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Conserved domains on  [gi|172044081|sp|A2RU49|]
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RecName: Full=Hydroxylysine kinase; Short=5-hydroxy-L-lysine kinase; AltName: Full=Aminoglycoside phosphotransferase domain-containing protein 1

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK06148 super family cl32120
hypothetical protein; Provisional
14-351 4.94e-51

hypothetical protein; Provisional


The actual alignment was detected with superfamily member PRK06148:

Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 183.30  E-value: 4.94e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081   14 KPTFSEEQASALVESVFGLKVSkVRPLPSYDDQNFHVyvsKTKDGpTEYVLKISNtkASKNPDLIEVQNHIIMFLKAAGf 93
Cdd:PRK06148    8 APEFTTKDAEALLAQHFGISAT-ATPLDGERDLNFRL---TTDDG-ADYILKIVN--PSEPRVESDFQTAALDHLAAVA- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081   94 PTASVCHTKGDNT-ASLVSVDSGSEiKSYLVRLLTYLPGRPIAEL-PVSPQLLYEIGKLAAKLDKTLQRFHHPklsSLHR 171
Cdd:PRK06148   80 PDLPVPRLIPSLSgASLASAQDPDG-EPRLLRLLSWLPGTPLAEAaPRTEALLDNLGRALGRLDRALQGFMHP---GALR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081  172 EnFIWNLKNVPLLEKYLYALGQNRNREIVEHVIHLFKEEVMTKLSHFRECINHGDLNDHNILIessksaSGNAEYQVSGI 251
Cdd:PRK06148  156 D-LDWDLRHAGRARDRLHFIDDPEDRALVERFLARFERNVAPRLAALPAQVIHNDANDYNILV------DADDGERISGL 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081  252 LDFGDMSYGYYVFEVAITIMYMMIESKSPIQVGGHVLAGFESITPLTAVEKGALFLLVCSRFCQSLVMAAYSCQLYPENk 331
Cdd:PRK06148  229 IDFGDAVHAPRICEVAIAAAYAILDHPDPIGAAAALVAGYHAVYPLQAQELDLLFDLIRMRLAVSVTNSASRREQTPDN- 307
                         330       340
                  ....*....|....*....|
gi 172044081  332 DYLMVTAKTGWKHLQQMFDM 351
Cdd:PRK06148  308 PYLAISEAPAWRLLERLDAM 327
 
Name Accession Description Interval E-value
PRK06148 PRK06148
hypothetical protein; Provisional
14-351 4.94e-51

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 183.30  E-value: 4.94e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081   14 KPTFSEEQASALVESVFGLKVSkVRPLPSYDDQNFHVyvsKTKDGpTEYVLKISNtkASKNPDLIEVQNHIIMFLKAAGf 93
Cdd:PRK06148    8 APEFTTKDAEALLAQHFGISAT-ATPLDGERDLNFRL---TTDDG-ADYILKIVN--PSEPRVESDFQTAALDHLAAVA- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081   94 PTASVCHTKGDNT-ASLVSVDSGSEiKSYLVRLLTYLPGRPIAEL-PVSPQLLYEIGKLAAKLDKTLQRFHHPklsSLHR 171
Cdd:PRK06148   80 PDLPVPRLIPSLSgASLASAQDPDG-EPRLLRLLSWLPGTPLAEAaPRTEALLDNLGRALGRLDRALQGFMHP---GALR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081  172 EnFIWNLKNVPLLEKYLYALGQNRNREIVEHVIHLFKEEVMTKLSHFRECINHGDLNDHNILIessksaSGNAEYQVSGI 251
Cdd:PRK06148  156 D-LDWDLRHAGRARDRLHFIDDPEDRALVERFLARFERNVAPRLAALPAQVIHNDANDYNILV------DADDGERISGL 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081  252 LDFGDMSYGYYVFEVAITIMYMMIESKSPIQVGGHVLAGFESITPLTAVEKGALFLLVCSRFCQSLVMAAYSCQLYPENk 331
Cdd:PRK06148  229 IDFGDAVHAPRICEVAIAAAYAILDHPDPIGAAAALVAGYHAVYPLQAQELDLLFDLIRMRLAVSVTNSASRREQTPDN- 307
                         330       340
                  ....*....|....*....|
gi 172044081  332 DYLMVTAKTGWKHLQQMFDM 351
Cdd:PRK06148  308 PYLAISEAPAWRLLERLDAM 327
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
20-347 5.95e-48

