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Conserved domains on  [gi|449455830|ref|XP_004145653|]
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aarF domain-containing protein kinase 1 isoform X1 [Cucumis sativus]

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 ...
 126-369 3.02e-129

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: 377.21  E-value: 3.02e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 126 SLQDQAVPCPFKDIKDMLISNLGSDISAMFLSLDEQPIAAASIAQVHRAILKSNKEVAIKVQYPGLMQNVKIDTTVMSFL 205
Cdd:cd13969    1 VLQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVHKAKLKDGEEVAVKVQHPDLRKQFAGDLATMEFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 206 SRTISWLFPEYRFEWLASEFGKTILLELDFLQEARNAERTAENFKKNNLVKIPRVYWEFTTRQVLTMEFCEGHKVDDIEF 285
Cdd:cd13969   81 VNLVEKLFPDFPFSWLVDELKKNLPKELDFLNEARNAERCAKLFKHRPDVYVPKVYWDLSSKRVLTMEFIDGIKIDDVEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 286 MKQSGIEPSKVAKALVEVFAEMVFVHGFLHGDPHPGNILVSPDNLNG-FTLVLLDHGIYKQLDEEFRLNYCQLWKAMITL 364
Cdd:cd13969  161 LKKLGIDPKEVARLLSEAFAEMIFVHGFVHCDPHPGNLLVRKNPGPGkPQIVLLDHGLYRELDEEFRLNYCRLWKALILG 240


                 ....*
gi 449455830 365 DTNKI 369
Cdd:cd13969  241 DEKKI 245
 
Name Accession Description Interval E-value
ADCK1-like cd13969
aarF domain containing kinase 1 and similar proteins; This subfamily is composed of ...
 126-369 3.02e-129

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: 377.21  E-value: 3.02e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 126 SLQDQAVPCPFKDIKDMLISNLGSDISAMFLSLDEQPIAAASIAQVHRAILKSNKEVAIKVQYPGLMQNVKIDTTVMSFL 205
Cdd:cd13969    1 VLQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVHKAKLKDGEEVAVKVQHPDLRKQFAGDLATMEFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 206 SRTISWLFPEYRFEWLASEFGKTILLELDFLQEARNAERTAENFKKNNLVKIPRVYWEFTTRQVLTMEFCEGHKVDDIEF 285
Cdd:cd13969   81 VNLVEKLFPDFPFSWLVDELKKNLPKELDFLNEARNAERCAKLFKHRPDVYVPKVYWDLSSKRVLTMEFIDGIKIDDVEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 286 MKQSGIEPSKVAKALVEVFAEMVFVHGFLHGDPHPGNILVSPDNLNG-FTLVLLDHGIYKQLDEEFRLNYCQLWKAMITL 364
Cdd:cd13969  161 LKKLGIDPKEVARLLSEAFAEMIFVHGFVHCDPHPGNLLVRKNPGPGkPQIVLLDHGLYRELDEEFRLNYCRLWKALILG 240


                 ....*
gi 449455830 365 DTNKI 369
Cdd:cd13969  241 DEKKI 245
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
 126-372 5.77e-110

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: 327.65  E-value: 5.77e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830  126 SLQDQAVPCPFKDIKDMLISNLGSDISAMFLSLDEQPIAAASIAQVHRAILKSNKEVAIKVQYPGLMQNVKIDTTVMSFL 205
Cdd:pfam03109   1 KLQDRAPPFPFEQAKKVIEEELGAPVEEIFAEFDEEPIAAASIAQVHRARLKDGEEVAVKVQRPGVKKRIRSDLLLLRFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830  206 SRTISWLFPEYR-FEWLASEFGKTILLELDFLQEARNAERTAENFKKNNLVKIPRVYWEFTTRQVLTMEFCEGHKVDDIE 284
Cdd:pfam03109  81 AKVAKRFFPGFRrLDWLVDEFRKSLPQELDFLREAANAEKFRENFADDPDVYVPKVYWELTTERVLTMEYVDGIKIDDLD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830  285 FMKQSGIEPSKVAKALVEVFAEMVFVHGFLHGDPHPGNILVSPDNlngfTLVLLDHGIYKQLDEEFRLNYCQLWKAMITL 364
Cdd:pfam03109 161 ALSEAGIDRKEIARRLVELFLEQIFRDGFFHADPHPGNILVRKDG----RIVLLDFGLMGRLDEKFRRLYAELLLALVNR 236


