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Conserved domains on  [gi|115503784|sp|Q86TW2|]
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RecName: Full=AarF domain-containing protein kinase 1; Flags: Precursor

Protein Classification

ABC1 kinase family protein( domain architecture ID 10195500)

ABC1 (activator of bc1 complex) kinase family protein similar to yeast Abc1p and its human homolog ADCK3 (aarF domain containing kinase 3), which are atypical protein kinases required for the biosynthesis of coenzyme Q (ubiquinone or Q), an essential lipid component in respiratory electron and proton transport

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ADCK1-like cd13969
aarF domain containing kinase 1 and similar proteins; This subfamily is composed of ...
124-376 2.61e-156

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: 445.39  E-value: 2.61e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 124 VLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVL 203
Cdd:cd13969    1 VLQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVHKAKLKDGEEVAVKVQHPDLRKQFAGDLATMEFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 204 VLAVKQLFPEFEFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDY 283
Cdd:cd13969   81 VNLVEKLFPDFPFSWLVDELKKNLPKELDFLNEARNAERCAKLFKHRPDVYVPKVYWDLSSKRVLTMEFIDGIKIDDVEA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 284 MERNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPGTGKAEIVLLDHGLYQMLTEEFRLNYCHLWQSLIWT 363
Cdd:cd13969  161 LKKLGIDPKEVARLLSEAFAEMIFVHGFVHCDPHPGNLLVRKNPGPGKPQIVLLDHGLYRELDEEFRLNYCRLWKALILG 240
                        250
                 ....*....|...
gi 115503784 364 DMKRVKEYSQRLG 376
Cdd:cd13969  241 DEKKIKKYSKALG 253
 
Name Accession Description Interval E-value
ADCK1-like cd13969
aarF domain containing kinase 1 and similar proteins; This subfamily is composed of ...
124-376 2.61e-156

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: 445.39  E-value: 2.61e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 124 VLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVL 203
Cdd:cd13969    1 VLQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVHKAKLKDGEEVAVKVQHPDLRKQFAGDLATMEFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 204 VLAVKQLFPEFEFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDY 283
Cdd:cd13969   81 VNLVEKLFPDFPFSWLVDELKKNLPKELDFLNEARNAERCAKLFKHRPDVYVPKVYWDLSSKRVLTMEFIDGIKIDDVEA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 284 MERNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPGTGKAEIVLLDHGLYQMLTEEFRLNYCHLWQSLIWT 363
Cdd:cd13969  161 LKKLGIDPKEVARLLSEAFAEMIFVHGFVHCDPHPGNLLVRKNPGPGKPQIVLLDHGLYRELDEEFRLNYCRLWKALILG 240
                        250
                 ....*....|...
gi 115503784 364 DMKRVKEYSQRLG 376
Cdd:cd13969  241 DEKKIKKYSKALG 253
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
125-372 5.04e-121

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: 355.39  E-value: 5.04e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784  125 LHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVLV 204
Cdd:pfam03109   2 LQDRAPPFPFEQAKKVIEEELGAPVEEIFAEFDEEPIAAASIAQVHRARLKDGEEVAVKVQRPGVKKRIRSDLLLLRFLA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784  205 LAVKQLFPEF-EFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDY 283
Cdd:pfam03109  82 KVAKRFFPGFrRLDWLVDEFRKSLPQELDFLREAANAEKFRENFADDPDVYVPKVYWELTTERVLTMEYVDGIKIDDLDA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784  284 MERNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPgtgkaEIVLLDHGLYQMLTEEFRLNYCHLWQSLIWT 363
Cdd:pfam03109 162 LSEAGIDRKEIARRLVELFLEQIFRDGFFHADPHPGNILVRKDG-----RIVLLDFGLMGRLDEKFRRLYAELLLALVNR 236

                  ....*....
gi 115503784  364 DMKRVKEYS 372
Cdd:pfam03109 237 DYKRVAEML 245
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
60-376 6.96e-85

