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Conserved domains on  [gi|18412437|ref|NP_565214|]
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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 ...
 109-554 1.59e-154

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: 456.59  E-value: 1.59e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 109 PFKALRRSLEILGALGGFALKLGIDQK-----------QGNLEKNMKKRAIELRRIFTRLGPTFVKLGQGLSTRPDLCPP 177
Cdd:COG0661   3 ALRRLRRLARIARVLLRYGLGELLDRLglprlrrlltgEERREELRRRRAERLRLALEELGPTFIKLGQLLSTRPDLLPP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 178 DYLEELAELQDALPTFPDAEAFACIERELDLSLETIFSSVSPEPIAAASLGQVYKAQLRySGQVVAVKVQRPGIEEAIGL 257
Cdd:COG0661  83 EYAEELAKLQDRVPPFPFEEVRAVIEEELGRPLEELFAEFDPEPLAAASIGQVHRARLK-DGREVAVKVQRPGIEEAIEA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 258 DFYLIRGVGKLINKYV-DFITTDVLTLIDEFACRVYQELNYVQEAQNARRFKKLYADKADVLVPDIFWDYTSRKVLTMEW 336
Cdd:COG0661 162 DLRILRRLARLLERLSpEGRRLDPVEVVDEFARSLLEELDYRREAANAERFRRNFADDPDVYVPKVYWELSTRRVLTMEW 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 337 VEGTKLNEQLAIESQGLKVLDLVNTGIQCSLRQLLEYGFFHADPHPGNLLATPDGKLAFLDFGMMSETPEEARFAIIGHV 416
Cdd:COG0661 242 IDGIKISDLEALDAAGIDRKRLAERLVRAFLRQVFRDGFFHADPHPGNIFVLPDGRLVLLDFGMVGRLDPETREGLAELL 321

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 417 VHLVNRDYEAMARDYYALKFLSPDVDVTPIIPALRDFFDDALNYTVSELNFKTLVDGLGAVFYQYPFNVPPYYALILRSL 496
Cdd:COG0661 322 LALLNRDYDRVAEALLELGFVPPDTDVDELERALRAVLEPYFGKPLKDISFGELLLELFELARRFPLRLPPELVLLQRTL 401

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18412437 497 TVLEGLALYADPNFKVLAASYPYFAKRLLTDPNP-----YLRDALIELLfKDGKFRWNRLENL 554
Cdd:COG0661 402 LTLEGVGRQLDPDFDLWEVAKPFLERLLRERLGPrallkRLKREAPELA-ELLPRLPRLLERA 463
 
Name Accession Description Interval E-value
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
 109-554 1.59e-154

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: 456.59  E-value: 1.59e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 109 PFKALRRSLEILGALGGFALKLGIDQK-----------QGNLEKNMKKRAIELRRIFTRLGPTFVKLGQGLSTRPDLCPP 177
Cdd:COG0661   3 ALRRLRRLARIARVLLRYGLGELLDRLglprlrrlltgEERREELRRRRAERLRLALEELGPTFIKLGQLLSTRPDLLPP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 178 DYLEELAELQDALPTFPDAEAFACIERELDLSLETIFSSVSPEPIAAASLGQVYKAQLRySGQVVAVKVQRPGIEEAIGL 257
Cdd:COG0661  83 EYAEELAKLQDRVPPFPFEEVRAVIEEELGRPLEELFAEFDPEPLAAASIGQVHRARLK-DGREVAVKVQRPGIEEAIEA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 258 DFYLIRGVGKLINKYV-DFITTDVLTLIDEFACRVYQELNYVQEAQNARRFKKLYADKADVLVPDIFWDYTSRKVLTMEW 336
Cdd:COG0661 162 DLRILRRLARLLERLSpEGRRLDPVEVVDEFARSLLEELDYRREAANAERFRRNFADDPDVYVPKVYWELSTRRVLTMEW 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 337 VEGTKLNEQLAIESQGLKVLDLVNTGIQCSLRQLLEYGFFHADPHPGNLLATPDGKLAFLDFGMMSETPEEARFAIIGHV 416
Cdd:COG0661 242 IDGIKISDLEALDAAGIDRKRLAERLVRAFLRQVFRDGFFHADPHPGNIFVLPDGRLVLLDFGMVGRLDPETREGLAELL 321

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 417 VHLVNRDYEAMARDYYALKFLSPDVDVTPIIPALRDFFDDALNYTVSELNFKTLVDGLGAVFYQYPFNVPPYYALILRSL 496
Cdd:COG0661 322 LALLNRDYDRVAEALLELGFVPPDTDVDELERALRAVLEPYFGKPLKDISFGELLLELFELARRFPLRLPPELVLLQRTL 401