                  ....*...
gi 449455830  365 DTNKILQL 372
Cdd:pfam03109 237 DYKRVAEM 244
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
 78-372 8.01e-103

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: 317.92  E-value: 8.01e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830  78 RLKLSEVHLRSAKRLLKLCQVNKGFYIKAGQFAaSLRQT--PNEYSSILSSLQDQAVPCPFKDIKDMLISNLGSDISAMF 155
Cdd:COG0661   41 EERREELRRRRAERLRLALEELGPTFIKLGQLL-STRPDllPPEYAEELAKLQDRVPPFPFEEVRAVIEEELGRPLEELF 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 156 LSLDEQPIAAASIAQVHRAILKSNKEVAIKVQYPGLMQNVKIDTTVMSFLSRTISWLFPE---YRFEWLASEFGKTILLE 232
Cdd:COG0661  120 AEFDPEPLAAASIGQVHRARLKDGREVAVKVQRPGIEEAIEADLRILRRLARLLERLSPEgrrLDPVEVVDEFARSLLEE 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 233 LDFLQEARNAERTAENFKKNNLVKIPRVYWEFTTRQVLTMEFCEGHKVDDIEFMKQSGIEPSKVAKALVEVFAEMVFVHG 312
Cdd:COG0661  200 LDYRREAANAERFRRNFADDPDVYVPKVYWELSTRRVLTMEWIDGIKISDLEALDAAGIDRKRLAERLVRAFLRQVFRDG 279

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 313 FLHGDPHPGNILVSPDNlngfTLVLLDHGIYKQLDEEFRLNYCQLWKAMITLDTNKILQL 372
Cdd:COG0661  280 FFHADPHPGNIFVLPDG----RLVLLDFGMVGRLDPETREGLAELLLALLNRDYDRVAEA 335
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
 103-379 3.49e-81

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: 260.31  E-value: 3.49e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830  103 YIKAGQFAASLRQT-PNEYSSILSSLQDQAVPCPFKDIKDMLISNLGSDISAMFLSLDEQPIAAASIAQVHRAILKSNKE 181
Cdd:TIGR01982  64 FIKFGQTLSTRADLlPADIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEEKPLAAASIAQVHRARLVDGKE 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830  182 VAIKVQYPGLMQNVKIDTTVMSFLSRTISWLFPE---YRFEWLASEFGKTILLELDFLQEARNAERTAENFKKNNLVKIP 258
Cdd:TIGR01982 144 VAVKVLRPGIEKTIAADIALLYRLARIVERLSPDsrrLRPTEVVKEFEKTLRRELDLRREAANASELGENFKNDPGVYVP 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830  259 RVYWEFTTRQVLTMEFCEGHKVDDIEFMKQSGIEPSKVAKALVEVFAEMVFVHGFLHGDPHPGNILVSPDNlngfTLVLL 338
Cdd:TIGR01982 224 EVYWDRTSERVLTMEWIDGIPLSDIAALDEAGLDRKALAENLARSFLNQVLRDGFFHADLHPGNIFVLKDG----KIIAL 299

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 449455830  339 DHGIYKQLDEEFRLNYCQLWKAMITLDTNKILQLG-EWFGVP 379
Cdd:TIGR01982 300 DFGIVGRLSEEDRRYLAEILYGFLNRDYRRVAEVHfDAGYVP 341
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
 124-349 8.29e-49

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 177.02  E-value: 8.29e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 124 LSSLQDQAVPCPFKDIKDMLISNLGSDISAMFLSLDEQPIAAASIAQVHRAILKSN-KEVAIKVQYPGLMQNVKIDTTVM 202
Cdd:PRK04750  88 LALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQVHFARLKDNgREVVVKVLRPDILPVIDADLALM 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 203 SFLSRTISWLFPEYR----FEWLAsEFGKTILLELDFLQEARNAERTAENFKKNNLVKIPRVYWEFTTRQVLTMEFCEGH 278
Cdd:PRK04750 168 YRLARWVERLLPDGRrlkpREVVA-EFEKTLHDELDLMREAANASQLRRNFEDSDMLYVPEVYWDYCSETVMVMERMYGI 246

