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Conserved domains on  [gi|1376347981|ref|WP_107381798|]
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MULTISPECIES: APH(3')-I family aminoglycoside O-phosphotransferase [Terrabacteria group]

Protein Classification

aminoglycoside 3'-phosphotransferase( domain architecture ID 10790026)

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 COG3231
Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];
12-271 8.35e-119

Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];


:

Pssm-ID: 442463 [Multi-domain]  Cd Length: 258  Bit Score: 340.35  E-value: 8.35e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981  12 RPRLNSNMDADLYGYKWARDNVGQSGATIYRLYGkPHAPELFLKHGKGSVANDVTDEMVRLNWLTEF-MPLPTIKHFIRT 90
Cdd:COG3231     1 GPRLPPALRELLGGYRWEPVTIGESGAKVFRLAD-GGRPTLYLKIEPAGPAAELEDEADRLRWLAGQgLPVPEVLDFGED 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981  91 PDDAWLLTTAIPGKTAFQVleEYPDSGENIVDALAVFLRRLHSIPVCNCPFNSDRVFRLAQAQSRMNNGLVDASDFDDER 170
Cdd:COG3231    80 DGGAWLLTTAVPGRPAASV--SEALDPERAVELLAEALRRLHALPVADCPFDRRLERRLAEARARVAAGLVDPDDFDEER 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981 171 NGWPVEQVWKEMHNLLPFSPDSVVTHGDFSLDNLIFDEGKLIGCIDVGRVGIADRYQDLAILWNCLGE-FSPSLQKRLFQ 249
Cdd:COG3231   158 RGRPPEELLAELLAERPAEEDLVVTHGDACLPNILVDPGTFSGFIDLGRLGVADRYQDLALAARSLREnLGEGWVEPFLD 237

                         250       260
                  ....*....|....*....|..
gi 1376347981 250 KYGIDnPDMNKLQFHLMLDEFF 271
Cdd:COG3231   238 AYGIA-PDPERLAFYRLLDEFF 258
 
Name Accession Description Interval E-value
Aph COG3231
Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];
12-271 8.35e-119

Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442463 [Multi-domain]  Cd Length: 258  Bit Score: 340.35  E-value: 8.35e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981  12 RPRLNSNMDADLYGYKWARDNVGQSGATIYRLYGkPHAPELFLKHGKGSVANDVTDEMVRLNWLTEF-MPLPTIKHFIRT 90
Cdd:COG3231     1 GPRLPPALRELLGGYRWEPVTIGESGAKVFRLAD-GGRPTLYLKIEPAGPAAELEDEADRLRWLAGQgLPVPEVLDFGED 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981  91 PDDAWLLTTAIPGKTAFQVleEYPDSGENIVDALAVFLRRLHSIPVCNCPFNSDRVFRLAQAQSRMNNGLVDASDFDDER 170
Cdd:COG3231    80 DGGAWLLTTAVPGRPAASV--SEALDPERAVELLAEALRRLHALPVADCPFDRRLERRLAEARARVAAGLVDPDDFDEER 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981 171 NGWPVEQVWKEMHNLLPFSPDSVVTHGDFSLDNLIFDEGKLIGCIDVGRVGIADRYQDLAILWNCLGE-FSPSLQKRLFQ 249
Cdd:COG3231   158 RGRPPEELLAELLAERPAEEDLVVTHGDACLPNILVDPGTFSGFIDLGRLGVADRYQDLALAARSLREnLGEGWVEPFLD 237

                         250       260
                  ....*....|....*....|..
gi 1376347981 250 KYGIDnPDMNKLQFHLMLDEFF 271
Cdd:COG3231   238 AYGIA-PDPERLAFYRLLDEFF 258
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
 26-271 2.91e-106

