NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|628823912|gb|AHY82607|]
View 

aminoglycoside phosphotransferase [Cloning vector pMRI-31]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Aph COG3231
Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];
10-269 2.53e-119

Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];


:

Pssm-ID: 442463 [Multi-domain]  Cd Length: 258  Bit Score: 341.51  E-value: 2.53e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912  10 RPRLNSNMDADLYGYKWARDNVGQSGATIYRLYGkPDAPELFLKHGKGSVANDVTDEMVRLNWLTEF-MPLPTIKHFIRT 88
Cdd:COG3231    1 GPRLPPALRELLGGYRWEPVTIGESGAKVFRLAD-GGRPTLYLKIEPAGPAAELEDEADRLRWLAGQgLPVPEVLDFGED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912  89 PDDAWLLTTAIPGKTAFQVleEYPDSGENIVDALAVFLRRLHSIPVCNCPFNSDRVFRLAQAQSRMNNGLVDASDFDDER 168
Cdd:COG3231   80 DGGAWLLTTAVPGRPAASV--SEALDPERAVELLAEALRRLHALPVADCPFDRRLERRLAEARARVAAGLVDPDDFDEER 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912 169 NGWPVEQVWKEMHKLLPFSPDSVVTHGDFSLDNLIFDEGKLIGCIDVGRVGIADRYQDLAILWNCLGE-FSPSLQKRLFQ 247
Cdd:COG3231  158 RGRPPEELLAELLAERPAEEDLVVTHGDACLPNILVDPGTFSGFIDLGRLGVADRYQDLALAARSLREnLGEGWVEPFLD 237

                        250       260
                 ....*....|....*....|..
gi 628823912 248 KYGIDnPDMNKLQFHLMLDEFF 269
Cdd:COG3231  238 AYGIA-PDPERLAFYRLLDEFF 258
 
Name Accession Description Interval E-value
Aph COG3231
Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];
10-269 2.53e-119

Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442463 [Multi-domain]  Cd Length: 258  Bit Score: 341.51  E-value: 2.53e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912  10 RPRLNSNMDADLYGYKWARDNVGQSGATIYRLYGkPDAPELFLKHGKGSVANDVTDEMVRLNWLTEF-MPLPTIKHFIRT 88
Cdd:COG3231    1 GPRLPPALRELLGGYRWEPVTIGESGAKVFRLAD-GGRPTLYLKIEPAGPAAELEDEADRLRWLAGQgLPVPEVLDFGED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912  89 PDDAWLLTTAIPGKTAFQVleEYPDSGENIVDALAVFLRRLHSIPVCNCPFNSDRVFRLAQAQSRMNNGLVDASDFDDER 168
Cdd:COG3231   80 DGGAWLLTTAVPGRPAASV--SEALDPERAVELLAEALRRLHALPVADCPFDRRLERRLAEARARVAAGLVDPDDFDEER 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912 169 NGWPVEQVWKEMHKLLPFSPDSVVTHGDFSLDNLIFDEGKLIGCIDVGRVGIADRYQDLAILWNCLGE-FSPSLQKRLFQ 247
Cdd:COG3231  158 RGRPPEELLAELLAERPAEEDLVVTHGDACLPNILVDPGTFSGFIDLGRLGVADRYQDLALAARSLREnLGEGWVEPFLD 237

