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Conserved domains on  [gi|134288902|ref|NP_001077081|]
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hydroxylysine kinase isoform 2 [Homo sapiens]

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
14-215 4.93e-25

hypothetical protein; Provisional


The actual alignment was detected with superfamily member PRK06148:

Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 102.41  E-value: 4.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288902   14 KPTFSEEQASALVESVFGLKVSkVRPLPSYDDQNFHVyvsKTKDGpTEYVLKISNtkASKNPDLIEVQNHIIMFLKAAGf 93
Cdd:PRK06148    8 APEFTTKDAEALLAQHFGISAT-ATPLDGERDLNFRL---TTDDG-ADYILKIVN--PSEPRVESDFQTAALDHLAAVA- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288902   94 PTASVCHTKGDNT-ASLVSVDSGSEiKSYLVRLLTYLPGRPIAEL-PVSPQLLYEIGKLAAKLDKTLQRFHHPklsSLHR 171
Cdd:PRK06148   80 PDLPVPRLIPSLSgASLASAQDPDG-EPRLLRLLSWLPGTPLAEAaPRTEALLDNLGRALGRLDRALQGFMHP---GALR 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 134288902  172 EnFIWNLKNVPLLEKYLYALGQNRNREIVEHVIHLFKEEVMTKL 215
Cdd:PRK06148  156 D-LDWDLRHAGRARDRLHFIDDPEDRALVERFLARFERNVAPRL 198
 
Name Accession Description Interval E-value
PRK06148 PRK06148
hypothetical protein; Provisional
14-215 4.93e-25

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 102.41  E-value: 4.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288902   14 KPTFSEEQASALVESVFGLKVSkVRPLPSYDDQNFHVyvsKTKDGpTEYVLKISNtkASKNPDLIEVQNHIIMFLKAAGf 93
Cdd:PRK06148    8 APEFTTKDAEALLAQHFGISAT-ATPLDGERDLNFRL---TTDDG-ADYILKIVN--PSEPRVESDFQTAALDHLAAVA- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288902   94 PTASVCHTKGDNT-ASLVSVDSGSEiKSYLVRLLTYLPGRPIAEL-PVSPQLLYEIGKLAAKLDKTLQRFHHPklsSLHR 171
Cdd:PRK06148   80 PDLPVPRLIPSLSgASLASAQDPDG-EPRLLRLLSWLPGTPLAEAaPRTEALLDNLGRALGRLDRALQGFMHP---GALR 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 134288902  172 EnFIWNLKNVPLLEKYLYALGQNRNREIVEHVIHLFKEEVMTKL 215
Cdd:PRK06148  156 D-LDWDLRHAGRARDRLHFIDDPEDRALVERFLARFERNVAPRL 198
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
20-219 2.76e-20

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: 86.52  E-value: 2.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288902  20 EQASALVESvFGL-KVSKVRPLPSYDDQNFHVyvsKTKDGPtEYVLKISNtKASKNPDLIEVQNHIIMFLKAAGFPTASV 98
Cdd:COG2334    1 DELAAALER-YGLgPLSSLKPLNSGENRNYRV---ETEDGR-RYVLKLYR-PGRWSPEEIPFELALLAHLAAAGLPVPAP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288902  99 CHTKGDNTasLVsvdsgsEIKSYLVRLLTYLPGRPIAELpvSPQLLYEIGKLAAKLDKTLQRFHHPKLSSLHRenfiWNL 178
Cdd:COG2334   75 VPTRDGET--LL------ELEGRPAALFPFLPGRSPEEP--SPEQLEELGRLLARLHRALADFPRPNARDLAW----WDE 140
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 134288902 179 KNVPLLEKYLYALGQnrnREIVEHVIHLFKEEVMTKLSHFR 219
Cdd:COG2334  141 LLERLLGPLLPDPED---RALLEELLDRLEARLAPLLGALP 178
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
19-217 6.24e-10