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: 307.97  E-value: 2.91e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981  26 YKWARDNVGQSGATIYRLYGKPhaPELFLKHGKGSVANDVTDEMVRLNWLTEFMPLPTIKHFIRTPDDAWLLTTAIPGKT 105
Cdd:cd05150     1 YRWEPDTIGESGARVYRLDGGG--PVLYLKTAPAGYAYELAREAERLRWLAGKLPVPEVLDYGSDDGGDWLLTTALPGRD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981 106 AFQvlEEYPDSGENIVDALAVFLRRLHSIPVCNCPFNSDRVFRLAQAQSRMNNGLVDASDFDDERNGWPVEQVWKEMHNL 185
Cdd:cd05150    79 AAS--LEPLLDPERLVDLLAEALRALHSLPIADCPFDRRLDARLAEARARVEAGLVDEDDFDEERQGRTAEELLAELEAT 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981 186 LPFSPDSVVTHGDFSLDNLIFDEGKLIGCIDVGRVGIADRYQDLAILWNCLGEF--SPSLQKRLFQKYGIDNPDMNKLQF 263
Cdd:cd05150   157 RPAEEDLVVTHGDACLPNIILDPGRFSGFIDLGRLGVADRYQDLALAVRSLRENlgGEEYAERFLDAYGIDAPDPERLAY 236


                  ....*...
gi 1376347981 264 HLMLDEFF 271
Cdd:cd05150   237 YRLLDEFF 244
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 27-257 1.22e-24

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: 98.34  E-value: 1.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981  27 KWARDNVGQSGATIYRLYGKPhapELFLK-HGKGSVANDVTDEMVRLNWLTE--FMPLPTIKHFIRTPDD---AWLLTTA 100
Cdd:pfam01636   1 TLRPISSGASNRTYLVTTGDG---RYVLRlPPPGRAAEELRRELALLRHLAAagVPPVPRVLAGCTDAELlglPFLLMEY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981 101 IPGKTAFQVLEeyPDSGENIVDALAVFLRRLHSIPVCNCPFNSDRVFRLAQAQSRMN--NGLVDASDFDdeRNGWPVEQV 178
Cdd:pfam01636  78 LPGEVLARPLL--PEERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAalARLLAAELLD--RLEELEERL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981 179 WKEMHNLLPFSPDSVVTHGDFSLDNLIFDE-GKLIGCIDVGRVGIADRYQDLAILWNCLG-EFSPSLQKRLFQKYGIDNP 256
Cdd:pfam01636 154 LAALLALLPAELPPVLVHGDLHPGNLLVDPgGRVSGVIDFEDAGLGDPAYDLAILLNSWGrELGAELLAAYLAAYGAFGY 233


                  .
gi 1376347981 257 D 257
Cdd:pfam01636 234 A 234
 
Name Accession Description Interval E-value
Aph COG3231
Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];
12-271 8.35e-119

Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442463 [Multi-domain]  Cd Length: 258  Bit Score: 340.35  E-value: 8.35e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981  12 RPRLNSNMDADLYGYKWARDNVGQSGATIYRLYGkPHAPELFLKHGKGSVANDVTDEMVRLNWLTEF-MPLPTIKHFIRT 90
Cdd:COG3231     1 GPRLPPALRELLGGYRWEPVTIGESGAKVFRLAD-GGRPTLYLKIEPAGPAAELEDEADRLRWLAGQgLPVPEVLDFGED 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981  91 PDDAWLLTTAIPGKTAFQVleEYPDSGENIVDALAVFLRRLHSIPVCNCPFNSDRVFRLAQAQSRMNNGLVDASDFDDER 170
Cdd:COG3231    80 DGGAWLLTTAVPGRPAASV--SEALDPERAVELLAEALRRLHALPVADCPFDRRLERRLAEARARVAAGLVDPDDFDEER 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981 171 NGWPVEQVWKEMHNLLPFSPDSVVTHGDFSLDNLIFDEGKLIGCIDVGRVGIADRYQDLAILWNCLGE-FSPSLQKRLFQ 249
Cdd:COG3231   158 RGRPPEELLAELLAERPAEEDLVVTHGDACLPNILVDPGTFSGFIDLGRLGVADRYQDLALAARSLREnLGEGWVEPFLD 237

                         250       260
                  ....*....|....*....|..
gi 1376347981 250 KYGIDnPDMNKLQFHLMLDEFF 271
Cdd:COG3231   238 AYGIA-PDPERLAFYRLLDEFF 258
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
 26-271 2.91e-106

