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Conserved domains on  [gi|1907089249|ref|XP_036013513|]
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aarF domain-containing protein kinase 1 isoform X6 [Mus musculus]

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 ...
68-297 8.00e-139

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: 398.40  E-value: 8.00e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249  68 CRIHDLFLSFDDTPLGAASLAQVHKAVLHDGRTVAVKVQHPKVQAQSSKDILLMEVLVLAVKQLFPDFEFMWLVDEAKKN 147
Cdd:cd13969    24 KPPEELFSEFDEEPIASASLAQVHKAKLKDGEEVAVKVQHPDLRKQFAGDLATMEFLVNLVEKLFPDFPFSWLVDELKKN 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249 148 LPLELDFLNEGRNAEKVAHMLRHFDFLKVPQIHWELSTKRVLLMEFVEGGQVNDRAYMEKNQIDVNEISCHLGKMYSEMI 227
Cdd:cd13969   104 LPKELDFLNEARNAERCAKLFKHRPDVYVPKVYWDLSSKRVLTMEFIDGIKIDDVEALKKLGIDPKEVARLLSEAFAEMI 183
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249 228 FVNGFVHCDPHPGNVLVRKRPDTGKAEIVLLDHGLYQVLTEEFRLDYCHLWQSLIWTDMDGLKQYSQRLG 297
Cdd:cd13969   184 FVHGFVHCDPHPGNLLVRKNPGPGKPQIVLLDHGLYRELDEEFRLNYCRLWKALILGDEKKIKKYSKALG 253
 
Name Accession Description Interval E-value
ADCK1-like cd13969
aarF domain containing kinase 1 and similar proteins; This subfamily is composed of ...
68-297 8.00e-139

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: 398.40  E-value: 8.00e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249  68 CRIHDLFLSFDDTPLGAASLAQVHKAVLHDGRTVAVKVQHPKVQAQSSKDILLMEVLVLAVKQLFPDFEFMWLVDEAKKN 147
Cdd:cd13969    24 KPPEELFSEFDEEPIASASLAQVHKAKLKDGEEVAVKVQHPDLRKQFAGDLATMEFLVNLVEKLFPDFPFSWLVDELKKN 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249 148 LPLELDFLNEGRNAEKVAHMLRHFDFLKVPQIHWELSTKRVLLMEFVEGGQVNDRAYMEKNQIDVNEISCHLGKMYSEMI 227
Cdd:cd13969   104 LPKELDFLNEARNAERCAKLFKHRPDVYVPKVYWDLSSKRVLTMEFIDGIKIDDVEALKKLGIDPKEVARLLSEAFAEMI 183
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249 228 FVNGFVHCDPHPGNVLVRKRPDTGKAEIVLLDHGLYQVLTEEFRLDYCHLWQSLIWTDMDGLKQYSQRLG 297
Cdd:cd13969   184 FVHGFVHCDPHPGNLLVRKNPGPGKPQIVLLDHGLYRELDEEFRLNYCRLWKALILGDEKKIKKYSKALG 253
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
55-293 3.43e-107

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: 317.64  E-value: 3.43e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249  55 FPQGTIQNHLAEE--CRIHDLFLSFDDTPLGAASLAQVHKAVLHDGRTVAVKVQHPKVQAQSSKDILLMEVLVLAVKQLF 132
Cdd:pfam03109   9 FPFEQAKKVIEEElgAPVEEIFAEFDEEPIAAASIAQVHRARLKDGEEVAVKVQRPGVKKRIRSDLLLLRFLAKVAKRFF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249 133 PDF-EFMWLVDEAKKNLPLELDFLNEGRNAEKVAHMLRHFDFLKVPQIHWELSTKRVLLMEFVEGGQVNDRAYMEKNQID 211
Cdd:pfam03109  89 PGFrRLDWLVDEFRKSLPQELDFLREAANAEKFRENFADDPDVYVPKVYWELTTERVLTMEYVDGIKIDDLDALSEAGID 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249 212 VNEISCHLGKMYSEMIFVNGFVHCDPHPGNVLVRKRPdtgkaEIVLLDHGLYQVLTEEFRLDYCHLWQSLIWTDMDGLKQ 291
Cdd:pfam03109 169 RKEIARRLVELFLEQIFRDGFFHADPHPGNILVRKDG-----RIVLLDFGLMGRLDEKFRRLYAELLLALVNRDYKRVAE 243

