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Conserved domains on  [gi|1819432840|ref|WP_165122183|]
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serine/threonine protein kinase [Proteus sp. ZN5]

Protein Classification

stress response kinase A( domain architecture ID 10013878)

stress response kinase A is involved in mediating the Cpx stress response pathway

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11768 PRK11768
serine/threonine protein kinase;
3-327 0e+00

serine/threonine protein kinase;


:

Pssm-ID: 236974 [Multi-domain]  Cd Length: 325  Bit Score: 557.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840   3 MSASFNFQGLSPDNIWDALVKIGFYPESGLTELNSYENRVFQFMDESRQRYVVKFYRPQRWSYEQIKEEHEFVLALKEAE 82
Cdd:PRK11768    2 NDSAFPFQTLTPDLILDALESLGLRVDGRLLALNSYENRVYQFGDEDGRRVVAKFYRPERWSDAQILEEHAFALELAEAE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840  83 VPVAAPLIINSETVHlSDDGFYFAIFPSIGGRAYETDNLFQLEEVGRTLGRIHQIGRKKSYEHRPTVSIAEYLIAPKLEF 162
Cdd:PRK11768   82 IPVVAPLAFNGQTLH-EHQGFRFALFPRRGGRAPELDNLDQLEWVGRFLGRIHQVGAKRPFEHRPTLDLQEYGIEPRDWL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840 163 ESSALVPNNLKPQFIEVIDKLIHDVRPRIEDSAWQILRLHGDCHPGNILWRDEVVMVDFDDSRMGPAVQDFWMLLNGSRQ 242
Cdd:PRK11768  161 LASDLIPSDLRPAYLAAADQLLAAVEACWARGDVRLLRLHGDCHPGNILWRDGPHFVDLDDARMGPAVQDLWMLLSGDRA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840 243 EQVMQLDTILESYYEYQDFDLRELSLIEPLRAMRMVQYLAWVLKRWNDPAFPRAFVWFQEQDFWFKQLALFKGQVEQLNE 322
Cdd:PRK11768  241 EQLMQLETLLEGYEEFCEFDPRELALIEPLRALRLIHYSAWLARRWDDPAFPKAFPWFGTEDYWEQQILELREQLAALQE 320

                  ....*
gi 1819432840 323 PPLQL 327
Cdd:PRK11768  321 PPLQL 325
 
Name Accession Description Interval E-value
PRK11768 PRK11768
serine/threonine protein kinase;
3-327 0e+00

serine/threonine protein kinase;


Pssm-ID: 236974 [Multi-domain]  Cd Length: 325  Bit Score: 557.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840   3 MSASFNFQGLSPDNIWDALVKIGFYPESGLTELNSYENRVFQFMDESRQRYVVKFYRPQRWSYEQIKEEHEFVLALKEAE 82
Cdd:PRK11768    2 NDSAFPFQTLTPDLILDALESLGLRVDGRLLALNSYENRVYQFGDEDGRRVVAKFYRPERWSDAQILEEHAFALELAEAE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840  83 VPVAAPLIINSETVHlSDDGFYFAIFPSIGGRAYETDNLFQLEEVGRTLGRIHQIGRKKSYEHRPTVSIAEYLIAPKLEF 162
Cdd:PRK11768   82 IPVVAPLAFNGQTLH-EHQGFRFALFPRRGGRAPELDNLDQLEWVGRFLGRIHQVGAKRPFEHRPTLDLQEYGIEPRDWL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840 163 ESSALVPNNLKPQFIEVIDKLIHDVRPRIEDSAWQILRLHGDCHPGNILWRDEVVMVDFDDSRMGPAVQDFWMLLNGSRQ 242
Cdd:PRK11768  161 LASDLIPSDLRPAYLAAADQLLAAVEACWARGDVRLLRLHGDCHPGNILWRDGPHFVDLDDARMGPAVQDLWMLLSGDRA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840 243 EQVMQLDTILESYYEYQDFDLRELSLIEPLRAMRMVQYLAWVLKRWNDPAFPRAFVWFQEQDFWFKQLALFKGQVEQLNE 322
Cdd:PRK11768  241 EQLMQLETLLEGYEEFCEFDPRELALIEPLRALRLIHYSAWLARRWDDPAFPKAFPWFGTEDYWEQQILELREQLAALQE 320

                  ....*
gi 1819432840 323 PPLQL 327
Cdd:PRK11768  321 PPLQL 325
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
15-295 2.07e-84

