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Conserved domains on  [gi|1487193358|ref|NP_001353417|]
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aarF domain-containing protein kinase 1 isoform f [Homo sapiens]

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 ...
117-299 1.40e-105

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: 312.50  E-value: 1.40e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 117 VLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVL 196
Cdd:cd13969     1 VLQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVHKAKLKDGEEVAVKVQHPDLRKQFAGDLATMEFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 197 VLAVKQLFPEFEFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKI---------------------------- 248
Cdd:cd13969    81 VNLVEKLFPDFPFSWLVDELKKNLPKELDFLNEARNAERCAKLFKHRPDVYVpkvywdlsskrvltmefidgikiddvea 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1487193358 249 -----------SRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPGTGKAEIVLLDHGLYQDL 299
Cdd:cd13969   161 lkklgidpkevARLLSEAFAEMIFVHGFVHCDPHPGNLLVRKNPGPGKPQIVLLDHGLYREL 222
 
Name Accession Description Interval E-value
ADCK1-like cd13969
aarF domain containing kinase 1 and similar proteins; This subfamily is composed of ...
117-299 1.40e-105

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: 312.50  E-value: 1.40e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 117 VLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVL 196
Cdd:cd13969     1 VLQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVHKAKLKDGEEVAVKVQHPDLRKQFAGDLATMEFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 197 VLAVKQLFPEFEFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKI---------------------------- 248
Cdd:cd13969    81 VNLVEKLFPDFPFSWLVDELKKNLPKELDFLNEARNAERCAKLFKHRPDVYVpkvywdlsskrvltmefidgikiddvea 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1487193358 249 -----------SRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPGTGKAEIVLLDHGLYQDL 299
Cdd:cd13969   161 lkklgidpkevARLLSEAFAEMIFVHGFVHCDPHPGNLLVRKNPGPGKPQIVLLDHGLYREL 222
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
118-302 6.43e-79

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: 244.07  E-value: 6.43e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 118 LHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVLV 197
Cdd:pfam03109   2 LQDRAPPFPFEQAKKVIEEELGAPVEEIFAEFDEEPIAAASIAQVHRARLKDGEEVAVKVQRPGVKKRIRSDLLLLRFLA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 198 LAVKQLFPEF-EFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLK----------------------------- 247
Cdd:pfam03109  82 KVAKRFFPGFrRLDWLVDEFRKSLPQELDFLREAANAEKFRENFADDPDVYvpkvywelttervltmeyvdgikiddlda 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1487193358 248 ----------ISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPgtgkaEIVLLDHGLYQDLEIR 302
Cdd:pfam03109 162 lseagidrkeIARRLVELFLEQIFRDGFFHADPHPGNILVRKDG-----RIVLLDFGLMGRLDEK 221
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
71-294 2.76e-57

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: 195.42  E-value: 2.76e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358  71 RSKVHLRSARRLCELCCANRGTFIKVGQHLGALDYLLPEEYTSTLKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFD 150
Cdd:COG0661    44 REELRRRRAERLRLALEELGPTFIKLGQLLSTRPDLLPPEYAEELAKLQDRVPPFPFEEVRAVIEEELGRPLEELFAEFD 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 151 DTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVLVLAVKQLFPE---FEFMWLVDEAKKNLPLELDFL 227
Cdd:COG0661   124 PEPLAAASIGQVHRARLKDGREVAVKVQRPGIEEAIEADLRILRRLARLLERLSPEgrrLDPVEVVDEFARSLLEELDYR 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 228 NEGRNAEKVSQMLRHFDFL---------------------------------------KISRHLGKMYSEMIFVNGFVHC 268
Cdd:COG0661   204 REAANAERFRRNFADDPDVyvpkvywelstrrvltmewidgikisdlealdaagidrkRLAERLVRAFLRQVFRDGFFHA 283
                         250       260
                  ....*....|....*....|....*.
gi 1487193358 269 DPHPGNVLVRKhpgTGKaeIVLLDHG 294
Cdd:COG0661   284 DPHPGNIFVLP---DGR--LVLLDFG 304
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
92-295 1.09e-41

