NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|87042826|gb|ABD16421|]
View 

aminoglycoside phosphotransferase [Binary vector pCsGFPBT]

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];
4-264 1.04e-111

Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];


:

Pssm-ID: 442463 [Multi-domain]  Cd Length: 258  Bit Score: 322.25  E-value: 1.04e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826   4 MRISPELKKLIEKYRCVKDTEGMSPAKVYKLV-GENENLYLKMTdsrYKGTTYDVEREKDMMLWLEGK-LPVPKVLHFER 81
Cdd:COG3231   2 PRLPPALRELLGGYRWEPVTIGESGAKVFRLAdGGRPTLYLKIE---PAGPAAELEDEADRLRWLAGQgLPVPEVLDFGE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826  82 HDGWSNLLMSEADGVLCSEEYEdEQSPEKIIELYAECIRLFHSIDISDCPYTNSLDSRLAELDYLLNNDLadVDCENWEE 161
Cdd:COG3231  79 DDGGAWLLTTAVPGRPAASVSE-ALDPERAVELLAEALRRLHALPVADCPFDRRLERRLAEARARVAAGL--VDPDDFDE 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826 162 DTPFKDPRELYDFLKTEKP-EEELVFSHGDLGDSNIFVKDGKVSGFIDLGRSGRADKWYDIAFCVRSIREDIGEEqYVEL 240
Cdd:COG3231 156 ERRGRPPEELLAELLAERPaEEDLVVTHGDACLPNILVDPGTFSGFIDLGRLGVADRYQDLALAARSLRENLGEG-WVEP 234

                       250       260
                ....*....|....*....|....
gi 87042826 241 FFDLLGIKPDWEKIKYYILLDELF 264
Cdd:COG3231 235 FLDAYGIAPDPERLAFYRLLDEFF 258
 
Name Accession Description Interval E-value
Aph COG3231
Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];
4-264 1.04e-111

Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442463 [Multi-domain]  Cd Length: 258  Bit Score: 322.25  E-value: 1.04e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826   4 MRISPELKKLIEKYRCVKDTEGMSPAKVYKLV-GENENLYLKMTdsrYKGTTYDVEREKDMMLWLEGK-LPVPKVLHFER 81
Cdd:COG3231   2 PRLPPALRELLGGYRWEPVTIGESGAKVFRLAdGGRPTLYLKIE---PAGPAAELEDEADRLRWLAGQgLPVPEVLDFGE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826  82 HDGWSNLLMSEADGVLCSEEYEdEQSPEKIIELYAECIRLFHSIDISDCPYTNSLDSRLAELDYLLNNDLadVDCENWEE 161
Cdd:COG3231  79 DDGGAWLLTTAVPGRPAASVSE-ALDPERAVELLAEALRRLHALPVADCPFDRRLERRLAEARARVAAGL--VDPDDFDE 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826 162 DTPFKDPRELYDFLKTEKP-EEELVFSHGDLGDSNIFVKDGKVSGFIDLGRSGRADKWYDIAFCVRSIREDIGEEqYVEL 240
Cdd:COG3231 156 ERRGRPPEELLAELLAERPaEEDLVVTHGDACLPNILVDPGTFSGFIDLGRLGVADRYQDLALAARSLRENLGEG-WVEP 234

                       250       260
                ....*....|....*....|....
gi 87042826 241 FFDLLGIKPDWEKIKYYILLDELF 264
Cdd:COG3231 235 FLDAYGIAPDPERLAFYRLLDEFF 258
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
 17-264 4.56e-103

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: 299.50  E-value: 4.56e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826  17 YRCVKDTEGMSPAKVYKLVGENENLYLKMTDSRYkgtTYDVEREKDMMLWLEGKLPVPKVLHFERHDGWSNLLMSEADGV 96
Cdd:cd05150   1 YRWEPDTIGESGARVYRLDGGGPVLYLKTAPAGY---AYELAREAERLRWLAGKLPVPEVLDYGSDDGGDWLLTTALPGR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826  97 LCSEEYEDEQsPEKIIELYAECIRLFHSIDISDCPYTNSLDSRLAELDYLLNNDLADVDceNWEEDTPFKDPRELYDFLK 176
Cdd:cd05150  78 DAASLEPLLD-PERLVDLLAEALRALHSLPIADCPFDRRLDARLAEARARVEAGLVDED--DFDEERQGRTAEELLAELE 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826 177 TEKPEEE-LVFSHGDLGDSNIFVKDGKVSGFIDLGRSGRADKWYDIAFCVRSIREDIGEEQYVELFFDLLGI-KPDWEKI 254
Cdd:cd05150 155 ATRPAEEdLVVTHGDACLPNIILDPGRFSGFIDLGRLGVADRYQDLALAVRSLRENLGGEEYAERFLDAYGIdAPDPERL 234

