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Conserved domains on  [gi|1095433689|gb|AOZ90814|]
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aminoglycoside phosphotransferase [Paenibacillus crassostreae]

Protein Classification

protein kinase family protein( domain architecture ID 229378)

protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to substrates such as serine/threonine and/or tyrosine residues on proteins, or may be a pseudokinase

CATH:  1.10.510.10
PubMed:  16244704
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
23-298 2.24e-41

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd05153:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 300  Bit Score: 145.86  E-value: 2.24e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095433689  23 NYEVHEPINLKYFLRG-MNDTYILETGSGKYIFRVYRAdRRNKSEISFELDLLNYLNENDVSVSIPITKKDGtlinEFFV 101
Cdd:cd05153    10 HYDLGELLSFEGIAAGiENTNYFVTTTDGRYVLTLFEK-RRSAAELPFELELLDHLAQAGLPVPRPLADKDG----ELLG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095433689 102 TEGVKFGVMFSFAEGNEKPIHAVEDSYLYGKSVAQIHKVTENF--RSEHVRSNLNLEYLIEKPLNIIKLHMEHrqedynf 179
Cdd:cd05153    85 ELNGKPAALFPFLPGESLTTPTPEQCRAIGAALARLHLALAGFppPRPNPRGLAWWKPLAERLKARLDLLAAD------- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095433689 180 IIELILELKEQLVMMLEEGLDWGICHGDLHGNtNVAFTDNGKLTHYDFDISGYGWRSYDIAefRLAREIHSGHNKDEVER 259
Cdd:cd05153   158 DRALLEDELARLQALAPSDLPRGVIHADLFRD-NVLFDGDRLSGIIDFYDACYDPLLYDLA--IALNDWCFDDDGKLDPE 234
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1095433689 260 LWEAFLHGYRDVRDFSENDVKAVSIFVALRQLWLFGLCF 298
Cdd:cd05153   235 RAKALLAGYQSVRPLTEEEKAALPLLLRAAALRFWLSRL 273
 
Name Accession Description Interval E-value
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
23-298 2.24e-41

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: 145.86  E-value: 2.24e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095433689  23 NYEVHEPINLKYFLRG-MNDTYILETGSGKYIFRVYRAdRRNKSEISFELDLLNYLNENDVSVSIPITKKDGtlinEFFV 101
Cdd:cd05153    10 HYDLGELLSFEGIAAGiENTNYFVTTTDGRYVLTLFEK-RRSAAELPFELELLDHLAQAGLPVPRPLADKDG----ELLG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095433689 102 TEGVKFGVMFSFAEGNEKPIHAVEDSYLYGKSVAQIHKVTENF--RSEHVRSNLNLEYLIEKPLNIIKLHMEHrqedynf 179
Cdd:cd05153    85 ELNGKPAALFPFLPGESLTTPTPEQCRAIGAALARLHLALAGFppPRPNPRGLAWWKPLAERLKARLDLLAAD------- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095433689 180 IIELILELKEQLVMMLEEGLDWGICHGDLHGNtNVAFTDNGKLTHYDFDISGYGWRSYDIAefRLAREIHSGHNKDEVER 259
Cdd:cd05153   158 DRALLEDELARLQALAPSDLPRGVIHADLFRD-NVLFDGDRLSGIIDFYDACYDPLLYDLA--IALNDWCFDDDGKLDPE 234
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1095433689 260 LWEAFLHGYRDVRDFSENDVKAVSIFVALRQLWLFGLCF 298
Cdd:cd05153   235 RAKALLAGYQSVRPLTEEEKAALPLLLRAAALRFWLSRL 273
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
15-294 2.46e-40

