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Conserved domains on  [gi|694154638|gb|AIS61209|]
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aminoglycoside phosphotransferase [Listeria ivanovii subsp. londoniensis]

Protein Classification

aminoglycoside phosphotransferase family protein( domain architecture ID 12025366)

aminoglycoside phosphotransferase family protein catalyzes the phosphorylation of small molecule substrates such as aminoglycoside antibiotics and N-acetylhexosamine, similar to Streptomyces vinaceus viomycin phosphotransferase

EC:  2.7.1.-
Gene Ontology:  GO:0005524|GO:0016310

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 14-230 1.16e-28

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: 109.90  E-value: 1.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638   14 VIKEIKKGFSiDQKYQV---DNSYLVRVFPENMWEERKM-EFEAIQKLSSL-APKVPRALDFGLL---QGKGYMVMDYLL 85
Cdd:pfam01636   1 TLRPISSGAS-NRTYLVttgDGRYVLRLPPPGRAAEELRrELALLRHLAAAgVPPVPRVLAGCTDaelLGLPFLLMEYLP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638   86 GEDAESGMVHLsnsEQFQAGVSAGAVLRKIHKMDINTTELNWYDFQKEKYYRKLSKLKKSNIEV---VFLQELESFIENN 162
Cdd:pfam01636  80 GEVLARPLLPE---ERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAAellDRLEELEERLLAA 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694154638  163 LD--LMKEREVRLQHGDFHPANIILN-NHQFAGIIDFNRLEFGDPLFDLAK-IGFFTTNSSIAFARGNILGY 230
Cdd:pfam01636 157 LLalLPAELPPVLVHGDLHPGNLLVDpGGRVSGVIDFEDAGLGDPAYDLAIlLNSWGRELGAELLAAYLAAY 228
 
Name Accession Description Interval E-value
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 14-230 1.16e-28

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: 109.90  E-value: 1.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638   14 VIKEIKKGFSiDQKYQV---DNSYLVRVFPENMWEERKM-EFEAIQKLSSL-APKVPRALDFGLL---QGKGYMVMDYLL 85
Cdd:pfam01636   1 TLRPISSGAS-NRTYLVttgDGRYVLRLPPPGRAAEELRrELALLRHLAAAgVPPVPRVLAGCTDaelLGLPFLLMEYLP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638   86 GEDAESGMVHLsnsEQFQAGVSAGAVLRKIHKMDINTTELNWYDFQKEKYYRKLSKLKKSNIEV---VFLQELESFIENN 162
Cdd:pfam01636  80 GEVLARPLLPE---ERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAAellDRLEELEERLLAA 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694154638  163 LD--LMKEREVRLQHGDFHPANIILN-NHQFAGIIDFNRLEFGDPLFDLAK-IGFFTTNSSIAFARGNILGY 230
Cdd:pfam01636 157 LLalLPAELPPVLVHGDLHPGNLLVDpGGRVSGVIDFEDAGLGDPAYDLAIlLNSWGRELGAELLAAYLAAY 228
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 15-259 2.61e-26

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 104.43  E-value: 2.61e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638  15 IKEIKKGFSiDQKYQVD--NSYLVRVFPENMWEERKM--EFEAIQKLSSLAP-KVPRALDFG---LLQGKGYMVMDYLLG 86
Cdd:COG3173   25 VEPLSGGWS-NLTYRLDtgDRLVLRRPPRGLASAHDVrrEARVLRALAPRLGvPVPRPLALGedgEVIGAPFYVMEWVEG 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638  87 EDAESGMVHLSNSEQFQAGVSAGAVLRKIHKMDINTTELNWY-----DFQKEKYYRKL-SKLKKSNIEVVFLQELESFIE 160
Cdd:COG3173  104 ETLEDALPDLSPAERRALARALGEFLAALHAVDPAAAGLADGrpeglERQLARWRAQLrRALARTDDLPALRERLAAWLA 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638 161 NNLDLmkEREVRLQHGDFHPANIIL--NNHQFAGIIDFNRLEFGDPLFDLAKIGFFTTNSSIAFARGNIL--GYIGKEDI 236
Cdd:COG3173  184 ANLPE--WGPPVLVHGDLRPGNLLVdpDDGRLTAVIDWELATLGDPAADLAYLLLYWRLPDDLLGPRAAFlaAYEEATGD 261

                        250       260
                 ....*....|....*....|...
gi 694154638 237 TDFWKLYALYTAMHIVFALSWAS 259
Cdd:COG3173  262 LDDLTWWALADPELAALGRRALE 284
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 15-216 1.21e-18

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: 80.81  E-value: 1.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638  15 IKEIKKGFSiDQKYQV--DNSYLVRVFPENMWEERKMEFEAIQKLSS-LAPKVPRALDFGLLQGKGYMVMDYLLGEDAES 91
Cdd:cd05120    3 VKLIKEGGD-NKVYLLgdPREYVLKIGPPRLKKDLEKEAAMLQLLAGkLSLPVPKVYGFGESDGWEYLLMERIEGETLSE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638  92 GMVHLSNSEQFQAGVSAGAVLRKIHKMDInttelnwydfqkekyyrklsklkksnieVVFLqelesfiennldlmkerev 171
Cdd:cd05120   82 VWPRLSEEEKEKIADQLAEILAALHRIDS----------------------------SVLT------------------- 114

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 694154638 172 rlqHGDFHPANIILNNH-QFAGIIDFNRLEFGDPLFDLAKIGFFTT 216
Cdd:cd05120  115 ---HGDLHPGNILVKPDgKLSGIIDWEFAGYGPPAFDYAAALRDWT 157
 
Name Accession Description Interval E-value
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 14-230 1.16e-28

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: 109.90  E-value: 1.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638   14 VIKEIKKGFSiDQKYQV---DNSYLVRVFPENMWEERKM-EFEAIQKLSSL-APKVPRALDFGLL---QGKGYMVMDYLL 85
Cdd:pfam01636   1 TLRPISSGAS-NRTYLVttgDGRYVLRLPPPGRAAEELRrELALLRHLAAAgVPPVPRVLAGCTDaelLGLPFLLMEYLP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638   86 GEDAESGMVHLsnsEQFQAGVSAGAVLRKIHKMDINTTELNWYDFQKEKYYRKLSKLKKSNIEV---VFLQELESFIENN 162
Cdd:pfam01636  80 GEVLARPLLPE---ERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAAellDRLEELEERLLAA 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694154638  163 LD--LMKEREVRLQHGDFHPANIILN-NHQFAGIIDFNRLEFGDPLFDLAK-IGFFTTNSSIAFARGNILGY 230
Cdd:pfam01636 157 LLalLPAELPPVLVHGDLHPGNLLVDpGGRVSGVIDFEDAGLGDPAYDLAIlLNSWGRELGAELLAAYLAAY 228
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 15-259 2.61e-26

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 104.43  E-value: 2.61e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638  15 IKEIKKGFSiDQKYQVD--NSYLVRVFPENMWEERKM--EFEAIQKLSSLAP-KVPRALDFG---LLQGKGYMVMDYLLG 86
Cdd:COG3173   25 VEPLSGGWS-NLTYRLDtgDRLVLRRPPRGLASAHDVrrEARVLRALAPRLGvPVPRPLALGedgEVIGAPFYVMEWVEG 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638  87 EDAESGMVHLSNSEQFQAGVSAGAVLRKIHKMDINTTELNWY-----DFQKEKYYRKL-SKLKKSNIEVVFLQELESFIE 160
Cdd:COG3173  104 ETLEDALPDLSPAERRALARALGEFLAALHAVDPAAAGLADGrpeglERQLARWRAQLrRALARTDDLPALRERLAAWLA 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638 161 NNLDLmkEREVRLQHGDFHPANIIL--NNHQFAGIIDFNRLEFGDPLFDLAKIGFFTTNSSIAFARGNIL--GYIGKEDI 236
Cdd:COG3173  184 ANLPE--WGPPVLVHGDLRPGNLLVdpDDGRLTAVIDWELATLGDPAADLAYLLLYWRLPDDLLGPRAAFlaAYEEATGD 261

                        250       260
                 ....*....|....*....|...
gi 694154638 237 TDFWKLYALYTAMHIVFALSWAS 259
Cdd:COG3173  262 LDDLTWWALADPELAALGRRALE 284
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 15-216 1.21e-18

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: 80.81  E-value: 1.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638  15 IKEIKKGFSiDQKYQV--DNSYLVRVFPENMWEERKMEFEAIQKLSS-LAPKVPRALDFGLLQGKGYMVMDYLLGEDAES 91
Cdd:cd05120    3 VKLIKEGGD-NKVYLLgdPREYVLKIGPPRLKKDLEKEAAMLQLLAGkLSLPVPKVYGFGESDGWEYLLMERIEGETLSE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638  92 GMVHLSNSEQFQAGVSAGAVLRKIHKMDInttelnwydfqkekyyrklsklkksnieVVFLqelesfiennldlmkerev 171
Cdd:cd05120   82 VWPRLSEEEKEKIADQLAEILAALHRIDS----------------------------SVLT------------------- 114

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 694154638 172 rlqHGDFHPANIILNNH-QFAGIIDFNRLEFGDPLFDLAKIGFFTT 216
Cdd:cd05120  115 ---HGDLHPGNILVKPDgKLSGIIDWEFAGYGPPAFDYAAALRDWT 157
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
 23-209 2.24e-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: 63.02  E-value: 2.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638  23 SIDQKYQVD----NSYLVRVFPENMW--EERKMEFEAIQKLSSLAPKVPRAL------DFGLLQGKGYMVMDYLLGEdae 90
Cdd:COG2334   24 GENRNYRVEtedgRRYVLKLYRPGRWspEEIPFELALLAHLAAAGLPVPAPVptrdgeTLLELEGRPAALFPFLPGR--- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638  91 sgMVHLSNSEQFQAgvsAGAVLRKIHKM-----DINTTELNWYDFQKEKYYRKLskLKKSNIEVVFLQELEsFIENNLDL 165
Cdd:COG2334  101 --SPEEPSPEQLEE---LGRLLARLHRAladfpRPNARDLAWWDELLERLLGPL--LPDPEDRALLEELLD-RLEARLAP 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 694154638 166 MKEREVRLQ-HGDFHPANIILNNHQFAGIIDFNRLEFGDPLFDLA 209
Cdd:COG2334  173 LLGALPRGViHGDLHPDNVLFDGDGVSGLIDFDDAGYGPRLYDLA 217
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
 50-209 2.85e-09

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: 56.47  E-value: 2.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638  50 EFEAIQKLSSLAPKVPRALDFG----LLqGKGYMVMDYLLGEDAESGMVH--LSNSEQFQAGVSAGAVLRKIHKMDINTT 123
Cdd:cd05154   48 EYRVLRALAGTGVPVPRVLALCedpsVL-GAPFYVMERVDGRVLPDPLPRpdLSPEERRALARSLVDALAALHSVDPAAL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638 124 EL-------NWYDFQKEKYYRKLSKLKKSNIEVvfLQELESFIENNLDlmKEREVRLQHGDFHPANIILNNH-QFAGIID 195
Cdd:cd05154  127 GLadlgrpeGYLERQVDRWRRQLEAAATDPPPA--LEEALRWLRANLP--ADGRPVLVHGDFRLGNLLFDPDgRVTAVLD 202

                        170
                 ....*....|....*..
gi 694154638 196 FnrlEF---GDPLFDLA 209
Cdd:cd05154  203 W---ELatlGDPLEDLA 216
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
 31-209 2.48e-08

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: 54.19  E-value: 2.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638  31 DNSYLVRVFpENMWEERKMEFEA--IQKLSSLAPKVPRAL------DFGLLQGKGYMVMDYLLGEDAESgmvhlSNSEQF 102
Cdd:cd05153   37 DGRYVLTLF-EKRRSAAELPFELelLDHLAQAGLPVPRPLadkdgeLLGELNGKPAALFPFLPGESLTT-----PTPEQC 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638 103 QAgvsAGAVLRKIHK--MDINTTELNWYDFQKEKYYRKLSKLKKSNIEVVFLQELESFIEnnlDLMKEREVRLQ----HG 176
Cdd:cd05153  111 RA---IGAALARLHLalAGFPPPRPNPRGLAWWKPLAERLKARLDLLAADDRALLEDELA---RLQALAPSDLPrgviHA 184

                        170       180       190
                 ....*....|....*....|....*....|...
gi 694154638 177 DFHPANIILNNHQFAGIIDFNRLEFGDPLFDLA 209
Cdd:cd05153  185 DLFRDNVLFDGDRLSGIIDFYDACYDPLLYDLA 217
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
 34-209 1.36e-07

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: 51.47  E-value: 1.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638  34 YLVRvFPENMWEERKMEFEAiQKLSSLAPKVPRALDFGLLQGK---GY----MVMDYLLGEDAEsgmvHLSNSEQFQAGV 106
Cdd:cd05155   21 LAVR-LPRRAWAAELLEKEQ-RWLPRLAPRLPLPVPVPLALGKpgaGYpwpwSVYRWLEGETAA----DAPLADPAAAAE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638 107 SAGAVLRKIHKMDI----NTTELNWYDFQKEKYYRKLSKLKKS--NIEVVFLQEL-ESFIENNLDlmkEREVRLQHGDFH 179
Cdd:cd05155   95 DLARFLAALHAIDPagppNPGRGNPLRGRDLAVRDAEEALAALagLLDVAAARALwERALAAPAW---AGPPVWLHGDLH 171

                        170       180       190
                 ....*....|....*....|....*....|
gi 694154638 180 PANIILNNHQFAGIIDFNRLEFGDPLFDLA 209
Cdd:cd05155  172 PGNLLVRDGRLSAVIDFGDLGVGDPACDLA 201
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
 31-209 5.05e-06

Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic choline kinases, as well as eukaryotic ethanolamine kinase. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. Bacterial ChoK is also referred to as licA protein. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK 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: 270700 [Multi-domain]  Cd Length: 152  Bit Score: 45.62  E-value: 5.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638  31 DNSYLVRVF---PENMwEERKMEFEAIQKLS--SLAPKVpraldFGLLQGKGYMVMDYLlgEDAESGMVHLSNSEQFQAg 105
Cdd:cd05151   21 GKKYVLRIPgagTELL-IDRENEKANSKAAAelGIAPEV-----IYFDPETGVKITEFI--EGATLLTNDFSDPENLER- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638 106 vsAGAVLRKIHKMDInttelnwydfqkekyyrklsklkksnievvflqelesfiennldlmkeREVRLQHGDFHPANIIL 185
Cdd:cd05151   92 --IAALLRKLHSSPL------------------------------------------------EDLVLCHNDLVPGNFLL 121

                        170       180
                 ....*....|....*....|....*..
gi 694154638 186 NNHQFaGIIDFnrlE---FGDPLFDLA 209
Cdd:cd05151  122 DDDRL-YLIDW---EyagMNDPLFDLA 144
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
175-258 3.67e-05

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 43.23  E-value: 3.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638 175 HGDFHPANIILNNHQFAGIIDFNRLEFGDPLFDLAKIG---FFTTNSSIAFARgnilGYIGKEDITDFWKLYALYTAMHI 251
Cdd:COG0510   53 HGDLHPGNFLVTDDGRLYLIDWEYAGLGDPAFDLAALLveyGLSPEQAEELLE----AYGFGRPTEELLRRLRAYRALAD 128


                 ....*..
gi 694154638 252 VFALSWA 258
Cdd:COG0510  129 LLWALWA 135
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
 50-209 2.13e-04

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: 41.80  E-value: 2.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638  50 EFEAIQKLSSLAPkVPRALDFGLLQGKGYMVMDYLLGEDAesgmVHLSNSEQFQAGVSA-GAVLRKIHkmdinttELNW- 127
Cdd:cd05150   41 EAERLRWLAGKLP-VPEVLDYGSDDGGDWLLTTALPGRDA----ASLEPLLDPERLVDLlAEALRALH-------SLPIa 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694154638 128 ---YDFQKEKYYRKLSKLKKSNIEVV--FL--------QELESFIENNLDLmKEREVrLQHGDFHPANIILNNHQFAGII 194
Cdd:cd05150  109 dcpFDRRLDARLAEARARVEAGLVDEddFDeerqgrtaEELLAELEATRPA-EEDLV-VTHGDACLPNIILDPGRFSGFI 186

                        170
                 ....*....|....*
gi 694154638 195 DFNRLEFGDPLFDLA 209
Cdd:cd05150  187 DLGRLGVADRYQDLA 201
 
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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