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: 57.65  E-value: 6.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288902  19 EEQASALVESVFGLKVSKVRPLPS-YDDQNFHVyvsKTKDGptEYVLKISNtkASKNPDLIEVQNHIIMFLKAAGFPTAS 97
Cdd:cd05153    1 DEELAEFLAHYDLGELLSFEGIAAgIENTNYFV---TTTDG--RYVLTLFE--KRRSAAELPFELELLDHLAQAGLPVPR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288902  98 VCHTKGDNTASlvsvdsgsEIKSYLVRLLTYLPGRPIAELpvSPQLLYEIGKLAAKLDKTLQRFhhpKLSSLHRENFIWN 177
Cdd:cd05153   74 PLADKDGELLG--------ELNGKPAALFPFLPGESLTTP--TPEQCRAIGAALARLHLALAGF---PPPRPNPRGLAWW 140
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 134288902 178 LKNVPLLEKYLYALGQnRNREIVEHVIHLFKEEVMTKLSH 217
Cdd:cd05153  141 KPLAERLKARLDLLAA-DDRALLEDELARLQALAPSDLPR 179
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
36-201 3.62e-06

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: 46.34  E-value: 3.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288902   36 KVRPLPS-YDDQNFHVyvsktKDGPTEYVLKISNtkASKNPDLIEVQNHIIMFLKAAGFPTASVchtkgdntasLVSVDS 114
Cdd:pfam01636   1 TLRPISSgASNRTYLV-----TTGDGRYVLRLPP--PGRAAEELRRELALLRHLAAAGVPPVPR----------VLAGCT 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288902  115 GSEIKSYLVRLLTYLPGRPIAELPvSPQLLYEIGKLAAKLDKTLQRFHHPKLSSLHREnfIWNLKNVPLLEKYLYALGQN 194
Cdd:pfam01636  64 DAELLGLPFLLMEYLPGEVLARPL-LPEERGALLEALGRALARLHAVDPAALPLAGRL--ARLLELLRQLEAALARLLAA 140

                  ....*..
gi 134288902  195 RNREIVE 201
Cdd:pfam01636 141 ELLDRLE 147
 
Name Accession Description Interval E-value
PRK06148 PRK06148
hypothetical protein; Provisional
14-215 4.93e-25

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 102.41  E-value: 4.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288902   14 KPTFSEEQASALVESVFGLKVSkVRPLPSYDDQNFHVyvsKTKDGpTEYVLKISNtkASKNPDLIEVQNHIIMFLKAAGf 93
Cdd:PRK06148    8 APEFTTKDAEALLAQHFGISAT-ATPLDGERDLNFRL---TTDDG-ADYILKIVN--PSEPRVESDFQTAALDHLAAVA- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288902   94 PTASVCHTKGDNT-ASLVSVDSGSEiKSYLVRLLTYLPGRPIAEL-PVSPQLLYEIGKLAAKLDKTLQRFHHPklsSLHR 171
Cdd:PRK06148   80 PDLPVPRLIPSLSgASLASAQDPDG-EPRLLRLLSWLPGTPLAEAaPRTEALLDNLGRALGRLDRALQGFMHP---GALR 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 134288902  172 EnFIWNLKNVPLLEKYLYALGQNRNREIVEHVIHLFKEEVMTKL 215
Cdd:PRK06148  156 D-LDWDLRHAGRARDRLHFIDDPEDRALVERFLARFERNVAPRL 198
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
20-219 2.76e-20

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: 86.52  E-value: 2.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288902  20 EQASALVESvFGL-KVSKVRPLPSYDDQNFHVyvsKTKDGPtEYVLKISNtKASKNPDLIEVQNHIIMFLKAAGFPTASV 98
Cdd:COG2334    1 DELAAALER-YGLgPLSSLKPLNSGENRNYRV---ETEDGR-RYVLKLYR-PGRWSPEEIPFELALLAHLAAAGLPVPAP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288902  99 CHTKGDNTasLVsvdsgsEIKSYLVRLLTYLPGRPIAELpvSPQLLYEIGKLAAKLDKTLQRFHHPKLSSLHRenfiWNL 178
Cdd:COG2334   75 VPTRDGET--LL------ELEGRPAALFPFLPGRSPEEP--SPEQLEELGRLLARLHRALADFPRPNARDLAW----WDE 140
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 134288902 179 KNVPLLEKYLYALGQnrnREIVEHVIHLFKEEVMTKLSHFR 219
Cdd:COG2334  141 LLERLLGPLLPDPED---RALLEELLDRLEARLAPLLGALP 178
PRK06149 PRK06149
aminotransferase;
11-202 1.52e-18

aminotransferase;


Pssm-ID: 235716 [Multi-domain]  Cd Length: 972  Bit Score: 83.51  E-value: 1.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288902  11 ALSKPTFSEEQASALVESVFGLKvSKVRPLPSYDDQNFHVyvsktKDGPTEYVLKISNtkASKNPDLIEVQNHIIMFLKA 90
Cdd:PRK06149  11 SLPAPDVSEAQAERILAEHYGLS-GTLTELGSQQDRNFRV-----DSDGGRFVLKICH--AAYAAVELEAQHAALRHLAE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288902  91 A--GFPTASVCHTKgdNTASLVSVDSGSEikSYLVRLLTYLPGRPIAELP-VSPQLLYEIGKLAAKLDKTLQRFHHPkls 167
Cdd:PRK06149  83 RepALRVPVVIPAL--DGEELLTLDVRGQ--GLRVRLLDYLPGQPLTRLGhLAPASVAGLGALCARVARALADFDHP--- 155
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 134288902 168 SLHREnFIWNLKN-VPLLEKYLYALGQNRNREIVEH 202
Cdd:PRK06149 156 GLDRT-LQWDLRHaGPVVAHLLSHITDPAQRARIAE 190
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
19-217 6.24e-10

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: 57.65  E-value: 6.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288902  19 EEQASALVESVFGLKVSKVRPLPS-YDDQNFHVyvsKTKDGptEYVLKISNtkASKNPDLIEVQNHIIMFLKAAGFPTAS 97
Cdd:cd05153    1 DEELAEFLAHYDLGELLSFEGIAAgIENTNYFV---TTTDG--RYVLTLFE--KRRSAAELPFELELLDHLAQAGLPVPR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288902  98 VCHTKGDNTASlvsvdsgsEIKSYLVRLLTYLPGRPIAELpvSPQLLYEIGKLAAKLDKTLQRFhhpKLSSLHRENFIWN 177
Cdd:cd05153   74 PLADKDGELLG--------ELNGKPAALFPFLPGESLTTP--TPEQCRAIGAALARLHLALAGF---PPPRPNPRGLAWW 140
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 134288902 178 LKNVPLLEKYLYALGQnRNREIVEHVIHLFKEEVMTKLSH 217
Cdd:cd05153  141 KPLAERLKARLDLLAA-DDRALLEDELARLQALAPSDLPR 179
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
36-201 3.62e-06

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: 46.34  E-value: 3.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288902   36 KVRPLPS-YDDQNFHVyvsktKDGPTEYVLKISNtkASKNPDLIEVQNHIIMFLKAAGFPTASVchtkgdntasLVSVDS 114
Cdd:pfam01636   1 TLRPISSgASNRTYLV-----TTGDGRYVLRLPP--PGRAAEELRRELALLRHLAAAGVPPVPR----------VLAGCT 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288902  115 GSEIKSYLVRLLTYLPGRPIAELPvSPQLLYEIGKLAAKLDKTLQRFHHPKLSSLHREnfIWNLKNVPLLEKYLYALGQN 194
Cdd:pfam01636  64 DAELLGLPFLLMEYLPGEVLARPL-LPEERGALLEALGRALARLHAVDPAALPLAGRL--ARLLELLRQLEAALARLLAA 140

                  ....*..
gi 134288902  195 RNREIVE 201
Cdd:pfam01636 141 ELLDRLE 147
 
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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