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18412437 497 TVLEGLALYADPNFKVLAASYPYFAKRLLTDPNP-----YLRDALIELLfKDGKFRWNRLENL 554
Cdd:COG0661 402 LTLEGVGRQLDPDFDLWEVAKPFLERLLRERLGPrallkRLKREAPELA-ELLPRLPRLLERA 463
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
 186-429 4.65e-103

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: 315.20  E-value: 4.65e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 186 LQDALPTFPDAEAFACIERELDLSLETIFSSVSPEPIAAASLGQVYKAQLRySGQVVAVKVQRPGIEEAIGLDFYLIRGV 265
Cdd:cd05121   2 LQDDVPPFPFEEVRKIIEEELGRPLEEVFAEFDPEPLAAASIAQVHRARLK-DGREVAVKVQRPGIEEIIEADLRILRRL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 266 GKLINKYVDFIT-TDVLTLIDEFACRVYQELNYVQEAQNARRFKKLYADKADVLVPDIFWDYTSRKVLTMEWVEGTKLNE 344
Cdd:cd05121  81 ARLLERLSPLLRrLDLVAIVDEFARSLLEELDFRREARNAERFRKNLKDSPDVYVPKVYPELSTRRVLVMEYIDGVKLTD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 345 QLAIESQGLKVLDLVNTGIQCSLRQLLEYGFFHADPHPGNLLATPDGKLAFLDFGMMSETPEEARFAIIGHVVHLVNRDY 424
Cdd:cd05121 161 LEALRAAGIDRKELARRLVDAYLKQIFEDGFFHADPHPGNILVLPDGRIALLDFGMVGRLDPETREALADLLLALVNGDA 240


                ....*
gi 18412437 425 EAMAR 429
Cdd:cd05121 241 EGLAE 245
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
 138-525 7.76e-101

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: 316.55  E-value: 7.76e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437   138 NLEKNMKKRAIELRRIFTRLGPTFVKLGQGLSTRPDLCPPDYLEELAELQDALPTFPDAEAFACIERELDLSLETIFSSV 217
Cdd:TIGR01982  41 NRENRLMSRGERLRLALEELGPTFIKFGQTLSTRADLLPADIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEF 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437   218 SPEPIAAASLGQVYKAQLrYSGQVVAVKVQRPGIEEAIGLDFYLIRGVGKLINKYV-DFITTDVLTLIDEFACRVYQELN 296
Cdd:TIGR01982 121 EEKPLAAASIAQVHRARL-VDGKEVAVKVLRPGIEKTIAADIALLYRLARIVERLSpDSRRLRPTEVVKEFEKTLRRELD 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437   297 YVQEAQNARRFKKLYADKADVLVPDIFWDYTSRKVLTMEWVEGTKLNEQLAIESQGLKVLDLVNTGIQCSLRQLLEYGFF 376
Cdd:TIGR01982 200 LRREAANASELGENFKNDPGVYVPEVYWDRTSERVLTMEWIDGIPLSDIAALDEAGLDRKALAENLARSFLNQVLRDGFF 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437   377 HADPHPGNLLATPDGKLAFLDFGMMSETPEEARFAIIGHVVHLVNRDYEAMARDYYALKFLSPDVDVTPIIPALRDFFDD 456
Cdd:TIGR01982 280 HADLHPGNIFVLKDGKIIALDFGIVGRLSEEDRRYLAEILYGFLNRDYRRVAEVHFDAGYVPSDTDMAEFEQAIRAIGEP 359

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18412437   457 ALNYTVSELNFKTLVDGLGAVFYQYPFNVPPYYALILRSLTVLEGLALYADPNFKVLAASYPyFAKRLL 525
Cdd:TIGR01982 360 IFGQPLKEISVGRLLAGLFKITRDFNMELQPQLLLLQKTLLTVEGVGRQLDPDLNMWKVAEP-FVKRWI 427
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
 186-431 6.74e-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: 275.65  E-value: 6.74e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437   186 LQDALPTFPDAEAFACIERELDLSLETIFSSVSPEPIAAASLGQVYKAQLRySGQVVAVKVQRPGIEEAIGLDFYLIRGV 265
Cdd:pfam03109   2 LQDRAPPFPFEQAKKVIEEELGAPVEEIFAEFDEEPIAAASIAQVHRARLK-DGEEVAVKVQRPGVKKRIRSDLLLLRFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437   266 GKLINKYV-DFITTDvlTLIDEFACRVYQELNYVQEAQNARRFKKLYADKADVLVPDIFWDYTSRKVLTMEWVEGTKLNE 344
Cdd:pfam03109  81 AKVAKRFFpGFRRLD--WLVDEFRKSLPQELDFLREAANAEKFRENFADDPDVYVPKVYWELTTERVLTMEYVDGIKIDD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437   345 QLAIESQGLKVLDLVNTGIQCSLRQLLEYGFFHADPHPGNLLATPDGKLAFLDFGMMSETPEEARFAIIGHVVHLVNRDY 424
Cdd:pfam03109 159 LDALSEAGIDRKEIARRLVELFLEQIFRDGFFHADPHPGNILVRKDGRIVLLDFGLMGRLDEKFRRLYAELLLALVNRDY 238