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: 307.97  E-value: 2.91e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981  26 YKWARDNVGQSGATIYRLYGKPhaPELFLKHGKGSVANDVTDEMVRLNWLTEFMPLPTIKHFIRTPDDAWLLTTAIPGKT 105
Cdd:cd05150     1 YRWEPDTIGESGARVYRLDGGG--PVLYLKTAPAGYAYELAREAERLRWLAGKLPVPEVLDYGSDDGGDWLLTTALPGRD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981 106 AFQvlEEYPDSGENIVDALAVFLRRLHSIPVCNCPFNSDRVFRLAQAQSRMNNGLVDASDFDDERNGWPVEQVWKEMHNL 185
Cdd:cd05150    79 AAS--LEPLLDPERLVDLLAEALRALHSLPIADCPFDRRLDARLAEARARVEAGLVDEDDFDEERQGRTAEELLAELEAT 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981 186 LPFSPDSVVTHGDFSLDNLIFDEGKLIGCIDVGRVGIADRYQDLAILWNCLGEF--SPSLQKRLFQKYGIDNPDMNKLQF 263
Cdd:cd05150   157 RPAEEDLVVTHGDACLPNIILDPGRFSGFIDLGRLGVADRYQDLALAVRSLRENlgGEEYAERFLDAYGIDAPDPERLAY 236


                  ....*...
gi 1376347981 264 HLMLDEFF 271
Cdd:cd05150   237 YRLLDEFF 244
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 27-257 1.22e-24

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: 98.34  E-value: 1.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981  27 KWARDNVGQSGATIYRLYGKPhapELFLK-HGKGSVANDVTDEMVRLNWLTE--FMPLPTIKHFIRTPDD---AWLLTTA 100
Cdd:pfam01636   1 TLRPISSGASNRTYLVTTGDG---RYVLRlPPPGRAAEELRRELALLRHLAAagVPPVPRVLAGCTDAELlglPFLLMEY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981 101 IPGKTAFQVLEeyPDSGENIVDALAVFLRRLHSIPVCNCPFNSDRVFRLAQAQSRMN--NGLVDASDFDdeRNGWPVEQV 178
Cdd:pfam01636  78 LPGEVLARPLL--PEERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAalARLLAAELLD--RLEELEERL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981 179 WKEMHNLLPFSPDSVVTHGDFSLDNLIFDE-GKLIGCIDVGRVGIADRYQDLAILWNCLG-EFSPSLQKRLFQKYGIDNP 256
Cdd:pfam01636 154 LAALLALLPAELPPVLVHGDLHPGNLLVDPgGRVSGVIDFEDAGLGDPAYDLAILLNSWGrELGAELLAAYLAAYGAFGY 233


                  .
gi 1376347981 257 D 257
Cdd:pfam01636 234 A 234
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 80-271 2.71e-15

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 74.00  E-value: 2.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981  80 PLPTIKHFIRTPDD---AWLLTTAIPGKTAFQVL-EEYPDSGENIVDALAVFLRRLHSIPVCNCPFNSDRVFRLAQAQSR 155
Cdd:COG3173    77 PVPRPLALGEDGEVigaPFYVMEWVEGETLEDALpDLSPAERRALARALGEFLAALHAVDPAAAGLADGRPEGLERQLAR 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981 156 MNNGLVDASDFDDERNGWpVEQVWKEMHNLLPFSPDSVVTHGDFSLDNLIFD--EGKLIGCIDVGRVGIADRYQDLAIL- 232
Cdd:COG3173   157 WRAQLRRALARTDDLPAL-RERLAAWLAANLPEWGPPVLVHGDLRPGNLLVDpdDGRLTAVIDWELATLGDPAADLAYLl 235

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1376347981 233 --WNCLGEFSPSLQkRLFQKYGIDNPDMNKLQFHLMLDEFF 271
Cdd:COG3173   236 lyWRLPDDLLGPRA-AFLAAYEEATGDLDDLTWWALADPEL 275
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
 95-238 6.43e-14

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: 69.19  E-value: 6.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981  95 WLLTTAIPGKTAFqvlEEYPDSGENIVDALAVFLRRLHSIPVCNCPF-NSDRVFRLAQAQSRMNNGLVDASDFDDERNgw 173
Cdd:cd05155    70 WSVYRWLEGETAA---DAPLADPAAAAEDLARFLAALHAIDPAGPPNpGRGNPLRGRDLAVRDAEEALAALAGLLDVA-- 144

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1376347981 174 PVEQVWKEMHNLLPFSPDSVVTHGDFSLDNLIFDEGKLIGCIDVGRVGIADRYQDLAILWNCLGE 238
Cdd:cd05155   145 AARALWERALAAPAWAGPPVWLHGDLHPGNLLVRDGRLSAVIDFGDLGVGDPACDLAIAWTLFDA 209
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 51-238 1.16e-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: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981  51 ELFLKHGKGSVANDVTDEMVRLNWLTEFM--PLPTIKHFIRTPDDAWLLTTAIPGKTAFQV-LEEYPDSGENIVDALAVF 127
Cdd:cd05120    22 EYVLKIGPPRLKKDLEKEAAMLQLLAGKLslPVPKVYGFGESDGWEYLLMERIEGETLSEVwPRLSEEEKEKIADQLAEI 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981 128 LRRLHSIPVcncpfnsdrvfrlaqaqsrmnnglvdasdfdderngwpveqvwkemhnllpfspdSVVTHGDFSLDNLIFD 207
Cdd:cd05120   102 LAALHRIDS-------------------------------------------------------SVLTHGDLHPGNILVK 126

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1376347981 208 -EGKLIGCIDVGRVGIADRYQDLAILWNCLGE 238
Cdd:cd05120   127 pDGKLSGIIDWEFAGYGPPAFDYAAALRDWTE 158
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
175-257 2.64e-07

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 49.01  E-value: 2.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981 175 VEQVWKEMHNLLPFSPDSVVTHGDFSLDNLIFDEGKLIGCIDVGRVGIADRYQDLAILWNCLGeFSPSLQKRLFQKYGID 254
Cdd:COG0510    32 LRRLEELERALAARPLPLVLCHGDLHPGNFLVTDDGRLYLIDWEYAGLGDPAFDLAALLVEYG-LSPEQAEELLEAYGFG 110


                  ...
gi 1376347981 255 NPD 257
Cdd:COG0510   111 RPT 113
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
 175-234 1.85e-06

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: 48.00  E-value: 1.85e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981 175 VEQVWKEMHNLLPFSpdsvVTHGDFSLDNLIFDEGKLIGCIDVGRVGIADRYQDLAILWN 234
Cdd:COG2334   166 LEARLAPLLGALPRG----VIHGDLHPDNVLFDGDGVSGLIDFDDAGYGPRLYDLAIALN 221
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
 91-236 8.69e-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: 46.07  E-value: 8.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981  91 PDDAWL-----LTTAIPGKTAFQVLEEYPDS-------GENIVDALAvflrRLHSIPVCNCPFnsDRVFRLAQAQSRMNN 158
Cdd:cd05154    70 EDPSVLgapfyVMERVDGRVLPDPLPRPDLSpeerralARSLVDALA----ALHSVDPAALGL--ADLGRPEGYLERQVD 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376347981 159 GLVDASDFDDERNGWPVEQV--WKEMHnlLPFSPDSVVTHGDFSLDNLIFDE-GKLIGCIDVGRVGIADRYQDLAilWNC 235
Cdd:cd05154   144 RWRRQLEAAATDPPPALEEAlrWLRAN--LPADGRPVLVHGDFRLGNLLFDPdGRVTAVLDWELATLGDPLEDLA--WLL 219


                  .
gi 1376347981 236 L 236
Cdd:cd05154   220 A 220
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
 175-231 3.11e-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: 41.48  E-value: 3.11e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1376347981 175 VEQVWKEMHNLLPFSPDSVVTHGDFSLDNLIFDEGKLIGCIDVGRVGIADRYQDLAI 231
Cdd:cd05153   162 LEDELARLQALAPSDLPRGVIHADLFRDNVLFDGDRLSGIIDFYDACYDPLLYDLAI 218
 
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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