                  ..
gi 1907089249 292 YS 293
Cdd:pfam03109 244 ML 245
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
55-362 1.95e-66

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: 220.46  E-value: 1.95e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249  55 FPQGTIQNHLAEE--CRIHDLFLSFDDTPLGAASLAQVHKAVLHDGRTVAVKVQHPKVQAQSSKDILLMEVLVLAVKQLF 132
Cdd:COG0661    98 FPFEEVRAVIEEElgRPLEELFAEFDPEPLAAASIGQVHRARLKDGREVAVKVQRPGIEEAIEADLRILRRLARLLERLS 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249 133 PD---FEFMWLVDEAKKNLPLELDFLNEGRNAEKVAHMLRHFDFLKVPQIHWELSTKRVLLMEFVEGGQVNDRAYMEKNQ 209
Cdd:COG0661   178 PEgrrLDPVEVVDEFARSLLEELDYRREAANAERFRRNFADDPDVYVPKVYWELSTRRVLTMEWIDGIKISDLEALDAAG 257
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249 210 IDVNEISCHLGKMYSEMIFVNGFVHCDPHPGNVLVRkrpDTGKaeIVLLDHGLYQVLTEEFRLDYCHLWQSLIWTDMDGL 289
Cdd:COG0661   258 IDRKRLAERLVRAFLRQVFRDGFFHADPHPGNIFVL---PDGR--LVLLDFGMVGRLDPETREGLAELLLALLNRDYDRV 332
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907089249 290 KQYSQRLGA----ADLYPLfacmltARSWDSVKQGIGQAPVSATEDSEIRNNAAcylpEISQLLN-HVPRQMLLILKT 362
Cdd:COG0661   333 AEALLELGFvppdTDVDEL------ERALRAVLEPYFGKPLKDISFGELLLELF----ELARRFPlRLPPELVLLQRT 400
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
59-271 1.63e-50

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: 177.10  E-value: 1.63e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249  59 TIQNHLAeeCRIHDLFLSFDDTPLGAASLAQVHKAVLHDGRTVAVKVQHPKVQAQSSKDILLMEVLVLAVKQLFPDF--- 135
Cdd:TIGR01982 104 VIEAALG--GPLEELFAEFEEKPLAAASIAQVHRARLVDGKEVAVKVLRPGIEKTIAADIALLYRLARIVERLSPDSrrl 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249 136 EFMWLVDEAKKNLPLELDFLNEGRNAEKVAHMLRHFDFLKVPQIHWELSTKRVLLMEFVEGGQVNDRAYMEKNQIDVNEI 215
Cdd:TIGR01982 182 RPTEVVKEFEKTLRRELDLRREAANASELGENFKNDPGVYVPEVYWDRTSERVLTMEWIDGIPLSDIAALDEAGLDRKAL 261
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907089249 216 SCHLGKMYSEMIFVNGFVHCDPHPGNVLVRKRPdtgkaEIVLLDHGLYQVLTEEFR 271
Cdd:TIGR01982 262 AENLARSFLNQVLRDGFFHADLHPGNIFVLKDG-----KIIALDFGIVGRLSEEDR 312
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
68-274 2.32e-31

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 126.17  E-value: 2.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249  68 CRIHDLFLSFDDTPLGAASLAQVHKAVLHD-GRTVAVKVQHPKVQAQSSKDILLMEVLVLAVKQLFPDF------EfmwL 140
Cdd:PRK04750  113 GPVEEWFDDFDIKPLASASIAQVHFARLKDnGREVVVKVLRPDILPVIDADLALMYRLARWVERLLPDGrrlkprE---V 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249 141 VDEAKKNLPLELDFLNEGRNAekvAHMLRHF---DFLKVPQIHWELSTKRVLLMEFVEGGQVNDRAYMEKNQIDVneisc 217
Cdd:PRK04750  190 VAEFEKTLHDELDLMREAANA---SQLRRNFedsDMLYVPEVYWDYCSETVMVMERMYGIPVSDVAALRAAGTDM----- 261
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907089249 218 hlgKMYSEM--------IFVNGFVHCDPHPGNVLVRKRPDTGKAEIVlLDHGLYQVLTEE------------FRLDY 274
Cdd:PRK04750  262 ---KLLAERgvevfftqVFRDGFFHADMHPGNIFVSYDPPENPRYIA-LDFGIVGSLNKEdkrylaenflafFNRDY 334
 