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: 143.14  E-value: 2.46e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095433689  15 ALLLHIKDNYEVHEPINLKYFLRGMNDTYILETGSGK-YIFRVYRADRRNKSEISFELDLLNYLNENDVSVSIPITKKDG 93
Cdd:COG2334     1 DELAAALERYGLGPLSSLKPLNSGENRNYRVETEDGRrYVLKLYRPGRWSPEEIPFELALLAHLAAAGLPVPAPVPTRDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095433689  94 tlinEFFVTEGVKFGVMFSFAEGNEKPIHAVEDSYLYGKSVAQIHKVTENFRSEHVRSNLNLEYLIEKPLNiiklHMEHR 173
Cdd:COG2334    81 ----ETLLELEGRPAALFPFLPGRSPEEPSPEQLEELGRLLARLHRALADFPRPNARDLAWWDELLERLLG----PLLPD 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095433689 174 QEDYNFIIELILELKEQLVMMLeEGLDWGICHGDLHGNtNVAFTDNGKLTHYDFDISGYGWRSYDiaefrLAREIHSGHN 253
Cdd:COG2334   153 PEDRALLEELLDRLEARLAPLL-GALPRGVIHGDLHPD-NVLFDGDGVSGLIDFDDAGYGPRLYD-----LAIALNGWAD 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1095433689 254 KDEVERLWEAFLHGYRDVRDFSENDVKAVSIFVALRQLWLF 294
Cdd:COG2334   226 GPLDPARLAALLEGYRAVRPLTEAELAALPPLLRLRALRFL 266
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
40-274 3.03e-14

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: 70.99  E-value: 3.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095433689  40 NDTYILETGSGKYIFRVYRaDRRNKSEISFELDLLNYLNENDVS-VSIPItkkDGTLINEFfvtEGVKFGVMfSFAEG-- 116
Cdd:pfam01636  11 NRTYLVTTGDGRYVLRLPP-PGRAAEELRRELALLRHLAAAGVPpVPRVL---AGCTDAEL---LGLPFLLM-EYLPGev 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095433689 117 NEKPIHAVEDSYLY---GKSVAQIHKV-TENFRSEHVRsnlnlEYLIEKPLNIIKLHMEHRQEDY-NFIIELILELKEQL 191
Cdd:pfam01636  83 LARPLLPEERGALLealGRALARLHAVdPAALPLAGRL-----ARLLELLRQLEAALARLLAAELlDRLEELEERLLAAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095433689 192 VMMLEEGLDWGICHGDLHGNtNVAFTDNGKLTH-YDFDISGYGWRSYDIAefRLAREIHSGHNKDEVERLWEAFLHGYRD 270
Cdd:pfam01636 158 LALLPAELPPVLVHGDLHPG-NLLVDPGGRVSGvIDFEDAGLGDPAYDLA--ILLNSWGRELGAELLAAYLAAYGAFGYA 234

                  ....
gi 1095433689 271 VRDF 274
Cdd:pfam01636 235 RLRE 238
PRK14879 PRK14879
Kae1-associated kinase Bud32;
202-272 9.61e-03

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 36.81  E-value: 9.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1095433689 202 GICHGDLHgNTNVAFTDnGKLTHYDFdisGYGWRSYDIAEFrlAREIH-------SGHnKDEVERLWEAFLHGYRDVR 272
Cdd:PRK14879  115 GIIHGDLT-TSNMILSG-GKIYLIDF---GLAEFSKDLEDR--AVDLHvllrsleSTH-PDWAEELFEAFLEGYREVM 184
 
Name Accession Description Interval E-value
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
23-298 2.24e-41

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: 145.86  E-value: 2.24e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095433689  23 NYEVHEPINLKYFLRG-MNDTYILETGSGKYIFRVYRAdRRNKSEISFELDLLNYLNENDVSVSIPITKKDGtlinEFFV 101
Cdd:cd05153    10 HYDLGELLSFEGIAAGiENTNYFVTTTDGRYVLTLFEK-RRSAAELPFELELLDHLAQAGLPVPRPLADKDG----ELLG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095433689 102 TEGVKFGVMFSFAEGNEKPIHAVEDSYLYGKSVAQIHKVTENF--RSEHVRSNLNLEYLIEKPLNIIKLHMEHrqedynf 179
Cdd:cd05153    85 ELNGKPAALFPFLPGESLTTPTPEQCRAIGAALARLHLALAGFppPRPNPRGLAWWKPLAERLKARLDLLAAD------- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095433689 180 IIELILELKEQLVMMLEEGLDWGICHGDLHGNtNVAFTDNGKLTHYDFDISGYGWRSYDIAefRLAREIHSGHNKDEVER 259
Cdd:cd05153   158 DRALLEDELARLQALAPSDLPRGVIHADLFRD-NVLFDGDRLSGIIDFYDACYDPLLYDLA--IALNDWCFDDDGKLDPE 234
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1095433689 260 LWEAFLHGYRDVRDFSENDVKAVSIFVALRQLWLFGLCF 298
Cdd:cd05153   235 RAKALLAGYQSVRPLTEEEKAALPLLLRAAALRFWLSRL 273
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
15-294 2.46e-40

