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Conserved domains on  [gi|110636414|ref|YP_676622|]
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2-octaprenylphenol hydroxylase [Chelativorans sp. BNC1]

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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 1.21e-122

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: 362.67  E-value: 1.21e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414  95 LQDRMDTFPQERAVMAIEASLGAPVGTLYREF-GAPVAAASIAQVHPAKIiREGeiQKVAVKVIRPGVRRRFYNDLESFF 173
Cdd:cd13972    2 LQDRVPPFSGKEARAIIEAELGKPLDALFSDFdEEPVAAASIAQVHKARL-LDG--REVAVKVLRPGIEKRIERDLELLR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 174 LAARLQERFIASSRRLRPVEVTQTLAQTTKIEMDLRLEAAAISEIHENSKEDPGFRVPWVDWQRTGRDVLTLEWIDGIKM 253
Cdd:cd13972   79 FLARLAERLLPEARRLRPVEVVKEFARSLLLELDLRLEAANASELRENFLDDPGFYVPEVYWELTSKNVLTMEWIDGIPI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 254 SDTEALRAAGHDLERLATTLIQSFLRHTLRDGFFHADMHPGNLFVEANGTIVAVDFGIVGRIGRKERRFLAEILYGFITR 333
Cdd:cd13972  159 SDIEALDAAGIDRKALAERLVEIFFRQVFRDGFFHADMHPGNIFVDPNGRIIAVDFGIMGRLDKKDRRYLAEILYGFLTR 238

                 ....*....
gi 110636414 334 DFRRVAEVH 342
Cdd:cd13972  239 DYRRVAELH 247
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
7-444 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: 569.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414    7 YLRLARAGWILLREGVIAAFPGDQFEGMPRFGWRLARLLSRRRSSHRARTERLAIAVDRLGPSYVKLGQFLATRPDVVGH 86
Cdd:TIGR01982   1 LRRLRRIIRVLIRYGFLALVESPIGPLSLRLLRRLLLPFSNRENRLMSRGERLRLALEELGPTFIKFGQTLSTRADLLPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414   87 ELARDLASLQDRMDTFPQERAVMAIEASLGAPVGTLYREFG-APVAAASIAQVHPAKIIrEGEiqKVAVKVIRPGVRRRF 165
Cdd:TIGR01982  81 DIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEeKPLAAASIAQVHRARLV-DGK--EVAVKVLRPGIEKTI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414  166 YNDLESFFLAARLQERFIASSRRLRPVEVTQTLAQTTKIEMDLRLEAAAISEIHENSKEDPGFRVPWVDWQRTGRDVLTL 245
Cdd:TIGR01982 158 AADIALLYRLARIVERLSPDSRRLRPTEVVKEFEKTLRRELDLRREAANASELGENFKNDPGVYVPEVYWDRTSERVLTM 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414  246 EWIDGIKMSDTEALRAAGHDLERLATTLIQSFLRHTLRDGFFHADMHPGNLFVEANGTIVAVDFGIVGRIGRKERRFLAE 325
Cdd:TIGR01982 238 EWIDGIPLSDIAALDEAGLDRKALAENLARSFLNQVLRDGFFHADLHPGNIFVLKDGKIIALDFGIVGRLSEEDRRYLAE 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414  326 ILYGFITRDFRRVAEVHFEAGYVPSHHDVAAFAQALRAIGEPIHGQPAETISMARLLTLLFEVTELFDMQTRPELLLLQK 405
Cdd:TIGR01982 318 ILYGFLNRDYRRVAEVHFDAGYVPSDTDMAEFEQAIRAIGEPIFGQPLKEISVGRLLAGLFKITRDFNMELQPQLLLLQK 397
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 110636414  406 TMVVVEGVSRTLDPHFNMWRAAEPVVSEWIEKNLGPQGL 444
Cdd:TIGR01982 398 TLLTVEGVGRQLDPDLNMWKVAEPFVKRWIRKRLGPKAK 436
 
Name Accession Description Interval E-value
UbiB cd13972
Ubiquinone biosynthetic protein UbiB; UbiB is the prokaryotic homolog of yeast Abc1p and human ...
95-342 1.21e-122

