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Conserved domains on  [gi|503669357|ref|WP_013903433|]
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MULTISPECIES: aminoglycoside phosphotransferase family protein [Streptococcus]

Protein Classification

aminoglycoside phosphotransferase family protein( domain architecture ID 12025366)

aminoglycoside phosphotransferase family protein may catalyze the phosphorylation of small molecules such as aminoglycosides and confer aminoglycoside antibiotic resistance; similar to Streptomyces coelicolor 3-hydroxyasparagine phosphotransferase

CATH:  3.90.1200.10|3.30.200.20
EC:  2.7.1.-
Gene Ontology:  GO:0005524|GO:0016310|GO:0016301
PubMed:  15888308|16244704|15888308

Graphical summary

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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 ...
 8-226 5.11e-26

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: 102.58  E-value: 5.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503669357    8 AINKGWSDDKKYCVTDQkqQKYFLRV-SDKEKLDSKKFEFDMMEKVASLGV-PMCKPISIELCDD---KVHSFHEWIDGK 82
Cdd:pfam01636   4 PISSGASNRTYLVTTGD--GRYVLRLpPPGRAAEELRRELALLRHLAAAGVpPVPRVLAGCTDAEllgLPFLLMEYLPGE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503669357   83 DARETILTvskEQQYIYGVEAGRILQKIHSLPVTEVREDWEVFYNRKIDDKIKKYKECPVQYENG-------QIFIDYLN 155
Cdd:pfam01636  82 VLARPLLP---EERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAAELLdrleeleERLLAALL 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503669357  156 ANreLLKDRPQVFQHGDYHIGNFMIGEDRKI-YVIDFDRFDLGDPWEEFNRIV--WSAQVSPSFASGMIDGYFD 226
Cdd:pfam01636 159 AL--LPAELPPVLVHGDLHPGNLLVDPGGRVsGVIDFEDAGLGDPAYDLAILLnsWGRELGAELLAAYLAAYGA 230
 
Name Accession Description Interval E-value
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 8-226 5.11e-26

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: 102.58  E-value: 5.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503669357    8 AINKGWSDDKKYCVTDQkqQKYFLRV-SDKEKLDSKKFEFDMMEKVASLGV-PMCKPISIELCDD---KVHSFHEWIDGK 82
Cdd:pfam01636   4 PISSGASNRTYLVTTGD--GRYVLRLpPPGRAAEELRRELALLRHLAAAGVpPVPRVLAGCTDAEllgLPFLLMEYLPGE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503669357   83 DARETILTvskEQQYIYGVEAGRILQKIHSLPVTEVREDWEVFYNRKIDDKIKKYKECPVQYENG-------QIFIDYLN 155
Cdd:pfam01636  82 VLARPLLP---EERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAAELLdrleeleERLLAALL 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503669357  156 ANreLLKDRPQVFQHGDYHIGNFMIGEDRKI-YVIDFDRFDLGDPWEEFNRIV--WSAQVSPSFASGMIDGYFD 226
Cdd:pfam01636 159 AL--LPAELPPVLVHGDLHPGNLLVDPGGRVsGVIDFEDAGLGDPAYDLAILLnsWGRELGAELLAAYLAAYGA 230
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 9-234 1.70e-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: 1.70e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503669357   9 INKGWSDDKkYCVTDQkqQKYFLRVSDK--EKLDSKKFEFDMMEKVAS-LGVPMCKPISieLCDDKVH-----SFHEWID 80
Cdd:COG3173   28 LSGGWSNLT-YRLDTG--DRLVLRRPPRglASAHDVRREARVLRALAPrLGVPVPRPLA--LGEDGEVigapfYVMEWVE 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503669357  81 GKDARETILTVSKEQQYIYGVEAGRILQKIHSLPVTEVR-------------EDWEVFYNRkiddKIKKYKECPVQYEng 147
Cdd:COG3173  103 GETLEDALPDLSPAERRALARALGEFLAALHAVDPAAAGladgrpeglerqlARWRAQLRR----ALARTDDLPALRE-- 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503669357 148 qIFIDYLNANRELlkDRPQVFQHGDYHIGNFMIGED--RKIYVIDFDRFDLGDPWEEFNRIVWSAQVSPSFASG---MID 222
Cdd:COG3173  177 -RLAAWLAANLPE--WGPPVLVHGDLRPGNLLVDPDdgRLTAVIDWELATLGDPAADLAYLLLYWRLPDDLLGPraaFLA 253

