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Conserved domains on  [gi|496332628|ref|WP_009041806|]
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MULTISPECIES: ubiquinone biosynthesis regulatory protein kinase UbiB [Pseudomonas]

Protein Classification

protein kinase family protein( domain architecture ID 229378)

protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to substrates such as serine/threonine and/or tyrosine residues on proteins, or may be a pseudokinase

CATH:  1.10.510.10
PubMed:  16244704
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
5-473 0e+00

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member PRK04750:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 537  Bit Score: 795.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628   5 AVRRLLRIQRVVIRYRLDDLLFALPLPWFLLALRYALPWRwfPRKPLELSRGARLRLALQDLGPIFIKFGQILSTRRDLL 84
Cdd:PRK04750   3 ELFRLYKIIRVFLRYGLDELILSHRLTRPLRLWRRSLFWM--PNRHKDKPRGERLRLALEELGPIFVKFGQMLSTRRDLF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628  85 PEDIADELMLLQDRVPPFDSKKSVALIEEQLGKKISEVFSRFDIEPLASASVAQVHAAQLKS-GEEVVVKVIRPGLKPVI 163
Cdd:PRK04750  81 PPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQVHFARLKDnGREVVVKVLRPDILPVI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 164 AQDLAWLFILARAAEKVSADARLLHPVDVVSDYEKTIYDELDLLREAANASQLKRNFEGSPLLYVPQVYWDWCRPKVLVM 243
Cdd:PRK04750 161 DADLALMYRLARWVERLLPDGRRLKPREVVAEFEKTLHDELDLMREAANASQLRRNFEDSDMLYVPEVYWDYCSETVMVM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 244 ERIYGIQVTDLATLADQRTDMKMLAERGVEIFFTQVFRDSFFHADMHPGNIFVSTVQPWSPQYIAIDCGIVGSLTPEDQD 323
Cdd:PRK04750 241 ERMYGIPVSDVAALRAAGTDMKLLAERGVEVFFTQVFRDGFFHADMHPGNIFVSYDPPENPRYIALDFGIVGSLNKEDKR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 324 YLARNLFAFFKRDYRRVAQLHIDSGWVPAETKLNEFEAAIRTVCEPIFEKPLKDISFGQVLMRLFQTARRFNMEVQPQLV 403
Cdd:PRK04750 321 YLAENFLAFFNRDYRRVAELHVESGWVPPDTRVEELEFAIRAVCEPIFDKPLAEISFGHVLLRLFNTARRFNVEIQPQLV 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 404 LLQKTLLNIEGLGRQLYPELDLWNTAQPFLERWMRERVSPKALLGNLHsqvEQLPHLANMTRDLLERMSQ 473
Cdd:PRK04750 401 LLQKTLLNVEGLGRQLDPQLDLWKTAKPFLERWMKEQVGPRALVRALK---EEAPFWAEKLPELPRLVHD 467
 
Name Accession Description Interval E-value
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
5-473 0e+00

