NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|522141400|ref|WP_020652609|]
View 

serine/threonine protein kinase [Massilia niastensis]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK11768 PRK11768
serine/threonine protein kinase;
8-334 0e+00

serine/threonine protein kinase;


:

Pssm-ID: 236974 [Multi-domain]  Cd Length: 325  Bit Score: 599.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400   8 TDPPSHPFTRLDPQLVLEAVESVGLYGDGRLLALNSYENRVYRVGREEGPPVVVKFYRPQRWSDEAILEEHGFMAELADK 87
Cdd:PRK11768   1 MNDSAFPFQTLTPDLILDALESLGLRVDGRLLALNSYENRVYQFGDEDGRRVVAKFYRPERWSDAQILEEHAFALELAEA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400  88 EVPVVPAQVLDGRTLHAFEGFRFAVFASQGGRAPELGDPDTLEWLGRFIGRIHAVGAARPYAARPSLDPQTFGREPFDYL 167
Cdd:PRK11768  81 EIPVVAPLAFNGQTLHEHQGFRFALFPRRGGRAPELDNLDQLEWVGRFLGRIHQVGAKRPFEHRPTLDLQEYGIEPRDWL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400 168 RSHDFVPRELAATWASVVEQALGGVARCYERaGDLPLLRLHGDCHVGNVLWTaDGPHFVDFDDSRMGPAVQDLWMLLSGE 247
Cdd:PRK11768 161 LASDLIPSDLRPAYLAAADQLLAAVEACWAR-GDVRLLRLHGDCHPGNILWR-DGPHFVDLDDARMGPAVQDLWMLLSGD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400 248 RHEMVRQMGDVLAGYEDFCDFHPRQLYLVEALRTLRLIHYSAWLAMRWDDPAFPAAFPWFNTQRYWQDRILELREQVALM 327
Cdd:PRK11768 239 RAEQLMQLETLLEGYEEFCEFDPRELALIEPLRALRLIHYSAWLARRWDDPAFPKAFPWFGTEDYWEQQILELREQLAAL 318

                 ....*..
gi 522141400 328 DEPPLWP 334
Cdd:PRK11768 319 QEPPLQL 325
 
Name Accession Description Interval E-value
PRK11768 PRK11768
serine/threonine protein kinase;
8-334 0e+00

serine/threonine protein kinase;


Pssm-ID: 236974 [Multi-domain]  Cd Length: 325  Bit Score: 599.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400   8 TDPPSHPFTRLDPQLVLEAVESVGLYGDGRLLALNSYENRVYRVGREEGPPVVVKFYRPQRWSDEAILEEHGFMAELADK 87
Cdd:PRK11768   1 MNDSAFPFQTLTPDLILDALESLGLRVDGRLLALNSYENRVYQFGDEDGRRVVAKFYRPERWSDAQILEEHAFALELAEA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400  88 EVPVVPAQVLDGRTLHAFEGFRFAVFASQGGRAPELGDPDTLEWLGRFIGRIHAVGAARPYAARPSLDPQTFGREPFDYL 167
Cdd:PRK11768  81 EIPVVAPLAFNGQTLHEHQGFRFALFPRRGGRAPELDNLDQLEWVGRFLGRIHQVGAKRPFEHRPTLDLQEYGIEPRDWL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400 168 RSHDFVPRELAATWASVVEQALGGVARCYERaGDLPLLRLHGDCHVGNVLWTaDGPHFVDFDDSRMGPAVQDLWMLLSGE 247
Cdd:PRK11768 161 LASDLIPSDLRPAYLAAADQLLAAVEACWAR-GDVRLLRLHGDCHPGNILWR-DGPHFVDLDDARMGPAVQDLWMLLSGD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400 248 RHEMVRQMGDVLAGYEDFCDFHPRQLYLVEALRTLRLIHYSAWLAMRWDDPAFPAAFPWFNTQRYWQDRILELREQVALM 327
Cdd:PRK11768 239 RAEQLMQLETLLEGYEEFCEFDPRELALIEPLRALRLIHYSAWLARRWDDPAFPKAFPWFGTEDYWEQQILELREQLAAL 318

