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Conserved domains on  [gi|23500787|ref|NP_700227|]
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ubiquinone biosynthesis protein UbiB [Brucella suis 1330]

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List of domain hits

Name Accession Description Interval E-value
UbiB cd13972
Ubiquinone biosynthetic protein UbiB; UbiB is the prokaryotic homolog of yeast Abc1p and human ...
95-342 7.73e-123

Ubiquinone biosynthetic protein UbiB; UbiB is the prokaryotic homolog of yeast Abc1p and human ADCK3 (aarF domain containing kinase 3). It is required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. It is required in the first monooxygenase step in Q biosynthesis. Mutant strains with disrupted ubiB genes lack Q and accumulate octaprenylphenol, a Q biosynthetic intermediate.


:

Pssm-ID: 270874  Cd Length: 247  Bit Score: 363.06  E-value: 7.73e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787  95 LQDRLDFFPQAGAVAAIEGSLGRKIDDLYVRFDA-PIAAASMAQVHPAEVmKDGapQKVAVKVIRPGVRQRFARDLESFF 173
Cdd:cd13972   2 LQDRVPPFSGKEARAIIEAELGKPLDALFSDFDEePVAAASIAQVHKARL-LDG--REVAVKVLRPGIEKRIERDLELLR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 174 MVARMQERHMPFTRRLRPVQVVETLSQTTRIEMDLRLEAAALSEIAENIKGDEGFRVPKVDWERTGRDVLTLEWIDGIKM 253
Cdd:cd13972  79 FLARLAERLLPEARRLRPVEVVKEFARSLLLELDLRLEAANASELRENFLDDPGFYVPEVYWELTSKNVLTMEWIDGIPI 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 254 SDIPALEAAGFDLKKLAETLIQSFLRHTLRDGFFHADMHPGNLFVDHQGLVVAVDFGITGRLDKQQRRFLAEILYGFITR 333
Cdd:cd13972 159 SDIEALDAAGIDRKALAERLVEIFFRQVFRDGFFHADMHPGNIFVDPNGRIIAVDFGIMGRLDKKDRRYLAEILYGFLTR 238

                ....*....
gi 23500787 334 DYMRVAEVH 342
Cdd:cd13972 239 DYRRVAELH 247
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
7-445 0e+00

2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the first hydroxylation step in the ubiquinone biosynthetic pathway in bacteria. It is believed that the reaction is 2-polyprenylphenol -> 6-hydroxy-2-polyprenylphenol. This model finds hits primarily in the proteobacteria. The gene is also known as AarF in certain species [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone].


:

Pssm-ID: 233667 [Multi-domain]  Cd Length: 437  Bit Score: 586.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787     7 VFRLMRAGWILTREGVISALPVEGLSGLPALGHRIAGFLARPRARQMERSERMSRAMNKLGPSYVKLGQFLATRPDIVGH 86
Cdd:TIGR01982   1 LRRLRRIIRVLIRYGFLALVESPIGPLSLRLLRRLLLPFSNRENRLMSRGERLRLALEELGPTFIKFGQTLSTRADLLPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787    87 DVAADLELLQDRLDFFPQAGAVAAIEGSLGRKIDDLYVRFD-APIAAASMAQVHPAEVMKDgapQKVAVKVIRPGVRQRF 165
Cdd:TIGR01982  81 DIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEeKPLAAASIAQVHRARLVDG---KEVAVKVLRPGIEKTI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787   166 ARDLESFFMVARMQERHMPFTRRLRPVQVVETLSQTTRIEMDLRLEAAALSEIAENIKGDEGFRVPKVDWERTGRDVLTL 245
Cdd:TIGR01982 158 AADIALLYRLARIVERLSPDSRRLRPTEVVKEFEKTLRRELDLRREAANASELGENFKNDPGVYVPEVYWDRTSERVLTM 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787   246 EWIDGIKMSDIPALEAAGFDLKKLAETLIQSFLRHTLRDGFFHADMHPGNLFVDHQGLVVAVDFGITGRLDKQQRRFLAE 325
Cdd:TIGR01982 238 EWIDGIPLSDIAALDEAGLDRKALAENLARSFLNQVLRDGFFHADLHPGNIFVLKDGKIIALDFGIVGRLSEEDRRYLAE 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787   326 ILYGFITRDYMRVAEVHFEAGYVPYTHDVASFAQAIRAIGEPIHGQPAETISMAKLLTLLFEVTELFDMETRPELLMLQK 405
Cdd:TIGR01982 318 ILYGFLNRDYRRVAEVHFDAGYVPSDTDMAEFEQAIRAIGEPIFGQPLKEISVGRLLAGLFKITRDFNMELQPQLLLLQK 397
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 23500787   406 TMVVVEGVSRTLDPHFNMWKAAEPVVGDWIRKNLGPQGMV 445
Cdd:TIGR01982 398 TLLTVEGVGRQLDPDLNMWKVAEPFVKRWIRKRLGPKAKI 437
 
Name Accession Description Interval E-value
UbiB cd13972
Ubiquinone biosynthetic protein UbiB; UbiB is the prokaryotic homolog of yeast Abc1p and human ...
95-342 7.73e-123

Ubiquinone biosynthetic protein UbiB; UbiB is the prokaryotic homolog of yeast Abc1p and human ADCK3 (aarF domain containing kinase 3). It is required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. It is required in the first monooxygenase step in Q biosynthesis. Mutant strains with disrupted ubiB genes lack Q and accumulate octaprenylphenol, a Q biosynthetic intermediate.


