|
Name |
Accession |
Description |
Interval |
E-value |
| AarF |
COG0661 |
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ... |
51-543 |
2.06e-114 |
|
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: 350.27 E-value: 2.06e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 51 RFSTLYIIQRFIIYYLGIQRRRITNKPDIQ-KNANELRQIFEDLGGFWVKTGQLLALRTDILPDEICDQLIRLQYEAIGF 129
Cdd:COG0661 19 RYGLGELLDRLGLPRLRRLLTGEERREELRrRRAERLRLALEELGPTFIKLGQLLSTRPDLLPPEYAEELAKLQDRVPPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 130 PMAIVRSTIESELGAPMEKIFQDFDETPLAAASIGQVHRATLRSKRKnvpVIVKIQRPNLAEAFKRDLDLIKVVAKVLIS 209
Cdd:COG0661 99 PFEEVRAVIEEELGRPLEELFAEFDPEPLAAASIGQVHRARLKDGRE---VAVKVQRPGIEEAIEADLRILRRLARLLER 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 210 F-NFMSYLRLDEAVSELDKIFNEELDYRYEASNTRNMRKTLKQHK-IYVPKIYNKYSKRRVLVMEYIDGvlasdyIKVLA 287
Cdd:COG0661 176 LsPEGRRLDPVEVVDEFARSLLEELDYRREAANAERFRRNFADDPdVYVPKVYWELSTRRVLTMEWIDG------IKISD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 288 RDPVRASQwqdendFDPKKAGETMFISLLRQVFEDNLYHGDLHPGNIIFLRRSKVAFIDMGSVGSLDRELRVTYNEYTNA 367
Cdd:COG0661 250 LEALDAAG------IDRKRLAERLVRAFLRQVFRDGFFHADPHPGNIFVLPDGRLVLLDFGMVGRLDPETREGLAELLLA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 368 LSDGDFAKAANYILRLAVDIPRVNVPRVRAEMSSAIEvwstkaQLKGIEYKEKSFGGATAEVSKVIARYGI--PSNWTFL 445
Cdd:COG0661 324 LLNRDYDRVAEALLELGFVPPDTDVDELERALRAVLE------PYFGKPLKDISFGELLLELFELARRFPLrlPPELVLL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 446 kvTRSFLTLDGALQYLLPEFDFFKTSRKYnrqsDRRALKQSLEPKSIrtsINQFFDTISEYNNLI--LPELRQRTIAFel 523
Cdd:COG0661 398 --QRTLLTLEGVGRQLDPDFDLWEVAKPF----LERLLRERLGPRAL---LKRLKREAPELAELLprLPRLLERAALI-- 466
|
490 500
....*....|....*....|
gi 332354893 524 tsnIFALLLVVGFQSLAYLL 543
Cdd:COG0661 467 ---IGSALLLLALLGLAALL 483
|
|
| ABC1_ADCK3-like |
cd05121 |
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ... |
121-380 |
2.49e-87 |
|
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: 271.68 E-value: 2.49e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 121 RLQYEAIGFPMAIVRSTIESELGAPMEKIFQDFDETPLAAASIGQVHRATLRSKRKnvpVIVKIQRPNLAEAFKRDLDLI 200
Cdd:cd05121 1 KLQDDVPPFPFEEVRKIIEEELGRPLEEVFAEFDPEPLAAASIAQVHRARLKDGRE---VAVKVQRPGIEEIIEADLRIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 201 KVVAKVLISFN-FMSYLRLDEAVSELDKIFNEELDYRYEASNTRNMRKTLKQH-KIYVPKIYNKYSKRRVLVMEYIDGVL 278
Cdd:cd05121 78 RRLARLLERLSpLLRRLDLVAIVDEFARSLLEELDFRREARNAERFRKNLKDSpDVYVPKVYPELSTRRVLVMEYIDGVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 279 ASDYIKVlardpvrasqwqDENDFDPKKAGETMFISLLRQVFEDNLYHGDLHPGNIIFLRRSKVAFIDMGSVGSLDRELR 358
Cdd:cd05121 158 LTDLEAL------------RAAGIDRKELARRLVDAYLKQIFEDGFFHADPHPGNILVLPDGRIALLDFGMVGRLDPETR 225
|
250 260
....*....|....*....|..
gi 332354893 359 VTYNEYTNALSDGDFAKAANYI 380
Cdd:cd05121 226 EALADLLLALVNGDAEGLAEAL 247
|
|
| UbiB |
TIGR01982 |
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ... |
58-492 |
1.04e-77 |
|
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: 253.37 E-value: 1.04e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 58 IQRFIIYYLGIQRRRITNKPDIQKNANE-LRQIFEDLGGFWVKTGQLLALRTDILPDEICDQLIRLQYEAIGFPMAIVRS 136
Cdd:TIGR01982 24 IGPLSLRLLRRLLLPFSNRENRLMSRGErLRLALEELGPTFIKFGQTLSTRADLLPADIAEELSLLQDRVPPFDFKVARK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 137 TIESELGAPMEKIFQDFDETPLAAASIGQVHRATLRSkrkNVPVIVKIQRPNLAEAFKRDLDLIKVVAKvlISFNFMSY- 215
Cdd:TIGR01982 104 VIEAALGGPLEELFAEFEEKPLAAASIAQVHRARLVD---GKEVAVKVLRPGIEKTIAADIALLYRLAR--IVERLSPDs 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 216 --LRLDEAVSELDKIFNEELDYRYEASN----TRNMRKtlkQHKIYVPKIYNKYSKRRVLVMEYIDGVLASDYIKVlard 289
Cdd:TIGR01982 179 rrLRPTEVVKEFEKTLRRELDLRREAANaselGENFKN---DPGVYVPEVYWDRTSERVLTMEWIDGIPLSDIAAL---- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 290 pvrasqwqDENDFDPKKAGETMFISLLRQVFEDNLYHGDLHPGNIIFLRRSKVAFIDMGSVGSLDRELRVTYNEYTNALS 369
Cdd:TIGR01982 252 --------DEAGLDRKALAENLARSFLNQVLRDGFFHADLHPGNIFVLKDGKIIALDFGIVGRLSEEDRRYLAEILYGFL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 370 DGDFAKAANYILRLAVDIPRVNVPRVRAEMSSAIEvwstkaQLKGIEYKEKSFGGATAEVSKVIARYGIPSNWTFLKVTR 449
Cdd:TIGR01982 324 NRDYRRVAEVHFDAGYVPSDTDMAEFEQAIRAIGE------PIFGQPLKEISVGRLLAGLFKITRDFNMELQPQLLLLQK 397
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 332354893 450 SFLTLDGALQYLLPEFDFFKTSRKYNrqsdRRALKQSLEPKSI 492
Cdd:TIGR01982 398 TLLTVEGVGRQLDPDLNMWKVAEPFV----KRWIRKRLGPKAK 436
|
|
| ABC1 |
pfam03109 |
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ... |
121-379 |
5.70e-64 |
|
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: 210.94 E-value: 5.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 121 RLQYEAIGFPMAIVRSTIESELGAPMEKIFQDFDETPLAAASIGQVHRATLRSKRKnvpVIVKIQRPNLAEAFKRDLDLI 200
Cdd:pfam03109 1 KLQDRAPPFPFEQAKKVIEEELGAPVEEIFAEFDEEPIAAASIAQVHRARLKDGEE---VAVKVQRPGVKKRIRSDLLLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 201 KVVAKVLISFnFMSYLRLDEAVSELDKIFNEELDYRYEASNTRNMRKTLKQHK-IYVPKIYNKYSKRRVLVMEYIDGVLA 279
Cdd:pfam03109 78 RFLAKVAKRF-FPGFRRLDWLVDEFRKSLPQELDFLREAANAEKFRENFADDPdVYVPKVYWELTTERVLTMEYVDGIKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 280 SDYIKVlardpvrasqwqDENDFDPKKAGETMFISLLRQVFEDNLYHGDLHPGNIIFLRRSKVAFIDMGSVGSLDRELRV 359
Cdd:pfam03109 157 DDLDAL------------SEAGIDRKEIARRLVELFLEQIFRDGFFHADPHPGNILVRKDGRIVLLDFGLMGRLDEKFRR 224
|
250 260
....*....|....*....|
gi 332354893 360 TYNEYTNALSDGDFAKAANY 379
Cdd:pfam03109 225 LYAELLLALVNRDYKRVAEM 244
|
|
| ubiB |
PRK04750 |
putative ubiquinone biosynthesis protein UbiB; Reviewed |
86-356 |
3.01e-50 |
|
putative ubiquinone biosynthesis protein UbiB; Reviewed
Pssm-ID: 235310 [Multi-domain] Cd Length: 537 Bit Score: 182.41 E-value: 3.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 86 LRQIFEDLGGFWVKTGQLLALRTDILPDEICDQLIRLQYEAIGFPMAIVRSTIESELGAPMEKIFQDFDETPLAAASIGQ 165
Cdd:PRK04750 55 LRLALEELGPIFVKFGQMLSTRRDLFPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQ 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 166 VHRATLRSKRKnvPVIVKIQRPNLAEAFKRDLDLIKVVAKVLISfnFMS---YLRLDEAVSELDKIFNEELDYRYEASNT 242
Cdd:PRK04750 135 VHFARLKDNGR--EVVVKVLRPDILPVIDADLALMYRLARWVER--LLPdgrRLKPREVVAEFEKTLHDELDLMREAANA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 243 ----RNMRKTlkqHKIYVPKIYNKYSKRRVLVMEYIDGVLASDY---------IKVLARDPVrasqwqdendfdpkkage 309
Cdd:PRK04750 211 sqlrRNFEDS---DMLYVPEVYWDYCSETVMVMERMYGIPVSDVaalraagtdMKLLAERGV------------------ 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 332354893 310 TMFISllrQVFEDNLYHGDLHPGNIIflrrskVAF----------IDMGSVGSLDRE 356
Cdd:PRK04750 270 EVFFT---QVFRDGFFHADMHPGNIF------VSYdppenpryiaLDFGIVGSLNKE 317
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AarF |
COG0661 |
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ... |
51-543 |
2.06e-114 |
|
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: 350.27 E-value: 2.06e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 51 RFSTLYIIQRFIIYYLGIQRRRITNKPDIQ-KNANELRQIFEDLGGFWVKTGQLLALRTDILPDEICDQLIRLQYEAIGF 129
Cdd:COG0661 19 RYGLGELLDRLGLPRLRRLLTGEERREELRrRRAERLRLALEELGPTFIKLGQLLSTRPDLLPPEYAEELAKLQDRVPPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 130 PMAIVRSTIESELGAPMEKIFQDFDETPLAAASIGQVHRATLRSKRKnvpVIVKIQRPNLAEAFKRDLDLIKVVAKVLIS 209
Cdd:COG0661 99 PFEEVRAVIEEELGRPLEELFAEFDPEPLAAASIGQVHRARLKDGRE---VAVKVQRPGIEEAIEADLRILRRLARLLER 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 210 F-NFMSYLRLDEAVSELDKIFNEELDYRYEASNTRNMRKTLKQHK-IYVPKIYNKYSKRRVLVMEYIDGvlasdyIKVLA 287
Cdd:COG0661 176 LsPEGRRLDPVEVVDEFARSLLEELDYRREAANAERFRRNFADDPdVYVPKVYWELSTRRVLTMEWIDG------IKISD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 288 RDPVRASQwqdendFDPKKAGETMFISLLRQVFEDNLYHGDLHPGNIIFLRRSKVAFIDMGSVGSLDRELRVTYNEYTNA 367
Cdd:COG0661 250 LEALDAAG------IDRKRLAERLVRAFLRQVFRDGFFHADPHPGNIFVLPDGRLVLLDFGMVGRLDPETREGLAELLLA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 368 LSDGDFAKAANYILRLAVDIPRVNVPRVRAEMSSAIEvwstkaQLKGIEYKEKSFGGATAEVSKVIARYGI--PSNWTFL 445
Cdd:COG0661 324 LLNRDYDRVAEALLELGFVPPDTDVDELERALRAVLE------PYFGKPLKDISFGELLLELFELARRFPLrlPPELVLL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 446 kvTRSFLTLDGALQYLLPEFDFFKTSRKYnrqsDRRALKQSLEPKSIrtsINQFFDTISEYNNLI--LPELRQRTIAFel 523
Cdd:COG0661 398 --QRTLLTLEGVGRQLDPDFDLWEVAKPF----LERLLRERLGPRAL---LKRLKREAPELAELLprLPRLLERAALI-- 466
|
490 500
....*....|....*....|
gi 332354893 524 tsnIFALLLVVGFQSLAYLL 543
Cdd:COG0661 467 ---IGSALLLLALLGLAALL 483
|
|
| ABC1_ADCK3-like |
cd05121 |
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ... |
121-380 |
2.49e-87 |
|
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: 271.68 E-value: 2.49e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 121 RLQYEAIGFPMAIVRSTIESELGAPMEKIFQDFDETPLAAASIGQVHRATLRSKRKnvpVIVKIQRPNLAEAFKRDLDLI 200
Cdd:cd05121 1 KLQDDVPPFPFEEVRKIIEEELGRPLEEVFAEFDPEPLAAASIAQVHRARLKDGRE---VAVKVQRPGIEEIIEADLRIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 201 KVVAKVLISFN-FMSYLRLDEAVSELDKIFNEELDYRYEASNTRNMRKTLKQH-KIYVPKIYNKYSKRRVLVMEYIDGVL 278
Cdd:cd05121 78 RRLARLLERLSpLLRRLDLVAIVDEFARSLLEELDFRREARNAERFRKNLKDSpDVYVPKVYPELSTRRVLVMEYIDGVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 279 ASDYIKVlardpvrasqwqDENDFDPKKAGETMFISLLRQVFEDNLYHGDLHPGNIIFLRRSKVAFIDMGSVGSLDRELR 358
Cdd:cd05121 158 LTDLEAL------------RAAGIDRKELARRLVDAYLKQIFEDGFFHADPHPGNILVLPDGRIALLDFGMVGRLDPETR 225
|
250 260
....*....|....*....|..
