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Conserved domains on  [gi|966955941|ref|XP_014999669|]
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uncharacterized aarF domain-containing protein kinase 1 isoform X2 [Macaca mulatta]

Protein Classification

ABC1 kinase family protein( domain architecture ID 10195500)

ABC1 (activator of bc1 complex) kinase family protein is an atypical protein kinase, similar to Saccharomyces cerevisiae ABC1 family protein MCP2 and to vertebrate AarF domain-containing protein kinase 1 (ADCK1), which appears to be essential for maintaining mitochondrial cristae formation and mitochondrial function

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 ...
122-374 1.40e-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: 446.16  E-value: 1.40e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 122 VLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVL 201
Cdd:cd13969    1 VLQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVHKAKLKDGEEVAVKVQHPDLRKQFAGDLATMEFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 202 ILAVKQLFPEFEFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLKHFDFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDY 281
Cdd:cd13969   81 VNLVEKLFPDFPFSWLVDELKKNLPKELDFLNEARNAERCAKLFKHRPDVYVPKVYWDLSSKRVLTMEFIDGIKIDDVEA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 282 MEKNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPGTGKAEIVLLDHGLYQVLTEEFRLNYCHLWQSLIWT 361
Cdd:cd13969  161 LKKLGIDPKEVARLLSEAFAEMIFVHGFVHCDPHPGNLLVRKNPGPGKPQIVLLDHGLYRELDEEFRLNYCRLWKALILG 240
                        250
                 ....*....|...
gi 966955941 362 DMKRVKEYSQRLG 374
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 ...
122-374 1.40e-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: 446.16  E-value: 1.40e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 122 VLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVL 201
Cdd:cd13969    1 VLQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVHKAKLKDGEEVAVKVQHPDLRKQFAGDLATMEFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 202 ILAVKQLFPEFEFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLKHFDFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDY 281
Cdd:cd13969   81 VNLVEKLFPDFPFSWLVDELKKNLPKELDFLNEARNAERCAKLFKHRPDVYVPKVYWDLSSKRVLTMEFIDGIKIDDVEA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 282 MEKNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPGTGKAEIVLLDHGLYQVLTEEFRLNYCHLWQSLIWT 361
Cdd:cd13969  161 LKKLGIDPKEVARLLSEAFAEMIFVHGFVHCDPHPGNLLVRKNPGPGKPQIVLLDHGLYRELDEEFRLNYCRLWKALILG 240
                        250
                 ....*....|...
gi 966955941 362 DMKRVKEYSQRLG 374
Cdd:cd13969  241 DEKKIKKYSKALG 253
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
123-370 7.97e-120

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: 352.31  E-value: 7.97e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941  123 LHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVLI 202
Cdd:pfam03109   2 LQDRAPPFPFEQAKKVIEEELGAPVEEIFAEFDEEPIAAASIAQVHRARLKDGEEVAVKVQRPGVKKRIRSDLLLLRFLA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941  203 LAVKQLFPEF-EFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLKHFDFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDY 281
Cdd:pfam03109  82 KVAKRFFPGFrRLDWLVDEFRKSLPQELDFLREAANAEKFRENFADDPDVYVPKVYWELTTERVLTMEYVDGIKIDDLDA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941  282 MEKNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPgtgkaEIVLLDHGLYQVLTEEFRLNYCHLWQSLIWT 361
Cdd:pfam03109 162 LSEAGIDRKEIARRLVELFLEQIFRDGFFHADPHPGNILVRKDG-----RIVLLDFGLMGRLDEKFRRLYAELLLALVNR 236