Pssm-ID: 270874  Cd Length: 247  Bit Score: 363.06  E-value: 7.73e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787  95 LQDRLDFFPQAGAVAAIEGSLGRKIDDLYVRFDA-PIAAASMAQVHPAEVmKDGapQKVAVKVIRPGVRQRFARDLESFF 173
Cdd:cd13972   2 LQDRVPPFSGKEARAIIEAELGKPLDALFSDFDEePVAAASIAQVHKARL-LDG--REVAVKVLRPGIEKRIERDLELLR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 174 MVARMQERHMPFTRRLRPVQVVETLSQTTRIEMDLRLEAAALSEIAENIKGDEGFRVPKVDWERTGRDVLTLEWIDGIKM 253
Cdd:cd13972  79 FLARLAERLLPEARRLRPVEVVKEFARSLLLELDLRLEAANASELRENFLDDPGFYVPEVYWELTSKNVLTMEWIDGIPI 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 254 SDIPALEAAGFDLKKLAETLIQSFLRHTLRDGFFHADMHPGNLFVDHQGLVVAVDFGITGRLDKQQRRFLAEILYGFITR 333
Cdd:cd13972 159 SDIEALDAAGIDRKALAERLVEIFFRQVFRDGFFHADMHPGNIFVDPNGRIIAVDFGIMGRLDKKDRRYLAEILYGFLTR 238

                ....*....
gi 23500787 334 DYMRVAEVH 342
Cdd:cd13972 239 DYRRVAELH 247
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
4-525 2.38e-126

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310  Cd Length: 537  Bit Score: 382.72  E-value: 2.38e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787    4 LSAVFRLMRAGWILTREGVISALPVEGLSGLPALGHRIAgFLARPRARQMERSERMSRAMNKLGPSYVKLGQFLATRPDI 83
Cdd:PRK04750   1 PMELFRLYKIIRVFLRYGLDELILSHRLTRPLRLWRRSL-FWMPNRHKDKPRGERLRLALEELGPIFVKFGQMLSTRRDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787   84 VGHDVAADLELLQDRLDFFPQAGAVAAIEGSLGRKIDDLYVRFDA-PIAAASMAQVHPAeVMKDGApQKVAVKVIRPGVR 162
Cdd:PRK04750  80 FPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIkPLASASIAQVHFA-RLKDNG-REVVVKVLRPDIL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787  163 QRFARDLESFFMVARMQERHMPFTRRLRPVQVVETLSQTTRIEMDLRLEAAALSEIAENIKGDEGFRVPKVDWERTGRDV 242
Cdd:PRK04750 158 PVIDADLALMYRLARWVERLLPDGRRLKPREVVAEFEKTLHDELDLMREAANASQLRRNFEDSDMLYVPEVYWDYCSETV 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787  243 LTLEWIDGIKMSDIPALEAAGFDLKKLAETLIQSFLRHTLRDGFFHADMHPGNLFVD----HQGLVVAVDFGITGRLDKQ 318
Cdd:PRK04750 238 MVMERMYGIPVSDVAALRAAGTDMKLLAERGVEVFFTQVFRDGFFHADMHPGNIFVSydppENPRYIALDFGIVGSLNKE 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787  319 QRRFLAEILYGFITRDYMRVAEVHFEAGYVPYTHDVASFAQAIRAIGEPIHGQPAETISMAKLLTLLFEVTELFDMETRP 398
Cdd:PRK04750 318 DKRYLAENFLAFFNRDYRRVAELHVESGWVPPDTRVEELEFAIRAVCEPIFDKPLAEISFGHVLLRLFNTARRFNVEIQP 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787  399 ELLMLQKTMVVVEGVSRTLDPHFNMWKAAEPVVGDWIRKNLGPQGMVLDAKESAyalLHFTRKTPELLQRIDRisvALDT 478
Cdd:PRK04750 398 QLVLLQKTLLNVEGLGRQLDPQLDLWKTAKPFLERWMKEQVGPRALVRALKEEA---PFWAEKLPELPRLVHD---SLRQ 471
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 23500787  479 MAANGLRFDDATAEAigraeAQHSRWGRIAQVVIAVSMAAIAIKLYI 525
Cdd:PRK04750 472 GKLLQHSVDLLAEQL-----RTNRLRQGQSRYLLGVGATLLLAGTLL 513
ABC1 pfam03109
ABC1 family; This family includes ABC1 from yeast and AarF from Escherichia coli. These ...
114-234 4.22e-31

ABC1 family; This family includes ABC1 from yeast and AarF from Escherichia coli. These proteins have a nuclear or mitochondrial subcellular location in eukaryotes. The exact molecular functions of these proteins is not clear, however yeast ABC1 suppresses a cytochrome b mRNA translation defect and is essential for the electron transfer in the bc 1 complex and Escherichia coli AarF is required for ubiquinone production. It has been suggested that members of the ABC1 family are novel chaperonins. These proteins are unrelated to the ABC transporter proteins.


Pssm-ID: 111949  Cd Length: 117  Bit Score: 116.54  E-value: 4.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787   114 SLGRKIDDLYVRFD-APIAAASMAQVHPAeVMKDGapQKVAVKVIRPGVRQRFARDLESFFMVARMQERHMPftrRLRPV 192
Cdd:pfam03109   2 ELGAPVEEVFAEFDeEPIAAASIAQVHRA-VLKDG--EEVAVKVQRPGVKKRIRSDLKLLKFLAKILKKFFP---GFDLD 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 23500787   193 QVVETLSQTTRIEMDLRLEAAALSEIAENIKGDEGFRVPKVD 234
Cdd:pfam03109  76 WLVDEFRKSLPQELDFLREAANAEKFRENFADLPWVYVPKVY 117
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
7-445 0e+00

2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the first hydroxylation step in the ubiquinone biosynthetic pathway in bacteria. It is believed that the reaction is 2-polyprenylphenol -> 6-hydroxy-2-polyprenylphenol. This model finds hits primarily in the proteobacteria. The gene is also known as AarF in certain species [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone].