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 795.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628   5 AVRRLLRIQRVVIRYRLDDLLFALPLPWFLLALRYALPWRwfPRKPLELSRGARLRLALQDLGPIFIKFGQILSTRRDLL 84
Cdd:PRK04750   3 ELFRLYKIIRVFLRYGLDELILSHRLTRPLRLWRRSLFWM--PNRHKDKPRGERLRLALEELGPIFVKFGQMLSTRRDLF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628  85 PEDIADELMLLQDRVPPFDSKKSVALIEEQLGKKISEVFSRFDIEPLASASVAQVHAAQLKS-GEEVVVKVIRPGLKPVI 163
Cdd:PRK04750  81 PPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQVHFARLKDnGREVVVKVLRPDILPVI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 164 AQDLAWLFILARAAEKVSADARLLHPVDVVSDYEKTIYDELDLLREAANASQLKRNFEGSPLLYVPQVYWDWCRPKVLVM 243
Cdd:PRK04750 161 DADLALMYRLARWVERLLPDGRRLKPREVVAEFEKTLHDELDLMREAANASQLRRNFEDSDMLYVPEVYWDYCSETVMVM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 244 ERIYGIQVTDLATLADQRTDMKMLAERGVEIFFTQVFRDSFFHADMHPGNIFVSTVQPWSPQYIAIDCGIVGSLTPEDQD 323
Cdd:PRK04750 241 ERMYGIPVSDVAALRAAGTDMKLLAERGVEVFFTQVFRDGFFHADMHPGNIFVSYDPPENPRYIALDFGIVGSLNKEDKR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 324 YLARNLFAFFKRDYRRVAQLHIDSGWVPAETKLNEFEAAIRTVCEPIFEKPLKDISFGQVLMRLFQTARRFNMEVQPQLV 403
Cdd:PRK04750 321 YLAENFLAFFNRDYRRVAELHVESGWVPPDTRVEELEFAIRAVCEPIFDKPLAEISFGHVLLRLFNTARRFNVEIQPQLV 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 404 LLQKTLLNIEGLGRQLYPELDLWNTAQPFLERWMRERVSPKALLGNLHsqvEQLPHLANMTRDLLERMSQ 473
Cdd:PRK04750 401 LLQKTLLNVEGLGRQLDPQLDLWKTAKPFLERWMKEQVGPRALVRALK---EEAPFWAEKLPELPRLVHD 467
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
2-473 0e+00

Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport and metabolism, Signal transduction mechanisms]; Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440425 [Multi-domain]  Cd Length: 487  Bit Score: 613.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628   2 KLLAVRRLLRIQRVVIRYRLDDLLFALPLPWFLLALRyalpwRWFPRKPLELSRGARLRLALQDLGPIFIKFGQILSTRR 81
Cdd:COG0661    3 ALRRLRRLARIARVLLRYGLGELLDRLGLPRLRRLLT-----GEERREELRRRRAERLRLALEELGPTFIKLGQLLSTRP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628  82 DLLPEDIADELMLLQDRVPPFDSKKSVALIEEQLGKKISEVFSRFDIEPLASASVAQVHAAQLKSGEEVVVKVIRPGLKP 161
Cdd:COG0661   78 DLLPPEYAEELAKLQDRVPPFPFEEVRAVIEEELGRPLEELFAEFDPEPLAAASIGQVHRARLKDGREVAVKVQRPGIEE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 162 VIAQDLAWLFILARAAEKVSADARLLHPVDVVSDYEKTIYDELDLLREAANASQLKRNFEGSPLLYVPQVYWDWCRPKVL 241
Cdd:COG0661  158 AIEADLRILRRLARLLERLSPEGRRLDPVEVVDEFARSLLEELDYRREAANAERFRRNFADDPDVYVPKVYWELSTRRVL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 242 VMERIYGIQVTDLATLADQRTDMKMLAERGVEIFFTQVFRDSFFHADMHPGNIFVSTvqpwSPQYIAIDCGIVGSLTPED 321
Cdd:COG0661  238 TMEWIDGIKISDLEALDAAGIDRKRLAERLVRAFLRQVFRDGFFHADPHPGNIFVLP----DGRLVLLDFGMVGRLDPET 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 322 QDYLARNLFAFFKRDYRRVAQLHIDSGWVPAETKLNEFEAAIRTVCEPIFEKPLKDISFGQVLMRLFQTARRFNMEVQPQ 401
Cdd:COG0661  314 REGLAELLLALLNRDYDRVAEALLELGFVPPDTDVDELERALRAVLEPYFGKPLKDISFGELLLELFELARRFPLRLPPE 393
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496332628 402 LVLLQKTLLNIEGLGRQLYPELDLWNTAQPFLERWMRERVSPKALLGNLhsqVEQLPHLANMTRDLLERMSQ 473
Cdd:COG0661  394 LVLLQRTLLTLEGVGRQLDPDFDLWEVAKPFLERLLRERLGPRALLKRL---KREAPELAELLPRLPRLLER 462
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
6-447 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: 273909  Cd Length: 437  Bit Score: 600.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628    6 VRRLLRIQRVVIRYRLDDLLFALPLPWFLLALRYALPWRWFPRKPLElSRGARLRLALQDLGPIFIKFGQILSTRRDLLP 85
Cdd:TIGR01982   1 LRRLRRIIRVLIRYGFLALVESPIGPLSLRLLRRLLLPFSNRENRLM-SRGERLRLALEELGPTFIKFGQTLSTRADLLP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628   86 EDIADELMLLQDRVPPFDSKKSVALIEEQLGKKISEVFSRFDIEPLASASVAQVHAAQLKSGEEVVVKVIRPGLKPVIAQ 165
Cdd:TIGR01982  80 ADIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEEKPLAAASIAQVHRARLVDGKEVAVKVLRPGIEKTIAA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628  166 DLAWLFILARAAEKVSADARLLHPVDVVSDYEKTIYDELDLLREAANASQLKRNFEGSPLLYVPQVYWDWCRPKVLVMER 245
Cdd:TIGR01982 160 DIALLYRLARIVERLSPDSRRLRPTEVVKEFEKTLRRELDLRREAANASELGENFKNDPGVYVPEVYWDRTSERVLTMEW 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628  246 IYGIQVTDLATLADQRTDMKMLAERGVEIFFTQVFRDSFFHADMHPGNIFVSTvqpwSPQYIAIDCGIVGSLTPEDQDYL 325
Cdd:TIGR01982 240 IDGIPLSDIAALDEAGLDRKALAENLARSFLNQVLRDGFFHADLHPGNIFVLK----DGKIIALDFGIVGRLSEEDRRYL 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628  326 ARNLFAFFKRDYRRVAQLHIDSGWVPAETKLNEFEAAIRTVCEPIFEKPLKDISFGQVLMRLFQTARRFNMEVQPQLVLL 405
Cdd:TIGR01982 316 AEILYGFLNRDYRRVAEVHFDAGYVPSDTDMAEFEQAIRAIGEPIFGQPLKEISVGRLLAGLFKITRDFNMELQPQLLLL 395
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 496332628  406 QKTLLNIEGLGRQLYPELDLWNTAQPFLERWMRERVSPKALL 447
Cdd:TIGR01982 396 QKTLLTVEGVGRQLDPDLNMWKVAEPFVKRWIRKRLGPKAKI 437
UbiB cd13972
Ubiquinone biosynthetic protein UbiB; UbiB is the prokaryotic homolog of yeast Abc1p and human ...
95-344 2.22e-130