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: 271.31  E-value: 6.96e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784  60 VPYGSEEYLQLRSKSWPVFLQVHLRSARRLCELCCANRGTFIKVGQHLGALDYLLPEEYTSTLKVLHSQAPQSSMQEIRQ 139
Cdd:COG0661   26 LDRLGLPRLRRLLTGEERREELRRRRAERLRLALEELGPTFIKLGQLLSTRPDLLPPEYAEELAKLQDRVPPFPFEEVRA 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 140 VIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVLVLAVKQLFPE---FEF 216
Cdd:COG0661  106 VIEEELGRPLEELFAEFDPEPLAAASIGQVHRARLKDGREVAVKVQRPGIEEAIEADLRILRRLARLLERLSPEgrrLDP 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 217 MWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDYMERNKIDVNEISR 296
Cdd:COG0661  186 VEVVDEFARSLLEELDYRREAANAERFRRNFADDPDVYVPKVYWELSTRRVLTMEWIDGIKISDLEALDAAGIDRKRLAE 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 297 HLGKMYSEMIFVNGFVHCDPHPGNVLVRKhpgTGKaeIVLLDHGLYQMLTEEFRLNYCHLWQSLIWTDMKRVKEYSQRLG 376
Cdd:COG0661  266 RLVRAFLRQVFRDGFFHADPHPGNIFVLP---DGR--LVLLDFGMVGRLDPETREGLAELLLALLNRDYDRVAEALLELG 340
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
99-377 7.21e-63

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: 212.16  E-value: 7.21e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784   99 TFIKVGQHLGALDYLLPEEYTSTLKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGR 178
Cdd:TIGR01982  63 TFIKFGQTLSTRADLLPADIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEEKPLAAASIAQVHRARLVDGK 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784  179 TVAVKVQHPKVRAQSSKDILLMEVLVLAVKQLFPEF---EFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKV 255
Cdd:TIGR01982 143 EVAVKVLRPGIEKTIAADIALLYRLARIVERLSPDSrrlRPTEVVKEFEKTLRRELDLRREAANASELGENFKNDPGVYV 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784  256 PRIHWDLSTERVLLMEFVDGGQVNDRDYMERNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPgtgkaEIV 335
Cdd:TIGR01982 223 PEVYWDRTSERVLTMEWIDGIPLSDIAALDEAGLDRKALAENLARSFLNQVLRDGFFHADLHPGNIFVLKDG-----KII 297
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 115503784  336 LLDHGLYQMLTEEFRLNYCHLWQSLIWTDMKRVKEYSQRLGA 377
Cdd:TIGR01982 298 ALDFGIVGRLSEEDRRYLAEILYGFLNRDYRRVAEVHFDAGY 339
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
100-348 3.58e-41

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 155.45  E-value: 3.58e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 100 FIKVGQHLGALDYLLPEEYTSTLKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHD-GR 178
Cdd:PRK04750  66 FVKFGQMLSTRRDLFPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQVHFARLKDnGR 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 179 TVAVKVQHPKVRAQSSKDILLMEVLVLAVKQLFPEF------EfmwLVDEAKKNLPLELDFLNEGRNAekvSQMLRHF-- 250
Cdd:PRK04750 146 EVVVKVLRPDILPVIDADLALMYRLARWVERLLPDGrrlkprE---VVAEFEKTLHDELDLMREAANA---SQLRRNFed 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 251 -DFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDYMERNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPGT 329
Cdd:PRK04750 220 sDMLYVPEVYWDYCSETVMVMERMYGIPVSDVAALRAAGTDMKLLAERGVEVFFTQVFRDGFFHADMHPGNIFVSYDPPE 299
                        250
                 ....*....|....*....
gi 115503784 330 GKAEIVlLDHGLYQMLTEE 348
Cdd:PRK04750 300 NPRYIA-LDFGIVGSLNKE 317
 
Name Accession Description Interval E-value
ADCK1-like cd13969
aarF domain containing kinase 1 and similar proteins; This subfamily is composed of ...
124-376 2.61e-156