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: 152.45  E-value: 1.09e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358  92 TFIKVGQHLGALDYLLPEEYTSTLKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGR 171
Cdd:TIGR01982  63 TFIKFGQTLSTRADLLPADIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEEKPLAAASIAQVHRARLVDGK 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 172 TVAVKVQHPKVRAQSSKDILLMEVLVLAVKQLFPEF---EFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKI 248
Cdd:TIGR01982 143 EVAVKVLRPGIEKTIAADIALLYRLARIVERLSPDSrrlRPTEVVKEFEKTLRRELDLRREAANASELGENFKNDPGVYV 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 249 ---------------------------------------SRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPgtgkaEIV 289
Cdd:TIGR01982 223 pevywdrtservltmewidgiplsdiaaldeagldrkalAENLARSFLNQVLRDGFFHADLHPGNIFVLKDG-----KII 297

                  ....*.
gi 1487193358 290 LLDHGL 295
Cdd:TIGR01982 298 ALDFGI 303
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
93-283 2.66e-24

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 104.99  E-value: 2.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358  93 FIKVGQHLGALDYLLPEEYTSTLKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHD-GR 171
Cdd:PRK04750   66 FVKFGQMLSTRRDLFPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQVHFARLKDnGR 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 172 TVAVKVQHPKVRAQSSKDILLMEVLVLAVKQLFPEF------EfmwLVDEAKKNLPLELDFLNEGRNAekvSQMLRHF-- 243
Cdd:PRK04750  146 EVVVKVLRPDILPVIDADLALMYRLARWVERLLPDGrrlkprE---VVAEFEKTLHDELDLMREAANA---SQLRRNFed 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 244 ----------------------------------------DFLKISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPGT 283
Cdd:PRK04750  220 sdmlyvpevywdycsetvmvmermygipvsdvaalraagtDMKLLAERGVEVFFTQVFRDGFFHADMHPGNIFVSYDPPE 299
 
Name Accession Description Interval E-value
ADCK1-like cd13969
aarF domain containing kinase 1 and similar proteins; This subfamily is composed of ...
117-299 1.40e-105

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: 312.50  E-value: 1.40e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 117 VLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVL 196
Cdd:cd13969     1 VLQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVHKAKLKDGEEVAVKVQHPDLRKQFAGDLATMEFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 197 VLAVKQLFPEFEFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKI---------------------------- 248
Cdd:cd13969    81 VNLVEKLFPDFPFSWLVDELKKNLPKELDFLNEARNAERCAKLFKHRPDVYVpkvywdlsskrvltmefidgikiddvea 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1487193358 249 -----------SRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPGTGKAEIVLLDHGLYQDL 299
Cdd:cd13969   161 lkklgidpkevARLLSEAFAEMIFVHGFVHCDPHPGNLLVRKNPGPGKPQIVLLDHGLYREL 222
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
118-302 6.43e-79

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: 244.07  E-value: 6.43e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 118 LHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVLV 197
Cdd:pfam03109   2 LQDRAPPFPFEQAKKVIEEELGAPVEEIFAEFDEEPIAAASIAQVHRARLKDGEEVAVKVQRPGVKKRIRSDLLLLRFLA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 198 LAVKQLFPEF-EFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLK----------------------------- 247
Cdd:pfam03109  82 KVAKRFFPGFrRLDWLVDEFRKSLPQELDFLREAANAEKFRENFADDPDVYvpkvywelttervltmeyvdgikiddlda 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1487193358 248 ----------ISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPgtgkaEIVLLDHGLYQDLEIR 302
Cdd:pfam03109 162 lseagidrkeIARRLVELFLEQIFRDGFFHADPHPGNILVRKDG-----RIVLLDFGLMGRLDEK 221
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
118-295 2.49e-59

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: 193.48  E-value: 2.49e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 118 LHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVLV 197
Cdd:cd05121     2 LQDDVPPFPFEEVRKIIEEELGRPLEEVFAEFDPEPLAAASIAQVHRARLKDGREVAVKVQRPGIEEIIEADLRILRRLA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 198 LAVKQLFPE---FEFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFL---------------------------- 246
Cdd:cd05121    82 RLLERLSPLlrrLDLVAIVDEFARSLLEELDFRREARNAERFRKNLKDSPDVyvpkvypelstrrvlvmeyidgvkltdl 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 247 -----------KISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHpgtGKaeIVLLDHGL 295
Cdd:cd05121   162 ealraagidrkELARRLVDAYLKQIFEDGFFHADPHPGNILVLPD---GR--IALLDFGM 216
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
71-294 2.76e-57

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: 195.42  E-value: 2.76e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358  71 RSKVHLRSARRLCELCCANRGTFIKVGQHLGALDYLLPEEYTSTLKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFD 150
Cdd:COG0661    44 REELRRRRAERLRLALEELGPTFIKLGQLLSTRPDLLPPEYAEELAKLQDRVPPFPFEEVRAVIEEELGRPLEELFAEFD 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 151 DTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVLVLAVKQLFPE---FEFMWLVDEAKKNLPLELDFL 227
Cdd:COG0661   124 PEPLAAASIGQVHRARLKDGREVAVKVQRPGIEEAIEADLRILRRLARLLERLSPEgrrLDPVEVVDEFARSLLEELDYR 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 228 NEGRNAEKVSQMLRHFDFL---------------------------------------KISRHLGKMYSEMIFVNGFVHC 268
Cdd:COG0661   204 REAANAERFRRNFADDPDVyvpkvywelstrrvltmewidgikisdlealdaagidrkRLAERLVRAFLRQVFRDGFFHA 283
                         250       260
                  ....*....|....*....|....*.
gi 1487193358 269 DPHPGNVLVRKhpgTGKaeIVLLDHG 294
Cdd:COG0661   284 DPHPGNIFVLP---DGR--LVLLDFG 304
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
92-295 1.09e-41

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: 152.45  E-value: 1.09e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358  92 TFIKVGQHLGALDYLLPEEYTSTLKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGR 171
Cdd:TIGR01982  63 TFIKFGQTLSTRADLLPADIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEEKPLAAASIAQVHRARLVDGK 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 172 TVAVKVQHPKVRAQSSKDILLMEVLVLAVKQLFPEF---EFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKI 248
Cdd:TIGR01982 143 EVAVKVLRPGIEKTIAADIALLYRLARIVERLSPDSrrlRPTEVVKEFEKTLRRELDLRREAANASELGENFKNDPGVYV 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 249 ---------------------------------------SRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPgtgkaEIV 289
Cdd:TIGR01982 223 pevywdrtservltmewidgiplsdiaaldeagldrkalAENLARSFLNQVLRDGFFHADLHPGNIFVLKDG-----KII 297

                  ....*.
gi 1487193358 290 LLDHGL 295
Cdd:TIGR01982 298 ALDFGI 303
ABC1_ADCK3 cd13970
Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This ...
115-324 6.31e-37

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: 134.95  E-value: 6.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 115 LKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLME 194
Cdd:cd13970     3 LARLRDSAPPMPWAQLEKVLEAELGEDWRELFAEFDEEPFAAASIGQVHRATLKDGREVAVKVQYPGVAESIDSDLNNLR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 195 VLVLAVKQLFPEFEFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFL---------------------------- 246
Cdd:cd13970    83 RLLKLTGLLPKGLDLDALIAELREELLEECDYEREAANQRRFRELLADDPRFvvpevipelstkrvlttefvdgvpldea 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 247 ---------KISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRkhPGTGKaeIVLLDHGLYQDLEiRNNAANYLPQISHLLN 317
Cdd:cd13970   163 adlsqeernRIGELLLRLCLRELFEFGFMQTDPNPGNFLYD--PEDGR--LGLLDFGAVREYP-PEFVDGYRRLVRAALE 237

                  ....*..
gi 1487193358 318 HVPRQML 324
Cdd:cd13970   238 GDREALL 244
UbiB cd13972
Ubiquinone biosynthetic protein UbiB; UbiB is the prokaryotic homolog of yeast Abc1p and human ...
126-294 9.74e-32

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: 120.77  E-value: 9.74e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 126 SMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVLVLAVKQLFP 205
Cdd:cd13972    10 SGKEARAIIEAELGKPLDALFSDFDEEPVAAASIAQVHKARLLDGREVAVKVLRPGIEKRIERDLELLRFLARLAERLLP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 206 EFEFMWL---VDEAKKNLPLELDFLNEGRNAekvSQMLRHF--------------------------------------- 243
Cdd:cd13972    90 EARRLRPvevVKEFARSLLLELDLRLEAANA---SELRENFlddpgfyvpevyweltsknvltmewidgipisdiealda 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1487193358 244 ---DFLKISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPGtgkaeIVLLDHG 294
Cdd:cd13972   167 agiDRKALAERLVEIFFRQVFRDGFFHADMHPGNIFVDPNGR-----IIAVDFG 215
ADCK2-like cd13971
aarF domain containing kinase 2 and similar proteins; This subfamily is composed of ...
118-309 8.74e-28

