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Conserved domains on  [gi|118616521|ref|YP_904853.1|]
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hypothetical protein MUL_0734 [Mycobacterium ulcerans Agy99]

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List of domain hits

Name Accession Description Interval E-value
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
105-353 2.44e-97

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: 295.94  E-value: 2.44e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 105 LLDRVPPADTDQVHKLFVEELGTEPAELFATFEEEPFASASIAQVHYATLKTGEEVVVKIQRPGIRRRVAADLQILQRFA 184
Cdd:cd05121    2 LQDDVPPFPFEEVRKIIEEELGRPLEEVFAEFDPEPLAAASIAQVHRARLKDGREVAVKVQRPGIEEIIEADLRILRRLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 185 QAVE-LAKLGRRLSAQDVVADFSDNLAVELDFRLEAQSMDAWVAHLHASPlgrNIRVPQVHWNFTSERVLTMERVHGVRI 263
Cdd:cd05121   82 RLLErLSPLLRRLDLVAIVDEFARSLLEELDFRREARNAERFRKNLKDSP---DVYVPKVYPELSTRRVLVMEYIDGVKL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 264 DNVAAIRKAGFDGTELVKALLFSVFEGGLRHGLFHGDLHAGNLYVDEEGRIVFFDFGIMGRIDPRTRWLLRELVYAlLVK 343
Cdd:cd05121  159 TDLEALRAAGIDRKELARRLVDAYLKQIFEDGFFHADPHPGNILVLPDGRIALLDFGMVGRLDPETREALADLLLA-LVN 237
                        250
                 ....*....|
gi 118616521 344 KDHAAAGKIV 353
Cdd:cd05121  238 GDAEGLAEAL 247
AarF COG0661
Predicted unusual protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family ...
6-450 3.31e-149

Predicted unusual protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport and metabolism, Signal transduction mechanisms];


:

Pssm-ID: 223733 [Multi-domain]  Cd Length: 517  Bit Score: 438.67  E-value: 3.31e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521   6 WHTAQMTTTKHREVAKLDRVPLPVEAARVAVTGWQVTRTAARFVTKLPGKGfasSWQQKIIKEIPQTFVDLGPTYVKFGQ 85
Cdd:COG0661    1 MLTLYAVSRLPRIIRVRLRYLLGRLLRLTGRLALLLRLLSWLGKSKLASSE---ELREKRAERLRLALEELGPTFIKLGQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521  86 IIASSPGAFGESLSREFRGLLDRVPPADTDQVHKLFVEELGTEPAELFATFEEEPFASASIAQVHYATLKTGEEVVVKIQ 165
Cdd:COG0661   78 ILSTRPDLVPPEYAEELAKLQDRVPPFPFEEAERIIEEELGRPIEELFSEFEPEPIASASIAQVHRAVLKSGEEVAVKVQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 166 RPGIRRRVAADLQILQRFAQAVELA-KLGRRLSAQDVVADFSDNLAVELDFRLEAQSMDAWVAHLHASPlgrNIRVPQVH 244
Cdd:COG0661  158 RPGIRERIEADLKLLRRLARLIKRLpPGGRRLDLVEVVDEFEKRLREELDYRREAANAERFRENFKDDP---DVYVPKVY 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 245 WNFTSERVLTMERVHGVRIDNVAAIRKAGFDGTELVKALLFSVFEGGLRHGLFHGDLHAGNLYVDEEGRIVFFDFGIMGR 324
Cdd:COG0661  235 WEYTTRRVLTMEWIDGIKISDIAALKSAGIDRKELAELLVRAFLRQLLRDGFFHADPHPGNILVRSDGRIVLLDFGIVGR 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 325 IDPRTRWLLRELVYALLvKKDHAAAGKIVVLMGAVGTMKPEAQAAKDLEKFATPLTMQSLGDMSYADIGRQLSALADAYD 404
Cdd:COG0661  315 LDPKFRRYLAELLLAFL-NRDYDRVAELHVELGYVPPDTDRDPLAAAIRAVLEPIYGKPLEEISFGEILDKLFEVARRFP 393
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 118616521 405 VKLPRELVLIGKQFLYVERYMKLLAPKWQMMS--DPQLTGYFANFMVE 450
Cdd:COG0661  394 MRLPPELVLLQRTLLLVEGVGRQLDPRFNLWAvaQPLLAKWLKKQLSP 441
 
