NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|523664670|ref|WP_020796039|]
View 

MULTISPECIES: serine/threonine protein kinase [Pseudomonas]

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;
1-323 0e+00

serine/threonine protein kinase;


:

Pssm-ID: 236974 [Multi-domain]  Cd Length: 325  Bit Score: 630.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670   1 MAHPFETLTPDLVLDAVESIGFLSDARILALNSYENRVYQVGIEDAEPLIAKFYRPQRWTNEAILEEHQFTFELAEVEVP 80
Cdd:PRK11768   4 SAFPFQTLTPDLILDALESLGLRVDGRLLALNSYENRVYQFGDEDGRRVVAKFYRPERWSDAQILEEHAFALELAEAEIP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670  81 VVAPLIHNGETLHEHNGFRFTLFPRRGGRAPEPGNLDQLYRLGQLLGRLHAVGSTKPFEHREALAVKNFGHDSLTTLLEG 160
Cdd:PRK11768  84 VVAPLAFNGQTLHEHQGFRFALFPRRGGRAPELDNLDQLEWVGRFLGRIHQVGAKRPFEHRPTLDLQEYGIEPRDWLLAS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670 161 NFIPRSLLPAYESVARDLLKRVEDVYSNTPHQNIRMHGDCHPGNMMCRDEmFHIVDLDDCRMGPAVQDIWMMLAGDRQEC 240
Cdd:PRK11768 164 DLIPSDLRPAYLAAADQLLAAVEACWARGDVRLLRLHGDCHPGNILWRDG-PHFVDLDDARMGPAVQDLWMLLSGDRAEQ 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670 241 LGQLSELMDGYNEFHDFNPRELALIEPLRALRLMHYSAWLARRWDDPAFPRSFPWFGTERYWGDQVLALREQLAALNEEP 320
Cdd:PRK11768 243 LMQLETLLEGYEEFCEFDPRELALIEPLRALRLIHYSAWLARRWDDPAFPKAFPWFGTEDYWEQQILELREQLAALQEPP 322

                 ...
gi 523664670 321 LKL 323
Cdd:PRK11768 323 LQL 325
 
Name Accession Description Interval E-value
PRK11768 PRK11768
serine/threonine protein kinase;
1-323 0e+00

serine/threonine protein kinase;


Pssm-ID: 236974 [Multi-domain]  Cd Length: 325  Bit Score: 630.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670   1 MAHPFETLTPDLVLDAVESIGFLSDARILALNSYENRVYQVGIEDAEPLIAKFYRPQRWTNEAILEEHQFTFELAEVEVP 80
Cdd:PRK11768   4 SAFPFQTLTPDLILDALESLGLRVDGRLLALNSYENRVYQFGDEDGRRVVAKFYRPERWSDAQILEEHAFALELAEAEIP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670  81 VVAPLIHNGETLHEHNGFRFTLFPRRGGRAPEPGNLDQLYRLGQLLGRLHAVGSTKPFEHREALAVKNFGHDSLTTLLEG 160
Cdd:PRK11768  84 VVAPLAFNGQTLHEHQGFRFALFPRRGGRAPELDNLDQLEWVGRFLGRIHQVGAKRPFEHRPTLDLQEYGIEPRDWLLAS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670 161 NFIPRSLLPAYESVARDLLKRVEDVYSNTPHQNIRMHGDCHPGNMMCRDEmFHIVDLDDCRMGPAVQDIWMMLAGDRQEC 240
Cdd:PRK11768 164 DLIPSDLRPAYLAAADQLLAAVEACWARGDVRLLRLHGDCHPGNILWRDG-PHFVDLDDARMGPAVQDLWMLLSGDRAEQ 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670 241 LGQLSELMDGYNEFHDFNPRELALIEPLRALRLMHYSAWLARRWDDPAFPRSFPWFGTERYWGDQVLALREQLAALNEEP 320
Cdd:PRK11768 243 LMQLETLLEGYEEFCEFDPRELALIEPLRALRLIHYSAWLARRWDDPAFPKAFPWFGTEDYWEQQILELREQLAALQEPP 322

                 ...
gi 523664670 321 LKL 323
Cdd:PRK11768 323 LQL 325
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
11-315 5.21e-88