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 [Multi-domain]  Cd Length: 247  Bit Score: 379.62  E-value: 2.22e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628  95 LQDRVPPFDSKKSVALIEEQLGKKISEVFSRFDIEPLASASVAQVHAAQLKSGEEVVVKVIRPGLKPVIAQDLAWLFILA 174
Cdd:cd13972    2 LQDRVPPFSGKEARAIIEAELGKPLDALFSDFDEEPVAAASIAQVHKARLLDGREVAVKVLRPGIEKRIERDLELLRFLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 175 RAAEKVSADARLLHPVDVVSDYEKTIYDELDLLREAANASQLKRNFEGSPLLYVPQVYWDWCRPKVLVMERIYGIQVTDL 254
Cdd:cd13972   82 RLAERLLPEARRLRPVEVVKEFARSLLLELDLRLEAANASELRENFLDDPGFYVPEVYWELTSKNVLTMEWIDGIPISDI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 255 ATLADQRTDMKMLAERGVEIFFTQVFRDSFFHADMHPGNIFVSTvqpwSPQYIAIDCGIVGSLTPEDQDYLARNLFAFFK 334
Cdd:cd13972  162 EALDAAGIDRKALAERLVEIFFRQVFRDGFFHADMHPGNIFVDP----NGRIIAVDFGIMGRLDKKDRRYLAEILYGFLT 237
                        250
                 ....*....|
gi 496332628 335 RDYRRVAQLH 344
Cdd:cd13972  238 RDYRRVAELH 247
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
95-344 2.82e-98

ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. 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 E. 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: 427143 [Multi-domain]  Cd Length: 245  Bit Score: 297.61  E-value: 2.82e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628   95 LQDRVPPFDSKKSVALIEEQLGKKISEVFSRFDIEPLASASVAQVHAAQLKSGEEVVVKVIRPGLKPVIAQDLAWLFILA 174
Cdd:pfam03109   2 LQDRAPPFPFEQAKKVIEEELGAPVEEIFAEFDEEPIAAASIAQVHRARLKDGEEVAVKVQRPGVKKRIRSDLLLLRFLA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628  175 RAAEKVSADARLLhpVDVVSDYEKTIYDELDLLREAANASQLKRNFEGSPLLYVPQVYWDWCRPKVLVMERIYGIQVTDL 254
Cdd:pfam03109  82 KVAKRFFPGFRRL--DWLVDEFRKSLPQELDFLREAANAEKFRENFADDPDVYVPKVYWELTTERVLTMEYVDGIKIDDL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628  255 ATLADQRTDMKMLAERGVEIFFTQVFRDSFFHADMHPGNIFVSTvqpwSPQYIAIDCGIVGSLTPEDQDYLARNLFAFFK 334
Cdd:pfam03109 160 DALSEAGIDRKEIARRLVELFLEQIFRDGFFHADPHPGNILVRK----DGRIVLLDFGLMGRLDEKFRRLYAELLLALVN 235
                         250
                  ....*....|
gi 496332628  335 RDYRRVAQLH 344
Cdd:pfam03109 236 RDYKRVAEML 245
 
Name Accession Description Interval E-value
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
5-473 0e+00

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 795.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628   5 AVRRLLRIQRVVIRYRLDDLLFALPLPWFLLALRYALPWRwfPRKPLELSRGARLRLALQDLGPIFIKFGQILSTRRDLL 84
Cdd:PRK04750   3 ELFRLYKIIRVFLRYGLDELILSHRLTRPLRLWRRSLFWM--PNRHKDKPRGERLRLALEELGPIFVKFGQMLSTRRDLF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628  85 PEDIADELMLLQDRVPPFDSKKSVALIEEQLGKKISEVFSRFDIEPLASASVAQVHAAQLKS-GEEVVVKVIRPGLKPVI 163
Cdd:PRK04750  81 PPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQVHFARLKDnGREVVVKVLRPDILPVI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 164 AQDLAWLFILARAAEKVSADARLLHPVDVVSDYEKTIYDELDLLREAANASQLKRNFEGSPLLYVPQVYWDWCRPKVLVM 243
Cdd:PRK04750 161 DADLALMYRLARWVERLLPDGRRLKPREVVAEFEKTLHDELDLMREAANASQLRRNFEDSDMLYVPEVYWDYCSETVMVM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 244 ERIYGIQVTDLATLADQRTDMKMLAERGVEIFFTQVFRDSFFHADMHPGNIFVSTVQPWSPQYIAIDCGIVGSLTPEDQD 323
Cdd:PRK04750 241 ERMYGIPVSDVAALRAAGTDMKLLAERGVEVFFTQVFRDGFFHADMHPGNIFVSYDPPENPRYIALDFGIVGSLNKEDKR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 324 YLARNLFAFFKRDYRRVAQLHIDSGWVPAETKLNEFEAAIRTVCEPIFEKPLKDISFGQVLMRLFQTARRFNMEVQPQLV 403
Cdd:PRK04750 321 YLAENFLAFFNRDYRRVAELHVESGWVPPDTRVEELEFAIRAVCEPIFDKPLAEISFGHVLLRLFNTARRFNVEIQPQLV 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 404 LLQKTLLNIEGLGRQLYPELDLWNTAQPFLERWMRERVSPKALLGNLHsqvEQLPHLANMTRDLLERMSQ 473
Cdd:PRK04750 401 LLQKTLLNVEGLGRQLDPQLDLWKTAKPFLERWMKEQVGPRALVRALK---EEAPFWAEKLPELPRLVHD 467
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
2-473 0e+00

Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport and metabolism, Signal transduction mechanisms]; Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440425 [Multi-domain]  Cd Length: 487  Bit Score: 613.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628   2 KLLAVRRLLRIQRVVIRYRLDDLLFALPLPWFLLALRyalpwRWFPRKPLELSRGARLRLALQDLGPIFIKFGQILSTRR 81
Cdd:COG0661    3 ALRRLRRLARIARVLLRYGLGELLDRLGLPRLRRLLT-----GEERREELRRRRAERLRLALEELGPTFIKLGQLLSTRP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628  82 DLLPEDIADELMLLQDRVPPFDSKKSVALIEEQLGKKISEVFSRFDIEPLASASVAQVHAAQLKSGEEVVVKVIRPGLKP 161
Cdd:COG0661   78 DLLPPEYAEELAKLQDRVPPFPFEEVRAVIEEELGRPLEELFAEFDPEPLAAASIGQVHRARLKDGREVAVKVQRPGIEE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 162 VIAQDLAWLFILARAAEKVSADARLLHPVDVVSDYEKTIYDELDLLREAANASQLKRNFEGSPLLYVPQVYWDWCRPKVL 241
Cdd:COG0661  158 AIEADLRILRRLARLLERLSPEGRRLDPVEVVDEFARSLLEELDYRREAANAERFRRNFADDPDVYVPKVYWELSTRRVL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 242 VMERIYGIQVTDLATLADQRTDMKMLAERGVEIFFTQVFRDSFFHADMHPGNIFVSTvqpwSPQYIAIDCGIVGSLTPED 321
Cdd:COG0661  238 TMEWIDGIKISDLEALDAAGIDRKRLAERLVRAFLRQVFRDGFFHADPHPGNIFVLP----DGRLVLLDFGMVGRLDPET 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 322 QDYLARNLFAFFKRDYRRVAQLHIDSGWVPAETKLNEFEAAIRTVCEPIFEKPLKDISFGQVLMRLFQTARRFNMEVQPQ 401
Cdd:COG0661  314 REGLAELLLALLNRDYDRVAEALLELGFVPPDTDVDELERALRAVLEPYFGKPLKDISFGELLLELFELARRFPLRLPPE 393
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496332628 402 LVLLQKTLLNIEGLGRQLYPELDLWNTAQPFLERWMRERVSPKALLGNLhsqVEQLPHLANMTRDLLERMSQ 473
Cdd:COG0661  394 LVLLQRTLLTLEGVGRQLDPDFDLWEVAKPFLERLLRERLGPRALLKRL---KREAPELAELLPRLPRLLER 462
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
6-447 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: 273909  Cd Length: 437  Bit Score: 600.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628    6 VRRLLRIQRVVIRYRLDDLLFALPLPWFLLALRYALPWRWFPRKPLElSRGARLRLALQDLGPIFIKFGQILSTRRDLLP 85
Cdd:TIGR01982   1 LRRLRRIIRVLIRYGFLALVESPIGPLSLRLLRRLLLPFSNRENRLM-SRGERLRLALEELGPTFIKFGQTLSTRADLLP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628   86 EDIADELMLLQDRVPPFDSKKSVALIEEQLGKKISEVFSRFDIEPLASASVAQVHAAQLKSGEEVVVKVIRPGLKPVIAQ 165
Cdd:TIGR01982  80 ADIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEEKPLAAASIAQVHRARLVDGKEVAVKVLRPGIEKTIAA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628  166 DLAWLFILARAAEKVSADARLLHPVDVVSDYEKTIYDELDLLREAANASQLKRNFEGSPLLYVPQVYWDWCRPKVLVMER 245
Cdd:TIGR01982 160 DIALLYRLARIVERLSPDSRRLRPTEVVKEFEKTLRRELDLRREAANASELGENFKNDPGVYVPEVYWDRTSERVLTMEW 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628  246 IYGIQVTDLATLADQRTDMKMLAERGVEIFFTQVFRDSFFHADMHPGNIFVSTvqpwSPQYIAIDCGIVGSLTPEDQDYL 325
Cdd:TIGR01982 240 IDGIPLSDIAALDEAGLDRKALAENLARSFLNQVLRDGFFHADLHPGNIFVLK----DGKIIALDFGIVGRLSEEDRRYL 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628  326 ARNLFAFFKRDYRRVAQLHIDSGWVPAETKLNEFEAAIRTVCEPIFEKPLKDISFGQVLMRLFQTARRFNMEVQPQLVLL 405
Cdd:TIGR01982 316 AEILYGFLNRDYRRVAEVHFDAGYVPSDTDMAEFEQAIRAIGEPIFGQPLKEISVGRLLAGLFKITRDFNMELQPQLLLL 395
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 496332628  406 QKTLLNIEGLGRQLYPELDLWNTAQPFLERWMRERVSPKALL 447
Cdd:TIGR01982 396 QKTLLTVEGVGRQLDPDLNMWKVAEPFVKRWIRKRLGPKAKI 437
UbiB cd13972
Ubiquinone biosynthetic protein UbiB; UbiB is the prokaryotic homolog of yeast Abc1p and human ...
95-344 2.22e-130