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: 362.67  E-value: 1.21e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414  95 LQDRMDTFPQERAVMAIEASLGAPVGTLYREF-GAPVAAASIAQVHPAKIiREGeiQKVAVKVIRPGVRRRFYNDLESFF 173
Cdd:cd13972    2 LQDRVPPFSGKEARAIIEAELGKPLDALFSDFdEEPVAAASIAQVHKARL-LDG--REVAVKVLRPGIEKRIERDLELLR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 174 LAARLQERFIASSRRLRPVEVTQTLAQTTKIEMDLRLEAAAISEIHENSKEDPGFRVPWVDWQRTGRDVLTLEWIDGIKM 253
Cdd:cd13972   79 FLARLAERLLPEARRLRPVEVVKEFARSLLLELDLRLEAANASELRENFLDDPGFYVPEVYWELTSKNVLTMEWIDGIPI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 254 SDTEALRAAGHDLERLATTLIQSFLRHTLRDGFFHADMHPGNLFVEANGTIVAVDFGIVGRIGRKERRFLAEILYGFITR 333
Cdd:cd13972  159 SDIEALDAAGIDRKALAERLVEIFFRQVFRDGFFHADMHPGNIFVDPNGRIIAVDFGIMGRLDKKDRRYLAEILYGFLTR 238

                 ....*....
gi 110636414 334 DFRRVAEVH 342
Cdd:cd13972  239 DYRRVAELH 247
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
4-466 1.08e-116

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310  Cd Length: 537  Bit Score: 357.68  E-value: 1.08e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414   4 LGAYLRLARAGWILLREGVIAAFPGDQFEGMPRFgWRLARLLSRRRSSHRARTERLAIAVDRLGPSYVKLGQFLATRPDV 83
Cdd:PRK04750   1 PMELFRLYKIIRVFLRYGLDELILSHRLTRPLRL-WRRSLFWMPNRHKDKPRGERLRLALEELGPIFVKFGQMLSTRRDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414  84 VGHELARDLASLQDRMDTFPQERAVMAIEASLGAPVGTLYREFGA-PVAAASIAQVHPAKIIREGeiQKVAVKVIRPGVR 162
Cdd:PRK04750  80 FPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIkPLASASIAQVHFARLKDNG--REVVVKVLRPDIL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 163 RRFYNDLESFFLAARLQERFIASSRRLRPVEVTQTLAQTTKIEMDLRLEAAAISEIHENSKEDPGFRVPWVDWQRTGRDV 242
Cdd:PRK04750 158 PVIDADLALMYRLARWVERLLPDGRRLKPREVVAEFEKTLHDELDLMREAANASQLRRNFEDSDMLYVPEVYWDYCSETV 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 243 LTLEWIDGIKMSDTEALRAAGHDLERLATTLIQSFLRHTLRDGFFHADMHPGNLFV----EANGTIVAVDFGIVGRIGRK 318
Cdd:PRK04750 238 MVMERMYGIPVSDVAALRAAGTDMKLLAERGVEVFFTQVFRDGFFHADMHPGNIFVsydpPENPRYIALDFGIVGSLNKE 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 319 ERRFLAEILYGFITRDFRRVAEVHFEAGYVPSHHDVAAFAQALRAIGEPIHGQPAETISMARLLTLLFEVTELFDMQTRP 398
Cdd:PRK04750 318 DKRYLAENFLAFFNRDYRRVAELHVESGWVPPDTRVEELEFAIRAVCEPIFDKPLAEISFGHVLLRLFNTARRFNVEIQP 397
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110636414 399 ELLLLQKTMVVVEGVSRTLDPHFNMWRAAEPVVSEWIEKNLGPQGLFMDAREGAHALMMLVRQAPELA 466
Cdd:PRK04750 398 QLVLLQKTLLNVEGLGRQLDPQLDLWKTAKPFLERWMKEQVGPRALVRALKEEAPFWAEKLPELPRLV 465
ABC1 pfam03109
ABC1 family; This family includes ABC1 from yeast and AarF from Escherichia coli. These ...
113-234 2.57e-26