                        250       260
                 ....*....|....*....|..
gi 628823912 248 KYGIDnPDMNKLQFHLMLDEFF 269
Cdd:COG3231  238 AYGIA-PDPERLAFYRLLDEFF 258
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
 24-269 4.92e-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: 307.20  E-value: 4.92e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912  24 YKWARDNVGQSGATIYRLYGKPdaPELFLKHGKGSVANDVTDEMVRLNWLTEFMPLPTIKHFIRTPDDAWLLTTAIPGKT 103
Cdd:cd05150    1 YRWEPDTIGESGARVYRLDGGG--PVLYLKTAPAGYAYELAREAERLRWLAGKLPVPEVLDYGSDDGGDWLLTTALPGRD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912 104 AFQvlEEYPDSGENIVDALAVFLRRLHSIPVCNCPFNSDRVFRLAQAQSRMNNGLVDASDFDDERNGWPVEQVWKEMHKL 183
Cdd:cd05150   79 AAS--LEPLLDPERLVDLLAEALRALHSLPIADCPFDRRLDARLAEARARVEAGLVDEDDFDEERQGRTAEELLAELEAT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912 184 LPFSPDSVVTHGDFSLDNLIFDEGKLIGCIDVGRVGIADRYQDLAILWNCLGEF--SPSLQKRLFQKYGIDNPDMNKLQF 261
Cdd:cd05150  157 RPAEEDLVVTHGDACLPNIILDPGRFSGFIDLGRLGVADRYQDLALAVRSLRENlgGEEYAERFLDAYGIDAPDPERLAY 236


                 ....*...
gi 628823912 262 HLMLDEFF 269
Cdd:cd05150  237 YRLLDEFF 244
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 25-255 4.87e-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: 99.50  E-value: 4.87e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912   25 KWARDNVGQSGATIYRLYGKPdapELFLK-HGKGSVANDVTDEMVRLNWLTE--FMPLPTIKHFIRTPDD---AWLLTTA 98
Cdd:pfam01636   1 TLRPISSGASNRTYLVTTGDG---RYVLRlPPPGRAAEELRRELALLRHLAAagVPPVPRVLAGCTDAELlglPFLLMEY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912   99 IPGKTAFQVLEeyPDSGENIVDALAVFLRRLHSIPVCNCPFNSDRVFRLAQAQSRMN--NGLVDASDFDdeRNGWPVEQV 176
Cdd:pfam01636  78 LPGEVLARPLL--PEERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAalARLLAAELLD--RLEELEERL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912  177 WKEMHKLLPFSPDSVVTHGDFSLDNLIFDE-GKLIGCIDVGRVGIADRYQDLAILWNCLG-EFSPSLQKRLFQKYGIDNP 254
Cdd:pfam01636 154 LAALLALLPAELPPVLVHGDLHPGNLLVDPgGRVSGVIDFEDAGLGDPAYDLAILLNSWGrELGAELLAAYLAAYGAFGY 233


                  .
gi 628823912  255 D 255
Cdd:pfam01636 234 A 234
 
Name Accession Description Interval E-value
Aph COG3231
Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];
10-269 2.53e-119

Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442463 [Multi-domain]  Cd Length: 258  Bit Score: 341.51  E-value: 2.53e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912  10 RPRLNSNMDADLYGYKWARDNVGQSGATIYRLYGkPDAPELFLKHGKGSVANDVTDEMVRLNWLTEF-MPLPTIKHFIRT 88
Cdd:COG3231    1 GPRLPPALRELLGGYRWEPVTIGESGAKVFRLAD-GGRPTLYLKIEPAGPAAELEDEADRLRWLAGQgLPVPEVLDFGED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912  89 PDDAWLLTTAIPGKTAFQVleEYPDSGENIVDALAVFLRRLHSIPVCNCPFNSDRVFRLAQAQSRMNNGLVDASDFDDER 168
Cdd:COG3231   80 DGGAWLLTTAVPGRPAASV--SEALDPERAVELLAEALRRLHALPVADCPFDRRLERRLAEARARVAAGLVDPDDFDEER 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912 169 NGWPVEQVWKEMHKLLPFSPDSVVTHGDFSLDNLIFDEGKLIGCIDVGRVGIADRYQDLAILWNCLGE-FSPSLQKRLFQ 247
Cdd:COG3231  158 RGRPPEELLAELLAERPAEEDLVVTHGDACLPNILVDPGTFSGFIDLGRLGVADRYQDLALAARSLREnLGEGWVEPFLD 237