                 ....*..
gi 522141400 328 DEPPLWP 334
Cdd:PRK11768 319 QEPPLQL 325
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
21-322 1.25e-86

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: 262.55  E-value: 1.25e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400  21 QLVLEAVESVGLYGDGRLLALNSYENRVYRVGREEGPPVVVKFYRPQRWSDEAILEEHGFMAELADKEVPVVPAQV-LDG 99
Cdd:COG2334    1 DELAAALERYGLGPLSSLKPLNSGENRNYRVETEDGRRYVLKLYRPGRWSPEEIPFELALLAHLAAAGLPVPAPVPtRDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400 100 RTLHAFEGFRFAVFASQGGRAPELGDPDTLEWLGRFIGRIHAVGAarPYAARPSLDPQTFGrEPFDYLRShdfvPRELAA 179
Cdd:COG2334   81 ETLLELEGRPAALFPFLPGRSPEEPSPEQLEELGRLLARLHRALA--DFPRPNARDLAWWD-ELLERLLG----PLLPDP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400 180 TWASVVEQALGGVARCYERA-GDLPLLRLHGDCHVGNVLWTADG-PHFVDFDDSRMGPAVQDLWMLLSG--ERHEMVRQM 255
Cdd:COG2334  154 EDRALLEELLDRLEARLAPLlGALPRGVIHGDLHPDNVLFDGDGvSGLIDFDDAGYGPRLYDLAIALNGwaDGPLDPARL 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522141400 256 GDVLAGYEDFCDFHPRQLYLVEALRTLRLIHYSAWLAMRW--DDPAFPaafpwfntqRYWQDRILELRE 322
Cdd:COG2334  234 AALLEGYRAVRPLTEAELAALPPLLRLRALRFLAWRLRRVraKDPAFE---------RYLRRQIALAWA 293
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
44-265 1.67e-28

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: 110.28  E-value: 1.67e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400   44 YENRVYRVGREEGPpVVVKFYRPqRWSDEAILEEHGFMAELADKEVPVVPaQVLDGRTLHAFEGFRFAVFASQGGRAPEL 123
Cdd:pfam01636   9 ASNRTYLVTTGDGR-YVLRLPPP-GRAAEELRRELALLRHLAAAGVPPVP-RVLAGCTDAELLGLPFLLMEYLPGEVLAR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400  124 GDPDT-----LEWLGRFIGRIHAVgaarPYAARPSLDPQTFGREPFDYLrsHDFVPRELAATWASVVEQALGGVARCYER 198
Cdd:pfam01636  86 PLLPEergalLEALGRALARLHAV----DPAALPLAGRLARLLELLRQL--EAALARLLAAELLDRLEELEERLLAALLA 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522141400  199 --AGDLPLLRLHGDCHVGNVLWTADGPH--FVDFDDSRMGPAVQDLWMLL-SGERHEMVRQMGDVLAGYEDF 265
Cdd:pfam01636 160 llPAELPPVLVHGDLHPGNLLVDPGGRVsgVIDFEDAGLGDPAYDLAILLnSWGRELGAELLAAYLAAYGAF 231
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
33-263 2.28e-13

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: 69.59  E-value: 2.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400  33 YGDGRLLAL----NSYENRVYRVGREEGPpVVVKFYRPQRwSDEAILEEHGFMAELADKEVPV-VPAQVLDGRTLHAFEG 107
Cdd:cd05153   11 YDLGELLSFegiaAGIENTNYFVTTTDGR-YVLTLFEKRR-SAAELPFELELLDHLAQAGLPVpRPLADKDGELLGELNG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400 108 FRFAVFASQGGRAPELGDPDTLEWLGRFIGRIHAVGAARPYAARPSLDPQTFgREPFDYLRSHdfvpreLAATWASVVEQ 187
Cdd:cd05153   89 KPAALFPFLPGESLTTPTPEQCRAIGAALARLHLALAGFPPPRPNPRGLAWW-KPLAERLKAR------LDLLAADDRAL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400 188 ALGGVARcYERAGDLPLLR--LHGDCHVGNVLWTADG-PHFVDFDDSRMGPAVQDLWMLLSG-----ERHEMVRQMGDVL 259
Cdd:cd05153  162 LEDELAR-LQALAPSDLPRgvIHADLFRDNVLFDGDRlSGIIDFYDACYDPLLYDLAIALNDwcfddDGKLDPERAKALL 240

                 ....
gi 522141400 260 AGYE 263
Cdd:cd05153  241 AGYQ 244
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
208-251 2.43e-04

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


Pssm-ID: 214734  Cd Length: 196  Bit Score: 41.55  E-value: 2.43e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 522141400   208 HGDCHVGNVLWTADGPH------FVDFDDSRMGPAVQDLW----MLLSGE-RHEM 251
Cdd:smart00587 124 HGDLWANNIMFKYDDEGkpedvaLIDFQLSHYGSPAEDLHyfllTSLSVEiRREH 178
 
Name Accession Description Interval E-value
PRK11768 PRK11768
serine/threonine protein kinase;
8-334 0e+00

serine/threonine protein kinase;


Pssm-ID: 236974 [Multi-domain]  Cd Length: 325  Bit Score: 599.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400   8 TDPPSHPFTRLDPQLVLEAVESVGLYGDGRLLALNSYENRVYRVGREEGPPVVVKFYRPQRWSDEAILEEHGFMAELADK 87
Cdd:PRK11768   1 MNDSAFPFQTLTPDLILDALESLGLRVDGRLLALNSYENRVYQFGDEDGRRVVAKFYRPERWSDAQILEEHAFALELAEA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400  88 EVPVVPAQVLDGRTLHAFEGFRFAVFASQGGRAPELGDPDTLEWLGRFIGRIHAVGAARPYAARPSLDPQTFGREPFDYL 167
Cdd:PRK11768  81 EIPVVAPLAFNGQTLHEHQGFRFALFPRRGGRAPELDNLDQLEWVGRFLGRIHQVGAKRPFEHRPTLDLQEYGIEPRDWL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400 168 RSHDFVPRELAATWASVVEQALGGVARCYERaGDLPLLRLHGDCHVGNVLWTaDGPHFVDFDDSRMGPAVQDLWMLLSGE 247
Cdd:PRK11768 161 LASDLIPSDLRPAYLAAADQLLAAVEACWAR-GDVRLLRLHGDCHPGNILWR-DGPHFVDLDDARMGPAVQDLWMLLSGD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400 248 RHEMVRQMGDVLAGYEDFCDFHPRQLYLVEALRTLRLIHYSAWLAMRWDDPAFPAAFPWFNTQRYWQDRILELREQVALM 327
Cdd:PRK11768 239 RAEQLMQLETLLEGYEEFCEFDPRELALIEPLRALRLIHYSAWLARRWDDPAFPKAFPWFGTEDYWEQQILELREQLAAL 318

                 ....*..
gi 522141400 328 DEPPLWP 334
Cdd:PRK11768 319 QEPPLQL 325
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
21-322 1.25e-86

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: 262.55  E-value: 1.25e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400  21 QLVLEAVESVGLYGDGRLLALNSYENRVYRVGREEGPPVVVKFYRPQRWSDEAILEEHGFMAELADKEVPVVPAQV-LDG 99
Cdd:COG2334    1 DELAAALERYGLGPLSSLKPLNSGENRNYRVETEDGRRYVLKLYRPGRWSPEEIPFELALLAHLAAAGLPVPAPVPtRDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400 100 RTLHAFEGFRFAVFASQGGRAPELGDPDTLEWLGRFIGRIHAVGAarPYAARPSLDPQTFGrEPFDYLRShdfvPRELAA 179
Cdd:COG2334   81 ETLLELEGRPAALFPFLPGRSPEEPSPEQLEELGRLLARLHRALA--DFPRPNARDLAWWD-ELLERLLG----PLLPDP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400 180 TWASVVEQALGGVARCYERA-GDLPLLRLHGDCHVGNVLWTADG-PHFVDFDDSRMGPAVQDLWMLLSG--ERHEMVRQM 255
Cdd:COG2334  154 EDRALLEELLDRLEARLAPLlGALPRGVIHGDLHPDNVLFDGDGvSGLIDFDDAGYGPRLYDLAIALNGwaDGPLDPARL 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522141400 256 GDVLAGYEDFCDFHPRQLYLVEALRTLRLIHYSAWLAMRW--DDPAFPaafpwfntqRYWQDRILELRE 322
Cdd:COG2334  234 AALLEGYRAVRPLTEAELAALPPLLRLRALRFLAWRLRRVraKDPAFE---------RYLRRQIALAWA 293
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
44-265 1.67e-28

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: 110.28  E-value: 1.67e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400   44 YENRVYRVGREEGPpVVVKFYRPqRWSDEAILEEHGFMAELADKEVPVVPaQVLDGRTLHAFEGFRFAVFASQGGRAPEL 123
Cdd:pfam01636   9 ASNRTYLVTTGDGR-YVLRLPPP-GRAAEELRRELALLRHLAAAGVPPVP-RVLAGCTDAELLGLPFLLMEYLPGEVLAR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400  124 GDPDT-----LEWLGRFIGRIHAVgaarPYAARPSLDPQTFGREPFDYLrsHDFVPRELAATWASVVEQALGGVARCYER 198
Cdd:pfam01636  86 PLLPEergalLEALGRALARLHAV----DPAALPLAGRLARLLELLRQL--EAALARLLAAELLDRLEELEERLLAALLA 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522141400  199 --AGDLPLLRLHGDCHVGNVLWTADGPH--FVDFDDSRMGPAVQDLWMLL-SGERHEMVRQMGDVLAGYEDF 265
Cdd:pfam01636 160 llPAELPPVLVHGDLHPGNLLVDPGGRVsgVIDFEDAGLGDPAYDLAILLnSWGRELGAELLAAYLAAYGAF 231
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
33-263 2.28e-13

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: 69.59  E-value: 2.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400  33 YGDGRLLAL----NSYENRVYRVGREEGPpVVVKFYRPQRwSDEAILEEHGFMAELADKEVPV-VPAQVLDGRTLHAFEG 107
Cdd:cd05153   11 YDLGELLSFegiaAGIENTNYFVTTTDGR-YVLTLFEKRR-SAAELPFELELLDHLAQAGLPVpRPLADKDGELLGELNG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400 108 FRFAVFASQGGRAPELGDPDTLEWLGRFIGRIHAVGAARPYAARPSLDPQTFgREPFDYLRSHdfvpreLAATWASVVEQ 187
Cdd:cd05153   89 KPAALFPFLPGESLTTPTPEQCRAIGAALARLHLALAGFPPPRPNPRGLAWW-KPLAERLKAR------LDLLAADDRAL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400 188 ALGGVARcYERAGDLPLLR--LHGDCHVGNVLWTADG-PHFVDFDDSRMGPAVQDLWMLLSG-----ERHEMVRQMGDVL 259
Cdd:cd05153  162 LEDELAR-LQALAPSDLPRgvIHADLFRDNVLFDGDRlSGIIDFYDACYDPLLYDLAIALNDwcfddDGKLDPERAKALL 240

                 ....
gi 522141400 260 AGYE 263
Cdd:cd05153  241 AGYQ 244
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
46-264 3.12e-09