                  ....*....
gi 966955941  362 DMKRVKEYS 370
Cdd:pfam03109 237 DYKRVAEML 245
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
76-374 3.55e-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: 271.69  E-value: 3.55e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941  76 RSKVHLRSARRLCELCCANRGTFIKVGQHLGALDYLLPEEYTSTLKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFD 155
Cdd:COG0661   44 REELRRRRAERLRLALEELGPTFIKLGQLLSTRPDLLPPEYAEELAKLQDRVPPFPFEEVRAVIEEELGRPLEELFAEFD 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 156 DTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVLILAVKQLFPE---FEFMWLVDEAKKNLPLELDFL 232
Cdd:COG0661  124 PEPLAAASIGQVHRARLKDGREVAVKVQRPGIEEAIEADLRILRRLARLLERLSPEgrrLDPVEVVDEFARSLLEELDYR 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 233 NEGRNAEKVSQMLKHFDFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDYMEKNKIDVNEISRHLGKMYSEMIFVNGFVHC 312
Cdd:COG0661  204 REAANAERFRRNFADDPDVYVPKVYWELSTRRVLTMEWIDGIKISDLEALDAAGIDRKRLAERLVRAFLRQVFRDGFFHA 283
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966955941 313 DPHPGNVLVRKhpgTGKaeIVLLDHGLYQVLTEEFRLNYCHLWQSLIWTDMKRVKEYSQRLG 374
Cdd:COG0661  284 DPHPGNIFVLP---DGR--LVLLDFGMVGRLDPETREGLAELLLALLNRDYDRVAEALLELG 340
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
97-375 1.04e-62

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: 211.39  E-value: 1.04e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941   97 TFIKVGQHLGALDYLLPEEYTSTLKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGR 176
Cdd:TIGR01982  63 TFIKFGQTLSTRADLLPADIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEEKPLAAASIAQVHRARLVDGK 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941  177 TVAVKVQHPKVRAQSSKDILLMEVLILAVKQLFPEF---EFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLKHFDFLKV 253
Cdd:TIGR01982 143 EVAVKVLRPGIEKTIAADIALLYRLARIVERLSPDSrrlRPTEVVKEFEKTLRRELDLRREAANASELGENFKNDPGVYV 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941  254 PRIHWDLSTERVLLMEFVDGGQVNDRDYMEKNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPgtgkaEIV 333
Cdd:TIGR01982 223 PEVYWDRTSERVLTMEWIDGIPLSDIAALDEAGLDRKALAENLARSFLNQVLRDGFFHADLHPGNIFVLKDG-----KII 297
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 966955941  334 LLDHGLYQVLTEEFRLNYCHLWQSLIWTDMKRVKEYSQRLGA 375
Cdd:TIGR01982 298 ALDFGIVGRLSEEDRRYLAEILYGFLNRDYRRVAEVHFDAGY 339
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
98-346 2.43e-40

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 153.14  E-value: 2.43e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941  98 FIKVGQHLGALDYLLPEEYTSTLKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHD-GR 176
Cdd:PRK04750  66 FVKFGQMLSTRRDLFPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQVHFARLKDnGR 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 177 TVAVKVQHPKVRAQSSKDILLMEVLILAVKQLFPEF------EfmwLVDEAKKNLPLELDFLNEGRNAekvSQMLKHF-- 248
Cdd:PRK04750 146 EVVVKVLRPDILPVIDADLALMYRLARWVERLLPDGrrlkprE---VVAEFEKTLHDELDLMREAANA---SQLRRNFed 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 249 -DFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDYMEKNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPGT 327
Cdd:PRK04750 220 sDMLYVPEVYWDYCSETVMVMERMYGIPVSDVAALRAAGTDMKLLAERGVEVFFTQVFRDGFFHADMHPGNIFVSYDPPE 299
                        250
                 ....*....|....*....
gi 966955941 328 GKAEIVlLDHGLYQVLTEE 346
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 ...
122-374 1.40e-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: 446.16  E-value: 1.40e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 122 VLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVL 201
Cdd:cd13969    1 VLQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVHKAKLKDGEEVAVKVQHPDLRKQFAGDLATMEFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 202 ILAVKQLFPEFEFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLKHFDFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDY 281
Cdd:cd13969   81 VNLVEKLFPDFPFSWLVDELKKNLPKELDFLNEARNAERCAKLFKHRPDVYVPKVYWDLSSKRVLTMEFIDGIKIDDVEA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 282 MEKNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPGTGKAEIVLLDHGLYQVLTEEFRLNYCHLWQSLIWT 361
Cdd:cd13969  161 LKKLGIDPKEVARLLSEAFAEMIFVHGFVHCDPHPGNLLVRKNPGPGKPQIVLLDHGLYRELDEEFRLNYCRLWKALILG 240
                        250
                 ....*....|...
gi 966955941 362 DMKRVKEYSQRLG 374
Cdd:cd13969  241 DEKKIKKYSKALG 253
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
123-370 7.97e-120