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: 256.78  E-value: 2.07e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840  15 DNIWDALVKIGFYPESGLTELNSYENRVFQFMDESRQRYVVKFYRPQRWSYEQIKEEHEFVLALKEAEVPVAAPLI-INS 93
Cdd:COG2334     1 DELAAALERYGLGPLSSLKPLNSGENRNYRVETEDGRRYVLKLYRPGRWSPEEIPFELALLAHLAAAGLPVPAPVPtRDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840  94 ETVHlSDDGFYFAIFPSIGGRAYETDNLFQLEEVGRTLGRIHQIGRkkSYEHRPTVSIAEYLIApklefESSALVPNNLK 173
Cdd:COG2334    81 ETLL-ELEGRPAALFPFLPGRSPEEPSPEQLEELGRLLARLHRALA--DFPRPNARDLAWWDEL-----LERLLGPLLPD 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840 174 PQFIEVIDKLIHDVRPRIED--SAWQILRLHGDCHPGNILWRDEVV--MVDFDDSRMGPAVQDFWMLLNGS--RQEQVMQ 247
Cdd:COG2334   153 PEDRALLEELLDRLEARLAPllGALPRGVIHGDLHPDNVLFDGDGVsgLIDFDDAGYGPRLYDLAIALNGWadGPLDPAR 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1819432840 248 LDTILESYYEYQDFDLRELSLIEPLRAMRMVQYLAWVLKRW--NDPAFPR 295
Cdd:COG2334   233 LAALLEGYRAVRPLTEAELAALPPLLRLRALRFLAWRLRRVraKDPAFER 282
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
38-266 3.55e-32

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: 119.91  E-value: 3.55e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840  38 YENRVFQFMDESRqRYVVKFYRPqRWSYEQIKEEHEFVLALKEAEVPvAAPLIINSETVHlSDDGFYFAIFPSIGGRAYE 117
Cdd:pfam01636   9 ASNRTYLVTTGDG-RYVLRLPPP-GRAAEELRRELALLRHLAAAGVP-PVPRVLAGCTDA-ELLGLPFLLMEYLPGEVLA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840 118 TDNL-----FQLEEVGRTLGRIHQIGRKK---SYEHRPTVSIAEYLIAPKLEFESSALvpnnlkPQFIEVIDKLIHDVRP 189
Cdd:pfam01636  85 RPLLpeergALLEALGRALARLHAVDPAAlplAGRLARLLELLRQLEAALARLLAAEL------LDRLEELEERLLAALL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840 190 RIEDSAWQILRLHGDCHPGNILWRDE---VVMVDFDDSRMGPAVQDFWMLLNGSRQEQVMQLDTILESYYEYQDFD-LRE 265
Cdd:pfam01636 159 ALLPAELPPVLVHGDLHPGNLLVDPGgrvSGVIDFEDAGLGDPAYDLAILLNSWGRELGAELLAAYLAAYGAFGYArLRE 238

                  .
gi 1819432840 266 L 266
Cdd:pfam01636 239 L 239
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
38-306 5.06e-20

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: 88.47  E-value: 5.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840  38 YENRVFqFMDESRQRYVVKFYRPQRwSYEQIKEEHEFVLALKEAEVPVAAPLI-INSETVHLSDdGFYFAIFPSIGGRAY 116
Cdd:cd05153    26 IENTNY-FVTTTDGRYVLTLFEKRR-SAAELPFELELLDHLAQAGLPVPRPLAdKDGELLGELN-GKPAALFPFLPGESL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840 117 ETDNLFQLEEVGRTLGRIHQIGRKKSYEHRPTVSIAEYLIapklefessalvpnnLKPQFIEVIDKLIHDVRPRIEDS-A 195
Cdd:cd05153   103 TTPTPEQCRAIGAALARLHLALAGFPPPRPNPRGLAWWKP---------------LAERLKARLDLLAADDRALLEDElA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840 196 WQILRL---------HGDCHPGNILWRDEVV--MVDFDDSRMGPAVQDFWMLLNGSRQEQVMQLDT-----ILESYYEYQ 259
Cdd:cd05153   168 RLQALApsdlprgviHADLFRDNVLFDGDRLsgIIDFYDACYDPLLYDLAIALNDWCFDDDGKLDPerakaLLAGYQSVR 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1819432840 260 DFDLRELSLIEPLRAMRMVQYLAWVLKRWNdpaFPRAFVWFQEQDFW 306
Cdd:cd05153   248 PLTEEEKAALPLLLRAAALRFWLSRLYDFH---LPREGALVTPKDPD 291
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
202-258 5.86e-06

ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases


Pssm-ID: 214734  Cd Length: 196  Bit Score: 46.17  E-value: 5.86e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1819432840  202 HGDCHPGNILWR-------DEVVMVDFDDSRMGPAVQDFWMLLNGS--RQEQVMQLDTILESYYEY 258
Cdd:smart00587 124 HGDLWANNIMFKyddegkpEDVALIDFQLSHYGSPAEDLHYFLLTSlsVEIRREHFDELLKFYYET 189
 
Name Accession Description Interval E-value
PRK11768 PRK11768
serine/threonine protein kinase;
3-327 0e+00

serine/threonine protein kinase;


Pssm-ID: 236974 [Multi-domain]  Cd Length: 325  Bit Score: 557.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840   3 MSASFNFQGLSPDNIWDALVKIGFYPESGLTELNSYENRVFQFMDESRQRYVVKFYRPQRWSYEQIKEEHEFVLALKEAE 82
Cdd:PRK11768    2 NDSAFPFQTLTPDLILDALESLGLRVDGRLLALNSYENRVYQFGDEDGRRVVAKFYRPERWSDAQILEEHAFALELAEAE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840  83 VPVAAPLIINSETVHlSDDGFYFAIFPSIGGRAYETDNLFQLEEVGRTLGRIHQIGRKKSYEHRPTVSIAEYLIAPKLEF 162
Cdd:PRK11768   82 IPVVAPLAFNGQTLH-EHQGFRFALFPRRGGRAPELDNLDQLEWVGRFLGRIHQVGAKRPFEHRPTLDLQEYGIEPRDWL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840 163 ESSALVPNNLKPQFIEVIDKLIHDVRPRIEDSAWQILRLHGDCHPGNILWRDEVVMVDFDDSRMGPAVQDFWMLLNGSRQ 242
Cdd:PRK11768  161 LASDLIPSDLRPAYLAAADQLLAAVEACWARGDVRLLRLHGDCHPGNILWRDGPHFVDLDDARMGPAVQDLWMLLSGDRA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840 243 EQVMQLDTILESYYEYQDFDLRELSLIEPLRAMRMVQYLAWVLKRWNDPAFPRAFVWFQEQDFWFKQLALFKGQVEQLNE 322
Cdd:PRK11768  241 EQLMQLETLLEGYEEFCEFDPRELALIEPLRALRLIHYSAWLARRWDDPAFPKAFPWFGTEDYWEQQILELREQLAALQE 320

                  ....*
gi 1819432840 323 PPLQL 327
Cdd:PRK11768  321 PPLQL 325
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
15-295 2.07e-84

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: 256.78  E-value: 2.07e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840  15 DNIWDALVKIGFYPESGLTELNSYENRVFQFMDESRQRYVVKFYRPQRWSYEQIKEEHEFVLALKEAEVPVAAPLI-INS 93
Cdd:COG2334     1 DELAAALERYGLGPLSSLKPLNSGENRNYRVETEDGRRYVLKLYRPGRWSPEEIPFELALLAHLAAAGLPVPAPVPtRDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840  94 ETVHlSDDGFYFAIFPSIGGRAYETDNLFQLEEVGRTLGRIHQIGRkkSYEHRPTVSIAEYLIApklefESSALVPNNLK 173
Cdd:COG2334    81 ETLL-ELEGRPAALFPFLPGRSPEEPSPEQLEELGRLLARLHRALA--DFPRPNARDLAWWDEL-----LERLLGPLLPD 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840 174 PQFIEVIDKLIHDVRPRIED--SAWQILRLHGDCHPGNILWRDEVV--MVDFDDSRMGPAVQDFWMLLNGS--RQEQVMQ 247
Cdd:COG2334   153 PEDRALLEELLDRLEARLAPllGALPRGVIHGDLHPDNVLFDGDGVsgLIDFDDAGYGPRLYDLAIALNGWadGPLDPAR 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1819432840 248 LDTILESYYEYQDFDLRELSLIEPLRAMRMVQYLAWVLKRW--NDPAFPR 295
Cdd:COG2334   233 LAALLEGYRAVRPLTEAELAALPPLLRLRALRFLAWRLRRVraKDPAFER 282
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
38-266 3.55e-32