                       250
                ....*....|
gi 87042826 255 KYYILLDELF 264
Cdd:cd05150 235 AYYRLLDEFF 244
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 31-257 4.77e-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: 4.77e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826    31 VYKLVGENENLYLKmtDSRYKGTTYDVEREKDMMLWL--EGKLPVPKVLHFER---HDGWSNLLMSEADGVLCsEEYEDE 105
Cdd:pfam01636  13 TYLVTTGDGRYVLR--LPPPGRAAEELRRELALLRHLaaAGVPPVPRVLAGCTdaeLLGLPFLLMEYLPGEVL-ARPLLP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826   106 QSPEKIIELYAECIRLFHSIDISDCPYTNSLDSRLAELDYLLNNDLADVDCENweEDTPFKDPRELYDFLKTEKP-EEEL 184
Cdd:pfam01636  90 EERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAAEL--LDRLEELEERLLAALLALLPaELPP 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 87042826   185 VFSHGDLGDSNIFV-KDGKVSGFIDLGRSGRADKWYDIAFCVRSIREDIGEEQYVELFFDLLgiKPDWEKIKYY 257
Cdd:pfam01636 168 VLVHGDLHPGNLLVdPGGRVSGVIDFEDAGLGDPAYDLAILLNSWGRELGAELLAAYLAAYG--AFGYARLREL 239
 
Name Accession Description Interval E-value
Aph COG3231
Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];
4-264 1.04e-111

Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442463 [Multi-domain]  Cd Length: 258  Bit Score: 322.25  E-value: 1.04e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826   4 MRISPELKKLIEKYRCVKDTEGMSPAKVYKLV-GENENLYLKMTdsrYKGTTYDVEREKDMMLWLEGK-LPVPKVLHFER 81
Cdd:COG3231   2 PRLPPALRELLGGYRWEPVTIGESGAKVFRLAdGGRPTLYLKIE---PAGPAAELEDEADRLRWLAGQgLPVPEVLDFGE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826  82 HDGWSNLLMSEADGVLCSEEYEdEQSPEKIIELYAECIRLFHSIDISDCPYTNSLDSRLAELDYLLNNDLadVDCENWEE 161
Cdd:COG3231  79 DDGGAWLLTTAVPGRPAASVSE-ALDPERAVELLAEALRRLHALPVADCPFDRRLERRLAEARARVAAGL--VDPDDFDE 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826 162 DTPFKDPRELYDFLKTEKP-EEELVFSHGDLGDSNIFVKDGKVSGFIDLGRSGRADKWYDIAFCVRSIREDIGEEqYVEL 240
Cdd:COG3231 156 ERRGRPPEELLAELLAERPaEEDLVVTHGDACLPNILVDPGTFSGFIDLGRLGVADRYQDLALAARSLRENLGEG-WVEP 234

                       250       260
                ....*....|....*....|....
gi 87042826 241 FFDLLGIKPDWEKIKYYILLDELF 264
Cdd:COG3231 235 FLDAYGIAPDPERLAFYRLLDEFF 258
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
 17-264 4.56e-103

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: 299.50  E-value: 4.56e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826  17 YRCVKDTEGMSPAKVYKLVGENENLYLKMTDSRYkgtTYDVEREKDMMLWLEGKLPVPKVLHFERHDGWSNLLMSEADGV 96
Cdd:cd05150   1 YRWEPDTIGESGARVYRLDGGGPVLYLKTAPAGY---AYELAREAERLRWLAGKLPVPEVLDYGSDDGGDWLLTTALPGR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826  97 LCSEEYEDEQsPEKIIELYAECIRLFHSIDISDCPYTNSLDSRLAELDYLLNNDLADVDceNWEEDTPFKDPRELYDFLK 176
Cdd:cd05150  78 DAASLEPLLD-PERLVDLLAEALRALHSLPIADCPFDRRLDARLAEARARVEAGLVDED--DFDEERQGRTAEELLAELE 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826 177 TEKPEEE-LVFSHGDLGDSNIFVKDGKVSGFIDLGRSGRADKWYDIAFCVRSIREDIGEEQYVELFFDLLGI-KPDWEKI 254
Cdd:cd05150 155 ATRPAEEdLVVTHGDACLPNIILDPGRFSGFIDLGRLGVADRYQDLALAVRSLRENLGGEEYAERFLDAYGIdAPDPERL 234

                       250
                ....*....|
gi 87042826 255 KYYILLDELF 264
Cdd:cd05150 235 AYYRLLDEFF 244
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 17-230 7.50e-31

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: 112.40  E-value: 7.50e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826  17 YRCVKDTEGMSpAKVYkLVGENENLYLKMTDSRYKgttYDVEREKDMMLWLEGK--LPVPKVLHFERHDGWSNLLMSEAD 94
Cdd:cd05120   1 ISVKLIKEGGD-NKVY-LLGDPREYVLKIGPPRLK---KDLEKEAAMLQLLAGKlsLPVPKVYGFGESDGWEYLLMERIE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826  95 GVLCSEEY--EDEQSPEKIIELYAECIRLFHSIDISdcpytnsldsrlaeldyllnndladvdcenweedtpfkdprely 172
Cdd:cd05120  76 GETLSEVWprLSEEEKEKIADQLAEILAALHRIDSS-------------------------------------------- 111

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 87042826 173 dflktekpeeelVFSHGDLGDSNIFVKD-GKVSGFIDLGRSGRADKWYDIAFCVRSIRE 230
Cdd:cd05120 112 ------------VLTHGDLHPGNILVKPdGKLSGIIDWEFAGYGPPAFDYAAALRDWTE 158
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
 22-210 2.86e-29

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 107.53  E-value: 2.86e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826  22 DTEGMsPAKVYKLVGE--NENLYLKMTDSRYKGTTYDVEREKDMMLWLEGK-LPVPKVLHFERHDGWSNLLMSEADGVLC 98
Cdd:cd13968   1 MGEGA-SAKVFWAEGEctTIGVAVKIGDDVNNEEGEDLESEMDILRRLKGLeLNIPKVLVTEDVDGPNILLMELVKGGTL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826  99 SE----EYEDEQSPEKIIELYAECIRLFHSIdisdcpytnsldsrlaeldyllnndladvdcenweedtpfkdprelydf 174
Cdd:cd13968  80 IAytqeEELDEKDVESIMYQLAECMRLLHSF------------------------------------------------- 110

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 87042826 175 lktekpeeelVFSHGDLGDSNIFVKDGKVSGFIDLG 210
Cdd:cd13968 111 ----------HLIHRDLNNDNILLSEDGNVKLIDFG 136
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 31-257 4.77e-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: 4.77e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826    31 VYKLVGENENLYLKmtDSRYKGTTYDVEREKDMMLWL--EGKLPVPKVLHFER---HDGWSNLLMSEADGVLCsEEYEDE 105
Cdd:pfam01636  13 TYLVTTGDGRYVLR--LPPPGRAAEELRRELALLRHLaaAGVPPVPRVLAGCTdaeLLGLPFLLMEYLPGEVL-ARPLLP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826   106 QSPEKIIELYAECIRLFHSIDISDCPYTNSLDSRLAELDYLLNNDLADVDCENweEDTPFKDPRELYDFLKTEKP-EEEL 184
Cdd:pfam01636  90 EERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAAEL--LDRLEELEERLLAALLALLPaELPP 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 87042826   185 VFSHGDLGDSNIFV-KDGKVSGFIDLGRSGRADKWYDIAFCVRSIREDIGEEQYVELFFDLLgiKPDWEKIKYY 257
Cdd:pfam01636 168 VLVHGDLHPGNLLVdPGGRVSGVIDFEDAGLGDPAYDLAILLNSWGRELGAELLAAYLAAYG--AFGYARLREL 239
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 34-264 2.53e-13

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 68.22  E-value: 2.53e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826  34 LVGENENLYLKMtDSRYKGTTYDVEREKDMMLWLEGKL--PVPKVLHFERHD---GWSNLLMSEADGVlCSEEYEDEQSP 108
Cdd:COG3173  38 RLDTGDRLVLRR-PPRGLASAHDVRREARVLRALAPRLgvPVPRPLALGEDGeviGAPFYVMEWVEGE-TLEDALPDLSP 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826 109 EKIIELYAECIRLF---HSIDISDCPYTnslDSRLAELDYLLNNDLADVDCENWEEDTPFKDPRELYDFLKTEKPEE-EL 184
Cdd:COG3173 116 AERRALARALGEFLaalHAVDPAAAGLA---DGRPEGLERQLARWRAQLRRALARTDDLPALRERLAAWLAANLPEWgPP 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826 185 VFSHGDLGDSNIFV--KDGKVSGFIDLGRSGRADKWYDIAFCVRSIREDIG----EEQYVELFFDLLGIKPDWEkikYYI 258
Cdd:COG3173 193 VLVHGDLRPGNLLVdpDDGRLTAVIDWELATLGDPAADLAYLLLYWRLPDDllgpRAAFLAAYEEATGDLDDLT---WWA 269


