNGRVTGLLDWTEAKVADPAKDFVLYQTIFGEKETARLLEYY--DQAG-- 259
Cdd:cd05155 155 aaPAWAGPPVW------LHGDLHPGNLLVR-DGRLSAVIDFGDLGVGDPACDLAIAWTLFDAAARAAFRAALgvDDATwa 227


                ....*.
gi 16077321 260 -GRIWA 264
Cdd:cd05155 228 rARGWA 233
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
180-277 2.51e-08

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 52.48  E-value: 2.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321 180 LWERWQKWVDDDaywPGFSSLIHGDLHPPHILIDQNGRVTgLLDWTEAKVADPAKDF--VLYQTIFGEKETARLLEYYdq 257
Cdd:COG0510  34 RLEELERALAAR---PLPLVLCHGDLHPGNFLVTDDGRLY-LIDWEYAGLGDPAFDLaaLLVEYGLSPEQAEELLEAY-- 107

                        90       100
                ....*....|....*....|
gi 16077321 258 AGGRIWAKMQEHISEMQAAY 277
Cdd:COG0510 108 GFGRPTEELLRRLRAYRALA 127
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
 30-235 3.10e-08

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: 53.39  E-value: 3.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321  30 QLNETgmdFQVVFAKDDTGMPWVLRKPRRSDVVERASA---EGITLAFLRAnltADVPdwrihTPELIAY---PMLKGTP 103
Cdd:cd05154  10 ASNET---YLVDAGGDGGGRRLVLRRPPPGGLLPSAHDlerEYRVLRALAG---TGVP-----VPRVLALcedPSVLGAP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321 104 AagidleqkqYVwnMDHQP---PSDDFV-------------RTLADILAELHGTDQISAGQSGIEviRPEDF-------- 159
Cdd:cd05154  79 F---------YV--MERVDgrvLPDPLPrpdlspeerralaRSLVDALAALHSVDPAALGLADLG--RPEGYlerqvdrw 145

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16077321 160 -RQMTADSMVDVknklgvstTLWERWQKWVDDDAYWPGFSSLIHGDLHPPHILIDQNGRVTGLLDWTEAKVADPAKD 235
Cdd:cd05154 146 rRQLEAAATDPP--------PALEEALRWLRANLPADGRPVLVHGDFRLGNLLFDPDGRVTAVLDWELATLGDPLED 214
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
 200-255 5.27e-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: 5.27e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16077321 200 LIHGDLHPPHILIDqNGRVTGLLDWTEAKVADPAKD-FVLYQTI----FGEKETARLLEYY 255
Cdd:cd05150 165 VTHGDACLPNIILD-PGRFSGFIDLGRLGVADRYQDlALAVRSLrenlGGEEYAERFLDAY 224
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
 122-257 6.30e-04

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: 40.70  E-value: 6.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321 122 PPSDDFVRTLADILAELHgtdqiSAGQsGIEVIRPED---------FRQMTADSMVDVKNKLGVSTTLWERWQKWVDDDA 192
Cdd:cd05153 104 TPTPEQCRAIGAALARLH-----LALA-GFPPPRPNPrglawwkplAERLKARLDLLAADDRALLEDELARLQALAPSDL 177

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16077321 193 ywPgfSSLIHGDLHPPHILIDqNGRVTGLLDWTEAKVADPAKD--------FVLYQTIFGEKETARLLEYYDQ 257
Cdd:cd05153 178 --P--RGVIHADLFRDNVLFD-GDRLSGIIDFYDACYDPLLYDlaialndwCFDDDGKLDPERAKALLAGYQS 245
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
 12-224 6.94e-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: 37.60  E-value: 6.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321  12 EIVGLARSQGLTVHSENAQLNEtGMDfQVVFAKDDTGMPWVLRKPRRsdvvERASAEGIT--LAFLRANLTADVPdwrih 89
Cdd:COG2334   2 ELAAALERYGLGPLSSLKPLNS-GEN-RNYRVETEDGRRYVLKLYRP----GRWSPEEIPfeLALLAHLAAAGLP----- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077321  90 TPELIA------YPMLKGTPAA------GIDLEQkqyvwnmdhqpPSDDFVRTLADILAELHgtdqiSAGQSgievIRPE 157
Cdd:COG2334  71 VPAPVPtrdgetLLELEGRPAAlfpflpGRSPEE-----------PSPEQLEELGRLLARLH-----RALAD----FPRP 130

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16077321 158 DFRqmTADSMVDVKNKLGVSTTLWERWQKWVDD-----DAYWPGFSS-----LIHGDLHPPHILIDqNGRVTGLLDW 224
Cdd:COG2334 131 NAR--DLAWWDELLERLLGPLLPDPEDRALLEElldrlEARLAPLLGalprgVIHGDLHPDNVLFD-GDGVSGLIDF 204
 
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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