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: 143.14  E-value: 2.46e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095433689  15 ALLLHIKDNYEVHEPINLKYFLRGMNDTYILETGSGK-YIFRVYRADRRNKSEISFELDLLNYLNENDVSVSIPITKKDG 93
Cdd:COG2334     1 DELAAALERYGLGPLSSLKPLNSGENRNYRVETEDGRrYVLKLYRPGRWSPEEIPFELALLAHLAAAGLPVPAPVPTRDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095433689  94 tlinEFFVTEGVKFGVMFSFAEGNEKPIHAVEDSYLYGKSVAQIHKVTENFRSEHVRSNLNLEYLIEKPLNiiklHMEHR 173
Cdd:COG2334    81 ----ETLLELEGRPAALFPFLPGRSPEEPSPEQLEELGRLLARLHRALADFPRPNARDLAWWDELLERLLG----PLLPD 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095433689 174 QEDYNFIIELILELKEQLVMMLeEGLDWGICHGDLHGNtNVAFTDNGKLTHYDFDISGYGWRSYDiaefrLAREIHSGHN 253
Cdd:COG2334   153 PEDRALLEELLDRLEARLAPLL-GALPRGVIHGDLHPD-NVLFDGDGVSGLIDFDDAGYGPRLYD-----LAIALNGWAD 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1095433689 254 KDEVERLWEAFLHGYRDVRDFSENDVKAVSIFVALRQLWLF 294
Cdd:COG2334   226 GPLDPARLAALLEGYRAVRPLTEAELAALPPLLRLRALRFL 266
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
40-274 3.03e-14

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: 70.99  E-value: 3.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095433689  40 NDTYILETGSGKYIFRVYRaDRRNKSEISFELDLLNYLNENDVS-VSIPItkkDGTLINEFfvtEGVKFGVMfSFAEG-- 116
Cdd:pfam01636  11 NRTYLVTTGDGRYVLRLPP-PGRAAEELRRELALLRHLAAAGVPpVPRVL---AGCTDAEL---LGLPFLLM-EYLPGev 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095433689 117 NEKPIHAVEDSYLY---GKSVAQIHKV-TENFRSEHVRsnlnlEYLIEKPLNIIKLHMEHRQEDY-NFIIELILELKEQL 191
Cdd:pfam01636  83 LARPLLPEERGALLealGRALARLHAVdPAALPLAGRL-----ARLLELLRQLEAALARLLAAELlDRLEELEERLLAAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095433689 192 VMMLEEGLDWGICHGDLHGNtNVAFTDNGKLTH-YDFDISGYGWRSYDIAefRLAREIHSGHNKDEVERLWEAFLHGYRD 270
Cdd:pfam01636 158 LALLPAELPPVLVHGDLHPG-NLLVDPGGRVSGvIDFEDAGLGDPAYDLA--ILLNSWGRELGAELLAAYLAAYGAFGYA 234

                  ....
gi 1095433689 271 VRDF 274
Cdd:pfam01636 235 RLRE 238
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
162-292 3.07e-06