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: 111.55  E-value: 8.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 118 LHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHD--------GRTVAVKVQHPKVRAQSSKD 189
Cdd:cd13971     2 LHSNAPPHSWAHTERALEAAFGKDWEDIFEEFDEEPIGSGSIAQVHRAKLKPdyggdgggPRVVAVKVLHPGVREQIERD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 190 ILLMEVLVLAVKQLFPefeFMWL-----VDEAKKNLPLELDFLNEGRNAEKVSQ-------------------------- 238
Cdd:cd13971    82 LAILRLFAKLLEAIPP---LRWLslpesVEQFASLMLRQLDLRVEAANLERFREnfkdrkdvsfpkplyplvteevlvet 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 239 ------MLRHFDF---LKISRHLGKM----YSEMIFVNGFVHCDPHPGNVLVRKHPGTGKA------------EIVLLDH 293
Cdd:cd13971   159 feegvpISRTVLAhggEPLKRKLARIgldaFLKMLFVDNFVHGDLHPGNILVRFNDSNRPSllvsldargsppRLVFLDA 238
                         250
                  ....*....|....*.
gi 1487193358 294 GLYQDLEiRNNAANYL 309
Cdd:cd13971   239 GLVTELS-PQDRRNFI 253
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
93-283 2.66e-24

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 104.99  E-value: 2.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358  93 FIKVGQHLGALDYLLPEEYTSTLKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHD-GR 171
Cdd:PRK04750   66 FVKFGQMLSTRRDLFPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQVHFARLKDnGR 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 172 TVAVKVQHPKVRAQSSKDILLMEVLVLAVKQLFPEF------EfmwLVDEAKKNLPLELDFLNEGRNAekvSQMLRHF-- 243
Cdd:PRK04750  146 EVVVKVLRPDILPVIDADLALMYRLARWVERLLPDGrrlkprE---VVAEFEKTLHDELDLMREAANA---SQLRRNFed 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 244 ----------------------------------------DFLKISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPGT 283
Cdd:PRK04750  220 sdmlyvpevywdycsetvmvmermygipvsdvaalraagtDMKLLAERGVEVFFTQVFRDGFFHADMHPGNIFVSYDPPE 299
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
154-295 2.36e-06

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK 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: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 48.81  E-value: 2.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 154 LGTASLAQVHKAVLHDGRTVAVKVQHPKvRAQSSKDILLMEVLVLA-------VKQL--FPEFEFMWLVDEAKKNLPLEl 224
Cdd:cd14066     1 IGSGGFGTVYKGVLENGTVVAVKRLNEM-NCAASKKEFLTELEMLGrlrhpnlVRLLgyCLESDEKLLVYEYMPNGSLE- 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1487193358 225 DFLNEGRNAEKVSQMLRhfdfLKISRHLGK----MYSEMIFVngFVHCDPHPGNVLVRKHPgtgkaEIVLLDHGL 295
Cdd:cd14066    79 DRLHCHKGSPPLPWPQR----LKIAKGIARgleyLHEECPPP--IIHGDIKSSNILLDEDF-----EPKLTDFGL 142
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
154-295 6.45e-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: 6.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 154 LGTASLAQVHKAV-LHDGRTVAVKVQHPKVRAQSSKDiLLMEVLVLA---------VKQLFPEFEFMWLVDE--AKKNLp 221
Cdd:cd00180     1 LGKGSFGKVYKARdKETGKKVAVKVIPKEKLKKLLEE-LLREIEILKklnhpnivkLYDVFETENFLYLVMEycEGGSL- 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1487193358 222 leLDFLNEgrNAEKVSQMLrhfdFLKISRHLGKMYsEMIFVNGFVHCDPHPGNVLVRKHPgtgkaEIVLLDHGL 295
Cdd:cd00180    79 --KDLLKE--NKGPLSEEE----ALSILRQLLSAL-EYLHSNGIIHRDLKPENILLDSDG-----TVKLADFGL 138
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
145-280 7.52e-03

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD 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: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 37.78  E-value: 7.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193358 145 LFQSFDDTPLGTASLAQVHKAVL-HDGRTVAVKVQHpKVRAQSSKDILLM-EVLVLA---------VKQLFPEFEFMWLV 213
Cdd:cd14082     2 LYQIFPDEVLGSGQFGIVYGGKHrKTGRDVAIKVID-KLRFPTKQESQLRnEVAILQqlshpgvvnLECMFETPERVFVV 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1487193358 214 DEAKKNLPLELDFLNE-GRNAEKVSQMLrhfdFLKISRHLGKMYSEMIfvngfVHCDPHPGNVLVRKH 280
Cdd:cd14082    81 MEKLHGDMLEMILSSEkGRLPERITKFL----VTQILVALRYLHSKNI-----VHCDLKPENVLLASA 139
 
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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