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: 103.44  E-value: 2.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414  113 ASLGAPVGTLYREFG-APVAAASIAQVHPAKIiREGEiqKVAVKVIRPGVRRRFYNDLESFFLAARLQERFIAssrRLRP 191
Cdd:pfam03109   1 EELGAPVEEVFAEFDeEPIAAASIAQVHRAVL-KDGE--EVAVKVQRPGVKKRIRSDLKLLKFLAKILKKFFP---GFDL 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 110636414  192 VEVTQTLAQTTKIEMDLRLEAAAISEIHENSKEDPGFRVPWVD 234
Cdd:pfam03109  75 DWLVDEFRKSLPQELDFLREAANAEKFRENFADLPWVYVPKVY 117
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
7-444 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: 569.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414    7 YLRLARAGWILLREGVIAAFPGDQFEGMPRFGWRLARLLSRRRSSHRARTERLAIAVDRLGPSYVKLGQFLATRPDVVGH 86
Cdd:TIGR01982   1 LRRLRRIIRVLIRYGFLALVESPIGPLSLRLLRRLLLPFSNRENRLMSRGERLRLALEELGPTFIKFGQTLSTRADLLPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414   87 ELARDLASLQDRMDTFPQERAVMAIEASLGAPVGTLYREFG-APVAAASIAQVHPAKIIrEGEiqKVAVKVIRPGVRRRF 165
Cdd:TIGR01982  81 DIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEeKPLAAASIAQVHRARLV-DGK--EVAVKVLRPGIEKTI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414  166 YNDLESFFLAARLQERFIASSRRLRPVEVTQTLAQTTKIEMDLRLEAAAISEIHENSKEDPGFRVPWVDWQRTGRDVLTL 245
Cdd:TIGR01982 158 AADIALLYRLARIVERLSPDSRRLRPTEVVKEFEKTLRRELDLRREAANASELGENFKNDPGVYVPEVYWDRTSERVLTM 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414  246 EWIDGIKMSDTEALRAAGHDLERLATTLIQSFLRHTLRDGFFHADMHPGNLFVEANGTIVAVDFGIVGRIGRKERRFLAE 325
Cdd:TIGR01982 238 EWIDGIPLSDIAALDEAGLDRKALAENLARSFLNQVLRDGFFHADLHPGNIFVLKDGKIIALDFGIVGRLSEEDRRYLAE 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414  326 ILYGFITRDFRRVAEVHFEAGYVPSHHDVAAFAQALRAIGEPIHGQPAETISMARLLTLLFEVTELFDMQTRPELLLLQK 405
Cdd:TIGR01982 318 ILYGFLNRDYRRVAEVHFDAGYVPSDTDMAEFEQAIRAIGEPIFGQPLKEISVGRLLAGLFKITRDFNMELQPQLLLLQK 397
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 110636414  406 TMVVVEGVSRTLDPHFNMWRAAEPVVSEWIEKNLGPQGL 444
Cdd:TIGR01982 398 TLLTVEGVGRQLDPDLNMWKVAEPFVKRWIRKRLGPKAK 436
AarF COG0661
Predicted unusual protein kinase [General function prediction only]
1-501 3.46e-167

Predicted unusual protein kinase [General function prediction only]