Pssm-ID: 233667 [Multi-domain]  Cd Length: 437  Bit Score: 586.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787     7 VFRLMRAGWILTREGVISALPVEGLSGLPALGHRIAGFLARPRARQMERSERMSRAMNKLGPSYVKLGQFLATRPDIVGH 86
Cdd:TIGR01982   1 LRRLRRIIRVLIRYGFLALVESPIGPLSLRLLRRLLLPFSNRENRLMSRGERLRLALEELGPTFIKFGQTLSTRADLLPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787    87 DVAADLELLQDRLDFFPQAGAVAAIEGSLGRKIDDLYVRFD-APIAAASMAQVHPAEVMKDgapQKVAVKVIRPGVRQRF 165
Cdd:TIGR01982  81 DIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEeKPLAAASIAQVHRARLVDG---KEVAVKVLRPGIEKTI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787   166 ARDLESFFMVARMQERHMPFTRRLRPVQVVETLSQTTRIEMDLRLEAAALSEIAENIKGDEGFRVPKVDWERTGRDVLTL 245
Cdd:TIGR01982 158 AADIALLYRLARIVERLSPDSRRLRPTEVVKEFEKTLRRELDLRREAANASELGENFKNDPGVYVPEVYWDRTSERVLTM 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787   246 EWIDGIKMSDIPALEAAGFDLKKLAETLIQSFLRHTLRDGFFHADMHPGNLFVDHQGLVVAVDFGITGRLDKQQRRFLAE 325
Cdd:TIGR01982 238 EWIDGIPLSDIAALDEAGLDRKALAENLARSFLNQVLRDGFFHADLHPGNIFVLKDGKIIALDFGIVGRLSEEDRRYLAE 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787   326 ILYGFITRDYMRVAEVHFEAGYVPYTHDVASFAQAIRAIGEPIHGQPAETISMAKLLTLLFEVTELFDMETRPELLMLQK 405
Cdd:TIGR01982 318 ILYGFLNRDYRRVAEVHFDAGYVPSDTDMAEFEQAIRAIGEPIFGQPLKEISVGRLLAGLFKITRDFNMELQPQLLLLQK 397
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 23500787   406 TMVVVEGVSRTLDPHFNMWKAAEPVVGDWIRKNLGPQGMV 445
Cdd:TIGR01982 398 TLLTVEGVGRQLDPDLNMWKVAEPFVKRWIRKRLGPKAKI 437
AarF COG0661
Predicted unusual protein kinase [General function prediction only]
1-524 0e+00

Predicted unusual protein kinase [General function prediction only]


Pssm-ID: 223733 [Multi-domain]  Cd Length: 517  Bit Score: 561.93  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787   1 MSNLSAVFRLMRAGWILTREGVISALPVEGLSGLPALGHRIAG--FLARPRARQMERSERMSRAMNKLGPSYVKLGQFLA 78
Cdd:COG0661   1 MLTLYAVSRLPRIIRVRLRYLLGRLLRLTGRLALLLRLLSWLGksKLASSEELREKRAERLRLALEELGPTFIKLGQILS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787  79 TRPDIVGHDVAADLELLQDRLDFFPQAGAVAAIEGSLGRKIDDLYVRFDA-PIAAASMAQVHPAEVmKDGapQKVAVKVI 157
Cdd:COG0661  81 TRPDLVPPEYAEELAKLQDRVPPFPFEEAERIIEEELGRPIEELFSEFEPePIASASIAQVHRAVL-KSG--EEVAVKVQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 158 RPGVRQRFARDLESFFMVARMQERHMPFTRRLRPVQVVETLSQTTRIEMDLRLEAAALSEIAENIKGDEGFRVPKVDWER 237
Cdd:COG0661 158 RPGIRERIEADLKLLRRLARLIKRLPPGGRRLDLVEVVDEFEKRLREELDYRREAANAERFRENFKDDPDVYVPKVYWEY 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 238 TGRDVLTLEWIDGIKMSDIPALEAAGFDLKKLAETLIQSFLRHTLRDGFFHADMHPGNLFVDHQGLVVAVDFGITGRLDK 317
Cdd:COG0661 238 TTRRVLTMEWIDGIKISDIAALKSAGIDRKELAELLVRAFLRQLLRDGFFHADPHPGNILVRSDGRIVLLDFGIVGRLDP 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 318 QQRRFLAEILYGFITRDYMRVAEVHFEAGYVPYTHDVASFAQAIRAIGEPIHGQPAETISMAKLLTLLFEVTELFDMETR 397
Cdd:COG0661 318 KFRRYLAELLLAFLNRDYDRVAELHVELGYVPPDTDRDPLAAAIRAVLEPIYGKPLEEISFGEILDKLFEVARRFPMRLP 397
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 398 PELLMLQKTMVVVEGVSRTLDPHFNMWKAAEPVVGDWIRKNLGPQgMVLDAKESAYALLHFTRKTPELLQRIDRIsvald 477
Cdd:COG0661 398 PELVLLQRTLLLVEGVGRQLDPRFNLWAVAQPLLAKWLKKQLSPK-LLRELKDEAVAVLNALPLLPRLLRDLLDN----- 471
                       490       500       510       520
                ....*....|....*....|....*....|....*....|....*..
gi 23500787 478 TMAANGLRFDDATAEAIGRAEAQHSrWGRIAQVVIAVSMAAIAIKLY 524
Cdd:COG0661 472 DREELSLRSSEELALLLLKAVARLS-IGSILLVVLAVTVLLIAILLL 517
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
267-347 6.70e-05

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 43.29  E-value: 6.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787    267 KKLAETLIQSFLRHTLR-------DGFFHADMHPGNLFVDHQGLVVAVDFGITGRLDKQQRrflaeiLYGFI-TRDYMrv 338
Cdd:smart00220  92 GRLSEDEARFYLRQILSaleylhsKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEK------LTTFVgTPEYM-- 163
                           90
                   ....*....|
gi 23500787    339 A-EVHFEAGY 347
Cdd:smart00220 164 ApEVLLGKGY 173
Pkinase pfam00069
Protein kinase domain;
234-357 4.40e-04

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 40.69  E-value: 4.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787   234 DWERTGRDV-LTLEWIDGIKMSDIpaLEAAGfdlkKLAETLIQSFLRHTLR-------DGFFHADMHPGNLFVDHQGLVV 305
Cdd:pfam00069  65 DAFEDKDHLyLVMEYCEGGDLFDY--LSRGG----PLSEDEAKKIALQILRgleylhsNGIIHRDLKPENILLDENGVVK 138
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 23500787   306 AVDFGITGRLDKQQRRFlaeilYGFI-TRDYMrvA-EVHFEAGYVPYTHDVASF 357
Cdd:pfam00069 139 IADFGLAKKLTKSSSSL-----TTFVgTPEYM--ApEVLLGGNGYGPKVDVWSL 185
 
Name Accession Description Interval E-value
UbiB cd13972
Ubiquinone biosynthetic protein UbiB; UbiB is the prokaryotic homolog of yeast Abc1p and human ...
95-342 7.73e-123

Ubiquinone biosynthetic protein UbiB; UbiB is the prokaryotic homolog of yeast Abc1p and human ADCK3 (aarF domain containing kinase 3). It is required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. It is required in the first monooxygenase step in Q biosynthesis. Mutant strains with disrupted ubiB genes lack Q and accumulate octaprenylphenol, a Q biosynthetic intermediate.


Pssm-ID: 270874  Cd Length: 247  Bit Score: 363.06  E-value: 7.73e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787  95 LQDRLDFFPQAGAVAAIEGSLGRKIDDLYVRFDA-PIAAASMAQVHPAEVmKDGapQKVAVKVIRPGVRQRFARDLESFF 173
Cdd:cd13972   2 LQDRVPPFSGKEARAIIEAELGKPLDALFSDFDEePVAAASIAQVHKARL-LDG--REVAVKVLRPGIEKRIERDLELLR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 174 MVARMQERHMPFTRRLRPVQVVETLSQTTRIEMDLRLEAAALSEIAENIKGDEGFRVPKVDWERTGRDVLTLEWIDGIKM 253
Cdd:cd13972  79 FLARLAERLLPEARRLRPVEVVKEFARSLLLELDLRLEAANASELRENFLDDPGFYVPEVYWELTSKNVLTMEWIDGIPI 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 254 SDIPALEAAGFDLKKLAETLIQSFLRHTLRDGFFHADMHPGNLFVDHQGLVVAVDFGITGRLDKQQRRFLAEILYGFITR 333
Cdd:cd13972 159 SDIEALDAAGIDRKALAERLVEIFFRQVFRDGFFHADMHPGNIFVDPNGRIIAVDFGIMGRLDKKDRRYLAEILYGFLTR 238

                ....*....
gi 23500787 334 DYMRVAEVH 342
Cdd:cd13972 239 DYRRVAELH 247
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
4-525 2.38e-126

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310  Cd Length: 537  Bit Score: 382.72  E-value: 2.38e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787    4 LSAVFRLMRAGWILTREGVISALPVEGLSGLPALGHRIAgFLARPRARQMERSERMSRAMNKLGPSYVKLGQFLATRPDI 83
Cdd:PRK04750   1 PMELFRLYKIIRVFLRYGLDELILSHRLTRPLRLWRRSL-FWMPNRHKDKPRGERLRLALEELGPIFVKFGQMLSTRRDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787   84 VGHDVAADLELLQDRLDFFPQAGAVAAIEGSLGRKIDDLYVRFDA-PIAAASMAQVHPAeVMKDGApQKVAVKVIRPGVR 162
Cdd:PRK04750  80 FPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIkPLASASIAQVHFA-RLKDNG-REVVVKVLRPDIL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787  163 QRFARDLESFFMVARMQERHMPFTRRLRPVQVVETLSQTTRIEMDLRLEAAALSEIAENIKGDEGFRVPKVDWERTGRDV 242
Cdd:PRK04750 158 PVIDADLALMYRLARWVERLLPDGRRLKPREVVAEFEKTLHDELDLMREAANASQLRRNFEDSDMLYVPEVYWDYCSETV 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787  243 LTLEWIDGIKMSDIPALEAAGFDLKKLAETLIQSFLRHTLRDGFFHADMHPGNLFVD----HQGLVVAVDFGITGRLDKQ 318
Cdd:PRK04750 238 MVMERMYGIPVSDVAALRAAGTDMKLLAERGVEVFFTQVFRDGFFHADMHPGNIFVSydppENPRYIALDFGIVGSLNKE 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787  319 QRRFLAEILYGFITRDYMRVAEVHFEAGYVPYTHDVASFAQAIRAIGEPIHGQPAETISMAKLLTLLFEVTELFDMETRP 398
Cdd:PRK04750 318 DKRYLAENFLAFFNRDYRRVAELHVESGWVPPDTRVEELEFAIRAVCEPIFDKPLAEISFGHVLLRLFNTARRFNVEIQP 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787  399 ELLMLQKTMVVVEGVSRTLDPHFNMWKAAEPVVGDWIRKNLGPQGMVLDAKESAyalLHFTRKTPELLQRIDRisvALDT 478
Cdd:PRK04750 398 QLVLLQKTLLNVEGLGRQLDPQLDLWKTAKPFLERWMKEQVGPRALVRALKEEA---PFWAEKLPELPRLVHD---SLRQ 471
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 23500787  479 MAANGLRFDDATAEAigraeAQHSRWGRIAQVVIAVSMAAIAIKLYI 525
Cdd:PRK04750 472 GKLLQHSVDLLAEQL-----RTNRLRQGQSRYLLGVGATLLLAGTLL 513
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
95-341 8.42e-85

Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and similar proteins; This family is composed of the atypical yeast protein kinase Abc1p, its human homolog ADCK3 (also called CABC1), and similar proteins. Abc1p (also called Coq8p) is required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. It is necessary for the formation of a multi-subunit Q-biosynthetic complex and may also function in the regulation of Q synthesis. Human ADCK3 is able to rescue defects in Q synthesis and the phosphorylation state of Coq proteins in yeast Abc1 (or Coq8) mutants. Mutations in ADCK3 cause progressive cerebellar ataxia and atrophy due to Q10 deficiency. Eukaryotes contain at least two more ABC1/ADCK3-like proteins: in humans, these are the putative atypical protein kinases named ADCK1 and ADCK2. In algae and higher plants, ABC1 kinases have proliferated to more than 15 subfamilies, most of which are located in plastids or mitochondria. Eight of these plant ABC1 kinase subfamilies (ABC1K1-8) are specific for photosynthetic organisms. ABC1 kinases are not related to the ATP-binding cassette (ABC) membrane transporter family.


Pssm-ID: 270691 [Multi-domain]  Cd Length: 247  Bit Score: 265.13  E-value: 8.42e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787  95 LQDRLDFFPQAGAVAAIEGSLGRKIDDLYVRFD-APIAAASMAQVHPAeVMKDGapQKVAVKVIRPGVRQRFARDLESFF 173
Cdd:cd05121   2 LQDDVPPFPFEEVRKIIEEELGRPLEEVFAEFDpEPLAAASIAQVHRA-RLKDG--REVAVKVQRPGIEEIIEADLRILR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 174 MVARMQERHMPFTRRLRPVQVVETLSQTTRIEMDLRLEAAALSEIAENIKGDEGFRVPKVDWERTGRDVLTLEWIDGIKM 253
Cdd:cd05121  79 RLARLLERLSPLLRRLDLVAIVDEFARSLLEELDFRREARNAERFRKNLKDSPDVYVPKVYPELSTRRVLVMEYIDGVKL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 254 SDIPALEAAGFDLKKLAETLIQSFLRHTLRDGFFHADMHPGNLFVDHQGLVVAVDFGITGRLDKQQRRFLAEILYGFITR 333
Cdd:cd05121 159 TDLEALRAAGIDRKELARRLVDAYLKQIFEDGFFHADPHPGNILVLPDGRIALLDFGMVGRLDPETREALADLLLALVNG 238

                ....*...
gi 23500787 334 DYMRVAEV 341
Cdd:cd05121 239 DAEGLAEA 246
ADCK1-like cd13969
aarF domain containing kinase 1 and similar proteins; This subfamily is composed of ...
95-341 3.88e-52

aarF domain containing kinase 1 and similar proteins; This subfamily is composed of uncharacterized ABC1 kinase-like proteins including the human protein called aarF domain containing kinase 1 (ADCK1). Eukaryotes contain at least three ABC1-like proteins: in humans, these are ADCK3 and the putative protein kinases named ADCK1 and ADCK2. Yeast Abc1p and its human homolog ADCK3 are atypical protein kinases required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. In algae and higher plants, ABC1 kinases have proliferated to more than 15 subfamilies, most of which are located in plastids or mitochondria. Plant subfamilies 14 and 15 (ABC1K14-15) belong to the same group of ABC1 kinases as human ADCK1. ABC1 kinases are not related to the ATP-binding cassette (ABC) membrane transporter family.


Pssm-ID: 270871  Cd Length: 253  Bit Score: 179.22  E-value: 3.88e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787  95 LQDRLDFFPQAGAVAAIEGSLGRKIDDLYVRFD-APIAAASMAQVHPAeVMKDGapQKVAVKVIRPGVRQRFARDLESFF 173
Cdd:cd13969   2 LQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDeEPIASASLAQVHKA-KLKDG--EEVAVKVQHPDLRKQFAGDLATME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 174 MVARMQER---HMPFTrrlrpvQVVETLSQTTRIEMDLRLEAAALSEIAENIKGDEGFRVPKVDWERTGRDVLTLEWIDG 250
Cdd:cd13969  79 FLVNLVEKlfpDFPFS------WLVDELKKNLPKELDFLNEARNAERCAKLFKHRPDVYVPKVYWDLSSKRVLTMEFIDG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 251 IKMSDIPALEAAGFDLKKLAETLIQSFLRHTLRDGFFHADMHPGNLFV-----DHQGLVVAVDFGITGRLDKQQRRFLAE 325
Cdd:cd13969 153 IKIDDVEALKKLGIDPKEVARLLSEAFAEMIFVHGFVHCDPHPGNLLVrknpgPGKPQIVLLDHGLYRELDEEFRLNYCR 232
                       250
                ....*....|....*.
gi 23500787 326 ILYGFITRDYMRVAEV 341
Cdd:cd13969 233 LWKALILGDEKKIKKY 248
ABC1_ADCK3 cd13970
Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This ...
92-346 4.94e-42

Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This subfamily is composed of the atypical yeast protein kinase Abc1p, its human homolog ADCK3 (also called CABC1), and similar proteins. Abc1p (also called Coq8p) is required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. It is necessary for the formation of a multi-subunit Q-biosynthetic complex and may also function in the regulation of Q synthesis. Human ADCK3 is able to rescue defects in Q synthesis and the phosphorylation state of Coq proteins in yeast Abc1 (or Coq8) mutants. Mutations in ADCK3 cause progressive cerebellar ataxia and atrophy due to Q10 deficiency. In algae and higher plants, ABC1 kinases have proliferated to more than 15 subfamilies, most of which are located in plastids or mitochondria. Subfamily 13 (ABC1K13) of plant ABC1 kinases belongs in this subfamily with yeast Abc1p and human ADCK3. ABC1 kinases are not related to the ATP-binding cassette (ABC) membrane transporter family.


Pssm-ID: 270872  Cd Length: 251  Bit Score: 151.51  E-value: 4.94e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787  92 LELLQDRLDFFPQAGAVAAIEGSLGRKIDDLYVRFDA-PIAAASMAQVHPAeVMKDGapQKVAVKVIRPGVRQRFARDLE 170
Cdd:cd13970   3 LARLRDSAPPMPWAQLEKVLEAELGEDWRELFAEFDEePFAAASIGQVHRA-TLKDG--REVAVKVQYPGVAESIDSDLN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 171 SFFMVARMqERHMPFTRRLRpvQVVETLSQTTRIEMDLRLEAAALSEIAENIKGDEGFRVPKVDWERTGRDVLTLEWIDG 250
Cdd:cd13970  80 NLRRLLKL-TGLLPKGLDLD--ALIAELREELLEECDYEREAANQRRFRELLADDPRFVVPEVIPELSTKRVLTTEFVDG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 251 IKMSDIPALEAAGFDlkKLAETLIQSFLRHTLRDGFFHADMHPGNLFVD-HQGLVVAVDFGITGRLDKQQRRFLAEILYG 329
Cdd:cd13970 157 VPLDEAADLSQEERN--RIGELLLRLCLRELFEFGFMQTDPNPGNFLYDpEDGRLGLLDFGAVREYPPEFVDGYRRLVRA 234
                       250
                ....*....|....*..
gi 23500787 330 FITRDYMRVAEVHFEAG 346
Cdd:cd13970 235 ALEGDREALLEASVELG 251
ADCK2-like cd13971
aarF domain containing kinase 2 and similar proteins; This subfamily is composed of ...
110-340 1.26e-40

aarF domain containing kinase 2 and similar proteins; This subfamily is composed of uncharacterized ABC1 kinase-like proteins including the human protein called aarF domain containing kinase 2 (ADCK2). Eukaryotes contain at least three ABC1-like proteins; in humans, these are ADCK3 and the putative protein kinases named ADCK1 and ADCK2. Yeast Abc1p and its human homolog ADCK3 are atypical protein kinases required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. In algae and higher plants, ABC1 kinases have proliferated to more than 15 subfamilies, most of which are located in plastids or mitochondria. Plant subfamily 10 (ABC1K10) belong to the same group of ABC1 kinases as human ADCK2. ABC1 kinases are not related to the ATP-binding cassette (ABC) membrane transporter family.


Pssm-ID: 270873 [Multi-domain]  Cd Length: 298  Bit Score: 148.91  E-value: 1.26e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 110 AIEGSLGRKIDDLYVRFDA-PIAAASMAQVHPAEVMKDGA-----PQKVAVKVIRPGVRQRFARDLESFFMVARMQErHM 183
Cdd:cd13971  17 ALEAAFGKDWEDIFEEFDEePIGSGSIAQVHRAKLKPDYGgdgggPRVVAVKVLHPGVREQIERDLAILRLFAKLLE-AI 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 184 PFTRRLRPVQVVETLSQTTRIEMDLRLEAAALSEIAENIKGDEGFRVPKVDWERTGRDVLTLEWIDGIKMSDIpALEAAG 263
Cdd:cd13971  96 PPLRWLSLPESVEQFASLMLRQLDLRVEAANLERFRENFKDRKDVSFPKPLYPLVTEEVLVETFEEGVPISRT-VLAHGG 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 264 FDLKK-LAETLIQSFLRHTLRDGFFHADMHPGNLFVDHQGL-----------------VVAVDFGITGRLDKQQRRFLAE 325
Cdd:cd13971 175 EPLKRkLARIGLDAFLKMLFVDNFVHGDLHPGNILVRFNDSnrpsllvsldargspprLVFLDAGLVTELSPQDRRNFID 254
                       250
                ....*....|....*
gi 23500787 326 ILYGFITRDYMRVAE 340
Cdd:cd13971 255 LFKAVARGDGYKAAE 269
ABC1 pfam03109
ABC1 family; This family includes ABC1 from yeast and AarF from Escherichia coli. These ...
114-234 4.22e-31

ABC1 family; This family includes ABC1 from yeast and AarF from Escherichia coli. These proteins have a nuclear or mitochondrial subcellular location in eukaryotes. The exact molecular functions of these proteins is not clear, however yeast ABC1 suppresses a cytochrome b mRNA translation defect and is essential for the electron transfer in the bc 1 complex and Escherichia coli AarF is required for ubiquinone production. It has been suggested that members of the ABC1 family are novel chaperonins. These proteins are unrelated to the ABC transporter proteins.


Pssm-ID: 111949  Cd Length: 117  Bit Score: 116.54  E-value: 4.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787   114 SLGRKIDDLYVRFD-APIAAASMAQVHPAeVMKDGapQKVAVKVIRPGVRQRFARDLESFFMVARMQERHMPftrRLRPV 192
Cdd:pfam03109   2 ELGAPVEEVFAEFDeEPIAAASIAQVHRA-VLKDG--EEVAVKVQRPGVKKRIRSDLKLLKFLAKILKKFFP---GFDLD 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 23500787   193 QVVETLSQTTRIEMDLRLEAAALSEIAENIKGDEGFRVPKVD 234
Cdd:pfam03109  76 WLVDEFRKSLPQELDFLREAANAEKFRENFADLPWVYVPKVY 117
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
225-309 7.63e-07

C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is present in archaea and eukaryotes. It contains an N-terminal winged helix (wHTH) domain and a C-terminal RIO kinase catalytic domain. The wHTH domain is primarily seen in DNA-binding proteins, although some wHTH domains may be involved in RNA recognition. RIO2 is essential for survival and is necessary for rRNA cleavage during 40S ribosomal subunit maturation. RIO kinases are atypical protein serine kinases containing a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. The RIO2 kinase catalytic domain 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), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270695  Cd Length: 183  Bit Score: 48.27  E-value: 7.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 225 DEGFRVPK-VDWERtgrDVLTLEWIDGIKMSDIPALEaagfDLKKLAETLIqSFLRHTLRDGFFHADMHPGNLFVDHQGL 303
Cdd:cd05144  77 EEGFPVPKpIDWNR---HAVVMELIDGYPLYQVRLLE----DPEEVLDEIL-ELIVKLAKHGLIHGDFSEFNILVDEDEK 148

                ....*.
gi 23500787 304 VVAVDF 309
Cdd:cd05144 149 ITVIDF 154
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed ...
201-310 1.30e-06

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  Cd Length: 158  Bit Score: 46.91  E-value: 1.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 201 TTRIEMDLRLEAAALSEIAENIkgdeGFRVPKV--DWERTGRDVLTLEWIDGIKMSDIPAL--EAAGFDLKK-LAETLIQ 275
Cdd:cd05120  29 PPRLKKDLEKEAAMLQLLAGKL----SLPVPKVygFGESDGWEYLLMERIEGETLSEVWPRlsEEEKEKIADqLAEILAA 104
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 23500787 276 sfLRHTLRDGFFHADMHPGNLFVDHQGLVVA-VDFG 310
Cdd:cd05120 105 --LHRIDSSVLTHGDLHPGNILVKPDGKLSGiIDWE 138
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
265-310 1.13e-03

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 39.44  E-value: 1.13e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 23500787 265 DLKKLAETLIQSFLRHTL-------RDGFFHADMHPGNLFVDHQGLVVAVDFG 310
Cdd:cd07830  92 KGKPFSESVIRSIIYQILqglahihKHGFFHRDLKPENLLVSGPEVVKIADFG 144
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
269-336 1.35e-03

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 39.39  E-value: 1.35e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 269 LAETLIQSFLRHtlRDGFFHADMHPGNLFVDHQGLVVAVDFGIT--GRLDKQQRRFLAeilygfiTRDYM 336
Cdd:cd05611 103 IAEVVLGVEDLH--QRGIIHRDIKPENLLIDQTGHLKLTDFGLSrnGLEKRHNKKFVG-------TPDYL 163
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
269-316 1.46e-03

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 39.05  E-value: 1.46e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23500787 269 LAETLIQSFLRHTLR-------DGFFHADMHPGNLFVDHQGLVVAVDFGITGRLD 316
Cdd:cd06628 103 FEESLVRNFVRQILKglnylhnRGIIHRDIKGANILVDNKGGIKISDFGISKKLE 157
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
203-372 1.76e-03

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 38.88  E-value: 1.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 203 RIEMD-LRLEAAALSEIA-ENIKGDEG-FRVPKVDWertgrdvLTLEWIDGIKMSDI--PALEAAGFDlkklaETLIQSF 277
Cdd:cd06610  40 QTSMDeLRKEIQAMSQCNhPNVVSYYTsFVVGDELW-------LVMPLLSGGSLLDImkSSYPRGGLD-----EAIIATV 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 278 LRHTL-------RDGFFHADMHPGNLFVDHQGLVVAVDFGITGRL-DKQQRRFLAeiLYGFI-TRDYMRVAEVHFEAGYv 348
Cdd:cd06610 108 LKEVLkgleylhSNGQIHRDVKAGNILLGEDGSVKIADFGVSASLaTGGDRTRKV--RKTFVgTPCWMAPEVMEQVRGY- 184
                       170       180
                ....*....|....*....|....
gi 23500787 349 PYTHDVASFaqAIRAIgEPIHGQP 372
Cdd:cd06610 185 DFKADIWSF--GITAI-ELATGAA 205
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
267-310 2.67e-03

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 38.27  E-value: 2.67e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 23500787 267 KKLAETLIQSFLRHTL-------RDGFFHADMHPGNLFVDHQGLVVAVDFG 310
Cdd:cd06606  94 GKLPEPVVRKYTRQILegleylhSNGIVHRDIKGANILVDSDGVVKLADFG 144
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
125-336 2.96e-03

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 38.34  E-value: 2.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 125 RFDAPIAAASMAQVHPAEVMKDGapQKVAVKVIRPG------VRQRFARDLESffmVARMQERHMpftrrlrpVQVVETL 198
Cdd:cd14014   3 RLVRLLGRGGMGEVYRARDTLLG--RPVAIKVLRPElaedeeFRERFLREARA---LARLSHPNI--------VRVYDVG 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 199 SQTTR--IEMDLrLEAAALSEIaenIKGDEGFRVPKVdwERTGRDVLtlewidgikmsdiPALEAAgfdlkklaetliqs 276
Cdd:cd14014  70 EDDGRpyIVMEY-VEGGSLADL---LRERGPLPPREA--LRILAQIA-------------DALAAA-------------- 116
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 277 flrHtlRDGFFHADMHPGNLFVDHQGLVVAVDFGITGRLDKQQRRFLAEILYgfiTRDYM 336
Cdd:cd14014 117 ---H--RAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTGSVLG---TPAYM 168
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
269-336 3.41e-03

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 38.05  E-value: 3.41e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23500787 269 LAETLIQSFLRHTLR-------DGFFHADMHPGNLFVDHQGLVVAVDFGITGRLDKQQRRFLAEILYGF-ITRDYM 336
Cdd:cd06626  96 LDEAVIRVYTLQLLEglaylheNGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNNTTTMAPGEVNSLvGTPAYM 171
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
277-405 4.97e-03

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 37.43  E-value: 4.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 277 FLrHTLRDGFFHADMHPGNLFVDHQGLVVAVDFG---ITGRLDKQQRRFLAEILYGfiTRDYMrvAEVHFEAGYVPYT-- 351
Cdd:cd13978 108 FL-HNMDPPLLHHDLKPENILLDNHFHVKISDFGlskLGMKSISANRRRGTENLGG--TPIYM--APEAFDDFNKKPTsk 182
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23500787 352 HDVASFAQAIRAI---GEPIHGQPAETISMAKLLT----LLFEVTELFDMETRPELLMLQK 405
Cdd:cd13978 183 SDVYSFAIVIWAVltrKEPFENAINPLLIMQIVSKgdrpSLDDIGRLKQIENVQELISLMI 243
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
266-315 8.56e-03

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 36.94  E-value: 8.56e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 23500787 266 LKKLAETLIQ--SFLRHTLrdGFFHADMHPGNLFVDHQGLVVAVDFGITGRL 315
Cdd:cd06605 101 LGKIAVAVVKglIYLHEKH--KIIHRDVKPSNILVNSRGQVKLCDFGVSGQL 150
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
239-320 9.80e-03

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 36.96  E-value: 9.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 239 GRDVLTLewidgIKMSDIPALEAAGFdlkKLAETLIQSFLRHTLrdGFFHADMHPGNLFVDHQGLVVAVDFGITGRLDKQ 318
Cdd:cd05627  86 GGDMMTL-----LMKKDTLSEEATQF---YIAETVLAIDAIHQL--GFIHRDIKPDNLLLDAKGHVKLSDFGLCTGLKKA 155

                ..
gi 23500787 319 QR 320
Cdd:cd05627 156 HR 157
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
7-445 0e+00

2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the first hydroxylation step in the ubiquinone biosynthetic pathway in bacteria. It is believed that the reaction is 2-polyprenylphenol -> 6-hydroxy-2-polyprenylphenol. This model finds hits primarily in the proteobacteria. The gene is also known as AarF in certain species [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone].


Pssm-ID: 233667 [Multi-domain]  Cd Length: 437  Bit Score: 586.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787     7 VFRLMRAGWILTREGVISALPVEGLSGLPALGHRIAGFLARPRARQMERSERMSRAMNKLGPSYVKLGQFLATRPDIVGH 86
Cdd:TIGR01982   1 LRRLRRIIRVLIRYGFLALVESPIGPLSLRLLRRLLLPFSNRENRLMSRGERLRLALEELGPTFIKFGQTLSTRADLLPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787    87 DVAADLELLQDRLDFFPQAGAVAAIEGSLGRKIDDLYVRFD-APIAAASMAQVHPAEVMKDgapQKVAVKVIRPGVRQRF 165
Cdd:TIGR01982  81 DIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEeKPLAAASIAQVHRARLVDG---KEVAVKVLRPGIEKTI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787   166 ARDLESFFMVARMQERHMPFTRRLRPVQVVETLSQTTRIEMDLRLEAAALSEIAENIKGDEGFRVPKVDWERTGRDVLTL 245
Cdd:TIGR01982 158 AADIALLYRLARIVERLSPDSRRLRPTEVVKEFEKTLRRELDLRREAANASELGENFKNDPGVYVPEVYWDRTSERVLTM 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787   246 EWIDGIKMSDIPALEAAGFDLKKLAETLIQSFLRHTLRDGFFHADMHPGNLFVDHQGLVVAVDFGITGRLDKQQRRFLAE 325
Cdd:TIGR01982 238 EWIDGIPLSDIAALDEAGLDRKALAENLARSFLNQVLRDGFFHADLHPGNIFVLKDGKIIALDFGIVGRLSEEDRRYLAE 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787   326 ILYGFITRDYMRVAEVHFEAGYVPYTHDVASFAQAIRAIGEPIHGQPAETISMAKLLTLLFEVTELFDMETRPELLMLQK 405
Cdd:TIGR01982 318 ILYGFLNRDYRRVAEVHFDAGYVPSDTDMAEFEQAIRAIGEPIFGQPLKEISVGRLLAGLFKITRDFNMELQPQLLLLQK 397
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 23500787   406 TMVVVEGVSRTLDPHFNMWKAAEPVVGDWIRKNLGPQGMV 445
Cdd:TIGR01982 398 TLLTVEGVGRQLDPDLNMWKVAEPFVKRWIRKRLGPKAKI 437
AarF COG0661
Predicted unusual protein kinase [General function prediction only]
1-524 0e+00

Predicted unusual protein kinase [General function prediction only]


Pssm-ID: 223733 [Multi-domain]  Cd Length: 517  Bit Score: 561.93  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787   1 MSNLSAVFRLMRAGWILTREGVISALPVEGLSGLPALGHRIAG--FLARPRARQMERSERMSRAMNKLGPSYVKLGQFLA 78
Cdd:COG0661   1 MLTLYAVSRLPRIIRVRLRYLLGRLLRLTGRLALLLRLLSWLGksKLASSEELREKRAERLRLALEELGPTFIKLGQILS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787  79 TRPDIVGHDVAADLELLQDRLDFFPQAGAVAAIEGSLGRKIDDLYVRFDA-PIAAASMAQVHPAEVmKDGapQKVAVKVI 157
Cdd:COG0661  81 TRPDLVPPEYAEELAKLQDRVPPFPFEEAERIIEEELGRPIEELFSEFEPePIASASIAQVHRAVL-KSG--EEVAVKVQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 158 RPGVRQRFARDLESFFMVARMQERHMPFTRRLRPVQVVETLSQTTRIEMDLRLEAAALSEIAENIKGDEGFRVPKVDWER 237
Cdd:COG0661 158 RPGIRERIEADLKLLRRLARLIKRLPPGGRRLDLVEVVDEFEKRLREELDYRREAANAERFRENFKDDPDVYVPKVYWEY 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 238 TGRDVLTLEWIDGIKMSDIPALEAAGFDLKKLAETLIQSFLRHTLRDGFFHADMHPGNLFVDHQGLVVAVDFGITGRLDK 317
Cdd:COG0661 238 TTRRVLTMEWIDGIKISDIAALKSAGIDRKELAELLVRAFLRQLLRDGFFHADPHPGNILVRSDGRIVLLDFGIVGRLDP 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 318 QQRRFLAEILYGFITRDYMRVAEVHFEAGYVPYTHDVASFAQAIRAIGEPIHGQPAETISMAKLLTLLFEVTELFDMETR 397
Cdd:COG0661 318 KFRRYLAELLLAFLNRDYDRVAELHVELGYVPPDTDRDPLAAAIRAVLEPIYGKPLEEISFGEILDKLFEVARRFPMRLP 397
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 398 PELLMLQKTMVVVEGVSRTLDPHFNMWKAAEPVVGDWIRKNLGPQgMVLDAKESAYALLHFTRKTPELLQRIDRIsvald 477
Cdd:COG0661 398 PELVLLQRTLLLVEGVGRQLDPRFNLWAVAQPLLAKWLKKQLSPK-LLRELKDEAVAVLNALPLLPRLLRDLLDN----- 471
                       490       500       510       520
                ....*....|....*....|....*....|....*....|....*..
gi 23500787 478 TMAANGLRFDDATAEAIGRAEAQHSrWGRIAQVVIAVSMAAIAIKLY 524
Cdd:COG0661 472 DREELSLRSSEELALLLLKAVARLS-IGSILLVVLAVTVLLIAILLL 517
COG0478 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
225-309 5.31e-07

RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction mechanisms]


Pssm-ID: 223554 [Multi-domain]  Cd Length: 304  Bit Score: 50.01  E-value: 5.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787 225 DEGFRVPK-VDWERtgrDVLTLEWIDGIKMSDIPALEAagfDLKKLAETLIQsFLRHTLRDGFFHADMHPGNLFVDHQGL 303
Cdd:COG0478 168 PEGVKVPKpIAWNR---HAVVMEYIEGVELYRLRLDVE---NPDEILDKILE-EVRKAYRRGIVHGDLSEFNILVTEDGD 240

                ....*.
gi 23500787 304 VVAVDF 309
Cdd:COG0478 241 IVVIDW 246
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
267-347 6.70e-05

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 43.29  E-value: 6.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787    267 KKLAETLIQSFLRHTLR-------DGFFHADMHPGNLFVDHQGLVVAVDFGITGRLDKQQRrflaeiLYGFI-TRDYMrv 338
Cdd:smart00220  92 GRLSEDEARFYLRQILSaleylhsKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEK------LTTFVgTPEYM-- 163
                           90
                   ....*....|
gi 23500787    339 A-EVHFEAGY 347
Cdd:smart00220 164 ApEVLLGKGY 173
Pkinase pfam00069
Protein kinase domain;
234-357 4.40e-04

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 40.69  E-value: 4.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23500787   234 DWERTGRDV-LTLEWIDGIKMSDIpaLEAAGfdlkKLAETLIQSFLRHTLR-------DGFFHADMHPGNLFVDHQGLVV 305
Cdd:pfam00069  65 DAFEDKDHLyLVMEYCEGGDLFDY--LSRGG----PLSEDEAKKIALQILRgleylhsNGIIHRDLKPENILLDENGVVK 138
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 23500787   306 AVDFGITGRLDKQQRRFlaeilYGFI-TRDYMrvA-EVHFEAGYVPYTHDVASF 357
Cdd:pfam00069 139 IADFGLAKKLTKSSSSL-----TTFVgTPEYM--ApEVLLGGNGYGPKVDVWSL 185
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.12
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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