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: 265.64  E-value: 5.21e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670  11 DLVLDAVESIGFLSDARILALNSYENRVYQVGIEDAEPLIAKFYRPQRWTNEAILEEHQFTFELAEVEVPVVAPLI-HNG 89
Cdd:COG2334    1 DELAAALERYGLGPLSSLKPLNSGENRNYRVETEDGRRYVLKLYRPGRWSPEEIPFELALLAHLAAAGLPVPAPVPtRDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670  90 ETLHEHNGFRFTLFPRRGGRAPEPGNLDQLYRLGQLLGRLHAVGstKPFEHREALAVKNFghDSLTTLLEGNFIPRsllP 169
Cdd:COG2334   81 ETLLELEGRPAALFPFLPGRSPEEPSPEQLEELGRLLARLHRAL--ADFPRPNARDLAWW--DELLERLLGPLLPD---P 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670 170 AYESVARDLLKRVED----VYSNTPHQNIrmHGDCHPGNMMCR-DEMFHIVDLDDCRMGPAVQDIWMMLAG--DRQECLG 242
Cdd:COG2334  154 EDRALLEELLDRLEArlapLLGALPRGVI--HGDLHPDNVLFDgDGVSGLIDFDDAGYGPRLYDLAIALNGwaDGPLDPA 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523664670 243 QLSELMDGYNEFHDFNPRELALIEPLRALRLMHYSAWLARRW--DDPAFPrsfpwfgteRYWGDQVLALREQLAA 315
Cdd:COG2334  232 RLAALLEGYRAVRPLTEAELAALPPLLRLRALRFLAWRLRRVraKDPAFE---------RYLRRQIALAWAALEA 297
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
34-265 3.59e-25

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: 101.04  E-value: 3.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670   34 YENRVYQVGIEDAEpLIAKFYRPqRWTNEAILEEHQFTFELAEVEVPVVaPLIHNGETLHEHNGFRFTLFPRRGGRAPEP 113
Cdd:pfam01636   9 ASNRTYLVTTGDGR-YVLRLPPP-GRAAEELRRELALLRHLAAAGVPPV-PRVLAGCTDAELLGLPFLLMEYLPGEVLAR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670  114 GNLD-----QLYRLGQLLGRLHAVGSTK-PFEHREALAVKNFghdslttLLEGNFIPRSLLPAYESVARDLLKRVEDVYS 187
Cdd:pfam01636  86 PLLPeergaLLEALGRALARLHAVDPAAlPLAGRLARLLELL-------RQLEAALARLLAAELLDRLEELEERLLAALL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670  188 NTPH---QNIRMHGDCHPGNMM--CRDEMFHIVDLDDCRMGPAVQDIWMMLA-GDRQECLGQLSELMDGYnefHDFNPRE 261
Cdd:pfam01636 159 ALLPaelPPVLVHGDLHPGNLLvdPGGRVSGVIDFEDAGLGDPAYDLAILLNsWGRELGAELLAAYLAAY---GAFGYAR 235

                  ....
gi 523664670  262 LALI 265
Cdd:pfam01636 236 LREL 239
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
34-288 2.14e-17

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: 81.15  E-value: 2.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670  34 YENRVYQVGIEDAEpLIAKFYRPQRwTNEAILEEHQFTFELAEVEVPVVAPLI-HNGETLHEHNGFRFTLFPRRGGRAPE 112
Cdd:cd05153   26 IENTNYFVTTTDGR-YVLTLFEKRR-SAAELPFELELLDHLAQAGLPVPRPLAdKDGELLGELNGKPAALFPFLPGESLT 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670 113 PGNLDQLYRLGQLLGRLHAVGSTKPFEHREALavknfGHDSLTTLLE-GNFIPRSLLPAYESVARDLLKRVEDV-YSNTP 190
Cdd:cd05153  104 TPTPEQCRAIGAALARLHLALAGFPPPRPNPR-----GLAWWKPLAErLKARLDLLAADDRALLEDELARLQALaPSDLP 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670 191 HQNIrmHGDCHPGNMMCRDEMF-HIVDLDDCRMGPAVQDI------WMMLAGDRQEcLGQLSELMDGYNEFHDFNPRELA 263
Cdd:cd05153  179 RGVI--HADLFRDNVLFDGDRLsGIIDFYDACYDPLLYDLaialndWCFDDDGKLD-PERAKALLAGYQSVRPLTEEEKA 255
                        250       260
                 ....*....|....*....|....*
gi 523664670 264 LIEPLRALRLMHYSAWLARRWDDPA 288
Cdd:cd05153  256 ALPLLLRAAALRFWLSRLYDFHLPR 280
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
183-251 3.34e-03

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


Pssm-ID: 214734  Cd Length: 196  Bit Score: 38.08  E-value: 3.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670   183 EDVYSNTPHQNIRMHGDCHPGNMMCRDEMFH------IVDLDDCRMGPAVQDIWMMLAG-----DRQEclgQLSELMDGY 251
Cdd:smart00587 110 EDKEPDEGEFNVLNHGDLWANNIMFKYDDEGkpedvaLIDFQLSHYGSPAEDLHYFLLTslsveIRRE---HFDELLKFY 186
 
