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Conserved domains on  [gi|740619435|ref|WP_038404948|]
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aminoglycoside O-phosphotransferase APH(3')-Ib [Plasmid RP4]

Protein Classification

aminoglycoside 3'-phosphotransferase( domain architecture ID 10142347)

aminoglycoside 3'-phosphotransferase phosphorylates and inactives antibiotic substrates such as kanamycin, streptomycin, neomycin, and gentamicin, among others

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
 26-271 2.17e-87

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: 260.21  E-value: 2.17e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435  26 YKWARDKVGQSGCAVYRLhsKSGGSDLFLKHGKDAFADDVTDEMVRLRWLAGHISVPSVVSFVRTPNQAWLLTTAIHGKT 105
Cdd:cd05150    1 YRWEPDTIGESGARVYRL--DGGGPVLYLKTAPAGYAYELAREAERLRWLAGKLPVPEVLDYGSDDGGDWLLTTALPGRD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435 106 AYQVLKSDfgARLVVVDALAAFMRRLHAIPVSECSVQqWTTHAGLPE-RGSIEAGVVDVDDFDKEREGWTAEQVWEAMHR 184
Cdd:cd05150   79 AASLEPLL--DPERLVDLLAEALRALHSLPIADCPFD-RRLDARLAEaRARVEAGLVDEDDFDEERQGRTAEELLAELEA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435 185 LLPLAPDPVVTHGDFSLDNLLIVEGKVVGCIDVGRAGIADRYQDLAVLWNCLEEF--EPSLQERLVAQYGIADPDRRKLQ 262
Cdd:cd05150  156 TRPAEEDLVVTHGDACLPNIILDPGRFSGFIDLGRLGVADRYQDLALAVRSLRENlgGEEYAERFLDAYGIDAPDPERLA 235


                 ....*....
gi 740619435 263 FHLLLDELF 271
Cdd:cd05150  236 YYRLLDEFF 244
 
Name Accession Description Interval E-value
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
 26-271 2.17e-87

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: 260.21  E-value: 2.17e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435  26 YKWARDKVGQSGCAVYRLhsKSGGSDLFLKHGKDAFADDVTDEMVRLRWLAGHISVPSVVSFVRTPNQAWLLTTAIHGKT 105
Cdd:cd05150    1 YRWEPDTIGESGARVYRL--DGGGPVLYLKTAPAGYAYELAREAERLRWLAGKLPVPEVLDYGSDDGGDWLLTTALPGRD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435 106 AYQVLKSDfgARLVVVDALAAFMRRLHAIPVSECSVQqWTTHAGLPE-RGSIEAGVVDVDDFDKEREGWTAEQVWEAMHR 184
Cdd:cd05150   79 AASLEPLL--DPERLVDLLAEALRALHSLPIADCPFD-RRLDARLAEaRARVEAGLVDEDDFDEERQGRTAEELLAELEA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435 185 LLPLAPDPVVTHGDFSLDNLLIVEGKVVGCIDVGRAGIADRYQDLAVLWNCLEEF--EPSLQERLVAQYGIADPDRRKLQ 262
Cdd:cd05150  156 TRPAEEDLVVTHGDACLPNIILDPGRFSGFIDLGRLGVADRYQDLALAVRSLRENlgGEEYAERFLDAYGIDAPDPERLA 235


                 ....*....
gi 740619435 263 FHLLLDELF 271
Cdd:cd05150  236 YYRLLDEFF 244
Aph COG3231
Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];
12-271 2.18e-85

Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442463 [Multi-domain]  Cd Length: 258  Bit Score: 255.61  E-value: 2.18e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435  12 AAAVPESMAAHVMGYKWARDKVGQSGCAVYRLhSKSGGSDLFLKHGKDAFADDVTDEMVRLRWLAGH-ISVPSVVSFVRT 90
Cdd:COG3231    1 GPRLPPALRELLGGYRWEPVTIGESGAKVFRL-ADGGRPTLYLKIEPAGPAAELEDEADRLRWLAGQgLPVPEVLDFGED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435  91 PNQAWLLTTAIHGKTAYQVlkSDFGARLVVVDALAAFMRRLHAIPVSECSVQqWTTHAGLPE-RGSIEAGVVDVDDFDKE 169
Cdd:COG3231   80 DGGAWLLTTAVPGRPAASV--SEALDPERAVELLAEALRRLHALPVADCPFD-RRLERRLAEaRARVAAGLVDPDDFDEE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435 170 REGWTAEQVWEAMHRLLPLAPDPVVTHGDFSLDNLLIVEGKVVGCIDVGRAGIADRYQDLAVLWNCLEE-FEPSLQERLV 248
Cdd:COG3231  157 RRGRPPEELLAELLAERPAEEDLVVTHGDACLPNILVDPGTFSGFIDLGRLGVADRYQDLALAARSLREnLGEGWVEPFL 236