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: 352.31  E-value: 7.97e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941  123 LHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVLI 202
Cdd:pfam03109   2 LQDRAPPFPFEQAKKVIEEELGAPVEEIFAEFDEEPIAAASIAQVHRARLKDGEEVAVKVQRPGVKKRIRSDLLLLRFLA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941  203 LAVKQLFPEF-EFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLKHFDFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDY 281
Cdd:pfam03109  82 KVAKRFFPGFrRLDWLVDEFRKSLPQELDFLREAANAEKFRENFADDPDVYVPKVYWELTTERVLTMEYVDGIKIDDLDA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941  282 MEKNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPgtgkaEIVLLDHGLYQVLTEEFRLNYCHLWQSLIWT 361
Cdd:pfam03109 162 LSEAGIDRKEIARRLVELFLEQIFRDGFFHADPHPGNILVRKDG-----RIVLLDFGLMGRLDEKFRRLYAELLLALVNR 236

                  ....*....
gi 966955941  362 DMKRVKEYS 370
Cdd:pfam03109 237 DYKRVAEML 245
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
123-359 1.91e-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: 269.36  E-value: 1.91e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 123 LHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVLI 202
Cdd:cd05121    2 LQDDVPPFPFEEVRKIIEEELGRPLEEVFAEFDPEPLAAASIAQVHRARLKDGREVAVKVQRPGIEEIIEADLRILRRLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 203 LAVKQLFPE---FEFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLKHFDFLKVPRIHWDLSTERVLLMEFVDGGQVNDR 279
Cdd:cd05121   82 RLLERLSPLlrrLDLVAIVDEFARSLLEELDFRREARNAERFRKNLKDSPDVYVPKVYPELSTRRVLVMEYIDGVKLTDL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 280 DYMEKNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHpgtGKaeIVLLDHGLYQVLTEEFRLNYCHLWQSLI 359
Cdd:cd05121  162 EALRAAGIDRKELARRLVDAYLKQIFEDGFFHADPHPGNILVLPD---GR--IALLDFGMVGRLDPETREALADLLLALV 236
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
76-374 3.55e-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: 271.69  E-value: 3.55e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941  76 RSKVHLRSARRLCELCCANRGTFIKVGQHLGALDYLLPEEYTSTLKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFD 155
Cdd:COG0661   44 REELRRRRAERLRLALEELGPTFIKLGQLLSTRPDLLPPEYAEELAKLQDRVPPFPFEEVRAVIEEELGRPLEELFAEFD 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 156 DTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVLILAVKQLFPE---FEFMWLVDEAKKNLPLELDFL 232
Cdd:COG0661  124 PEPLAAASIGQVHRARLKDGREVAVKVQRPGIEEAIEADLRILRRLARLLERLSPEgrrLDPVEVVDEFARSLLEELDYR 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 233 NEGRNAEKVSQMLKHFDFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDYMEKNKIDVNEISRHLGKMYSEMIFVNGFVHC 312
Cdd:COG0661  204 REAANAERFRRNFADDPDVYVPKVYWELSTRRVLTMEWIDGIKISDLEALDAAGIDRKRLAERLVRAFLRQVFRDGFFHA 283
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966955941 313 DPHPGNVLVRKhpgTGKaeIVLLDHGLYQVLTEEFRLNYCHLWQSLIWTDMKRVKEYSQRLG 374
Cdd:COG0661  284 DPHPGNIFVLP---DGR--LVLLDFGMVGRLDPETREGLAELLLALLNRDYDRVAEALLELG 340
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
97-375 1.04e-62

