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Conserved domains on  [gi|18409920|ref|NP_565025|]
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Protein kinase superfamily protein [Arabidopsis thaliana]

Protein Classification

ABC1 kinase family protein( domain architecture ID 11429476)

ABC1 (activator of bc1 complex) kinase family protein is an atypical protein kinase belonging to the protein kinase superfamily, similar to Arabidopsis thaliana ABC1-like kinases

CATH:  1.10.510.10
EC:  2.7.-.-
Gene Ontology:  GO:0006468|GO:0004672|GO:0005524
PubMed:  16244704|19614568
SCOP:  3000066

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
86-495 1.80e-149

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: 443.11  E-value: 1.80e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920  86 LRRLAQIGTTFS-----------YWFGLRLADEALERSDQMFKVRAAELRKLLVELGPAYVKIAQAVSSRPDLIPPIYLD 154
Cdd:COG0661   7 LRRLARIARVLLryglgelldrlGLPRLRRLLTGEERREELRRRRAERLRLALEELGPTFIKLGQLLSTRPDLLPPEYAE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 155 ELSLLQDQITPFSTEVAFNMIEDELGLPIDELFSEISPEPVAAASLGQVYQARLRrSGKVVAVKVQRPGVRAAIALDTLI 234
Cdd:COG0661  87 ELAKLQDRVPPFPFEEVRAVIEEELGRPLEELFAEFDPEPLAAASIGQVHRARLK-DGREVAVKVQRPGIEEAIEADLRI 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 235 LRYIAGLIKKAGRFNS--DLEAVVDEWATSLFKEMDYLNEAQNGIKFRKLYGGIKDVLVPKMYTEYSTSKVLVMEWVEGQ 312
Cdd:COG0661 166 LRRLARLLERLSPEGRrlDPVEVVDEFARSLLEELDYRREAANAERFRRNFADDPDVYVPKVYWELSTRRVLTMEWIDGI 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 313 KLNEVNDL--------YLVEVGVYCSFNQLLEYGFYHADPHPGNFLRTYDGQLAYLDFGMMGDFRPELRDGFMEACLHLV 384
Cdd:COG0661 246 KISDLEALdaagidrkRLAERLVRAFLRQVFRDGFFHADPHPGNIFVLPDGRLVLLDFGMVGRLDPETREGLAELLLALL 325
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 385 NRDFKALAKDFVTLGLLPPTAEKSAVTKALTDVFQDAISRGVRNISFGDLLGDLGKTMYRFKFRIPPYFSLVIRSLAVLE 464
Cdd:COG0661 326 NRDYDRVAEALLELGFVPPDTDVDELERALRAVLEPYFGKPLKDISFGELLLELFELARRFPLRLPPELVLLQRTLLTLE 405
                       410       420       430
                ....*....|....*....|....*....|.
gi 18409920 465 GIAIGISPNYKVLGSTYPWIARKILTDSSPQ 495
Cdd:COG0661 406 GVGRQLDPDFDLWEVAKPFLERLLRERLGPR 436
 
Name Accession Description Interval E-value
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
86-495 1.80e-149

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: 443.11  E-value: 1.80e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920  86 LRRLAQIGTTFS-----------YWFGLRLADEALERSDQMFKVRAAELRKLLVELGPAYVKIAQAVSSRPDLIPPIYLD 154
Cdd:COG0661   7 LRRLARIARVLLryglgelldrlGLPRLRRLLTGEERREELRRRRAERLRLALEELGPTFIKLGQLLSTRPDLLPPEYAE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 155 ELSLLQDQITPFSTEVAFNMIEDELGLPIDELFSEISPEPVAAASLGQVYQARLRrSGKVVAVKVQRPGVRAAIALDTLI 234
Cdd:COG0661  87 ELAKLQDRVPPFPFEEVRAVIEEELGRPLEELFAEFDPEPLAAASIGQVHRARLK-DGREVAVKVQRPGIEEAIEADLRI 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 235 LRYIAGLIKKAGRFNS--DLEAVVDEWATSLFKEMDYLNEAQNGIKFRKLYGGIKDVLVPKMYTEYSTSKVLVMEWVEGQ 312
Cdd:COG0661 166 LRRLARLLERLSPEGRrlDPVEVVDEFARSLLEELDYRREAANAERFRRNFADDPDVYVPKVYWELSTRRVLTMEWIDGI 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 313 KLNEVNDL--------YLVEVGVYCSFNQLLEYGFYHADPHPGNFLRTYDGQLAYLDFGMMGDFRPELRDGFMEACLHLV 384
Cdd:COG0661 246 KISDLEALdaagidrkRLAERLVRAFLRQVFRDGFFHADPHPGNIFVLPDGRLVLLDFGMVGRLDPETREGLAELLLALL 325
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 385 NRDFKALAKDFVTLGLLPPTAEKSAVTKALTDVFQDAISRGVRNISFGDLLGDLGKTMYRFKFRIPPYFSLVIRSLAVLE 464
Cdd:COG0661 326 NRDYDRVAEALLELGFVPPDTDVDELERALRAVLEPYFGKPLKDISFGELLLELFELARRFPLRLPPELVLLQRTLLTLE 405
                       410       420       430
                ....*....|....*....|....*....|.
gi 18409920 465 GIAIGISPNYKVLGSTYPWIARKILTDSSPQ 495
Cdd:COG0661 406 GVGRQLDPDFDLWEVAKPFLERLLRERLGPR 436
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
159-395 4.44e-101

