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Conserved domains on  [gi|1487193389|ref|NP_001353415|]
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aarF domain-containing protein kinase 1 isoform d [Homo sapiens]

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

EC:  2.7.-.-
Gene Ontology:  GO:0016020|GO:0006468|GO:0005524|GO:0004672
PubMed:  19614568|16244704|8081750

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 ...
 117-338 1.28e-137

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: 395.32  E-value: 1.28e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 117 VLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVL 196
Cdd:cd13969     1 VLQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVHKAKLKDGEEVAVKVQHPDLRKQFAGDLATMEFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 197 VLAVKQLFPEFEFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDY 276
Cdd:cd13969    81 VNLVEKLFPDFPFSWLVDELKKNLPKELDFLNEARNAERCAKLFKHRPDVYVPKVYWDLSSKRVLTMEFIDGIKIDDVEA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1487193389 277 MERNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPGTGKAEIVLLDHGLYQDL 338
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 ...
 117-338 1.28e-137

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: 395.32  E-value: 1.28e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 117 VLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVL 196
Cdd:cd13969     1 VLQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVHKAKLKDGEEVAVKVQHPDLRKQFAGDLATMEFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 197 VLAVKQLFPEFEFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDY 276
Cdd:cd13969    81 VNLVEKLFPDFPFSWLVDELKKNLPKELDFLNEARNAERCAKLFKHRPDVYVPKVYWDLSSKRVLTMEFIDGIKIDDVEA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1487193389 277 MERNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPGTGKAEIVLLDHGLYQDL 338
Cdd:cd13969   161 LKKLGIDPKEVARLLSEAFAEMIFVHGFVHCDPHPGNLLVRKNPGPGKPQIVLLDHGLYREL 222
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
 118-341 3.39e-108

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: 320.33  E-value: 3.39e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 118 LHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVLV 197
Cdd:pfam03109   2 LQDRAPPFPFEQAKKVIEEELGAPVEEIFAEFDEEPIAAASIAQVHRARLKDGEEVAVKVQRPGVKKRIRSDLLLLRFLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 198 LAVKQLFPEF-EFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDY 276
Cdd:pfam03109  82 KVAKRFFPGFrRLDWLVDEFRKSLPQELDFLREAANAEKFRENFADDPDVYVPKVYWELTTERVLTMEYVDGIKIDDLDA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1487193389 277 MERNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPgtgkaEIVLLDHGLYQDLEIR 341
Cdd:pfam03109 162 LSEAGIDRKEIARRLVELFLEQIFRDGFFHADPHPGNILVRKDG-----RIVLLDFGLMGRLDEK 221
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
 71-333 4.90e-82

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: 261.29  E-value: 4.90e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389  71 RSKVHLRSARRLCELCCANRGTFIKVGQHLGALDYLLPEEYTSTLKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFD 150
Cdd:COG0661    44 REELRRRRAERLRLALEELGPTFIKLGQLLSTRPDLLPPEYAEELAKLQDRVPPFPFEEVRAVIEEELGRPLEELFAEFD 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 151 DTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVLVLAVKQLFPE---FEFMWLVDEAKKNLPLELDFL 227
Cdd:COG0661   124 PEPLAAASIGQVHRARLKDGREVAVKVQRPGIEEAIEADLRILRRLARLLERLSPEgrrLDPVEVVDEFARSLLEELDYR 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 228 NEGRNAEKVSQMLRHFDFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDYMERNKIDVNEISRHLGKMYSEMIFVNGFVHC 307
Cdd:COG0661   204 REAANAERFRRNFADDPDVYVPKVYWELSTRRVLTMEWIDGIKISDLEALDAAGIDRKRLAERLVRAFLRQVFRDGFFHA 283

                         250       260
                  ....*....|....*....|....*.
gi 1487193389 308 DPHPGNVLVRKhpgTGKaeIVLLDHG 333
Cdd:COG0661   284 DPHPGNIFVLP---DGR--LVLLDFG 304
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
 92-334 2.96e-61

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: 205.61  E-value: 2.96e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389  92 TFIKVGQHLGALDYLLPEEYTSTLKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGR 171
Cdd:TIGR01982  63 TFIKFGQTLSTRADLLPADIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEEKPLAAASIAQVHRARLVDGK 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 172 TVAVKVQHPKVRAQSSKDILLMEVLVLAVKQLFPEF---EFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKV 248
Cdd:TIGR01982 143 EVAVKVLRPGIEKTIAADIALLYRLARIVERLSPDSrrlRPTEVVKEFEKTLRRELDLRREAANASELGENFKNDPGVYV 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 249 PRIHWDLSTERVLLMEFVDGGQVNDRDYMERNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPgtgkaEIV 328
Cdd:TIGR01982 223 PEVYWDRTSERVLTMEWIDGIPLSDIAALDEAGLDRKALAENLARSFLNQVLRDGFFHADLHPGNIFVLKDG-----KII 297


                  ....*.
gi 1487193389 329 LLDHGL 334
Cdd:TIGR01982 298 ALDFGI 303
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
 93-322 5.01e-41

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 153.52  E-value: 5.01e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389  93 FIKVGQHLGALDYLLPEEYTSTLKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHD-GR 171
Cdd:PRK04750   66 FVKFGQMLSTRRDLFPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQVHFARLKDnGR 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 172 TVAVKVQHPKVRAQSSKDILLMEVLVLAVKQLFPEF------EfmwLVDEAKKNLPLELDFLNEGRNAekvSQMLRHF-- 243
Cdd:PRK04750  146 EVVVKVLRPDILPVIDADLALMYRLARWVERLLPDGrrlkprE---VVAEFEKTLHDELDLMREAANA---SQLRRNFed 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 244 -DFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDYMERNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPGT 322
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 ...
 117-338 1.28e-137

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: 395.32  E-value: 1.28e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 117 VLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVL 196
Cdd:cd13969     1 VLQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVHKAKLKDGEEVAVKVQHPDLRKQFAGDLATMEFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 197 VLAVKQLFPEFEFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDY 276
Cdd:cd13969    81 VNLVEKLFPDFPFSWLVDELKKNLPKELDFLNEARNAERCAKLFKHRPDVYVPKVYWDLSSKRVLTMEFIDGIKIDDVEA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1487193389 277 MERNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPGTGKAEIVLLDHGLYQDL 338
Cdd:cd13969   161 LKKLGIDPKEVARLLSEAFAEMIFVHGFVHCDPHPGNLLVRKNPGPGKPQIVLLDHGLYREL 222
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
 118-341 3.39e-108

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: 320.33  E-value: 3.39e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 118 LHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVLV 197
Cdd:pfam03109   2 LQDRAPPFPFEQAKKVIEEELGAPVEEIFAEFDEEPIAAASIAQVHRARLKDGEEVAVKVQRPGVKKRIRSDLLLLRFLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 198 LAVKQLFPEF-EFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDY 276
Cdd:pfam03109  82 KVAKRFFPGFrRLDWLVDEFRKSLPQELDFLREAANAEKFRENFADDPDVYVPKVYWELTTERVLTMEYVDGIKIDDLDA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1487193389 277 MERNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPgtgkaEIVLLDHGLYQDLEIR 341
Cdd:pfam03109 162 LSEAGIDRKEIARRLVELFLEQIFRDGFFHADPHPGNILVRKDG-----RIVLLDFGLMGRLDEK 221
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
 118-334 3.19e-84

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: 258.96  E-value: 3.19e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 118 LHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVLV 197
Cdd:cd05121     2 LQDDVPPFPFEEVRKIIEEELGRPLEEVFAEFDPEPLAAASIAQVHRARLKDGREVAVKVQRPGIEEIIEADLRILRRLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 198 LAVKQLFPE---FEFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKVPRIHWDLSTERVLLMEFVDGGQVNDR 274
Cdd:cd05121    82 RLLERLSPLlrrLDLVAIVDEFARSLLEELDFRREARNAERFRKNLKDSPDVYVPKVYPELSTRRVLVMEYIDGVKLTDL 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 275 DYMERNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHpgtGKaeIVLLDHGL 334
Cdd:cd05121   162 EALRAAGIDRKELARRLVDAYLKQIFEDGFFHADPHPGNILVLPD---GR--IALLDFGM 216
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
 71-333 4.90e-82

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: 261.29  E-value: 4.90e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389  71 RSKVHLRSARRLCELCCANRGTFIKVGQHLGALDYLLPEEYTSTLKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFD 150
Cdd:COG0661    44 REELRRRRAERLRLALEELGPTFIKLGQLLSTRPDLLPPEYAEELAKLQDRVPPFPFEEVRAVIEEELGRPLEELFAEFD 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 151 DTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVLVLAVKQLFPE---FEFMWLVDEAKKNLPLELDFL 227
Cdd:COG0661   124 PEPLAAASIGQVHRARLKDGREVAVKVQRPGIEEAIEADLRILRRLARLLERLSPEgrrLDPVEVVDEFARSLLEELDYR 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 228 NEGRNAEKVSQMLRHFDFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDYMERNKIDVNEISRHLGKMYSEMIFVNGFVHC 307
Cdd:COG0661   204 REAANAERFRRNFADDPDVYVPKVYWELSTRRVLTMEWIDGIKISDLEALDAAGIDRKRLAERLVRAFLRQVFRDGFFHA 283