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: 445.39  E-value: 2.61e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 124 VLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVL 203
Cdd:cd13969    1 VLQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVHKAKLKDGEEVAVKVQHPDLRKQFAGDLATMEFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 204 VLAVKQLFPEFEFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDY 283
Cdd:cd13969   81 VNLVEKLFPDFPFSWLVDELKKNLPKELDFLNEARNAERCAKLFKHRPDVYVPKVYWDLSSKRVLTMEFIDGIKIDDVEA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 284 MERNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPGTGKAEIVLLDHGLYQMLTEEFRLNYCHLWQSLIWT 363
Cdd:cd13969  161 LKKLGIDPKEVARLLSEAFAEMIFVHGFVHCDPHPGNLLVRKNPGPGKPQIVLLDHGLYRELDEEFRLNYCRLWKALILG 240
                        250
                 ....*....|...
gi 115503784 364 DMKRVKEYSQRLG 376
Cdd:cd13969  241 DEKKIKKYSKALG 253
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
125-372 5.04e-121

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: 355.39  E-value: 5.04e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784  125 LHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVLV 204
Cdd:pfam03109   2 LQDRAPPFPFEQAKKVIEEELGAPVEEIFAEFDEEPIAAASIAQVHRARLKDGEEVAVKVQRPGVKKRIRSDLLLLRFLA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784  205 LAVKQLFPEF-EFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDY 283
Cdd:pfam03109  82 KVAKRFFPGFrRLDWLVDEFRKSLPQELDFLREAANAEKFRENFADDPDVYVPKVYWELTTERVLTMEYVDGIKIDDLDA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784  284 MERNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPgtgkaEIVLLDHGLYQMLTEEFRLNYCHLWQSLIWT 363
Cdd:pfam03109 162 LSEAGIDRKEIARRLVELFLEQIFRDGFFHADPHPGNILVRKDG-----RIVLLDFGLMGRLDEKFRRLYAELLLALVNR 236

                  ....*....
gi 115503784  364 DMKRVKEYS 372
Cdd:pfam03109 237 DYKRVAEML 245
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
125-361 5.42e-87

Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and similar proteins; This family is composed of the atypical yeast protein kinase Abc1p, its human homolog ADCK3 (also called CABC1), and similar proteins. Abc1p (also called Coq8p) is required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. It is necessary for the formation of a multi-subunit Q-biosynthetic complex and may also function in the regulation of Q synthesis. Human ADCK3 is able to rescue defects in Q synthesis and the phosphorylation state of Coq proteins in yeast Abc1 (or Coq8) mutants. Mutations in ADCK3 cause progressive cerebellar ataxia and atrophy due to Q10 deficiency. Eukaryotes contain at least two more ABC1/ADCK3-like proteins: in humans, these are the putative atypical protein kinases named ADCK1 and ADCK2. In algae and higher plants, ABC1 kinases have proliferated to more than 15 subfamilies, most of which are located in plastids or mitochondria. Eight of these plant ABC1 kinase subfamilies (ABC1K1-8) are specific for photosynthetic organisms. ABC1 kinases are not related to the ATP-binding cassette (ABC) membrane transporter family.


Pssm-ID: 270691 [Multi-domain]  Cd Length: 247  Bit Score: 268.21  E-value: 5.42e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 125 LHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVLV 204
Cdd:cd05121    2 LQDDVPPFPFEEVRKIIEEELGRPLEEVFAEFDPEPLAAASIAQVHRARLKDGREVAVKVQRPGIEEIIEADLRILRRLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 205 LAVKQLFPE---FEFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKVPRIHWDLSTERVLLMEFVDGGQVNDR 281
Cdd:cd05121   82 RLLERLSPLlrrLDLVAIVDEFARSLLEELDFRREARNAERFRKNLKDSPDVYVPKVYPELSTRRVLVMEYIDGVKLTDL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 282 DYMERNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHpgtGKaeIVLLDHGLYQMLTEEFRLNYCHLWQSLI 361
Cdd:cd05121  162 EALRAAGIDRKELARRLVDAYLKQIFEDGFFHADPHPGNILVLPD---GR--IALLDFGMVGRLDPETREALADLLLALV 236
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
60-376 6.96e-85