Name Accession Description Interval E-value
ADCK1-like cd13969
aarF domain containing kinase 1 and similar proteins; This subfamily is composed of ...
68-297 8.00e-139

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: 398.40  E-value: 8.00e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249  68 CRIHDLFLSFDDTPLGAASLAQVHKAVLHDGRTVAVKVQHPKVQAQSSKDILLMEVLVLAVKQLFPDFEFMWLVDEAKKN 147
Cdd:cd13969    24 KPPEELFSEFDEEPIASASLAQVHKAKLKDGEEVAVKVQHPDLRKQFAGDLATMEFLVNLVEKLFPDFPFSWLVDELKKN 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249 148 LPLELDFLNEGRNAEKVAHMLRHFDFLKVPQIHWELSTKRVLLMEFVEGGQVNDRAYMEKNQIDVNEISCHLGKMYSEMI 227
Cdd:cd13969   104 LPKELDFLNEARNAERCAKLFKHRPDVYVPKVYWDLSSKRVLTMEFIDGIKIDDVEALKKLGIDPKEVARLLSEAFAEMI 183
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249 228 FVNGFVHCDPHPGNVLVRKRPDTGKAEIVLLDHGLYQVLTEEFRLDYCHLWQSLIWTDMDGLKQYSQRLG 297
Cdd:cd13969   184 FVHGFVHCDPHPGNLLVRKNPGPGKPQIVLLDHGLYRELDEEFRLNYCRLWKALILGDEKKIKKYSKALG 253
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
55-293 3.43e-107

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: 317.64  E-value: 3.43e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249  55 FPQGTIQNHLAEE--CRIHDLFLSFDDTPLGAASLAQVHKAVLHDGRTVAVKVQHPKVQAQSSKDILLMEVLVLAVKQLF 132
Cdd:pfam03109   9 FPFEQAKKVIEEElgAPVEEIFAEFDEEPIAAASIAQVHRARLKDGEEVAVKVQRPGVKKRIRSDLLLLRFLAKVAKRFF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249 133 PDF-EFMWLVDEAKKNLPLELDFLNEGRNAEKVAHMLRHFDFLKVPQIHWELSTKRVLLMEFVEGGQVNDRAYMEKNQID 211
Cdd:pfam03109  89 PGFrRLDWLVDEFRKSLPQELDFLREAANAEKFRENFADDPDVYVPKVYWELTTERVLTMEYVDGIKIDDLDALSEAGID 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249 212 VNEISCHLGKMYSEMIFVNGFVHCDPHPGNVLVRKRPdtgkaEIVLLDHGLYQVLTEEFRLDYCHLWQSLIWTDMDGLKQ 291
Cdd:pfam03109 169 RKEIARRLVELFLEQIFRDGFFHADPHPGNILVRKDG-----RIVLLDFGLMGRLDEKFRRLYAELLLALVNRDYKRVAE 243

                  ..
gi 1907089249 292 YS 293
Cdd:pfam03109 244 ML 245
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
70-282 7.22e-76

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: 237.39  E-value: 7.22e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249  70 IHDLFLSFDDTPLGAASLAQVHKAVLHDGRTVAVKVQHPKVQAQSSKDILLMEVLVLAVKQLFPD---FEFMWLVDEAKK 146
Cdd:cd05121    26 LEEVFAEFDPEPLAAASIAQVHRARLKDGREVAVKVQRPGIEEIIEADLRILRRLARLLERLSPLlrrLDLVAIVDEFAR 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249 147 NLPLELDFLNEGRNAEKVAHMLRHFDFLKVPQIHWELSTKRVLLMEFVEGGQVNDRAYMEKNQIDVNEISCHLGKMYSEM 226
Cdd:cd05121   106 SLLEELDFRREARNAERFRKNLKDSPDVYVPKVYPELSTRRVLVMEYIDGVKLTDLEALRAAGIDRKELARRLVDAYLKQ 185
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907089249 227 IFVNGFVHCDPHPGNVLVRKRpdtGKaeIVLLDHGLYQVLTEEFRLDYCHLWQSLI 282
Cdd:cd05121   186 IFEDGFFHADPHPGNILVLPD---GR--IALLDFGMVGRLDPETREALADLLLALV 236
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
55-362 1.95e-66