Pssm-ID: 223733 [Multi-domain]  Cd Length: 517  Bit Score: 486.82  E-value: 3.46e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414   1 MSTLGAYLRLARAGWILLREGVIAAFP-GDQFEGMPRF-GWRLARLLSRRRSSHRARTERLAIAVDRLGPSYVKLGQFLA 78
Cdd:COG0661    1 MLTLYAVSRLPRIIRVRLRYLLGRLLRlTGRLALLLRLlSWLGKSKLASSEELREKRAERLRLALEELGPTFIKLGQILS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414  79 TRPDVVGHELARDLASLQDRMDTFPQERAVMAIEASLGAPVGTLYREFGA-PVAAASIAQVHPAKIiREGEiqKVAVKVI 157
Cdd:COG0661   81 TRPDLVPPEYAEELAKLQDRVPPFPFEEAERIIEEELGRPIEELFSEFEPePIASASIAQVHRAVL-KSGE--EVAVKVQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 158 RPGVRRRFYNDLESFFLAARLQERFIASSRRLRPVEVTQTLAQTTKIEMDLRLEAAAISEIHENSKEDPGFRVPWVDWQR 237
Cdd:COG0661  158 RPGIRERIEADLKLLRRLARLIKRLPPGGRRLDLVEVVDEFEKRLREELDYRREAANAERFRENFKDDPDVYVPKVYWEY 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 238 TGRDVLTLEWIDGIKMSDTEALRAAGHDLERLATTLIQSFLRHTLRDGFFHADMHPGNLFVEANGTIVAVDFGIVGRIGR 317
Cdd:COG0661  238 TTRRVLTMEWIDGIKISDIAALKSAGIDRKELAELLVRAFLRQLLRDGFFHADPHPGNILVRSDGRIVLLDFGIVGRLDP 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 318 KERRFLAEILYGFITRDFRRVAEVHFEAGYVPSHHDVAAFAQALRAIGEPIHGQPAETISMARLLTLLFEVTELFDMQTR 397
Cdd:COG0661  318 KFRRYLAELLLAFLNRDYDRVAELHVELGYVPPDTDRDPLAAAIRAVLEPIYGKPLEEISFGEILDKLFEVARRFPMRLP 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 398 PELLLLQKTMVVVEGVSRTLDPHFNMWRAAEPVVSEWIEKNLGPQgLFMDAREGAHALMMLVRQAPELAIRLDHVSRgme 477
Cdd:COG0661  398 PELVLLQRTLLLVEGVGRQLDPRFNLWAVAQPLLAKWLKKQLSPK-LLRELKDEAVAVLNALPLLPRLLRDLLDNDR--- 473
                        490       500
                 ....*....|....*....|....
gi 110636414 478 afLNSGLRLETETTRAIGRARARY 501
Cdd:COG0661  474 --EELSLRSSEELALLLLKAVARL 495
 
Name Accession Description Interval E-value
UbiB cd13972
Ubiquinone biosynthetic protein UbiB; UbiB is the prokaryotic homolog of yeast Abc1p and human ...
95-342 1.21e-122

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: 362.67  E-value: 1.21e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414  95 LQDRMDTFPQERAVMAIEASLGAPVGTLYREF-GAPVAAASIAQVHPAKIiREGeiQKVAVKVIRPGVRRRFYNDLESFF 173
Cdd:cd13972    2 LQDRVPPFSGKEARAIIEAELGKPLDALFSDFdEEPVAAASIAQVHKARL-LDG--REVAVKVLRPGIEKRIERDLELLR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 174 LAARLQERFIASSRRLRPVEVTQTLAQTTKIEMDLRLEAAAISEIHENSKEDPGFRVPWVDWQRTGRDVLTLEWIDGIKM 253
Cdd:cd13972   79 FLARLAERLLPEARRLRPVEVVKEFARSLLLELDLRLEAANASELRENFLDDPGFYVPEVYWELTSKNVLTMEWIDGIPI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 254 SDTEALRAAGHDLERLATTLIQSFLRHTLRDGFFHADMHPGNLFVEANGTIVAVDFGIVGRIGRKERRFLAEILYGFITR 333
Cdd:cd13972  159 SDIEALDAAGIDRKALAERLVEIFFRQVFRDGFFHADMHPGNIFVDPNGRIIAVDFGIMGRLDKKDRRYLAEILYGFLTR 238

                 ....*....
gi 110636414 334 DFRRVAEVH 342
Cdd:cd13972  239 DYRRVAELH 247
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
4-466 1.08e-116