                        250       260
                 ....*....|....*....|...
gi 740619435 249 AQYGIAdPDRRKLQFHLLLDELF 271
Cdd:COG3231  237 DAYGIA-PDPERLAFYRLLDEFF 258
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 40-261 2.33e-25

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: 100.27  E-value: 2.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435   40 VYRLHSKSGgsDLFLKHGKDAFADDVTDEMVR-LRWLAGH--ISVPSVVSFVRTPN---QAWLLTTAIHGKTAYQVLKSD 113
Cdd:pfam01636  13 TYLVTTGDG--RYVLRLPPPGRAAEELRRELAlLRHLAAAgvPPVPRVLAGCTDAEllgLPFLLMEYLPGEVLARPLLPE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435  114 FGARLVvvDALAAFMRRLHAIPVSECSVQQWTTHAGLPERGSIEAGVVDVDDFDKEREGWTAEQVWEAMHRLLPLAPDPV 193
Cdd:pfam01636  91 ERGALL--EALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAAELLDRLEELEERLLAALLALLPAELPPV 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435  194 VTHGDFSLDNLLI-VEGKVVGCIDVGRAGIADRYQDLAVLWNCL-EEFEPSLQERLVAQYGIADPDRRKL 261
Cdd:pfam01636 169 LVHGDLHPGNLLVdPGGRVSGVIDFEDAGLGDPAYDLAILLNSWgRELGAELLAAYLAAYGAFGYARLRE 238
 
Name Accession Description Interval E-value
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
 26-271 2.17e-87

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: 260.21  E-value: 2.17e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435  26 YKWARDKVGQSGCAVYRLhsKSGGSDLFLKHGKDAFADDVTDEMVRLRWLAGHISVPSVVSFVRTPNQAWLLTTAIHGKT 105
Cdd:cd05150    1 YRWEPDTIGESGARVYRL--DGGGPVLYLKTAPAGYAYELAREAERLRWLAGKLPVPEVLDYGSDDGGDWLLTTALPGRD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435 106 AYQVLKSDfgARLVVVDALAAFMRRLHAIPVSECSVQqWTTHAGLPE-RGSIEAGVVDVDDFDKEREGWTAEQVWEAMHR 184
Cdd:cd05150   79 AASLEPLL--DPERLVDLLAEALRALHSLPIADCPFD-RRLDARLAEaRARVEAGLVDEDDFDEERQGRTAEELLAELEA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435 185 LLPLAPDPVVTHGDFSLDNLLIVEGKVVGCIDVGRAGIADRYQDLAVLWNCLEEF--EPSLQERLVAQYGIADPDRRKLQ 262
Cdd:cd05150  156 TRPAEEDLVVTHGDACLPNIILDPGRFSGFIDLGRLGVADRYQDLALAVRSLRENlgGEEYAERFLDAYGIDAPDPERLA 235


                 ....*....
gi 740619435 263 FHLLLDELF 271
Cdd:cd05150  236 YYRLLDEFF 244
Aph COG3231
Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];
12-271 2.18e-85

Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442463 [Multi-domain]  Cd Length: 258  Bit Score: 255.61  E-value: 2.18e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435  12 AAAVPESMAAHVMGYKWARDKVGQSGCAVYRLhSKSGGSDLFLKHGKDAFADDVTDEMVRLRWLAGH-ISVPSVVSFVRT 90
Cdd:COG3231    1 GPRLPPALRELLGGYRWEPVTIGESGAKVFRL-ADGGRPTLYLKIEPAGPAAELEDEADRLRWLAGQgLPVPEVLDFGED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435  91 PNQAWLLTTAIHGKTAYQVlkSDFGARLVVVDALAAFMRRLHAIPVSECSVQqWTTHAGLPE-RGSIEAGVVDVDDFDKE 169
Cdd:COG3231   80 DGGAWLLTTAVPGRPAASV--SEALDPERAVELLAEALRRLHALPVADCPFD-RRLERRLAEaRARVAAGLVDPDDFDEE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435 170 REGWTAEQVWEAMHRLLPLAPDPVVTHGDFSLDNLLIVEGKVVGCIDVGRAGIADRYQDLAVLWNCLEE-FEPSLQERLV 248
Cdd:COG3231  157 RRGRPPEELLAELLAERPAEEDLVVTHGDACLPNILVDPGTFSGFIDLGRLGVADRYQDLALAARSLREnLGEGWVEPFL 236

                        250       260
                 ....*....|....*....|...
gi 740619435 249 AQYGIAdPDRRKLQFHLLLDELF 271
Cdd:COG3231  237 DAYGIA-PDPERLAFYRLLDEFF 258
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 40-261 2.33e-25

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: 100.27  E-value: 2.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435   40 VYRLHSKSGgsDLFLKHGKDAFADDVTDEMVR-LRWLAGH--ISVPSVVSFVRTPN---QAWLLTTAIHGKTAYQVLKSD 113
Cdd:pfam01636  13 TYLVTTGDG--RYVLRLPPPGRAAEELRRELAlLRHLAAAgvPPVPRVLAGCTDAEllgLPFLLMEYLPGEVLARPLLPE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435  114 FGARLVvvDALAAFMRRLHAIPVSECSVQQWTTHAGLPERGSIEAGVVDVDDFDKEREGWTAEQVWEAMHRLLPLAPDPV 193
Cdd:pfam01636  91 ERGALL--EALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAAELLDRLEELEERLLAALLALLPAELPPV 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435  194 VTHGDFSLDNLLI-VEGKVVGCIDVGRAGIADRYQDLAVLWNCL-EEFEPSLQERLVAQYGIADPDRRKL 261
Cdd:pfam01636 169 LVHGDLHPGNLLVdPGGRVSGVIDFEDAGLGDPAYDLAILLNSWgRELGAELLAAYLAAYGAFGYARLRE 238
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 12-271 6.89e-16

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 75.54  E-value: 6.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435  12 AAAVPESMAAHVMGYKWARD----KVGQSgCAVYRLHSksgGSDLFLK---HGKDAfADDVTDEMVRLRWLAGH--ISVP 82
Cdd:COG3173    5 EAALRALLAAQLPGLAGLPEveplSGGWS-NLTYRLDT---GDRLVLRrppRGLAS-AHDVRREARVLRALAPRlgVPVP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435  83 SVVSFVRTPN---QAWLLTTAIHGKTAYQVL-KSDFGARLVVVDALAAFMRRLHAIPVsecsvqqwtTHAGLPErGSIEA 158
Cdd:COG3173   80 RPLALGEDGEvigAPFYVMEWVEGETLEDALpDLSPAERRALARALGEFLAALHAVDP---------AAAGLAD-GRPEG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435 159 GVVDVDDFDKE-----REGWTAEQVWEAMHRLL----PLAPDPVVTHGDFSLDNLLIV--EGKVVGCIDVGRAGIADRYQ 227
Cdd:COG3173  150 LERQLARWRAQlrralARTDDLPALRERLAAWLaanlPEWGPPVLVHGDLRPGNLLVDpdDGRLTAVIDWELATLGDPAA 229

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 740619435 228 DLAVL---WNCLEEFEPSLqERLVAQYGIADPDRRKLQFHLLLDELF 271
Cdd:COG3173  230 DLAYLllyWRLPDDLLGPR-AAFLAAYEEATGDLDDLTWWALADPEL 275
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
 39-234 9.72e-15

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: 71.50  E-value: 9.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435  39 AVYRLhsksgGSDLF--LKHGKDAfADDVTDEMVRLRWLAGHISVP-SVVSFVRTPNQ----AWLLTTAIHGKTAYQVLK 111
Cdd:cd05155   13 ATFRL-----GDDLAvrLPRRAWA-AELLEKEQRWLPRLAPRLPLPvPVPLALGKPGAgypwPWSVYRWLEGETAADAPL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435 112 SDfgaRLVVVDALAAFMRRLHAIPVSECSVQQ---WTTHAGLPERGSIEAGVVDVDDFDKERegwtAEQVWEAMHRLLPL 188
Cdd:cd05155   87 AD---PAAAAEDLARFLAALHAIDPAGPPNPGrgnPLRGRDLAVRDAEEALAALAGLLDVAA----ARALWERALAAPAW 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 740619435 189 APDPVVTHGDFSLDNLLIVEGKVVGCIDVGRAGIADRYQDLAVLWN 234
Cdd:cd05155  160 AGPPVWLHGDLHPGNLLVRDGRLSAVIDFGDLGVGDPACDLAIAWT 205
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
173-270 2.56e-10

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 57.48  E-value: 2.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435 173 WTAEQVWEAMHRLLPLAPDPVVTHGDFSLDNLLIVEGKVVGCIDVGRAGIADRYQDLAVLWNCLeEFEPSLQERLVAQYG 252
Cdd:COG0510   30 ELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTDDGRLYLIDWEYAGLGDPAFDLAALLVEY-GLSPEQAEELLEAYG 108