Name Accession Description Interval E-value
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
105-353 2.44e-97

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: 295.94  E-value: 2.44e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 105 LLDRVPPADTDQVHKLFVEELGTEPAELFATFEEEPFASASIAQVHYATLKTGEEVVVKIQRPGIRRRVAADLQILQRFA 184
Cdd:cd05121    2 LQDDVPPFPFEEVRKIIEEELGRPLEEVFAEFDPEPLAAASIAQVHRARLKDGREVAVKVQRPGIEEIIEADLRILRRLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 185 QAVE-LAKLGRRLSAQDVVADFSDNLAVELDFRLEAQSMDAWVAHLHASPlgrNIRVPQVHWNFTSERVLTMERVHGVRI 263
Cdd:cd05121   82 RLLErLSPLLRRLDLVAIVDEFARSLLEELDFRREARNAERFRKNLKDSP---DVYVPKVYPELSTRRVLVMEYIDGVKL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 264 DNVAAIRKAGFDGTELVKALLFSVFEGGLRHGLFHGDLHAGNLYVDEEGRIVFFDFGIMGRIDPRTRWLLRELVYAlLVK 343
Cdd:cd05121  159 TDLEALRAAGIDRKELARRLVDAYLKQIFEDGFFHADPHPGNILVLPDGRIALLDFGMVGRLDPETREALADLLLA-LVN 237
                        250
                 ....*....|
gi 118616521 344 KDHAAAGKIV 353
Cdd:cd05121  238 GDAEGLAEAL 247
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
75-323 5.95e-63

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310  Cd Length: 537  Bit Score: 214.77  E-value: 5.95e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521  75 DLGPTYVKFGQIIASSPGAFGESLSREFRGLLDRVPPADTDQVHKLFVEELGTEPAELFATFEEEPFASASIAQVHYATL 154
Cdd:PRK04750  61 ELGPIFVKFGQMLSTRRDLFPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQVHFARL 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 155 K-TGEEVVVKIQRPGIRRRVAADLQILQRFAQAVE-LAKLGRRLSAQDVVADFSDNLAVELDFRLEAQSmdawvahlhAS 232
Cdd:PRK04750 141 KdNGREVVVKVLRPDILPVIDADLALMYRLARWVErLLPDGRRLKPREVVAEFEKTLHDELDLMREAAN---------AS 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 233 PLGRN------IRVPQVHWNFTSERVLTMERVHGVRIDNVAAIRKAGFDGTEL----VKALLFSVFegglRHGLFHGDLH 302
Cdd:PRK04750 212 QLRRNfedsdmLYVPEVYWDYCSETVMVMERMYGIPVSDVAALRAAGTDMKLLaergVEVFFTQVF----RDGFFHADMH 287
                        250       260
                 ....*....|....*....|....*
gi 118616521 303 AGNLYVD----EEGRIVFFDFGIMG 323
Cdd:PRK04750 288 PGNIFVSydppENPRYIALDFGIVG 312
ABC1 pfam03109
ABC1 family; This family includes ABC1 from yeast and AarF from Escherichia coli. These ...
123-244 7.58e-42

ABC1 family; This family includes ABC1 from yeast and AarF from Escherichia 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 Escherichia 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: 111949  Cd Length: 117  Bit Score: 145.81  E-value: 7.58e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521  123 EELGTEPAELFATFEEEPFASASIAQVHYATLKTGEEVVVKIQRPGIRRRVAADLQILQRFAQAVELAKLGRRLsaQDVV 202
Cdd:pfam03109   1 EELGAPVEEVFAEFDEEPIAAASIAQVHRAVLKDGEEVAVKVQRPGVKKRIRSDLKLLKFLAKILKKFFPGFDL--DWLV 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 118616521  203 ADFSDNLAVELDFRLEAQSMDAWVAHLHASPlgrNIRVPQVH 244
Cdd:pfam03109  79 DEFRKSLPQELDFLREAANAEKFRENFADLP---WVYVPKVY 117
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function ...
293-352 2.07e-03

Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction only];


Pssm-ID: 225714  Cd Length: 321  Bit Score: 38.57  E-value: 2.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 293 RHGLFHGDLHAGNLYVDEEGRIVFFDFGIMGRIDPRTrwllrELVYALLVKKDHAAAGKI 352
Cdd:COG3173  197 PPVLVHGDYRPGNLIIDPGRPTGVLDWELATLGDPLE-----DLAIICWTIFDEPAARAI 251
AarF COG0661
Predicted unusual protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family ...
6-450 3.31e-149

Predicted unusual protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 223733 [Multi-domain]  Cd Length: 517  Bit Score: 438.67  E-value: 3.31e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521   6 WHTAQMTTTKHREVAKLDRVPLPVEAARVAVTGWQVTRTAARFVTKLPGKGfasSWQQKIIKEIPQTFVDLGPTYVKFGQ 85
Cdd:COG0661    1 MLTLYAVSRLPRIIRVRLRYLLGRLLRLTGRLALLLRLLSWLGKSKLASSE---ELREKRAERLRLALEELGPTFIKLGQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521  86 IIASSPGAFGESLSREFRGLLDRVPPADTDQVHKLFVEELGTEPAELFATFEEEPFASASIAQVHYATLKTGEEVVVKIQ 165
Cdd:COG0661   78 ILSTRPDLVPPEYAEELAKLQDRVPPFPFEEAERIIEEELGRPIEELFSEFEPEPIASASIAQVHRAVLKSGEEVAVKVQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 166 RPGIRRRVAADLQILQRFAQAVELA-KLGRRLSAQDVVADFSDNLAVELDFRLEAQSMDAWVAHLHASPlgrNIRVPQVH 244
Cdd:COG0661  158 RPGIRERIEADLKLLRRLARLIKRLpPGGRRLDLVEVVDEFEKRLREELDYRREAANAERFRENFKDDP---DVYVPKVY 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 245 WNFTSERVLTMERVHGVRIDNVAAIRKAGFDGTELVKALLFSVFEGGLRHGLFHGDLHAGNLYVDEEGRIVFFDFGIMGR 324
Cdd:COG0661  235 WEYTTRRVLTMEWIDGIKISDIAALKSAGIDRKELAELLVRAFLRQLLRDGFFHADPHPGNILVRSDGRIVLLDFGIVGR 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 325 IDPRTRWLLRELVYALLvKKDHAAAGKIVVLMGAVGTMKPEAQAAKDLEKFATPLTMQSLGDMSYADIGRQLSALADAYD 404
Cdd:COG0661  315 LDPKFRRYLAELLLAFL-NRDYDRVAELHVELGYVPPDTDRDPLAAAIRAVLEPIYGKPLEEISFGEILDKLFEVARRFP 393
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 118616521 405 VKLPRELVLIGKQFLYVERYMKLLAPKWQMMS--DPQLTGYFANFMVE 450
Cdd:COG0661  394 MRLPPELVLLQRTLLLVEGVGRQLDPRFNLWAvaQPLLAKWLKKQLSP 441
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
72-422 9.45e-100