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310  Cd Length: 537  Bit Score: 357.68  E-value: 1.08e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414   4 LGAYLRLARAGWILLREGVIAAFPGDQFEGMPRFgWRLARLLSRRRSSHRARTERLAIAVDRLGPSYVKLGQFLATRPDV 83
Cdd:PRK04750   1 PMELFRLYKIIRVFLRYGLDELILSHRLTRPLRL-WRRSLFWMPNRHKDKPRGERLRLALEELGPIFVKFGQMLSTRRDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414  84 VGHELARDLASLQDRMDTFPQERAVMAIEASLGAPVGTLYREFGA-PVAAASIAQVHPAKIIREGeiQKVAVKVIRPGVR 162
Cdd:PRK04750  80 FPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIkPLASASIAQVHFARLKDNG--REVVVKVLRPDIL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 163 RRFYNDLESFFLAARLQERFIASSRRLRPVEVTQTLAQTTKIEMDLRLEAAAISEIHENSKEDPGFRVPWVDWQRTGRDV 242
Cdd:PRK04750 158 PVIDADLALMYRLARWVERLLPDGRRLKPREVVAEFEKTLHDELDLMREAANASQLRRNFEDSDMLYVPEVYWDYCSETV 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 243 LTLEWIDGIKMSDTEALRAAGHDLERLATTLIQSFLRHTLRDGFFHADMHPGNLFV----EANGTIVAVDFGIVGRIGRK 318
Cdd:PRK04750 238 MVMERMYGIPVSDVAALRAAGTDMKLLAERGVEVFFTQVFRDGFFHADMHPGNIFVsydpPENPRYIALDFGIVGSLNKE 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 319 ERRFLAEILYGFITRDFRRVAEVHFEAGYVPSHHDVAAFAQALRAIGEPIHGQPAETISMARLLTLLFEVTELFDMQTRP 398
Cdd:PRK04750 318 DKRYLAENFLAFFNRDYRRVAELHVESGWVPPDTRVEELEFAIRAVCEPIFDKPLAEISFGHVLLRLFNTARRFNVEIQP 397
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110636414 399 ELLLLQKTMVVVEGVSRTLDPHFNMWRAAEPVVSEWIEKNLGPQGLFMDAREGAHALMMLVRQAPELA 466
Cdd:PRK04750 398 QLVLLQKTLLNVEGLGRQLDPQLDLWKTAKPFLERWMKEQVGPRALVRALKEEAPFWAEKLPELPRLV 465
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
95-341 2.02e-80

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: 253.57  E-value: 2.02e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414  95 LQDRMDTFPQERAVMAIEASLGAPVGTLYREFG-APVAAASIAQVHPAKIiREGEiqKVAVKVIRPGVRRRFYNDLESFF 173
Cdd:cd05121    2 LQDDVPPFPFEEVRKIIEEELGRPLEEVFAEFDpEPLAAASIAQVHRARL-KDGR--EVAVKVQRPGIEEIIEADLRILR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 174 LAARLQERFIASSRRLRPVEVTQTLAQTTKIEMDLRLEAAAISEIHENSKEDPGFRVPWVDWQRTGRDVLTLEWIDGIKM 253
Cdd:cd05121   79 RLARLLERLSPLLRRLDLVAIVDEFARSLLEELDFRREARNAERFRKNLKDSPDVYVPKVYPELSTRRVLVMEYIDGVKL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 254 SDTEALRAAGHDLERLATTLIQSFLRHTLRDGFFHADMHPGNLFVEANGTIVAVDFGIVGRIGRKERRFLAEILYGFITR 333
Cdd:cd05121  159 TDLEALRAAGIDRKELARRLVDAYLKQIFEDGFFHADPHPGNILVLPDGRIALLDFGMVGRLDPETREALADLLLALVNG 238

                 ....*...
gi 110636414 334 DFRRVAEV 341
Cdd:cd05121  239 DAEGLAEA 246
ADCK1-like cd13969
aarF domain containing kinase 1 and similar proteins; This subfamily is composed of ...
94-341 2.41e-42