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: 211.39  E-value: 1.04e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941   97 TFIKVGQHLGALDYLLPEEYTSTLKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGR 176
Cdd:TIGR01982  63 TFIKFGQTLSTRADLLPADIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEEKPLAAASIAQVHRARLVDGK 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941  177 TVAVKVQHPKVRAQSSKDILLMEVLILAVKQLFPEF---EFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLKHFDFLKV 253
Cdd:TIGR01982 143 EVAVKVLRPGIEKTIAADIALLYRLARIVERLSPDSrrlRPTEVVKEFEKTLRRELDLRREAANASELGENFKNDPGVYV 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941  254 PRIHWDLSTERVLLMEFVDGGQVNDRDYMEKNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPgtgkaEIV 333
Cdd:TIGR01982 223 PEVYWDRTSERVLTMEWIDGIPLSDIAALDEAGLDRKALAENLARSFLNQVLRDGFFHADLHPGNIFVLKDG-----KII 297
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 966955941  334 LLDHGLYQVLTEEFRLNYCHLWQSLIWTDMKRVKEYSQRLGA 375
Cdd:TIGR01982 298 ALDFGIVGRLSEEDRRYLAEILYGFLNRDYRRVAEVHFDAGY 339
ABC1_ADCK3 cd13970
Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This ...
120-374 1.02e-59

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: 197.73  E-value: 1.02e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 120 LKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLME 199
Cdd:cd13970    3 LARLRDSAPPMPWAQLEKVLEAELGEDWRELFAEFDEEPFAAASIGQVHRATLKDGREVAVKVQYPGVAESIDSDLNNLR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 200 VLILAVKQLFPEFEFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLKHFDFLKVPRIHWDLSTERVLLMEFVDGGQVND- 278
Cdd:cd13970   83 RLLKLTGLLPKGLDLDALIAELREELLEECDYEREAANQRRFRELLADDPRFVVPEVIPELSTKRVLTTEFVDGVPLDEa 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 279 RDYMEKNKidvNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRkhPGTGKaeIVLLDHGLYQVLTEEFRLNYCHLWQSL 358
Cdd:cd13970  163 ADLSQEER---NRIGELLLRLCLRELFEFGFMQTDPNPGNFLYD--PEDGR--LGLLDFGAVREYPPEFVDGYRRLVRAA 235
                        250
                 ....*....|....*.
gi 966955941 359 IWTDMKRVKEYSQRLG 374
Cdd:cd13970  236 LEGDREALLEASVELG 251
UbiB cd13972
Ubiquinone biosynthetic protein UbiB; UbiB is the prokaryotic homolog of yeast Abc1p and human ...
131-368 1.12e-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: 1.12e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 131 SMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVLILAVKQLFP 210
Cdd:cd13972   10 SGKEARAIIEAELGKPLDALFSDFDEEPVAAASIAQVHKARLLDGREVAVKVLRPGIEKRIERDLELLRFLARLAERLLP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 211 EFEFMWL---VDEAKKNLPLELDFLNEGRNAEKVSQMLKHFDFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDYMEKNKI 287
Cdd:cd13972   90 EARRLRPvevVKEFARSLLLELDLRLEAANASELRENFLDDPGFYVPEVYWELTSKNVLTMEWIDGIPISDIEALDAAGI 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 288 DVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPGtgkaeIVLLDHGLYQVLTEEFRLNYCHLWQSLIWTDMKRVK 367
Cdd:cd13972  170 DRKALAERLVEIFFRQVFRDGFFHADMHPGNIFVDPNGR-----IIAVDFGIMGRLDKKDRRYLAEILYGFLTRDYRRVA 244

                 .
gi 966955941 368 E 368
Cdd:cd13972  245 E 245
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
98-346 2.43e-40