Name Accession Description Interval E-value
PRK11768 PRK11768
serine/threonine protein kinase;
1-323 0e+00

serine/threonine protein kinase;


Pssm-ID: 236974 [Multi-domain]  Cd Length: 325  Bit Score: 630.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670   1 MAHPFETLTPDLVLDAVESIGFLSDARILALNSYENRVYQVGIEDAEPLIAKFYRPQRWTNEAILEEHQFTFELAEVEVP 80
Cdd:PRK11768   4 SAFPFQTLTPDLILDALESLGLRVDGRLLALNSYENRVYQFGDEDGRRVVAKFYRPERWSDAQILEEHAFALELAEAEIP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670  81 VVAPLIHNGETLHEHNGFRFTLFPRRGGRAPEPGNLDQLYRLGQLLGRLHAVGSTKPFEHREALAVKNFGHDSLTTLLEG 160
Cdd:PRK11768  84 VVAPLAFNGQTLHEHQGFRFALFPRRGGRAPELDNLDQLEWVGRFLGRIHQVGAKRPFEHRPTLDLQEYGIEPRDWLLAS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670 161 NFIPRSLLPAYESVARDLLKRVEDVYSNTPHQNIRMHGDCHPGNMMCRDEmFHIVDLDDCRMGPAVQDIWMMLAGDRQEC 240
Cdd:PRK11768 164 DLIPSDLRPAYLAAADQLLAAVEACWARGDVRLLRLHGDCHPGNILWRDG-PHFVDLDDARMGPAVQDLWMLLSGDRAEQ 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670 241 LGQLSELMDGYNEFHDFNPRELALIEPLRALRLMHYSAWLARRWDDPAFPRSFPWFGTERYWGDQVLALREQLAALNEEP 320
Cdd:PRK11768 243 LMQLETLLEGYEEFCEFDPRELALIEPLRALRLIHYSAWLARRWDDPAFPKAFPWFGTEDYWEQQILELREQLAALQEPP 322

                 ...
gi 523664670 321 LKL 323
Cdd:PRK11768 323 LQL 325
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
11-315 5.21e-88

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: 265.64  E-value: 5.21e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670  11 DLVLDAVESIGFLSDARILALNSYENRVYQVGIEDAEPLIAKFYRPQRWTNEAILEEHQFTFELAEVEVPVVAPLI-HNG 89
Cdd:COG2334    1 DELAAALERYGLGPLSSLKPLNSGENRNYRVETEDGRRYVLKLYRPGRWSPEEIPFELALLAHLAAAGLPVPAPVPtRDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670  90 ETLHEHNGFRFTLFPRRGGRAPEPGNLDQLYRLGQLLGRLHAVGstKPFEHREALAVKNFghDSLTTLLEGNFIPRsllP 169
Cdd:COG2334   81 ETLLELEGRPAALFPFLPGRSPEEPSPEQLEELGRLLARLHRAL--ADFPRPNARDLAWW--DELLERLLGPLLPD---P 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670 170 AYESVARDLLKRVED----VYSNTPHQNIrmHGDCHPGNMMCR-DEMFHIVDLDDCRMGPAVQDIWMMLAG--DRQECLG 242
Cdd:COG2334  154 EDRALLEELLDRLEArlapLLGALPRGVI--HGDLHPDNVLFDgDGVSGLIDFDDAGYGPRLYDLAIALNGwaDGPLDPA 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523664670 243 QLSELMDGYNEFHDFNPRELALIEPLRALRLMHYSAWLARRW--DDPAFPrsfpwfgteRYWGDQVLALREQLAA 315
Cdd:COG2334  232 RLAALLEGYRAVRPLTEAELAALPPLLRLRALRFLAWRLRRVraKDPAFE---------RYLRRQIALAWAALEA 297
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
34-265 3.59e-25

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: 101.04  E-value: 3.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670   34 YENRVYQVGIEDAEpLIAKFYRPqRWTNEAILEEHQFTFELAEVEVPVVaPLIHNGETLHEHNGFRFTLFPRRGGRAPEP 113
Cdd:pfam01636   9 ASNRTYLVTTGDGR-YVLRLPPP-GRAAEELRRELALLRHLAAAGVPPV-PRVLAGCTDAELLGLPFLLMEYLPGEVLAR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670  114 GNLD-----QLYRLGQLLGRLHAVGSTK-PFEHREALAVKNFghdslttLLEGNFIPRSLLPAYESVARDLLKRVEDVYS 187
Cdd:pfam01636  86 PLLPeergaLLEALGRALARLHAVDPAAlPLAGRLARLLELL-------RQLEAALARLLAAELLDRLEELEERLLAALL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670  188 NTPH---QNIRMHGDCHPGNMM--CRDEMFHIVDLDDCRMGPAVQDIWMMLA-GDRQECLGQLSELMDGYnefHDFNPRE 261
Cdd:pfam01636 159 ALLPaelPPVLVHGDLHPGNLLvdPGGRVSGVIDFEDAGLGDPAYDLAILLNsWGRELGAELLAAYLAAY---GAFGYAR 235