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: 220.46  E-value: 1.95e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249  55 FPQGTIQNHLAEE--CRIHDLFLSFDDTPLGAASLAQVHKAVLHDGRTVAVKVQHPKVQAQSSKDILLMEVLVLAVKQLF 132
Cdd:COG0661    98 FPFEEVRAVIEEElgRPLEELFAEFDPEPLAAASIGQVHRARLKDGREVAVKVQRPGIEEAIEADLRILRRLARLLERLS 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249 133 PD---FEFMWLVDEAKKNLPLELDFLNEGRNAEKVAHMLRHFDFLKVPQIHWELSTKRVLLMEFVEGGQVNDRAYMEKNQ 209
Cdd:COG0661   178 PEgrrLDPVEVVDEFARSLLEELDYRREAANAERFRRNFADDPDVYVPKVYWELSTRRVLTMEWIDGIKISDLEALDAAG 257
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249 210 IDVNEISCHLGKMYSEMIFVNGFVHCDPHPGNVLVRkrpDTGKaeIVLLDHGLYQVLTEEFRLDYCHLWQSLIWTDMDGL 289
Cdd:COG0661   258 IDRKRLAERLVRAFLRQVFRDGFFHADPHPGNIFVL---PDGR--LVLLDFGMVGRLDPETREGLAELLLALLNRDYDRV 332
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907089249 290 KQYSQRLGA----ADLYPLfacmltARSWDSVKQGIGQAPVSATEDSEIRNNAAcylpEISQLLN-HVPRQMLLILKT 362
Cdd:COG0661   333 AEALLELGFvppdTDVDEL------ERALRAVLEPYFGKPLKDISFGELLLELF----ELARRFPlRLPPELVLLQRT 400
ABC1_ADCK3 cd13970
Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This ...
72-297 4.41e-57

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: 188.87  E-value: 4.41e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249  72 DLFLSFDDTPLGAASLAQVHKAVLHDGRTVAVKVQHPKVqAQS--SkDILLMEVLVLAVKQLFPDFEFMWLVDEAKKNLP 149
Cdd:cd13970    32 ELFAEFDEEPFAAASIGQVHRATLKDGREVAVKVQYPGV-AESidS-DLNNLRRLLKLTGLLPKGLDLDALIAELREELL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249 150 LELDFLNEGRNAEKVAHMLRHFDFLKVPQIHWELSTKRVLLMEFVEGGQVNDRAYMEknQIDVNEISCHLGKMYSEMIFV 229
Cdd:cd13970   110 EECDYEREAANQRRFRELLADDPRFVVPEVIPELSTKRVLTTEFVDGVPLDEAADLS--QEERNRIGELLLRLCLRELFE 187
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907089249 230 NGFVHCDPHPGNVLVrkRPDTGKaeIVLLDHGLYQVLTEEFRLDYCHLWQSLIWTDMDGLKQYSQRLG 297
Cdd:cd13970   188 FGFMQTDPNPGNFLY--DPEDGR--LGLLDFGAVREYPPEFVDGYRRLVRAALEGDREALLEASVELG 251
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
59-271 1.63e-50