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: 164.33  E-value: 5.95e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081  20 EQASALVESvFGL-KVSKVRPLPSYDDQNFHVyvsKTKDGPtEYVLKISNtKASKNPDLIEVQNHIIMFLKAAGFPTASV 98
Cdd:COG2334    1 DELAAALER-YGLgPLSSLKPLNSGENRNYRV---ETEDGR-RYVLKLYR-PGRWSPEEIPFELALLAHLAAAGLPVPAP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081  99 CHTKGDNTasLVsvdsgsEIKSYLVRLLTYLPGRPIAELpvSPQLLYEIGKLAAKLDKTLQRFHHPKLSSLHRenfiWNL 178
Cdd:COG2334   75 VPTRDGET--LL------ELEGRPAALFPFLPGRSPEEP--SPEQLEELGRLLARLHRALADFPRPNARDLAW----WDE 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081 179 KNVPLLEKYLYALGQnrnREIVEHVIHLFKEEVMTKLSHFRECINHGDLNDHNILIessksaSGNaeyQVSGILDFGDMS 258
Cdd:COG2334  141 LLERLLGPLLPDPED---RALLEELLDRLEARLAPLLGALPRGVIHGDLHPDNVLF------DGD---GVSGLIDFDDAG 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081 259 YGYYVFEVAITIMYMMIESKSPIQVgGHVLAGFESITPLTAVEKGALFLLVCSRFCQSLVMAAYSCQ-LYPENKDYLMVT 337
Cdd:COG2334  209 YGPRLYDLAIALNGWADGPLDPARL-AALLEGYRAVRPLTEAELAALPPLLRLRALRFLAWRLRRVRaKDPAFERYLRRQ 287
                        330
                 ....*....|
gi 172044081 338 AKTGWKHLQQ 347
Cdd:COG2334  288 IALAWAALEA 297
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
19-308 7.56e-27

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: 108.11  E-value: 7.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081  19 EEQASALVESVFGLKVSKVRPLPS-YDDQNFHVyvsKTKDGptEYVLKISNtkASKNPDLIEVQNHIIMFLKAAGFPTAS 97
Cdd:cd05153    1 DEELAEFLAHYDLGELLSFEGIAAgIENTNYFV---TTTDG--RYVLTLFE--KRRSAAELPFELELLDHLAQAGLPVPR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081  98 VCHTKGDNTASlvsvdsgsEIKSYLVRLLTYLPGRPIAELpvSPQLLYEIGKLAAKLDKTLQRFhhpKLSSLHRENFIWN 177
Cdd:cd05153   74 PLADKDGELLG--------ELNGKPAALFPFLPGESLTTP--TPEQCRAIGAALARLHLALAGF---PPPRPNPRGLAWW 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081 178 LKNVPLLEKYLYALGQnRNREIVEHVIHLFKEEVMTKLSHfreCINHGDLNDHNILIEssksasgnaEYQVSGILDFGDM 257
Cdd:cd05153  141 KPLAERLKARLDLLAA-DDRALLEDELARLQALAPSDLPR---GVIHADLFRDNVLFD---------GDRLSGIIDFYDA 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 172044081 258 SYGYYVFEVAITIMYMMIES--KSPIQVGGHVLAGFESITPLTAVEKGALFLL 308
Cdd:cd05153  208 CYDPLLYDLAIALNDWCFDDdgKLDPERAKALLAGYQSVRPLTEEEKAALPLL 260
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
36-276 3.30e-19

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: 85.63  E-value: 3.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081   36 KVRPLPS-YDDQNFHVyvsktKDGPTEYVLKISNtkASKNPDLIEVQNHIIMFLKAAGFPTASVchtkgdntasLVSVDS 114
Cdd:pfam01636   1 TLRPISSgASNRTYLV-----TTGDGRYVLRLPP--PGRAAEELRRELALLRHLAAAGVPPVPR----------VLAGCT 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081  115 GSEIKSYLVRLLTYLPGRPIAELPvSPQLLYEIGKLAAKLDKTLQRFHHPKLSSLHREnfIWNLKNVPLLEKYLYALGQN 194
Cdd:pfam01636  64 DAELLGLPFLLMEYLPGEVLARPL-LPEERGALLEALGRALARLHAVDPAALPLAGRL--ARLLELLRQLEAALARLLAA 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081  195 RNREIVEHVIHLFKEEVM-TKLSHFRECINHGDLNDHNILIessksasgNAEYQVSGILDFGDMSYGYYVFEVAITIMYM 273
Cdd:pfam01636 141 ELLDRLEELEERLLAALLaLLPAELPPVLVHGDLHPGNLLV--------DPGGRVSGVIDFEDAGLGDPAYDLAILLNSW 212

                  ...
gi 172044081  274 MIE 276
Cdd:pfam01636 213 GRE 215
 
Name Accession Description Interval E-value
PRK06148 PRK06148
hypothetical protein; Provisional
14-351 4.94e-51

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 183.30  E-value: 4.94e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081   14 KPTFSEEQASALVESVFGLKVSkVRPLPSYDDQNFHVyvsKTKDGpTEYVLKISNtkASKNPDLIEVQNHIIMFLKAAGf 93
Cdd:PRK06148    8 APEFTTKDAEALLAQHFGISAT-ATPLDGERDLNFRL---TTDDG-ADYILKIVN--PSEPRVESDFQTAALDHLAAVA- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081   94 PTASVCHTKGDNT-ASLVSVDSGSEiKSYLVRLLTYLPGRPIAEL-PVSPQLLYEIGKLAAKLDKTLQRFHHPklsSLHR 171
Cdd:PRK06148   80 PDLPVPRLIPSLSgASLASAQDPDG-EPRLLRLLSWLPGTPLAEAaPRTEALLDNLGRALGRLDRALQGFMHP---GALR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081  172 EnFIWNLKNVPLLEKYLYALGQNRNREIVEHVIHLFKEEVMTKLSHFRECINHGDLNDHNILIessksaSGNAEYQVSGI 251
Cdd:PRK06148  156 D-LDWDLRHAGRARDRLHFIDDPEDRALVERFLARFERNVAPRLAALPAQVIHNDANDYNILV------DADDGERISGL 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081  252 LDFGDMSYGYYVFEVAITIMYMMIESKSPIQVGGHVLAGFESITPLTAVEKGALFLLVCSRFCQSLVMAAYSCQLYPENk 331
Cdd:PRK06148  229 IDFGDAVHAPRICEVAIAAAYAILDHPDPIGAAAALVAGYHAVYPLQAQELDLLFDLIRMRLAVSVTNSASRREQTPDN- 307
                         330       340
                  ....*....|....*....|
gi 172044081  332 DYLMVTAKTGWKHLQQMFDM 351
Cdd:PRK06148  308 PYLAISEAPAWRLLERLDAM 327
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
20-347 5.95e-48

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: 164.33  E-value: 5.95e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081  20 EQASALVESvFGL-KVSKVRPLPSYDDQNFHVyvsKTKDGPtEYVLKISNtKASKNPDLIEVQNHIIMFLKAAGFPTASV 98
Cdd:COG2334    1 DELAAALER-YGLgPLSSLKPLNSGENRNYRV---ETEDGR-RYVLKLYR-PGRWSPEEIPFELALLAHLAAAGLPVPAP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081  99 CHTKGDNTasLVsvdsgsEIKSYLVRLLTYLPGRPIAELpvSPQLLYEIGKLAAKLDKTLQRFHHPKLSSLHRenfiWNL 178
Cdd:COG2334   75 VPTRDGET--LL------ELEGRPAALFPFLPGRSPEEP--SPEQLEELGRLLARLHRALADFPRPNARDLAW----WDE 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081 179 KNVPLLEKYLYALGQnrnREIVEHVIHLFKEEVMTKLSHFRECINHGDLNDHNILIessksaSGNaeyQVSGILDFGDMS 258
Cdd:COG2334  141 LLERLLGPLLPDPED---RALLEELLDRLEARLAPLLGALPRGVIHGDLHPDNVLF------DGD---GVSGLIDFDDAG 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081 259 YGYYVFEVAITIMYMMIESKSPIQVgGHVLAGFESITPLTAVEKGALFLLVCSRFCQSLVMAAYSCQ-LYPENKDYLMVT 337
Cdd:COG2334  209 YGPRLYDLAIALNGWADGPLDPARL-AALLEGYRAVRPLTEAELAALPPLLRLRALRFLAWRLRRVRaKDPAFERYLRRQ 287
                        330
                 ....*....|
gi 172044081 338 AKTGWKHLQQ 347
Cdd:COG2334  288 IALAWAALEA 297
PRK06149 PRK06149
aminotransferase;
11-350 2.56e-29

aminotransferase;


Pssm-ID: 235716 [Multi-domain]  Cd Length: 972  Bit Score: 119.72  E-value: 2.56e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081  11 ALSKPTFSEEQASALVESVFGLKvSKVRPLPSYDDQNFHVyvsktKDGPTEYVLKISNtkASKNPDLIEVQNHIIMFLKA 90
Cdd:PRK06149  11 SLPAPDVSEAQAERILAEHYGLS-GTLTELGSQQDRNFRV-----DSDGGRFVLKICH--AAYAAVELEAQHAALRHLAE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081  91 A--GFPTASVCHTKgdNTASLVSVDSGSEikSYLVRLLTYLPGRPIAELP-VSPQLLYEIGKLAAKLDKTLQRFHHPkls 167
Cdd:PRK06149  83 RepALRVPVVIPAL--DGEELLTLDVRGQ--GLRVRLLDYLPGQPLTRLGhLAPASVAGLGALCARVARALADFDHP--- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081 168 SLHREnFIWNLKN-VPLLEKYLYALGQNRNREIVEHVIHLFKEEVMTKLSHFRECINHGDLNDHNILieSSKSASGnaEY 246
Cdd:PRK06149 156 GLDRT-LQWDLRHaGPVVAHLLSHITDPAQRARIAEATRDAARRLQPLAPALPLQAVHLDITDDNVV--GSRDADG--RW 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081 247 QVSGILDFGDMSYGYYVFEVAITIMYMMieskspIQVGG---HVL---AGFESITPLTAVEKGALFLLVCSRFCQSLVMA 320
Cdd:PRK06149 231 QPDGVIDFGDLVRTWRVADLAVTCASLL------HHAGGdpfSILpavRAYHAVRPLSEAELKALWPLVVARAAVLVASS 304
                        330       340       350
                 ....*....|....*....|....*....|
gi 172044081 321 AYSCQLYPENkDYLMVTAKTGWkhlqQMFD 350
Cdd:PRK06149 305 EQQLAVDPDN-AYVRDNLAHEW----EIFD 329
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
19-308 7.56e-27

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: 108.11  E-value: 7.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081  19 EEQASALVESVFGLKVSKVRPLPS-YDDQNFHVyvsKTKDGptEYVLKISNtkASKNPDLIEVQNHIIMFLKAAGFPTAS 97
Cdd:cd05153    1 DEELAEFLAHYDLGELLSFEGIAAgIENTNYFV---TTTDG--RYVLTLFE--KRRSAAELPFELELLDHLAQAGLPVPR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081  98 VCHTKGDNTASlvsvdsgsEIKSYLVRLLTYLPGRPIAELpvSPQLLYEIGKLAAKLDKTLQRFhhpKLSSLHRENFIWN 177
Cdd:cd05153   74 PLADKDGELLG--------ELNGKPAALFPFLPGESLTTP--TPEQCRAIGAALARLHLALAGF---PPPRPNPRGLAWW 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081 178 LKNVPLLEKYLYALGQnRNREIVEHVIHLFKEEVMTKLSHfreCINHGDLNDHNILIEssksasgnaEYQVSGILDFGDM 257
Cdd:cd05153  141 KPLAERLKARLDLLAA-DDRALLEDELARLQALAPSDLPR---GVIHADLFRDNVLFD---------GDRLSGIIDFYDA 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 172044081 258 SYGYYVFEVAITIMYMMIES--KSPIQVGGHVLAGFESITPLTAVEKGALFLL 308
Cdd:cd05153  208 CYDPLLYDLAIALNDWCFDDdgKLDPERAKALLAGYQSVRPLTEEEKAALPLL 260
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
36-276 3.30e-19