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 449455830 279 KVDDIEFMKQSGIEPSKVAKALVEVFAEMVFVHGFLHGDPHPGNILVSPDNLNGFTLVLLDHGIYKQLDEE 349
Cdd:PRK04750 247 PVSDVAALRAAGTDMKLLAERGVEVFFTQVFRDGFFHADMHPGNIFVSYDPPENPRYIALDFGIVGSLNKE 317
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
 167-353 4.24e-04

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 42.13  E-value: 4.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830   167 SIAQVHRAI-LKSNKEVAIKVqypglMQNVKIDTTVmsflsrtiswlfpeyrfewlasefgKTILLELDFLQEARNaert 245
Cdd:smart00220  11 SFGKVYLARdKKTGKLVAIKV-----IKKKKIKKDR-------------------------ERILREIKILKKLKH---- 56

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830   246 aenfkkNNLVKIPRVYwEFTTRQVLTMEFCEGHKVDDIefMKQSGIEPSKVAKALV-EVFAEMVFVH--GFLHGDPHPGN 322
Cdd:smart00220  57 ------PNIVRLYDVF-EDEDKLYLVMEYCEGGDLFDL--LKKRGRLSEDEARFYLrQILSALEYLHskGIVHRDLKPEN 127

                          170       180       190
                   ....*....|....*....|....*....|.
gi 449455830   323 ILVSPDNlngfTLVLLDHGIYKQLDEEFRLN 353
Cdd:smart00220 128 ILLDEDG----HVKLADFGLARQLDPGEKLT 154
 
Name Accession Description Interval E-value
ADCK1-like cd13969
aarF domain containing kinase 1 and similar proteins; This subfamily is composed of ...
 126-369 3.02e-129

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: 377.21  E-value: 3.02e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 126 SLQDQAVPCPFKDIKDMLISNLGSDISAMFLSLDEQPIAAASIAQVHRAILKSNKEVAIKVQYPGLMQNVKIDTTVMSFL 205
Cdd:cd13969    1 VLQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVHKAKLKDGEEVAVKVQHPDLRKQFAGDLATMEFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 206 SRTISWLFPEYRFEWLASEFGKTILLELDFLQEARNAERTAENFKKNNLVKIPRVYWEFTTRQVLTMEFCEGHKVDDIEF 285
Cdd:cd13969   81 VNLVEKLFPDFPFSWLVDELKKNLPKELDFLNEARNAERCAKLFKHRPDVYVPKVYWDLSSKRVLTMEFIDGIKIDDVEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 286 MKQSGIEPSKVAKALVEVFAEMVFVHGFLHGDPHPGNILVSPDNLNG-FTLVLLDHGIYKQLDEEFRLNYCQLWKAMITL 364
Cdd:cd13969  161 LKKLGIDPKEVARLLSEAFAEMIFVHGFVHCDPHPGNLLVRKNPGPGkPQIVLLDHGLYRELDEEFRLNYCRLWKALILG 240


                 ....*
gi 449455830 365 DTNKI 369
Cdd:cd13969  241 DEKKI 245
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
 126-372 5.77e-110

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: 327.65  E-value: 5.77e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830  126 SLQDQAVPCPFKDIKDMLISNLGSDISAMFLSLDEQPIAAASIAQVHRAILKSNKEVAIKVQYPGLMQNVKIDTTVMSFL 205
Cdd:pfam03109   1 KLQDRAPPFPFEQAKKVIEEELGAPVEEIFAEFDEEPIAAASIAQVHRARLKDGEEVAVKVQRPGVKKRIRSDLLLLRFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830  206 SRTISWLFPEYR-FEWLASEFGKTILLELDFLQEARNAERTAENFKKNNLVKIPRVYWEFTTRQVLTMEFCEGHKVDDIE 284
Cdd:pfam03109  81 AKVAKRFFPGFRrLDWLVDEFRKSLPQELDFLREAANAEKFRENFADDPDVYVPKVYWELTTERVLTMEYVDGIKIDDLD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830  285 FMKQSGIEPSKVAKALVEVFAEMVFVHGFLHGDPHPGNILVSPDNlngfTLVLLDHGIYKQLDEEFRLNYCQLWKAMITL 364
Cdd:pfam03109 161 ALSEAGIDRKEIARRLVELFLEQIFRDGFFHADPHPGNILVRKDG----RIVLLDFGLMGRLDEKFRRLYAELLLALVNR 236


                  ....*...
gi 449455830  365 DTNKILQL 372
Cdd:pfam03109 237 DYKRVAEM 244
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
 78-372 8.01e-103

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: 317.92  E-value: 8.01e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830  78 RLKLSEVHLRSAKRLLKLCQVNKGFYIKAGQFAaSLRQT--PNEYSSILSSLQDQAVPCPFKDIKDMLISNLGSDISAMF 155
Cdd:COG0661   41 EERREELRRRRAERLRLALEELGPTFIKLGQLL-STRPDllPPEYAEELAKLQDRVPPFPFEEVRAVIEEELGRPLEELF 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 156 LSLDEQPIAAASIAQVHRAILKSNKEVAIKVQYPGLMQNVKIDTTVMSFLSRTISWLFPE---YRFEWLASEFGKTILLE 232
Cdd:COG0661  120 AEFDPEPLAAASIGQVHRARLKDGREVAVKVQRPGIEEAIEADLRILRRLARLLERLSPEgrrLDPVEVVDEFARSLLEE 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 233 LDFLQEARNAERTAENFKKNNLVKIPRVYWEFTTRQVLTMEFCEGHKVDDIEFMKQSGIEPSKVAKALVEVFAEMVFVHG 312
Cdd:COG0661  200 LDYRREAANAERFRRNFADDPDVYVPKVYWELSTRRVLTMEWIDGIKISDLEALDAAGIDRKRLAERLVRAFLRQVFRDG 279

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 313 FLHGDPHPGNILVSPDNlngfTLVLLDHGIYKQLDEEFRLNYCQLWKAMITLDTNKILQL 372
Cdd:COG0661  280 FFHADPHPGNIFVLPDG----RLVLLDFGMVGRLDPETREGLAELLLALLNRDYDRVAEA 335
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
 127-372 1.40e-100

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: 303.65  E-value: 1.40e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 127 LQDQAVPCPFKDIKDMLISNLGSDISAMFLSLDEQPIAAASIAQVHRAILKSNKEVAIKVQYPGLMQNVKIDTTVMSFLS 206
Cdd:cd05121    2 LQDDVPPFPFEEVRKIIEEELGRPLEEVFAEFDPEPLAAASIAQVHRARLKDGREVAVKVQRPGIEEIIEADLRILRRLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 207 RTISWLFPE---YRFEWLASEFGKTILLELDFLQEARNAERTAENFKKNNLVKIPRVYWEFTTRQVLTMEFCEGHKVDDI 283
Cdd:cd05121   82 RLLERLSPLlrrLDLVAIVDEFARSLLEELDFRREARNAERFRKNLKDSPDVYVPKVYPELSTRRVLVMEYIDGVKLTDL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 284 EFMKQSGIEPSKVAKALVEVFAEMVFVHGFLHGDPHPGNILVSPDNlngfTLVLLDHGIYKQLDEEFRLNYCQLWKAMIT 363
Cdd:cd05121  162 EALRAAGIDRKELARRLVDAYLKQIFEDGFFHADPHPGNILVLPDG----RIALLDFGMVGRLDPETREALADLLLALVN 237


                 ....*....
gi 449455830 364 LDTNKILQL 372
Cdd:cd05121  238 GDAEGLAEA 246
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
 103-379 3.49e-81

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: 260.31  E-value: 3.49e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830  103 YIKAGQFAASLRQT-PNEYSSILSSLQDQAVPCPFKDIKDMLISNLGSDISAMFLSLDEQPIAAASIAQVHRAILKSNKE 181
Cdd:TIGR01982  64 FIKFGQTLSTRADLlPADIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEEKPLAAASIAQVHRARLVDGKE 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830  182 VAIKVQYPGLMQNVKIDTTVMSFLSRTISWLFPE---YRFEWLASEFGKTILLELDFLQEARNAERTAENFKKNNLVKIP 258
Cdd:TIGR01982 144 VAVKVLRPGIEKTIAADIALLYRLARIVERLSPDsrrLRPTEVVKEFEKTLRRELDLRREAANASELGENFKNDPGVYVP 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830  259 RVYWEFTTRQVLTMEFCEGHKVDDIEFMKQSGIEPSKVAKALVEVFAEMVFVHGFLHGDPHPGNILVSPDNlngfTLVLL 338
Cdd:TIGR01982 224 EVYWDRTSERVLTMEWIDGIPLSDIAALDEAGLDRKALAENLARSFLNQVLRDGFFHADLHPGNIFVLKDG----KIIAL 299

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 449455830  339 DHGIYKQLDEEFRLNYCQLWKAMITLDTNKILQLG-EWFGVP 379
Cdd:TIGR01982 300 DFGIVGRLSEEDRRYLAEILYGFLNRDYRRVAEVHfDAGYVP 341
UbiB cd13972
Ubiquinone biosynthetic protein UbiB; UbiB is the prokaryotic homolog of yeast Abc1p and human ...
 127-372 8.15e-69

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: 221.69  E-value: 8.15e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 127 LQDQAVPCPFKDIKDMLISNLGSDISAMFLSLDEQPIAAASIAQVHRAILKSNKEVAIKVQYPGLMQNVKIDTTVMSFLS 206
Cdd:cd13972    2 LQDRVPPFSGKEARAIIEAELGKPLDALFSDFDEEPVAAASIAQVHKARLLDGREVAVKVLRPGIEKRIERDLELLRFLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 207 RTISWLFPEYRF---EWLASEFGKTILLELDFLQEARNAERTAENFKKNNLVKIPRVYWEFTTRQVLTMEFCEGHKVDDI 283
Cdd:cd13972   82 RLAERLLPEARRlrpVEVVKEFARSLLLELDLRLEAANASELRENFLDDPGFYVPEVYWELTSKNVLTMEWIDGIPISDI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 284 EFMKQSGIEPSKVAKALVEVFAEMVFVHGFLHGDPHPGNILVSPDNlngfTLVLLDHGIYKQLDEEFRLNYCQLWKAMIT 363
Cdd:cd13972  162 EALDAAGIDRKALAERLVEIFFRQVFRDGFFHADMHPGNIFVDPNG----RIIAVDFGIMGRLDKKDRRYLAEILYGFLT 237


                 ....*....
gi 449455830 364 LDTNKILQL 372
Cdd:cd13972  238 RDYRRVAEL 246
ABC1_ADCK3 cd13970
Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This ...
 123-372 1.64e-67

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: 218.54  E-value: 1.64e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 123 ILSSLQDQAVPCPFKDIKDMLISNLGSDISAMFLSLDEQPIAAASIAQVHRAILKSNKEVAIKVQYPGLMQNVKIDTTVM 202
Cdd:cd13970    2 ALARLRDSAPPMPWAQLEKVLEAELGEDWRELFAEFDEEPFAAASIGQVHRATLKDGREVAVKVQYPGVAESIDSDLNNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 203 SFLSRTISWLFPEYRFEWLASEFGKTILLELDFLQEARNAERTAENFKKNNLVKIPRVYWEFTTRQVLTMEFCEGHKVDD 282
Cdd:cd13970   82 RRLLKLTGLLPKGLDLDALIAELREELLEECDYEREAANQRRFRELLADDPRFVVPEVIPELSTKRVLTTEFVDGVPLDE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 283 IEFMKQsgIEPSKVAKALVEVFAEMVFVHGFLHGDPHPGNILVSPDNlngFTLVLLDHGIYKQLDEEFRLNYCQLWKAMI 362
Cdd:cd13970  162 AADLSQ--EERNRIGELLLRLCLRELFEFGFMQTDPNPGNFLYDPED---GRLGLLDFGAVREYPPEFVDGYRRLVRAAL 236

                        250
                 ....*....|
gi 449455830 363 TLDTNKILQL 372
Cdd:cd13970  237 EGDREALLEA 246
ADCK2-like cd13971
aarF domain containing kinase 2 and similar proteins; This subfamily is composed of ...
 127-372 1.49e-52

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: 180.50  E-value: 1.49e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 127 LQDQAVPCPFKDIKDMLISNLGSDISAMFLSLDEQPIAAASIAQVHRAILKSNK--------EVAIKVQYPGLMQNVKID 198
Cdd:cd13971    2 LHSNAPPHSWAHTERALEAAFGKDWEDIFEEFDEEPIGSGSIAQVHRAKLKPDYggdgggprVVAVKVLHPGVREQIERD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 199 TTVMSFLSRTISWLFPeyrFEWLA-----SEFGKTILLELDFLQEARNAERTAENFKKNNLVKIPRVYWEFTTRQVLTME 273
Cdd:cd13971   82 LAILRLFAKLLEAIPP---LRWLSlpesvEQFASLMLRQLDLRVEAANLERFRENFKDRKDVSFPKPLYPLVTEEVLVET 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 274 FCEGHKVDDIEFMKQSGIEPSKVAKALVEVFAEMVFVHGFLHGDPHPGNILVSPDNLNGF-------------TLVLLDH 340
Cdd:cd13971  159 FEEGVPISRTVLAHGGEPLKRKLARIGLDAFLKMLFVDNFVHGDLHPGNILVRFNDSNRPsllvsldargsppRLVFLDA 238

                        250       260       270
                 ....*....|....*....|....*....|..
gi 449455830 341 GIYKQLDEEFRLNYCQLWKAMITLDTNKILQL 372
Cdd:cd13971  239 GLVTELSPQDRRNFIDLFKAVARGDGYKAAEL 270
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
 124-349 8.29e-49

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 177.02  E-value: 8.29e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 124 LSSLQDQAVPCPFKDIKDMLISNLGSDISAMFLSLDEQPIAAASIAQVHRAILKSN-KEVAIKVQYPGLMQNVKIDTTVM 202
Cdd:PRK04750  88 LALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQVHFARLKDNgREVVVKVLRPDILPVIDADLALM 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 203 SFLSRTISWLFPEYR----FEWLAsEFGKTILLELDFLQEARNAERTAENFKKNNLVKIPRVYWEFTTRQVLTMEFCEGH 278
Cdd:PRK04750 168 YRLARWVERLLPDGRrlkpREVVA-EFEKTLHDELDLMREAANASQLRRNFEDSDMLYVPEVYWDYCSETVMVMERMYGI 246

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 449455830 279 KVDDIEFMKQSGIEPSKVAKALVEVFAEMVFVHGFLHGDPHPGNILVSPDNLNGFTLVLLDHGIYKQLDEE 349
Cdd:PRK04750 247 PVSDVAALRAAGTDMKLLAERGVEVFFTQVFRDGFFHADMHPGNIFVSYDPPENPRYIALDFGIVGSLNKE 317
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
 160-349 1.23e-10

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: 62.22  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 160 EQPIAAASIAQVHRAI-LKSNKEVAIKVQYPGLMQNVKidttvmsFLSRtiswlfpeyrfewlasefgktilleldFLQE 238
Cdd:cd14014    5 VRLLGRGGMGEVYRARdTLLGRPVAIKVLRPELAEDEE-------FRER---------------------------FLRE 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 239 ARNAERtaenFKKNNLVKIPRVYwEFTTRQVLTMEFCEGHKVDDIefMKQSG-IEPSKVAKALVEVFAEMVFVH--GFLH 315
Cdd:cd14014   51 ARALAR----LSHPNIVRVYDVG-EDDGRPYIVMEYVEGGSLADL--LRERGpLPPREALRILAQIADALAAAHraGIVH 123

                        170       180       190
                 ....*....|....*....|....*....|....
gi 449455830 316 GDPHPGNILVSPDNlngfTLVLLDHGIYKQLDEE 349
Cdd:cd14014  124 RDIKPANILLTEDG----RVKLTDFGIARALGDS 153
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
160-349 5.11e-09

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 58.49  E-value: 5.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 160 EQPIAAASIAQVHRAI-LKSNKEVAIKVQYPGLMQNVKidttvmsFLSRtiswlfpeyrfewlasefgktilleldFLQE 238
Cdd:COG0515   12 LRLLGRGGMGVVYLARdLRLGRPVALKVLRPELAADPE-------ARER---------------------------FRRE 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 239 ARNAER-TAENfkknnlvkIPRVY--WEFTTRQVLTMEFCEGHKVDDIefMKQSG-IEPSKVAKALVEVFAEMVFVH--G 312
Cdd:COG0515   58 ARALARlNHPN--------IVRVYdvGEEDGRPYLVMEYVEGESLADL--LRRRGpLPPAEALRILAQLAEALAAAHaaG 127

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 449455830 313 FLHGDPHPGNILVSPDNlngfTLVLLDHGIYKQLDEE 349
Cdd:COG0515  128 IVHRDIKPANILLTPDG----RVKLIDFGIARALGGA 160
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 236-329 1.22e-07

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: 51.15  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 236 LQEARNAERTAENFKKNNL-VKIPRVY--WEFTTRQVLTMEFCEGHKVDDiEFMKQSGIEPSKVAKALVEVFAEM--VFV 310
Cdd:cd05120   32 LKKDLEKEAAMLQLLAGKLsLPVPKVYgfGESDGWEYLLMERIEGETLSE-VWPRLSEEEKEKIADQLAEILAALhrIDS 110

                         90
                 ....*....|....*....
gi 449455830 311 HGFLHGDPHPGNILVSPDN 329
Cdd:cd05120  111 SVLTHGDLHPGNILVKPDG 129
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 232-341 2.41e-06

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 47.65  E-value: 2.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 232 ELDFLQEARNAErtaenfkknnlVKIPRVYWEFTTRQVLTMEFCEGHKVDDIefmKQSGIEPSKVAKALVEVFAEMvfvH 311
Cdd:COG3642    6 EARLLRELREAG-----------VPVPKVLDVDPDDADLVMEYIEGETLADL---LEEGELPPELLRELGRLLARL---H 68

                         90       100       110
                 ....*....|....*....|....*....|..
gi 449455830 312 --GFLHGDPHPGNILVSPDNlngftLVLLDHG 341
Cdd:COG3642   69 raGIVHGDLTTSNILVDDGG-----VYLIDFG 95
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
 240-349 2.62e-04

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK 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: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 43.08  E-value: 2.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 240 RNAERTAENFKKNNLVKIPRVYWEF---TTRQVLTMEFCEGHKVDdiEFMKQSGIEPSKVAKALV-EVFAEMVFVH---- 311
Cdd:cd13990   49 KHALREYEIHKSLDHPRIVKLYDVFeidTDSFCTVLEYCDGNDLD--FYLKQHKSIPEREARSIImQVVSALKYLNeikp 126

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 449455830 312 GFLHGDPHPGNILVSPDNLNGfTLVLLDHGIYKQLDEE 349
Cdd:cd13990  127 PIIHYDLKPGNILLHSGNVSG-EIKITDFGLSKIMDDE 163
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
 222-341 4.00e-04

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


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 40.50  E-value: 4.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 222 ASEFGKTILLELDFLQEARNAERTAENFkknnlvkipRVYWEFTTRQVLTMEFCEGHKVDDIEFMKQ-SGIEPSKVAKAL 300
Cdd:cd13968   30 NNEEGEDLESEMDILRRLKGLELNIPKV---------LVTEDVDGPNILLMELVKGGTLIAYTQEEElDEKDVESIMYQL 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 449455830 301 VEVFAEMvFVHGFLHGDPHPGNILVSPDNlngfTLVLLDHG 341
Cdd:cd13968  101 AECMRLL-HSFHLIHRDLNNDNILLSEDG----NVKLIDFG 136
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
 167-353 4.24e-04

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 42.13  E-value: 4.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830   167 SIAQVHRAI-LKSNKEVAIKVqypglMQNVKIDTTVmsflsrtiswlfpeyrfewlasefgKTILLELDFLQEARNaert 245
Cdd:smart00220  11 SFGKVYLARdKKTGKLVAIKV-----IKKKKIKKDR-------------------------ERILREIKILKKLKH---- 56

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830   246 aenfkkNNLVKIPRVYwEFTTRQVLTMEFCEGHKVDDIefMKQSGIEPSKVAKALV-EVFAEMVFVH--GFLHGDPHPGN 322
Cdd:smart00220  57 ------PNIVRLYDVF-EDEDKLYLVMEYCEGGDLFDL--LKKRGRLSEDEARFYLrQILSALEYLHskGIVHRDLKPEN 127

                          170       180       190
                   ....*....|....*....|....*....|.
gi 449455830   323 ILVSPDNlngfTLVLLDHGIYKQLDEEFRLN 353
Cdd:smart00220 128 ILLDEDG----HVKLADFGLARQLDPGEKLT 154
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
 262-342 4.97e-04

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 42.02  E-value: 4.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 262 WEFTTRQVLTMEFCEGHKVDDI--EFMKQSGIEPSKVAKALVEVFAEMVFVH--GFLHGDPHPGNILVSPDNlngfTLVL 337
Cdd:cd14052   72 WEYHGHLYIQTELCENGSLDVFlsELGLLGRLDEFRVWKILVELSLGLRFIHdhHFVHLDLKPANVLITFEG----TLKI 147


                 ....*
gi 449455830 338 LDHGI 342
Cdd:cd14052  148 GDFGM 152
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
 224-350 9.29e-04

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family 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: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 41.07  E-value: 9.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 224 EFGKTILLELDFLQEARNAERTAenfkknNLVKIPRV-YWEFTTRQVLTMEFCeGHKVDDIEFMKQSGIEPSKVAKALVE 302
Cdd:cd05118   37 RHPKAALREIKLLKHLNDVEGHP------NIVKLLDVfEHRGGNHLCLVFELM-GMNLYELIKDYPRGLPLDLIKSYLYQ 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 449455830 303 VFAEMVFVH--GFLHGDPHPGNILVSPDNlngFTLVLLDHGIYKQLDEEF 350
Cdd:cd05118  110 LLQALDFLHsnGIIHRDLKPENILINLEL---GQLKLADFGLARSFTSPP 156
PRK14879 PRK14879
Kae1-associated kinase Bud32;
255-330 1.01e-03

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 40.66  E-value: 1.01e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 449455830 255 VKIPRVYWEFTTRQVLTMEFCEGHKVDDIefMKQSGIEPSKVAKALVEVFAEMvfvH--GFLHGDPHPGNILVSPDNL 330
Cdd:PRK14879  61 VNVPAVYFVDPENFIIVMEYIEGEPLKDL--INSNGMEELELSREIGRLVGKL---HsaGIIHGDLTTSNMILSGGKI 133
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
 232-350 2.65e-03

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 39.12  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830  232 ELDflqEARNAERTAENFK-----KNNLVKIPRVYWEFTTRQVLTMEFCEGHKVDDIefMKQSGIEpskvakaLVEVFAE 306
Cdd:TIGR03724  34 ELD---ERLRKERTRREARllsraRKAGVNTPVIYDVDPDNKTIVMEYIEGKPLKDV--IEENGDE-------LAREIGR 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 449455830  307 MVFV---HGFLHGDPHPGNILVSPDNlngftLVLLDHGI--YKQLDEEF 350
Cdd:TIGR03724 102 LVGKlhkAGIVHGDLTTSNIIVRDDK-----VYLIDFGLgkYSDEIEDK 145
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
 234-349 6.00e-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: 38.41  E-value: 6.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449455830 234 DFLQEARNAERtaenFKKNNLVKIpRVYWEFTTRQVLTMEFCEGhkVDDIEFMKQ--SGIEPSKVAKALVEVFAEMVFVH 311
Cdd:cd00180   37 ELLREIEILKK----LNHPNIVKL-YDVFETENFLYLVMEYCEG--GSLKDLLKEnkGPLSEEEALSILRQLLSALEYLH 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 449455830 312 --GFLHGDPHPGNILVSPDNlngfTLVLLDHGIYKQLDEE 349
Cdd:cd00180  110 snGIIHRDLKPENILLDSDG----TVKLADFGLAKDLDSD 145
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
 258-330 6.06e-03

Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic choline kinases, as well as eukaryotic ethanolamine kinase. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. Bacterial ChoK is also referred to as licA protein. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK subfamily 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: 270700 [Multi-domain]  Cd Length: 152  Bit Score: 37.53  E-value: 6.06e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 449455830 258 PRVYWEFTTRQVLTMEFCEGHKVDDIEFMKQsgIEPSKVAKALVEVFAEMVFVHGFLHGDPHPGNILVSPDNL 330
Cdd:cd05151   56 PEVIYFDPETGVKITEFIEGATLLTNDFSDP--ENLERIAALLRKLHSSPLEDLVLCHNDLVPGNFLLDDDRL 126
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
 314-332 6.92e-03

Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and Choline kinase; This subfamily is composed of uncharacterized bacterial proteins with similarity to APH and ChoK. Other APH/ChoK-like proteins include 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). These proteins 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-like subfamily 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: 270704 [Multi-domain]  Cd Length: 234  Bit Score: 38.37  E-value: 6.92e-03
                         10
                 ....*....|....*....
gi 449455830 314 LHGDPHPGNILVSPDNLNG 332
Cdd:cd05155  166 LHGDLHPGNLLVRDGRLSA 184
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
313-339 7.62e-03

Thiamine kinase or a related kinase [Coenzyme transport and metabolism];


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 37.45  E-value: 7.62e-03
                         10        20
                 ....*....|....*....|....*..
gi 449455830 313 FLHGDPHPGNILVSPDNlngfTLVLLD 339
Cdd:COG0510   51 LCHGDLHPGNFLVTDDG----RLYLID 73
 
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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