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Conserved domains on  [gi|446988260|ref|WP_001065516|]
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MULTISPECIES: stress response kinase SrkA [Enterobacteriaceae]

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;
1-324 0e+00

serine/threonine protein kinase;


:

Pssm-ID: 236974 [Multi-domain]  Cd Length: 325  Bit Score: 615.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260   1 MNNSAFTFQTLHPDTIMDALFEQGIRVDSGLTPLNSYENRVYQFQDEDRRRFVVKFYRPERWTADQILEEHQFALQLVND 80
Cdd:PRK11768   1 MNDSAFPFQTLTPDLILDALESLGLRVDGRLLALNSYENRVYQFGDEDGRRVVAKFYRPERWSDAQILEEHAFALELAEA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260  81 EVPVAAPVAFNGQTLLNHQGFYFAVFPSVGGRQFEADNIDQMEAVGRYLGRMHQTGRKQLFIHRPTIGLNEYLIEPRKLF 160
Cdd:PRK11768  81 EIPVVAPLAFNGQTLHEHQGFRFALFPRRGGRAPELDNLDQLEWVGRFLGRIHQVGAKRPFEHRPTLDLQEYGIEPRDWL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260 161 EDATLIPSGLKAAFLKATDELIAAVTAHW-REDFTVLRLHGDCHAGNILWRDGPMFVDLDDARNGPAIQDLWMLLNGDKA 239
Cdd:PRK11768 161 LASDLIPSDLRPAYLAAADQLLAAVEACWaRGDVRLLRLHGDCHPGNILWRDGPHFVDLDDARMGPAVQDLWMLLSGDRA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260 240 EQRMQLETIIEAYEEFSEFDTAEIGLIEPLRAMRLVYYLAWLMRRWADPAFPKNFPWLTGEDYWLRQTATFIEQAKVLQE 319
Cdd:PRK11768 241 EQLMQLETLLEGYEEFCEFDPRELALIEPLRALRLIHYSAWLARRWDDPAFPKAFPWFGTEDYWEQQILELREQLAALQE 320

                 ....*
gi 446988260 320 PPLQL 324
Cdd:PRK11768 321 PPLQL 325
 
Name Accession Description Interval E-value
PRK11768 PRK11768
serine/threonine protein kinase;
1-324 0e+00

serine/threonine protein kinase;


Pssm-ID: 236974 [Multi-domain]  Cd Length: 325  Bit Score: 615.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260   1 MNNSAFTFQTLHPDTIMDALFEQGIRVDSGLTPLNSYENRVYQFQDEDRRRFVVKFYRPERWTADQILEEHQFALQLVND 80
Cdd:PRK11768   1 MNDSAFPFQTLTPDLILDALESLGLRVDGRLLALNSYENRVYQFGDEDGRRVVAKFYRPERWSDAQILEEHAFALELAEA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260  81 EVPVAAPVAFNGQTLLNHQGFYFAVFPSVGGRQFEADNIDQMEAVGRYLGRMHQTGRKQLFIHRPTIGLNEYLIEPRKLF 160
Cdd:PRK11768  81 EIPVVAPLAFNGQTLHEHQGFRFALFPRRGGRAPELDNLDQLEWVGRFLGRIHQVGAKRPFEHRPTLDLQEYGIEPRDWL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260 161 EDATLIPSGLKAAFLKATDELIAAVTAHW-REDFTVLRLHGDCHAGNILWRDGPMFVDLDDARNGPAIQDLWMLLNGDKA 239
Cdd:PRK11768 161 LASDLIPSDLRPAYLAAADQLLAAVEACWaRGDVRLLRLHGDCHPGNILWRDGPHFVDLDDARMGPAVQDLWMLLSGDRA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260 240 EQRMQLETIIEAYEEFSEFDTAEIGLIEPLRAMRLVYYLAWLMRRWADPAFPKNFPWLTGEDYWLRQTATFIEQAKVLQE 319
Cdd:PRK11768 241 EQLMQLETLLEGYEEFCEFDPRELALIEPLRALRLIHYSAWLARRWDDPAFPKAFPWFGTEDYWEQQILELREQLAALQE 320

                 ....*
gi 446988260 320 PPLQL 324
Cdd:PRK11768 321 PPLQL 325
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
14-319 1.22e-93

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: 280.27  E-value: 1.22e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260  14 DTIMDALFEQGIRVDSGLTPLNSYENRVYQFQDEDRRRFVVKFYRPERWTADQILEEHQFALQLVNDEVPVAAPVA-FNG 92
Cdd:COG2334    1 DELAAALERYGLGPLSSLKPLNSGENRNYRVETEDGRRYVLKLYRPGRWSPEEIPFELALLAHLAAAGLPVPAPVPtRDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260  93 QTLLNHQGFYFAVFPSVGGRQFEADNIDQMEAVGRYLGRMHQTGRKqlFIHRPTIGLNEYLIEPRKLfedatLIPSGLKA 172
Cdd:COG2334   81 ETLLELEGRPAALFPFLPGRSPEEPSPEQLEELGRLLARLHRALAD--FPRPNARDLAWWDELLERL-----LGPLLPDP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260 173 AFLKATDELIAAVTAHWRE---DFTVLRLHGDCHAGNILWRDG--PMFVDLDDARNGPAIQDLWMLLNG--DKAEQRMQL 245
Cdd:COG2334  154 EDRALLEELLDRLEARLAPllgALPRGVIHGDLHPDNVLFDGDgvSGLIDFDDAGYGPRLYDLAIALNGwaDGPLDPARL 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446988260 246 ETIIEAYEEFSEFDTAEIGLIEPLRAMRLVYYLAWLMRRWA--DPAFPknfpwltgeDYWLRQTAtfiEQAKVLQE 319
Cdd:COG2334  234 AALLEGYRAVRPLTEAELAALPPLLRLRALRFLAWRLRRVRakDPAFE---------RYLRRQIA---LAWAALEA 297
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
31-255 1.29e-37

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: 134.17  E-value: 1.29e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260   31 LTPLNS-YENRVYQFQDEDRRrFVVKFYRPeRWTADQILEEHQFaLQLVNDEVPVAAPVAFNGQTLLNHQGFYFAVFPSV 109
Cdd:pfam01636   2 LRPISSgASNRTYLVTTGDGR-YVLRLPPP-GRAAEELRRELAL-LRHLAAAGVPPVPRVLAGCTDAELLGLPFLLMEYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260  110 GGRQFEADNIDQM-----EAVGRYLGRMHQTG---RKQLFIHRPTIGLNEYLIEprklfEDATLIPSGLKAAFLKATDEL 181
Cdd:pfam01636  79 PGEVLARPLLPEErgallEALGRALARLHAVDpaaLPLAGRLARLLELLRQLEA-----ALARLLAAELLDRLEELEERL 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446988260  182 IAAVTAHWREDFTVLRLHGDCHAGNILWRDGPM---FVDLDDARNGPAIQDLWMLLN-GDKAEQRMQLETIIEAYEEF 255
Cdd:pfam01636 154 LAALLALLPAELPPVLVHGDLHPGNLLVDPGGRvsgVIDFEDAGLGDPAYDLAILLNsWGRELGAELLAAYLAAYGAF 231
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
37-285 7.53e-19

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: 85.00  E-value: 7.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260  37 YENRVYqFQDEDRRRFVVKFYRPeRWTADQILEEHQFALQLVNDEVPVAAPVA-FNGQTLLNHQGFYFAVFPSVGGRQFE 115
Cdd:cd05153   26 IENTNY-FVTTTDGRYVLTLFEK-RRSAAELPFELELLDHLAQAGLPVPRPLAdKDGELLGELNGKPAALFPFLPGESLT 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260 116 ADNIDQMEAVGRYLGRMHQTGRKqlFIHRPTIGLNEYLIEPrkLFEDATLIPSGLKAAFLKATDELIAAVTAHWREDFTV 195
Cdd:cd05153  104 TPTPEQCRAIGAALARLHLALAG--FPPPRPNPRGLAWWKP--LAERLKARLDLLAADDRALLEDELARLQALAPSDLPR 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260 196 LRLHGDCHAGNILWRDGPM--FVDLDDARNGPAIQDLWMLLN-------GDKAEQRMQleTIIEAYEEFSEFDTAEIGLI 266
Cdd:cd05153  180 GVIHADLFRDNVLFDGDRLsgIIDFYDACYDPLLYDLAIALNdwcfdddGKLDPERAK--ALLAGYQSVRPLTEEEKAAL 257
                        250
                 ....*....|....*....
gi 446988260 267 EPLRAMRLVYYLAWLMRRW 285
Cdd:cd05153  258 PLLLRAAALRFWLSRLYDF 276
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
91-306 3.97e-05

spore coat protein, CotS family; Members of this family include the spore coat proteins CotS and YtaA from Bacillus subtilis and, from other endospore-forming bacteria, homologs that are more closely related to these two than to the spore coat proteins YutH and YsxE. The CotS family is more broadly distributed than YutH or YsxE, but still is not universal among spore-formers. [Cellular processes, Sporulation and germination]


Pssm-ID: 131952 [Multi-domain]  Cd Length: 313  Bit Score: 44.58  E-value: 3.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260   91 NGQTLLNHQGFYFAVFPSVGGRQFEADNIDQMEAVGRYLGRMHQTGR-------------------------KQLFIHRP 145
Cdd:TIGR02906  59 DGELYVKYNGDLYVLTEWIEGRECDFNNPIDLKKAAKGLALFHHASKgyvppdgskirsklgkwpkqfekrlKELERFKK 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260  146 TIGLNEYLIEPRKLFedatlipsgLKA--AFLKATDELIAAVTAHWREDFT--VLRLHGDCH----AGNILWRDGPMFV- 216
Cdd:TIGR02906 139 IALEKKYKDEFDKLY---------LKEvdYFLERGKKALELLNKSKYYDLCkeAKKIRGFCHqdyaYHNILLKDNEVYVi 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260  217 DLDDARNGPAIQDLWMLLNGdKAEQRMQ-----LETIIEAYEEFSEFDTAEIGLIeplramrlvyylawlmrrWADPAFP 291
Cdd:TIGR02906 210 DFDYCTIDLPVRDLRKLIIK-LMKKNGVwdlekAKEIIEAYSSINPLSKEEKEVL------------------YIDLAFP 270
                         250
                  ....*....|....*
gi 446988260  292 KNFpWLTGEDYWLRQ 306
Cdd:TIGR02906 271 HKF-WKIGKQYYYKR 284
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
191-257 3.23e-04

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


Pssm-ID: 214734  Cd Length: 196  Bit Score: 41.16  E-value: 3.23e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446988260   191 EDFTVLRlHGDCHAGNILWRDGP-------MFVDLDDARNGPAIQDLWMLLNG--DKAEQRMQLETIIEAY-EEFSE 257
Cdd:smart00587 117 GEFNVLN-HGDLWANNIMFKYDDegkpedvALIDFQLSHYGSPAEDLHYFLLTslSVEIRREHFDELLKFYyETLVE 192
 
Name Accession Description Interval E-value
PRK11768 PRK11768
serine/threonine protein kinase;
1-324 0e+00

serine/threonine protein kinase;


Pssm-ID: 236974 [Multi-domain]  Cd Length: 325  Bit Score: 615.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260   1 MNNSAFTFQTLHPDTIMDALFEQGIRVDSGLTPLNSYENRVYQFQDEDRRRFVVKFYRPERWTADQILEEHQFALQLVND 80
Cdd:PRK11768   1 MNDSAFPFQTLTPDLILDALESLGLRVDGRLLALNSYENRVYQFGDEDGRRVVAKFYRPERWSDAQILEEHAFALELAEA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260  81 EVPVAAPVAFNGQTLLNHQGFYFAVFPSVGGRQFEADNIDQMEAVGRYLGRMHQTGRKQLFIHRPTIGLNEYLIEPRKLF 160
Cdd:PRK11768  81 EIPVVAPLAFNGQTLHEHQGFRFALFPRRGGRAPELDNLDQLEWVGRFLGRIHQVGAKRPFEHRPTLDLQEYGIEPRDWL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260 161 EDATLIPSGLKAAFLKATDELIAAVTAHW-REDFTVLRLHGDCHAGNILWRDGPMFVDLDDARNGPAIQDLWMLLNGDKA 239
Cdd:PRK11768 161 LASDLIPSDLRPAYLAAADQLLAAVEACWaRGDVRLLRLHGDCHPGNILWRDGPHFVDLDDARMGPAVQDLWMLLSGDRA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260 240 EQRMQLETIIEAYEEFSEFDTAEIGLIEPLRAMRLVYYLAWLMRRWADPAFPKNFPWLTGEDYWLRQTATFIEQAKVLQE 319
Cdd:PRK11768 241 EQLMQLETLLEGYEEFCEFDPRELALIEPLRALRLIHYSAWLARRWDDPAFPKAFPWFGTEDYWEQQILELREQLAALQE 320

                 ....*
gi 446988260 320 PPLQL 324
Cdd:PRK11768 321 PPLQL 325
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
14-319 1.22e-93

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: 280.27  E-value: 1.22e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260  14 DTIMDALFEQGIRVDSGLTPLNSYENRVYQFQDEDRRRFVVKFYRPERWTADQILEEHQFALQLVNDEVPVAAPVA-FNG 92
Cdd:COG2334    1 DELAAALERYGLGPLSSLKPLNSGENRNYRVETEDGRRYVLKLYRPGRWSPEEIPFELALLAHLAAAGLPVPAPVPtRDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260  93 QTLLNHQGFYFAVFPSVGGRQFEADNIDQMEAVGRYLGRMHQTGRKqlFIHRPTIGLNEYLIEPRKLfedatLIPSGLKA 172
Cdd:COG2334   81 ETLLELEGRPAALFPFLPGRSPEEPSPEQLEELGRLLARLHRALAD--FPRPNARDLAWWDELLERL-----LGPLLPDP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260 173 AFLKATDELIAAVTAHWRE---DFTVLRLHGDCHAGNILWRDG--PMFVDLDDARNGPAIQDLWMLLNG--DKAEQRMQL 245
Cdd:COG2334  154 EDRALLEELLDRLEARLAPllgALPRGVIHGDLHPDNVLFDGDgvSGLIDFDDAGYGPRLYDLAIALNGwaDGPLDPARL 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446988260 246 ETIIEAYEEFSEFDTAEIGLIEPLRAMRLVYYLAWLMRRWA--DPAFPknfpwltgeDYWLRQTAtfiEQAKVLQE 319
Cdd:COG2334  234 AALLEGYRAVRPLTEAELAALPPLLRLRALRFLAWRLRRVRakDPAFE---------RYLRRQIA---LAWAALEA 297
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
31-255 1.29e-37

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: 134.17  E-value: 1.29e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260   31 LTPLNS-YENRVYQFQDEDRRrFVVKFYRPeRWTADQILEEHQFaLQLVNDEVPVAAPVAFNGQTLLNHQGFYFAVFPSV 109
Cdd:pfam01636   2 LRPISSgASNRTYLVTTGDGR-YVLRLPPP-GRAAEELRRELAL-LRHLAAAGVPPVPRVLAGCTDAELLGLPFLLMEYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260  110 GGRQFEADNIDQM-----EAVGRYLGRMHQTG---RKQLFIHRPTIGLNEYLIEprklfEDATLIPSGLKAAFLKATDEL 181
Cdd:pfam01636  79 PGEVLARPLLPEErgallEALGRALARLHAVDpaaLPLAGRLARLLELLRQLEA-----ALARLLAAELLDRLEELEERL 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446988260  182 IAAVTAHWREDFTVLRLHGDCHAGNILWRDGPM---FVDLDDARNGPAIQDLWMLLN-GDKAEQRMQLETIIEAYEEF 255
Cdd:pfam01636 154 LAALLALLPAELPPVLVHGDLHPGNLLVDPGGRvsgVIDFEDAGLGDPAYDLAILLNsWGRELGAELLAAYLAAYGAF 231
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
37-285 7.53e-19

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: 85.00  E-value: 7.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260  37 YENRVYqFQDEDRRRFVVKFYRPeRWTADQILEEHQFALQLVNDEVPVAAPVA-FNGQTLLNHQGFYFAVFPSVGGRQFE 115
Cdd:cd05153   26 IENTNY-FVTTTDGRYVLTLFEK-RRSAAELPFELELLDHLAQAGLPVPRPLAdKDGELLGELNGKPAALFPFLPGESLT 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260 116 ADNIDQMEAVGRYLGRMHQTGRKqlFIHRPTIGLNEYLIEPrkLFEDATLIPSGLKAAFLKATDELIAAVTAHWREDFTV 195
Cdd:cd05153  104 TPTPEQCRAIGAALARLHLALAG--FPPPRPNPRGLAWWKP--LAERLKARLDLLAADDRALLEDELARLQALAPSDLPR 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260 196 LRLHGDCHAGNILWRDGPM--FVDLDDARNGPAIQDLWMLLN-------GDKAEQRMQleTIIEAYEEFSEFDTAEIGLI 266
Cdd:cd05153  180 GVIHADLFRDNVLFDGDRLsgIIDFYDACYDPLLYDLAIALNdwcfdddGKLDPERAK--ALLAGYQSVRPLTEEEKAAL 257
                        250
                 ....*....|....*....
gi 446988260 267 EPLRAMRLVYYLAWLMRRW 285
Cdd:cd05153  258 PLLLRAAALRFWLSRLYDF 276
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
9-256 1.86e-08

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 54.74  E-value: 1.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260   9 QTLHPDTIMDALFEQ--GIRVDSGLTPLNS-YENRVYQFQDEDRrrFVVKFYRPERWTADQILEEHQfALQLVNDE--VP 83
Cdd:COG3173    1 EELDEAALRALLAAQlpGLAGLPEVEPLSGgWSNLTYRLDTGDR--LVLRRPPRGLASAHDVRREAR-VLRALAPRlgVP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260  84 VAAPVAF--NGQTLlnhqGFYFAVFPSVGGRQFEADNIDQ--------MEAVGRYLGRMHQ--TGRKQLFIHRPTiGLNE 151
Cdd:COG3173   78 VPRPLALgeDGEVI----GAPFYVMEWVEGETLEDALPDLspaerralARALGEFLAALHAvdPAAAGLADGRPE-GLER 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260 152 YLIEPRKLFEDATLIPSGLKAAflkaTDELIAAVTAHWREDFTVLRLHGDCHAGNILWRDGPM----FVDLDDARNGPAI 227
Cdd:COG3173  153 QLARWRAQLRRALARTDDLPAL----RERLAAWLAANLPEWGPPVLVHGDLRPGNLLVDPDDGrltaVIDWELATLGDPA 228
                        250       260       270
                 ....*....|....*....|....*....|.
gi 446988260 228 QDL-WMLLNGDKAEQ-RMQLETIIEAYEEFS 256
Cdd:COG3173  229 ADLaYLLLYWRLPDDlLGPRAAFLAAYEEAT 259
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
154-286 2.15e-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: 2.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260 154 IEPRKLFEDATLIPSGLKAAFLKATDELIAAVTAHwrEDFTVLrLHGDCHAGNILWRDG--PMFVDLDDARNGPAIQDLW 231
Cdd:COG0510   11 FDLFARLERYLALGPRDLPELLRRLEELERALAAR--PLPLVL-CHGDLHPGNFLVTDDgrLYLIDWEYAGLGDPAFDLA 87
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446988260 232 MLLNGDKAEQRmQLETIIEAYeEFSEFDTAEIGLIEPLRAMRLVYYLAWLMRRWA 286
Cdd:COG0510   88 ALLVEYGLSPE-QAEELLEAY-GFGRPTEELLRRLRAYRALADLLWALWALVRAA 140
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
91-306 3.97e-05

spore coat protein, CotS family; Members of this family include the spore coat proteins CotS and YtaA from Bacillus subtilis and, from other endospore-forming bacteria, homologs that are more closely related to these two than to the spore coat proteins YutH and YsxE. The CotS family is more broadly distributed than YutH or YsxE, but still is not universal among spore-formers. [Cellular processes, Sporulation and germination]