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 [Multi-domain]  Cd Length: 247  Bit Score: 379.62  E-value: 2.22e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628  95 LQDRVPPFDSKKSVALIEEQLGKKISEVFSRFDIEPLASASVAQVHAAQLKSGEEVVVKVIRPGLKPVIAQDLAWLFILA 174
Cdd:cd13972    2 LQDRVPPFSGKEARAIIEAELGKPLDALFSDFDEEPVAAASIAQVHKARLLDGREVAVKVLRPGIEKRIERDLELLRFLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 175 RAAEKVSADARLLHPVDVVSDYEKTIYDELDLLREAANASQLKRNFEGSPLLYVPQVYWDWCRPKVLVMERIYGIQVTDL 254
Cdd:cd13972   82 RLAERLLPEARRLRPVEVVKEFARSLLLELDLRLEAANASELRENFLDDPGFYVPEVYWELTSKNVLTMEWIDGIPISDI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 255 ATLADQRTDMKMLAERGVEIFFTQVFRDSFFHADMHPGNIFVSTvqpwSPQYIAIDCGIVGSLTPEDQDYLARNLFAFFK 334
Cdd:cd13972  162 EALDAAGIDRKALAERLVEIFFRQVFRDGFFHADMHPGNIFVDP----NGRIIAVDFGIMGRLDKKDRRYLAEILYGFLT 237
                        250
                 ....*....|
gi 496332628 335 RDYRRVAQLH 344
Cdd:cd13972  238 RDYRRVAELH 247
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
95-343 1.51e-98

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: 298.25  E-value: 1.51e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628  95 LQDRVPPFDSKKSVALIEEQLGKKISEVFSRFDIEPLASASVAQVHAAQLKSGEEVVVKVIRPGLKPVIAQDLAWLFILA 174
Cdd:cd05121    2 LQDDVPPFPFEEVRKIIEEELGRPLEEVFAEFDPEPLAAASIAQVHRARLKDGREVAVKVQRPGIEEIIEADLRILRRLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 175 RAAEKVSADARLLHPVDVVSDYEKTIYDELDLLREAANASQLKRNFEGSPLLYVPQVYWDWCRPKVLVMERIYGIQVTDL 254
Cdd:cd05121   82 RLLERLSPLLRRLDLVAIVDEFARSLLEELDFRREARNAERFRKNLKDSPDVYVPKVYPELSTRRVLVMEYIDGVKLTDL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 255 ATLADQRTDMKMLAERGVEIFFTQVFRDSFFHADMHPGNIFVSTvqpwSPQYIAIDCGIVGSLTPEDQDYLARNLFAFFK 334
Cdd:cd05121  162 EALRAAGIDRKELARRLVDAYLKQIFEDGFFHADPHPGNILVLP----DGRIALLDFGMVGRLDPETREALADLLLALVN 237

                 ....*....
gi 496332628 335 RDYRRVAQL 343
Cdd:cd05121  238 GDAEGLAEA 246
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
95-344 2.82e-98

ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. 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 E. 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: 427143 [Multi-domain]  Cd Length: 245  Bit Score: 297.61  E-value: 2.82e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628   95 LQDRVPPFDSKKSVALIEEQLGKKISEVFSRFDIEPLASASVAQVHAAQLKSGEEVVVKVIRPGLKPVIAQDLAWLFILA 174
Cdd:pfam03109   2 LQDRAPPFPFEQAKKVIEEELGAPVEEIFAEFDEEPIAAASIAQVHRARLKDGEEVAVKVQRPGVKKRIRSDLLLLRFLA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628  175 RAAEKVSADARLLhpVDVVSDYEKTIYDELDLLREAANASQLKRNFEGSPLLYVPQVYWDWCRPKVLVMERIYGIQVTDL 254
Cdd:pfam03109  82 KVAKRFFPGFRRL--DWLVDEFRKSLPQELDFLREAANAEKFRENFADDPDVYVPKVYWELTTERVLTMEYVDGIKIDDL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628  255 ATLADQRTDMKMLAERGVEIFFTQVFRDSFFHADMHPGNIFVSTvqpwSPQYIAIDCGIVGSLTPEDQDYLARNLFAFFK 334
Cdd:pfam03109 160 DALSEAGIDRKEIARRLVELFLEQIFRDGFFHADPHPGNILVRK----DGRIVLLDFGLMGRLDEKFRRLYAELLLALVN 235
                         250
                  ....*....|
gi 496332628  335 RDYRRVAQLH 344
Cdd:pfam03109 236 RDYKRVAEML 245
ADCK1-like cd13969
aarF domain containing kinase 1 and similar proteins; This subfamily is composed of ...
95-342 1.50e-59

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 [Multi-domain]  Cd Length: 253  Bit Score: 197.32  E-value: 1.50e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628  95 LQDRVPPFDSKKSVALIEEQLGKKISEVFSRFDIEPLASASVAQVHAAQLKSGEEVVVKVIRPGLKPVIAQDLAWLFILA 174
Cdd:cd13969    2 LQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVHKAKLKDGEEVAVKVQHPDLRKQFAGDLATMEFLV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 175 RAAEKVSADARLLhpvDVVSDYEKTIYDELDLLREAANASQLKRNFEGSPLLYVPQVYWDWCRPKVLVMERIYGIQVTDL 254
Cdd:cd13969   82 NLVEKLFPDFPFS---WLVDELKKNLPKELDFLNEARNAERCAKLFKHRPDVYVPKVYWDLSSKRVLTMEFIDGIKIDDV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 255 ATLADQRTDMKMLAERGVEIFFTQVFRDSFFHADMHPGNIFVSTVQ-PWSPQYIAIDCGIVGSLTPEDQDYLARNLFAFF 333
Cdd:cd13969  159 EALKKLGIDPKEVARLLSEAFAEMIFVHGFVHCDPHPGNLLVRKNPgPGKPQIVLLDHGLYRELDEEFRLNYCRLWKALI 238

                 ....*....
gi 496332628 334 KRDYRRVAQ 342
Cdd:cd13969  239 LGDEKKIKK 247
ADCK2-like cd13971
aarF domain containing kinase 2 and similar proteins; This subfamily is composed of ...
95-346 5.25e-52