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: 271.31  E-value: 6.96e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784  60 VPYGSEEYLQLRSKSWPVFLQVHLRSARRLCELCCANRGTFIKVGQHLGALDYLLPEEYTSTLKVLHSQAPQSSMQEIRQ 139
Cdd:COG0661   26 LDRLGLPRLRRLLTGEERREELRRRRAERLRLALEELGPTFIKLGQLLSTRPDLLPPEYAEELAKLQDRVPPFPFEEVRA 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 140 VIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVLVLAVKQLFPE---FEF 216
Cdd:COG0661  106 VIEEELGRPLEELFAEFDPEPLAAASIGQVHRARLKDGREVAVKVQRPGIEEAIEADLRILRRLARLLERLSPEgrrLDP 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 217 MWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDYMERNKIDVNEISR 296
Cdd:COG0661  186 VEVVDEFARSLLEELDYRREAANAERFRRNFADDPDVYVPKVYWELSTRRVLTMEWIDGIKISDLEALDAAGIDRKRLAE 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 297 HLGKMYSEMIFVNGFVHCDPHPGNVLVRKhpgTGKaeIVLLDHGLYQMLTEEFRLNYCHLWQSLIWTDMKRVKEYSQRLG 376
Cdd:COG0661  266 RLVRAFLRQVFRDGFFHADPHPGNIFVLP---DGR--LVLLDFGMVGRLDPETREGLAELLLALLNRDYDRVAEALLELG 340
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
99-377 7.21e-63

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: 212.16  E-value: 7.21e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784   99 TFIKVGQHLGALDYLLPEEYTSTLKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGR 178
Cdd:TIGR01982  63 TFIKFGQTLSTRADLLPADIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEEKPLAAASIAQVHRARLVDGK 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784  179 TVAVKVQHPKVRAQSSKDILLMEVLVLAVKQLFPEF---EFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKV 255
Cdd:TIGR01982 143 EVAVKVLRPGIEKTIAADIALLYRLARIVERLSPDSrrlRPTEVVKEFEKTLRRELDLRREAANASELGENFKNDPGVYV 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784  256 PRIHWDLSTERVLLMEFVDGGQVNDRDYMERNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPgtgkaEIV 335
Cdd:TIGR01982 223 PEVYWDRTSERVLTMEWIDGIPLSDIAALDEAGLDRKALAENLARSFLNQVLRDGFFHADLHPGNIFVLKDG-----KII 297
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 115503784  336 LLDHGLYQMLTEEFRLNYCHLWQSLIWTDMKRVKEYSQRLGA 377
Cdd:TIGR01982 298 ALDFGIVGRLSEEDRRYLAEILYGFLNRDYRRVAEVHFDAGY 339
ABC1_ADCK3 cd13970
Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This ...
122-376 2.77e-60

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: 199.28  E-value: 2.77e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 122 LKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLME 201
Cdd:cd13970    3 LARLRDSAPPMPWAQLEKVLEAELGEDWRELFAEFDEEPFAAASIGQVHRATLKDGREVAVKVQYPGVAESIDSDLNNLR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 202 VLVLAVKQLFPEFEFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKVPRIHWDLSTERVLLMEFVDG---GQV 278
Cdd:cd13970   83 RLLKLTGLLPKGLDLDALIAELREELLEECDYEREAANQRRFRELLADDPRFVVPEVIPELSTKRVLTTEFVDGvplDEA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 279 NDRDYMERNKidvneISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRkhPGTGKaeIVLLDHGLYQMLTEEFRLNYCHLWQ 358
Cdd:cd13970  163 ADLSQEERNR-----IGELLLRLCLRELFEFGFMQTDPNPGNFLYD--PEDGR--LGLLDFGAVREYPPEFVDGYRRLVR 233
                        250
                 ....*....|....*...
gi 115503784 359 SLIWTDMKRVKEYSQRLG 376
Cdd:cd13970  234 AALEGDREALLEASVELG 251
UbiB cd13972
Ubiquinone biosynthetic protein UbiB; UbiB is the prokaryotic homolog of yeast Abc1p and human ...
133-370 1.14e-52