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 57.05  E-value: 3.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400  46 NRVYRVgrEEGPPVVVKFYRPQRWSDEAILEEHGFMAELADKEVPVVPAQVLDGRTlHAFEGFRFAVFASQGGRAPELGD 125
Cdd:COG3173   34 NLTYRL--DTGDRLVLRRPPRGLASAHDVRREARVLRALAPRLGVPVPRPLALGED-GEVIGAPFYVMEWVEGETLEDAL 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400 126 PDTLEW--------LGRFIGRIHAVGAARpyAARPSLDPQTFGREPFDYLRSHDFVPRElAATWASVVEQALGGVARCYE 197
Cdd:COG3173  111 PDLSPAerralaraLGEFLAALHAVDPAA--AGLADGRPEGLERQLARWRAQLRRALAR-TDDLPALRERLAAWLAANLP 187
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522141400 198 RAGDLPLLrlHGDCHVGNVLWTADGPHFV---DFDDSRMGPAVQDLWMLLS--GERHEMVRQMGDVLAGYED 264
Cdd:COG3173  188 EWGPPVLV--HGDLRPGNLLVDPDDGRLTaviDWELATLGDPAADLAYLLLywRLPDDLLGPRAAFLAAYEE 257
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
207-296 2.36e-05

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 44.00  E-value: 2.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400 207 LHGDCHVGNVLWTADG-PHFVDFDDSRMGPAVQDLWMLLSGERHEMvRQMGDVLAGYeDFCDFHPRQLYLVEALRTLRLI 285
Cdd:COG0510   52 CHGDLHPGNFLVTDDGrLYLIDWEYAGLGDPAFDLAALLVEYGLSP-EQAEELLEAY-GFGRPTEELLRRLRAYRALADL 129
                         90
                 ....*....|.
gi 522141400 286 HYSAWLAMRWD 296
Cdd:COG0510  130 LWALWALVRAA 140
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
45-258 5.60e-05

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: 43.76  E-value: 5.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400  45 ENRVYRVGREegppVVVKFYRpQRWSDEAILEEHGFMAELADKeVPV-VPAQVLDGRTLHAFEgFRFAVFASQGGRAPEL 123
Cdd:cd05155   11 DNATFRLGDD----LAVRLPR-RAWAAELLEKEQRWLPRLAPR-LPLpVPVPLALGKPGAGYP-WPWSVYRWLEGETAAD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400 124 GDPDTL----EWLGRFIGRIHAV---GAARPYAARP--SLDPQTFGREPFDYLRSHDFVPRELAATWasvvEQALGGVAR 194
Cdd:cd05155   84 APLADPaaaaEDLARFLAALHAIdpaGPPNPGRGNPlrGRDLAVRDAEEALAALAGLLDVAAARALW----ERALAAPAW 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522141400 195 cyeragDLPLLRLHGDCHVGNVLwTADG--PHFVDFDDSRMG-PAVqDL---WMLLSGERHEMVRQMGDV 258
Cdd:cd05155  160 ------AGPPVWLHGDLHPGNLL-VRDGrlSAVIDFGDLGVGdPAC-DLaiaWTLFDAAARAAFRAALGV 221
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
208-264 2.34e-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: 41.10  E-value: 2.34e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522141400 208 HGDCHVGNVLWTADGPHFVDFDDSRMGPAVQ----DLWML---LSGERHE-MVRQMGDVLAGYED 264
Cdd:COG3642   74 HGDLTTSNILVDDGGVYLIDFGLARYSDPLEdkavDLAVLkrsLESTHPDpAEELWEAFLEGYRE 138
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
208-251 2.43e-04

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


Pssm-ID: 214734  Cd Length: 196  Bit Score: 41.55  E-value: 2.43e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 522141400   208 HGDCHVGNVLWTADGPH------FVDFDDSRMGPAVQDLW----MLLSGE-RHEM 251
Cdd:smart00587 124 HGDLWANNIMFKYDDEGkpedvaLIDFQLSHYGSPAEDLHyfllTSLSVEiRREH 178
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH