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Conserved domains on  [gi|801185686|emb|CFA20858|]
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protein kinase [Mycobacterium tuberculosis]

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

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List of domain hits

Name Accession Description Interval E-value
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
77-477 2.37e-130

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: 386.87  E-value: 2.37e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686  77 RFIGRLPRKGPWQQKVIKELPQTFADLGPTYVKFGQIIASSPGAFGESLSREFRGLLDRVPPAKTDEVHKLFVEELGDEP 156
Cdd:COG0661   36 RLLTGEERREELRRRRAERLRLALEELGPTFIKLGQLLSTRPDLLPPEYAEELAKLQDRVPPFPFEEVRAVIEEELGRPL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 157 ARLFASFEEEPFASASIAQVHYATLRSGEEVVVKIQRPGIRRRVAADLQILKRFAQTVE-LAKLGRRLSAQDVVADFADN 235
Cdd:COG0661  116 EELFAEFDPEPLAAASIGQVHRARLKDGREVAVKVQRPGIEEAIEADLRILRRLARLLErLSPEGRRLDPVEVVDEFARS 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 236 LAEELDFRLEAQSMEAWVSHLHASPlgkNIRVPQVHWDFTTERVLTMERVHGIRIDNAAAIRKAGFDGVELVKALLFSVF 315
Cdd:COG0661  196 LLEELDYRREAANAERFRRNFADDP---DVYVPKVYWELSTRRVLTMEWIDGIKISDLEALDAAGIDRKRLAERLVRAFL 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 316 EGGLRHGLFHGDLHAGNLYVDEAGRIVFFDFGIMGRIDPRTRWLLRELVYAlLVKKDHAAAGKIVVLMGAVGTMKPETQA 395
Cdd:COG0661  273 RQVFRDGFFHADPHPGNIFVLPDGRLVLLDFGMVGRLDPETREGLAELLLA-LLNRDYDRVAEALLELGFVPPDTDVDEL 351
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 396 AKDLERFATPLTMQSLGDMSYADIGRQLSALADAYDVKLPRELVLIGKQFLYVERYMKLLAPRWQMMSDpqLTGYFANFM 475
Cdd:COG0661  352 ERALRAVLEPYFGKPLKDISFGELLLELFELARRFPLRLPPELVLLQRTLLTLEGVGRQLDPDFDLWEV--AKPFLERLL 429

                 ..
gi 801185686 476 VE 477
Cdd:COG0661  430 RE 431
 
Name Accession Description Interval E-value
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
77-477 2.37e-130

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: 386.87  E-value: 2.37e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686  77 RFIGRLPRKGPWQQKVIKELPQTFADLGPTYVKFGQIIASSPGAFGESLSREFRGLLDRVPPAKTDEVHKLFVEELGDEP 156
Cdd:COG0661   36 RLLTGEERREELRRRRAERLRLALEELGPTFIKLGQLLSTRPDLLPPEYAEELAKLQDRVPPFPFEEVRAVIEEELGRPL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 157 ARLFASFEEEPFASASIAQVHYATLRSGEEVVVKIQRPGIRRRVAADLQILKRFAQTVE-LAKLGRRLSAQDVVADFADN 235
Cdd:COG0661  116 EELFAEFDPEPLAAASIGQVHRARLKDGREVAVKVQRPGIEEAIEADLRILRRLARLLErLSPEGRRLDPVEVVDEFARS 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 236 LAEELDFRLEAQSMEAWVSHLHASPlgkNIRVPQVHWDFTTERVLTMERVHGIRIDNAAAIRKAGFDGVELVKALLFSVF 315
Cdd:COG0661  196 LLEELDYRREAANAERFRRNFADDP---DVYVPKVYWELSTRRVLTMEWIDGIKISDLEALDAAGIDRKRLAERLVRAFL 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 316 EGGLRHGLFHGDLHAGNLYVDEAGRIVFFDFGIMGRIDPRTRWLLRELVYAlLVKKDHAAAGKIVVLMGAVGTMKPETQA 395
Cdd:COG0661  273 RQVFRDGFFHADPHPGNIFVLPDGRLVLLDFGMVGRLDPETREGLAELLLA-LLNRDYDRVAEALLELGFVPPDTDVDEL 351
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 396 AKDLERFATPLTMQSLGDMSYADIGRQLSALADAYDVKLPRELVLIGKQFLYVERYMKLLAPRWQMMSDpqLTGYFANFM 475
Cdd:COG0661  352 ERALRAVLEPYFGKPLKDISFGELLLELFELARRFPLRLPPELVLLQRTLLTLEGVGRQLDPDFDLWEV--AKPFLERLL 429

                 ..
gi 801185686 476 VE 477
Cdd:COG0661  430 RE 431
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
132-379 7.25e-100

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: 299.92  E-value: 7.25e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686  132 LLDRVPPAKTDEVHKLFVEELGDEPARLFASFEEEPFASASIAQVHYATLRSGEEVVVKIQRPGIRRRVAADLQILKRFA 211
Cdd:pfam03109   2 LQDRAPPFPFEQAKKVIEEELGAPVEEIFAEFDEEPIAAASIAQVHRARLKDGEEVAVKVQRPGVKKRIRSDLLLLRFLA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686  212 QTVE-LAKLGRRLsaQDVVADFADNLAEELDFRLEAQSMEAWVSHLHASPlgkNIRVPQVHWDFTTERVLTMERVHGIRI 290
Cdd:pfam03109  82 KVAKrFFPGFRRL--DWLVDEFRKSLPQELDFLREAANAEKFRENFADDP---DVYVPKVYWELTTERVLTMEYVDGIKI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686  291 DNAAAIRKAGFDGVELVKALLFSVFEGGLRHGLFHGDLHAGNLYVDEAGRIVFFDFGIMGRIDPRTRWLLRELVYAlLVK 370
Cdd:pfam03109 157 DDLDALSEAGIDRKEIARRLVELFLEQIFRDGFFHADPHPGNILVRKDGRIVLLDFGLMGRLDEKFRRLYAELLLA-LVN 235

                  ....*....
gi 801185686  371 KDHAAAGKI 379
Cdd:pfam03109 236 RDYKRVAEM 244
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
132-380 6.73e-98

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: 295.17  E-value: 6.73e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 132 LLDRVPPAKTDEVHKLFVEELGDEPARLFASFEEEPFASASIAQVHYATLRSGEEVVVKIQRPGIRRRVAADLQILKRFA 211
Cdd:cd05121    2 LQDDVPPFPFEEVRKIIEEELGRPLEEVFAEFDPEPLAAASIAQVHRARLKDGREVAVKVQRPGIEEIIEADLRILRRLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 212 QTVE-LAKLGRRLSAQDVVADFADNLAEELDFRLEAQSMEAWVSHLHASPlgkNIRVPQVHWDFTTERVLTMERVHGIRI 290
Cdd:cd05121   82 RLLErLSPLLRRLDLVAIVDEFARSLLEELDFRREARNAERFRKNLKDSP---DVYVPKVYPELSTRRVLVMEYIDGVKL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 291 DNAAAIRKAGFDGVELVKALLFSVFEGGLRHGLFHGDLHAGNLYVDEAGRIVFFDFGIMGRIDPRTRWLLRELVYAlLVK 370
Cdd:cd05121  159 TDLEALRAAGIDRKELARRLVDAYLKQIFEDGFFHADPHPGNILVLPDGRIALLDFGMVGRLDPETREALADLLLA-LVN 237
                        250
                 ....*....|
gi 801185686 371 KDHAAAGKIV 380
Cdd:cd05121  238 GDAEGLAEAL 247
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
71-461 1.14e-97

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: 301.14  E-value: 1.14e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686   71 VTRTAVRFIGRLPRKG-PWQQKVIKE-------LPQTFADLGPTYVKFGQIIASSPGAFGESLSREFRGLLDRVPPAKTD 142
Cdd:TIGR01982  20 VESPIGPLSLRLLRRLlLPFSNRENRlmsrgerLRLALEELGPTFIKFGQTLSTRADLLPADIAEELSLLQDRVPPFDFK 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686  143 EVHKLFVEELGDEPARLFASFEEEPFASASIAQVHYATLRSGEEVVVKIQRPGIRRRVAADLQILKRFAQTVE-LAKLGR 221
Cdd:TIGR01982 100 VARKVIEAALGGPLEELFAEFEEKPLAAASIAQVHRARLVDGKEVAVKVLRPGIEKTIAADIALLYRLARIVErLSPDSR 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686  222 RLSAQDVVADFADNLAEELDFRLEAQsmeawvshlHASPLGKN------IRVPQVHWDFTTERVLTMERVHGIRIDNAAA 295
Cdd:TIGR01982 180 RLRPTEVVKEFEKTLRRELDLRREAA---------NASELGENfkndpgVYVPEVYWDRTSERVLTMEWIDGIPLSDIAA 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686  296 IRKAGFDGVELVKALLFSVFEGGLRHGLFHGDLHAGNLYVDEAGRIVFFDFGIMGRIDPRTRWLLRELVYAlLVKKDHAA 375
Cdd:TIGR01982 251 LDEAGLDRKALAENLARSFLNQVLRDGFFHADLHPGNIFVLKDGKIIALDFGIVGRLSEEDRRYLAEILYG-FLNRDYRR 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686  376 AGKIVVLMGAVGTMKPETQAAKDLERFATPLTMQSLGDMSYADIGRQLSALADAYDVKLPRELVLIGKQFLYVERYMKLL 455
Cdd:TIGR01982 330 VAEVHFDAGYVPSDTDMAEFEQAIRAIGEPIFGQPLKEISVGRLLAGLFKITRDFNMELQPQLLLLQKTLLTVEGVGRQL 409

                  ....*.
gi 801185686  456 APRWQM 461
Cdd:TIGR01982 410 DPDLNM 415
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
102-350 4.01e-61

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 208.61  E-value: 4.01e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 102 DLGPTYVKFGQIIASSPGAFGESLSREFRGLLDRVPPAKTDEVHKLFVEELGDEPARLFASFEEEPFASASIAQVHYATL 181
Cdd:PRK04750  61 ELGPIFVKFGQMLSTRRDLFPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQVHFARL 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 182 RS-GEEVVVKIQRPGIRRRVAADLQILKRFAQTVE-LAKLGRRLSAQDVVADFADNLAEELDFRLEAQSmeawvshlhAS 259
Cdd:PRK04750 141 KDnGREVVVKVLRPDILPVIDADLALMYRLARWVErLLPDGRRLKPREVVAEFEKTLHDELDLMREAAN---------AS 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 260 PLGKN------IRVPQVHWDFTTERVLTMERVHGIRIDNAAAIRKAGFD-------GVElvkaLLFS-VFegglRHGLFH 325
Cdd:PRK04750 212 QLRRNfedsdmLYVPEVYWDYCSETVMVMERMYGIPVSDVAALRAAGTDmkllaerGVE----VFFTqVF----RDGFFH 283
                        250       260
                 ....*....|....*....|....*....
gi 801185686 326 GDLHAGNLYVD----EAGRIVFFDFGIMG 350
Cdd:PRK04750 284 ADMHPGNIFVSydppENPRYIALDFGIVG 312
 
Name Accession Description Interval E-value
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
77-477 2.37e-130

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: 386.87  E-value: 2.37e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686  77 RFIGRLPRKGPWQQKVIKELPQTFADLGPTYVKFGQIIASSPGAFGESLSREFRGLLDRVPPAKTDEVHKLFVEELGDEP 156
Cdd:COG0661   36 RLLTGEERREELRRRRAERLRLALEELGPTFIKLGQLLSTRPDLLPPEYAEELAKLQDRVPPFPFEEVRAVIEEELGRPL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 157 ARLFASFEEEPFASASIAQVHYATLRSGEEVVVKIQRPGIRRRVAADLQILKRFAQTVE-LAKLGRRLSAQDVVADFADN 235
Cdd:COG0661  116 EELFAEFDPEPLAAASIGQVHRARLKDGREVAVKVQRPGIEEAIEADLRILRRLARLLErLSPEGRRLDPVEVVDEFARS 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 236 LAEELDFRLEAQSMEAWVSHLHASPlgkNIRVPQVHWDFTTERVLTMERVHGIRIDNAAAIRKAGFDGVELVKALLFSVF 315
Cdd:COG0661  196 LLEELDYRREAANAERFRRNFADDP---DVYVPKVYWELSTRRVLTMEWIDGIKISDLEALDAAGIDRKRLAERLVRAFL 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 316 EGGLRHGLFHGDLHAGNLYVDEAGRIVFFDFGIMGRIDPRTRWLLRELVYAlLVKKDHAAAGKIVVLMGAVGTMKPETQA 395
Cdd:COG0661  273 RQVFRDGFFHADPHPGNIFVLPDGRLVLLDFGMVGRLDPETREGLAELLLA-LLNRDYDRVAEALLELGFVPPDTDVDEL 351
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 396 AKDLERFATPLTMQSLGDMSYADIGRQLSALADAYDVKLPRELVLIGKQFLYVERYMKLLAPRWQMMSDpqLTGYFANFM 475
Cdd:COG0661  352 ERALRAVLEPYFGKPLKDISFGELLLELFELARRFPLRLPPELVLLQRTLLTLEGVGRQLDPDFDLWEV--AKPFLERLL 429

                 ..
gi 801185686 476 VE 477
Cdd:COG0661  430 RE 431
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
132-379 7.25e-100

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: 299.92  E-value: 7.25e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686  132 LLDRVPPAKTDEVHKLFVEELGDEPARLFASFEEEPFASASIAQVHYATLRSGEEVVVKIQRPGIRRRVAADLQILKRFA 211
Cdd:pfam03109   2 LQDRAPPFPFEQAKKVIEEELGAPVEEIFAEFDEEPIAAASIAQVHRARLKDGEEVAVKVQRPGVKKRIRSDLLLLRFLA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686  212 QTVE-LAKLGRRLsaQDVVADFADNLAEELDFRLEAQSMEAWVSHLHASPlgkNIRVPQVHWDFTTERVLTMERVHGIRI 290
Cdd:pfam03109  82 KVAKrFFPGFRRL--DWLVDEFRKSLPQELDFLREAANAEKFRENFADDP---DVYVPKVYWELTTERVLTMEYVDGIKI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686  291 DNAAAIRKAGFDGVELVKALLFSVFEGGLRHGLFHGDLHAGNLYVDEAGRIVFFDFGIMGRIDPRTRWLLRELVYAlLVK 370
Cdd:pfam03109 157 DDLDALSEAGIDRKEIARRLVELFLEQIFRDGFFHADPHPGNILVRKDGRIVLLDFGLMGRLDEKFRRLYAELLLA-LVN 235

                  ....*....
gi 801185686  371 KDHAAAGKI 379
Cdd:pfam03109 236 RDYKRVAEM 244
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
132-380 6.73e-98

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: 295.17  E-value: 6.73e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 132 LLDRVPPAKTDEVHKLFVEELGDEPARLFASFEEEPFASASIAQVHYATLRSGEEVVVKIQRPGIRRRVAADLQILKRFA 211
Cdd:cd05121    2 LQDDVPPFPFEEVRKIIEEELGRPLEEVFAEFDPEPLAAASIAQVHRARLKDGREVAVKVQRPGIEEIIEADLRILRRLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 212 QTVE-LAKLGRRLSAQDVVADFADNLAEELDFRLEAQSMEAWVSHLHASPlgkNIRVPQVHWDFTTERVLTMERVHGIRI 290
Cdd:cd05121   82 RLLErLSPLLRRLDLVAIVDEFARSLLEELDFRREARNAERFRKNLKDSP---DVYVPKVYPELSTRRVLVMEYIDGVKL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 291 DNAAAIRKAGFDGVELVKALLFSVFEGGLRHGLFHGDLHAGNLYVDEAGRIVFFDFGIMGRIDPRTRWLLRELVYAlLVK 370
Cdd:cd05121  159 TDLEALRAAGIDRKELARRLVDAYLKQIFEDGFFHADPHPGNILVLPDGRIALLDFGMVGRLDPETREALADLLLA-LVN 237
                        250
                 ....*....|
gi 801185686 371 KDHAAAGKIV 380
Cdd:cd05121  238 GDAEGLAEAL 247
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
71-461 1.14e-97

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: 301.14  E-value: 1.14e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686   71 VTRTAVRFIGRLPRKG-PWQQKVIKE-------LPQTFADLGPTYVKFGQIIASSPGAFGESLSREFRGLLDRVPPAKTD 142
Cdd:TIGR01982  20 VESPIGPLSLRLLRRLlLPFSNRENRlmsrgerLRLALEELGPTFIKFGQTLSTRADLLPADIAEELSLLQDRVPPFDFK 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686  143 EVHKLFVEELGDEPARLFASFEEEPFASASIAQVHYATLRSGEEVVVKIQRPGIRRRVAADLQILKRFAQTVE-LAKLGR 221
Cdd:TIGR01982 100 VARKVIEAALGGPLEELFAEFEEKPLAAASIAQVHRARLVDGKEVAVKVLRPGIEKTIAADIALLYRLARIVErLSPDSR 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686  222 RLSAQDVVADFADNLAEELDFRLEAQsmeawvshlHASPLGKN------IRVPQVHWDFTTERVLTMERVHGIRIDNAAA 295
Cdd:TIGR01982 180 RLRPTEVVKEFEKTLRRELDLRREAA---------NASELGENfkndpgVYVPEVYWDRTSERVLTMEWIDGIPLSDIAA 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686  296 IRKAGFDGVELVKALLFSVFEGGLRHGLFHGDLHAGNLYVDEAGRIVFFDFGIMGRIDPRTRWLLRELVYAlLVKKDHAA 375
Cdd:TIGR01982 251 LDEAGLDRKALAENLARSFLNQVLRDGFFHADLHPGNIFVLKDGKIIALDFGIVGRLSEEDRRYLAEILYG-FLNRDYRR 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686  376 AGKIVVLMGAVGTMKPETQAAKDLERFATPLTMQSLGDMSYADIGRQLSALADAYDVKLPRELVLIGKQFLYVERYMKLL 455
Cdd:TIGR01982 330 VAEVHFDAGYVPSDTDMAEFEQAIRAIGEPIFGQPLKEISVGRLLAGLFKITRDFNMELQPQLLLLQKTLLTVEGVGRQL 409

                  ....*.
gi 801185686  456 APRWQM 461
Cdd:TIGR01982 410 DPDLNM 415
UbiB cd13972
Ubiquinone biosynthetic protein UbiB; UbiB is the prokaryotic homolog of yeast Abc1p and human ...
132-368 6.76e-78

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: 243.65  E-value: 6.76e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 132 LLDRVPPAKTDEVHKLFVEELGDEPARLFASFEEEPFASASIAQVHYATLRSGEEVVVKIQRPGIRRRVAADLQILKRFA 211
Cdd:cd13972    2 LQDRVPPFSGKEARAIIEAELGKPLDALFSDFDEEPVAAASIAQVHKARLLDGREVAVKVLRPGIEKRIERDLELLRFLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 212 QTVE-LAKLGRRLSAQDVVADFADNLAEELDFRLEAQSMEAWVSHLHASPlgkNIRVPQVHWDFTTERVLTMERVHGIRI 290
Cdd:cd13972   82 RLAErLLPEARRLRPVEVVKEFARSLLLELDLRLEAANASELRENFLDDP---GFYVPEVYWELTSKNVLTMEWIDGIPI 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 801185686 291 DNAAAIRKAGFDGVELVKALLFSVFEGGLRHGLFHGDLHAGNLYVDEAGRIVFFDFGIMGRIDPRTRWLLRELVYALL 368
Cdd:cd13972  159 SDIEALDAAGIDRKALAERLVEIFFRQVFRDGFFHADMHPGNIFVDPNGRIIAVDFGIMGRLDKKDRRYLAEILYGFL 236
ADCK1-like cd13969
aarF domain containing kinase 1 and similar proteins; This subfamily is composed of ...
132-384 1.87e-62

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: 203.87  E-value: 1.87e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 132 LLDRVPPAKTDEVHKLFVEELGDEPARLFASFEEEPFASASIAQVHYATLRSGEEVVVKIQRPGIRRRVAADLQILKRFA 211
Cdd:cd13969    2 LQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVHKAKLKDGEEVAVKVQHPDLRKQFAGDLATMEFLV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 212 QTVElaKLGRRLSAQDVVADFADNLAEELDFRLEAQSMEAWVSHLHaspLGKNIRVPQVHWDFTTERVLTMERVHGIRID 291
Cdd:cd13969   82 NLVE--KLFPDFPFSWLVDELKKNLPKELDFLNEARNAERCAKLFK---HRPDVYVPKVYWDLSSKRVLTMEFIDGIKID 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 292 NAAAIRKAGFDgVELVKALLFSVF-EGGLRHGLFHGDLHAGNLYV-----DEAGRIVFFDFGIMGRIDPRTRWLLRELVY 365
Cdd:cd13969  157 DVEALKKLGID-PKEVARLLSEAFaEMIFVHGFVHCDPHPGNLLVrknpgPGKPQIVLLDHGLYRELDEEFRLNYCRLWK 235
                        250
                 ....*....|....*....
gi 801185686 366 AlLVKKDHAAAGKIVVLMG 384
Cdd:cd13969  236 A-LILGDEKKIKKYSKALG 253
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
102-350 4.01e-61

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 208.61  E-value: 4.01e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 102 DLGPTYVKFGQIIASSPGAFGESLSREFRGLLDRVPPAKTDEVHKLFVEELGDEPARLFASFEEEPFASASIAQVHYATL 181
Cdd:PRK04750  61 ELGPIFVKFGQMLSTRRDLFPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQVHFARL 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 182 RS-GEEVVVKIQRPGIRRRVAADLQILKRFAQTVE-LAKLGRRLSAQDVVADFADNLAEELDFRLEAQSmeawvshlhAS 259
Cdd:PRK04750 141 KDnGREVVVKVLRPDILPVIDADLALMYRLARWVErLLPDGRRLKPREVVAEFEKTLHDELDLMREAAN---------AS 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 260 PLGKN------IRVPQVHWDFTTERVLTMERVHGIRIDNAAAIRKAGFD-------GVElvkaLLFS-VFegglRHGLFH 325
Cdd:PRK04750 212 QLRRNfedsdmLYVPEVYWDYCSETVMVMERMYGIPVSDVAALRAAGTDmkllaerGVE----VFFTqVF----RDGFFH 283
                        250       260
                 ....*....|....*....|....*....
gi 801185686 326 GDLHAGNLYVD----EAGRIVFFDFGIMG 350
Cdd:PRK04750 284 ADMHPGNIFVSydppENPRYIALDFGIVG 312
ABC1_ADCK3 cd13970
Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This ...
132-368 1.12e-55

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: 186.18  E-value: 1.12e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 132 LLDRVPPAKTDEVHKLFVEELGDEPARLFASFEEEPFASASIAQVHYATLRSGEEVVVKIQRPGIRRRVAADLQILKRFA 211
Cdd:cd13970    6 LRDSAPPMPWAQLEKVLEAELGEDWRELFAEFDEEPFAAASIGQVHRATLKDGREVAVKVQYPGVAESIDSDLNNLRRLL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 212 QTVELAKLGRRLsaQDVVADFADNLAEELDFRLEAQSMEAWVSHLHASPlgkNIRVPQVHWDFTTERVLTMERVHGIRID 291
Cdd:cd13970   86 KLTGLLPKGLDL--DALIAELREELLEECDYEREAANQRRFRELLADDP---RFVVPEVIPELSTKRVLTTEFVDGVPLD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 292 NAA----AIRKAGfdGVELVKALLFSVFEgglrHGLFHGDLHAGN-LYVDEAGRIVFFDFGIMGRIDPRTRWLLRELVYA 366
Cdd:cd13970  161 EAAdlsqEERNRI--GELLLRLCLRELFE----FGFMQTDPNPGNfLYDPEDGRLGLLDFGAVREYPPEFVDGYRRLVRA 234

                 ..
gi 801185686 367 LL 368
Cdd:cd13970  235 AL 236
ADCK2-like cd13971
aarF domain containing kinase 2 and similar proteins; This subfamily is composed of ...
150-404 9.11e-33

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


Pssm-ID: 270873 [Multi-domain]  Cd Length: 298  Bit Score: 126.18  E-value: 9.11e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 150 EELGDEPARLFASFEEEPFASASIAQVHYATLRS--------GEEVVVKIQRPGIRRRVAADLQILKRFAQTVELAKLGR 221
Cdd:cd13971   20 AAFGKDWEDIFEEFDEEPIGSGSIAQVHRAKLKPdyggdgggPRVVAVKVLHPGVREQIERDLAILRLFAKLLEAIPPLR 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 222 RLSAQDVVADFADNLAEELDFRLEAQSMEAWVSHLHASplgKNIRVPQVHWDFTTERVLTMERVHGIRI------DNAAA 295
Cdd:cd13971  100 WLSLPESVEQFASLMLRQLDLRVEAANLERFRENFKDR---KDVSFPKPLYPLVTEEVLVETFEEGVPIsrtvlaHGGEP 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 296 IRKA----GFDgvelvkALLFSVFegglRHGLFHGDLHAGNLYVDEAG-----------------RIVFFDFGIMGRIDP 354
Cdd:cd13971  177 LKRKlariGLD------AFLKMLF----VDNFVHGDLHPGNILVRFNDsnrpsllvsldargsppRLVFLDAGLVTELSP 246
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 801185686 355 RTRWLLRELVYALLVKKDHAAAGKIVvlmgavgTMKPETQAAKDLERFAT 404
Cdd:cd13971  247 QDRRNFIDLFKAVARGDGYKAAELML-------ERSRSSQTCPDPEGFKS 289
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
265-358 7.27e-05

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: 43.02  E-value: 7.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 265 IRVPQVHwDFTTER-VLTMERVHGIRIdnAAAIRKAGFDgVELVKALlfsvfeGGL-----RHGLFHGDLHAGNLYVDEa 338
Cdd:COG3642   18 VPVPKVL-DVDPDDaDLVMEYIEGETL--ADLLEEGELP-PELLREL------GRLlarlhRAGIVHGDLTTSNILVDD- 86
                         90       100
                 ....*....|....*....|
gi 801185686 339 GRIVFFDFGiMGRIDPRTRW 358
Cdd:COG3642   87 GGVYLIDFG-LARYSDPLED 105
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
219-348 5.51e-04

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 42.31  E-value: 5.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 219 LGRRLSAQDVVA------DFADNLAEELDFRLEAQSMEAwVSHLHasplgknirVPQVHwDFTTER---VLTMERVHGIR 289
Cdd:COG0515   25 LARDLRLGRPVAlkvlrpELAADPEARERFRREARALAR-LNHPN---------IVRVY-DVGEEDgrpYLVMEYVEGES 93
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 801185686 290 IdnAAAIRKAGFDGVELVKALLFSVFEGgL----RHGLFHGDLHAGNLYVDEAGRIVFFDFGI 348
Cdd:COG0515   94 L--ADLLRRRGPLPPAEALRILAQLAEA-LaaahAAGIVHRDIKPANILLTPDGRVKLIDFGI 153
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
237-354 2.03e-03

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


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 38.82  E-value: 2.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 237 AEELDFRLEAQSMEAWVSHLhasplgkNIRVPQVHWDFTTER--VLTMERVHGIRIDNAAairkaGFDGVELVKALLFSV 314
Cdd:cd05120   31 RLKKDLEKEAAMLQLLAGKL-------SLPVPKVYGFGESDGweYLLMERIEGETLSEVW-----PRLSEEEKEKIADQL 98
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 801185686 315 FEGgLRH-------GLFHGDLHAGNLYVDEAGRIV-FFDFGIMGRIDP 354
Cdd:cd05120   99 AEI-LAAlhridssVLTHGDLHPGNILVKPDGKLSgIIDWEFAGYGPP 145
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
301-367 4.00e-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: 38.35  E-value: 4.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801185686 301 FDGVELVKALLfSVFEGGL-----------RHGLFHGDLHAGNLYVDEAGRIVFFDF--GIMGRIDPRTRWLLRELVYAL 367
Cdd:COG0478   79 IEGVELARLKL-EDPEEVLdkileeirrahDAGIVHADLSEYNILVDDDGGVWIIDWpqAVPRDHPNAEELLERDLENLL 157
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
311-374 5.26e-03

Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal transduction mechanisms]; Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist is part of the Pathway/BioSystem: Threonine biosynthesis


Pssm-ID: 441905 [Multi-domain]  Cd Length: 297  Bit Score: 38.75  E-value: 5.26e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 801185686 311 LFSVFEGGLRHGLFHGDLHAGNLYVDEAGRIVFFDFGIMgridpRTRWLLRELVYALLVKKDHA 374
Cdd:COG2334  169 RLAPLLGALPRGVIHGDLHPDNVLFDGDGVSGLIDFDDA-----GYGPRLYDLAIALNGWADGP 227
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
318-354 8.31e-03

Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.


Pssm-ID: 426359 [Multi-domain]  Cd Length: 239  Bit Score: 37.87  E-value: 8.31e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 801185686  318 GLRHGLFHGDLHAGNLYVDEAGRIV-FFDFGIMGRIDP 354
Cdd:pfam01636 164 ELPPVLVHGDLHPGNLLVDPGGRVSgVIDFEDAGLGDP 201
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
324-354 9.39e-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: 37.60  E-value: 9.39e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 801185686 324 FHGDLHAGNLYVDEaGRIV-FFDFGIMGRIDP 354
Cdd:cd05155  166 LHGDLHPGNLLVRD-GRLSaVIDFGDLGVGDP 196
 
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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