                         250       260
                  ....*....|....*....|....*.
gi 1487193389 308 DPHPGNVLVRKhpgTGKaeIVLLDHG 333
Cdd:COG0661   284 DPHPGNIFVLP---DGR--LVLLDFG 304
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
 92-334 2.96e-61

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: 205.61  E-value: 2.96e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389  92 TFIKVGQHLGALDYLLPEEYTSTLKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGR 171
Cdd:TIGR01982  63 TFIKFGQTLSTRADLLPADIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEEKPLAAASIAQVHRARLVDGK 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 172 TVAVKVQHPKVRAQSSKDILLMEVLVLAVKQLFPEF---EFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKV 248
Cdd:TIGR01982 143 EVAVKVLRPGIEKTIAADIALLYRLARIVERLSPDSrrlRPTEVVKEFEKTLRRELDLRREAANASELGENFKNDPGVYV 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 249 PRIHWDLSTERVLLMEFVDGGQVNDRDYMERNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPgtgkaEIV 328
Cdd:TIGR01982 223 PEVYWDRTSERVLTMEWIDGIPLSDIAALDEAGLDRKALAENLARSFLNQVLRDGFFHADLHPGNIFVLKDG-----KII 297


                  ....*.
gi 1487193389 329 LLDHGL 334
Cdd:TIGR01982 298 ALDFGI 303
ABC1_ADCK3 cd13970
Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This ...
 115-363 6.86e-54

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: 180.79  E-value: 6.86e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 115 LKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLME 194
Cdd:cd13970     3 LARLRDSAPPMPWAQLEKVLEAELGEDWRELFAEFDEEPFAAASIGQVHRATLKDGREVAVKVQYPGVAESIDSDLNNLR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 195 VLVLAVKQLFPEFEFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKVPRIHWDLSTERVLLMEFVDG---GQV 271
Cdd:cd13970    83 RLLKLTGLLPKGLDLDALIAELREELLEECDYEREAANQRRFRELLADDPRFVVPEVIPELSTKRVLTTEFVDGvplDEA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 272 NDRDYMERNKidvneISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRkhPGTGKaeIVLLDHGLYQDLEiRNNAANYLPQI 351
Cdd:cd13970   163 ADLSQEERNR-----IGELLLRLCLRELFEFGFMQTDPNPGNFLYD--PEDGR--LGLLDFGAVREYP-PEFVDGYRRLV 232

                         250
                  ....*....|..
gi 1487193389 352 SHLLNHVPRQML 363
Cdd:cd13970   233 RAALEGDREALL 244
UbiB cd13972
Ubiquinone biosynthetic protein UbiB; UbiB is the prokaryotic homolog of yeast Abc1p and human ...
 126-333 5.17e-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: 175.47  E-value: 5.17e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 126 SMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVLVLAVKQLFP 205
Cdd:cd13972    10 SGKEARAIIEAELGKPLDALFSDFDEEPVAAASIAQVHKARLLDGREVAVKVLRPGIEKRIERDLELLRFLARLAERLLP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 206 EFEFMWL---VDEAKKNLPLELDFLNEGRNAekvSQMLRHF---DFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDYMER 279
Cdd:cd13972    90 EARRLRPvevVKEFARSLLLELDLRLEAANA---SELRENFlddPGFYVPEVYWELTSKNVLTMEWIDGIPISDIEALDA 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1487193389 280 NKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPGtgkaeIVLLDHG 333
Cdd:cd13972   167 AGIDRKALAERLVEIFFRQVFRDGFFHADMHPGNIFVDPNGR-----IIAVDFG 215
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
 93-322 5.01e-41

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 153.52  E-value: 5.01e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389  93 FIKVGQHLGALDYLLPEEYTSTLKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHD-GR 171
Cdd:PRK04750   66 FVKFGQMLSTRRDLFPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQVHFARLKDnGR 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 172 TVAVKVQHPKVRAQSSKDILLMEVLVLAVKQLFPEF------EfmwLVDEAKKNLPLELDFLNEGRNAekvSQMLRHF-- 243
Cdd:PRK04750  146 EVVVKVLRPDILPVIDADLALMYRLARWVERLLPDGrrlkprE---VVAEFEKTLHDELDLMREAANA---SQLRRNFed 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 244 -DFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDYMERNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPGT 322
Cdd:PRK04750  220 sDMLYVPEVYWDYCSETVMVMERMYGIPVSDVAALRAAGTDMKLLAERGVEVFFTQVFRDGFFHADMHPGNIFVSYDPPE 299
ADCK2-like cd13971
aarF domain containing kinase 2 and similar proteins; This subfamily is composed of ...
 118-348 8.69e-37

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: 136.58  E-value: 8.69e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 118 LHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHD--------GRTVAVKVQHPKVRAQSSKD 189
Cdd:cd13971     2 LHSNAPPHSWAHTERALEAAFGKDWEDIFEEFDEEPIGSGSIAQVHRAKLKPdyggdgggPRVVAVKVLHPGVREQIERD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 190 ILLMEVLVLAVKQLFPefeFMWL-----VDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKVPRIHWDLSTERVLLME 264
Cdd:cd13971    82 LAILRLFAKLLEAIPP---LRWLslpesVEQFASLMLRQLDLRVEAANLERFRENFKDRKDVSFPKPLYPLVTEEVLVET 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 265 FVDGGQVNDRDYMERNkidvNEISRHLGKM----YSEMIFVNGFVHCDPHPGNVLVRKHPGTGKA------------EIV 328
Cdd:cd13971   159 FEEGVPISRTVLAHGG----EPLKRKLARIgldaFLKMLFVDNFVHGDLHPGNILVRFNDSNRPSllvsldargsppRLV 234

                         250       260
                  ....*....|....*....|
gi 1487193389 329 LLDHGLYQDLEiRNNAANYL 348
Cdd:cd13971   235 FLDAGLVTELS-PQDRRNFI 253
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 246-336 3.83e-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: 46.88  E-value: 3.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 246 LKVPRIHwDLSTER-VLLMEFVDGGQVndRDYMERNKID---VNEISRHLGKMYSemifvNGFVHCDPHPGNVLVRKHpg 321
Cdd:COG3642    18 VPVPKVL-DVDPDDaDLVMEYIEGETL--ADLLEEGELPpelLRELGRLLARLHR-----AGIVHGDLTTSNILVDDG-- 87

                          90
                  ....*....|....*
gi 1487193389 322 tgkaEIVLLDHGLYQ 336
Cdd:COG3642    88 ----GVYLIDFGLAR 98
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
258-334 3.89e-06

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


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 49.12  E-value: 3.89e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1487193389 258 ERVLLMEFVDGGQVndRDYMERNKIDVNEISRHLGKMYSemifvNGFVHCDPHPGNVLVRkhpgtgKAEIVLLDHGL 334
Cdd:PRK09605  410 EKTIVMEYIGGKDL--KDVLEGNPELVRKVGEIVAKLHK-----AGIVHGDLTTSNFIVR------DDRLYLIDFGL 473
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
 153-334 9.44e-05

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


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 44.11  E-value: 9.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 153 PLGTASLAQVHKAV-LHDGRTVAVKVQHPKVRAQsskdillmevlvlavkqlfpefefmwlvDEAKKnlplelDFLNEGR 231
Cdd:cd14014     7 LLGRGGMGEVYRARdTLLGRPVAIKVLRPELAED----------------------------EEFRE------RFLREAR 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 232 NAEKvsqmLRH------FDFLKVPRIHWdlstervLLMEFVDGGQVndRDYMERNK-IDVNEISRHLGKMYSEMIFV--N 302
Cdd:cd14014    53 ALAR----LSHpnivrvYDVGEDDGRPY-------IVMEYVEGGSL--ADLLRERGpLPPREALRILAQIADALAAAhrA 119

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1487193389 303 GFVHCDPHPGNVLVRKHPgtgkaEIVLLDHGL 334
Cdd:cd14014   120 GIVHRDIKPANILLTEDG-----RVKLTDFGI 146
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
153-334 2.84e-04

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 43.08  E-value: 2.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 153 PLGTASLAQVHKAV-LHDGRTVAVKVQHPKVRAQsskdillmevlvlavkqlfPEFefmwlvdeakknlpLELdFLNEGR 231
Cdd:COG0515    14 LLGRGGMGVVYLARdLRLGRPVALKVLRPELAAD-------------------PEA--------------RER-FRREAR 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 232 NAEKvsqmLRHFdflKVPRIHwDLSTER---VLLMEFVDGGQVndRDYMERNK-IDVNEISRHLGKMYSEMIFV--NGFV 305
Cdd:COG0515    60 ALAR----LNHP---NIVRVY-DVGEEDgrpYLVMEYVEGESL--ADLLRRRGpLPPAEALRILAQLAEALAAAhaAGIV 129

                         170       180
                  ....*....|....*....|....*....
gi 1487193389 306 HCDPHPGNVLVRKhpgTGkaEIVLLDHGL 334
Cdd:COG0515   130 HRDIKPANILLTP---DG--RVKLIDFGI 153
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 238-319 3.55e-04

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 41.13  E-value: 3.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 238 QMLRHFDFLKVPRIH--WDLSTERVLLMEFVDGgQVNDRDYMERNKIDVNEISRHLGKMYSEM--IFVNGFVHCDPHPGN 313
Cdd:cd05120    44 QLLAGKLSLPVPKVYgfGESDGWEYLLMERIEG-ETLSEVWPRLSEEEKEKIADQLAEILAALhrIDSSVLTHGDLHPGN 122


                  ....*.
gi 1487193389 314 VLVRKH 319
Cdd:cd05120   123 ILVKPD 128
PRK14879 PRK14879
Kae1-associated kinase Bud32;
246-334 2.10e-03

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 39.50  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 246 LKVPRIHW-DLStERVLLMEFVDGgqVNDRDYMERNKIDVNEISRHLG----KMYSemifvNGFVHCDPHPGNVLVRkhp 320
Cdd:PRK14879   61 VNVPAVYFvDPE-NFIIVMEYIEG--EPLKDLINSNGMEELELSREIGrlvgKLHS-----AGIIHGDLTTSNMILS--- 129

                          90
                  ....*....|....
gi 1487193389 321 gtgKAEIVLLDHGL 334
Cdd:PRK14879  130 ---GGKIYLIDFGL 140
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
 246-334 3.17e-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: 39.23  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 246 LKVPRI-----HWDLSTERVLLMEFVDGGQVND-----RDYMERNKID-VNEISRHLGKMYSEMIfvngfVHCDPHPGNV 314
Cdd:cd14095    55 VKHPNIvqlieEYDTDTELYLVMELVKGGDLFDaitssTKFTERDASRmVTDLAQALKYLHSLSI-----VHRDIKPENL 129

                          90       100
                  ....*....|....*....|
gi 1487193389 315 LVRKHpGTGKAEIVLLDHGL 334
Cdd:cd14095   130 LVVEH-EDGSKSLKLADFGL 148
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
 219-316 4.62e-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: 37.42  E-value: 4.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 219 NLPLELDFLNEGRNAEKVSQMLRHFDFLKVPRIHwdlSTERVLLMEFVDGGQVNDRDYMERNK-IDVNEISRHLGKmYSE 297
Cdd:cd13968    30 NNEEGEDLESEMDILRRLKGLELNIPKVLVTEDV---DGPNILLMELVKGGTLIAYTQEEELDeKDVESIMYQLAE-CMR 105

                          90
                  ....*....|....*....
gi 1487193389 298 MIFVNGFVHCDPHPGNVLV 316
Cdd:cd13968   106 LLHSFHLIHRDLNNDNILL 124
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
 261-334 5.60e-03

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


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 38.49  E-value: 5.60e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1487193389 261 LLMEFVDGGQVndRDYMER-NKIDVNEISRHLGKMYSEMIFV--NGFVHCDPHPGNVLVRKHPGTGKAEivLLDHGL 334
Cdd:cd14012    81 LLTEYAPGGSL--SELLDSvGSVPLDTARRWTLQLLEALEYLhrNGVVHKSLHAGNVLLDRDAGTGIVK--LTDYSL 153
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
 197-316 6.71e-03

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 38.27  E-value: 6.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487193389 197 VLAVKQLfpefefmwlvdEAKKNLPLELDFLnegRNAEKVSQMLRHfdflkvPRI---HWDLSTERVL--LMEFVDGGQV 271
Cdd:cd06606    27 LMAVKEV-----------ELSGDSEEELEAL---EREIRILSSLKH------PNIvryLGTERTENTLniFLEYVPGGSL 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1487193389 272 ndRDYMERN-KIDVNEIsrhlgKMYSEMIF-------VNGFVHCDPHPGNVLV 316
Cdd:cd06606    87 --ASLLKKFgKLPEPVV-----RKYTRQILegleylhSNGIVHRDIKGANILV 132
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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