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 [Multi-domain]  Cd Length: 437  Bit Score: 308.84  E-value: 9.45e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521   72 TFVDLGPTYVKFGQIIASSPGAFGESLSREFRGLLDRVPPADTDQVHKLFVEELGTEPAELFATFEEEPFASASIAQVHY 151
Cdd:TIGR01982  56 ALEELGPTFIKFGQTLSTRADLLPADIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEEKPLAAASIAQVHR 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521  152 ATLKTGEEVVVKIQRPGIRRRVAADLQILQRFAQAVE-LAKLGRRLSAQDVVADFSDNLAVELDFRLEAQsmdawvahlH 230
Cdd:TIGR01982 136 ARLVDGKEVAVKVLRPGIEKTIAADIALLYRLARIVErLSPDSRRLRPTEVVKEFEKTLRRELDLRREAA---------N 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521  231 ASPLGRN------IRVPQVHWNFTSERVLTMERVHGVRIDNVAAIRKAGFDGTELVKALLFSVFEGGLRHGLFHGDLHAG 304
Cdd:TIGR01982 207 ASELGENfkndpgVYVPEVYWDRTSERVLTMEWIDGIPLSDIAALDEAGLDRKALAENLARSFLNQVLRDGFFHADLHPG 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521  305 NLYVDEEGRIVFFDFGIMGRIDPRTRWLLRELVYAlLVKKDHAAAGKIVVLMGAVGTMKPEAQAAKDLEKFATPLTMQSL 384
Cdd:TIGR01982 287 NIFVLKDGKIIALDFGIVGRLSEEDRRYLAEILYG-FLNRDYRRVAEVHFDAGYVPSDTDMAEFEQAIRAIGEPIFGQPL 365
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 118616521  385 GDMSYADIGRQLSALADAYDVKLPRELVLIGKQFLYVE 422
Cdd:TIGR01982 366 KEISVGRLLAGLFKITRDFNMELQPQLLLLQKTLLTVE 403
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
292-327 5.25e-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: 250760 [Multi-domain]  Cd Length: 237  Bit Score: 37.15  E-value: 5.25e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 118616521  292 LRHGLFHGDLHAGNLYVDEEGRIV-FFDFGIMGRIDP 327
Cdd:pfam01636 163 LPLVLVHGDLHPGNLLVDPGGRVSgVIDFEDAGLGDP 199
 
Name Accession Description Interval E-value
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
105-353 2.44e-97

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: 295.94  E-value: 2.44e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 105 LLDRVPPADTDQVHKLFVEELGTEPAELFATFEEEPFASASIAQVHYATLKTGEEVVVKIQRPGIRRRVAADLQILQRFA 184
Cdd:cd05121    2 LQDDVPPFPFEEVRKIIEEELGRPLEEVFAEFDPEPLAAASIAQVHRARLKDGREVAVKVQRPGIEEIIEADLRILRRLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 185 QAVE-LAKLGRRLSAQDVVADFSDNLAVELDFRLEAQSMDAWVAHLHASPlgrNIRVPQVHWNFTSERVLTMERVHGVRI 263
Cdd:cd05121   82 RLLErLSPLLRRLDLVAIVDEFARSLLEELDFRREARNAERFRKNLKDSP---DVYVPKVYPELSTRRVLVMEYIDGVKL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 264 DNVAAIRKAGFDGTELVKALLFSVFEGGLRHGLFHGDLHAGNLYVDEEGRIVFFDFGIMGRIDPRTRWLLRELVYAlLVK 343
Cdd:cd05121  159 TDLEALRAAGIDRKELARRLVDAYLKQIFEDGFFHADPHPGNILVLPDGRIALLDFGMVGRLDPETREALADLLLA-LVN 237
                        250
                 ....*....|
gi 118616521 344 KDHAAAGKIV 353
Cdd:cd05121  238 GDAEGLAEAL 247
UbiB cd13972
Ubiquinone biosynthetic protein UbiB; UbiB is the prokaryotic homolog of yeast Abc1p and human ...
105-341 6.17e-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  Cd Length: 247  Bit Score: 245.57  E-value: 6.17e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 105 LLDRVPPADTDQVHKLFVEELGTEPAELFATFEEEPFASASIAQVHYATLKTGEEVVVKIQRPGIRRRVAADLQILQRFA 184
Cdd:cd13972    2 LQDRVPPFSGKEARAIIEAELGKPLDALFSDFDEEPVAAASIAQVHKARLLDGREVAVKVLRPGIEKRIERDLELLRFLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 185 QAVE-LAKLGRRLSAQDVVADFSDNLAVELDFRLEAQSMDAWVAHLHASPlgrNIRVPQVHWNFTSERVLTMERVHGVRI 263
Cdd:cd13972   82 RLAErLLPEARRLRPVEVVKEFARSLLLELDLRLEAANASELRENFLDDP---GFYVPEVYWELTSKNVLTMEWIDGIPI 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118616521 264 DNVAAIRKAGFDGTELVKALLFSVFEGGLRHGLFHGDLHAGNLYVDEEGRIVFFDFGIMGRIDPRTRWLLRELVYALL 341
Cdd:cd13972  159 SDIEALDAAGIDRKALAERLVEIFFRQVFRDGFFHADMHPGNIFVDPNGRIIAVDFGIMGRLDKKDRRYLAEILYGFL 236
ADCK1-like cd13969
aarF domain containing kinase 1 and similar proteins; This subfamily is composed of ...
105-357 3.32e-65

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  Cd Length: 253  Bit Score: 212.73  E-value: 3.32e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 105 LLDRVPPADTDQVHKLFVEELGTEPAELFATFEEEPFASASIAQVHYATLKTGEEVVVKIQRPGIRRRVAADLQILQRFA 184
Cdd:cd13969    2 LQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVHKAKLKDGEEVAVKVQHPDLRKQFAGDLATMEFLV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 185 QAVElaKLGRRLSAQDVVADFSDNLAVELDFRLEAQSMDAWVAHLHASPlgrNIRVPQVHWNFTSERVLTMERVHGVRID 264
Cdd:cd13969   82 NLVE--KLFPDFPFSWLVDELKKNLPKELDFLNEARNAERCAKLFKHRP---DVYVPKVYWDLSSKRVLTMEFIDGIKID 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 265 NVAAIRKAGFDGTELVKAL--LFS--VFegglRHGLFHGDLHAGNLYV-----DEEGRIVFFDFGIMGRIDPRTRWLLRE 335
Cdd:cd13969  157 DVEALKKLGIDPKEVARLLseAFAemIF----VHGFVHCDPHPGNLLVrknpgPGKPQIVLLDHGLYRELDEEFRLNYCR 232
                        250       260
                 ....*....|....*....|..
gi 118616521 336 LVYAlLVKKDHAAAGKIVVLMG 357
Cdd:cd13969  233 LWKA-LILGDEKKIKKYSKALG 253
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
75-323 5.95e-63

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310  Cd Length: 537  Bit Score: 214.77  E-value: 5.95e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521  75 DLGPTYVKFGQIIASSPGAFGESLSREFRGLLDRVPPADTDQVHKLFVEELGTEPAELFATFEEEPFASASIAQVHYATL 154
Cdd:PRK04750  61 ELGPIFVKFGQMLSTRRDLFPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQVHFARL 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 155 K-TGEEVVVKIQRPGIRRRVAADLQILQRFAQAVE-LAKLGRRLSAQDVVADFSDNLAVELDFRLEAQSmdawvahlhAS 232
Cdd:PRK04750 141 KdNGREVVVKVLRPDILPVIDADLALMYRLARWVErLLPDGRRLKPREVVAEFEKTLHDELDLMREAAN---------AS 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 233 PLGRN------IRVPQVHWNFTSERVLTMERVHGVRIDNVAAIRKAGFDGTEL----VKALLFSVFegglRHGLFHGDLH 302
Cdd:PRK04750 212 QLRRNfedsdmLYVPEVYWDYCSETVMVMERMYGIPVSDVAALRAAGTDMKLLaergVEVFFTQVF----RDGFFHADMH 287
                        250       260
                 ....*....|....*....|....*
gi 118616521 303 AGNLYVD----EEGRIVFFDFGIMG 323
Cdd:PRK04750 288 PGNIFVSydppENPRYIALDFGIVG 312
ABC1_ADCK3 cd13970
Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This ...
105-341 7.12e-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  Cd Length: 251  Bit Score: 185.41  E-value: 7.12e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 105 LLDRVPPADTDQVHKLFVEELGTEPAELFATFEEEPFASASIAQVHYATLKTGEEVVVKIQRPGIRRRVAADLQILQRFA 184
Cdd:cd13970    6 LRDSAPPMPWAQLEKVLEAELGEDWRELFAEFDEEPFAAASIGQVHRATLKDGREVAVKVQYPGVAESIDSDLNNLRRLL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 185 QAVELAKLGRRLsaQDVVADFSDNLAVELDFRLEAQSMdAWVAHLHAspLGRNIRVPQVHWNFTSERVLTMERVHGVRID 264
Cdd:cd13970   86 KLTGLLPKGLDL--DALIAELREELLEECDYEREAANQ-RRFRELLA--DDPRFVVPEVIPELSTKRVLTTEFVDGVPLD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 265 NVA----AIRKAGfdGTELVKALLFSVFEgglrHGLFHGDLHAGN-LYVDEEGRIVFFDFGIMGRIDPRTRWLLRELVYA 339
Cdd:cd13970  161 EAAdlsqEERNRI--GELLLRLCLRELFE----FGFMQTDPNPGNfLYDPEDGRLGLLDFGAVREYPPEFVDGYRRLVRA 234

                 ..
gi 118616521 340 LL 341
Cdd:cd13970  235 AL 236
ABC1 pfam03109
ABC1 family; This family includes ABC1 from yeast and AarF from Escherichia coli. These ...
123-244 7.58e-42

ABC1 family; This family includes ABC1 from yeast and AarF from Escherichia 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 Escherichia 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: 111949  Cd Length: 117  Bit Score: 145.81  E-value: 7.58e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521  123 EELGTEPAELFATFEEEPFASASIAQVHYATLKTGEEVVVKIQRPGIRRRVAADLQILQRFAQAVELAKLGRRLsaQDVV 202
Cdd:pfam03109   1 EELGAPVEEVFAEFDEEPIAAASIAQVHRAVLKDGEEVAVKVQRPGVKKRIRSDLKLLKFLAKILKKFFPGFDL--DWLV 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 118616521  203 ADFSDNLAVELDFRLEAQSMDAWVAHLHASPlgrNIRVPQVH 244
Cdd:pfam03109  79 DEFRKSLPQELDFLREAANAEKFRENFADLP---WVYVPKVY 117
ADCK2-like cd13971
aarF domain containing kinase 2 and similar proteins; This subfamily is composed of ...
105-377 3.79e-32

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: 123.87  E-value: 3.79e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 105 LLDRVPPADTDQVHKLFVEELGTEPAELFATFEEEPFASASIAQVHYATLKT--------GEEVVVKIQRPGIRRRVAAD 176
Cdd:cd13971    2 LHSNAPPHSWAHTERALEAAFGKDWEDIFEEFDEEPIGSGSIAQVHRAKLKPdyggdgggPRVVAVKVLHPGVREQIERD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 177 LQILQRFAQAVELAKLGRRLSAQDVVADFSDNLAVELDFRLEAQSMDAWVAHLHASPlgrNIRVPQVHWNFTSERVLTME 256
Cdd:cd13971   82 LAILRLFAKLLEAIPPLRWLSLPESVEQFASLMLRQLDLRVEAANLERFRENFKDRK---DVSFPKPLYPLVTEEVLVET 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 257 RVHGVRIDNVAAIRKAGFDGTELVKALLFSVFEGGLRHGLFHGDLHAGNLYVDEEG-----------------RIVFFDF 319
Cdd:cd13971  159 FEEGVPISRTVLAHGGEPLKRKLARIGLDAFLKMLFVDNFVHGDLHPGNILVRFNDsnrpsllvsldargsppRLVFLDA 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 118616521 320 GIMGRIDPRTRWLLRELVYALLVKKDHAAAGKIVvlmgavgTMKPEAQAAKDLEKFAT 377
Cdd:cd13971  239 GLVTELSPQDRRNFIDLFKAVARGDGYKAAELML-------ERSRSSQTCPDPEGFKS 289
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
237-327 1.19e-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  Cd Length: 158  Bit Score: 41.13  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 237 NIRVPQVH--WNFTSERVLTMERVHGVRIDNVAairkaGFDGTELVKALLFSVFEGgLRH-------GLFHGDLHAGNLY 307
Cdd:cd05120   51 SLPVPKVYgfGESDGWEYLLMERIEGETLSEVW-----PRLSEEEKEKIADQLAEI-LAAlhridssVLTHGDLHPGNIL 124
                         90       100
                 ....*....|....*....|.
gi 118616521 308 VDEEGRIV-FFDFGIMGRIDP 327
Cdd:cd05120  125 VKPDGKLSgIIDWEFAGYGPP 145
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
216-320 5.61e-04

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 39.89  E-value: 5.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 216 RLEAQSMdawvahLHASPLGrnIRVPQVHWNFTSERVLTMERVHGVRIDNVaaIRKAGFDGTELVKALLFSVfegGLRH- 294
Cdd:PRK14879  47 RREARIM------SRARKAG--VNVPAVYFVDPENFIIVMEYIEGEPLKDL--INSNGMEELELSREIGRLV---GKLHs 113
                         90       100
                 ....*....|....*....|....*..
gi 118616521 295 -GLFHGDLHAGNLYVdEEGRIVFFDFG 320
Cdd:PRK14879 114 aGIIHGDLTTSNMIL-SGGKIYLIDFG 139
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
255-334 7.41e-04

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  Cd Length: 183  Bit Score: 39.02  E-value: 7.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 255 MERVHGV---RIDNVAAIRKAGFDGTELVKALLfsvfegglRHGLFHGDLHAGNLYVDEEGRIVFFDFGIMGRID-PRTR 330
Cdd:cd05144   95 MELIDGYplyQVRLLEDPEEVLDEILELIVKLA--------KHGLIHGDFSEFNILVDEDEKITVIDFPQMVSTShPNAE 166

                 ....
gi 118616521 331 WLLR 334
Cdd:cd05144  167 EYFD 170
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
297-327 1.67e-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  Cd Length: 234  Bit Score: 38.76  E-value: 1.67e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 118616521 297 FHGDLHAGNLYVDeEGRIV-FFDFGIMGRIDP 327
Cdd:cd05155  166 LHGDLHPGNLLVR-DGRLSaVIDFGDLGVGDP 196
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function ...
293-352 2.07e-03

Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction only];


Pssm-ID: 225714  Cd Length: 321  Bit Score: 38.57  E-value: 2.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 293 RHGLFHGDLHAGNLYVDEEGRIVFFDFGIMGRIDPRTrwllrELVYALLVKKDHAAAGKI 352
Cdd:COG3173  197 PPVLVHGDYRPGNLIIDPGRPTGVLDWELATLGDPLE-----DLAIICWTIFDEPAARAI 251
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
292-340 5.94e-03

Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal transduction mechanisms];


Pssm-ID: 225213  Cd Length: 331  Bit Score: 37.32  E-value: 5.94e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 118616521 292 LRHGLFHGDLHAGNLYVDEEGRIV-FFDFGimgriDPRTRWLLRELVYAL 340
Cdd:COG2334  195 LGDQIIHGDLHPDNVLFDDDTDVSgFIDFD-----DAGYGWFIYDLAIAL 239
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
238-326 7.01e-03

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 226168  Cd Length: 204  Bit Score: 36.49  E-value: 7.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 238 IRVPQVHWNFTSERVLTMERVHGVRIDNvaAIRKAGFDGTELVKALLfsvfeGGL-RHGLFHGDLHAGNLYVdEEGRIVF 316
Cdd:COG3642   61 VPVPIVYDVDPDNGLIVMEYIEGELLKD--ALEEARPDLLREVGRLV-----GKLhKAGIVHGDLTTSNIIL-SGGRIYF 132
                         90
                 ....*....|
gi 118616521 317 FDFGiMGRID 326
Cdd:COG3642  133 IDFG-LGEFS 141
AarF COG0661
Predicted unusual protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family ...
6-450 3.31e-149

Predicted unusual protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 223733 [Multi-domain]  Cd Length: 517  Bit Score: 438.67  E-value: 3.31e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521   6 WHTAQMTTTKHREVAKLDRVPLPVEAARVAVTGWQVTRTAARFVTKLPGKGfasSWQQKIIKEIPQTFVDLGPTYVKFGQ 85
Cdd:COG0661    1 MLTLYAVSRLPRIIRVRLRYLLGRLLRLTGRLALLLRLLSWLGKSKLASSE---ELREKRAERLRLALEELGPTFIKLGQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521  86 IIASSPGAFGESLSREFRGLLDRVPPADTDQVHKLFVEELGTEPAELFATFEEEPFASASIAQVHYATLKTGEEVVVKIQ 165
Cdd:COG0661   78 ILSTRPDLVPPEYAEELAKLQDRVPPFPFEEAERIIEEELGRPIEELFSEFEPEPIASASIAQVHRAVLKSGEEVAVKVQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 166 RPGIRRRVAADLQILQRFAQAVELA-KLGRRLSAQDVVADFSDNLAVELDFRLEAQSMDAWVAHLHASPlgrNIRVPQVH 244
Cdd:COG0661  158 RPGIRERIEADLKLLRRLARLIKRLpPGGRRLDLVEVVDEFEKRLREELDYRREAANAERFRENFKDDP---DVYVPKVY 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 245 WNFTSERVLTMERVHGVRIDNVAAIRKAGFDGTELVKALLFSVFEGGLRHGLFHGDLHAGNLYVDEEGRIVFFDFGIMGR 324
Cdd:COG0661  235 WEYTTRRVLTMEWIDGIKISDIAALKSAGIDRKELAELLVRAFLRQLLRDGFFHADPHPGNILVRSDGRIVLLDFGIVGR 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521 325 IDPRTRWLLRELVYALLvKKDHAAAGKIVVLMGAVGTMKPEAQAAKDLEKFATPLTMQSLGDMSYADIGRQLSALADAYD 404
Cdd:COG0661  315 LDPKFRRYLAELLLAFL-NRDYDRVAELHVELGYVPPDTDRDPLAAAIRAVLEPIYGKPLEEISFGEILDKLFEVARRFP 393
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 118616521 405 VKLPRELVLIGKQFLYVERYMKLLAPKWQMMS--DPQLTGYFANFMVE 450
Cdd:COG0661  394 MRLPPELVLLQRTLLLVEGVGRQLDPRFNLWAvaQPLLAKWLKKQLSP 441
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
72-422 9.45e-100

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 [Multi-domain]  Cd Length: 437  Bit Score: 308.84  E-value: 9.45e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521   72 TFVDLGPTYVKFGQIIASSPGAFGESLSREFRGLLDRVPPADTDQVHKLFVEELGTEPAELFATFEEEPFASASIAQVHY 151
Cdd:TIGR01982  56 ALEELGPTFIKFGQTLSTRADLLPADIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEEKPLAAASIAQVHR 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521  152 ATLKTGEEVVVKIQRPGIRRRVAADLQILQRFAQAVE-LAKLGRRLSAQDVVADFSDNLAVELDFRLEAQsmdawvahlH 230
Cdd:TIGR01982 136 ARLVDGKEVAVKVLRPGIEKTIAADIALLYRLARIVErLSPDSRRLRPTEVVKEFEKTLRRELDLRREAA---------N 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521  231 ASPLGRN------IRVPQVHWNFTSERVLTMERVHGVRIDNVAAIRKAGFDGTELVKALLFSVFEGGLRHGLFHGDLHAG 304
Cdd:TIGR01982 207 ASELGENfkndpgVYVPEVYWDRTSERVLTMEWIDGIPLSDIAALDEAGLDRKALAENLARSFLNQVLRDGFFHADLHPG 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118616521  305 NLYVDEEGRIVFFDFGIMGRIDPRTRWLLRELVYAlLVKKDHAAAGKIVVLMGAVGTMKPEAQAAKDLEKFATPLTMQSL 384
Cdd:TIGR01982 287 NIFVLKDGKIIALDFGIVGRLSEEDRRYLAEILYG-FLNRDYRRVAEVHFDAGYVPSDTDMAEFEQAIRAIGEPIFGQPL 365
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 118616521  385 GDMSYADIGRQLSALADAYDVKLPRELVLIGKQFLYVE 422
Cdd:TIGR01982 366 KEISVGRLLAGLFKITRDFNMELQPQLLLLQKTLLTVE 403
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
292-327 5.25e-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: 250760 [Multi-domain]  Cd Length: 237  Bit Score: 37.15  E-value: 5.25e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 118616521  292 LRHGLFHGDLHAGNLYVDEEGRIV-FFDFGIMGRIDP 327
Cdd:pfam01636 163 LPLVLVHGDLHPGNLLVDPGGRVSgVIDFEDAGLGDP 199
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.14
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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