                  ....*..
gi 18412437   425 EAMARDY 431
Cdd:pfam03109 239 KRVAEML 245
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
 144-401 4.06e-58

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 205.91  E-value: 4.06e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437  144 KKRAIELRRIFTRLGPTFVKLGQGLSTRPDLCPPDYLEELAELQDALPTFPDAEAFACIERELDLSLETIFSSVSPEPIA 223
Cdd:PRK04750  49 KPRGERLRLALEELGPIFVKFGQMLSTRRDLFPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLA 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437  224 AASLGQVYKAQLRYSGQVVAVKVQRPGIEEAIGLDFYLIRGVGKLinkyVDFITTDVLTL-----IDEFACRVYQELNYV 298
Cdd:PRK04750 129 SASIAQVHFARLKDNGREVVVKVLRPDILPVIDADLALMYRLARW----VERLLPDGRRLkprevVAEFEKTLHDELDLM 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437  299 QEAQNARRFKKLYADKADVLVPDIFWDYTSRKVLTMEWVEGTKLNEQLAIESQGLKVLDLVNTGIQCSLRQLLEYGFFHA 378
Cdd:PRK04750 205 REAANASQLRRNFEDSDMLYVPEVYWDYCSETVMVMERMYGIPVSDVAALRAAGTDMKLLAERGVEVFFTQVFRDGFFHA 284

                        250       260
                 ....*....|....*....|....*..
gi 18412437  379 DPHPGNLLATPDGKLAF----LDFGMM 401
Cdd:PRK04750 285 DMHPGNIFVSYDPPENPryiaLDFGIV 311
 
Name Accession Description Interval E-value
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
 109-554 1.59e-154

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: 456.59  E-value: 1.59e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 109 PFKALRRSLEILGALGGFALKLGIDQK-----------QGNLEKNMKKRAIELRRIFTRLGPTFVKLGQGLSTRPDLCPP 177
Cdd:COG0661   3 ALRRLRRLARIARVLLRYGLGELLDRLglprlrrlltgEERREELRRRRAERLRLALEELGPTFIKLGQLLSTRPDLLPP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 178 DYLEELAELQDALPTFPDAEAFACIERELDLSLETIFSSVSPEPIAAASLGQVYKAQLRySGQVVAVKVQRPGIEEAIGL 257
Cdd:COG0661  83 EYAEELAKLQDRVPPFPFEEVRAVIEEELGRPLEELFAEFDPEPLAAASIGQVHRARLK-DGREVAVKVQRPGIEEAIEA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 258 DFYLIRGVGKLINKYV-DFITTDVLTLIDEFACRVYQELNYVQEAQNARRFKKLYADKADVLVPDIFWDYTSRKVLTMEW 336
Cdd:COG0661 162 DLRILRRLARLLERLSpEGRRLDPVEVVDEFARSLLEELDYRREAANAERFRRNFADDPDVYVPKVYWELSTRRVLTMEW 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 337 VEGTKLNEQLAIESQGLKVLDLVNTGIQCSLRQLLEYGFFHADPHPGNLLATPDGKLAFLDFGMMSETPEEARFAIIGHV 416
Cdd:COG0661 242 IDGIKISDLEALDAAGIDRKRLAERLVRAFLRQVFRDGFFHADPHPGNIFVLPDGRLVLLDFGMVGRLDPETREGLAELL 321

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 417 VHLVNRDYEAMARDYYALKFLSPDVDVTPIIPALRDFFDDALNYTVSELNFKTLVDGLGAVFYQYPFNVPPYYALILRSL 496
Cdd:COG0661 322 LALLNRDYDRVAEALLELGFVPPDTDVDELERALRAVLEPYFGKPLKDISFGELLLELFELARRFPLRLPPELVLLQRTL 401