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: 178.93  E-value: 1.14e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 133 SMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVLVLAVKQLFP 212
Cdd:cd13972   10 SGKEARAIIEAELGKPLDALFSDFDEEPVAAASIAQVHKARLLDGREVAVKVLRPGIEKRIERDLELLRFLARLAERLLP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 213 EFEFMWL---VDEAKKNLPLELDFLNEGRNAekvSQMLRHF---DFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDYMER 286
Cdd:cd13972   90 EARRLRPvevVKEFARSLLLELDLRLEAANA---SELRENFlddPGFYVPEVYWELTSKNVLTMEWIDGIPISDIEALDA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 287 NKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPGtgkaeIVLLDHGLYQMLTEEFRLNYCHLWQSLIWTDMK 366
Cdd:cd13972  167 AGIDRKALAERLVEIFFRQVFRDGFFHADMHPGNIFVDPNGR-----IIAVDFGIMGRLDKKDRRYLAEILYGFLTRDYR 241

                 ....
gi 115503784 367 RVKE 370
Cdd:cd13972  242 RVAE 245
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
100-348 3.58e-41

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 155.45  E-value: 3.58e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 100 FIKVGQHLGALDYLLPEEYTSTLKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHD-GR 178
Cdd:PRK04750  66 FVKFGQMLSTRRDLFPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQVHFARLKDnGR 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 179 TVAVKVQHPKVRAQSSKDILLMEVLVLAVKQLFPEF------EfmwLVDEAKKNLPLELDFLNEGRNAekvSQMLRHF-- 250
Cdd:PRK04750 146 EVVVKVLRPDILPVIDADLALMYRLARWVERLLPDGrrlkprE---VVAEFEKTLHDELDLMREAANA---SQLRRNFed 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 251 -DFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDYMERNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPGT 329
Cdd:PRK04750 220 sDMLYVPEVYWDYCSETVMVMERMYGIPVSDVAALRAAGTDMKLLAERGVEVFFTQVFRDGFFHADMHPGNIFVSYDPPE 299
                        250
                 ....*....|....*....
gi 115503784 330 GKAEIVlLDHGLYQMLTEE 348
Cdd:PRK04750 300 NPRYIA-LDFGIVGSLNKE 317
ADCK2-like cd13971
aarF domain containing kinase 2 and similar proteins; This subfamily is composed of ...
125-361 3.95e-38

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: 141.59  E-value: 3.95e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 125 LHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHD--------GRTVAVKVQHPKVRAQSSKD 196
Cdd:cd13971    2 LHSNAPPHSWAHTERALEAAFGKDWEDIFEEFDEEPIGSGSIAQVHRAKLKPdyggdgggPRVVAVKVLHPGVREQIERD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 197 ILLMEVLVLAVKQLFPefeFMWL-----VDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKVPRIHWDLSTERVLLME 271
Cdd:cd13971   82 LAILRLFAKLLEAIPP---LRWLslpesVEQFASLMLRQLDLRVEAANLERFRENFKDRKDVSFPKPLYPLVTEEVLVET 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 272 FVDGGQVNDRDYMERNkidvNEISRHLGKM----YSEMIFVNGFVHCDPHPGNVLVRKHPGTGKA------------EIV 335
Cdd:cd13971  159 FEEGVPISRTVLAHGG----EPLKRKLARIgldaFLKMLFVDNFVHGDLHPGNILVRFNDSNRPSllvsldargsppRLV 234
                        250       260
                 ....*....|....*....|....*.
gi 115503784 336 LLDHGLYQMLTEEFRLNYCHLWQSLI 361
Cdd:cd13971  235 FLDAGLVTELSPQDRRNFIDLFKAVA 260
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
253-343 3.02e-06