                        250
                 ....*....|....
gi 503669357 223 GYFD--GKVPDLFW 234
Cdd:COG3173  254 AYEEatGDLDDLTW 267
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 11-203 2.92e-06

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: 46.14  E-value: 2.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503669357  11 KGWSDDKKYCVTDQkqQKYFLRVSDKEKLDSKKFEFDMMEKVAS-LGVPMCKPISIELCDDKVHSFHEWIDGKDARETIL 89
Cdd:cd05120    7 KEGGDNKVYLLGDP--REYVLKIGPPRLKKDLEKEAAMLQLLAGkLSLPVPKVYGFGESDGWEYLLMERIEGETLSEVWP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503669357  90 TVSKEQQYIYGVEAGRILQKIHSLPVTevredwevfynrkiddkikkykecpvqyengqifidylnanrellkdrpqVFQ 169
Cdd:cd05120   85 RLSEEEKEKIADQLAEILAALHRIDSS--------------------------------------------------VLT 114

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 503669357 170 HGDYHIGNFMI-GEDRKIYVIDFDRFDLGDPWEEF 203
Cdd:cd05120  115 HGDLHPGNILVkPDGKLSGIIDWEFAGYGPPAFDY 149
 
Name Accession Description Interval E-value
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 8-226 5.11e-26

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: 102.58  E-value: 5.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503669357    8 AINKGWSDDKKYCVTDQkqQKYFLRV-SDKEKLDSKKFEFDMMEKVASLGV-PMCKPISIELCDD---KVHSFHEWIDGK 82
Cdd:pfam01636   4 PISSGASNRTYLVTTGD--GRYVLRLpPPGRAAEELRRELALLRHLAAAGVpPVPRVLAGCTDAEllgLPFLLMEYLPGE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503669357   83 DARETILTvskEQQYIYGVEAGRILQKIHSLPVTEVREDWEVFYNRKIDDKIKKYKECPVQYENG-------QIFIDYLN 155
Cdd:pfam01636  82 VLARPLLP---EERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAAELLdrleeleERLLAALL 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503669357  156 ANreLLKDRPQVFQHGDYHIGNFMIGEDRKI-YVIDFDRFDLGDPWEEFNRIV--WSAQVSPSFASGMIDGYFD 226
Cdd:pfam01636 159 AL--LPAELPPVLVHGDLHPGNLLVDPGGRVsGVIDFEDAGLGDPAYDLAILLnsWGRELGAELLAAYLAAYGA 230
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 9-234 1.70e-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: 1.70e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503669357   9 INKGWSDDKkYCVTDQkqQKYFLRVSDK--EKLDSKKFEFDMMEKVAS-LGVPMCKPISieLCDDKVH-----SFHEWID 80
Cdd:COG3173   28 LSGGWSNLT-YRLDTG--DRLVLRRPPRglASAHDVRREARVLRALAPrLGVPVPRPLA--LGEDGEVigapfYVMEWVE 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503669357  81 GKDARETILTVSKEQQYIYGVEAGRILQKIHSLPVTEVR-------------EDWEVFYNRkiddKIKKYKECPVQYEng 147
Cdd:COG3173  103 GETLEDALPDLSPAERRALARALGEFLAALHAVDPAAAGladgrpeglerqlARWRAQLRR----ALARTDDLPALRE-- 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503669357 148 qIFIDYLNANRELlkDRPQVFQHGDYHIGNFMIGED--RKIYVIDFDRFDLGDPWEEFNRIVWSAQVSPSFASG---MID 222
Cdd:COG3173  177 -RLAAWLAANLPE--WGPPVLVHGDLRPGNLLVDPDdgRLTAVIDWELATLGDPAADLAYLLLYWRLPDDLLGPraaFLA 253

                        250
                 ....*....|....
gi 503669357 223 GYFD--GKVPDLFW 234
Cdd:COG3173  254 AYEEatGDLDDLTW 267
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
163-260 2.71e-10

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 57.87  E-value: 2.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503669357 163 DRPQVFQHGDYHIGNFMIGEDRKIYVIDFDRFDLGDPWEEFNRIVWSAQVSPSFASGMIDGYFDGKVPDLFWKLLAIYIL 242
Cdd:COG0510   46 PLPLVLCHGDLHPGNFLVTDDGRLYLIDWEYAGLGDPAFDLAALLVEYGLSPEQAEELLEAYGFGRPTEELLRRLRAYRA 125

                         90
                 ....*....|....*...
gi 503669357 243 NNIVGALSWAVPYGAEEI 260
Cdd:COG0510  126 LADLLWALWALVRAAQEA 143
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 43-224 1.87e-07

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: 49.57  E-value: 1.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503669357  43 KFEFDMMEKVASLGVPMCKPISIELCDDKVhsFHEWIDGKDARETILTVSKEQQYIYgvEAGRILQKIHSLPVTevredw 122
Cdd:COG3642    4 RREARLLRELREAGVPVPKVLDVDPDDADL--VMEYIEGETLADLLEEGELPPELLR--ELGRLLARLHRAGIV------ 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503669357 123 evfynrkiddkikkykecpvqyengqifidylnanrellkdrpqvfqHGDYHIGNFMIGEDRkIYVIDFDRFDLGDPWEE 202
Cdd:COG3642   74 -----------------------------------------------HGDLTTSNILVDDGG-VYLIDFGLARYSDPLED 105

                        170       180       190
                 ....*....|....*....|....*....|.
gi 503669357 203 F--NRIVW-------SAQVSPSFASGMIDGY 224
Cdd:COG3642  106 KavDLAVLkrslestHPDPAEELWEAFLEGY 136
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 11-203 2.92e-06

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: 46.14  E-value: 2.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503669357  11 KGWSDDKKYCVTDQkqQKYFLRVSDKEKLDSKKFEFDMMEKVAS-LGVPMCKPISIELCDDKVHSFHEWIDGKDARETIL 89
Cdd:cd05120    7 KEGGDNKVYLLGDP--REYVLKIGPPRLKKDLEKEAAMLQLLAGkLSLPVPKVYGFGESDGWEYLLMERIEGETLSEVWP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503669357  90 TVSKEQQYIYGVEAGRILQKIHSLPVTevredwevfynrkiddkikkykecpvqyengqifidylnanrellkdrpqVFQ 169
Cdd:cd05120   85 RLSEEEKEKIADQLAEILAALHRIDSS--------------------------------------------------VLT 114

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 503669357 170 HGDYHIGNFMI-GEDRKIYVIDFDRFDLGDPWEEF 203
Cdd:cd05120  115 HGDLHPGNILVkPDGKLSGIIDWEFAGYGPPAFDY 149
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
 19-224 7.66e-06

Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal transduction mechanisms]; Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist is part of the Pathway/BioSystem: Threonine biosynthesis


Pssm-ID: 441905 [Multi-domain]  Cd Length: 297  Bit Score: 46.46  E-value: 7.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503669357  19 YCVTDQKQQKYFLRVSDKEKLDSK--KFEFDMMEKVASLGVPMCKPI------SIELCDDKVHSFHEWIDGkdarETILT 90
Cdd:COG2334   29 YRVETEDGRRYVLKLYRPGRWSPEeiPFELALLAHLAAAGLPVPAPVptrdgeTLLELEGRPAALFPFLPG----RSPEE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503669357  91 VSKEQQYiygvEAGRILQKIH------SLPVTEVREDWEVFYNRKIDDKIKKykecPVQYENGQIFIDYLNANRELLKDR 164
Cdd:COG2334  105 PSPEQLE----ELGRLLARLHraladfPRPNARDLAWWDELLERLLGPLLPD----PEDRALLEELLDRLEARLAPLLGA 176

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503669357 165 -PQVFQHGDYHIGNFMIGEDRKIYVIDFDR-------FDL-----GDPWEEFNrivwsaqvsPSFASGMIDGY 224
Cdd:COG2334  177 lPRGVIHGDLHPDNVLFDGDGVSGLIDFDDagygprlYDLaialnGWADGPLD---------PARLAALLEGY 240
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
 45-201 6.57e-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: 43.37  E-value: 6.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503669357  45 EFDMMEKVASLGVPMckPISIELCDDkvHSFH-------EWIDGKDARETILT--VSKEQQYIYGVEAGRILQKIHSLPV 115
Cdd:cd05154   48 EYRVLRALAGTGVPV--PRVLALCED--PSVLgapfyvmERVDGRVLPDPLPRpdLSPEERRALARSLVDALAALHSVDP 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503669357 116 TEVR---------------EDWEVFYNRKIDDKIKKYKECpvqyengqifIDYLNANRelLKDRPQVFQHGDYHIGNFMI 180
Cdd:cd05154  124 AALGladlgrpegylerqvDRWRRQLEAAATDPPPALEEA----------LRWLRANL--PADGRPVLVHGDFRLGNLLF 191

                        170       180
                 ....*....|....*....|..
gi 503669357 181 GEDRKIY-VIDFDRFDLGDPWE 201
Cdd:cd05154  192 DPDGRVTaVLDWELATLGDPLE 213
COG3178 COG3178
Predicted phosphotransferase, aminoglycoside/choline kinase (APH/ChoK) family [General ...
 165-191 5.74e-04

Predicted phosphotransferase, aminoglycoside/choline kinase (APH/ChoK) family [General function prediction only];


Pssm-ID: 442411  Cd Length: 327  Bit Score: 40.95  E-value: 5.74e-04
                         10        20
                 ....*....|....*....|....*..
gi 503669357 165 PQVFQHGDYHIGNFMIGEDRKIYVIDF 191
Cdd:COG3178  181 PRVLVHRDFHSRNLMVLPDGRPGLIDF 207
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
 19-224 1.11e-03

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: 39.93  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503669357  19 YCVTDqKQQKYFLRVSDK-EKLDSKKFEFDMMEKVASLGVPMCKPIS-------IELCDdKVHSFHEWIDGKDARetilT 90
Cdd:cd05153   31 YFVTT-TDGRYVLTLFEKrRSAAELPFELELLDHLAQAGLPVPRPLAdkdgellGELNG-KPAALFPFLPGESLT----T 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503669357  91 VSKEQQYiygvEAGRILQKIHSL--------PVTEVREDWEVFYNRKIDDKIKKYKEcpvqyENGQIFIDYLNANRELLK 162
Cdd:cd05153  105 PTPEQCR----AIGAALARLHLAlagfppprPNPRGLAWWKPLAERLKARLDLLAAD-----DRALLEDELARLQALAPS 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503669357 163 DRPQVFQHGDYHIGNFMIGEDRKIYVIDFDR-------FDLGD---PWeefnRIVWSAQVSPSFASGMIDGY 224
Cdd:cd05153  176 DLPRGVIHADLFRDNVLFDGDRLSGIIDFYDacydpllYDLAIalnDW----CFDDDGKLDPERAKALLAGY 243
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
 158-242 1.80e-03

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: 39.10  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503669357 158 RELLKDRPQ----VFQHGDYHIGNFMIGEDRKIYVIDFDRFDLGDPWEEFNRIVWSAQ---VSPSFASGMIDGYfdG-KV 229
Cdd:cd05150  151 AELEATRPAeedlVVTHGDACLPNIILDPGRFSGFIDLGRLGVADRYQDLALAVRSLRenlGGEEYAERFLDAY--GiDA 228

                         90
                 ....*....|...
gi 503669357 230 PDlfWKLLAIYIL 242
Cdd:cd05150  229 PD--PERLAYYRL 239
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
 166-191 4.63e-03

Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and similar proteins; This family is composed of the atypical yeast protein kinase Abc1p, its human homolog ADCK3 (also called CABC1), and similar proteins. Abc1p (also called Coq8p) is required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. It is necessary for the formation of a multi-subunit Q-biosynthetic complex and may also function in the regulation of Q synthesis. Human ADCK3 is able to rescue defects in Q synthesis and the phosphorylation state of Coq proteins in yeast Abc1 (or Coq8) mutants. Mutations in ADCK3 cause progressive cerebellar ataxia and atrophy due to Q10 deficiency. Eukaryotes contain at least two more ABC1/ADCK3-like proteins: in humans, these are the putative atypical protein kinases named ADCK1 and ADCK2. In algae and higher plants, ABC1 kinases have proliferated to more than 15 subfamilies, most of which are located in plastids or mitochondria. Eight of these plant ABC1 kinase subfamilies (ABC1K1-8) are specific for photosynthetic organisms. ABC1 kinases are not related to the ATP-binding cassette (ABC) membrane transporter family.


Pssm-ID: 270691 [Multi-domain]  Cd Length: 247  Bit Score: 37.86  E-value: 4.63e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 503669357 166 QVFQ----HGDYHIGNFMIGEDRKIYVIDF 191
Cdd:cd05121  185 QIFEdgffHADPHPGNILVLPDGRIALLDF 214
CotI COG5881
Spore coat protein CotI/CotS, protein kinase superfamily [Cell cycle control, cell division, ...
 166-196 4.75e-03

Spore coat protein CotI/CotS, protein kinase superfamily [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444583 [Multi-domain]  Cd Length: 331  Bit Score: 37.95  E-value: 4.75e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 503669357 166 QVFQHGDYHIGNFMIGEDRKIYVIDFD--RFDL 196
Cdd:COG5881  201 GGFCHHDYAYHNILIDEDGKIYIIDFDycIYDL 233
 
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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