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: 177.10  E-value: 1.63e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249  59 TIQNHLAeeCRIHDLFLSFDDTPLGAASLAQVHKAVLHDGRTVAVKVQHPKVQAQSSKDILLMEVLVLAVKQLFPDF--- 135
Cdd:TIGR01982 104 VIEAALG--GPLEELFAEFEEKPLAAASIAQVHRARLVDGKEVAVKVLRPGIEKTIAADIALLYRLARIVERLSPDSrrl 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249 136 EFMWLVDEAKKNLPLELDFLNEGRNAEKVAHMLRHFDFLKVPQIHWELSTKRVLLMEFVEGGQVNDRAYMEKNQIDVNEI 215
Cdd:TIGR01982 182 RPTEVVKEFEKTLRRELDLRREAANASELGENFKNDPGVYVPEVYWDRTSERVLTMEWIDGIPLSDIAALDEAGLDRKAL 261
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907089249 216 SCHLGKMYSEMIFVNGFVHCDPHPGNVLVRKRPdtgkaEIVLLDHGLYQVLTEEFR 271
Cdd:TIGR01982 262 AENLARSFLNQVLRDGFFHADLHPGNIFVLKDG-----KIIALDFGIVGRLSEEDR 312
UbiB cd13972
Ubiquinone biosynthetic protein UbiB; UbiB is the prokaryotic homolog of yeast Abc1p and human ...
68-261 7.07e-46

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: 159.29  E-value: 7.07e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249  68 CRIHDLFLSFDDTPLGAASLAQVHKAVLHDGRTVAVKVQHPKVQAQSSKDILLMEVLVLAVKQLFPDFEFMWL---VDEA 144
Cdd:cd13972    24 KPLDALFSDFDEEPVAAASIAQVHKARLLDGREVAVKVLRPGIEKRIERDLELLRFLARLAERLLPEARRLRPvevVKEF 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249 145 KKNLPLELDFLNEGRNAEKVAHMLRHFDFLKVPQIHWELSTKRVLLMEFVEGGQVNDRAYMEKNQIDVNEISCHLGKMYS 224
Cdd:cd13972   104 ARSLLLELDLRLEAANASELRENFLDDPGFYVPEVYWELTSKNVLTMEWIDGIPISDIEALDAAGIDRKALAERLVEIFF 183
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907089249 225 EMIFVNGFVHCDPHPGNVLVRKRPDtgkaeIVLLDHG 261
Cdd:cd13972   184 RQVFRDGFFHADMHPGNIFVDPNGR-----IIAVDFG 215
ADCK2-like cd13971
aarF domain containing kinase 2 and similar proteins; This subfamily is composed of ...
68-269 2.42e-33

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: 127.34  E-value: 2.42e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249  68 CRIHDLFLSFDDTPLGAASLAQVHKAVLHD--------GRTVAVKVQHPKVQAQSSKDILLMEVLVLAVKQLFPdfeFMW 139
Cdd:cd13971    24 KDWEDIFEEFDEEPIGSGSIAQVHRAKLKPdyggdgggPRVVAVKVLHPGVREQIERDLAILRLFAKLLEAIPP---LRW 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249 140 L-----VDEAKKNLPLELDFLNEGRNAEKVAHMLRHFDFLKVPQIHWELSTKRVLLMEFVEGGQVNdRAYMEKNQIDVNE 214
Cdd:cd13971   101 LslpesVEQFASLMLRQLDLRVEAANLERFRENFKDRKDVSFPKPLYPLVTEEVLVETFEEGVPIS-RTVLAHGGEPLKR 179
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907089249 215 ISCHLG-KMYSEMIFVNGFVHCDPHPGNVLVR------------KRPDTGKAEIVLLDHGLYQVLTEE 269
Cdd:cd13971   180 KLARIGlDAFLKMLFVDNFVHGDLHPGNILVRfndsnrpsllvsLDARGSPPRLVFLDAGLVTELSPQ 247
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
68-274 2.32e-31

