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Conserved domains on  [gi|1028083029|ref|WP_063842185|]
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aminoglycoside O-phosphotransferase APH(7'')-Ia [Streptomyces hygroscopicus]

Protein Classification

phosphotransferase family protein( domain architecture ID 10007008)

phosphotransferase family protein may catalyze the phosphorylation of aminoglycosides and confer aminoglycoside antibiotic resistance

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 29-251 3.65e-23

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


:

Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 97.11  E-value: 3.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029  29 EPLARRALEELGlPVPPVLRVPGESTNPV-LVGEPDP-VIKLFGEHWCGPESLASESEAYAVLAD-APVPVPRLLGRGEl 105
Cdd:COG3173     9 RALLAAQLPGLA-GLPEVEPLSGGWSNLTyRLDTGDRlVLRRPPRGLASAHDVRREARVLRALAPrLGVPVPRPLALGE- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029 106 rpGTGAWPWPYLVMSRMTGTTWRSAMDGTTDRnALLALARELGRVLGRLHRVPLTGNTVLTPHSEVFPELLReRRAATVE 185
Cdd:COG3173    87 --DGEVIGAPFYVMEWVEGETLEDALPDLSPA-ERRALARALGEFLAALHAVDPAAAGLADGRPEGLERQLA-RWRAQLR 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1028083029 186 DHRGWGYLSPRLLDRLEDWLPDVDTllAGREPRFVHGDLHGTNIFVDLAATEVTGIVDFTDVYAGD 251
Cdd:COG3173   163 RALARTDDLPALRERLAAWLAANLP--EWGPPVLVHGDLRPGNLLVDPDDGRLTAVIDWELATLGD 226
 
Name Accession Description Interval E-value
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 29-251 3.65e-23

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 97.11  E-value: 3.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029  29 EPLARRALEELGlPVPPVLRVPGESTNPV-LVGEPDP-VIKLFGEHWCGPESLASESEAYAVLAD-APVPVPRLLGRGEl 105
Cdd:COG3173     9 RALLAAQLPGLA-GLPEVEPLSGGWSNLTyRLDTGDRlVLRRPPRGLASAHDVRREARVLRALAPrLGVPVPRPLALGE- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029 106 rpGTGAWPWPYLVMSRMTGTTWRSAMDGTTDRnALLALARELGRVLGRLHRVPLTGNTVLTPHSEVFPELLReRRAATVE 185
Cdd:COG3173    87 --DGEVIGAPFYVMEWVEGETLEDALPDLSPA-ERRALARALGEFLAALHAVDPAAAGLADGRPEGLERQLA-RWRAQLR 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1028083029 186 DHRGWGYLSPRLLDRLEDWLPDVDTllAGREPRFVHGDLHGTNIFVDLAATEVTGIVDFTDVYAGD 251
Cdd:COG3173   163 RALARTDDLPALRERLAAWLAANLP--EWGPPVLVHGDLRPGNLLVDPDDGRLTAVIDWELATLGD 226
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 76-290 7.81e-20

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: 86.79  E-value: 7.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029  76 PESLASESEAYAVLADA-PVPVPRLLGRGELRPGTGawpWPYLVMSRMTGTTWRSAMDgttdRNALLALARELGRVLGRL 154
Cdd:pfam01636  34 AEELRRELALLRHLAAAgVPPVPRVLAGCTDAELLG---LPFLLMEYLPGEVLARPLL----PEERGALLEALGRALARL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029 155 HRVPLTGNTVLTPHSEVFPELLRERRAATVEDHRGWGYLSPRLLDRLEDWLPdvDTLLAGREPRFVHGDLHGTNIFVDlA 234
Cdd:pfam01636 107 HAVDPAALPLAGRLARLLELLRQLEAALARLLAAELLDRLEELEERLLAALL--ALLPAELPPVLVHGDLHPGNLLVD-P 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1028083029 235 ATEVTGIVDFTDVYAGDSRYSLVQLHLNAFRGDREILAALLDGAQWKRTEDFAREL 290
Cdd:pfam01636 184 GGRVSGVIDFEDAGLGDPAYDLAILLNSWGRELGAELLAAYLAAYGAFGYARLREL 239
MPH2' cd05152
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ...
 142-276 4.98e-12

Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group from ATP to the 2'-hydroxyl of macrolide antibiotics such as erythromycin, clarithromycin, and azithromycin, among others. Macrolides penetrate the bacterial cell and bind to ribosomes, where it interrupts protein elongation, leading ultimately to the demise of the bacterium. Phosphorylation of macrolides leads to their inactivation. Based on substrate specificity and amino acid sequence, MPH2' is divided into types I and II, encoded by mphA and mphB genes, respectively. MPH2'I inactivates 14-membered ring macrolides while MPH2'II inactivates both 14- and 16-membered ring macrolides. Enzymatic inactivation of macrolides has been reported as a mechanism for bacterial resistance in clinical samples. MPH2' is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270701 [Multi-domain]  Cd Length: 276  Bit Score: 65.34  E-value: 4.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029 142 ALARELGRVLGRLHRVPL-----TGNTVLTPhsevfpELLRERRAATVEDHRGWGYLSPRLLDRLEDWLPDvDTLLAGRe 216
Cdd:cd05152   113 VFARSLGKALAALHSIPAdlaaaAGLPVYTA------EEVRARMAARMDRVKETFGVPPALLARWQAWLAD-DSLWPFH- 184

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029 217 PRFVHGDLHGTNIFVDlAATEVTGIVDFTDVYAGDSRYSLVqLHLNAFrgDREILAALLD 276
Cdd:cd05152   185 TVLVHGDLHPGHILVD-EDGRVTGLIDWTEAKVGDPADDFA-WHYAAF--GEEALERLLD 240
 
Name Accession Description Interval E-value
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 29-251 3.65e-23

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 97.11  E-value: 3.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029  29 EPLARRALEELGlPVPPVLRVPGESTNPV-LVGEPDP-VIKLFGEHWCGPESLASESEAYAVLAD-APVPVPRLLGRGEl 105
Cdd:COG3173     9 RALLAAQLPGLA-GLPEVEPLSGGWSNLTyRLDTGDRlVLRRPPRGLASAHDVRREARVLRALAPrLGVPVPRPLALGE- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029 106 rpGTGAWPWPYLVMSRMTGTTWRSAMDGTTDRnALLALARELGRVLGRLHRVPLTGNTVLTPHSEVFPELLReRRAATVE 185
Cdd:COG3173    87 --DGEVIGAPFYVMEWVEGETLEDALPDLSPA-ERRALARALGEFLAALHAVDPAAAGLADGRPEGLERQLA-RWRAQLR 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1028083029 186 DHRGWGYLSPRLLDRLEDWLPDVDTllAGREPRFVHGDLHGTNIFVDLAATEVTGIVDFTDVYAGD 251
Cdd:COG3173   163 RALARTDDLPALRERLAAWLAANLP--EWGPPVLVHGDLRPGNLLVDPDDGRLTAVIDWELATLGD 226
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 76-290 7.81e-20

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: 86.79  E-value: 7.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029  76 PESLASESEAYAVLADA-PVPVPRLLGRGELRPGTGawpWPYLVMSRMTGTTWRSAMDgttdRNALLALARELGRVLGRL 154
Cdd:pfam01636  34 AEELRRELALLRHLAAAgVPPVPRVLAGCTDAELLG---LPFLLMEYLPGEVLARPLL----PEERGALLEALGRALARL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029 155 HRVPLTGNTVLTPHSEVFPELLRERRAATVEDHRGWGYLSPRLLDRLEDWLPdvDTLLAGREPRFVHGDLHGTNIFVDlA 234
Cdd:pfam01636 107 HAVDPAALPLAGRLARLLELLRQLEAALARLLAAELLDRLEELEERLLAALL--ALLPAELPPVLVHGDLHPGNLLVD-P 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1028083029 235 ATEVTGIVDFTDVYAGDSRYSLVQLHLNAFRGDREILAALLDGAQWKRTEDFAREL 290
Cdd:pfam01636 184 GGRVSGVIDFEDAGLGDPAYDLAILLNSWGRELGAELLAAYLAAYGAFGYARLREL 239
MPH2' cd05152
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ...
 142-276 4.98e-12

Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group from ATP to the 2'-hydroxyl of macrolide antibiotics such as erythromycin, clarithromycin, and azithromycin, among others. Macrolides penetrate the bacterial cell and bind to ribosomes, where it interrupts protein elongation, leading ultimately to the demise of the bacterium. Phosphorylation of macrolides leads to their inactivation. Based on substrate specificity and amino acid sequence, MPH2' is divided into types I and II, encoded by mphA and mphB genes, respectively. MPH2'I inactivates 14-membered ring macrolides while MPH2'II inactivates both 14- and 16-membered ring macrolides. Enzymatic inactivation of macrolides has been reported as a mechanism for bacterial resistance in clinical samples. MPH2' is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270701 [Multi-domain]  Cd Length: 276  Bit Score: 65.34  E-value: 4.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029 142 ALARELGRVLGRLHRVPL-----TGNTVLTPhsevfpELLRERRAATVEDHRGWGYLSPRLLDRLEDWLPDvDTLLAGRe 216
Cdd:cd05152   113 VFARSLGKALAALHSIPAdlaaaAGLPVYTA------EEVRARMAARMDRVKETFGVPPALLARWQAWLAD-DSLWPFH- 184

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029 217 PRFVHGDLHGTNIFVDlAATEVTGIVDFTDVYAGDSRYSLVqLHLNAFrgDREILAALLD 276
Cdd:cd05152   185 TVLVHGDLHPGHILVD-EDGRVTGLIDWTEAKVGDPADDFA-WHYAAF--GEEALERLLD 240
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
 75-243 3.71e-11

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: 62.25  E-value: 3.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029  75 GPESLASESEAYAVLADAPVPVPRLLGRGELRPGTGAwpwPYLVMSRMTGTTWRSAMDGT-TDRNALLALARELGRVLGR 153
Cdd:cd05154    41 SAHDLEREYRVLRALAGTGVPVPRVLALCEDPSVLGA---PFYVMERVDGRVLPDPLPRPdLSPEERRALARSLVDALAA 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029 154 LHRVPLTGNTVLT-PHSEVFPELLRERRAATVEDHRGWGylsPRLLDRLEDWLPdvDTLLAGREPRFVHGDLHGTNIFVD 232
Cdd:cd05154   118 LHSVDPAALGLADlGRPEGYLERQVDRWRRQLEAAATDP---PPALEEALRWLR--ANLPADGRPVLVHGDFRLGNLLFD 192

                         170
                  ....*....|.
gi 1028083029 233 lAATEVTGIVD 243
Cdd:cd05154   193 -PDGRVTAVLD 202
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
 31-277 9.92e-11

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: 61.48  E-value: 9.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029  31 LARRALEELGLPVPPVLRVPGESTNPV-LVGEPDP---VIKLFGEHWCGPESLASESEAYAVLADAPVPVPRLL----GR 102
Cdd:COG2334     2 ELAAALERYGLGPLSSLKPLNSGENRNyRVETEDGrryVLKLYRPGRWSPEEIPFELALLAHLAAAGLPVPAPVptrdGE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029 103 GELRPGtgawPWPYLVMSRMTGTTWRSAmdgttdrnaLLALARELGRVLGRLHRVpltGNTVLTPHSEVFPELLRERRAA 182
Cdd:COG2334    82 TLLELE----GRPAALFPFLPGRSPEEP---------SPEQLEELGRLLARLHRA---LADFPRPNARDLAWWDELLERL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029 183 TVEDhrgwgYLSPRLLDRLEDWLPDVDTLLAGREPRF----VHGDLHGTNIFVDlaATEVTGIVDFtdvyaGDSRYSLVQ 258
Cdd:COG2334   146 LGPL-----LPDPEDRALLEELLDRLEARLAPLLGALprgvIHGDLHPDNVLFD--GDGVSGLIDF-----DDAGYGPRL 213

                         250       260
                  ....*....|....*....|....*.
gi 1028083029 259 L-------HLNAFRGDREILAALLDG 277
Cdd:COG2334   214 YdlaialnGWADGPLDPARLAALLEG 239
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
 77-251 6.16e-10

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: 58.40  E-value: 6.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029  77 ESLASESEAYAVLADA-PVPVPRLLGRGelRPGTGaWPWPYLVMSRMTGTTWRSAMDgtTDRNALlalARELGRVLGRLH 155
Cdd:cd05155    33 ELLEKEQRWLPRLAPRlPLPVPVPLALG--KPGAG-YPWPWSVYRWLEGETAADAPL--ADPAAA---AEDLARFLAALH 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029 156 RVPLTGNTVltPHSEVFpelLRERRAATvedhrgwgYLSPRLLDRLEDwLPDVDTLLA-----------GREPRFVHGDL 224
Cdd:cd05155   105 AIDPAGPPN--PGRGNP---LRGRDLAV--------RDAEEALAALAG-LLDVAAARAlweralaapawAGPPVWLHGDL 170

                         170       180
                  ....*....|....*....|....*..
gi 1028083029 225 HGTNIFVDlaATEVTGIVDFTDVYAGD 251
Cdd:cd05155   171 HPGNLLVR--DGRLSAVIDFGDLGVGD 195
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
 65-322 5.41e-09

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: 56.50  E-value: 5.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029  65 VIKLFgEHWCGPESLASESEAYAVLADAPVPVPRLLGRGE---LRPGTGAwpwPYLVMSRMTGTTWRSAMDgttdrnall 141
Cdd:cd05153    41 VLTLF-EKRRSAAELPFELELLDHLAQAGLPVPRPLADKDgelLGELNGK---PAALFPFLPGESLTTPTP--------- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029 142 ALARELGRVLGRLHrvpLTGNTVLTPHSEVFPELLRERRAATVEDHrgWGYLSPRLLDRLEDWLPDVDTLLAGREPR-FV 220
Cdd:cd05153   108 EQCRAIGAALARLH---LALAGFPPPRPNPRGLAWWKPLAERLKAR--LDLLAADDRALLEDELARLQALAPSDLPRgVI 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029 221 HGDLHGTNIFVDlaATEVTGIVDFTDVYAGDSRYSL-----VQLHLNAFRGDREILAALLDGAQWKR--TE------DFA 287
Cdd:cd05153   183 HADLFRDNVLFD--GDRLSGIIDFYDACYDPLLYDLaialnDWCFDDDGKLDPERAKALLAGYQSVRplTEeekaalPLL 260

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1028083029 288 RELLAFTF----LHDFEVFEETplDLSGFTDPEELAQFL 322
Cdd:cd05153   261 LRAAALRFwlsrLYDFHLPREG--ALVTPKDPDEFLRRL 297
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 57-251 1.25e-08

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: 53.46  E-value: 1.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029  57 VLVGEPDPVI-KLFGEHwcGPESLASESEAYAVLA-DAPVPVPRLLGRGELRPgtgawpWPYLVMSRMTGTTWRSAMDgT 134
Cdd:cd05120    15 YLLGDPREYVlKIGPPR--LKKDLEKEAAMLQLLAgKLSLPVPKVYGFGESDG------WEYLLMERIEGETLSEVWP-R 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029 135 TDRNALLALARELGRVLGRLHRVPLTGntvltphsevfpellrerraatvedhrgwgylsprlldrledwlpdvdtllag 214
Cdd:cd05120    86 LSEEEKEKIADQLAEILAALHRIDSSV----------------------------------------------------- 112

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1028083029 215 reprFVHGDLHGTNIFVDLAAtEVTGIVDFTDVYAGD 251
Cdd:cd05120   113 ----LTHGDLHPGNILVKPDG-KLSGIIDWEFAGYGP 144
FN3K COG3001
Fructosamine-3-kinase [Carbohydrate transport and metabolism];
75-251 8.12e-06

Fructosamine-3-kinase [Carbohydrate transport and metabolism];


Pssm-ID: 442239 [Multi-domain]  Cd Length: 287  Bit Score: 46.73  E-value: 8.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029  75 GPESLASESEAYAVLADA-PVPVPRLLGRGELRPGtgawpwPYLVMSRMtgttwrsAMDGTTDRNAllalaRELGRVLGR 153
Cdd:COG3001    50 PLGMFEAEAAGLRALAATgTIRVPEVIGVGTTGDH------AFLVLEYL-------ELGPPTAGAW-----ERLGRQLAA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028083029 154 LHRVP----------LTGNTVL--TPHSEvFPELLRERR-AATVEDHRGWGYLSPRLLDRLEDWLPDVDTLLAGREPR-- 218
Cdd:COG3001   112 LHQATaprfgwdrdnFIGSTPQpnTWTDD-WAEFFAEQRlGPQLQLAAEKGLLFAADRERIERLVERLPELLAPHEPQps 190

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1028083029 219 FVHGDLHGTNIFVDlaATEVTGIVDfTDVYAGD 251
Cdd:COG3001   191 LLHGDLWSGNVLFT--ADGEPVLID-PAVYYGD 220
 
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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