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 153.14  E-value: 2.43e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941  98 FIKVGQHLGALDYLLPEEYTSTLKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHD-GR 176
Cdd:PRK04750  66 FVKFGQMLSTRRDLFPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQVHFARLKDnGR 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 177 TVAVKVQHPKVRAQSSKDILLMEVLILAVKQLFPEF------EfmwLVDEAKKNLPLELDFLNEGRNAekvSQMLKHF-- 248
Cdd:PRK04750 146 EVVVKVLRPDILPVIDADLALMYRLARWVERLLPDGrrlkprE---VVAEFEKTLHDELDLMREAANA---SQLRRNFed 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 249 -DFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDYMEKNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPGT 327
Cdd:PRK04750 220 sDMLYVPEVYWDYCSETVMVMERMYGIPVSDVAALRAAGTDMKLLAERGVEVFFTQVFRDGFFHADMHPGNIFVSYDPPE 299
                        250
                 ....*....|....*....
gi 966955941 328 GKAEIVlLDHGLYQVLTEE 346
Cdd:PRK04750 300 NPRYIA-LDFGIVGSLNKE 317
ADCK2-like cd13971
aarF domain containing kinase 2 and similar proteins; This subfamily is composed of ...
123-359 1.85e-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: 142.75  E-value: 1.85e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 123 LHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHD--------GRTVAVKVQHPKVRAQSSKD 194
Cdd:cd13971    2 LHSNAPPHSWAHTERALEAAFGKDWEDIFEEFDEEPIGSGSIAQVHRAKLKPdyggdgggPRVVAVKVLHPGVREQIERD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 195 ILLMEVLILAVKQLFPefeFMWL-----VDEAKKNLPLELDFLNEGRNAEKVSQMLKHFDFLKVPRIHWDLSTERVLLME 269
Cdd:cd13971   82 LAILRLFAKLLEAIPP---LRWLslpesVEQFASLMLRQLDLRVEAANLERFRENFKDRKDVSFPKPLYPLVTEEVLVET 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 270 FVDGGQVNDRDYMEKNkidvNEISRHLGKM----YSEMIFVNGFVHCDPHPGNVLVRKHPGTGKA------------EIV 333
Cdd:cd13971  159 FEEGVPISRTVLAHGG----EPLKRKLARIgldaFLKMLFVDNFVHGDLHPGNILVRFNDSNRPSllvsldargsppRLV 234
                        250       260
                 ....*....|....*....|....*.
gi 966955941 334 LLDHGLYQVLTEEFRLNYCHLWQSLI 359
Cdd:cd13971  235 FLDAGLVTELSPQDRRNFIDLFKAVA 260
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
251-341 2.30e-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: 47.65  E-value: 2.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 251 LKVPRIHwDLSTER-VLLMEFVDGGQVNDR-DYMEKNKIDVNEISRHLGKMYSemifvNGFVHCDPHPGNVLVRKHpgtg 328
Cdd:COG3642   18 VPVPKVL-DVDPDDaDLVMEYIEGETLADLlEEGELPPELLRELGRLLARLHR-----AGIVHGDLTTSNILVDDG---- 87
                         90
                 ....*....|...
gi 966955941 329 kaEIVLLDHGLYQ 341
Cdd:COG3642   88 --GVYLIDFGLAR 98
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
263-339 2.79e-06

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


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 49.89  E-value: 2.79e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966955941 263 ERVLLMEFVDGGQVndRDYMEKNKIDVNEISRHLGKMYSemifvNGFVHCDPHPGNVLVRkhpgtgKAEIVLLDHGL 339
Cdd:PRK09605 410 EKTIVMEYIGGKDL--KDVLEGNPELVRKVGEIVAKLHK-----AGIVHGDLTTSNFIVR------DDRLYLIDFGL 473
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
158-339 1.89e-04

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: 43.34  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 158 PLGTASLAQVHKAV-LHDGRTVAVKVQHPKVRAQsskdillmevlilavkqlfpefefmwlvDEAKKnlplelDFLNEGR 236
Cdd:cd14014    7 LLGRGGMGEVYRARdTLLGRPVAIKVLRPELAED----------------------------EEFRE------RFLREAR 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 237 NAEKvsqmLKH------FDFLKVPRIHWdlstervLLMEFVDGGQVndRDYMEKNK-IDVNEISRHLGKMYSEMIFV--N 307
Cdd:cd14014   53 ALAR----LSHpnivrvYDVGEDDGRPY-------IVMEYVEGGSL--ADLLRERGpLPPREALRILAQIADALAAAhrA 119
                        170       180       190
                 ....*....|....*....|....*....|..
gi 966955941 308 GFVHCDPHPGNVLVRKHPgtgkaEIVLLDHGL 339
Cdd:cd14014  120 GIVHRDIKPANILLTEDG-----RVKLTDFGI 146
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
224-321 4.38e-04