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: 119.91  E-value: 3.55e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840  38 YENRVFQFMDESRqRYVVKFYRPqRWSYEQIKEEHEFVLALKEAEVPvAAPLIINSETVHlSDDGFYFAIFPSIGGRAYE 117
Cdd:pfam01636   9 ASNRTYLVTTGDG-RYVLRLPPP-GRAAEELRRELALLRHLAAAGVP-PVPRVLAGCTDA-ELLGLPFLLMEYLPGEVLA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840 118 TDNL-----FQLEEVGRTLGRIHQIGRKK---SYEHRPTVSIAEYLIAPKLEFESSALvpnnlkPQFIEVIDKLIHDVRP 189
Cdd:pfam01636  85 RPLLpeergALLEALGRALARLHAVDPAAlplAGRLARLLELLRQLEAALARLLAAEL------LDRLEELEERLLAALL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840 190 RIEDSAWQILRLHGDCHPGNILWRDE---VVMVDFDDSRMGPAVQDFWMLLNGSRQEQVMQLDTILESYYEYQDFD-LRE 265
Cdd:pfam01636 159 ALLPAELPPVLVHGDLHPGNLLVDPGgrvSGVIDFEDAGLGDPAYDLAILLNSWGRELGAELLAAYLAAYGAFGYArLRE 238

                  .
gi 1819432840 266 L 266
Cdd:pfam01636 239 L 239
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
38-306 5.06e-20

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: 88.47  E-value: 5.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840  38 YENRVFqFMDESRQRYVVKFYRPQRwSYEQIKEEHEFVLALKEAEVPVAAPLI-INSETVHLSDdGFYFAIFPSIGGRAY 116
Cdd:cd05153    26 IENTNY-FVTTTDGRYVLTLFEKRR-SAAELPFELELLDHLAQAGLPVPRPLAdKDGELLGELN-GKPAALFPFLPGESL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840 117 ETDNLFQLEEVGRTLGRIHQIGRKKSYEHRPTVSIAEYLIapklefessalvpnnLKPQFIEVIDKLIHDVRPRIEDS-A 195
Cdd:cd05153   103 TTPTPEQCRAIGAALARLHLALAGFPPPRPNPRGLAWWKP---------------LAERLKARLDLLAADDRALLEDElA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840 196 WQILRL---------HGDCHPGNILWRDEVV--MVDFDDSRMGPAVQDFWMLLNGSRQEQVMQLDT-----ILESYYEYQ 259
Cdd:cd05153   168 RLQALApsdlprgviHADLFRDNVLFDGDRLsgIIDFYDACYDPLLYDLAIALNDWCFDDDGKLDPerakaLLAGYQSVR 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1819432840 260 DFDLRELSLIEPLRAMRMVQYLAWVLKRWNdpaFPRAFVWFQEQDFW 306
Cdd:cd05153   248 PLTEEEKAALPLLLRAAALRFWLSRLYDFH---LPREGALVTPKDPD 291
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
40-257 1.17e-11

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 64.37  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840  40 NRVFQFmdESRQRYVVKFYRPQRWSYEQIKEEHEfVLALKEAEVPVAAPliinsETVHLSDD----GFYFAIFPSIGGRA 115
Cdd:COG3173    34 NLTYRL--DTGDRLVLRRPPRGLASAHDVRREAR-VLRALAPRLGVPVP-----RPLALGEDgeviGAPFYVMEWVEGET 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840 116 YeTDNLFQL---------EEVGRTLGRIHQI---------GRKKSYEHRPTVSIAEYLIAPKLEFESSALVpnnlkpqfi 177
Cdd:COG3173   106 L-EDALPDLspaerralaRALGEFLAALHAVdpaaagladGRPEGLERQLARWRAQLRRALARTDDLPALR--------- 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840 178 EVIDKLIHDVRPRIEDSAWqilrLHGDCHPGNILWRDE----VVMVDFDDSRMGPAVQDFWMLLNGSRQEQVM--QLDTI 251
Cdd:COG3173   176 ERLAAWLAANLPEWGPPVL----VHGDLRPGNLLVDPDdgrlTAVIDWELATLGDPAADLAYLLLYWRLPDDLlgPRAAF 251

                  ....*.
gi 1819432840 252 LESYYE 257
Cdd:COG3173   252 LAAYEE 257
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
172-312 9.48e-07