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: 309.43  E-value: 4.44e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 159 LQDQITPFSTEVAFNMIEDELGLPIDELFSEISPEPVAAASLGQVYQARLRrSGKVVAVKVQRPGVRAAIALDTLILRYI 238
Cdd:cd05121   2 LQDDVPPFPFEEVRKIIEEELGRPLEEVFAEFDPEPLAAASIAQVHRARLK-DGREVAVKVQRPGIEEIIEADLRILRRL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 239 AGLIKKAGRFNS--DLEAVVDEWATSLFKEMDYLNEAQNGIKFRKLYGGIKDVLVPKMYTEYSTSKVLVMEWVEGQKLNE 316
Cdd:cd05121  81 ARLLERLSPLLRrlDLVAIVDEFARSLLEELDFRREARNAERFRKNLKDSPDVYVPKVYPELSTRRVLVMEYIDGVKLTD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 317 VNDLY--------LVEVGVYCSFNQLLEYGFYHADPHPGNFLRTYDGQLAYLDFGMMGDFRPELRDGFMEACLHLVNRDF 388
Cdd:cd05121 161 LEALRaagidrkeLARRLVDAYLKQIFEDGFFHADPHPGNILVLPDGRIALLDFGMVGRLDPETREALADLLLALVNGDA 240

                ....*..
gi 18409920 389 KALAKDF 395
Cdd:cd05121 241 EGLAEAL 247
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
66-497 1.30e-95

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: 302.29  E-value: 1.30e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920    66 LSEYNF-PRIDGMYKKKPLILLRRLAQIgttfsyWFGLRLADEAlersdqmfkvRAAELRKLLVELGPAYVKIAQAVSSR 144
Cdd:TIGR01982  11 LIRYGFlALVESPIGPLSLRLLRRLLLP------FSNRENRLMS----------RGERLRLALEELGPTFIKFGQTLSTR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920   145 PDLIPPIYLDELSLLQDQITPFSTEVAFNMIEDELGLPIDELFSEISPEPVAAASLGQVYQARLRrSGKVVAVKVQRPGV 224
Cdd:TIGR01982  75 ADLLPADIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEEKPLAAASIAQVHRARLV-DGKEVAVKVLRPGI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920   225 RAAIALDTLILRYIAgliKKAGRFNSDLE-----AVVDEWATSLFKEMDYLNEAQNGIKFRKLYGGIKDVLVPKMYTEYS 299
Cdd:TIGR01982 154 EKTIAADIALLYRLA---RIVERLSPDSRrlrptEVVKEFEKTLRRELDLRREAANASELGENFKNDPGVYVPEVYWDRT 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920   300 TSKVLVMEWVEGQKLNEVNDL--------YLVEVGVYCSFNQLLEYGFYHADPHPGNFLRTYDGQLAYLDFGMMGDFRPE 371
Cdd:TIGR01982 231 SERVLTMEWIDGIPLSDIAALdeagldrkALAENLARSFLNQVLRDGFFHADLHPGNIFVLKDGKIIALDFGIVGRLSEE 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920   372 LRDGFMEACLHLVNRDFKALAKDFVTLGLLPPTAEKSAVTKALTDVFQDAISRGVRNISFGDLLGDLGKTMYRFKFRIPP 451
Cdd:TIGR01982 311 DRRYLAEILYGFLNRDYRRVAEVHFDAGYVPSDTDMAEFEQAIRAIGEPIFGQPLKEISVGRLLAGLFKITRDFNMELQP 390
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 18409920   452 YFSLVIRSLAVLEGIAIGISPNYKVLGSTYPWIARKILTDSSPQLK 497
Cdd:TIGR01982 391 QLLLLQKTLLTVEGVGRQLDPDLNMWKVAEPFVKRWIRKRLGPKAK 436
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
159-394 7.98e-88