                        250       260
                 ....*....|....*....|..
gi 628823912 248 KYGIDnPDMNKLQFHLMLDEFF 269
Cdd:COG3231  238 AYGIA-PDPERLAFYRLLDEFF 258
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
 24-269 4.92e-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: 307.20  E-value: 4.92e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912  24 YKWARDNVGQSGATIYRLYGKPdaPELFLKHGKGSVANDVTDEMVRLNWLTEFMPLPTIKHFIRTPDDAWLLTTAIPGKT 103
Cdd:cd05150    1 YRWEPDTIGESGARVYRLDGGG--PVLYLKTAPAGYAYELAREAERLRWLAGKLPVPEVLDYGSDDGGDWLLTTALPGRD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912 104 AFQvlEEYPDSGENIVDALAVFLRRLHSIPVCNCPFNSDRVFRLAQAQSRMNNGLVDASDFDDERNGWPVEQVWKEMHKL 183
Cdd:cd05150   79 AAS--LEPLLDPERLVDLLAEALRALHSLPIADCPFDRRLDARLAEARARVEAGLVDEDDFDEERQGRTAEELLAELEAT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912 184 LPFSPDSVVTHGDFSLDNLIFDEGKLIGCIDVGRVGIADRYQDLAILWNCLGEF--SPSLQKRLFQKYGIDNPDMNKLQF 261
Cdd:cd05150  157 RPAEEDLVVTHGDACLPNIILDPGRFSGFIDLGRLGVADRYQDLALAVRSLRENlgGEEYAERFLDAYGIDAPDPERLAY 236


                 ....*...
gi 628823912 262 HLMLDEFF 269
Cdd:cd05150  237 YRLLDEFF 244
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 25-255 4.87e-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: 99.50  E-value: 4.87e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912   25 KWARDNVGQSGATIYRLYGKPdapELFLK-HGKGSVANDVTDEMVRLNWLTE--FMPLPTIKHFIRTPDD---AWLLTTA 98
Cdd:pfam01636   1 TLRPISSGASNRTYLVTTGDG---RYVLRlPPPGRAAEELRRELALLRHLAAagVPPVPRVLAGCTDAELlglPFLLMEY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912   99 IPGKTAFQVLEeyPDSGENIVDALAVFLRRLHSIPVCNCPFNSDRVFRLAQAQSRMN--NGLVDASDFDdeRNGWPVEQV 176
Cdd:pfam01636  78 LPGEVLARPLL--PEERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAalARLLAAELLD--RLEELEERL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912  177 WKEMHKLLPFSPDSVVTHGDFSLDNLIFDE-GKLIGCIDVGRVGIADRYQDLAILWNCLG-EFSPSLQKRLFQKYGIDNP 254
Cdd:pfam01636 154 LAALLALLPAELPPVLVHGDLHPGNLLVDPgGRVSGVIDFEDAGLGDPAYDLAILLNSWGrELGAELLAAYLAAYGAFGY 233


                  .
gi 628823912  255 D 255
Cdd:pfam01636 234 A 234
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 78-269 1.81e-15

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 74.38  E-value: 1.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912  78 PLPTIKHFIRTPDD---AWLLTTAIPGKTAFQVL-EEYPDSGENIVDALAVFLRRLHSIPVCNCPFNSDRVFRLAQAQSR 153
Cdd:COG3173   77 PVPRPLALGEDGEVigaPFYVMEWVEGETLEDALpDLSPAERRALARALGEFLAALHAVDPAAAGLADGRPEGLERQLAR 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912 154 MNNGLVDASDfdderNGWPVEQVWKEMHKLL----PFSPDSVVTHGDFSLDNLIFD--EGKLIGCIDVGRVGIADRYQDL 227
Cdd:COG3173  157 WRAQLRRALA-----RTDDLPALRERLAAWLaanlPEWGPPVLVHGDLRPGNLLVDpdDGRLTAVIDWELATLGDPAADL 231

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 628823912 228 AIL---WNCLGEFSPSLQkRLFQKYGIDNPDMNKLQFHLMLDEFF 269
Cdd:COG3173  232 AYLllyWRLPDDLLGPRA-AFLAAYEEATGDLDDLTWWALADPEL 275
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
 93-236 1.29e-13