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18412437 497 TVLEGLALYADPNFKVLAASYPYFAKRLLTDPNP-----YLRDALIELLfKDGKFRWNRLENL 554
Cdd:COG0661 402 LTLEGVGRQLDPDFDLWEVAKPFLERLLRERLGPrallkRLKREAPELA-ELLPRLPRLLERA 463
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
 186-429 4.65e-103

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: 315.20  E-value: 4.65e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 186 LQDALPTFPDAEAFACIERELDLSLETIFSSVSPEPIAAASLGQVYKAQLRySGQVVAVKVQRPGIEEAIGLDFYLIRGV 265
Cdd:cd05121   2 LQDDVPPFPFEEVRKIIEEELGRPLEEVFAEFDPEPLAAASIAQVHRARLK-DGREVAVKVQRPGIEEIIEADLRILRRL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 266 GKLINKYVDFIT-TDVLTLIDEFACRVYQELNYVQEAQNARRFKKLYADKADVLVPDIFWDYTSRKVLTMEWVEGTKLNE 344
Cdd:cd05121  81 ARLLERLSPLLRrLDLVAIVDEFARSLLEELDFRREARNAERFRKNLKDSPDVYVPKVYPELSTRRVLVMEYIDGVKLTD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 345 QLAIESQGLKVLDLVNTGIQCSLRQLLEYGFFHADPHPGNLLATPDGKLAFLDFGMMSETPEEARFAIIGHVVHLVNRDY 424
Cdd:cd05121 161 LEALRAAGIDRKELARRLVDAYLKQIFEDGFFHADPHPGNILVLPDGRIALLDFGMVGRLDPETREALADLLLALVNGDA 240


                ....*
gi 18412437 425 EAMAR 429
Cdd:cd05121 241 EGLAE 245
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
 138-525 7.76e-101

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: 316.55  E-value: 7.76e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437   138 NLEKNMKKRAIELRRIFTRLGPTFVKLGQGLSTRPDLCPPDYLEELAELQDALPTFPDAEAFACIERELDLSLETIFSSV 217
Cdd:TIGR01982  41 NRENRLMSRGERLRLALEELGPTFIKFGQTLSTRADLLPADIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEF 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437   218 SPEPIAAASLGQVYKAQLrYSGQVVAVKVQRPGIEEAIGLDFYLIRGVGKLINKYV-DFITTDVLTLIDEFACRVYQELN 296
Cdd:TIGR01982 121 EEKPLAAASIAQVHRARL-VDGKEVAVKVLRPGIEKTIAADIALLYRLARIVERLSpDSRRLRPTEVVKEFEKTLRRELD 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437   297 YVQEAQNARRFKKLYADKADVLVPDIFWDYTSRKVLTMEWVEGTKLNEQLAIESQGLKVLDLVNTGIQCSLRQLLEYGFF 376
Cdd:TIGR01982 200 LRREAANASELGENFKNDPGVYVPEVYWDRTSERVLTMEWIDGIPLSDIAALDEAGLDRKALAENLARSFLNQVLRDGFF 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437   377 HADPHPGNLLATPDGKLAFLDFGMMSETPEEARFAIIGHVVHLVNRDYEAMARDYYALKFLSPDVDVTPIIPALRDFFDD 456
Cdd:TIGR01982 280 HADLHPGNIFVLKDGKIIALDFGIVGRLSEEDRRYLAEILYGFLNRDYRRVAEVHFDAGYVPSDTDMAEFEQAIRAIGEP 359

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18412437   457 ALNYTVSELNFKTLVDGLGAVFYQYPFNVPPYYALILRSLTVLEGLALYADPNFKVLAASYPyFAKRLL 525
Cdd:TIGR01982 360 IFGQPLKEISVGRLLAGLFKITRDFNMELQPQLLLLQKTLLTVEGVGRQLDPDLNMWKVAEP-FVKRWI 427
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
 186-431 6.74e-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: 275.65  E-value: 6.74e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437   186 LQDALPTFPDAEAFACIERELDLSLETIFSSVSPEPIAAASLGQVYKAQLRySGQVVAVKVQRPGIEEAIGLDFYLIRGV 265
Cdd:pfam03109   2 LQDRAPPFPFEQAKKVIEEELGAPVEEIFAEFDEEPIAAASIAQVHRARLK-DGEEVAVKVQRPGVKKRIRSDLLLLRFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437   266 GKLINKYV-DFITTDvlTLIDEFACRVYQELNYVQEAQNARRFKKLYADKADVLVPDIFWDYTSRKVLTMEWVEGTKLNE 344
Cdd:pfam03109  81 AKVAKRFFpGFRRLD--WLVDEFRKSLPQELDFLREAANAEKFRENFADDPDVYVPKVYWELTTERVLTMEYVDGIKIDD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437   345 QLAIESQGLKVLDLVNTGIQCSLRQLLEYGFFHADPHPGNLLATPDGKLAFLDFGMMSETPEEARFAIIGHVVHLVNRDY 424
Cdd:pfam03109 159 LDALSEAGIDRKEIARRLVELFLEQIFRDGFFHADPHPGNILVRKDGRIVLLDFGLMGRLDEKFRRLYAELLLALVNRDY 238


                  ....*..
gi 18412437   425 EAMARDY 431
Cdd:pfam03109 239 KRVAEML 245
UbiB cd13972
Ubiquinone biosynthetic protein UbiB; UbiB is the prokaryotic homolog of yeast Abc1p and human ...
 186-429 6.45e-64

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: 212.45  E-value: 6.45e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 186 LQDALPTFPDAEAFACIERELDLSLETIFSSVSPEPIAAASLGQVYKAQLRySGQVVAVKVQRPGIEEAIGLDFYLIRGV 265
Cdd:cd13972   2 LQDRVPPFSGKEARAIIEAELGKPLDALFSDFDEEPVAAASIAQVHKARLL-DGREVAVKVLRPGIEKRIERDLELLRFL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 266 GKLINKYV-DFITTDVLTLIDEFACRVYQELNYVQEAQNARRFKKLYADKADVLVPDIFWDYTSRKVLTMEWVEGTKLNE 344
Cdd:cd13972  81 ARLAERLLpEARRLRPVEVVKEFARSLLLELDLRLEAANASELRENFLDDPGFYVPEVYWELTSKNVLTMEWIDGIPISD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 345 QLAIESQGLKVLDLVNTGIQCSLRQLLEYGFFHADPHPGNLLATPDGKLAFLDFGMMSETPEEARFAIIGHVVHLVNRDY 424
Cdd:cd13972 161 IEALDAAGIDRKALAERLVEIFFRQVFRDGFFHADMHPGNIFVDPNGRIIAVDFGIMGRLDKKDRRYLAEILYGFLTRDY 240


                ....*
gi 18412437 425 EAMAR 429
Cdd:cd13972 241 RRVAE 245
ADCK1-like cd13969
aarF domain containing kinase 1 and similar proteins; This subfamily is composed of ...
 185-409 1.47e-59

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


Pssm-ID: 270871 [Multi-domain]  Cd Length: 253  Bit Score: 201.18  E-value: 1.47e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 185 ELQDALPTFPDAEAFACIERELDLSLETIFSSVSPEPIAAASLGQVYKAQLRySGQVVAVKVQRPGIEEAIGLDFYLIRG 264
Cdd:cd13969   1 VLQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVHKAKLK-DGEEVAVKVQHPDLRKQFAGDLATMEF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 265 VGKLINKYV-DFittDVLTLIDEFACRVYQELNYVQEAQNARRFKKLYADKADVLVPDIFWDYTSRKVLTMEWVEGTKLN 343
Cdd:cd13969  80 LVNLVEKLFpDF---PFSWLVDELKKNLPKELDFLNEARNAERCAKLFKHRPDVYVPKVYWDLSSKRVLTMEFIDGIKID 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18412437 344 EQLAIESQGLKVLDLVNTGIQCSLRQLLEYGFFHADPHPGNLLATPDGK-----LAFLDFGMMSETPEEAR 409
Cdd:cd13969 157 DVEALKKLGIDPKEVARLLSEAFAEMIFVHGFVHCDPHPGNLLVRKNPGpgkpqIVLLDHGLYRELDEEFR 227
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
 144-401 4.06e-58

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 205.91  E-value: 4.06e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437  144 KKRAIELRRIFTRLGPTFVKLGQGLSTRPDLCPPDYLEELAELQDALPTFPDAEAFACIERELDLSLETIFSSVSPEPIA 223
Cdd:PRK04750  49 KPRGERLRLALEELGPIFVKFGQMLSTRRDLFPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLA 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437  224 AASLGQVYKAQLRYSGQVVAVKVQRPGIEEAIGLDFYLIRGVGKLinkyVDFITTDVLTL-----IDEFACRVYQELNYV 298
Cdd:PRK04750 129 SASIAQVHFARLKDNGREVVVKVLRPDILPVIDADLALMYRLARW----VERLLPDGRRLkprevVAEFEKTLHDELDLM 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437  299 QEAQNARRFKKLYADKADVLVPDIFWDYTSRKVLTMEWVEGTKLNEQLAIESQGLKVLDLVNTGIQCSLRQLLEYGFFHA 378
Cdd:PRK04750 205 REAANASQLRRNFEDSDMLYVPEVYWDYCSETVMVMERMYGIPVSDVAALRAAGTDMKLLAERGVEVFFTQVFRDGFFHA 284

                        250       260
                 ....*....|....*....|....*..
gi 18412437  379 DPHPGNLLATPDGKLAF----LDFGMM 401
Cdd:PRK04750 285 DMHPGNIFVSYDPPENPryiaLDFGIV 311
ABC1_ADCK3 cd13970
Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This ...
 181-435 2.41e-56

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: 192.34  E-value: 2.41e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 181 EELAELQDALPTFPDAEAFACIERELDLSLETIFSSVSPEPIAAASLGQVYKAQLRySGQVVAVKVQRPGIEEAIGLDfy 260
Cdd:cd13970   1 EALARLRDSAPPMPWAQLEKVLEAELGEDWRELFAEFDEEPFAAASIGQVHRATLK-DGREVAVKVQYPGVAESIDSD-- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 261 lIRGVgKLINKYVDFI--TTDVLTLIDEFACRVYQELNYVQEAQNARRFKKLYADKADVLVPDIFWDYTSRKVLTMEWVE 338
Cdd:cd13970  78 -LNNL-RRLLKLTGLLpkGLDLDALIAELREELLEECDYEREAANQRRFRELLADDPRFVVPEVIPELSTKRVLTTEFVD 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 339 GTKLnEQLAIESQ------GLKVLDLVntgiqcsLRQLLEYGFFHADPHPGNLLATP-DGKLAFLDFGMMSETPEEARFA 411
Cdd:cd13970 156 GVPL-DEAADLSQeernriGELLLRLC-------LRELFEFGFMQTDPNPGNFLYDPeDGRLGLLDFGAVREYPPEFVDG 227

                       250       260
                ....*....|....*....|....
gi 18412437 412 IIGHVVHLVNRDYEAMARDYYALK 435
Cdd:cd13970 228 YRRLVRAALEGDREALLEASVELG 251
ADCK2-like cd13971
aarF domain containing kinase 2 and similar proteins; This subfamily is composed of ...
 185-423 2.02e-34

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


Pssm-ID: 270873 [Multi-domain]  Cd Length: 298  Bit Score: 133.12  E-value: 2.02e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 185 ELQDALPTFPDAEAFACIERELDLSLETIFSSVSPEPIAAASLGQVYKAQLRYS-------GQVVAVKVQRPGIEEAIGL 257
Cdd:cd13971   1 KLHSNAPPHSWAHTERALEAAFGKDWEDIFEEFDEEPIGSGSIAQVHRAKLKPDyggdgggPRVVAVKVLHPGVREQIER 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 258 DFYLIRGVGKLINKyvdFITTDVLTL---IDEFACRVYQELNYVQEAQNARRFKKLYADKADVLVPDIFWDYTSRKVLTM 334
Cdd:cd13971  81 DLAILRLFAKLLEA---IPPLRWLSLpesVEQFASLMLRQLDLRVEAANLERFRENFKDRKDVSFPKPLYPLVTEEVLVE 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 335 EWVEGTKLNEQLAIESQGLKVLDLVNTGIQCSLRQLLEYGFFHADPHPGNLLATPDGKLAFLDFGMMSETPEEARFAII- 413
Cdd:cd13971 158 TFEEGVPISRTVLAHGGEPLKRKLARIGLDAFLKMLFVDNFVHGDLHPGNILVRFNDSNRPSLLVSLDARGSPPRLVFLd 237

                       250
                ....*....|.
gi 18412437 414 -GHVVHLVNRD 423
Cdd:cd13971 238 aGLVTELSPQD 248
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 304-411 1.73e-08

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: 54.19  E-value: 1.73e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 304 ARRFKKLYadKADVLVPDIFWDYTSRKVLTMEWVEGTKLNEqlAIESQGLKVLDLVNTGIQcsLRQLLEYGFFHADPHPG 383
Cdd:COG3642   7 ARLLRELR--EAGVPVPKVLDVDPDDADLVMEYIEGETLAD--LLEEGELPPELLRELGRL--LARLHRAGIVHGDLTTS 80

                        90       100
                ....*....|....*....|....*...
gi 18412437 384 NLLATpDGKLAFLDFGMMSETPEEARFA 411
Cdd:COG3642  81 NILVD-DGGVYLIDFGLARYSDPLEDKA 107
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
 220-399 1.21e-05

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


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 47.58  E-value: 1.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 220 EPIAAASLGQVYKAQLRYSGQVVAVKVQRPGIEEaigldfylirgvgklinkyvdfittdvltliDEFACRVYQelnyvQ 299
Cdd:cd14014   6 RLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAE-------------------------------DEEFRERFL-----R 49

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 300 EAQNARRFK-----KLYadkaDVLV-PDIFWdytsrkvLTMEWVEGTKLNEQLAiESQGLKVLDLVNTGIQ-CS-LRQLL 371
Cdd:cd14014  50 EARALARLShpnivRVY----DVGEdDGRPY-------IVMEYVEGGSLADLLR-ERGPLPPREALRILAQiADaLAAAH 117

                       170       180
                ....*....|....*....|....*...
gi 18412437 372 EYGFFHADPHPGNLLATPDGKLAFLDFG 399
Cdd:cd14014 118 RAGIVHRDIKPANILLTEDGRVKLTDFG 145
PRK14879 PRK14879
Kae1-associated kinase Bud32;
312-407 1.55e-05

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 46.44  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437  312 ADKADVLVPDIFWDYTSRKVLTMEWVEGTKLNEqlAIESQGLKVLDLVNT-GIQCSLrqLLEYGFFHADPHPGNLLATpD 390
Cdd:PRK14879  56 ARKAGVNVPAVYFVDPENFIIVMEYIEGEPLKD--LINSNGMEELELSREiGRLVGK--LHSAGIIHGDLTTSNMILS-G 130

                         90
                 ....*....|....*....
gi 18412437  391 GKLAFLDFGM--MSETPEE 407
Cdd:PRK14879 131 GKIYLIDFGLaeFSKDLED 149
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
 330-399 1.83e-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: 44.74  E-value: 1.83e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18412437 330 KVLTMEWVEGTKLNEQLAIESqgLKVLDLVNTGIQCS--LRQLLEYGFFHADPHPGNLLATPDGKLAFLDFG 399
Cdd:cd13968  67 NILLMELVKGGTLIAYTQEEE--LDEKDVESIMYQLAecMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
 311-400 3.53e-05

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: 45.28  E-value: 3.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437   311 YADKADVLVPDIFWDYTSRKVLTMEWVEGTKLNEqlAIESQGLKVldLVNTGIQcsLRQLLEYGFFHADPHPGNLLATpD 390
Cdd:TIGR03724  53 RARKAGVNTPVIYDVDPDNKTIVMEYIEGKPLKD--VIEENGDEL--AREIGRL--VGKLHKAGIVHGDLTTSNIIVR-D 125

                          90
                  ....*....|
gi 18412437   391 GKLAFLDFGM 400
Cdd:TIGR03724 126 DKVYLIDFGL 135
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
 285-417 4.35e-05

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma 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: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 46.10  E-value: 4.35e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 285 DEFACRVYQELNYVQEAQNARRFKKLyadkaDVLVPDIFWDYTSRKVLTMEWVeGTKLNEQLAIESQGLKVLDLVNTGIQ 364
Cdd:cd07880  55 ELFAKRAYRELRLLKHMKHENVIGLL-----DVFTPDLSLDRFHDFYLVMPFM-GTDLGKLMKHEKLSEDRIQFLVYQML 128

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 18412437 365 CSLRQLLEYGFFHADPHPGNLLATPDGKLAFLDFGMMSETPEEarfaIIGHVV 417
Cdd:cd07880 129 KGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQTDSE----MTGYVV 177
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 314-418 2.45e-04

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: 42.29  E-value: 2.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 314 KADVLVPDIFWDYTS--RKVLTMEWVEGTKLNEQ---LAIESQGLKVLDLVNTGIQcsLRQLLEYGFFHADPHPGNLLAT 388
Cdd:cd05120  49 KLSLPVPKVYGFGESdgWEYLLMERIEGETLSEVwprLSEEEKEKIADQLAEILAA--LHRIDSSVLTHGDLHPGNILVK 126

                        90       100       110
                ....*....|....*....|....*....|.
gi 18412437 389 PDGKL-AFLDFGMMSETPEEARFAIIGHVVH 418
Cdd:cd05120 127 PDGKLsGIIDWEFAGYGPPAFDYAAALRDWT 157
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
220-399 1.18e-03

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 41.92  E-value: 1.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 220 EPIAAASLGQVYKAQLRYSGQVVAVKVQRPGIEEAigldfylirgvgklinkyvdfittdvLTLIDEFacrvyqelnyVQ 299
Cdd:COG0515  13 RLLGRGGMGVVYLARDLRLGRPVALKVLRPELAAD--------------------------PEARERF----------RR 56

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 300 EAQNARRFK-----KLYAdkadvlvpdiFWDYTSRKVLTMEWVEGTKLNEQLAiESQGLKVLDLVNTGIQ-CS-LRQLLE 372
Cdd:COG0515  57 EARALARLNhpnivRVYD----------VGEEDGRPYLVMEYVEGESLADLLR-RRGPLPPAEALRILAQlAEaLAAAHA 125

                       170       180
                ....*....|....*....|....*..
gi 18412437 373 YGFFHADPHPGNLLATPDGKLAFLDFG 399
Cdd:COG0515 126 AGIVHRDIKPANILLTPDGRVKLIDFG 152
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
 376-402 3.23e-03

Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and Choline kinase; This subfamily is composed of uncharacterized bacterial proteins with similarity to APH and ChoK. Other APH/ChoK-like proteins include 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). These proteins 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-like subfamily 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: 270704 [Multi-domain]  Cd Length: 234  Bit Score: 39.91  E-value: 3.23e-03
                        10        20
                ....*....|....*....|....*...
gi 18412437 376 FHADPHPGNLLATpDGKL-AFLDFGMMS 402
Cdd:cd05155 166 LHGDLHPGNLLVR-DGRLsAVIDFGDLG 192
PRK10359 PRK10359
lipopolysaccharide core heptose(II) kinase RfaY;
326-391 3.34e-03

lipopolysaccharide core heptose(II) kinase RfaY;


Pssm-ID: 182407  Cd Length: 232  Bit Score: 39.74  E-value: 3.34e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18412437  326 YTSRKVLTMEWVEGTKLNEQLAIEsqglkvlDLVNTGIQCSLRQLLEYGFFHADPHPGNLLATPDG 391
Cdd:PRK10359 114 YAHTYIMLIEYIEGVELNDMPEIS-------EDVKAKIKASIESLHQHGMVSGDPHKGNFIVSKNG 172
PLN03224 PLN03224
probable serine/threonine protein kinase; Provisional
 339-399 3.42e-03

probable serine/threonine protein kinase; Provisional


Pssm-ID: 178763 [Multi-domain]  Cd Length: 507  Bit Score: 40.44  E-value: 3.42e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18412437  339 GTKLNEQLAIESQGLKVLDLVNTGIQCSLRQLLEYGFFHADPHPGNLLATPDGKLAFLDFG 399
Cdd:PLN03224 294 GKKIPDNMPQDKRDINVIKGVMRQVLTGLRKLHRIGIVHRDIKPENLLVTVDGQVKIIDFG 354
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 367-413 6.63e-03

Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.


Pssm-ID: 426359 [Multi-domain]  Cd Length: 239  Bit Score: 39.02  E-value: 6.63e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 18412437   367 LRQLLEYGFFHADPHPGNLLATPDGKL-AFLDFGMMSETPEEARFAII 413
Cdd:pfam01636 161 LPAELPPVLVHGDLHPGNLLVDPGGRVsGVIDFEDAGLGDPAYDLAIL 208
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
 217-426 6.72e-03

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta 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: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 39.50  E-value: 6.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 217 VSPEPIAAASLGQVYKAQLRYSGQVVAVK-VQRPGIEEAigldfylirgvgklinkyvdfittdvltlideFACRVYQEL 295
Cdd:cd07879  18 TSLKQVGSGAYGSVCSAIDKRTGEKVAIKkLSRPFQSEI--------------------------------FAKRAYREL 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18412437 296 NYVQEAQNARRFKKLyadkaDVLVPDIFWDYTSRKVLTMEWVEgTKLNEQLAIESQGLKVLDLVNTGIqCSLRQLLEYGF 375
Cdd:cd07879  66 TLLKHMQHENVIGLL-----DVFTSAVSGDEFQDFYLVMPYMQ-TDLQKIMGHPLSEDKVQYLVYQML-CGLKYIHSAGI 138

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 18412437 376 FHADPHPGNLLATPDGKLAFLDFGMmsetpeeARFAIIGHVVHLVNRDYEA 426
Cdd:cd07879 139 IHRDLKPGNLAVNEDCELKILDFGL-------ARHADAEMTGYVVTRWYRA 182
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
 220-246 9.43e-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: 38.39  E-value: 9.43e-03
                        10        20
                ....*....|....*....|....*..
gi 18412437 220 EPIAAASLGQVYKAQLRYSGQVVAVKV 246
Cdd:cd14002   7 ELIGEGSFGKVYKGRRKYTGQVVALKF 33
 
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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