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: 274.88  E-value: 7.98e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920   159 LQDQITPFSTEVAFNMIEDELGLPIDELFSEISPEPVAAASLGQVYQARLRrSGKVVAVKVQRPGVRAAIALDTLILRYI 238
Cdd:pfam03109   2 LQDRAPPFPFEQAKKVIEEELGAPVEEIFAEFDEEPIAAASIAQVHRARLK-DGEEVAVKVQRPGVKKRIRSDLLLLRFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920   239 AGLIKKAGRFNSDLEAVVDEWATSLFKEMDYLNEAQNGIKFRKLYGGIKDVLVPKMYTEYSTSKVLVMEWVEGQKLNEVN 318
Cdd:pfam03109  81 AKVAKRFFPGFRRLDWLVDEFRKSLPQELDFLREAANAEKFRENFADDPDVYVPKVYWELTTERVLTMEYVDGIKIDDLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920   319 DL--------YLVEVGVYCSFNQLLEYGFYHADPHPGNFLRTYDGQLAYLDFGMMGDFRPELRDGFMEACLHLVNRDFKA 390
Cdd:pfam03109 161 ALseagidrkEIARRLVELFLEQIFRDGFFHADPHPGNILVRKDGRIVLLDFGLMGRLDEKFRRLYAELLLALVNRDYKR 240

                  ....
gi 18409920   391 LAKD 394
Cdd:pfam03109 241 VAEM 244
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
74-466 1.82e-64

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 222.86  E-value: 1.82e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920   74 IDGMYKKKPLILLRRLAqigttfsYWFGLRLADEAlersdqmfkvRAAELRKLLVELGPAYVKIAQAVSSRPDLIPPIYL 153
Cdd:PRK04750  23 ILSHRLTRPLRLWRRSL-------FWMPNRHKDKP----------RGERLRLALEELGPIFVKFGQMLSTRRDLFPPDIA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920  154 DELSLLQDQITPFSTEVAFNMIEDELGLPIDELFSEISPEPVAAASLGQVYQARLRRSGKVVAVKVQRPGVRAAIALDTL 233
Cdd:PRK04750  86 DELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQVHFARLKDNGREVVVKVLRPDILPVIDADLA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920  234 ILRYIAGLIKKA---GRFNSDLEaVVDEWATSLFKEMDYLNEAQNGIKFRKLYGGIKDVLVPKMYTEYSTSKVLVMEWVE 310
Cdd:PRK04750 166 LMYRLARWVERLlpdGRRLKPRE-VVAEFEKTLHDELDLMREAANASQLRRNFEDSDMLYVPEVYWDYCSETVMVMERMY 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920  311 GQKLNEVNDL--------YLVEVGVYCSFNQLLEYGFYHADPHPGNFLRTYD----GQLAYLDFGMMGDFRPELRDGFME 378
Cdd:PRK04750 245 GIPVSDVAALraagtdmkLLAERGVEVFFTQVFRDGFFHADMHPGNIFVSYDppenPRYIALDFGIVGSLNKEDKRYLAE 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920  379 ACLHLVNRDFKALAKDFVTLGLLPPTaeksavTKAltDVFQDAIsRGV---------RNISFGDLLGDLGKTMYRFKFRI 449
Cdd:PRK04750 325 NFLAFFNRDYRRVAELHVESGWVPPD------TRV--EELEFAI-RAVcepifdkplAEISFGHVLLRLFNTARRFNVEI 395
                        410
                 ....*....|....*..
gi 18409920  450 PPYFSLVIRSLAVLEGI 466
Cdd:PRK04750 396 QPQLVLLQKTLLNVEGL 412
 
Name Accession Description Interval E-value
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
86-495 1.80e-149

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: 443.11  E-value: 1.80e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920  86 LRRLAQIGTTFS-----------YWFGLRLADEALERSDQMFKVRAAELRKLLVELGPAYVKIAQAVSSRPDLIPPIYLD 154
Cdd:COG0661   7 LRRLARIARVLLryglgelldrlGLPRLRRLLTGEERREELRRRRAERLRLALEELGPTFIKLGQLLSTRPDLLPPEYAE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 155 ELSLLQDQITPFSTEVAFNMIEDELGLPIDELFSEISPEPVAAASLGQVYQARLRrSGKVVAVKVQRPGVRAAIALDTLI 234
Cdd:COG0661  87 ELAKLQDRVPPFPFEEVRAVIEEELGRPLEELFAEFDPEPLAAASIGQVHRARLK-DGREVAVKVQRPGIEEAIEADLRI 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 235 LRYIAGLIKKAGRFNS--DLEAVVDEWATSLFKEMDYLNEAQNGIKFRKLYGGIKDVLVPKMYTEYSTSKVLVMEWVEGQ 312
Cdd:COG0661 166 LRRLARLLERLSPEGRrlDPVEVVDEFARSLLEELDYRREAANAERFRRNFADDPDVYVPKVYWELSTRRVLTMEWIDGI 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 313 KLNEVNDL--------YLVEVGVYCSFNQLLEYGFYHADPHPGNFLRTYDGQLAYLDFGMMGDFRPELRDGFMEACLHLV 384
Cdd:COG0661 246 KISDLEALdaagidrkRLAERLVRAFLRQVFRDGFFHADPHPGNIFVLPDGRLVLLDFGMVGRLDPETREGLAELLLALL 325
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 385 NRDFKALAKDFVTLGLLPPTAEKSAVTKALTDVFQDAISRGVRNISFGDLLGDLGKTMYRFKFRIPPYFSLVIRSLAVLE 464
Cdd:COG0661 326 NRDYDRVAEALLELGFVPPDTDVDELERALRAVLEPYFGKPLKDISFGELLLELFELARRFPLRLPPELVLLQRTLLTLE 405
                       410       420       430
                ....*....|....*....|....*....|.
gi 18409920 465 GIAIGISPNYKVLGSTYPWIARKILTDSSPQ 495
Cdd:COG0661 406 GVGRQLDPDFDLWEVAKPFLERLLRERLGPR 436
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
159-395 4.44e-101

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: 309.43  E-value: 4.44e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 159 LQDQITPFSTEVAFNMIEDELGLPIDELFSEISPEPVAAASLGQVYQARLRrSGKVVAVKVQRPGVRAAIALDTLILRYI 238
Cdd:cd05121   2 LQDDVPPFPFEEVRKIIEEELGRPLEEVFAEFDPEPLAAASIAQVHRARLK-DGREVAVKVQRPGIEEIIEADLRILRRL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 239 AGLIKKAGRFNS--DLEAVVDEWATSLFKEMDYLNEAQNGIKFRKLYGGIKDVLVPKMYTEYSTSKVLVMEWVEGQKLNE 316
Cdd:cd05121  81 ARLLERLSPLLRrlDLVAIVDEFARSLLEELDFRREARNAERFRKNLKDSPDVYVPKVYPELSTRRVLVMEYIDGVKLTD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 317 VNDLY--------LVEVGVYCSFNQLLEYGFYHADPHPGNFLRTYDGQLAYLDFGMMGDFRPELRDGFMEACLHLVNRDF 388
Cdd:cd05121 161 LEALRaagidrkeLARRLVDAYLKQIFEDGFFHADPHPGNILVLPDGRIALLDFGMVGRLDPETREALADLLLALVNGDA 240

                ....*..
gi 18409920 389 KALAKDF 395
Cdd:cd05121 241 EGLAEAL 247
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
66-497 1.30e-95

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: 302.29  E-value: 1.30e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920    66 LSEYNF-PRIDGMYKKKPLILLRRLAQIgttfsyWFGLRLADEAlersdqmfkvRAAELRKLLVELGPAYVKIAQAVSSR 144
Cdd:TIGR01982  11 LIRYGFlALVESPIGPLSLRLLRRLLLP------FSNRENRLMS----------RGERLRLALEELGPTFIKFGQTLSTR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920   145 PDLIPPIYLDELSLLQDQITPFSTEVAFNMIEDELGLPIDELFSEISPEPVAAASLGQVYQARLRrSGKVVAVKVQRPGV 224
Cdd:TIGR01982  75 ADLLPADIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEEKPLAAASIAQVHRARLV-DGKEVAVKVLRPGI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920   225 RAAIALDTLILRYIAgliKKAGRFNSDLE-----AVVDEWATSLFKEMDYLNEAQNGIKFRKLYGGIKDVLVPKMYTEYS 299
Cdd:TIGR01982 154 EKTIAADIALLYRLA---RIVERLSPDSRrlrptEVVKEFEKTLRRELDLRREAANASELGENFKNDPGVYVPEVYWDRT 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920   300 TSKVLVMEWVEGQKLNEVNDL--------YLVEVGVYCSFNQLLEYGFYHADPHPGNFLRTYDGQLAYLDFGMMGDFRPE 371
Cdd:TIGR01982 231 SERVLTMEWIDGIPLSDIAALdeagldrkALAENLARSFLNQVLRDGFFHADLHPGNIFVLKDGKIIALDFGIVGRLSEE 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920   372 LRDGFMEACLHLVNRDFKALAKDFVTLGLLPPTAEKSAVTKALTDVFQDAISRGVRNISFGDLLGDLGKTMYRFKFRIPP 451
Cdd:TIGR01982 311 DRRYLAEILYGFLNRDYRRVAEVHFDAGYVPSDTDMAEFEQAIRAIGEPIFGQPLKEISVGRLLAGLFKITRDFNMELQP 390
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 18409920   452 YFSLVIRSLAVLEGIAIGISPNYKVLGSTYPWIARKILTDSSPQLK 497
Cdd:TIGR01982 391 QLLLLQKTLLTVEGVGRQLDPDLNMWKVAEPFVKRWIRKRLGPKAK 436
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
159-394 7.98e-88

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: 274.88  E-value: 7.98e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920   159 LQDQITPFSTEVAFNMIEDELGLPIDELFSEISPEPVAAASLGQVYQARLRrSGKVVAVKVQRPGVRAAIALDTLILRYI 238
Cdd:pfam03109   2 LQDRAPPFPFEQAKKVIEEELGAPVEEIFAEFDEEPIAAASIAQVHRARLK-DGEEVAVKVQRPGVKKRIRSDLLLLRFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920   239 AGLIKKAGRFNSDLEAVVDEWATSLFKEMDYLNEAQNGIKFRKLYGGIKDVLVPKMYTEYSTSKVLVMEWVEGQKLNEVN 318
Cdd:pfam03109  81 AKVAKRFFPGFRRLDWLVDEFRKSLPQELDFLREAANAEKFRENFADDPDVYVPKVYWELTTERVLTMEYVDGIKIDDLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920   319 DL--------YLVEVGVYCSFNQLLEYGFYHADPHPGNFLRTYDGQLAYLDFGMMGDFRPELRDGFMEACLHLVNRDFKA 390
Cdd:pfam03109 161 ALseagidrkEIARRLVELFLEQIFRDGFFHADPHPGNILVRKDGRIVLLDFGLMGRLDEKFRRLYAELLLALVNRDYKR 240

                  ....
gi 18409920   391 LAKD 394
Cdd:pfam03109 241 VAEM 244
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
74-466 1.82e-64

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 222.86  E-value: 1.82e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920   74 IDGMYKKKPLILLRRLAqigttfsYWFGLRLADEAlersdqmfkvRAAELRKLLVELGPAYVKIAQAVSSRPDLIPPIYL 153
Cdd:PRK04750  23 ILSHRLTRPLRLWRRSL-------FWMPNRHKDKP----------RGERLRLALEELGPIFVKFGQMLSTRRDLFPPDIA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920  154 DELSLLQDQITPFSTEVAFNMIEDELGLPIDELFSEISPEPVAAASLGQVYQARLRRSGKVVAVKVQRPGVRAAIALDTL 233
Cdd:PRK04750  86 DELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQVHFARLKDNGREVVVKVLRPDILPVIDADLA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920  234 ILRYIAGLIKKA---GRFNSDLEaVVDEWATSLFKEMDYLNEAQNGIKFRKLYGGIKDVLVPKMYTEYSTSKVLVMEWVE 310
Cdd:PRK04750 166 LMYRLARWVERLlpdGRRLKPRE-VVAEFEKTLHDELDLMREAANASQLRRNFEDSDMLYVPEVYWDYCSETVMVMERMY 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920  311 GQKLNEVNDL--------YLVEVGVYCSFNQLLEYGFYHADPHPGNFLRTYD----GQLAYLDFGMMGDFRPELRDGFME 378
Cdd:PRK04750 245 GIPVSDVAALraagtdmkLLAERGVEVFFTQVFRDGFFHADMHPGNIFVSYDppenPRYIALDFGIVGSLNKEDKRYLAE 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920  379 ACLHLVNRDFKALAKDFVTLGLLPPTaeksavTKAltDVFQDAIsRGV---------RNISFGDLLGDLGKTMYRFKFRI 449
Cdd:PRK04750 325 NFLAFFNRDYRRVAELHVESGWVPPD------TRV--EELEFAI-RAVcepifdkplAEISFGHVLLRLFNTARRFNVEI 395
                        410
                 ....*....|....*..
gi 18409920  450 PPYFSLVIRSLAVLEGI 466
Cdd:PRK04750 396 QPQLVLLQKTLLNVEGL 412
ABC1_ADCK3 cd13970
Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This ...
154-399 2.34e-62

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: 208.13  E-value: 2.34e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 154 DELSLLQDQITPFSTEVAFNMIEDELGLPIDELFSEISPEPVAAASLGQVYQARLRrSGKVVAVKVQRPGVRAAIA--LD 231
Cdd:cd13970   1 EALARLRDSAPPMPWAQLEKVLEAELGEDWRELFAEFDEEPFAAASIGQVHRATLK-DGREVAVKVQYPGVAESIDsdLN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 232 TL--ILRYIAGLIKKAgrfnsDLEAVVDEWATSLFKEMDYLNEAQNGIKFRKLYGGIKDVLVPKMYTEYSTSKVLVMEWV 309
Cdd:cd13970  80 NLrrLLKLTGLLPKGL-----DLDALIAELREELLEECDYEREAANQRRFRELLADDPRFVVPEVIPELSTKRVLTTEFV 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 310 EGQKLNEVNDL------YLVEVGVYCSFNQLLEYGFYHADPHPGNFL-RTYDGQLAYLDFGMMGDFRPELRDGFMEACLH 382
Cdd:cd13970 155 DGVPLDEAADLsqeernRIGELLLRLCLRELFEFGFMQTDPNPGNFLyDPEDGRLGLLDFGAVREYPPEFVDGYRRLVRA 234
                       250
                ....*....|....*..
gi 18409920 383 LVNRDFKALAKDFVTLG 399
Cdd:cd13970 235 ALEGDREALLEASVELG 251
UbiB cd13972
Ubiquinone biosynthetic protein UbiB; UbiB is the prokaryotic homolog of yeast Abc1p and human ...
159-393 7.74e-59

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: 198.58  E-value: 7.74e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 159 LQDQITPFSTEVAFNMIEDELGLPIDELFSEISPEPVAAASLGQVYQARLrRSGKVVAVKVQRPGVRAAIALDTLILRYI 238
Cdd:cd13972   2 LQDRVPPFSGKEARAIIEAELGKPLDALFSDFDEEPVAAASIAQVHKARL-LDGREVAVKVLRPGIEKRIERDLELLRFL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 239 AGLI----KKAGRFNsdLEAVVDEWATSLFKEMDYLNEAQNGIKFRKLYGGIKDVLVPKMYTEYSTSKVLVMEWVEGQKL 314
Cdd:cd13972  81 ARLAerllPEARRLR--PVEVVKEFARSLLLELDLRLEAANASELRENFLDDPGFYVPEVYWELTSKNVLTMEWIDGIPI 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 315 NEVNDLY--------LVEVGVYCSFNQLLEYGFYHADPHPGNFLRTYDGQLAYLDFGMMGDFRPELRDGFMEACLHLVNR 386
Cdd:cd13972 159 SDIEALDaagidrkaLAERLVEIFFRQVFRDGFFHADMHPGNIFVDPNGRIIAVDFGIMGRLDKKDRRYLAEILYGFLTR 238

                ....*..
gi 18409920 387 DFKALAK 393
Cdd:cd13972 239 DYRRVAE 245
ADCK1-like cd13969
aarF domain containing kinase 1 and similar proteins; This subfamily is composed of ...
159-399 7.75e-57

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: 193.47  E-value: 7.75e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 159 LQDQITPFSTEVAFNMIEDELGLPIDELFSEISPEPVAAASLGQVYQARLRrSGKVVAVKVQRPGVRAAIALDTLILRYI 238
Cdd:cd13969   2 LQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVHKAKLK-DGEEVAVKVQHPDLRKQFAGDLATMEFL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 239 AGLIKKAGrFNSDLEAVVDEWATSLFKEMDYLNEAQNGIKFRKLYGGIKDVLVPKMYTEYSTSKVLVMEWVEGQKLNEVN 318
Cdd:cd13969  81 VNLVEKLF-PDFPFSWLVDELKKNLPKELDFLNEARNAERCAKLFKHRPDVYVPKVYWDLSSKRVLTMEFIDGIKIDDVE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 319 DLY-----LVEVGVYCS--FN-QLLEYGFYHADPHPGNFL-----RTYDGQLAYLDFGMMGDFRPELRdgfMEACL---H 382
Cdd:cd13969 160 ALKklgidPKEVARLLSeaFAeMIFVHGFVHCDPHPGNLLvrknpGPGKPQIVLLDHGLYRELDEEFR---LNYCRlwkA 236
                       250
                ....*....|....*..
gi 18409920 383 LVNRDFKALAKDFVTLG 399
Cdd:cd13969 237 LILGDEKKIKKYSKALG 253
ADCK2-like cd13971
aarF domain containing kinase 2 and similar proteins; This subfamily is composed of ...
159-364 1.25e-30

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: 121.95  E-value: 1.25e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 159 LQDQITPFSTEVAFNMIEDELGLPIDELFSEISPEPVAAASLGQVYQARLR-------RSGKVVAVKVQRPGVRAAIALD 231
Cdd:cd13971   2 LHSNAPPHSWAHTERALEAAFGKDWEDIFEEFDEEPIGSGSIAQVHRAKLKpdyggdgGGPRVVAVKVLHPGVREQIERD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 232 TLILRYIAGLIKKAGRFNSD-LEAVVDEWATSLFKEMDYLNEAQNGIKFRKLYGGIKDVLVPKMYTEYSTSKVLVMEWVE 310
Cdd:cd13971  82 LAILRLFAKLLEAIPPLRWLsLPESVEQFASLMLRQLDLRVEAANLERFRENFKDRKDVSFPKPLYPLVTEEVLVETFEE 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18409920 311 GQKLNEVNDLY--------LVEVGVYCSFNQLLEYGFYHADPHPGNFL-RTYDG----------------QLAYLDFGM 364
Cdd:cd13971 162 GVPISRTVLAHggeplkrkLARIGLDAFLKMLFVDNFVHGDLHPGNILvRFNDSnrpsllvsldargsppRLVFLDAGL 240
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
271-395 8.08e-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: 8.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 271 NEAQNgikFRKLYGgiKDVLVPKMYTEYSTSKVLVMEWVEGQKLNEV------NDLYLVEVGVYcsFNQLLEYGFYHADP 344
Cdd:COG3642   5 REARL---LRELRE--AGVPVPKVLDVDPDDADLVMEYIEGETLADLleegelPPELLRELGRL--LARLHRAGIVHGDL 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 18409920 345 HPGNFLRTyDGQLAYLDFGmMGDFRPELRDgfMEACLHLVNRDFKALAKDF 395
Cdd:COG3642  78 TTSNILVD-DGGVYLIDFG-LARYSDPLED--KAVDLAVLKRSLESTHPDP 124
PRK14879 PRK14879
Kae1-associated kinase Bud32;
271-395 2.77e-05

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 45.67  E-value: 2.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920  271 NEAQNGIKFRKLygGIKdvlVPKMYTEYSTSKVLVMEWVEGQKLNEVND-------LYLVEVGVYcsFNQLLEYGFYHAD 343
Cdd:PRK14879  48 REARIMSRARKA--GVN---VPAVYFVDPENFIIVMEYIEGEPLKDLINsngmeelELSREIGRL--VGKLHSAGIIHGD 120
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18409920  344 PHPGNFLRTyDGQLAYLDFGmMGDFRPELRDgfMEACLHLVNRDFKALAKDF 395
Cdd:PRK14879 121 LTTSNMILS-GGKIYLIDFG-LAEFSKDLED--RAVDLHVLLRSLESTHPDW 168
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
285-363 3.17e-05

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: 44.36  E-value: 3.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 285 GIKDVLVPKMYTEYSTS--KVLVMEWVEGQKLNE-VNDLYLVEVGVYCSFNQLLEY-------GFYHADPHPGNFLRTYD 354
Cdd:cd13968  48 KGLELNIPKVLVTEDVDgpNILLMELVKGGTLIAyTQEEELDEKDVESIMYQLAECmrllhsfHLIHRDLNNDNILLSED 127

                ....*....
gi 18409920 355 GQLAYLDFG 363
Cdd:cd13968 128 GNVKLIDFG 136
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
302-395 5.52e-04

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


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 41.81  E-value: 5.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920   302 KVLVMEWVEGQKLNEV----NDLYLVEVGVycSFNQLLEYGFYHADPHPGNFLRTyDGQLAYLDFGmMGDFRPELRDGFM 377
Cdd:TIGR03724  72 KTIVMEYIEGKPLKDVieenGDELAREIGR--LVGKLHKAGIVHGDLTTSNIIVR-DDKVYLIDFG-LGKYSDEIEDKAV 147
                          90
                  ....*....|....*...
gi 18409920   378 EacLHLVNRDFKALAKDF 395
Cdd:TIGR03724 148 D--LHVLKRSLESTHPDK 163
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
193-363 1.50e-03

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 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: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 41.08  E-value: 1.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 193 EPVAAASLGQVYQARLRRSGKVVAVKVqrpgvraaialdtlilryiaglIKKAGRFNSDLeavvdewaTSLFKEMDYLne 272
Cdd:cd14002   7 ELIGEGSFGKVYKGRRKYTGQVVALKF----------------------IPKRGKSEKEL--------RNLRQEIEIL-- 54
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 273 aqngikfRKLyggiKDVLVPKMYTEYSTSK--VLVMEWVEGQkLNEV--NDLYLVEVGVYCSFNQLLEYGFY-------H 341
Cdd:cd14002  55 -------RKL----NHPNIIEMLDSFETKKefVVVTEYAQGE-LFQIleDDGTLPEEEVRSIAKQLVSALHYlhsnriiH 122
                       170       180
                ....*....|....*....|..
gi 18409920 342 ADPHPGNFLRTYDGQLAYLDFG 363
Cdd:cd14002 123 RDMKPQNILIGKGGVVKLCDFG 144
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
302-398 3.67e-03

bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 40.26  E-value: 3.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920  302 KVLVMEWVEGQKLNEV---NDLYLVEVGVYCSfnQLLEYGFYHADPHPGNFLRTyDGQLAYLDFGmMGDFRPELRDGFME 378
Cdd:PRK09605 411 KTIVMEYIGGKDLKDVlegNPELVRKVGEIVA--KLHKAGIVHGDLTTSNFIVR-DDRLYLIDFG-LGKYSDLIEDKAVD 486
                         90       100
                 ....*....|....*....|
gi 18409920  379 acLHLVNRDFKALAKDFVTL 398
Cdd:PRK09605 487 --LHVLKQSLESTHYDFEEL 504
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
199-402 8.38e-03

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK 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: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 38.69  E-value: 8.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 199 SLGQVYQARLRRSGKVVAVKVqrpgvraaiaLDTLILRYIAGLIKKAGRFNSDLEAVVDEWAtsLFKEMDYLNEAqngik 278
Cdd:cd14008   5 SFGKVKLALDTETGQLYAIKI----------FNKSRLRKRREGKNDRGKIKNALDDVRREIA--IMKKLDHPNIV----- 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409920 279 frKLYGGIKDVLVPKMYteystskvLVMEWVEGQKLNEVNDLY----LVEVGVYCSFNQL---LEY----GFYHADPHPG 347
Cdd:cd14008  68 --RLYEVIDDPESDKLY--------LVLEYCEGGPVMELDSGDrvppLPEETARKYFRDLvlgLEYlhenGIVHRDIKPE 137
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18409920 348 NFLRTYDGQLAYLDFG---MMGDFRPELRD--G---FM--EACLHLvNRDFKALAKDF----VTL-----GLLP 402
Cdd:cd14008 138 NLLLTADGTVKISDFGvseMFEDGNDTLQKtaGtpaFLapELCDGD-SKTYSGKAADIwalgVTLyclvfGRLP 210
 
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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