                ....*.
gi 87042826 259 LLDELF 264
Cdd:COG3173 270 LADPEL 275
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
 188-243 1.23e-05

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: 45.69  E-value: 1.23e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 87042826 188 HGDLGDSNIFVKDGKVSGFIDLGRSGRADKWYDIAFCVRSIREDIGEEQYVELFFD 243
Cdd:COG2334 183 HGDLHPDNVLFDGDGVSGLIDFDDAGYGPRLYDLAIALNGWADGPLDPARLAALLE 238
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
 53-247 3.53e-05

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: 44.14  E-value: 3.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826  53 TTYDVEREKDMMLWLEGK-LPVPKVLHFE---RHDGWSNLLMSEADG-VLCSEEYEDEQSPEKIIELYAECIRLF---HS 124
Cdd:cd05154  41 SAHDLEREYRVLRALAGTgVPVPRVLALCedpSVLGAPFYVMERVDGrVLPDPLPRPDLSPEERRALARSLVDALaalHS 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826 125 IDISDCP---YTNSLDSRLAELDYLLnndladvdcENWEEDTPFKDP--RELYDFLKTEKPEE-ELVFSHGDLGDSN-IF 197
Cdd:cd05154 121 VDPAALGladLGRPEGYLERQVDRWR---------RQLEAAATDPPPalEEALRWLRANLPADgRPVLVHGDFRLGNlLF 191

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 87042826 198 VKDGKVSGFIDLGRSGRADKWYDIA-FCVRSIREdiGEEQYVELFFDLLGI 247
Cdd:cd05154 192 DPDGRVTAVLDWELATLGDPLEDLAwLLARWWRP--GDPPGLAAPTRLPGF 240
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
 188-243 1.24e-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: 42.63  E-value: 1.24e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 87042826 188 HGDLGDSNIFVKDGKVSGFIDLGRSGRADKWYDIA-FCVRSIREDIG--EEQYVELFFD 243
Cdd:cd05153 183 HADLFRDNVLFDGDRLSGIIDFYDACYDPLLYDLAiALNDWCFDDDGklDPERAKALLA 241
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
169-263 1.88e-04

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 40.92  E-value: 1.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826 169 RELYDFLKT--EKPEEELVFSHGDLGDSNIFV-KDGKVSgFIDLGRSGRADKWYDIA-FCVRSIREDIGEEQYVELFFDL 244
Cdd:COG0510  32 LRRLEELERalAARPLPLVLCHGDLHPGNFLVtDDGRLY-LIDWEYAGLGDPAFDLAaLLVEYGLSPEQAEELLEAYGFG 110

                        90
                ....*....|....*....
gi 87042826 245 LGIKPDWEKIKYYILLDEL 263
Cdd:COG0510 111 RPTEELLRRLRAYRALADL 129
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 57-222 2.56e-03

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 37.63  E-value: 2.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826  57 VEREKDMMLWLEGK-LPVPKVLHFERHDGWsnLLMSEADGVLCSEEYEDEQSPEKIIELYAECIRLFHSIDIsdcpytns 135
Cdd:COG3642   3 TRREARLLRELREAgVPVPKVLDVDPDDAD--LVMEYIEGETLADLLEEGELPPELLRELGRLLARLHRAGI-------- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87042826 136 ldsrlaeldyllnndladvdcenweedtpfkdprelydflktekpeeelvfSHGDLGDSNIFVKDGKVsGFIDLGRSGRA 215
Cdd:COG3642  73 ---------------------------------------------------VHGDLTTSNILVDDGGV-YLIDFGLARYS 100


                ....*..
gi 87042826 216 DKWYDIA 222
Cdd:COG3642 101 DPLEDKA 107
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
 185-216 3.08e-03

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: 37.99  E-value: 3.08e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 87042826 185 VFSHGDLGDSNIFVKDGKVSGFIDLGRSGRAD 216
Cdd:cd05155 164 VWLHGDLHPGNLLVRDGRLSAVIDFGDLGVGD 195
 
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