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: 178.96  E-value: 5.25e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628  95 LQDRVPPFDSKKSVALIEEQLGKKISEVFSRFDIEPLASASVAQVHAAQLKS--------GEEVVVKVIRPGLKPVIAQD 166
Cdd:cd13971    2 LHSNAPPHSWAHTERALEAAFGKDWEDIFEEFDEEPIGSGSIAQVHRAKLKPdyggdgggPRVVAVKVLHPGVREQIERD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 167 LAWLFILARAAEKVSAdARLLHPVDVVSDYEKTIYDELDLLREAANASQLKRNFEGSPLLYVPQVYWDWCRPKVLVMERI 246
Cdd:cd13971   82 LAILRLFAKLLEAIPP-LRWLSLPESVEQFASLMLRQLDLRVEAANLERFRENFKDRKDVSFPKPLYPLVTEEVLVETFE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 247 YGIQVTDLATLADQRTDMKMLAERGVEIFFTQVFRDSFFHADMHPGNIFVSTVQPWS-------------PQYIAIDCGI 313
Cdd:cd13971  161 EGVPISRTVLAHGGEPLKRKLARIGLDAFLKMLFVDNFVHGDLHPGNILVRFNDSNRpsllvsldargspPRLVFLDAGL 240
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 496332628 314 VGSLTPEDQdylaRNLFAFFK----RDYRRVAQLHID 346
Cdd:cd13971  241 VTELSPQDR----RNFIDLFKavarGDGYKAAELMLE 273
ABC1_ADCK3 cd13970
Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This ...
90-343 8.79e-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 [Multi-domain]  Cd Length: 251  Bit Score: 150.35  E-value: 8.79e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628  90 DELMLLQDRVPPFDSKKSVALIEEQLGKKISEVFSRFDIEPLASASVAQVHAAQLKSGEEVVVKVIRPGLKPVIAQDLAW 169
Cdd:cd13970    1 EALARLRDSAPPMPWAQLEKVLEAELGEDWRELFAEFDEEPFAAASIGQVHRATLKDGREVAVKVQYPGVAESIDSDLNN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 170 LFILARAAEKVSADARLLHPVDVVsdyEKTIYDELDLLREAANASQLKRNFEGSPLLYVPQVYWDWCRPKVLVMERIYGI 249
Cdd:cd13970   81 LRRLLKLTGLLPKGLDLDALIAEL---REELLEECDYEREAANQRRFRELLADDPRFVVPEVIPELSTKRVLTTEFVDGV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 250 QVTDLATLADQRTDmkMLAERGVEIFFTQVFRDSFFHADMHPGNIFVStvqPWSPQYIAIDCGIVGSLTPEDQDYLARNL 329
Cdd:cd13970  158 PLDEAADLSQEERN--RIGELLLRLCLRELFEFGFMQTDPNPGNFLYD---PEDGRLGLLDFGAVREYPPEFVDGYRRLV 232
                        250
                 ....*....|....
gi 496332628 330 FAFFKRDYRRVAQL 343
Cdd:cd13970  233 RAALEGDREALLEA 246
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
226-343 2.84e-04

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


Pssm-ID: 440246 [Multi-domain]  Cd Length: 183  Bit Score: 41.81  E-value: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 226 LYVPQVYwDWCRpKVLVMERIYGIQVTDLATLADQRTDMKMLAErgVEIFFtqvfRDSFFHADMHPGNIFVSTV-QPWS- 303
Cdd:COG0478   61 LPVPRPI-AANR-HAIVMERIEGVELARLKLEDPEEVLDKILEE--IRRAH----DAGIVHADLSEYNILVDDDgGVWIi 132
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 496332628 304 --PQYIAIDcgivgslTPEDQDYLAR---NLFAFFKRDYRRVAQL 343
Cdd:COG0478  133 dwPQAVPRD-------HPNAEELLERdleNLLRSFRKKYGLEVDL 170
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
195-335 4.87e-04

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 [Multi-domain]  Cd Length: 183  Bit Score: 41.34  E-value: 4.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 195 DY--EKTIYDELDLLREAAnasqlKRNFEGSPLLY-----VPQVYwDWCRpKVLVMERIYGIQVTDLATLADQRT----- 262
Cdd:cd05144   47 DYlkHRKHASWLYLSRLAA-----EKEFAALKALYeegfpVPKPI-DWNR-HAVVMELIDGYPLYQVRLLEDPEEvldei 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332628 263 --DMKMLAERGVeifftqvfrdsfFHADMHPGNIFVS-----TVQPWsPQYIAIDCgivgsltPEDQDYLAR---NLFAF 332
Cdd:cd05144  120 leLIVKLAKHGL------------IHGDFSEFNILVDedekiTVIDF-PQMVSTSH-------PNAEEYFDRdveCIIKF 179

                 ...
gi 496332628 333 FKR 335
Cdd:cd05144  180 FRR 182
 
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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