                         90       100
                 ....*....|....*....|.
gi 740619435 253 IADPD---RRKLQFHLLLDEL 270
Cdd:COG0510  109 FGRPTeelLRRLRAYRALADL 129
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 30-238 1.12e-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: 55.77  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435  30 RDKVGQSGcAVYRLHSKSggsDLFLKHGKDAFADDVTDEMVRLRWLAGH--ISVPSVVSFVRTPNQAWLLTTAIHGKTAY 107
Cdd:cd05120    5 LIKEGGDN-KVYLLGDPR---EYVLKIGPPRLKKDLEKEAAMLQLLAGKlsLPVPKVYGFGESDGWEYLLMERIEGETLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435 108 QVLKSDFGARLVVV-DALAAFMRRLHAIPVSecsvqqwtthaglpergsieagvvdvddfdkeregwtaeqvweamhrll 186
Cdd:cd05120   81 EVWPRLSEEEKEKIaDQLAEILAALHRIDSS------------------------------------------------- 111

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 740619435 187 plapdpVVTHGDFSLDNLLIV-EGKVVGCIDVGRAGIADRYQDLAVLWNCLEE 238
Cdd:cd05120  112 ------VLTHGDLHPGNILVKpDGKLSGIIDWEFAGYGPPAFDYAAALRDWTE 158
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
 120-257 7.12e-07

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: 49.15  E-value: 7.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435 120 VVDALAafmrRLHAIPVSEcsvqqwtthAGLPERGSIEAGVVD-VDDFDKEREgWTAEQVWEAMHRLL-------PLAPD 191
Cdd:cd05154  111 LVDALA----ALHSVDPAA---------LGLADLGRPEGYLERqVDRWRRQLE-AAATDPPPALEEALrwlranlPADGR 176

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435 192 PVVTHGDFSLDNLLIVE-GKVVGCIDVGRAGIADRYQDLAvlWNCL---EEFEPSLQERLVAQYGIADPD 257
Cdd:cd05154  177 PVLVHGDFRLGNLLFDPdGRVTAVLDWELATLGDPLEDLA--WLLArwwRPGDPPGLAAPTRLPGFPSRE 244
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
 39-240 9.65e-07

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: 49.15  E-value: 9.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435  39 AVYRLHSkSGGSDLFLK-HGKDAFADDVTDEMVRL-RWLAGH-ISVPSVV------SFVRTPNQAWLLTTAIHGKTAYQV 109
Cdd:COG2334   27 RNYRVET-EDGRRYVLKlYRPGRWSPEEIPFELALlAHLAAAgLPVPAPVptrdgeTLLELEGRPAALFPFLPGRSPEEP 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435 110 LKSDFGArlvvvdaLAAFMRRLHAIpvsecsVQQWT--THAGLPERGSIEAGVVDVDDFDKEREGWtAEQVWEAMHRLLP 187
Cdd:COG2334  106 SPEQLEE-------LGRLLARLHRA------LADFPrpNARDLAWWDELLERLLGPLLPDPEDRAL-LEELLDRLEARLA 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 740619435 188 LAPDPV---VTHGDFSLDNLLIVEGKVVGCIDVGRAGIADRYQDLAVLWNCLEEFE 240
Cdd:COG2334  172 PLLGALprgVIHGDLHPDNVLFDGDGVSGLIDFDDAGYGPRLYDLAIALNGWADGP 227
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
 175-251 1.55e-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: 42.25  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435 175 AEQVWEAMHRLLPLAPDPVVTHGDFSLDNLLIVEGKVVGCIDVGRAGIADRYQDLAVLWN--CLEE---FEPSLQERLVA 249
Cdd:cd05153  162 LEDELARLQALAPSDLPRGVIHADLFRDNVLFDGDRLSGIIDFYDACYDPLLYDLAIALNdwCFDDdgkLDPERAKALLA 241


                 ..
gi 740619435 250 QY 251
Cdd:cd05153  242 GY 243
MPH2' cd05152
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ...
 121-262 8.25e-04

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: 39.92  E-value: 8.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435 121 VDALAAFMRRLHAIPVSECsvqqwtTHAGLPergsieagVVDVDDFdkeREGWTA--EQV-------------WEAMhrl 185
Cdd:cd05152  115 ARSLGKALAALHSIPADLA------AAAGLP--------VYTAEEV---RARMAArmDRVketfgvppallarWQAW--- 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740619435 186 lpLAPD------PVVTHGDFSLDNLLIVE-GKVVGCIDVGRAGIADRYQDLAVLwncLEEFEPSLQERLVAQYGIAD--- 255
Cdd:cd05152  175 --LADDslwpfhTVLVHGDLHPGHILVDEdGRVTGLIDWTEAKVGDPADDFAWH---YAAFGEEALERLLDAYEKAGgev 249


                 ....*..
gi 740619435 256 PDRRKLQ 262
Cdd:cd05152  250 WPRMLEH 256
 
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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