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 46.31  E-value: 3.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095433689 162 PLNIIKLHMEHRQEDYNFIIELILELKEQLVmmlEEGLDWGICHGDLHGNtNVAFTDNGKLTHYDFDISGYGWRSYDIAE 241
Cdd:COG0510    13 LFARLERYLALGPRDLPELLRRLEELERALA---ARPLPLVLCHGDLHPG-NFLVTDDGRLYLIDWEYAGLGDPAFDLAA 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1095433689 242 FRlareIHSGHNKDEVERLWEAFlhGYRDVRDFSENDVKAVSIFVALRQ-LW 292
Cdd:COG0510    89 LL----VEYGLSPEQAEELLEAY--GFGRPTEELLRRLRAYRALADLLWaLW 134
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
202-276 2.59e-05

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: 43.79  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095433689 202 GICHGDLHgNTNVAFTDNGklTHY-DFDISGYG----WRSYDIAefRLAREIHSGHNkDEVERLWEAFLHGYRDVRDFSE 276
Cdd:COG3642    71 GIVHGDLT-TSNILVDDGG--VYLiDFGLARYSdpleDKAVDLA--VLKRSLESTHP-DPAEELWEAFLEGYREVGPAEE 144
CotI COG5881
Spore coat protein CotI/CotS, protein kinase superfamily [Cell cycle control, cell division, ...
43-287 5.21e-05

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: 44.50  E-value: 5.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095433689  43 YILETGSGKYIFRVYRadrRNKSEISFELDLLNYLNENDVSVSIPITK-KDGTLInefFVTEGVKFGVM--FSFAEGNEK 119
Cdd:COG5881    26 YKIETDQGPKCLKKIK---YSPERLLFIYEAQEHLKKNGFNNIPRIVPtKDGKPY---VKYGGKLYYLTewIEGRECDYK 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095433689 120 PIhavEDSYLYGKSVAQIHKVTENF---RSEHVRSNL-NLEYLIEKPLNIIK--LHMEHRQEDYN-----------FIIE 182
Cdd:COG5881   100 NP---EDLKKAAETLAEFHKASKGFeppPGSKGRSHLgKWPERFEKRLEELEkfKKIAEKKKNKNefdrlflknidYFLE 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1095433689 183 LILELKEQL------VMMLEEGLDWGICHGDLhGNTNVAFTDNGKLTHYDFDISGYGWRSYDIAEF--RLAREIHSghNK 254
Cdd:COG5881   177 QAEKALELLeksayyKLVKEAKKEGGFCHHDY-AYHNILIDEDGKIYIIDFDYCIYDLPVHDLAKLlrRVMKRGNW--DI 253
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1095433689 255 DEVERLWEAflhgYRDVRDFSENDVKAVSIFVA 287
Cdd:COG5881   254 EKAKEILEA----YNKINPLSKEEIEVLLAFLL 282
ChoK-like_euk cd14021
Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline ...
203-242 5.49e-03

Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline kinase, ethanolamine kinase, and similar proteins. 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. 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: 270923 [Multi-domain]  Cd Length: 229  Bit Score: 37.63  E-value: 5.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1095433689 203 ICHGDLHGNTNVAFTDNGKLTHYDFDISGYGWRSYDIAEF 242
Cdd:cd14021   114 FCHNDLQENNILLTNDQDGLRLIDFEYSGFNYRGYDIANF 153
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
187-240 7.53e-03

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: 36.51  E-value: 7.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1095433689 187 LKEQLVMMLEE--GLDW-GICHGDLHGNtNVAFTDNGKLTH-YDFDISGYGWRSYDIA 240
Cdd:cd05120    94 IADQLAEILAAlhRIDSsVLTHGDLHPG-NILVKPDGKLSGiIDWEFAGYGPPAFDYA 150
PRK14879 PRK14879
Kae1-associated kinase Bud32;
202-272 9.61e-03

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 36.81  E-value: 9.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1095433689 202 GICHGDLHgNTNVAFTDnGKLTHYDFdisGYGWRSYDIAEFrlAREIH-------SGHnKDEVERLWEAFLHGYRDVR 272
Cdd:PRK14879  115 GIIHGDLT-TSNMILSG-GKIYLIDF---GLAEFSKDLEDR--AVDLHvllrsleSTH-PDWAEELFEAFLEGYREVM 184
 
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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