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: 68.42  E-value: 1.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912  93 WLLTTAIPGKTAFqvlEEYPDSGENIVDALAVFLRRLHSIPVCNCPF-NSDRVFRLAQAQSRMNNGLVDASDFDDERNgw 171
Cdd:cd05155   70 WSVYRWLEGETAA---DAPLADPAAAAEDLARFLAALHAIDPAGPPNpGRGNPLRGRDLAVRDAEEALAALAGLLDVA-- 144

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 628823912 172 PVEQVWKEMHKLLPFSPDSVVTHGDFSLDNLIFDEGKLIGCIDVGRVGIADRYQDLAILWNCLGE 236
Cdd:cd05155  145 AARALWERALAAPAWAGPPVWLHGDLHPGNLLVRDGRLSAVIDFGDLGVGDPACDLAIAWTLFDA 209
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 46-236 1.04e-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: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912  46 DAPELFLKHGKGSVANDVTDEMVRLNWLTEFM--PLPTIKHFIRTPDDAWLLTTAIPGKTAFQV-LEEYPDSGENIVDAL 122
Cdd:cd05120   19 DPREYVLKIGPPRLKKDLEKEAAMLQLLAGKLslPVPKVYGFGESDGWEYLLMERIEGETLSEVwPRLSEEEKEKIADQL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912 123 AVFLRRLHSIPVcncpfnsdrvfrlaqaqsrmnnglvdasdfdderngwpveqvwkemhkllpfspdSVVTHGDFSLDNL 202
Cdd:cd05120   99 AEILAALHRIDS-------------------------------------------------------SVLTHGDLHPGNI 123

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 628823912 203 IFD-EGKLIGCIDVGRVGIADRYQDLAILWNCLGE 236
Cdd:cd05120  124 LVKpDGKLSGIIDWEFAGYGPPAFDYAAALRDWTE 158
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
175-255 1.27e-07

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 50.16  E-value: 1.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912 175 QVWKEMHKLLPFSP-DSVVTHGDFSLDNLIFDEGKLIGCIDVGRVGIADRYQDLAILWNCLGeFSPSLQKRLFQKYGIDN 253
Cdd:COG0510   33 RRLEELERALAARPlPLVLCHGDLHPGNFLVTDDGRLYLIDWEYAGLGDPAFDLAALLVEYG-LSPEQAEELLEAYGFGR 111


                 ..
gi 628823912 254 PD 255
Cdd:COG0510  112 PT 113
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
 173-232 1.63e-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: 48.38  E-value: 1.63e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912 173 VEQVWKEMHKLLPFSpdsvVTHGDFSLDNLIFDEGKLIGCIDVGRVGIADRYQDLAILWN 232
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 ...
 89-234 8.64e-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: 45.68  E-value: 8.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912  89 PDDAWL-----LTTAIPGKTAFQVLEEYPDS-------GENIVDALAvflrRLHSIPVCNCPFnsDRVFRLAQAQSRMNN 156
Cdd:cd05154   70 EDPSVLgapfyVMERVDGRVLPDPLPRPDLSpeerralARSLVDALA----ALHSVDPAALGL--ADLGRPEGYLERQVD 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628823912 157 GLVDASDFDDERNGWPVEQV--WKEMHklLPFSPDSVVTHGDFSLDNLIFDE-GKLIGCIDVGRVGIADRYQDLAilWNC 233
Cdd:cd05154  144 RWRRQLEAAATDPPPALEEAlrWLRAN--LPADGRPVLVHGDFRLGNLLFDPdGRVTAVLDWELATLGDPLEDLA--WLL 219


                 .
gi 628823912 234 L 234
Cdd:cd05154  220 A 220
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
 173-229 2.80e-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: 2.80e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 628823912 173 VEQVWKEMHKLLPFSPDSVVTHGDFSLDNLIFDEGKLIGCIDVGRVGIADRYQDLAI 229
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH