NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|186530942|ref|NP_001119407|]
View 

Protein kinase superfamily protein [Arabidopsis thaliana]

Protein Classification

ABC1 kinase family protein( domain architecture ID 11429476)

ABC1 (activator of bc1 complex) kinase family protein is an atypical protein kinase belonging to the protein kinase superfamily, similar to Arabidopsis thaliana ABC1-like kinases

CATH:  1.10.510.10
EC:  2.7.-.-
Gene Ontology:  GO:0006468|GO:0004672|GO:0005524
PubMed:  16244704|19614568
SCOP:  3000066

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
 16-406 3.22e-86

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: 272.46  E-value: 3.22e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942  16 SFRPWQRSFQFWVRATNIYTGYKVFQLRVSLVKDAKKQEEMWERQHEQAADKIYFMCSDLGGFFLKIAQLLA-KPDMAPA 94
Cdd:COG0661    3 ALRRLRRLARIARVLLRYGLGELLDRLGLPRLRRLLTGEERREELRRRRAERLRLALEELGPTFIKLGQLLStRPDLLPP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942  95 AWVKKLVTLCDQAPATPFDAIQLVLEKELGKSIGEIFETFDEKPLGSASIAQV---------------QHPGIERLMMTD 159
Cdd:COG0661   83 EYAEELAKLQDRVPPFPFEEVRAVIEEELGRPLEELFAEFDPEPLAAASIGQVhrarlkdgrevavkvQRPGIEEAIEAD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 160 IRNLQLFALYMQRTD---IKFDLHSITKEMEKQIGYEFDFKREANAMERIRcflyENNKKSP-VLVPRVLRDMVTKRVLV 235
Cdd:COG0661  163 LRILRRLARLLERLSpegRRLDPVEVVDEFARSLLEELDYRREAANAERFR----RNFADDPdVYVPKVYWELSTRRVLT 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 236 MEYINGIPILSIgDEMAKRGINPHgKIAEAakhnilnsLSRAYGQMILKSGFFHADPHPGNILICKGQEVALLDYGQVKE 315
Cdd:COG0661  239 MEWIDGIKISDL-EALDAAGIDRK-RLAER--------LVRAFLRQVFRDGFFHADPHPGNIFVLPDGRLVLLDFGMVGR 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 316 LPNKLRLGYANLVIAMADNNASRVSQSFWEMGLHTVakcENEQQELLRLAQTLFDtkmptgqtvlqPFSDDsSIKKIAVE 395
Cdd:COG0661  309 LDPETREGLAELLLALLNRDYDRVAEALLELGFVPP---DTDVDELERALRAVLE-----------PYFGK-PLKDISFG 373

                        410
                 ....*....|.
gi 186530942 396 TFPEELFSVLR 406
Cdd:COG0661  374 ELLLELFELAR 384
 
Name Accession Description Interval E-value
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
 16-406 3.22e-86

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: 272.46  E-value: 3.22e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942  16 SFRPWQRSFQFWVRATNIYTGYKVFQLRVSLVKDAKKQEEMWERQHEQAADKIYFMCSDLGGFFLKIAQLLA-KPDMAPA 94
Cdd:COG0661    3 ALRRLRRLARIARVLLRYGLGELLDRLGLPRLRRLLTGEERREELRRRRAERLRLALEELGPTFIKLGQLLStRPDLLPP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942  95 AWVKKLVTLCDQAPATPFDAIQLVLEKELGKSIGEIFETFDEKPLGSASIAQV---------------QHPGIERLMMTD 159
Cdd:COG0661   83 EYAEELAKLQDRVPPFPFEEVRAVIEEELGRPLEELFAEFDPEPLAAASIGQVhrarlkdgrevavkvQRPGIEEAIEAD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 160 IRNLQLFALYMQRTD---IKFDLHSITKEMEKQIGYEFDFKREANAMERIRcflyENNKKSP-VLVPRVLRDMVTKRVLV 235
Cdd:COG0661  163 LRILRRLARLLERLSpegRRLDPVEVVDEFARSLLEELDYRREAANAERFR----RNFADDPdVYVPKVYWELSTRRVLT 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 236 MEYINGIPILSIgDEMAKRGINPHgKIAEAakhnilnsLSRAYGQMILKSGFFHADPHPGNILICKGQEVALLDYGQVKE 315
Cdd:COG0661  239 MEWIDGIKISDL-EALDAAGIDRK-RLAER--------LVRAFLRQVFRDGFFHADPHPGNIFVLPDGRLVLLDFGMVGR 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 316 LPNKLRLGYANLVIAMADNNASRVSQSFWEMGLHTVakcENEQQELLRLAQTLFDtkmptgqtvlqPFSDDsSIKKIAVE 395
Cdd:COG0661  309 LDPETREGLAELLLALLNRDYDRVAEALLELGFVPP---DTDVDELERALRAVLE-----------PYFGK-PLKDISFG 373

                        410
                 ....*....|.
gi 186530942 396 TFPEELFSVLR 406
Cdd:COG0661  374 ELLLELFELAR 384
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
 103-343 4.38e-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: 258.58  E-value: 4.38e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 103 LCDQAPATPFDAIQLVLEKELGKSIGEIFETFDEKPLGSASIAQV---------------QHPGIERLMMTDIRNLQLFA 167
Cdd:cd05121    2 LQDDVPPFPFEEVRKIIEEELGRPLEEVFAEFDPEPLAAASIAQVhrarlkdgrevavkvQRPGIEEIIEADLRILRRLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 168 LYMQR---TDIKFDLHSITKEMEKQIGYEFDFKREANAMERIRcflyENNKKSP-VLVPRVLRDMVTKRVLVMEYINGIP 243
Cdd:cd05121   82 RLLERlspLLRRLDLVAIVDEFARSLLEELDFRREARNAERFR----KNLKDSPdVYVPKVYPELSTRRVLVMEYIDGVK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 244 ILSIgDEMAKRGINPHgkiaeaakhNILNSLSRAYGQMILKSGFFHADPHPGNILICKGQEVALLDYGQVKELPNKLRLG 323
Cdd:cd05121  158 LTDL-EALRAAGIDRK---------ELARRLVDAYLKQIFEDGFFHADPHPGNILVLPDGRIALLDFGMVGRLDPETREA 227

                        250       260
                 ....*....|....*....|
gi 186530942 324 YANLVIAMADNNASRVSQSF 343
Cdd:cd05121  228 LADLLLALVNGDAEGLAEAL 247
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
 105-342 7.30e-62

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: 201.31  E-value: 7.30e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942  105 DQAPATPFDAIQLVLEKELGKSIGEIFETFDEKPLGSASIAQV---------------QHPGIERLMMTDIRNLQLFALY 169
Cdd:pfam03109   4 DRAPPFPFEQAKKVIEEELGAPVEEIFAEFDEEPIAAASIAQVhrarlkdgeevavkvQRPGVKKRIRSDLLLLRFLAKV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942  170 MQR-TDIKFDLHSITKEMEKQIGYEFDFKREANAMERIRcflyENNKKSP-VLVPRVLRDMVTKRVLVMEYINGIPILSI 247
Cdd:pfam03109  84 AKRfFPGFRRLDWLVDEFRKSLPQELDFLREAANAEKFR----ENFADDPdVYVPKVYWELTTERVLTMEYVDGIKIDDL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942  248 gDEMAKRGINPHgkiaeaakhNILNSLSRAYGQMILKSGFFHADPHPGNILICKGQEVALLDYGQVKELPNKLRLGYANL 327
Cdd:pfam03109 160 -DALSEAGIDRK---------EIARRLVELFLEQIFRDGFFHADPHPGNILVRKDGRIVLLDFGLMGRLDEKFRRLYAEL 229

                         250
                  ....*....|....*
gi 186530942  328 VIAMADNNASRVSQS 342
Cdd:pfam03109 230 LLALVNRDYKRVAEM 244
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
 73-347 8.07e-55

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: 188.66  E-value: 8.07e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942   73 SDLGGFFLKIAQLLA-KPDMAPAAWVKKLVTLCDQAPATPFDAIQLVLEKELGKSIGEIFETFDEKPLGSASIAQVQH-- 149
Cdd:TIGR01982  58 EELGPTFIKFGQTLStRADLLPADIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEEKPLAAASIAQVHRar 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942  150 -------------PGIERLMMTDIRNLQLFALYMQRTD---IKFDLHSITKEMEKQIGYEFDFKREANAMERIRcflyEN 213
Cdd:TIGR01982 138 lvdgkevavkvlrPGIEKTIAADIALLYRLARIVERLSpdsRRLRPTEVVKEFEKTLRRELDLRREAANASELG----EN 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942  214 NKKSP-VLVPRVLRDMVTKRVLVMEYINGIPI--LSIGDEMakrGINPHgKIAEAAKHNILNslsraygqMILKSGFFHA 290
Cdd:TIGR01982 214 FKNDPgVYVPEVYWDRTSERVLTMEWIDGIPLsdIAALDEA---GLDRK-ALAENLARSFLN--------QVLRDGFFHA 281

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 186530942  291 DPHPGNILICKGQEVALLDYGQVKELPNKLRLGYANLVIAMADNNASRVSQSFWEMG 347
Cdd:TIGR01982 282 DLHPGNIFVLKDGKIIALDFGIVGRLSEEDRRYLAEILYGFLNRDYRRVAEVHFDAG 338
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
 74-316 1.77e-28

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 118.08  E-value: 1.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942  74 DLGGFFLKIAQLLA-KPDMAPAAWVKKLVTLCDQAPATPFDAIQLVLEKELGKSIGEIFETFDEKPLGSASIAQVqH--- 149
Cdd:PRK04750  61 ELGPIFVKFGQMLStRRDLFPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQV-Hfar 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 150 --------------PGIERLMMTDIRNLQLFALYMQRtdikfdLHS---------ITKEMEKQIGYEFDFKRE-ANAMEr 205
Cdd:PRK04750 140 lkdngrevvvkvlrPDILPVIDADLALMYRLARWVER------LLPdgrrlkpreVVAEFEKTLHDELDLMREaANASQ- 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 206 ircfLYENNKKSP-VLVPRVLRDMVTKRVLVMEYINGIPILSIgDEMAKRGINphgkiaeaakhniLNSLSRA-----YG 279
Cdd:PRK04750 213 ----LRRNFEDSDmLYVPEVYWDYCSETVMVMERMYGIPVSDV-AALRAAGTD-------------MKLLAERgvevfFT 274

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 186530942 280 QmILKSGFFHADPHPGNILI-----CKGQEVAlLDYGQVKEL 316
Cdd:PRK04750 275 Q-VFRDGFFHADMHPGNIFVsydppENPRYIA-LDFGIVGSL 314
 
Name Accession Description Interval E-value
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
 16-406 3.22e-86

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: 272.46  E-value: 3.22e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942  16 SFRPWQRSFQFWVRATNIYTGYKVFQLRVSLVKDAKKQEEMWERQHEQAADKIYFMCSDLGGFFLKIAQLLA-KPDMAPA 94
Cdd:COG0661    3 ALRRLRRLARIARVLLRYGLGELLDRLGLPRLRRLLTGEERREELRRRRAERLRLALEELGPTFIKLGQLLStRPDLLPP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942  95 AWVKKLVTLCDQAPATPFDAIQLVLEKELGKSIGEIFETFDEKPLGSASIAQV---------------QHPGIERLMMTD 159
Cdd:COG0661   83 EYAEELAKLQDRVPPFPFEEVRAVIEEELGRPLEELFAEFDPEPLAAASIGQVhrarlkdgrevavkvQRPGIEEAIEAD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 160 IRNLQLFALYMQRTD---IKFDLHSITKEMEKQIGYEFDFKREANAMERIRcflyENNKKSP-VLVPRVLRDMVTKRVLV 235
Cdd:COG0661  163 LRILRRLARLLERLSpegRRLDPVEVVDEFARSLLEELDYRREAANAERFR----RNFADDPdVYVPKVYWELSTRRVLT 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 236 MEYINGIPILSIgDEMAKRGINPHgKIAEAakhnilnsLSRAYGQMILKSGFFHADPHPGNILICKGQEVALLDYGQVKE 315
Cdd:COG0661  239 MEWIDGIKISDL-EALDAAGIDRK-RLAER--------LVRAFLRQVFRDGFFHADPHPGNIFVLPDGRLVLLDFGMVGR 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 316 LPNKLRLGYANLVIAMADNNASRVSQSFWEMGLHTVakcENEQQELLRLAQTLFDtkmptgqtvlqPFSDDsSIKKIAVE 395
Cdd:COG0661  309 LDPETREGLAELLLALLNRDYDRVAEALLELGFVPP---DTDVDELERALRAVLE-----------PYFGK-PLKDISFG 373

                        410
                 ....*....|.
gi 186530942 396 TFPEELFSVLR 406
Cdd:COG0661  374 ELLLELFELAR 384
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
 103-343 4.38e-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: 258.58  E-value: 4.38e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 103 LCDQAPATPFDAIQLVLEKELGKSIGEIFETFDEKPLGSASIAQV---------------QHPGIERLMMTDIRNLQLFA 167
Cdd:cd05121    2 LQDDVPPFPFEEVRKIIEEELGRPLEEVFAEFDPEPLAAASIAQVhrarlkdgrevavkvQRPGIEEIIEADLRILRRLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 168 LYMQR---TDIKFDLHSITKEMEKQIGYEFDFKREANAMERIRcflyENNKKSP-VLVPRVLRDMVTKRVLVMEYINGIP 243
Cdd:cd05121   82 RLLERlspLLRRLDLVAIVDEFARSLLEELDFRREARNAERFR----KNLKDSPdVYVPKVYPELSTRRVLVMEYIDGVK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 244 ILSIgDEMAKRGINPHgkiaeaakhNILNSLSRAYGQMILKSGFFHADPHPGNILICKGQEVALLDYGQVKELPNKLRLG 323
Cdd:cd05121  158 LTDL-EALRAAGIDRK---------ELARRLVDAYLKQIFEDGFFHADPHPGNILVLPDGRIALLDFGMVGRLDPETREA 227

                        250       260
                 ....*....|....*....|
gi 186530942 324 YANLVIAMADNNASRVSQSF 343
Cdd:cd05121  228 LADLLLALVNGDAEGLAEAL 247
ADCK1-like cd13969
aarF domain containing kinase 1 and similar proteins; This subfamily is composed of ...
 102-347 7.26e-66

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: 211.96  E-value: 7.26e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 102 TLCDQAPATPFDAIQLVLEKELGKSIGEIFETFDEKPLGSASIAQV---------------QHPGIERLMMTDIRNLQLF 166
Cdd:cd13969    1 VLQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVhkaklkdgeevavkvQHPDLRKQFAGDLATMEFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 167 ALYMQRTDIKFDLHSITKEMEKQIGYEFDFKREANAMERIRCFLYENNKkspVLVPRVLRDMVTKRVLVMEYINGIPILS 246
Cdd:cd13969   81 VNLVEKLFPDFPFSWLVDELKKNLPKELDFLNEARNAERCAKLFKHRPD---VYVPKVYWDLSSKRVLTMEFIDGIKIDD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 247 IgDEMAKRGINPHgKIAEaakhnilnSLSRAYGQMILKSGFFHADPHPGNILICKG-----QEVALLDYGQVKELPNKLR 321
Cdd:cd13969  158 V-EALKKLGIDPK-EVAR--------LLSEAFAEMIFVHGFVHCDPHPGNLLVRKNpgpgkPQIVLLDHGLYRELDEEFR 227

                        250       260
                 ....*....|....*....|....*.
gi 186530942 322 LGYANLVIAMADNNASRVSQSFWEMG 347
Cdd:cd13969  228 LNYCRLWKALILGDEKKIKKYSKALG 253
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
 105-342 7.30e-62

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: 201.31  E-value: 7.30e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942  105 DQAPATPFDAIQLVLEKELGKSIGEIFETFDEKPLGSASIAQV---------------QHPGIERLMMTDIRNLQLFALY 169
Cdd:pfam03109   4 DRAPPFPFEQAKKVIEEELGAPVEEIFAEFDEEPIAAASIAQVhrarlkdgeevavkvQRPGVKKRIRSDLLLLRFLAKV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942  170 MQR-TDIKFDLHSITKEMEKQIGYEFDFKREANAMERIRcflyENNKKSP-VLVPRVLRDMVTKRVLVMEYINGIPILSI 247
Cdd:pfam03109  84 AKRfFPGFRRLDWLVDEFRKSLPQELDFLREAANAEKFR----ENFADDPdVYVPKVYWELTTERVLTMEYVDGIKIDDL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942  248 gDEMAKRGINPHgkiaeaakhNILNSLSRAYGQMILKSGFFHADPHPGNILICKGQEVALLDYGQVKELPNKLRLGYANL 327
Cdd:pfam03109 160 -DALSEAGIDRK---------EIARRLVELFLEQIFRDGFFHADPHPGNILVRKDGRIVLLDFGLMGRLDEKFRRLYAEL 229

                         250
                  ....*....|....*
gi 186530942  328 VIAMADNNASRVSQS 342
Cdd:pfam03109 230 LLALVNRDYKRVAEM 244
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
 73-347 8.07e-55

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: 188.66  E-value: 8.07e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942   73 SDLGGFFLKIAQLLA-KPDMAPAAWVKKLVTLCDQAPATPFDAIQLVLEKELGKSIGEIFETFDEKPLGSASIAQVQH-- 149
Cdd:TIGR01982  58 EELGPTFIKFGQTLStRADLLPADIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEEKPLAAASIAQVHRar 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942  150 -------------PGIERLMMTDIRNLQLFALYMQRTD---IKFDLHSITKEMEKQIGYEFDFKREANAMERIRcflyEN 213
Cdd:TIGR01982 138 lvdgkevavkvlrPGIEKTIAADIALLYRLARIVERLSpdsRRLRPTEVVKEFEKTLRRELDLRREAANASELG----EN 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942  214 NKKSP-VLVPRVLRDMVTKRVLVMEYINGIPI--LSIGDEMakrGINPHgKIAEAAKHNILNslsraygqMILKSGFFHA 290
Cdd:TIGR01982 214 FKNDPgVYVPEVYWDRTSERVLTMEWIDGIPLsdIAALDEA---GLDRK-ALAENLARSFLN--------QVLRDGFFHA 281

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 186530942  291 DPHPGNILICKGQEVALLDYGQVKELPNKLRLGYANLVIAMADNNASRVSQSFWEMG 347
Cdd:TIGR01982 282 DLHPGNIFVLKDGKIIALDFGIVGRLSEEDRRYLAEILYGFLNRDYRRVAEVHFDAG 338
ABC1_ADCK3 cd13970
Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This ...
 98-347 4.82e-48

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: 165.38  E-value: 4.82e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942  98 KKLVTLCDQAPATPFDAIQLVLEKELGKSIGEIFETFDEKPLGSASIAQV---------------QHPGIERLMMTDIRN 162
Cdd:cd13970    1 EALARLRDSAPPMPWAQLEKVLEAELGEDWRELFAEFDEEPFAAASIGQVhratlkdgrevavkvQYPGVAESIDSDLNN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 163 LQLFALYMQRTDIKFDLHSITKEMEKQIGYEFDFKREANAMERIRcflyENNKKSP-VLVPRVLRDMVTKRVLVMEYING 241
Cdd:cd13970   81 LRRLLKLTGLLPKGLDLDALIAELREELLEECDYEREAANQRRFR----ELLADDPrFVVPEVIPELSTKRVLTTEFVDG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 242 IPILSIGDEMAKRgINphgKIAEAakhnilnsLSRAYGQMILKSGFFHADPHPGNILIC-KGQEVALLDYGQVKELPNKL 320
Cdd:cd13970  157 VPLDEAADLSQEE-RN---RIGEL--------LLRLCLRELFEFGFMQTDPNPGNFLYDpEDGRLGLLDFGAVREYPPEF 224

                        250       260
                 ....*....|....*....|....*..
gi 186530942 321 RLGYANLVIAMADNNASRVSQSFWEMG 347
Cdd:cd13970  225 VDGYRRLVRAALEGDREALLEASVELG 251
UbiB cd13972
Ubiquinone biosynthetic protein UbiB; UbiB is the prokaryotic homolog of yeast Abc1p and human ...
 103-341 1.17e-37

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: 137.72  E-value: 1.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 103 LCDQAPATPFDAIQLVLEKELGKSIGEIFETFDEKPLGSASIAQVQH---------------PGIERLMMTDIRNLQLFA 167
Cdd:cd13972    2 LQDRVPPFSGKEARAIIEAELGKPLDALFSDFDEEPVAAASIAQVHKarlldgrevavkvlrPGIEKRIERDLELLRFLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 168 LYMQRTDIKFD---LHSITKEMEKQIGYEFDFKREANAMERIRcflyENNKKSPVL-VPRVLRDMVTKRVLVMEYINGIP 243
Cdd:cd13972   82 RLAERLLPEARrlrPVEVVKEFARSLLLELDLRLEAANASELR----ENFLDDPGFyVPEVYWELTSKNVLTMEWIDGIP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 244 ILSIgDEMAKRGINPHgKIAEAAKHNILNSlsraygqmILKSGFFHADPHPGNILICKGQEVALLDYGQVKELPNKLRLG 323
Cdd:cd13972  158 ISDI-EALDAAGIDRK-ALAERLVEIFFRQ--------VFRDGFFHADMHPGNIFVDPNGRIIAVDFGIMGRLDKKDRRY 227

                        250
                 ....*....|....*...
gi 186530942 324 YANLVIAMADNNASRVSQ 341
Cdd:cd13972  228 LAEILYGFLTRDYRRVAE 245
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
 74-316 1.77e-28

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 118.08  E-value: 1.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942  74 DLGGFFLKIAQLLA-KPDMAPAAWVKKLVTLCDQAPATPFDAIQLVLEKELGKSIGEIFETFDEKPLGSASIAQVqH--- 149
Cdd:PRK04750  61 ELGPIFVKFGQMLStRRDLFPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQV-Hfar 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 150 --------------PGIERLMMTDIRNLQLFALYMQRtdikfdLHS---------ITKEMEKQIGYEFDFKRE-ANAMEr 205
Cdd:PRK04750 140 lkdngrevvvkvlrPDILPVIDADLALMYRLARWVER------LLPdgrrlkpreVVAEFEKTLHDELDLMREaANASQ- 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 206 ircfLYENNKKSP-VLVPRVLRDMVTKRVLVMEYINGIPILSIgDEMAKRGINphgkiaeaakhniLNSLSRA-----YG 279
Cdd:PRK04750 213 ----LRRNFEDSDmLYVPEVYWDYCSETVMVMERMYGIPVSDV-AALRAAGTD-------------MKLLAERgvevfFT 274

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 186530942 280 QmILKSGFFHADPHPGNILI-----CKGQEVAlLDYGQVKEL 316
Cdd:PRK04750 275 Q-VFRDGFFHADMHPGNIFVsydppENPRYIA-LDFGIVGSL 314
ADCK2-like cd13971
aarF domain containing kinase 2 and similar proteins; This subfamily is composed of ...
 102-322 6.57e-28

aarF domain containing kinase 2 and similar proteins; This subfamily is composed of uncharacterized ABC1 kinase-like proteins including the human protein called aarF domain containing kinase 2 (ADCK2). Eukaryotes contain at least three ABC1-like proteins; in humans, these are ADCK3 and the putative protein kinases named ADCK1 and ADCK2. Yeast Abc1p and its human homolog ADCK3 are atypical protein kinases required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. In algae and higher plants, ABC1 kinases have proliferated to more than 15 subfamilies, most of which are located in plastids or mitochondria. Plant subfamily 10 (ABC1K10) belong to the same group of ABC1 kinases as human ADCK2. ABC1 kinases are not related to the ATP-binding cassette (ABC) membrane transporter family.


Pssm-ID: 270873 [Multi-domain]  Cd Length: 298  Bit Score: 112.70  E-value: 6.57e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 102 TLCDQAPATPFDAIQLVLEKELGKSIGEIFETFDEKPLGSASIAQ-----------------------VQHPGIERLMMT 158
Cdd:cd13971    1 KLHSNAPPHSWAHTERALEAAFGKDWEDIFEEFDEEPIGSGSIAQvhraklkpdyggdgggprvvavkVLHPGVREQIER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 159 DIRNLQLFA------LYMQRTDIKFDLHSITKEMEKQIgyefDFKREANAMERIRcflyeNNKKSP--VLVPRVLRDMVT 230
Cdd:cd13971   81 DLAILRLFAklleaiPPLRWLSLPESVEQFASLMLRQL----DLRVEAANLERFR-----ENFKDRkdVSFPKPLYPLVT 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 231 KRVLVMEYINGIPILSIGDEMakrginphgkIAEAAKHNILNSLSRAYGQMILKSGFFHADPHPGNILICKGQEVALLDY 310
Cdd:cd13971  152 EEVLVETFEEGVPISRTVLAH----------GGEPLKRKLARIGLDAFLKMLFVDNFVHGDLHPGNILVRFNDSNRPSLL 221

                        250
                 ....*....|..
gi 186530942 311 GQVKELPNKLRL 322
Cdd:cd13971  222 VSLDARGSPPRL 233
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 197-312 4.62e-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: 46.49  E-value: 4.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 197 KREANAMERircfLYENNkkspVLVPRVLRDMVTKRVLVMEYINGIPILSIGDEMAKRginphgkiaeaakhnilNSLSR 276
Cdd:COG3642    4 RREARLLRE----LREAG----VPVPKVLDVDPDDADLVMEYIEGETLADLLEEGELP-----------------PELLR 58

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 186530942 277 AYGQMILK---SGFFHADPHPGNILICkGQEVALLDYGQ 312
Cdd:COG3642   59 ELGRLLARlhrAGIVHGDLTTSNILVD-DGGVYLIDFGL 96
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
 236-352 1.06e-05

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK 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: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 47.03  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 236 MEYINGIPILSIGDEMAKRG--INPH--GKIAEaakhNILNSLSRAYGQMILksgffHADPHPGNILICKGQEVALLDYG 311
Cdd:cd06621   80 MEYCEGGSLDSIYKKVKKKGgrIGEKvlGKIAE----SVLKGLSYLHSRKII-----HRDIKPSNILLTRKGQVKLCDFG 150

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 186530942 312 QVKELPNKLRLGYANLVIAMA----DNNASRVSQSFWEMG--LHTVA 352
Cdd:cd06621  151 VSGELVNSLAGTFTGTSYYMAperiQGGPYSITSDVWSLGltLLEVA 197
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
 195-316 1.27e-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: 46.81  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 195 DFKREANAMERIRcflyENNkkspvlVPRVLrDMVT--KRV-LVMEYINGIpilSIGDEMAKRGINPHGKIAEAAKHnIL 271
Cdd:cd14014   46 RFLREARALARLS----HPN------IVRVY-DVGEddGRPyIVMEYVEGG---SLADLLRERGPLPPREALRILAQ-IA 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 186530942 272 NSLSRAYGQmilksGFFHADPHPGNILICKGQEVALLDYGQVKEL 316
Cdd:cd14014  111 DALAAAHRA-----GIVHRDIKPANILLTEDGRVKLTDFGIARAL 150
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
196-311 3.14e-05

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 46.16  E-value: 3.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 196 FKREANAMERIRcflYENnkkspvlVPRVLrDMVTKR---VLVMEYINGIpilSIGDEMAKRGINPhgkIAEAAK--HNI 270
Cdd:COG0515   54 FRREARALARLN---HPN-------IVRVY-DVGEEDgrpYLVMEYVEGE---SLADLLRRRGPLP---PAEALRilAQL 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 186530942 271 LNSLSRAYGQmilksGFFHADPHPGNILICKGQEVALLDYG 311
Cdd:COG0515  117 AEALAAAHAA-----GIVHRDIKPANILLTPDGRVKLIDFG 152
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 195-311 2.49e-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: 41.52  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 195 DFKREANAMErircFLyenNKKSPVLVPRVLrDMVTKR---VLVMEYINGIPILSIGDEMAkrgINPHGKIAEAAKhNIL 271
Cdd:cd05120   35 DLEKEAAMLQ----LL---AGKLSLPVPKVY-GFGESDgweYLLMERIEGETLSEVWPRLS---EEEKEKIADQLA-EIL 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 186530942 272 NSLSRaygqmILKSGFFHADPHPGNILI-CKGQEVALLDYG 311
Cdd:cd05120  103 AALHR-----IDSSVLTHGDLHPGNILVkPDGKLSGIIDWE 138
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
 197-311 5.85e-04

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: 41.04  E-value: 5.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942  197 KREANAMERIRcflyennkKSPVLVPrVLRDM-VTKRVLVMEYINGipilsigdEMAKRGINPHGkiaeaakhnilNSLS 275
Cdd:TIGR03724  45 RREARLLSRAR--------KAGVNTP-VIYDVdPDNKTIVMEYIEG--------KPLKDVIEENG-----------DELA 96

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 186530942  276 RAYGQMILK---SGFFHADPHPGNILICKGQEVaLLDYG 311
Cdd:TIGR03724  97 REIGRLVGKlhkAGIVHGDLTTSNIIVRDDKVY-LIDFG 134
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
 195-381 6.20e-04

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: 41.10  E-value: 6.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 195 DFKREANAMERIRCflyennkkspvlvPRVLR--DMVTKR---VLVMEYINGIpilSIGDEMAKRGinphGKIAEAAKHN 269
Cdd:cd00180   37 ELLREIEILKKLNH-------------PNIVKlyDVFETEnflYLVMEYCEGG---SLKDLLKENK----GPLSEEEALS 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 270 ILNSLSRAYgQMILKSGFFHADPHPGNILICKGQEVALLDYGQVKELPNK----LRLGYANLVIAMADNNASRVSQS--- 342
Cdd:cd00180   97 ILRQLLSAL-EYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDdsllKTTGGTTPPYYAPPELLGGRYYGpkv 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 186530942 343 --------FWEMglhtvakceNEQQELLRLAQTLFDTKMPTGQTVLQ 381
Cdd:cd00180  176 diwslgviLYEL---------EELKDLIRRMLQYDPKKRPSAKELLE 213
PRK14879 PRK14879
Kae1-associated kinase Bud32;
197-311 9.02e-04

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 40.66  E-value: 9.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 197 KREANAMERIRcflyennkKSPVLVPRVLRDMVTKRVLVMEYINGIPILSIGDEMAkrginphgkiaeaakhNILNSLSR 276
Cdd:PRK14879  47 RREARIMSRAR--------KAGVNVPAVYFVDPENFIIVMEYIEGEPLKDLINSNG----------------MEELELSR 102

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 186530942 277 AYGQMILK---SGFFHADPHPGNILIcKGQEVALLDYG 311
Cdd:PRK14879 103 EIGRLVGKlhsAGIIHGDLTTSNMIL-SGGKIYLIDFG 139
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
 197-309 1.24e-03

RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction mechanisms];


Pssm-ID: 440246 [Multi-domain]  Cd Length: 183  Bit Score: 39.89  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 197 KREANAMERircfLYENNkkspVLVPRVLRdmVTKRVLVMEYINGIpilsigdEMAKRGINPHGKIAEAakhnILNSLSR 276
Cdd:COG0478   47 EREFRALER----LYPAG----LPVPRPIA--ANRHAIVMERIEGV-------ELARLKLEDPEEVLDK----ILEEIRR 105

                         90       100       110
                 ....*....|....*....|....*....|...
gi 186530942 277 AYgqmilKSGFFHADPHPGNILICKGQEVALLD 309
Cdd:COG0478  106 AH-----DAGIVHADLSEYNILVDDDGGVWIID 133
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
 175-312 1.74e-03

RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria and eukaryotes. Activity of Rio1 is vital in Saccharomyces cerevisiae for the processing of ribosomal RNA, as well as for proper cell cycle progression and chromosome maintenance. The structure of RIO1 has been determined.


Pssm-ID: 460091 [Multi-domain]  Cd Length: 184  Bit Score: 39.52  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942  175 IKFDLHSIT--KEMEKQIGYEFDFK---------------REANAMERircfLYEnnkkSPVLVPRVLrdMVTKRVLVME 237
Cdd:pfam01163  15 VKIYRTGTTsfKKRKRYRSGDFRFRdrktswrylvrlwaeKEFRNLKR----LYE----AGVPVPKPI--DVNRHVLVME 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186530942  238 YINgipilSIGDEMAKRGINPHGKIAEAAkHNILNSLSRAYGqmilKSGFFHADPHPGNILICKGqEVALLDYGQ 312
Cdd:pfam01163  85 FIG-----KDGVPAPKLKDVELEEAEEIY-DEIIREMRRLYQ----EAGLVHGDLSEYNILVHDD-KPVIIDVPQ 148
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
 234-311 3.33e-03

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK 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: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 39.26  E-value: 3.33e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 186530942 234 LVMEYINGIPILSIGDEMAKRGINPHGKIAEAAKhNILNSLSraYgqmILKSGFFHADPHPGNILICKGQEVALLDYG 311
Cdd:cd06610   76 LVMPLLSGGSLLDIMKSSYPRGGLDEAIIATVLK-EVLKGLE--Y---LHSNGQIHRDVKAGNILLGEDGSVKIADFG 147
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
 197-312 7.17e-03

C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is present in archaea and eukaryotes. It contains an N-terminal winged helix (wHTH) domain and a C-terminal RIO kinase catalytic domain. The wHTH domain is primarily seen in DNA-binding proteins, although some wHTH domains may be involved in RNA recognition. RIO2 is essential for survival and is necessary for rRNA cleavage during 40S ribosomal subunit maturation. RIO kinases are atypical protein serine kinases containing a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. The RIO2 kinase catalytic domain 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), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270695 [Multi-domain]  Cd Length: 183  Bit Score: 37.48  E-value: 7.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186530942 197 KREANAMERircfLYENNkkspVLVPRVL---RDMVtkrvlVMEYINGIPILSIgdemaKRGINPhgkiaEAAKHNILNS 273
Cdd:cd05144   66 EKEFAALKA----LYEEG----FPVPKPIdwnRHAV-----VMELIDGYPLYQV-----RLLEDP-----EEVLDEILEL 122

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 186530942 274 LSRAYgqmilKSGFFHADPHPGNILICKGQEVALLDYGQ 312
Cdd:cd05144  123 IVKLA-----KHGLIHGDFSEFNILVDEDEKITVIDFPQ 156
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH