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Conserved domains on  [gi|576290949|gb|AHH29445|]
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neomycin phosphotransferase III, partial [Enterococcus faecium]

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 ...
5-252 6.95e-102

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: 296.03  E-value: 6.95e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949   5 YRCVKDTEGMSPAKVYKLVGENENLYLKMTDSRYkgtTYDVEREKDMMLWLEGKLPVPKVLHFERHDGWSNLLMSEADGV 84
Cdd:cd05150    1 YRWEPDTIGESGARVYRLDGGGPVLYLKTAPAGY---AYELAREAERLRWLAGKLPVPEVLDYGSDDGGDWLLTTALPGR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949  85 LCSEEYEDEQsPEKIIELYAECIRLFHSIDISDCPYTNSLDSRLAELDYLLNNDLADVDceNWEEDTPFKDPRELYDFLK 164
Cdd:cd05150   78 DAASLEPLLD-PERLVDLLAEALRALHSLPIADCPFDRRLDARLAEARARVEAGLVDED--DFDEERQGRTAEELLAELE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949 165 TEKPEEE-LVFSHGDLGDSNIFVKDGKVSGFIDLGRSGRADKWYDIAFCVRSIREDIGEEQYVELFFDLLGI-KPDWEKI 242
Cdd:cd05150  155 ATRPAEEdLVVTHGDACLPNIILDPGRFSGFIDLGRLGVADRYQDLALAVRSLRENLGGEEYAERFLDAYGIdAPDPERL 234
                        250
                 ....*....|
gi 576290949 243 KYYILLDELF 252
Cdd:cd05150  235 AYYRLLDEFF 244
 
Name Accession Description Interval E-value
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
5-252 6.95e-102

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: 296.03  E-value: 6.95e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949   5 YRCVKDTEGMSPAKVYKLVGENENLYLKMTDSRYkgtTYDVEREKDMMLWLEGKLPVPKVLHFERHDGWSNLLMSEADGV 84
Cdd:cd05150    1 YRWEPDTIGESGARVYRLDGGGPVLYLKTAPAGY---AYELAREAERLRWLAGKLPVPEVLDYGSDDGGDWLLTTALPGR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949  85 LCSEEYEDEQsPEKIIELYAECIRLFHSIDISDCPYTNSLDSRLAELDYLLNNDLADVDceNWEEDTPFKDPRELYDFLK 164
Cdd:cd05150   78 DAASLEPLLD-PERLVDLLAEALRALHSLPIADCPFDRRLDARLAEARARVEAGLVDED--DFDEERQGRTAEELLAELE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949 165 TEKPEEE-LVFSHGDLGDSNIFVKDGKVSGFIDLGRSGRADKWYDIAFCVRSIREDIGEEQYVELFFDLLGI-KPDWEKI 242
Cdd:cd05150  155 ATRPAEEdLVVTHGDACLPNIILDPGRFSGFIDLGRLGVADRYQDLALAVRSLRENLGGEEYAERFLDAYGIdAPDPERL 234
                        250
                 ....*....|
gi 576290949 243 KYYILLDELF 252
Cdd:cd05150  235 AYYRLLDEFF 244
Aph COG3231
Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];
5-252 3.53e-49

Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 225771 [Multi-domain]  Cd Length: 266  Bit Score: 162.65  E-value: 3.53e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949   5 YRCVKDTEGMSPAKVYKL-VGENENLYLKMTDSrykGTTYDVEREKDMMLWLEG-KLPVPKVLHFERHDGWSNLLMSEAD 82
Cdd:COG3231   21 RRWRRVTEGESGAGVFRLfADSRPGLYLKIASS---GPAAELEGEAARLRWLAGqGLGCPRVLGLEDDADQAWLLMSALP 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949  83 GVLCSEEyEDEQSPEKIIELYAECIRLFHSIDISDCPYTNSLDSRLAELDYLLNNDLadVDCENWEEDTPFKDPRELYDF 162
Cdd:COG3231   98 GEDASHP-RYALDPKRAVPLLAEALRRLHELPVEACPFDRRLARRLAKARARVRAGL--VDESDFDEERQGRTAEELFDE 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949 163 LKTEKPEEE-LVFSHGDLGDSNIFVKDGKVSGFIDLGRSGRADKWYDIAFCVRSIREDIGEEQYVELFFDLLGI-KPDWE 240
Cdd:COG3231  175 LEARRPAVEdLVVTHGDACLPNFILDGWRFSGFIDLGRLGVADRHQDLALATWSLRFNLGGDVWDDPFLDAYGRgAIDPA 254
                        250
                 ....*....|..
gi 576290949 241 KIKYYILLDELF 252
Cdd:COG3231  255 RLAYYRLLDEFF 266
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
19-245 1.88e-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: 97.57  E-value: 1.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949   19 VYKLVGENENLYLKmtDSRYKGTTYDVEREKDMMLWL--EGKLPVPKVLHFER---HDGWSNLLMSEADGVLCsEEYEDE 93
Cdd:pfam01636  13 TYLVTTGDGRYVLR--LPPPGRAAEELRRELALLRHLaaAGVPPVPRVLAGCTdaeLLGLPFLLMEYLPGEVL-ARPLLP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949   94 QSPEKIIELYAECIRLFHSIDISDCPYTNSLDSRLAELDYLLNNDLADVDCENweEDTPFKDPRELYDFLKTEKP-EEEL 172
Cdd:pfam01636  90 EERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAAEL--LDRLEELEERLLAALLALLPaELPP 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 576290949  173 VFSHGDLGDSNIFV-KDGKVSGFIDLGRSGRADKWYDIAFCVRSIREDIGEEQYVELFFDLLgiKPDWEKIKYY 245
Cdd:pfam01636 168 VLVHGDLHPGNLLVdPGGRVSGVIDFEDAGLGDPAYDLAILLNSWGRELGAELLAAYLAAYG--AFGYARLREL 239
 
Name Accession Description Interval E-value
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
5-252 6.95e-102

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: 296.03  E-value: 6.95e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949   5 YRCVKDTEGMSPAKVYKLVGENENLYLKMTDSRYkgtTYDVEREKDMMLWLEGKLPVPKVLHFERHDGWSNLLMSEADGV 84
Cdd:cd05150    1 YRWEPDTIGESGARVYRLDGGGPVLYLKTAPAGY---AYELAREAERLRWLAGKLPVPEVLDYGSDDGGDWLLTTALPGR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949  85 LCSEEYEDEQsPEKIIELYAECIRLFHSIDISDCPYTNSLDSRLAELDYLLNNDLADVDceNWEEDTPFKDPRELYDFLK 164
Cdd:cd05150   78 DAASLEPLLD-PERLVDLLAEALRALHSLPIADCPFDRRLDARLAEARARVEAGLVDED--DFDEERQGRTAEELLAELE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949 165 TEKPEEE-LVFSHGDLGDSNIFVKDGKVSGFIDLGRSGRADKWYDIAFCVRSIREDIGEEQYVELFFDLLGI-KPDWEKI 242
Cdd:cd05150  155 ATRPAEEdLVVTHGDACLPNIILDPGRFSGFIDLGRLGVADRYQDLALAVRSLRENLGGEEYAERFLDAYGIdAPDPERL 234
                        250
                 ....*....|
gi 576290949 243 KYYILLDELF 252
Cdd:cd05150  235 AYYRLLDEFF 244
Aph COG3231
Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];
5-252 3.53e-49

Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 225771 [Multi-domain]  Cd Length: 266  Bit Score: 162.65  E-value: 3.53e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949   5 YRCVKDTEGMSPAKVYKL-VGENENLYLKMTDSrykGTTYDVEREKDMMLWLEG-KLPVPKVLHFERHDGWSNLLMSEAD 82
Cdd:COG3231   21 RRWRRVTEGESGAGVFRLfADSRPGLYLKIASS---GPAAELEGEAARLRWLAGqGLGCPRVLGLEDDADQAWLLMSALP 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949  83 GVLCSEEyEDEQSPEKIIELYAECIRLFHSIDISDCPYTNSLDSRLAELDYLLNNDLadVDCENWEEDTPFKDPRELYDF 162
Cdd:COG3231   98 GEDASHP-RYALDPKRAVPLLAEALRRLHELPVEACPFDRRLARRLAKARARVRAGL--VDESDFDEERQGRTAEELFDE 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949 163 LKTEKPEEE-LVFSHGDLGDSNIFVKDGKVSGFIDLGRSGRADKWYDIAFCVRSIREDIGEEQYVELFFDLLGI-KPDWE 240
Cdd:COG3231  175 LEARRPAVEdLVVTHGDACLPNFILDGWRFSGFIDLGRLGVADRHQDLALATWSLRFNLGGDVWDDPFLDAYGRgAIDPA 254
                        250
                 ....*....|..
gi 576290949 241 KIKYYILLDELF 252
Cdd:COG3231  255 RLAYYRLLDEFF 266
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
5-218 1.37e-30

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: 111.24  E-value: 1.37e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949   5 YRCVKDTEGMSpAKVYkLVGENENLYLKMTDSRYKgttYDVEREKDMMLWLEGK--LPVPKVLHFERHDGWSNLLMSEAD 82
Cdd:cd05120    1 ISVKLIKEGGD-NKVY-LLGDPREYVLKIGPPRLK---KDLEKEAAMLQLLAGKlsLPVPKVYGFGESDGWEYLLMERIE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949  83 GVLCSEEY--EDEQSPEKIIELYAECIRLFHSIDISdcpytnsldsrlaeldyllnndladvdcenweedtpfkdprely 160
Cdd:cd05120   76 GETLSEVWprLSEEEKEKIADQLAEILAALHRIDSS-------------------------------------------- 111
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 576290949 161 dflktekpeeelVFSHGDLGDSNIFVKD-GKVSGFIDLGRSGRADKWYDIAFCVRSIRE 218
Cdd:cd05120  112 ------------VLTHGDLHPGNILVKPdGKLSGIIDWEFAGYGPPAFDYAAALRDWTE 158
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
10-198 1.36e-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: 107.91  E-value: 1.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949  10 DTEGMsPAKVYKLVGE--NENLYLKMTDSRYKGTTYDVEREKDMMLWLEGK-LPVPKVLHFERHDGWSNLLMSEADGVLC 86
Cdd:cd13968    1 MGEGA-SAKVFWAEGEctTIGVAVKIGDDVNNEEGEDLESEMDILRRLKGLeLNIPKVLVTEDVDGPNILLMELVKGGTL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949  87 SE----EYEDEQSPEKIIELYAECIRLFHSIdisdcpytnsldsrlaeldyllnndladvdcenweedtpfkdprelydf 162
Cdd:cd13968   80 IAytqeEELDEKDVESIMYQLAECMRLLHSF------------------------------------------------- 110
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 576290949 163 lktekpeeelVFSHGDLGDSNIFVKDGKVSGFIDLG 198
Cdd:cd13968  111 ----------HLIHRDLNNDNILLSEDGNVKLIDFG 136
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
19-245 1.88e-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: 97.57  E-value: 1.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949   19 VYKLVGENENLYLKmtDSRYKGTTYDVEREKDMMLWL--EGKLPVPKVLHFER---HDGWSNLLMSEADGVLCsEEYEDE 93
Cdd:pfam01636  13 TYLVTTGDGRYVLR--LPPPGRAAEELRRELALLRHLaaAGVPPVPRVLAGCTdaeLLGLPFLLMEYLPGEVL-ARPLLP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949   94 QSPEKIIELYAECIRLFHSIDISDCPYTNSLDSRLAELDYLLNNDLADVDCENweEDTPFKDPRELYDFLKTEKP-EEEL 172
Cdd:pfam01636  90 EERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAAEL--LDRLEELEERLLAALLALLPaELPP 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 576290949  173 VFSHGDLGDSNIFV-KDGKVSGFIDLGRSGRADKWYDIAFCVRSIREDIGEEQYVELFFDLLgiKPDWEKIKYY 245
Cdd:pfam01636 168 VLVHGDLHPGNLLVdPGGRVSGVIDFEDAGLGDPAYDLAILLNSWGRELGAELLAAYLAAYG--AFGYARLREL 239
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function ...
13-210 2.92e-07

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


Pssm-ID: 225714 [Multi-domain]  Cd Length: 321  Bit Score: 50.51  E-value: 2.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949  13 GMSPAKVYkLVGENENLYLKM-TDSRYKGTTYDVERE-KDMMLWLEGKLPVPKVLHFE--RHDGWSNLLMSEADG-VLCS 87
Cdd:COG3173   36 GWSNDTFR-LGDTGQKYVLRKpPRGDPVESAHDEKREyRVIAALLDVDVPVPRAFGLCgeGYLGTPFYVMEWVEGeVVWS 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949  88 EEYEDEQSPEKIIELYAECIRLFHSIDISDCP-------YTNS-LDSRLAELDYLLNNDladvdcenwEEDTPFKDPREL 159
Cdd:COG3173  115 ALPPESLGRQFALDALADFLAELHSIDAAGLPdpgkpnaYRGRqLARWDDEYRRAKKEL---------GGRIPLADRLIK 185
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 576290949 160 YDFLKTEKPEEELVFSHGDLGDSNIFVKDGKVSGFIDLGRSGRADKWYDIA 210
Cdd:COG3173  186 WLEANRPPWAGPPVLVHGDYRPGNLIIDPGRPTGVLDWELATLGDPLEDLA 236
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
41-235 6.72e-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: 42.99  E-value: 6.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949  41 TTYDVEREKDMMLWLEGK-LPVPKVLHFE---RHDGWSNLLMSEADG-VLCSEEYEDEQSPEKIIELYAECIRLF---HS 112
Cdd:cd05154   41 SAHDLEREYRVLRALAGTgVPVPRVLALCedpSVLGAPFYVMERVDGrVLPDPLPRPDLSPEERRALARSLVDALaalHS 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576290949 113 IDISDCP---YTNSLDSRLAELDYLLnndladvdcENWEEDTPFKDP--RELYDFLKTEKPEE-ELVFSHGDLGDSN-IF 185
Cdd:cd05154  121 VDPAALGladLGRPEGYLERQVDRWR---------RQLEAAATDPPPalEEALRWLRANLPADgRPVLVHGDFRLGNlLF 191
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 576290949 186 VKDGKVSGFIDLGRSGRADKWYDIA-FCVRSIREdiGEEQYVELFFDLLGI 235
Cdd:cd05154  192 DPDGRVTAVLDWELATLGDPLEDLAwLLARWWRP--GDPPGLAAPTRLPGF 240
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
176-231 1.39e-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: 1.39e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 576290949 176 HGDLGDSNIFVKDGKVSGFIDLGRSGRADKWYDIA-FCVRSIREDIG--EEQYVELFFD 231
Cdd:cd05153  183 HADLFRDNVLFDGDRLSGIIDFYDACYDPLLYDLAiALNDWCFDDDGklDPERAKALLA 241
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
173-204 2.74e-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: 2.74e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 576290949 173 VFSHGDLGDSNIFVKDGKVSGFIDLGRSGRAD 204
Cdd:cd05155  164 VWLHGDLHPGNLLVRDGRLSAVIDFGDLGVGD 195
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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