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: 85.63  E-value: 3.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081   36 KVRPLPS-YDDQNFHVyvsktKDGPTEYVLKISNtkASKNPDLIEVQNHIIMFLKAAGFPTASVchtkgdntasLVSVDS 114
Cdd:pfam01636   1 TLRPISSgASNRTYLV-----TTGDGRYVLRLPP--PGRAAEELRRELALLRHLAAAGVPPVPR----------VLAGCT 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081  115 GSEIKSYLVRLLTYLPGRPIAELPvSPQLLYEIGKLAAKLDKTLQRFHHPKLSSLHREnfIWNLKNVPLLEKYLYALGQN 194
Cdd:pfam01636  64 DAELLGLPFLLMEYLPGEVLARPL-LPEERGALLEALGRALARLHAVDPAALPLAGRL--ARLLELLRQLEAALARLLAA 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081  195 RNREIVEHVIHLFKEEVM-TKLSHFRECINHGDLNDHNILIessksasgNAEYQVSGILDFGDMSYGYYVFEVAITIMYM 273
Cdd:pfam01636 141 ELLDRLEELEERLLAALLaLLPAELPPVLVHGDLHPGNLLV--------DPGGRVSGVIDFEDAGLGDPAYDLAILLNSW 212

                  ...
gi 172044081  274 MIE 276
Cdd:pfam01636 213 GRE 215
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
207-269 3.62e-04

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: 40.75  E-value: 3.62e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 172044081 207 FKEEVMTKLSHFRE----CINHGDLNDHNILIESsksasgnaEYQVSGILDFGDMSYGYYVFEVAIT 269
Cdd:cd05120   94 IADQLAEILAALHRidssVLTHGDLHPGNILVKP--------DGKLSGIIDWEFAGYGPPAFDYAAA 152
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
15-274 6.18e-03

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 38.17  E-value: 6.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081  15 PTFSEEQASALVESVFG--LKVSKVRPLPS-YDDQNFHVyvsktkDGPTEYVLKISnTKASKNPDLIEVQNHIIMFLKA- 90
Cdd:COG3173    1 EELDEAALRALLAAQLPglAGLPEVEPLSGgWSNLTYRL------DTGDRLVLRRP-PRGLASAHDVRREARVLRALAPr 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081  91 AGFPTASVchtkgdntasLVSVDSGSEIKSYLVrLLTYLPGRPIAEL--PVSPQLLYEIGKLAAKldkTLQRFH-----H 163
Cdd:COG3173   74 LGVPVPRP----------LALGEDGEVIGAPFY-VMEWVEGETLEDAlpDLSPAERRALARALGE---FLAALHavdpaA 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172044081 164 PKLSSLHRENFIWNLKnvPLLEKYLYALGQNRNREIVEHVIHLFKEEVMTKLShfRECINHGDLNDHNILIEssksasgN 243
Cdd:COG3173  140 AGLADGRPEGLERQLA--RWRAQLRRALARTDDLPALRERLAAWLAANLPEWG--PPVLVHGDLRPGNLLVD-------P 208
                        250       260       270
                 ....*....|....*....|....*....|.
gi 172044081 244 AEYQVSGILDFGDMSYGYYVFEVAITIMYMM 274
Cdd:COG3173  209 DDGRLTAVIDWELATLGDPAADLAYLLLYWR 239
 
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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