gi 332354893 359 VTYNEYTNALSDGDFAKAANYI 380
Cdd:cd05121 226 EALADLLLALVNGDAEGLAEAL 247
|
|
| UbiB |
TIGR01982 |
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ... |
58-492 |
1.04e-77 |
|
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: 253.37 E-value: 1.04e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 58 IQRFIIYYLGIQRRRITNKPDIQKNANE-LRQIFEDLGGFWVKTGQLLALRTDILPDEICDQLIRLQYEAIGFPMAIVRS 136
Cdd:TIGR01982 24 IGPLSLRLLRRLLLPFSNRENRLMSRGErLRLALEELGPTFIKFGQTLSTRADLLPADIAEELSLLQDRVPPFDFKVARK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 137 TIESELGAPMEKIFQDFDETPLAAASIGQVHRATLRSkrkNVPVIVKIQRPNLAEAFKRDLDLIKVVAKvlISFNFMSY- 215
Cdd:TIGR01982 104 VIEAALGGPLEELFAEFEEKPLAAASIAQVHRARLVD---GKEVAVKVLRPGIEKTIAADIALLYRLAR--IVERLSPDs 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 216 --LRLDEAVSELDKIFNEELDYRYEASN----TRNMRKtlkQHKIYVPKIYNKYSKRRVLVMEYIDGVLASDYIKVlard 289
Cdd:TIGR01982 179 rrLRPTEVVKEFEKTLRRELDLRREAANaselGENFKN---DPGVYVPEVYWDRTSERVLTMEWIDGIPLSDIAAL---- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 290 pvrasqwqDENDFDPKKAGETMFISLLRQVFEDNLYHGDLHPGNIIFLRRSKVAFIDMGSVGSLDRELRVTYNEYTNALS 369
Cdd:TIGR01982 252 --------DEAGLDRKALAENLARSFLNQVLRDGFFHADLHPGNIFVLKDGKIIALDFGIVGRLSEEDRRYLAEILYGFL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 370 DGDFAKAANYILRLAVDIPRVNVPRVRAEMSSAIEvwstkaQLKGIEYKEKSFGGATAEVSKVIARYGIPSNWTFLKVTR 449
Cdd:TIGR01982 324 NRDYRRVAEVHFDAGYVPSDTDMAEFEQAIRAIGE------PIFGQPLKEISVGRLLAGLFKITRDFNMELQPQLLLLQK 397
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 332354893 450 SFLTLDGALQYLLPEFDFFKTSRKYNrqsdRRALKQSLEPKSI 492
Cdd:TIGR01982 398 TLLTVEGVGRQLDPDLNMWKVAEPFV----KRWIRKRLGPKAK 436
|
|
| ABC1 |
pfam03109 |
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ... |
121-379 |
5.70e-64 |
|
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: 210.94 E-value: 5.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 121 RLQYEAIGFPMAIVRSTIESELGAPMEKIFQDFDETPLAAASIGQVHRATLRSKRKnvpVIVKIQRPNLAEAFKRDLDLI 200
Cdd:pfam03109 1 KLQDRAPPFPFEQAKKVIEEELGAPVEEIFAEFDEEPIAAASIAQVHRARLKDGEE---VAVKVQRPGVKKRIRSDLLLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 201 KVVAKVLISFnFMSYLRLDEAVSELDKIFNEELDYRYEASNTRNMRKTLKQHK-IYVPKIYNKYSKRRVLVMEYIDGVLA 279
Cdd:pfam03109 78 RFLAKVAKRF-FPGFRRLDWLVDEFRKSLPQELDFLREAANAEKFRENFADDPdVYVPKVYWELTTERVLTMEYVDGIKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 280 SDYIKVlardpvrasqwqDENDFDPKKAGETMFISLLRQVFEDNLYHGDLHPGNIIFLRRSKVAFIDMGSVGSLDRELRV 359
Cdd:pfam03109 157 DDLDAL------------SEAGIDRKEIARRLVELFLEQIFRDGFFHADPHPGNILVRKDGRIVLLDFGLMGRLDEKFRR 224
|
250 260
....*....|....*....|
gi 332354893 360 TYNEYTNALSDGDFAKAANY 379
Cdd:pfam03109 225 LYAELLLALVNRDYKRVAEM 244
|
|
| ABC1_ADCK3 |
cd13970 |
Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This ... |
119-383 |
4.96e-58 |
|
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: 195.42 E-value: 4.96e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 119 LIRLQYEAIGFPMAIVRSTIESELGAPMEKIFQDFDETPLAAASIGQVHRATLRSKRKnvpVIVKIQRPNLAEAFKRDLD 198
Cdd:cd13970 3 LARLRDSAPPMPWAQLEKVLEAELGEDWRELFAEFDEEPFAAASIGQVHRATLKDGRE---VAVKVQYPGVAESIDSDLN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 199 LIKVVAKVliSFNFMSYLRLDEAVSELDKIFNEELDYRYEASNTRNMRKTLKQH-KIYVPKIYNKYSKRRVLVMEYIDGV 277
Cdd:cd13970 80 NLRRLLKL--TGLLPKGLDLDALIAELREELLEECDYEREAANQRRFRELLADDpRFVVPEVIPELSTKRVLTTEFVDGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 278 lasdyikvlardPV-RASQW-QDENDfdpkKAGETMFISLLRQVFEDNLYHGDLHPGNIIFLRRS-KVAFIDMGSVGSLD 354
Cdd:cd13970 158 ------------PLdEAADLsQEERN----RIGELLLRLCLRELFEFGFMQTDPNPGNFLYDPEDgRLGLLDFGAVREYP 221
|
250 260
....*....|....*....|....*....
gi 332354893 355 RELRVTYNEYTNALSDGDFAKAANYILRL 383
Cdd:cd13970 222 PEFVDGYRRLVRAALEGDREALLEASVEL 250
|
|
| UbiB |
cd13972 |
Ubiquinone biosynthetic protein UbiB; UbiB is the prokaryotic homolog of yeast Abc1p and human ... |
129-378 |
1.43e-57 |
|
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: 193.96 E-value: 1.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 129 FPMAIVRSTIESELGAPMEKIFQDFDETPLAAASIGQVHRATLRSKRKnvpVIVKIQRPNLAEAFKRDLDLIKVVAKVLI 208
Cdd:cd13972 9 FSGKEARAIIEAELGKPLDALFSDFDEEPVAAASIAQVHKARLLDGRE---VAVKVLRPGIEKRIERDLELLRFLARLAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 209 SFNFMS-YLRLDEAVSELDKIFNEELDYRYEASNTRNMRK-TLKQHKIYVPKIYNKYSKRRVLVMEYIDGVLASDyIKVL 286
Cdd:cd13972 86 RLLPEArRLRPVEVVKEFARSLLLELDLRLEAANASELREnFLDDPGFYVPEVYWELTSKNVLTMEWIDGIPISD-IEAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 287 ardpvrasqwqDENDFDPKKAGETMFISLLRQVFEDNLYHGDLHPGNIIFLRRSKVAFIDMGSVGSLDRELRVTYNEYTN 366
Cdd:cd13972 165 -----------DAAGIDRKALAERLVEIFFRQVFRDGFFHADMHPGNIFVDPNGRIIAVDFGIMGRLDKKDRRYLAEILY 233
|
250
....*....|..
gi 332354893 367 ALSDGDFAKAAN 378
Cdd:cd13972 234 GFLTRDYRRVAE 245
|
|
| ubiB |
PRK04750 |
putative ubiquinone biosynthesis protein UbiB; Reviewed |
86-356 |
3.01e-50 |
|
putative ubiquinone biosynthesis protein UbiB; Reviewed
Pssm-ID: 235310 [Multi-domain] Cd Length: 537 Bit Score: 182.41 E-value: 3.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 86 LRQIFEDLGGFWVKTGQLLALRTDILPDEICDQLIRLQYEAIGFPMAIVRSTIESELGAPMEKIFQDFDETPLAAASIGQ 165
Cdd:PRK04750 55 LRLALEELGPIFVKFGQMLSTRRDLFPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQ 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 166 VHRATLRSKRKnvPVIVKIQRPNLAEAFKRDLDLIKVVAKVLISfnFMS---YLRLDEAVSELDKIFNEELDYRYEASNT 242
Cdd:PRK04750 135 VHFARLKDNGR--EVVVKVLRPDILPVIDADLALMYRLARWVER--LLPdgrRLKPREVVAEFEKTLHDELDLMREAANA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 243 ----RNMRKTlkqHKIYVPKIYNKYSKRRVLVMEYIDGVLASDY---------IKVLARDPVrasqwqdendfdpkkage 309
Cdd:PRK04750 211 sqlrRNFEDS---DMLYVPEVYWDYCSETVMVMERMYGIPVSDVaalraagtdMKLLAERGV------------------ 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 332354893 310 TMFISllrQVFEDNLYHGDLHPGNIIflrrskVAF----------IDMGSVGSLDRE 356
Cdd:PRK04750 270 EVFFT---QVFRDGFFHADMHPGNIF------VSYdppenpryiaLDFGIVGSLNKE 317
|
|
| ADCK1-like |
cd13969 |
aarF domain containing kinase 1 and similar proteins; This subfamily is composed of ... |
130-375 |
3.05e-49 |
|
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: 171.90 E-value: 3.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 130 PMAIVRSTIESELGAPMEKIFQDFDETPLAAASIGQVHRATLRSKRKnvpVIVKIQRPNLAEAFKRDLDLIKVVAKVL-- 207
Cdd:cd13969 10 PYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVHKAKLKDGEE---VAVKVQHPDLRKQFAGDLATMEFLVNLVek 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 208 ISFNFMSYLRLDEAVSELDKifneELDYRYEASNTRNMRKTLK-QHKIYVPKIYNKYSKRRVLVMEYIDGVLASD--YIK 284
Cdd:cd13969 87 LFPDFPFSWLVDELKKNLPK----ELDFLNEARNAERCAKLFKhRPDVYVPKVYWDLSSKRVLTMEFIDGIKIDDveALK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 285 vlardpvrasqwqdENDFDPKKAGETMFISLLRQVFEDNLYHGDLHPGNiIFLRRSK------VAFIDMGSVGSLDRELR 358
Cdd:cd13969 163 --------------KLGIDPKEVARLLSEAFAEMIFVHGFVHCDPHPGN-LLVRKNPgpgkpqIVLLDHGLYRELDEEFR 227
|
250
....*....|....*..
gi 332354893 359 VTYNEYTNALSDGDFAK 375
Cdd:cd13969 228 LNYCRLWKALILGDEKK 244
|
|
| ADCK2-like |
cd13971 |
aarF domain containing kinase 2 and similar proteins; This subfamily is composed of ... |
135-384 |
2.82e-36 |
|
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: 137.74 E-value: 2.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 135 RSTIESELGAPMEKIFQDFDETPLAAASIGQVHRATLR-----SKRKNVPVIVKIQRPNLAEAFKRDLDLIKVVAKVLIS 209
Cdd:cd13971 15 ERALEAAFGKDWEDIFEEFDEEPIGSGSIAQVHRAKLKpdyggDGGGPRVVAVKVLHPGVREQIERDLAILRLFAKLLEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 210 FNFMSYLRLDEAVSELDKIFNEELDYRYEASNTRNMRKTLKQHK-IYVPKIYNKYSKRRVLVMEYIDGVlasdyikvlar 288
Cdd:cd13971 95 IPPLRWLSLPESVEQFASLMLRQLDLRVEAANLERFRENFKDRKdVSFPKPLYPLVTEEVLVETFEEGV----------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 289 dPV-RASQWQDENDFDPKKA--GETMFislLRQVFEDNLYHGDLHPGNII-----------------FLRRSKVAFIDMG 348
Cdd:cd13971 164 -PIsRTVLAHGGEPLKRKLAriGLDAF---LKMLFVDNFVHGDLHPGNILvrfndsnrpsllvsldaRGSPPRLVFLDAG 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 332354893 349 SVGSLDRELRVTYNEYTNALSDGDFAKAANYILRLA 384
Cdd:cd13971 240 LVTELSPQDRRNFIDLFKAVARGDGYKAAELMLERS 275
|
|
| Bud32 |
COG3642 |
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ... |
243-348 |
8.02e-09 |
|
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 442859 [Multi-domain] Cd Length: 159 Bit Score: 54.97 E-value: 8.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 243 RNMRKtLKQHKIYVPKIYNKYSKRRVLVMEYIDGVLASDyikVLARDPVRASQWQDendfdpkkAGEtmfisLLRQVFED 322
Cdd:COG3642 8 RLLRE-LREAGVPVPKVLDVDPDDADLVMEYIEGETLAD---LLEEGELPPELLRE--------LGR-----LLARLHRA 70
|
90 100
....*....|....*....|....*.
gi 332354893 323 NLYHGDLHPGNIIfLRRSKVAFIDMG 348
Cdd:COG3642 71 GIVHGDLTTSNIL-VDDGGVYLIDFG 95
|
|
| APH_ChoK_like |
cd05120 |
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ... |
227-356 |
2.36e-07 |
|
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).
Pssm-ID: 270690 [Multi-domain] Cd Length: 158 Bit Score: 50.76 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 227 KIFNEELDYRYEasNTRNMRKTLKQHK-IYVPKIYNKY--SKRRVLVMEYIDGVLASDyikvlardpvrasQWQDENDFD 303
Cdd:cd05120 26 KIGPPRLKKDLE--KEAAMLQLLAGKLsLPVPKVYGFGesDGWEYLLMERIEGETLSE-------------VWPRLSEEE 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 332354893 304 PKKAGE--TMFISLLRQVFEDNLYHGDLHPGNIIFLRRSKV-AFIDMGSVGSLDRE 356
Cdd:cd05120 91 KEKIADqlAEILAALHRIDSSVLTHGDLHPGNILVKPDGKLsGIIDWEFAGYGPPA 146
|
|
| PRK14879 |
PRK14879 |
Kae1-associated kinase Bud32; |
190-348 |
2.49e-07 |
|
Kae1-associated kinase Bud32;
Pssm-ID: 237847 [Multi-domain] Cd Length: 211 Bit Score: 51.83 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 190 AEA--FKRDLDLIKVVAKVLISFNFMsylrldeaVSELDKIFNEElDYRYEAsntRNMRKTLKQhKIYVPKIYNKYSKRR 267
Cdd:PRK14879 8 AEAeiYLGDFLGIKAVIKWRIPKRYR--------HPELDERIRRE-RTRREA---RIMSRARKA-GVNVPAVYFVDPENF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 268 VLVMEYIDGVLASDYIKVLARDPVRASqwqdendfdpKKAGEtmfisLLRQVFEDNLYHGDLHPGNIIfLRRSKVAFIDM 347
Cdd:PRK14879 75 IIVMEYIEGEPLKDLINSNGMEELELS----------REIGR-----LVGKLHSAGIIHGDLTTSNMI-LSGGKIYLIDF 138
|
.
gi 332354893 348 G 348
Cdd:PRK14879 139 G 139
|
|
| arch_bud32 |
TIGR03724 |
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ... |
230-348 |
5.42e-06 |
|
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]
Pssm-ID: 274749 [Multi-domain] Cd Length: 199 Bit Score: 47.59 E-value: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 230 NEELDYRYEASNTRN----MRKtLKQHKIYVPKIYNKYSKRRVLVMEYIDGVLASDYIKVLARDPVRasqwqdendfdpk 305
Cdd:TIGR03724 32 HPELDERLRKERTRRearlLSR-ARKAGVNTPVIYDVDPDNKTIVMEYIEGKPLKDVIEENGDELAR------------- 97
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 332354893 306 KAGEtmfisLLRQVFEDNLYHGDLHPGNIIfLRRSKVAFIDMG 348
Cdd:TIGR03724 98 EIGR-----LVGKLHKAGIVHGDLTTSNII-VRDDKVYLIDFG 134
|
|
| PRK09605 |
PRK09605 |
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase; |
231-348 |
1.38e-05 |
|
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
Pssm-ID: 236586 [Multi-domain] Cd Length: 535 Bit Score: 47.96 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 231 EELDYRYEASNTRNMRK---TLKQHKIYVPKIYNKYSKRRVLVMEYIDGVLASDYIKvlaRDPVRAsqwqdendfdpKKA 307
Cdd:PRK09605 372 PELDERLRTERTRAEARllsEARRAGVPTPVIYDVDPEEKTIVMEYIGGKDLKDVLE---GNPELV-----------RKV 437
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 332354893 308 GEtmfisLLRQVFEDNLYHGDLHPGNIIfLRRSKVAFIDMG 348
Cdd:PRK09605 438 GE-----IVAKLHKAGIVHGDLTTSNFI-VRDDRLYLIDFG 472
|
|
| PKc_like |
cd13968 |
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ... |
240-348 |
1.36e-04 |
|
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.
Pssm-ID: 270870 [Multi-domain] Cd Length: 136 Bit Score: 42.04 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 240 SNTRNMRKtLKQHKIYVPKIYNKYSKRR--VLVMEYIDGVLASDYIkvlardpvrasQWQDENDFDPKKAGETMfISLLR 317
Cdd:cd13968 39 SEMDILRR-LKGLELNIPKVLVTEDVDGpnILLMELVKGGTLIAYT-----------QEEELDEKDVESIMYQL-AECMR 105
|
90 100 110
....*....|....*....|....*....|.
gi 332354893 318 QVFEDNLYHGDLHPGNIIFLRRSKVAFIDMG 348
Cdd:cd13968 106 LLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
|
|
| RIO2 |
COG0478 |
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ... |
247-346 |
1.49e-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: 42.97 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 247 KTLKQHKIYVPKIYnkYSKRRVLVMEYIDGVLasdyikvLARDPVRASQWQdendFDpkkagetMFISLLRQVFEDNLYH 326
Cdd:COG0478 54 ERLYPAGLPVPRPI--AANRHAIVMERIEGVE-------LARLKLEDPEEV----LD-------KILEEIRRAHDAGIVH 113
|
90 100
....*....|....*....|
gi 332354893 327 GDLHPGNIIFLRRSKVAFID 346
Cdd:COG0478 114 ADLSEYNILVDDDGGVWIID 133
|
|
| SPS1 |
COG0515 |
Serine/threonine protein kinase [Signal transduction mechanisms]; |
157-356 |
1.60e-04 |
|
Serine/threonine protein kinase [Signal transduction mechanisms];
Pssm-ID: 440281 [Multi-domain] Cd Length: 482 Bit Score: 44.62 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 157 PLAAASIGQVHRATLRSKRKnvPVIVKIQRPNLAEafkrdldlikvvakvlisfnfmsylrlDEAVSELdkifneeldYR 236
Cdd:COG0515 14 LLGRGGMGVVYLARDLRLGR--PVALKVLRPELAA---------------------------DPEARER---------FR 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 237 YEASNTRNMRktlkqHKiYVPKIYN--KYSKRRVLVMEYIDGVLASDYIKvlARDPvrasqwqdendFDPKKAgetmfIS 314
Cdd:COG0515 56 REARALARLN-----HP-NIVRVYDvgEEDGRPYLVMEYVEGESLADLLR--RRGP-----------LPPAEA-----LR 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 332354893 315 LLRQVFED-------NLYHGDLHPGNIIFLRRSKVAFIDMGSVGSLDRE 356
Cdd:COG0515 112 ILAQLAEAlaaahaaGIVHRDIKPANILLTPDGRVKLIDFGIARALGGA 160
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|
| RIO2_C |
cd05144 |
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ... |
247-346 |
5.44e-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: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 247 KTLKQHKIYVPKI--YNkyskRRVLVMEYIDGVLASDyIKVLArdpvrasqwqdendfDPKKAGETMfISLLRQVFEDNL 324
Cdd:cd05144 73 KALYEEGFPVPKPidWN----RHAVVMELIDGYPLYQ-VRLLE---------------DPEEVLDEI-LELIVKLAKHGL 131
|
90 100
....*....|....*....|..
gi 332354893 325 YHGDLHPGNIIFLRRSKVAFID 346
Cdd:cd05144 132 IHGDFSEFNILVDEDEKITVID 153
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|
| RIO1 |
pfam01163 |
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ... |
243-346 |
8.49e-04 |
|
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria and eukaryotes. Activity of Rio1 is vital in Saccharomyces cerevisiae for the processing of ribosomal RNA, as well as for proper cell cycle progression and chromosome maintenance. The structure of RIO1 has been determined.
Pssm-ID: 460091 [Multi-domain] Cd Length: 184 Bit Score: 40.68 E-value: 8.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 243 RNMRKtLKQHKIYVPKIYNkySKRRVLVMEYIDgvlasdyikvlaRDPVRASQWQDENDFDPKKAGETMFISLLRQVFED 322
Cdd:pfam01163 58 RNLKR-LYEAGVPVPKPID--VNRHVLVMEFIG------------KDGVPAPKLKDVELEEAEEIYDEIIREMRRLYQEA 122
|
90 100
....*....|....*....|....
gi 332354893 323 NLYHGDLHPGNIIfLRRSKVAFID 346
Cdd:pfam01163 123 GLVHGDLSEYNIL-VHDDKPVIID 145
|
|
| COG2112 |
COG2112 |
Predicted Ser/Thr protein kinase [Signal transduction mechanisms]; |
257-349 |
9.82e-03 |
|
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
Pssm-ID: 441715 [Multi-domain] Cd Length: 225 Bit Score: 38.08 E-value: 9.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332354893 257 PKIYNkYSkRRVLVMEYIDGVLASDYIKVLARDPVRAsqwqdendfdpkkagetMFISLLRQVFE-DN--LYHGDLH-PG 332
Cdd:COG2112 97 PKLYD-YG-RDFLVMEYIEGEPLKDWLENLDKEELRK-----------------VIRELLEAAYLlDRigIDHGELSrPG 157
|
90
....*....|....*..
gi 332354893 333 NIIFLRRSKVAFIDMGS 349
Cdd:COG2112 158 KHVIVDKGRPYIIDFES 174
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