Pssm-ID: 131952 [Multi-domain]  Cd Length: 313  Bit Score: 44.58  E-value: 3.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260   91 NGQTLLNHQGFYFAVFPSVGGRQFEADNIDQMEAVGRYLGRMHQTGR-------------------------KQLFIHRP 145
Cdd:TIGR02906  59 DGELYVKYNGDLYVLTEWIEGRECDFNNPIDLKKAAKGLALFHHASKgyvppdgskirsklgkwpkqfekrlKELERFKK 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260  146 TIGLNEYLIEPRKLFedatlipsgLKA--AFLKATDELIAAVTAHWREDFT--VLRLHGDCH----AGNILWRDGPMFV- 216
Cdd:TIGR02906 139 IALEKKYKDEFDKLY---------LKEvdYFLERGKKALELLNKSKYYDLCkeAKKIRGFCHqdyaYHNILLKDNEVYVi 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260  217 DLDDARNGPAIQDLWMLLNGdKAEQRMQ-----LETIIEAYEEFSEFDTAEIGLIeplramrlvyylawlmrrWADPAFP 291
Cdd:TIGR02906 210 DFDYCTIDLPVRDLRKLIIK-LMKKNGVwdlekAKEIIEAYSSINPLSKEEKEVL------------------YIDLAFP 270
                         250
                  ....*....|....*
gi 446988260  292 KNFpWLTGEDYWLRQ 306
Cdd:TIGR02906 271 HKF-WKIGKQYYYKR 284
MPH2' cd05152
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ...
45-254 2.32e-04

Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group from ATP to the 2'-hydroxyl of macrolide antibiotics such as erythromycin, clarithromycin, and azithromycin, among others. Macrolides penetrate the bacterial cell and bind to ribosomes, where it interrupts protein elongation, leading ultimately to the demise of the bacterium. Phosphorylation of macrolides leads to their inactivation. Based on substrate specificity and amino acid sequence, MPH2' is divided into types I and II, encoded by mphA and mphB genes, respectively. MPH2'I inactivates 14-membered ring macrolides while MPH2'II inactivates both 14- and 16-membered ring macrolides. Enzymatic inactivation of macrolides has been reported as a mechanism for bacterial resistance in clinical samples. MPH2' 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: 270701 [Multi-domain]  Cd Length: 276  Bit Score: 42.23  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260  45 QDEDRRRFVVKF-YRPERWTAdqiLEEHQFALQLVNDEVPVAAP--VAFNGQTLlnhqgfyfaVFPSVGGR--------- 112
Cdd:cd05152   31 RDTEGRRWVLRIpRRPDVSER---LEAEKKVLDLVTPHLPFAVPdwRIHTPELI---------AYPLLPGVpaatidpei 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260 113 -------QFEADNIDQMEAVGRYLGRMHQTgrkqlfihrptiglneyliePRKLFEDATLI---PSGLKAAFL------K 176
Cdd:cd05152   99 qnyvwnwDPLAPPPVFARSLGKALAALHSI--------------------PADLAAAAGLPvytAEEVRARMAarmdrvK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446988260 177 ATDELIAAVTAHWRE---------DFTVLrLHGDCHAGNILWRDGPM---FVDLDDARNG-PAIQDLWMLLNGDKAEqrm 243
Cdd:cd05152  159 ETFGVPPALLARWQAwladdslwpFHTVL-VHGDLHPGHILVDEDGRvtgLIDWTEAKVGdPADDFAWHYAAFGEEA--- 234
                        250
                 ....*....|.
gi 446988260 244 qLETIIEAYEE 254
Cdd:cd05152  235 -LERLLDAYEK 244
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
191-257 3.23e-04

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


Pssm-ID: 214734  Cd Length: 196  Bit Score: 41.16  E-value: 3.23e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446988260   191 EDFTVLRlHGDCHAGNILWRDGP-------MFVDLDDARNGPAIQDLWMLLNG--DKAEQRMQLETIIEAY-EEFSE 257
Cdd:smart00587 117 GEFNVLN-HGDLWANNIMFKYDDegkpedvALIDFQLSHYGSPAEDLHYFLLTslSVEIRREHFDELLKFYyETLVE 192
EcKL pfam02958
Ecdysteroid kinase-like family; This family includes ecdysteroid 22-kinase, an enzyme ...
190-252 2.07e-03

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: 39.17  E-value: 2.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446988260  190 REDFTVLrLHGDCHAGNILWRDGP-------MFVDLDDARNGPAIQDLWMLLNG--DKAEQRMQLETIIEAY 252
Cdd:pfam02958 210 PGEFNVL-NHGDLWVNNIMFKYDDegepedvILVDFQLSRYGSPAIDLNYFLYTstELELRLEHFDELLRYY 280
 
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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