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 126.17  E-value: 2.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249  68 CRIHDLFLSFDDTPLGAASLAQVHKAVLHD-GRTVAVKVQHPKVQAQSSKDILLMEVLVLAVKQLFPDF------EfmwL 140
Cdd:PRK04750  113 GPVEEWFDDFDIKPLASASIAQVHFARLKDnGREVVVKVLRPDILPVIDADLALMYRLARWVERLLPDGrrlkprE---V 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249 141 VDEAKKNLPLELDFLNEGRNAekvAHMLRHF---DFLKVPQIHWELSTKRVLLMEFVEGGQVNDRAYMEKNQIDVneisc 217
Cdd:PRK04750  190 VAEFEKTLHDELDLMREAANA---SQLRRNFedsDMLYVPEVYWDYCSETVMVMERMYGIPVSDVAALRAAGTDM----- 261
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907089249 218 hlgKMYSEM--------IFVNGFVHCDPHPGNVLVRKRPDTGKAEIVlLDHGLYQVLTEE------------FRLDY 274
Cdd:PRK04750  262 ---KLLAERgvevfftqVFRDGFFHADMHPGNIFVSYDPPENPRYIA-LDFGIVGSLNKEdkrylaenflafFNRDY 334
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
174-264 2.88e-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: 2.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249 174 LKVPQIHWELSTKRVLLMEFVEGGQVNDR-AYMEKNQIDVNEISCHLGKMYSemifvNGFVHCDPHPGNVLVRKRpdtgk 252
Cdd:COG3642    18 VPVPKVLDVDPDDADLVMEYIEGETLADLlEEGELPPELLRELGRLLARLHR-----AGIVHGDLTTSNILVDDG----- 87
                          90
                  ....*....|..
gi 1907089249 253 aEIVLLDHGLYQ 264
Cdd:COG3642    88 -GVYLIDFGLAR 98
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
188-262 3.30e-04

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


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 42.95  E-value: 3.30e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907089249 188 VLLMEFVEGGQVNDraYMEKNQIDVNEISCHLGKMYSemifvNGFVHCDPHPGNVLVRKRpdtgkaEIVLLDHGL 262
Cdd:PRK09605  412 TIVMEYIGGKDLKD--VLEGNPELVRKVGEIVAKLHK-----AGIVHGDLTTSNFIVRDD------RLYLIDFGL 473
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
157-245 2.00e-03

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: 38.82  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249 157 EGRNAEKVAH-MLRHFDFLKVPQIH--WELSTKRVLLMEFVEGGQVNDRAY-MEKNQIDVneISCHLGKMYSEM--IFVN 230
Cdd:cd05120    34 KDLEKEAAMLqLLAGKLSLPVPKVYgfGESDGWEYLLMERIEGETLSEVWPrLSEEEKEK--IADQLAEILAALhrIDSS 111
                          90
                  ....*....|....*
gi 1907089249 231 GFVHCDPHPGNVLVR 245
Cdd:cd05120   112 VLTHGDLHPGNILVK 126
PRK14879 PRK14879
Kae1-associated kinase Bud32;
188-262 4.69e-03

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 38.35  E-value: 4.69e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907089249 188 VLLMEFVEGGQVNDraYMEKNQIDVNEISCHLG----KMYSemifvNGFVHCDPHPGNVLVRKRpdtgkaEIVLLDHGL 262
Cdd:PRK14879   75 IIVMEYIEGEPLKD--LINSNGMEELELSREIGrlvgKLHS-----AGIIHGDLTTSNMILSGG------KIYLIDFGL 140
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
180-268 5.41e-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: 38.46  E-value: 5.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249 180 HWELSTKRVLLMEFVEGGQVNDrAYMEKNQIDVNEISCHLGKMYSEMIFVN--GFVHCDPHPGNVLVRKRPDtGKAEIVL 257
Cdd:cd14095    66 EYDTDTELYLVMELVKGGDLFD-AITSSTKFTERDASRMVTDLAQALKYLHslSIVHRDIKPENLLVVEHED-GSKSLKL 143
                          90
                  ....*....|.
gi 1907089249 258 LDHGLYQVLTE 268
Cdd:cd14095   144 ADFGLATEVKE 154
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
147-261 5.92e-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: 37.04  E-value: 5.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089249 147 NLPLELDFLNEGRNAEKVAHMLRHFDFLKVPQIHwelSTKRVLLMEFVEGGQVNDRAYMEKNQIDVNEISCHLGKMYSEM 226
Cdd:cd13968    30 NNEEGEDLESEMDILRRLKGLELNIPKVLVTEDV---DGPNILLMELVKGGTLIAYTQEEELDEKDVESIMYQLAECMRL 106
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907089249 227 IFVNGFVHCDPHPGNVLVRkrpDTGKaeIVLLDHG 261
Cdd:cd13968   107 LHSFHLIHRDLNNDNILLS---EDGN--VKLIDFG 136
 
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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