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Conserved domains on  [gi|521080697|ref|WP_020411604|]
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serine/threonine protein kinase [Microbulbifer variabilis]

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;
1-325 0e+00

serine/threonine protein kinase;


:

Pssm-ID: 236974 [Multi-domain]  Cd Length: 325  Bit Score: 565.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697   1 MAQNHHPYEALTPDVVIDCVESSGLVSDARIFPLNSYENRVYQVGIEGTEPLIAKFYRPDRWSDQQILEEHQFTLELAEE 80
Cdd:PRK11768   1 MNDSAFPFQTLTPDLILDALESLGLRVDGRLLALNSYENRVYQFGDEDGRRVVAKFYRPERWSDAQILEEHAFALELAEA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697  81 EIPVVAPLQFDGRTLLESQGFRFALFPRRGGRQLEMDNFDHLEQVGTMLGRIHAVGSAKPFSHRPSLTLQHFAIDSREFI 160
Cdd:PRK11768  81 EIPVVAPLAFNGQTLHEHQGFRFALFPRRGGRAPELDNLDQLEWVGRFLGRIHQVGAKRPFEHRPTLDLQEYGIEPRDWL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697 161 LGGDFLPLENREAYASVTGHIIEQVAPLFER-DWDLLRLHGDCHSGNFLWRdDTPWFVDLDDCLMGPAIQDIWMLISGNR 239
Cdd:PRK11768 161 LASDLIPSDLRPAYLAAADQLLAAVEACWARgDVRLLRLHGDCHPGNILWR-DGPHFVDLDDARMGPAVQDLWMLLSGDR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697 240 AEQTAYLDTVLEGYETFYRFDPQQLQLVEPLRCLRQMHHAAWLARRWQDPAFPQAFPWFNTARYWAEHILALREQQSALL 319
Cdd:PRK11768 240 AEQLMQLETLLEGYEEFCEFDPRELALIEPLRALRLIHYSAWLARRWDDPAFPKAFPWFGTEDYWEQQILELREQLAALQ 319

                 ....*.
gi 521080697 320 EPPLTL 325
Cdd:PRK11768 320 EPPLQL 325
 
Name Accession Description Interval E-value
PRK11768 PRK11768
serine/threonine protein kinase;
1-325 0e+00

serine/threonine protein kinase;


Pssm-ID: 236974 [Multi-domain]  Cd Length: 325  Bit Score: 565.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697   1 MAQNHHPYEALTPDVVIDCVESSGLVSDARIFPLNSYENRVYQVGIEGTEPLIAKFYRPDRWSDQQILEEHQFTLELAEE 80
Cdd:PRK11768   1 MNDSAFPFQTLTPDLILDALESLGLRVDGRLLALNSYENRVYQFGDEDGRRVVAKFYRPERWSDAQILEEHAFALELAEA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697  81 EIPVVAPLQFDGRTLLESQGFRFALFPRRGGRQLEMDNFDHLEQVGTMLGRIHAVGSAKPFSHRPSLTLQHFAIDSREFI 160
Cdd:PRK11768  81 EIPVVAPLAFNGQTLHEHQGFRFALFPRRGGRAPELDNLDQLEWVGRFLGRIHQVGAKRPFEHRPTLDLQEYGIEPRDWL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697 161 LGGDFLPLENREAYASVTGHIIEQVAPLFER-DWDLLRLHGDCHSGNFLWRdDTPWFVDLDDCLMGPAIQDIWMLISGNR 239
Cdd:PRK11768 161 LASDLIPSDLRPAYLAAADQLLAAVEACWARgDVRLLRLHGDCHPGNILWR-DGPHFVDLDDARMGPAVQDLWMLLSGDR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697 240 AEQTAYLDTVLEGYETFYRFDPQQLQLVEPLRCLRQMHHAAWLARRWQDPAFPQAFPWFNTARYWAEHILALREQQSALL 319
Cdd:PRK11768 240 AEQLMQLETLLEGYEEFCEFDPRELALIEPLRALRLIHYSAWLARRWDDPAFPKAFPWFGTEDYWEQQILELREQLAALQ 319

                 ....*.
gi 521080697 320 EPPLTL 325
Cdd:PRK11768 320 EPPLQL 325
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
14-313 4.46e-83

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: 253.31  E-value: 4.46e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697  14 DVVIDCVESSGLVSDARIFPLNSYENRVYQVGIEGTEPLIAKFYRPDRWSDQQILEEHQFTLELAEEEIPVVAPL-QFDG 92
Cdd:COG2334    1 DELAAALERYGLGPLSSLKPLNSGENRNYRVETEDGRRYVLKLYRPGRWSPEEIPFELALLAHLAAAGLPVPAPVpTRDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697  93 RTLLESQGFRFALFPRRGGRQLEMDNFDHLEQVGTMLGRIHAVGsaKPFSHRPSLTLQHFaIDSREFILGgdflPLENRE 172
Cdd:COG2334   81 ETLLELEGRPAALFPFLPGRSPEEPSPEQLEELGRLLARLHRAL--ADFPRPNARDLAWW-DELLERLLG----PLLPDP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697 173 AYASVTGHIIEQVAPLFERDWDLLR---LHGDCHSGNFLWRDDT-PWFVDLDDCLMGPAIQDIWMLISG--NRAEQTAYL 246
Cdd:COG2334  154 EDRALLEELLDRLEARLAPLLGALPrgvIHGDLHPDNVLFDGDGvSGLIDFDDAGYGPRLYDLAIALNGwaDGPLDPARL 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521080697 247 DTVLEGYETFYRFDPQQLQLVEPLRCLRQMHHAAWLARRWQ--DPAFPqafpwfntaRYWAEHILALRE 313
Cdd:COG2334  234 AALLEGYRAVRPLTEAELAALPPLLRLRALRFLAWRLRRVRakDPAFE---------RYLRRQIALAWA 293
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
37-258 3.00e-26

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: 104.12  E-value: 3.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697   37 YENRVYQVGIEGtEPLIAKFYRPdRWSDQQILEEHQFTLELAEEEIPVVaPLQFDGRTLLESQGFRFALFPRRGGRQLEM 116
Cdd:pfam01636   9 ASNRTYLVTTGD-GRYVLRLPPP-GRAAEELRRELALLRHLAAAGVPPV-PRVLAGCTDAELLGLPFLLMEYLPGEVLAR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697  117 DNFDH-----LEQVGTMLGRIHAVGSAK-PFSHRPSLTLQHFAIDSREFILGgdfLPLENREAYASVTGHIIEQVAPLFE 190
Cdd:pfam01636  86 PLLPEergalLEALGRALARLHAVDPAAlPLAGRLARLLELLRQLEAALARL---LAAELLDRLEELEERLLAALLALLP 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521080697  191 RDWDLLRLHGDCHSGNFLWRDDTPW--FVDLDDCLMGPAIQDIWMLISGNRAEQTA-YLDTVLEGYETFYR 258
Cdd:pfam01636 163 AELPPVLVHGDLHPGNLLVDPGGRVsgVIDFEDAGLGDPAYDLAILLNSWGRELGAeLLAAYLAAYGAFGY 233
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
37-255 3.60e-11

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: 63.05  E-value: 3.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697  37 YENRVYqvGIEGTE-PLIAKFYRPDRwSDQQILEEHQFTLELAEEEIPVVAPLQ-FDGRTLLESQGFRFALFPRRGGRQL 114
Cdd:cd05153   26 IENTNY--FVTTTDgRYVLTLFEKRR-SAAELPFELELLDHLAQAGLPVPRPLAdKDGELLGELNGKPAALFPFLPGESL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697 115 EMDNFDHLEQVGTMLGRIHAVGSAKPFSHRPSLTLQHFAidsrefILGGDFLPLENREAyASVTGHIIEQVAPLFERDWD 194
Cdd:cd05153  103 TTPTPEQCRAIGAALARLHLALAGFPPPRPNPRGLAWWK------PLAERLKARLDLLA-ADDRALLEDELARLQALAPS 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697 195 LLR---LHGDCHSGNFLWRDD-TPWFVDLDDCLMGPAIQDIWMLISGNRAEQTAYLDTV-----LEGYET 255
Cdd:cd05153  176 DLPrgvIHADLFRDNVLFDGDrLSGIIDFYDACYDPLLYDLAIALNDWCFDDDGKLDPErakalLAGYQS 245
 
Name Accession Description Interval E-value
PRK11768 PRK11768
serine/threonine protein kinase;
1-325 0e+00

serine/threonine protein kinase;


Pssm-ID: 236974 [Multi-domain]  Cd Length: 325  Bit Score: 565.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697   1 MAQNHHPYEALTPDVVIDCVESSGLVSDARIFPLNSYENRVYQVGIEGTEPLIAKFYRPDRWSDQQILEEHQFTLELAEE 80
Cdd:PRK11768   1 MNDSAFPFQTLTPDLILDALESLGLRVDGRLLALNSYENRVYQFGDEDGRRVVAKFYRPERWSDAQILEEHAFALELAEA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697  81 EIPVVAPLQFDGRTLLESQGFRFALFPRRGGRQLEMDNFDHLEQVGTMLGRIHAVGSAKPFSHRPSLTLQHFAIDSREFI 160
Cdd:PRK11768  81 EIPVVAPLAFNGQTLHEHQGFRFALFPRRGGRAPELDNLDQLEWVGRFLGRIHQVGAKRPFEHRPTLDLQEYGIEPRDWL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697 161 LGGDFLPLENREAYASVTGHIIEQVAPLFER-DWDLLRLHGDCHSGNFLWRdDTPWFVDLDDCLMGPAIQDIWMLISGNR 239
Cdd:PRK11768 161 LASDLIPSDLRPAYLAAADQLLAAVEACWARgDVRLLRLHGDCHPGNILWR-DGPHFVDLDDARMGPAVQDLWMLLSGDR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697 240 AEQTAYLDTVLEGYETFYRFDPQQLQLVEPLRCLRQMHHAAWLARRWQDPAFPQAFPWFNTARYWAEHILALREQQSALL 319
Cdd:PRK11768 240 AEQLMQLETLLEGYEEFCEFDPRELALIEPLRALRLIHYSAWLARRWDDPAFPKAFPWFGTEDYWEQQILELREQLAALQ 319

                 ....*.
gi 521080697 320 EPPLTL 325
Cdd:PRK11768 320 EPPLQL 325
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
14-313 4.46e-83

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: 253.31  E-value: 4.46e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697  14 DVVIDCVESSGLVSDARIFPLNSYENRVYQVGIEGTEPLIAKFYRPDRWSDQQILEEHQFTLELAEEEIPVVAPL-QFDG 92
Cdd:COG2334    1 DELAAALERYGLGPLSSLKPLNSGENRNYRVETEDGRRYVLKLYRPGRWSPEEIPFELALLAHLAAAGLPVPAPVpTRDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697  93 RTLLESQGFRFALFPRRGGRQLEMDNFDHLEQVGTMLGRIHAVGsaKPFSHRPSLTLQHFaIDSREFILGgdflPLENRE 172
Cdd:COG2334   81 ETLLELEGRPAALFPFLPGRSPEEPSPEQLEELGRLLARLHRAL--ADFPRPNARDLAWW-DELLERLLG----PLLPDP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697 173 AYASVTGHIIEQVAPLFERDWDLLR---LHGDCHSGNFLWRDDT-PWFVDLDDCLMGPAIQDIWMLISG--NRAEQTAYL 246
Cdd:COG2334  154 EDRALLEELLDRLEARLAPLLGALPrgvIHGDLHPDNVLFDGDGvSGLIDFDDAGYGPRLYDLAIALNGwaDGPLDPARL 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521080697 247 DTVLEGYETFYRFDPQQLQLVEPLRCLRQMHHAAWLARRWQ--DPAFPqafpwfntaRYWAEHILALRE 313
Cdd:COG2334  234 AALLEGYRAVRPLTEAELAALPPLLRLRALRFLAWRLRRVRakDPAFE---------RYLRRQIALAWA 293
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
37-258 3.00e-26

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: 104.12  E-value: 3.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697   37 YENRVYQVGIEGtEPLIAKFYRPdRWSDQQILEEHQFTLELAEEEIPVVaPLQFDGRTLLESQGFRFALFPRRGGRQLEM 116
Cdd:pfam01636   9 ASNRTYLVTTGD-GRYVLRLPPP-GRAAEELRRELALLRHLAAAGVPPV-PRVLAGCTDAELLGLPFLLMEYLPGEVLAR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697  117 DNFDH-----LEQVGTMLGRIHAVGSAK-PFSHRPSLTLQHFAIDSREFILGgdfLPLENREAYASVTGHIIEQVAPLFE 190
Cdd:pfam01636  86 PLLPEergalLEALGRALARLHAVDPAAlPLAGRLARLLELLRQLEAALARL---LAAELLDRLEELEERLLAALLALLP 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521080697  191 RDWDLLRLHGDCHSGNFLWRDDTPW--FVDLDDCLMGPAIQDIWMLISGNRAEQTA-YLDTVLEGYETFYR 258
Cdd:pfam01636 163 AELPPVLVHGDLHPGNLLVDPGGRVsgVIDFEDAGLGDPAYDLAILLNSWGRELGAeLLAAYLAAYGAFGY 233
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
37-255 3.60e-11

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: 63.05  E-value: 3.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697  37 YENRVYqvGIEGTE-PLIAKFYRPDRwSDQQILEEHQFTLELAEEEIPVVAPLQ-FDGRTLLESQGFRFALFPRRGGRQL 114
Cdd:cd05153   26 IENTNY--FVTTTDgRYVLTLFEKRR-SAAELPFELELLDHLAQAGLPVPRPLAdKDGELLGELNGKPAALFPFLPGESL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697 115 EMDNFDHLEQVGTMLGRIHAVGSAKPFSHRPSLTLQHFAidsrefILGGDFLPLENREAyASVTGHIIEQVAPLFERDWD 194
Cdd:cd05153  103 TTPTPEQCRAIGAALARLHLALAGFPPPRPNPRGLAWWK------PLAERLKARLDLLA-ADDRALLEDELARLQALAPS 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697 195 LLR---LHGDCHSGNFLWRDD-TPWFVDLDDCLMGPAIQDIWMLISGNRAEQTAYLDTV-----LEGYET 255
Cdd:cd05153  176 DLPrgvIHADLFRDNVLFDGDrLSGIIDFYDACYDPLLYDLAIALNDWCFDDDGKLDPErakalLAGYQS 245
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
198-287 3.60e-06

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 46.31  E-value: 3.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697 198 LHGDCHSGNFLWRDD-TPWFVDLDDCLMGPAIQDIWMLISGNRAEQTAYlDTVLEGYEtFYRFDPQQLQLVEPLRCLRQM 276
Cdd:COG0510   52 CHGDLHPGNFLVTDDgRLYLIDWEYAGLGDPAFDLAALLVEYGLSPEQA-EELLEAYG-FGRPTEELLRRLRAYRALADL 129
                         90
                 ....*....|.
gi 521080697 277 HHAAWLARRWQ 287
Cdd:COG0510  130 LWALWALVRAA 140
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
199-271 4.86e-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: 39.94  E-value: 4.86e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521080697 199 HGDCHSGNFLWRDDTPWFVDLDDCLMGPAIQ----DIWMLISGNRAEQTAYLDTVLEGYETFYRFDPQQLQLVEPLR 271
Cdd:COG3642   74 HGDLTTSNILVDDGGVYLIDFGLARYSDPLEdkavDLAVLKRSLESTHPDPAEELWEAFLEGYREVGPAEEVLRRLR 150
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
9-254 3.58e-03

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 38.56  E-value: 3.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697   9 EALTPDVVIDCVES--SGLVSDARIFPLNS-YENRVYQVGIEgtEPLIAKFYRPDRWSDQQILEEHQFTLELAEE-EIPV 84
Cdd:COG3173    1 EELDEAALRALLAAqlPGLAGLPEVEPLSGgWSNLTYRLDTG--DRLVLRRPPRGLASAHDVRREARVLRALAPRlGVPV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697  85 VAPLQFDGRTllESQGFRFALFPRRGGRQLEmDNFDHL---------EQVGTMLGRIHAV--GSAKPFSHRPSLTLQHFA 153
Cdd:COG3173   79 PRPLALGEDG--EVIGAPFYVMEWVEGETLE-DALPDLspaerralaRALGEFLAALHAVdpAAAGLADGRPEGLERQLA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521080697 154 IDSREfilggdflpLENREAYASVTGHIIEQVAPLFERDWDLLR----LHGDCHSGNFLWRDDTP---WFVDLDDCLMGP 226
Cdd:COG3173  156 RWRAQ---------LRRALARTDDLPALRERLAAWLAANLPEWGppvlVHGDLRPGNLLVDPDDGrltAVIDWELATLGD 226
                        250       260       270
                 ....*....|....*....|....*....|
gi 521080697 227 AIQDI-WMLISGNRAEQTA-YLDTVLEGYE 254
Cdd:COG3173  227 PAADLaYLLLYWRLPDDLLgPRAAFLAAYE 256
 
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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