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 40.50  E-value: 4.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 224 NLPLELDFLNEGRNAEKVSQMLKHFDFLKVPRIHwdlSTERVLLMEFVDGGQVNDRDYM-EKNKIDVNEISRHLGKmYSE 302
Cdd:cd13968   30 NNEEGEDLESEMDILRRLKGLELNIPKVLVTEDV---DGPNILLMELVKGGTLIAYTQEeELDEKDVESIMYQLAE-CMR 105
                         90
                 ....*....|....*....
gi 966955941 303 MIFVNGFVHCDPHPGNVLV 321
Cdd:cd13968  106 LLHSFHLIHRDLNNDNILL 124
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
243-324 5.20e-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: 40.75  E-value: 5.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 243 QMLKHFDFLKVPRIH--WDLSTERVLLMEFVDGgQVNDRDYMEKNKIDVNEISRHLGKMYSEM--IFVNGFVHCDPHPGN 318
Cdd:cd05120   44 QLLAGKLSLPVPKVYgfGESDGWEYLLMERIEG-ETLSEVWPRLSEEEKEKIADQLAEILAALhrIDSSVLTHGDLHPGN 122

                 ....*.
gi 966955941 319 VLVRKH 324
Cdd:cd05120  123 ILVKPD 128
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
202-321 1.51e-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: 40.58  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 202 ILAVKQLfpefefmwlvdEAKKNLPLELDFLnegRNAEKVSQMLKHfdflkvPRI---HWDLSTERVL--LMEFVDGGQV 276
Cdd:cd06606   27 LMAVKEV-----------ELSGDSEEELEAL---EREIRILSSLKH------PNIvryLGTERTENTLniFLEYVPGGSL 86
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 966955941 277 ndRDYMEKN-KIDVNEIsrhlgKMYSEMIF-------VNGFVHCDPHPGNVLV 321
Cdd:cd06606   87 --ASLLKKFgKLPEPVV-----RKYTRQILegleylhSNGIVHRDIKGANILV 132
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
251-345 2.05e-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: 40.00  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 251 LKVPRI-----HWDLSTERVLLMEFVDGGQVND-----RDYMEKNKID-VNEISRHLGKMYSEMIfvngfVHCDPHPGNV 319
Cdd:cd14095   55 VKHPNIvqlieEYDTDTELYLVMELVKGGDLFDaitssTKFTERDASRmVTDLAQALKYLHSLSI-----VHRDIKPENL 129
                         90       100
                 ....*....|....*....|....*.
gi 966955941 320 LVRKHpGTGKAEIVLLDHGLYQVLTE 345
Cdd:cd14095  130 LVVEH-EDGSKSLKLADFGLATEVKE 154
PRK14879 PRK14879
Kae1-associated kinase Bud32;
251-339 2.24e-03

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 39.50  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 251 LKVPRIHW-DLStERVLLMEFVDGgqVNDRDYMEKNKIDVNEISRHLG----KMYSemifvNGFVHCDPHPGNVLVRkhp 325
Cdd:PRK14879  61 VNVPAVYFvDPE-NFIIVMEYIEG--EPLKDLINSNGMEELELSREIGrlvgKLHS-----AGIIHGDLTTSNMILS--- 129
                         90
                 ....*....|....
gi 966955941 326 gtgKAEIVLLDHGL 339
Cdd:PRK14879 130 ---GGKIYLIDFGL 140
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
159-339 9.22e-03

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 37.64  E-value: 9.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 159 LGTASLAQVHKAV-LHDGRTVAVKVQHPKvraqsskdillmevlilavkqlfpefefmwLVDEAKKNLPLELdflnegrn 237
Cdd:cd00180    1 LGKGSFGKVYKARdKETGKKVAVKVIPKE------------------------------KLKKLLEELLREI-------- 42
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966955941 238 aekvsQMLKHFDFLKVPRIH--WDLSTERVLLMEFVDGGqvNDRDYMEKN--KIDVNEISRHLGKMYS--EMIFVNGFVH 311
Cdd:cd00180   43 -----EILKKLNHPNIVKLYdvFETENFLYLVMEYCEGG--SLKDLLKENkgPLSEEEALSILRQLLSalEYLHSNGIIH 115
                        170       180
                 ....*....|....*....|....*...
gi 966955941 312 CDPHPGNVLVRKHPgtgkaEIVLLDHGL 339
Cdd:cd00180  116 RDLKPENILLDSDG-----TVKLADFGL 138
 
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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