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: 47.26  E-value: 3.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 253 LKVPRIHwDLSTER-VLLMEFVDGGQVndRDYMERNKID---VNEISRHLGKMYSemifvNGFVHCDPHPGNVLVRKHpg 328
Cdd:COG3642   18 VPVPKVL-DVDPDDaDLVMEYIEGETL--ADLLEEGELPpelLRELGRLLARLHR-----AGIVHGDLTTSNILVDDG-- 87
                         90
                 ....*....|....*
gi 115503784 329 tgkaEIVLLDHGLYQ 343
Cdd:COG3642   88 ----GVYLIDFGLAR 98
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
265-341 3.98e-06

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


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 49.50  E-value: 3.98e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115503784 265 ERVLLMEFVDGGQVndRDYMERNKIDVNEISRHLGKMYSemifvNGFVHCDPHPGNVLVRkhpgtgKAEIVLLDHGL 341
Cdd:PRK09605 410 EKTIVMEYIGGKDL--KDVLEGNPELVRKVGEIVAKLHK-----AGIVHGDLTTSNFIVR------DDRLYLIDFGL 473
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
160-341 6.15e-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: 44.88  E-value: 6.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 160 PLGTASLAQVHKAV-LHDGRTVAVKVQHPKVRAQsskdillmevlvlavkqlfpefefmwlvDEAKKnlplelDFLNEGR 238
Cdd:cd14014    7 LLGRGGMGEVYRARdTLLGRPVAIKVLRPELAED----------------------------EEFRE------RFLREAR 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 239 NAEKvsqmLRH------FDFLKVPRIHWdlstervLLMEFVDGGQVndRDYMERNK-IDVNEISRHLGKMYSEMIFV--N 309
Cdd:cd14014   53 ALAR----LSHpnivrvYDVGEDDGRPY-------IVMEYVEGGSL--ADLLRERGpLPPREALRILAQIADALAAAhrA 119
                        170       180       190
                 ....*....|....*....|....*....|..
gi 115503784 310 GFVHCDPHPGNVLVRKHPgtgkaEIVLLDHGL 341
Cdd:cd14014  120 GIVHRDIKPANILLTEDG-----RVKLTDFGI 146
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
160-341 2.43e-04

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 43.85  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 160 PLGTASLAQVHKAV-LHDGRTVAVKVQHPKVRAQsskdillmevlvlavkqlfPEFefmwlvdeakknlpLELdFLNEGR 238
Cdd:COG0515   14 LLGRGGMGVVYLARdLRLGRPVALKVLRPELAAD-------------------PEA--------------RER-FRREAR 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 239 NAEKvsqmLRHFdflKVPRIHwDLSTER---VLLMEFVDGGQVndRDYMERNK-IDVNEISRHLGKMYSEMIFV--NGFV 312
Cdd:COG0515   60 ALAR----LNHP---NIVRVY-DVGEEDgrpYLVMEYVEGESL--ADLLRRRGpLPPAEALRILAQLAEALAAAhaAGIV 129
                        170       180
                 ....*....|....*....|....*....
gi 115503784 313 HCDPHPGNVLVRKhpgTGkaEIVLLDHGL 341
Cdd:COG0515  130 HRDIKPANILLTP---DG--RVKLIDFGI 153
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
245-326 4.09e-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: 41.13  E-value: 4.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 245 QMLRHFDFLKVPRIH--WDLSTERVLLMEFVDGgQVNDRDYMERNKIDVNEISRHLGKMYSEM--IFVNGFVHCDPHPGN 320
Cdd:cd05120   44 QLLAGKLSLPVPKVYgfGESDGWEYLLMERIEG-ETLSEVWPRLSEEEKEKIADQLAEILAALhrIDSSVLTHGDLHPGN 122

                 ....*.
gi 115503784 321 VLVRKH 326
Cdd:cd05120  123 ILVKPD 128
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
253-347 1.59e-03

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL 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: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 40.39  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 253 LKVPRI-----HWDLSTERVLLMEFVDGGQVND-----RDYMERNKID-VNEISRHLGKMYSEMIfvngfVHCDPHPGNV 321
Cdd:cd14095   55 VKHPNIvqlieEYDTDTELYLVMELVKGGDLFDaitssTKFTERDASRmVTDLAQALKYLHSLSI-----VHRDIKPENL 129
                         90       100
                 ....*....|....*....|....*.
gi 115503784 322 LVRKHpGTGKAEIVLLDHGLYQMLTE 347
Cdd:cd14095  130 LVVEH-EDGSKSLKLADFGLATEVKE 154
PRK14879 PRK14879
Kae1-associated kinase Bud32;
253-341 1.65e-03

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 39.89  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 253 LKVPRIHW-DLStERVLLMEFVDGgqVNDRDYMERNKIDVNEISRHLG----KMYSemifvNGFVHCDPHPGNVLVRkhp 327
Cdd:PRK14879  61 VNVPAVYFvDPE-NFIIVMEYIEG--EPLKDLINSNGMEELELSREIGrlvgKLHS-----AGIIHGDLTTSNMILS--- 129
                         90
                 ....*....|....
gi 115503784 328 gtgKAEIVLLDHGL 341
Cdd:PRK14879 130 ---GGKIYLIDFGL 140
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
151-350 3.67e-03

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 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: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 39.53  E-value: 3.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 151 DLFQS-FDDTP---LGTASLAQVHKAVLHD-GRTVAVKVQHPKVRAQSSKDILLMEVLVLAVKQLFPefefmWLVdeakk 225
Cdd:cd14197    3 EPFQErYSLSPgreLGRGKFAVVRKCVEKDsGKEFAAKFMRKRRKGQDCRMEIIHEIAVLELAQANP-----WVI----- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 226 nlpleldflnegrNAEKVSQMlrhfdflkvprihwdlSTERVLLMEFVDGGQVNDRDYMERNK-IDVNEISRHLGKMYSE 304
Cdd:cd14197   73 -------------NLHEVYET----------------ASEMILVLEYAAGGEIFNQCVADREEaFKEKDVKRLMKQILEG 123
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 115503784 305 MIFV--NGFVHCDPHPGNVLVRKHPGTGKAEIVllDHGLYQML--TEEFR 350
Cdd:cd14197  124 VSFLhnNNVVHLDLKPQNILLTSESPLGDIKIV--DFGLSRILknSEELR 171
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
226-323 3.71e-03

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: 37.81  E-value: 3.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 226 NLPLELDFLNEGRNAEKVSQMLRHFDFLKVPRIHwdlSTERVLLMEFVDGGQVNDRDYMERNK-IDVNEISRHLGKmYSE 304
Cdd:cd13968   30 NNEEGEDLESEMDILRRLKGLELNIPKVLVTEDV---DGPNILLMELVKGGTLIAYTQEEELDeKDVESIMYQLAE-CMR 105
                         90
                 ....*....|....*....
gi 115503784 305 MIFVNGFVHCDPHPGNVLV 323
Cdd:cd13968  106 LLHSFHLIHRDLNNDNILL 124
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
268-341 6.27e-03

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 38.49  E-value: 6.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115503784 268 LLMEFVDGGQVndRDYMER-NKIDVNEISRHLGKMYSEMIFV--NGFVHCDPHPGNVLVRKHPGTGKAEivLLDHGL 341
Cdd:cd14012   81 LLTEYAPGGSL--SELLDSvGSVPLDTARRWTLQLLEALEYLhrNGVVHKSLHAGNVLLDRDAGTGIVK--LTDYSL 153
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
204-323 7.33e-03

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK 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: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 38.27  E-value: 7.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115503784 204 VLAVKQLfpefefmwlvdEAKKNLPLELDFLnegRNAEKVSQMLRHfdflkvPRI---HWDLSTERVL--LMEFVDGGQV 278
Cdd:cd06606   27 LMAVKEV-----------ELSGDSEEELEAL---EREIRILSSLKH------PNIvryLGTERTENTLniFLEYVPGGSL 86
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 115503784 279 ndRDYMERN-KIDVNEIsrhlgKMYSEMIF-------VNGFVHCDPHPGNVLV 323
Cdd:cd06606   87 --ASLLKKFgKLPEPVV-----RKYTRQILegleylhSNGIVHRDIKGANILV 132
 
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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