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: 152.26  E-value: 2.41e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414  94 SLQDRMDTFPQERAVMAIEASLGAPVGTLYREFG-APVAAASIAQVHPAKIiREGEiqKVAVKVIRPGVRRRFYNDLESF 172
Cdd:cd13969    1 VLQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDeEPIASASLAQVHKAKL-KDGE--EVAVKVQHPDLRKQFAGDLATM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 173 FLAARLQERFIassrrlrP--------VEVTQTLAQttkiEMDLRLEAAAISEIHENSKEDPGFRVPWVDWQRTGRDVLT 244
Cdd:cd13969   78 EFLVNLVEKLF-------PdfpfswlvDELKKNLPK----ELDFLNEARNAERCAKLFKHRPDVYVPKVYWDLSSKRVLT 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 245 LEWIDGIKMSDTEALRAAGHDLERLATTLIQSFLRHTLRDGFFHADMHPGNLFVEANGT-----IVAVDFGIVGRIGRKE 319
Cdd:cd13969  147 MEFIDGIKIDDVEALKKLGIDPKEVARLLSEAFAEMIFVHGFVHCDPHPGNLLVRKNPGpgkpqIVLLDHGLYRELDEEF 226
                        250       260
                 ....*....|....*....|..
gi 110636414 320 RRFLAEILYGFITRDFRRVAEV 341
Cdd:cd13969  227 RLNYCRLWKALILGDEKKIKKY 248
ADCK2-like cd13971
aarF domain containing kinase 2 and similar proteins; This subfamily is composed of ...
95-340 1.20e-34

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: 131.58  E-value: 1.20e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414  95 LQDRMDTFPQERAVMAIEASLGAPVGTLYREF-GAPVAAASIAQVHPAK-----IIREGEIQKVAVKVIRPGVRRRFYND 168
Cdd:cd13971    2 LHSNAPPHSWAHTERALEAAFGKDWEDIFEEFdEEPIGSGSIAQVHRAKlkpdyGGDGGGPRVVAVKVLHPGVREQIERD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 169 LESFFLAARLQErFIASSRRLRPVEVTQTLAQTTKIEMDLRLEAAAISEIHENSKEDPGFRVPWVDWQRTGRDVLTLEWI 248
Cdd:cd13971   82 LAILRLFAKLLE-AIPPLRWLSLPESVEQFASLMLRQLDLRVEAANLERFRENFKDRKDVSFPKPLYPLVTEEVLVETFE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 249 DGIKMSDTEALRAAGHDLERLATTLIQSFLRHTLRDGFFHADMHPGNLFVEANG-----------------TIVAVDFGI 311
Cdd:cd13971  161 EGVPISRTVLAHGGEPLKRKLARIGLDAFLKMLFVDNFVHGDLHPGNILVRFNDsnrpsllvsldargsppRLVFLDAGL 240
                        250       260
                 ....*....|....*....|....*....
gi 110636414 312 VGRIGRKERRFLAEILYGFITRDFRRVAE 340
Cdd:cd13971  241 VTELSPQDRRNFIDLFKAVARGDGYKAAE 269
ABC1_ADCK3 cd13970
Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This ...
92-346 5.59e-33

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: 125.70  E-value: 5.59e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414  92 LASLQDRMDTFPQERAVMAIEASLGAPVGTLYREFGA-PVAAASIAQVHPAkIIREGeiQKVAVKVIRPGVRRRFYNDLE 170
Cdd:cd13970    3 LARLRDSAPPMPWAQLEKVLEAELGEDWRELFAEFDEePFAAASIGQVHRA-TLKDG--REVAVKVQYPGVAESIDSDLN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 171 SFFLAARLqERFIASSRRLRPV--EVTQTLAQttkiEMDLRLEAAAISEIHENSKEDPGFRVPWVDWQRTGRDVLTLEWI 248
Cdd:cd13970   80 NLRRLLKL-TGLLPKGLDLDALiaELREELLE----ECDYEREAANQRRFRELLADDPRFVVPEVIPELSTKRVLTTEFV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 249 DGIKMSDTEALRAAGHDleRLATTLIQSFLRHTLRDGFFHADMHPGN-LFVEANGTIVAVDFGIVGRIGRKERRFLAEIL 327
Cdd:cd13970  155 DGVPLDEAADLSQEERN--RIGELLLRLCLRELFEFGFMQTDPNPGNfLYDPEDGRLGLLDFGAVREYPPEFVDGYRRLV 232
                        250
                 ....*....|....*....
gi 110636414 328 YGFITRDFRRVAEVHFEAG 346
Cdd:cd13970  233 RAALEGDREALLEASVELG 251
ABC1 pfam03109
ABC1 family; This family includes ABC1 from yeast and AarF from Escherichia coli. These ...
113-234 2.57e-26

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: 103.44  E-value: 2.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414  113 ASLGAPVGTLYREFG-APVAAASIAQVHPAKIiREGEiqKVAVKVIRPGVRRRFYNDLESFFLAARLQERFIAssrRLRP 191
Cdd:pfam03109   1 EELGAPVEEVFAEFDeEPIAAASIAQVHRAVL-KDGE--EVAVKVQRPGVKKRIRSDLKLLKFLAKILKKFFP---GFDL 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 110636414  192 VEVTQTLAQTTKIEMDLRLEAAAISEIHENSKEDPGFRVPWVD 234
Cdd:pfam03109  75 DWLVDEFRKSLPQELDFLREAANAEKFRENFADLPWVYVPKVY 117
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
278-322 2.60e-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: 38.23  E-value: 2.60e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 110636414 278 LRHTLRDGFFHADMHPGNLFVEANGTIVAVDFGI--VGRIGRKERRF 322
Cdd:cd05611  110 VEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLsrNGLEKRHNKKF 156
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed ...
207-313 9.05e-03

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: 35.74  E-value: 9.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 207 DLRLEAAAISEIHENskedPGFRVPWV--DWQRTGRDVLTLEWIDGIKMSDtEALRAAGHDLERLATtLIQSFLR--HTL 282
Cdd:cd05120   35 DLEKEAAMLQLLAGK----LSLPVPKVygFGESDGWEYLLMERIEGETLSE-VWPRLSEEEKEKIAD-QLAEILAalHRI 108
                         90       100       110
                 ....*....|....*....|....*....|...
gi 110636414 283 RD-GFFHADMHPGNLFVEANGTIVA-VDFGIVG 313
Cdd:cd05120  109 DSsVLTHGDLHPGNILVKPDGKLSGiIDWEFAG 141
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
211-309 9.42e-03

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: 35.94  E-value: 9.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 211 EAAAISEIHENskedpGFRVPW-VDWQRtgrDVLTLEWIDGIKMSDTEALRAAGHDLERlattlIQSFLRHTLRDGFFHA 289
Cdd:cd05144   68 EFAALKALYEE-----GFPVPKpIDWNR---HAVVMELIDGYPLYQVRLLEDPEEVLDE-----ILELIVKLAKHGLIHG 134
                         90       100
                 ....*....|....*....|
gi 110636414 290 DMHPGNLFVEANGTIVAVDF 309
Cdd:cd05144  135 DFSEFNILVDEDEKITVIDF 154
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
7-444 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: 569.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414    7 YLRLARAGWILLREGVIAAFPGDQFEGMPRFGWRLARLLSRRRSSHRARTERLAIAVDRLGPSYVKLGQFLATRPDVVGH 86
Cdd:TIGR01982   1 LRRLRRIIRVLIRYGFLALVESPIGPLSLRLLRRLLLPFSNRENRLMSRGERLRLALEELGPTFIKFGQTLSTRADLLPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414   87 ELARDLASLQDRMDTFPQERAVMAIEASLGAPVGTLYREFG-APVAAASIAQVHPAKIIrEGEiqKVAVKVIRPGVRRRF 165
Cdd:TIGR01982  81 DIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEeKPLAAASIAQVHRARLV-DGK--EVAVKVLRPGIEKTI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414  166 YNDLESFFLAARLQERFIASSRRLRPVEVTQTLAQTTKIEMDLRLEAAAISEIHENSKEDPGFRVPWVDWQRTGRDVLTL 245
Cdd:TIGR01982 158 AADIALLYRLARIVERLSPDSRRLRPTEVVKEFEKTLRRELDLRREAANASELGENFKNDPGVYVPEVYWDRTSERVLTM 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414  246 EWIDGIKMSDTEALRAAGHDLERLATTLIQSFLRHTLRDGFFHADMHPGNLFVEANGTIVAVDFGIVGRIGRKERRFLAE 325
Cdd:TIGR01982 238 EWIDGIPLSDIAALDEAGLDRKALAENLARSFLNQVLRDGFFHADLHPGNIFVLKDGKIIALDFGIVGRLSEEDRRYLAE 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414  326 ILYGFITRDFRRVAEVHFEAGYVPSHHDVAAFAQALRAIGEPIHGQPAETISMARLLTLLFEVTELFDMQTRPELLLLQK 405
Cdd:TIGR01982 318 ILYGFLNRDYRRVAEVHFDAGYVPSDTDMAEFEQAIRAIGEPIFGQPLKEISVGRLLAGLFKITRDFNMELQPQLLLLQK 397
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 110636414  406 TMVVVEGVSRTLDPHFNMWRAAEPVVSEWIEKNLGPQGL 444
Cdd:TIGR01982 398 TLLTVEGVGRQLDPDLNMWKVAEPFVKRWIRKRLGPKAK 436
AarF COG0661
Predicted unusual protein kinase [General function prediction only]
1-501 3.46e-167

Predicted unusual protein kinase [General function prediction only]


Pssm-ID: 223733 [Multi-domain]  Cd Length: 517  Bit Score: 486.82  E-value: 3.46e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414   1 MSTLGAYLRLARAGWILLREGVIAAFP-GDQFEGMPRF-GWRLARLLSRRRSSHRARTERLAIAVDRLGPSYVKLGQFLA 78
Cdd:COG0661    1 MLTLYAVSRLPRIIRVRLRYLLGRLLRlTGRLALLLRLlSWLGKSKLASSEELREKRAERLRLALEELGPTFIKLGQILS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414  79 TRPDVVGHELARDLASLQDRMDTFPQERAVMAIEASLGAPVGTLYREFGA-PVAAASIAQVHPAKIiREGEiqKVAVKVI 157
Cdd:COG0661   81 TRPDLVPPEYAEELAKLQDRVPPFPFEEAERIIEEELGRPIEELFSEFEPePIASASIAQVHRAVL-KSGE--EVAVKVQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 158 RPGVRRRFYNDLESFFLAARLQERFIASSRRLRPVEVTQTLAQTTKIEMDLRLEAAAISEIHENSKEDPGFRVPWVDWQR 237
Cdd:COG0661  158 RPGIRERIEADLKLLRRLARLIKRLPPGGRRLDLVEVVDEFEKRLREELDYRREAANAERFRENFKDDPDVYVPKVYWEY 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 238 TGRDVLTLEWIDGIKMSDTEALRAAGHDLERLATTLIQSFLRHTLRDGFFHADMHPGNLFVEANGTIVAVDFGIVGRIGR 317
Cdd:COG0661  238 TTRRVLTMEWIDGIKISDIAALKSAGIDRKELAELLVRAFLRQLLRDGFFHADPHPGNILVRSDGRIVLLDFGIVGRLDP 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 318 KERRFLAEILYGFITRDFRRVAEVHFEAGYVPSHHDVAAFAQALRAIGEPIHGQPAETISMARLLTLLFEVTELFDMQTR 397
Cdd:COG0661  318 KFRRYLAELLLAFLNRDYDRVAELHVELGYVPPDTDRDPLAAAIRAVLEPIYGKPLEEISFGEILDKLFEVARRFPMRLP 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 398 PELLLLQKTMVVVEGVSRTLDPHFNMWRAAEPVVSEWIEKNLGPQgLFMDAREGAHALMMLVRQAPELAIRLDHVSRgme 477
Cdd:COG0661  398 PELVLLQRTLLLVEGVGRQLDPRFNLWAVAQPLLAKWLKKQLSPK-LLRELKDEAVAVLNALPLLPRLLRDLLDNDR--- 473
                        490       500
                 ....*....|....*....|....
gi 110636414 478 afLNSGLRLETETTRAIGRARARY 501
Cdd:COG0661  474 --EELSLRSSEELALLLLKAVARL 495
COG0478 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
227-309 1.02e-04

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: 43.08  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110636414 227 GFRVPW-VDWQRtgrDVLTLEWIDGIKMSDteaLRAAGHDLERLATTLIQsFLRHTLRDGFFHADMHPGNLFVEANGTIV 305
Cdd:COG0478  170 GVKVPKpIAWNR---HAVVMEYIEGVELYR---LRLDVENPDEILDKILE-EVRKAYRRGIVHGDLSEFNILVTEDGDIV 242

                 ....
gi 110636414 306 AVDF 309
Cdd:COG0478  243 VIDW 246
 
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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