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 47.85  E-value: 9.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840 172 LKPQFIEVIDKLIHDVRPRIEDSAWQILRLHGDCHPGNILWRDE--VVMVDFDDSRMGPAVQDFWMLLNGSRQEQVmQLD 249
Cdd:COG0510    23 LGPRDLPELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTDDgrLYLIDWEYAGLGDPAFDLAALLVEYGLSPE-QAE 101
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1819432840 250 TILESYyeyqDFDLRELSLIEPLRAMRMVQYLAWVLkrWndpafpRAFVWFQEQDFWFKQLAL 312
Cdd:COG0510   102 ELLEAY----GFGRPTEELLRRLRAYRALADLLWAL--W------ALVRAAQEANGDLLKYLL 152
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
202-258 5.86e-06

ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases


Pssm-ID: 214734  Cd Length: 196  Bit Score: 46.17  E-value: 5.86e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1819432840  202 HGDCHPGNILWR-------DEVVMVDFDDSRMGPAVQDFWMLLNGS--RQEQVMQLDTILESYYEY 258
Cdd:smart00587 124 HGDLWANNIMFKyddegkpEDVALIDFQLSHYGSPAEDLHYFLLTSlsVEIRREHFDELLKFYYET 189
EcKL pfam02958
Ecdysteroid kinase-like family; This family includes ecdysteroid 22-kinase, an enzyme ...
202-257 1.39e-04

Ecdysteroid kinase-like family; This family includes ecdysteroid 22-kinase, an enzyme responsible for the phosphorylation of ecdysteroids (insect growth and moulting hormones) at C-22, to form physiologically inactive ecdysteroid 22-phosphates. Most insects contain 12 to 105 genes encoding this family and yet so far only one enzyme (ecdysteroid 22-kinase from Bombyx mori) has characterized substrates (2-deoxyecdysone, ecdysone, 20-hydroxyecdysone). There are good reasons to believe that this family includes kinases that act on other small molecule substrates and that they may function in detoxification processes.


Pssm-ID: 397213 [Multi-domain]  Cd Length: 293  Bit Score: 43.03  E-value: 1.39e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819432840 202 HGDCHPGNILWR-------DEVVMVDFDDSRMGPAVQDFWMLLNGSRQEQVM--QLDTILESYYE 257
Cdd:pfam02958 218 HGDLWVNNIMFKyddegepEDVILVDFQLSRYGSPAIDLNYFLYTSTELELRleHFDELLRYYHS 282
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
202-270 4.43e-04

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: 40.33  E-value: 4.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840 202 HGDCHPGNILWRDE-VVMVDFDDSRMGPAVQD----------FWMLLNGSRQEQVMQLdtILESYYEYQDFD--LRELSL 268
Cdd:COG3642    74 HGDLTTSNILVDDGgVYLIDFGLARYSDPLEDkavdlavlkrSLESTHPDPAEELWEA--FLEGYREVGPAEevLRRLRE 151

                  ..
gi 1819432840 269 IE 270
Cdd:COG3642   152 IE 153
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
201-239 4.87e-03

Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and Choline kinase; This subfamily is composed of uncharacterized bacterial proteins with similarity to APH and ChoK. Other APH/ChoK-like proteins include ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). These proteins catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates, such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides, and macrolides leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270704 [Multi-domain]  Cd Length: 234  Bit Score: 37.99  E-value: 4.87e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1819432840 201 LHGDCHPGNILWRDEVV--MVDFDDSRMG-PAVqDF---WMLLNG 239
Cdd:cd05155   166 LHGDLHPGNLLVRDGRLsaVIDFGDLGVGdPAC-DLaiaWTLFDA 209
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
38-228 5.74e-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: 36.90  E-value: 5.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840  38 YENRVFQFMDEsrQRYVVKFYRPQrwSYEQIKEEHEfVLALKEAEVPVAAPLIINSETvhlsDDGFYFAIFPSIGGRAYE 117
Cdd:cd05120    10 GDNKVYLLGDP--REYVLKIGPPR--LKKDLEKEAA-MLQLLAGKLSLPVPKVYGFGE----SDGWEYLLMERIEGETLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819432840 118 TDNLFQleevgrtlgrihqigrkkSYEHRPTV--SIAEYLIApklefessalvpnnlkpqfievidklIHdvrpRIEDSA 195
Cdd:cd05120    81 EVWPRL------------------SEEEKEKIadQLAEILAA--------------------------LH----RIDSSV 112
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1819432840 196 WqilrLHGDCHPGNILWRDE---VVMVDFDDSRMGP 228
Cdd:cd05120   113 L----THGDLHPGNILVKPDgklSGIIDWEFAGYGP 144
 
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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