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Conserved domains on  [gi|2225572730|ref|WP_245583036|]
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phosphotransferase enzyme family protein [Paenibacillus daejeonensis]

Protein Classification

phosphotransferase enzyme family protein( domain architecture ID 11457111)

phosphotransferase enzyme family protein such as serine/threonine protein kinase RdoA, type II homoserine kinase, N-acetylhexosamine 1-kinase, hydroxylysine kinase, and amicoumacin kinase, all of which play crucial roles in transferring phosphate groups to specific substrates

CATH:  1.10.510.10
Gene Ontology:  GO:0016301|GO:0005524|GO:0016310
PubMed:  16244704
SCOP:  3000066

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
23-328 5.51e-35

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: 129.66  E-value: 5.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730  23 ALQRYDL-EWTGISYIQMSESVTYRITSHPDHQYLLRIH-IGKSNQAEIASELAFLRALNDHsDIEVPTGIASLDGsevl 100
Cdd:COG2334     6 ALERYGLgPLSSLKPLNSGENRNYRVETEDGRRYVLKLYrPGRWSPEEIPFELALLAHLAAA-GLPVPAPVPTRDG---- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730 101 EITAEHDDEPpllVTVMKWMDGEPVHgAVMDNHAMAVGVMIARLHAAsmlfvpGENFTRPSL-DADSFKGKFAKLAnyRD 179
Cdd:COG2334    81 ETLLELEGRP---AALFPFLPGRSPE-EPSPEQLEELGRLLARLHRA------LADFPRPNArDLAWWDELLERLL--GP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730 180 RFVSDADWALYQEAAAKVVSHLSEMKPtSENYGLIHGDLHLGNIVFR-DGAPFPIDFGLCGYGYYLYDVASVMLG----- 253
Cdd:COG2334   149 LLPDPEDRALLEELLDRLEARLAPLLG-ALPRGVIHGDLHPDNVLFDgDGVSGLIDFDDAGYGPRLYDLAIALNGwadgp 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2225572730 254 LNPTQRWLLLDRYEALRGSNPNSSHLLETFFIMIMIENYSHHAPNPAETEslqseqPSALAYLRKFVEGAAFLFE 328
Cdd:COG2334   228 LDPARLAALLEGYRAVRPLTEAELAALPPLLRLRALRFLAWRLRRVRAKD------PAFERYLRRQIALAWAALE 296
 
Name Accession Description Interval E-value
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
23-328 5.51e-35

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: 129.66  E-value: 5.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730  23 ALQRYDL-EWTGISYIQMSESVTYRITSHPDHQYLLRIH-IGKSNQAEIASELAFLRALNDHsDIEVPTGIASLDGsevl 100
Cdd:COG2334     6 ALERYGLgPLSSLKPLNSGENRNYRVETEDGRRYVLKLYrPGRWSPEEIPFELALLAHLAAA-GLPVPAPVPTRDG---- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730 101 EITAEHDDEPpllVTVMKWMDGEPVHgAVMDNHAMAVGVMIARLHAAsmlfvpGENFTRPSL-DADSFKGKFAKLAnyRD 179
Cdd:COG2334    81 ETLLELEGRP---AALFPFLPGRSPE-EPSPEQLEELGRLLARLHRA------LADFPRPNArDLAWWDELLERLL--GP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730 180 RFVSDADWALYQEAAAKVVSHLSEMKPtSENYGLIHGDLHLGNIVFR-DGAPFPIDFGLCGYGYYLYDVASVMLG----- 253
Cdd:COG2334   149 LLPDPEDRALLEELLDRLEARLAPLLG-ALPRGVIHGDLHPDNVLFDgDGVSGLIDFDDAGYGPRLYDLAIALNGwadgp 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2225572730 254 LNPTQRWLLLDRYEALRGSNPNSSHLLETFFIMIMIENYSHHAPNPAETEslqseqPSALAYLRKFVEGAAFLFE 328
Cdd:COG2334   228 LDPARLAALLEGYRAVRPLTEAELAALPPLLRLRALRFLAWRLRRVRAKD------PAFERYLRRQIALAWAALE 296
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
23-270 2.14e-22

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: 95.40  E-value: 2.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730  23 ALQRYDL----EWTGISyiQMSESVTYRITShPDHQYLLRIHIGKSNQAEIASELAFLRALNDHsDIEVPTGIASLDGse 98
Cdd:cd05153     7 FLAHYDLgellSFEGIA--AGIENTNYFVTT-TDGRYVLTLFEKRRSAAELPFELELLDHLAQA-GLPVPRPLADKDG-- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730  99 vlEITAEHDDEPpllVTVMKWMDGEPVhGAVMDNHAMAVGVMIARLHAASMLFVPGenfTRPSLDADSFKGKFAKLANYR 178
Cdd:cd05153    81 --ELLGELNGKP---AALFPFLPGESL-TTPTPEQCRAIGAALARLHLALAGFPPP---RPNPRGLAWWKPLAERLKARL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730 179 DRFVSDadwalYQEAAAKVVSHLSEMKPTSENYGLIHGDLHLGNIVFRDG--APFpIDFGLCGYGYYLYDVASVMLG--- 253
Cdd:cd05153   152 DLLAAD-----DRALLEDELARLQALAPSDLPRGVIHADLFRDNVLFDGDrlSGI-IDFYDACYDPLLYDLAIALNDwcf 225
                         250       260
                  ....*....|....*....|..
gi 2225572730 254 -----LNPTQRWLLLDRYEALR 270
Cdd:cd05153   226 dddgkLDPERAKALLAGYQSVR 247
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
44-250 2.40e-21

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: 91.41  E-value: 2.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730  44 TYRITsHPDHQYLLRIHIGKSNQAEIASELAFLRALNDHSDIEVPTGIASLDGSEVLEitaehddeppLLVTVMKWMDGE 123
Cdd:pfam01636  13 TYLVT-TGDGRYVLRLPPPGRAAEELRRELALLRHLAAAGVPPVPRVLAGCTDAELLG----------LPFLLMEYLPGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730 124 PVHGAVMDNHAMA----VGVMIARLHAASMLFVPGENFTRPSLDADSFkgkfakLANYRDRFVSDADWALYQEAAAKVVS 199
Cdd:pfam01636  82 VLARPLLPEERGAlleaLGRALARLHAVDPAALPLAGRLARLLELLRQ------LEAALARLLAAELLDRLEELEERLLA 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2225572730 200 HLSEMKPTSENYGLIHGDLHLGNIVFRDGAPFP--IDFGLCGYGYYLYDVASV 250
Cdd:pfam01636 156 ALLALLPAELPPVLVHGDLHPGNLLVDPGGRVSgvIDFEDAGLGDPAYDLAIL 208
PRK05231 PRK05231
homoserine kinase; Provisional
70-270 6.76e-06

homoserine kinase; Provisional


Pssm-ID: 235369 [Multi-domain]  Cd Length: 319  Bit Score: 47.10  E-value: 6.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730  70 ASELAFLRALNDH---SDIEVPTGIASLDGSEVLEItaehDDEPPLLVTVM--KWMDgepvhgAVMDNHAMAVGVMIARL 144
Cdd:PRK05231   58 AEDLPFFLGLMQHlaaRGVPVPAPVARRDGAALGEL----AGKPAAIVTFLegKWPR------APTAAHCAEVGEMLARM 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730 145 HAAsmlfvpGENF--TRP-SLDADSFKGKFAKLANYRdrfvSDADWAL----YQEAAAKVVSHLSEMKPTsenyGLIHGD 217
Cdd:PRK05231  128 HLA------GRDFplERPnLRGLAWWRELAPRLLPFL----ADEQAALleaeLAAQLAFLASAAWPALPR----GVIHAD 193
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2225572730 218 LhlgnivFRDGAPFP-------IDFGLCGYGYYLYDVAsVML---------GLNPTQRWLLLDRYEALR 270
Cdd:PRK05231  194 L------FRDNVLFEgdrlsgfIDFYFACNDKLLYDVA-ITLndwcfeadgSLDATKARALLAAYQSVR 255
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
141-288 1.22e-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: 46.51  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730 141 IARLHAASMLFVPGEN-------------FTRPSLDADSFKgKFAKLANYRDRF----VSDADWalYQEAAAKVVSHL-- 201
Cdd:TIGR02906  97 LALFHHASKGYVPPDGskirsklgkwpkqFEKRLKELERFK-KIALEKKYKDEFdklyLKEVDY--FLERGKKALELLnk 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730 202 SE----MKPTSENYGLIHGDLHLGNIVFRDGAPFPIDFGLCGYGYYLYDVASVMLG-LNPTQRW------LLLDRYEALr 270
Cdd:TIGR02906 174 SKyydlCKEAKKIRGFCHQDYAYHNILLKDNEVYVIDFDYCTIDLPVRDLRKLIIKlMKKNGVWdlekakEIIEAYSSI- 252
                         170
                  ....*....|....*...
gi 2225572730 271 gsNPNSSHLLETFFIMIM 288
Cdd:TIGR02906 253 --NPLSKEEKEVLYIDLA 268
 
Name Accession Description Interval E-value
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
23-328 5.51e-35

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: 129.66  E-value: 5.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730  23 ALQRYDL-EWTGISYIQMSESVTYRITSHPDHQYLLRIH-IGKSNQAEIASELAFLRALNDHsDIEVPTGIASLDGsevl 100
Cdd:COG2334     6 ALERYGLgPLSSLKPLNSGENRNYRVETEDGRRYVLKLYrPGRWSPEEIPFELALLAHLAAA-GLPVPAPVPTRDG---- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730 101 EITAEHDDEPpllVTVMKWMDGEPVHgAVMDNHAMAVGVMIARLHAAsmlfvpGENFTRPSL-DADSFKGKFAKLAnyRD 179
Cdd:COG2334    81 ETLLELEGRP---AALFPFLPGRSPE-EPSPEQLEELGRLLARLHRA------LADFPRPNArDLAWWDELLERLL--GP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730 180 RFVSDADWALYQEAAAKVVSHLSEMKPtSENYGLIHGDLHLGNIVFR-DGAPFPIDFGLCGYGYYLYDVASVMLG----- 253
Cdd:COG2334   149 LLPDPEDRALLEELLDRLEARLAPLLG-ALPRGVIHGDLHPDNVLFDgDGVSGLIDFDDAGYGPRLYDLAIALNGwadgp 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2225572730 254 LNPTQRWLLLDRYEALRGSNPNSSHLLETFFIMIMIENYSHHAPNPAETEslqseqPSALAYLRKFVEGAAFLFE 328
Cdd:COG2334   228 LDPARLAALLEGYRAVRPLTEAELAALPPLLRLRALRFLAWRLRRVRAKD------PAFERYLRRQIALAWAALE 296
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
23-270 2.14e-22

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: 95.40  E-value: 2.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730  23 ALQRYDL----EWTGISyiQMSESVTYRITShPDHQYLLRIHIGKSNQAEIASELAFLRALNDHsDIEVPTGIASLDGse 98
Cdd:cd05153     7 FLAHYDLgellSFEGIA--AGIENTNYFVTT-TDGRYVLTLFEKRRSAAELPFELELLDHLAQA-GLPVPRPLADKDG-- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730  99 vlEITAEHDDEPpllVTVMKWMDGEPVhGAVMDNHAMAVGVMIARLHAASMLFVPGenfTRPSLDADSFKGKFAKLANYR 178
Cdd:cd05153    81 --ELLGELNGKP---AALFPFLPGESL-TTPTPEQCRAIGAALARLHLALAGFPPP---RPNPRGLAWWKPLAERLKARL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730 179 DRFVSDadwalYQEAAAKVVSHLSEMKPTSENYGLIHGDLHLGNIVFRDG--APFpIDFGLCGYGYYLYDVASVMLG--- 253
Cdd:cd05153   152 DLLAAD-----DRALLEDELARLQALAPSDLPRGVIHADLFRDNVLFDGDrlSGI-IDFYDACYDPLLYDLAIALNDwcf 225
                         250       260
                  ....*....|....*....|..
gi 2225572730 254 -----LNPTQRWLLLDRYEALR 270
Cdd:cd05153   226 dddgkLDPERAKALLAGYQSVR 247
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
44-250 2.40e-21

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: 91.41  E-value: 2.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730  44 TYRITsHPDHQYLLRIHIGKSNQAEIASELAFLRALNDHSDIEVPTGIASLDGSEVLEitaehddeppLLVTVMKWMDGE 123
Cdd:pfam01636  13 TYLVT-TGDGRYVLRLPPPGRAAEELRRELALLRHLAAAGVPPVPRVLAGCTDAELLG----------LPFLLMEYLPGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730 124 PVHGAVMDNHAMA----VGVMIARLHAASMLFVPGENFTRPSLDADSFkgkfakLANYRDRFVSDADWALYQEAAAKVVS 199
Cdd:pfam01636  82 VLARPLLPEERGAlleaLGRALARLHAVDPAALPLAGRLARLLELLRQ------LEAALARLLAAELLDRLEELEERLLA 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2225572730 200 HLSEMKPTSENYGLIHGDLHLGNIVFRDGAPFP--IDFGLCGYGYYLYDVASV 250
Cdd:pfam01636 156 ALLALLPAELPPVLVHGDLHPGNLLVDPGGRVSgvIDFEDAGLGDPAYDLAIL 208
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
42-272 7.77e-17

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 79.39  E-value: 7.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730  42 SVTYRITShpDHQYLLRIH-IGKSNQAEIASELAFLRALNDHSDIEVPTGIASLDGSEVLeitaehddepPLLVTVMKWM 120
Cdd:COG3173    34 NLTYRLDT--GDRLVLRRPpRGLASAHDVRREARVLRALAPRLGVPVPRPLALGEDGEVI----------GAPFYVMEWV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730 121 DGEPVHGAVMDNH-------AMAVGVMIARLHAasmlfVPGENFTRPSLDADSFKGKFAKLANYRDRFVSDADW--ALYQ 191
Cdd:COG3173   102 EGETLEDALPDLSpaerralARALGEFLAALHA-----VDPAAAGLADGRPEGLERQLARWRAQLRRALARTDDlpALRE 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730 192 EAAAKVVSHLSEMKPTSenygLIHGDLHLGNIVFRDGAPFP---IDFGLCGYGYYLYDVASVMLGLNPT-----QRWLLL 263
Cdd:COG3173   177 RLAAWLAANLPEWGPPV----LVHGDLRPGNLLVDPDDGRLtavIDWELATLGDPAADLAYLLLYWRLPddllgPRAAFL 252

                  ....*....
gi 2225572730 264 DRYEALRGS 272
Cdd:COG3173   253 AAYEEATGD 261
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
171-266 7.95e-08

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 51.32  E-value: 7.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730 171 FAKLANYRDRFVSDADWALyqEAAAKVVSHLSemkPTSENYGLIHGDLHLGNIVF-RDGAPFPIDFGLCGYGYYLYDVAS 249
Cdd:COG0510    14 FARLERYLALGPRDLPELL--RRLEELERALA---ARPLPLVLCHGDLHPGNFLVtDDGRLYLIDWEYAGLGDPAFDLAA 88
                          90
                  ....*....|....*....
gi 2225572730 250 VML--GLNPTQRWLLLDRY 266
Cdd:COG0510    89 LLVeyGLSPEQAEELLEAY 107
PRK05231 PRK05231
homoserine kinase; Provisional
70-270 6.76e-06

homoserine kinase; Provisional


Pssm-ID: 235369 [Multi-domain]  Cd Length: 319  Bit Score: 47.10  E-value: 6.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730  70 ASELAFLRALNDH---SDIEVPTGIASLDGSEVLEItaehDDEPPLLVTVM--KWMDgepvhgAVMDNHAMAVGVMIARL 144
Cdd:PRK05231   58 AEDLPFFLGLMQHlaaRGVPVPAPVARRDGAALGEL----AGKPAAIVTFLegKWPR------APTAAHCAEVGEMLARM 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730 145 HAAsmlfvpGENF--TRP-SLDADSFKGKFAKLANYRdrfvSDADWAL----YQEAAAKVVSHLSEMKPTsenyGLIHGD 217
Cdd:PRK05231  128 HLA------GRDFplERPnLRGLAWWRELAPRLLPFL----ADEQAALleaeLAAQLAFLASAAWPALPR----GVIHAD 193
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2225572730 218 LhlgnivFRDGAPFP-------IDFGLCGYGYYLYDVAsVML---------GLNPTQRWLLLDRYEALR 270
Cdd:PRK05231  194 L------FRDNVLFEgdrlsgfIDFYFACNDKLLYDVA-ITLndwcfeadgSLDATKARALLAAYQSVR 255
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
43-265 8.10e-06