                  ....
gi 523664670  262 LALI 265
Cdd:pfam01636 236 LREL 239
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
34-288 2.14e-17

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: 81.15  E-value: 2.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670  34 YENRVYQVGIEDAEpLIAKFYRPQRwTNEAILEEHQFTFELAEVEVPVVAPLI-HNGETLHEHNGFRFTLFPRRGGRAPE 112
Cdd:cd05153   26 IENTNYFVTTTDGR-YVLTLFEKRR-SAAELPFELELLDHLAQAGLPVPRPLAdKDGELLGELNGKPAALFPFLPGESLT 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670 113 PGNLDQLYRLGQLLGRLHAVGSTKPFEHREALavknfGHDSLTTLLE-GNFIPRSLLPAYESVARDLLKRVEDV-YSNTP 190
Cdd:cd05153  104 TPTPEQCRAIGAALARLHLALAGFPPPRPNPR-----GLAWWKPLAErLKARLDLLAADDRALLEDELARLQALaPSDLP 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670 191 HQNIrmHGDCHPGNMMCRDEMF-HIVDLDDCRMGPAVQDI------WMMLAGDRQEcLGQLSELMDGYNEFHDFNPRELA 263
Cdd:cd05153  179 RGVI--HADLFRDNVLFDGDRLsGIIDFYDACYDPLLYDLaialndWCFDDDGKLD-PERAKALLAGYQSVRPLTEEEKA 255
                        250       260
                 ....*....|....*....|....*
gi 523664670 264 LIEPLRALRLMHYSAWLARRWDDPA 288
Cdd:cd05153  256 ALPLLLRAAALRFWLSRLYDFHLPR 280
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
6-253 8.65e-07

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 49.73  E-value: 8.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670   6 ETLTPDLVLDAVES--IGFLSDARILALNS-YENRVYQVgiEDAEPLIAKFYRPQRWTNEAILEEHQFTFELAEVEVPVV 82
Cdd:COG3173    1 EELDEAALRALLAAqlPGLAGLPEVEPLSGgWSNLTYRL--DTGDRLVLRRPPRGLASAHDVRREARVLRALAPRLGVPV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670  83 APLIHNGETlHEHNGFRFTLFPRRGGRAPE-------PGNLDQLYR-LGQLLGRLHAV-------GSTKPFEHREALavk 147
Cdd:COG3173   79 PRPLALGED-GEVIGAPFYVMEWVEGETLEdalpdlsPAERRALARaLGEFLAALHAVdpaaaglADGRPEGLERQL--- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670 148 nfghDSLTTLLEGNFIPRSLLPAYESVARDLLKRVEDVysntPHQNIRMHGDCHPGNMMCRDEMFHIV---DLDDCRMGP 224
Cdd:COG3173  155 ----ARWRAQLRRALARTDDLPALRERLAAWLAANLPE----WGPPVLVHGDLRPGNLLVDPDDGRLTaviDWELATLGD 226
                        250       260       270
                 ....*....|....*....|....*....|.
gi 523664670 225 AVQDIWMMLAGDRQ--ECLGQLSELMDGYNE 253
Cdd:COG3173  227 PAADLAYLLLYWRLpdDLLGPRAAFLAAYEE 257
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
177-285 5.50e-04

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 39.76  E-value: 5.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670 177 DLLKRVEDVYSNTPHQNIRM---HGDCHPGNMMCRDE-MFHIVDLDDCRMGPAVQDIWMMLAG---DRQeclgQLSELMD 249
Cdd:COG0510   30 ELLRRLEELERALAARPLPLvlcHGDLHPGNFLVTDDgRLYLIDWEYAGLGDPAFDLAALLVEyglSPE----QAEELLE 105
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 523664670 250 GYNeFHDFNPRELALIEPLRALRLMHYSAWLARRWD 285
Cdd:COG0510  106 AYG-FGRPTEELLRRLRAYRALADLLWALWALVRAA 140
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
183-251 3.34e-03

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


Pssm-ID: 214734  Cd Length: 196  Bit Score: 38.08  E-value: 3.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523664670   183 EDVYSNTPHQNIRMHGDCHPGNMMCRDEMFH------IVDLDDCRMGPAVQDIWMMLAG-----DRQEclgQLSELMDGY 251
Cdd:smart00587 110 EDKEPDEGEFNVLNHGDLWANNIMFKYDDEGkpedvaLIDFQLSHYGSPAEDLHYFLLTslsveIRRE---HFDELLKFY 186
 
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