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: 46.46  E-value: 8.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730  43 VTYRITSHpdhqYLLRIHIGKSNQAEIASELAFLRALNDHSDIEVPTGIAsldgsevleiTAEHDDEPPLLVTVMKWMDG 122
Cdd:cd05155    13 ATFRLGDD----LAVRLPRRAWAAELLEKEQRWLPRLAPRLPLPVPVPLA----------LGKPGAGYPWPWSVYRWLEG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730 123 EPV-HGAVMDNHAMAV--GVMIARLHAASM----LFVPGENFTRPSLDADSFKGKFAKLANYRDRfvsdadwalyqEAAA 195
Cdd:cd05155    79 ETAaDAPLADPAAAAEdlARFLAALHAIDPagppNPGRGNPLRGRDLAVRDAEEALAALAGLLDV-----------AAAR 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2225572730 196 KVVSHLSEMKPTSENYGLIHGDLHLGNIVFRDG---ApfPIDFGLCGYGYYLYDVASVmlglnptqrWLLLDR 265
Cdd:cd05155   148 ALWERALAAPAWAGPPVWLHGDLHPGNLLVRDGrlsA--VIDFGDLGVGDPACDLAIA---------WTLFDA 209
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
141-288 1.22e-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: 46.51  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730 141 IARLHAASMLFVPGEN-------------FTRPSLDADSFKgKFAKLANYRDRF----VSDADWalYQEAAAKVVSHL-- 201
Cdd:TIGR02906  97 LALFHHASKGYVPPDGskirsklgkwpkqFEKRLKELERFK-KIALEKKYKDEFdklyLKEVDY--FLERGKKALELLnk 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730 202 SE----MKPTSENYGLIHGDLHLGNIVFRDGAPFPIDFGLCGYGYYLYDVASVMLG-LNPTQRW------LLLDRYEALr 270
Cdd:TIGR02906 174 SKyydlCKEAKKIRGFCHQDYAYHNILLKDNEVYVIDFDYCTIDLPVRDLRKLIIKlMKKNGVWdlekakEIIEAYSSI- 252
                         170
                  ....*....|....*...
gi 2225572730 271 gsNPNSSHLLETFFIMIM 288
Cdd:TIGR02906 253 --NPLSKEEKEVLYIDLA 268
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
181-251 1.52e-05

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


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 44.60  E-value: 1.52e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2225572730 181 FVSDADWALYQEAAAKVVSHLSEMKPtsenYGLIHGDLHLGNIVFRDGAPFP--IDFGLCGYGYYLYDVASVM 251
Cdd:cd05120    85 RLSEEEKEKIADQLAEILAALHRIDS----SVLTHGDLHPGNILVKPDGKLSgiIDWEFAGYGPPAFDYAAAL 153
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
210-241 4.37e-05

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: 43.41  E-value: 4.37e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2225572730 210 NYGLIHGDLHLGNIVFRDGAPFPIDFGLCGYG 241
Cdd:COG3642    69 RAGIVHGDLTTSNILVDDGGVYLIDFGLARYS 100
PRK14879 PRK14879
Kae1-associated kinase Bud32;
212-240 9.95e-05

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 42.97  E-value: 9.95e-05
                          10        20
                  ....*....|....*....|....*....
gi 2225572730 212 GLIHGDLHLGNIVFRDGAPFPIDFGLCGY 240
Cdd:PRK14879  115 GIIHGDLTTSNMILSGGKIYLIDFGLAEF 143
PRK11768 PRK11768
serine/threonine protein kinase;
137-235 1.00e-04

serine/threonine protein kinase;


Pssm-ID: 236974 [Multi-domain]  Cd Length: 325  Bit Score: 43.62  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730 137 VGVMIARLHA--ASMLFVpgenfTRPSLDADSF---------KGKFAKlANYRDRFVSDADWALyqeaaAKVVSHLSEMK 205
Cdd:PRK11768  125 VGRFLGRIHQvgAKRPFE-----HRPTLDLQEYgieprdwllASDLIP-SDLRPAYLAAADQLL-----AAVEACWARGD 193
                          90       100       110
                  ....*....|....*....|....*....|
gi 2225572730 206 PTSENyglIHGDLHLGNIVFRDGaPFPIDF 235
Cdd:PRK11768  194 VRLLR---LHGDCHPGNILWRDG-PHFVDL 219
PRK06148 PRK06148
hypothetical protein; Provisional
45-236 1.23e-04

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 43.86  E-value: 1.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730   45 YRITSHPDHQYLLRIHigksNQAEIASELAFLRALNDH-----SDIEVPTGIASLDGSEVLEITAEhdDEPPLLVTVMKW 119
Cdd:PRK06148    41 FRLTTDDGADYILKIV----NPSEPRVESDFQTAALDHlaavaPDLPVPRLIPSLSGASLASAQDP--DGEPRLLRLLSW 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730  120 MDGEPVHGAVMDNHAM--AVGVMIARLHAASMlfvpgeNFTRPSLDADsFKGKFAKLANYRDRF---VSDADWALYQEAA 194
Cdd:PRK06148   115 LPGTPLAEAAPRTEALldNLGRALGRLDRALQ------GFMHPGALRD-LDWDLRHAGRARDRLhfiDDPEDRALVERFL 187
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2225572730  195 AKVVSHLS---EMKPTSenygLIHGDLHLGNIVFRDGAPFP----IDFG 236
Cdd:PRK06148   188 ARFERNVAprlAALPAQ----VIHNDANDYNILVDADDGERisglIDFG 232
COG2187 COG2187
Aminoglycoside phosphotransferase family enzyme [General function prediction only];
215-271 3.64e-04

Aminoglycoside phosphotransferase family enzyme [General function prediction only];


Pssm-ID: 441790  Cd Length: 341  Bit Score: 42.07  E-value: 3.64e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2225572730 215 HGDLHLGNIVFRDGAPFPIDfglC-------GYGYYLYDVA-SVM----LGLnPTQRWLLLDRYEALRG 271
Cdd:COG2187   218 HGDLHLGNICLIDGKPVLFD---CiefnerlRWIDVLYDLAfLLMdleaRGR-PDLANRFLNRYLEATG 282
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
212-240 9.73e-04

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 39.89  E-value: 9.73e-04
                          10        20
                  ....*....|....*....|....*....
gi 2225572730 212 GLIHGDLHLGNIVFRDGAPFPIDFGLCGY 240
Cdd:TIGR03724 110 GIVHGDLTTSNIIVRDDKVYLIDFGLGKY 138
EcKL pfam02958
Ecdysteroid kinase-like family; This family includes ecdysteroid 22-kinase, an enzyme ...
133-245 1.41e-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: 39.94  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730 133 HAMAVGVMIARLHAASMLFV--PGENFTR------PSLDADSFKGKFAK------LANYRDRFVSD-ADWALYQEAAAKV 197
Cdd:pfam02958 115 HTKLVLEKLAKFHAASAALKelQPEVFKQlkkglfEEDYVNGAIKEFFEplmetgLDAAAEALREQlPEYEKYAEKLEKL 194
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2225572730 198 VSHLSE-----MKPTSENYG-LIHGDLHLGNIVFR-DGAPFP-----IDFGLCGYG-------YYLY 245
Cdd:pfam02958 195 KDNYFDrllrlVEPTPGEFNvLNHGDLWVNNIMFKyDDEGEPedvilVDFQLSRYGspaidlnYFLY 261
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
44-228 2.97e-03

N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This subfamily is composed of the N-terminal domains of vertebrate ACAD10 and ACAD11, and similar uncharacterized bacterial and eukaryotic proteins. ACADs are a family of flavoproteins that are involved in the beta-oxidation of fatty acyl-CoA derivatives. ACAD deficiency can cause metabolic disorders including muscle fatigue, hypoglycemia, and hepatic lipidosis. There are at least 11 distinct ACADs, some of which show distinct substrate specificities to either straight-chain or branched-chain fatty acids. ACAD10 is widely expressed in human tissues and highly expressed in liver, kidney, pancreas, and spleen. ACAD10 and ACAD11 are both significantly expressed in human brain tissues. They contain a long N-terminal domain with similarity to phosphotransferases with a Protein Kinase fold, which is absent in other ACADs. They may exhibit multiple functions in acyl-CoA oxidation pathways. ACAD11 utilizes substrates with carbon chain lengths of 20 to 26, with optimal activity towards C22CoA. ACAD10 may be associated with an increased risk in type II diabetes. The ACAD10/11-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: 270703 [Multi-domain]  Cd Length: 254  Bit Score: 38.75  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730  44 TYRIT---SHPDHQYLLRI----HIGKSNQAeIASELAFLRALNDHsDIEVPTGIASLDGSEVLEitaehddePPLLVtv 116
Cdd:cd05154    14 TYLVDaggDGGGRRLVLRRpppgGLLPSAHD-LEREYRVLRALAGT-GVPVPRVLALCEDPSVLG--------APFYV-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730 117 MKWMDGEPVHGAVMDN-------HAMAVGVM--IARLHaasmlfvpgenftrpSLDADSFK-GKFAKLANYRDRFVsdAD 186
Cdd:cd05154    82 MERVDGRVLPDPLPRPdlspeerRALARSLVdaLAALH---------------SVDPAALGlADLGRPEGYLERQV--DR 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2225572730 187 W-ALYQEAAA-------KVVSHLSEMKPTSENYGLIHGDLHLGNIVFRDG 228
Cdd:cd05154   145 WrRQLEAAATdpppaleEALRWLRANLPADGRPVLVHGDFRLGNLLFDPD 194
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
200-252 4.16e-03

Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic choline kinases, as well as eukaryotic ethanolamine kinase. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. Bacterial ChoK is also referred to as licA protein. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK 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: 270700 [Multi-domain]  Cd Length: 152  Bit Score: 37.15  E-value: 4.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2225572730 200 HLSEMKPtsenYGLIHGDLHLGNIVFRDGAPFPIDFGLCGYGYYLYDVASVML 252
Cdd:cd05151   100 HSSPLED----LVLCHNDLVPGNFLLDDDRLYLIDWEYAGMNDPLFDLAALFS 148
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
30-266 4.30e-03

Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group from ATP to aminoglycoside antibiotics such as kanamycin, streptomycin, neomycin, and gentamicin, among others. The aminoglycoside antibiotics target the 30S ribosome and promote miscoding, leading to the production of defective proteins which insert into the bacterial membrane, resulting in membrane damage and the ultimate demise of the bacterium. Phosphorylation of the aminoglycoside antibiotics results in their inactivation, leading to bacterial antibiotic resistance. The APH gene is found on transposons and plasmids and is thought to have originated as a self-defense mechanism used by microorganisms that produce the antibiotics. The APH 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: 270699 [Multi-domain]  Cd Length: 244  Bit Score: 38.33  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730  30 EWTGISyIQMSESVTYRITSHPDHQYLLRIHIGKSnqAEIASELAFLRALndHSDIEVPtgiasldgsEVLEiTAEHDDE 109
Cdd:cd05150     2 RWEPDT-IGESGARVYRLDGGGPVLYLKTAPAGYA--YELAREAERLRWL--AGKLPVP---------EVLD-YGSDDGG 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730 110 PPLLvtvMKWMDGEP-VHGAVMDNHAMAVGVM---IARLHAASMLFVPgenFTRpSLDAdsfkgKFAKL-ANYRDRFVSD 184
Cdd:cd05150    67 DWLL---TTALPGRDaASLEPLLDPERLVDLLaeaLRALHSLPIADCP---FDR-RLDA-----RLAEArARVEAGLVDE 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2225572730 185 ADW--ALYQEAAAKVVSHLSEMKPTSENYGLIHGDLHLGNIVFRDGAP--FpIDFGLCGYGYYLYDVASVM--LGLN-PT 257
Cdd:cd05150   135 DDFdeERQGRTAEELLAELEATRPAEEDLVVTHGDACLPNIILDPGRFsgF-IDLGRLGVADRYQDLALAVrsLRENlGG 213
                         250
                  ....*....|.
gi 2225572730 258 QRW--LLLDRY 266
Cdd:cd05150   214 EEYaeRFLDAY 224
 
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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