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Conserved domains on  [gi|83572016|gb|ABC18568|]
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2-octaprenylphenol hydroxylase [Moorella thermoacetica ATCC 39073]

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List of domain hits

Name Accession Description Interval E-value
AarF COG0661
Predicted unusual protein kinase [General function prediction only]
19-513 1.05e-155

Predicted unusual protein kinase [General function prediction only]


:

Pssm-ID: 223733  Cd Length: 517  Bit Score: 458.31  E-value: 1.05e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016  19 VLARYGFGYLLDQVGLGELILRR----------SREEAPLSLGQRLRLALEELGPTFIKLGQLLSTRPDLLPADIISELT 88
Cdd:COG0661  16 VRLRYLLGRLLRLTGRLALLLRLlswlgksklaSSEELREKRAERLRLALEELGPTFIKLGQILSTRPDLVPPEYAEELA 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016  89 RLQDRVPPFPFADVRKAVEEELGQPLEELFASFDPEPLAVASIGQVHLATLPDGSQVIVKVQRPGIARQVRVDLEILFDL 168
Cdd:COG0661  96 KLQDRVPPFPFEEAERIIEEELGRPIEELFSEFEPEPIASASIAQVHRAVLKSGEEVAVKVQRPGIRERIEADLKLLRRL 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016 169 ARLAQRHTPYGKIYDFNQMAAEFARALTEELDYTREGRNADRFRENFAGDASVYFPAVYWDYTTRGVLTQEYVEAVKLNN 248
Cdd:COG0661 176 ARLIKRLPPGGRRLDLVEVVDEFEKRLREELDYRREAANAERFRENFKDDPDVYVPKVYWEYTTRRVLTMEWIDGIKISD 255
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016 249 LEEIDRRGYSRRRIAVNLARAVYQQVLVDGFFHGDPHPGNLAVLPGEVIVFMDFGLTGTLTEELKEQFVNLVLGIIRRRS 328
Cdd:COG0661 256 IAALKSAGIDRKELAELLVRAFLRQLLRDGFFHADPHPGNILVRSDGRIVLLDFGIVGRLDPKFRRYLAELLLAFLNRDY 335
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016 329 QDVLRTIIAMGMVPAEVDRGALRREIEALRDKYYHLSFRQISLGQAIEELLQLAFRYHLRMPPELTLLGKTLLTLEGLVR 408
Cdd:COG0661 336 DRVAELHVELGYVPPDTDRDPLAAAIRAVLEPIYGKPLEEISFGEILDKLFEVARRFPMRLPPELVLLQRTLLLVEGVGR 415
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016 409 KLDPELELAELAEPYGRELLRRRFSVRFLwRALTENLASGWEVMQSLPRQFQHLLDLAERGELTLRVEplhlrGLVRQID 488
Cdd:COG0661 416 QLDPRFNLWAVAQPLLAKWLKKQLSPKLL-RELKDEAVAVLNALPLLPRLLRDLLDNDREELSLRSSE-----ELALLLL 489
                       490       500
                ....*....|....*....|....*.
gi 83572016 489 RIINKLTM-SVVLLAFSIIMASLIIS 513
Cdd:COG0661 490 KAVARLSIgSILLVVLAVTVLLIAIL 515
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
12-438 1.69e-151

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: 233667 [Multi-domain]  Cd Length: 437  Bit Score: 444.82  E-value: 1.69e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016    12 RYRQVVNVLARYGFGYLLD-QVGLGELILRR-------SREEAPLSLGQRLRLALEELGPTFIKLGQLLSTRPDLLPADI 83
Cdd:TIGR01982   3 RLRRIIRVLIRYGFLALVEsPIGPLSLRLLRrlllpfsNRENRLMSRGERLRLALEELGPTFIKFGQTLSTRADLLPADI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016    84 ISELTRLQDRVPPFPFADVRKAVEEELGQPLEELFASFDPEPLAVASIGQVHLATLPDGSQVIVKVQRPGIARQVRVDLE 163
Cdd:TIGR01982  83 AEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEEKPLAAASIAQVHRARLVDGKEVAVKVLRPGIEKTIAADIA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016   164 ILFDLARLAQRHTPYGKIYDFNQMAAEFARALTEELDYTREGRNADRFRENFAGDASVYFPAVYWDYTTRGVLTQEYVEA 243
Cdd:TIGR01982 163 LLYRLARIVERLSPDSRRLRPTEVVKEFEKTLRRELDLRREAANASELGENFKNDPGVYVPEVYWDRTSERVLTMEWIDG 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016   244 VKLNNLEEIDRRGYSRRRIAVNLARAVYQQVLVDGFFHGDPHPGNLAVLPGEVIVFMDFGLTGTLTEELKEQFVNLVLGI 323
Cdd:TIGR01982 243 IPLSDIAALDEAGLDRKALAENLARSFLNQVLRDGFFHADLHPGNIFVLKDGKIIALDFGIVGRLSEEDRRYLAEILYGF 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016   324 IRRRSQDVLRTIIAMGMVPAEVDRGALRREIEALRDKYYHLSFRQISLGQAIEELLQLAFRYHLRMPPELTLLGKTLLTL 403
Cdd:TIGR01982 323 LNRDYRRVAEVHFDAGYVPSDTDMAEFEQAIRAIGEPIFGQPLKEISVGRLLAGLFKITRDFNMELQPQLLLLQKTLLTV 402
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 83572016   404 EGLVRKLDPELELAELAEPYGRELLRRRFSVRFLW 438
Cdd:TIGR01982 403 EGVGRQLDPDLNMWKVAEPFVKRWIRKRLGPKAKI 437
 
Name Accession Description Interval E-value
AarF COG0661
Predicted unusual protein kinase [General function prediction only]
19-513 1.05e-155

Predicted unusual protein kinase [General function prediction only]


Pssm-ID: 223733  Cd Length: 517  Bit Score: 458.31  E-value: 1.05e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016  19 VLARYGFGYLLDQVGLGELILRR----------SREEAPLSLGQRLRLALEELGPTFIKLGQLLSTRPDLLPADIISELT 88
Cdd:COG0661  16 VRLRYLLGRLLRLTGRLALLLRLlswlgksklaSSEELREKRAERLRLALEELGPTFIKLGQILSTRPDLVPPEYAEELA 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016  89 RLQDRVPPFPFADVRKAVEEELGQPLEELFASFDPEPLAVASIGQVHLATLPDGSQVIVKVQRPGIARQVRVDLEILFDL 168
Cdd:COG0661  96 KLQDRVPPFPFEEAERIIEEELGRPIEELFSEFEPEPIASASIAQVHRAVLKSGEEVAVKVQRPGIRERIEADLKLLRRL 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016 169 ARLAQRHTPYGKIYDFNQMAAEFARALTEELDYTREGRNADRFRENFAGDASVYFPAVYWDYTTRGVLTQEYVEAVKLNN 248
Cdd:COG0661 176 ARLIKRLPPGGRRLDLVEVVDEFEKRLREELDYRREAANAERFRENFKDDPDVYVPKVYWEYTTRRVLTMEWIDGIKISD 255
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016 249 LEEIDRRGYSRRRIAVNLARAVYQQVLVDGFFHGDPHPGNLAVLPGEVIVFMDFGLTGTLTEELKEQFVNLVLGIIRRRS 328
Cdd:COG0661 256 IAALKSAGIDRKELAELLVRAFLRQLLRDGFFHADPHPGNILVRSDGRIVLLDFGIVGRLDPKFRRYLAELLLAFLNRDY 335
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016 329 QDVLRTIIAMGMVPAEVDRGALRREIEALRDKYYHLSFRQISLGQAIEELLQLAFRYHLRMPPELTLLGKTLLTLEGLVR 408
Cdd:COG0661 336 DRVAELHVELGYVPPDTDRDPLAAAIRAVLEPIYGKPLEEISFGEILDKLFEVARRFPMRLPPELVLLQRTLLLVEGVGR 415
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016 409 KLDPELELAELAEPYGRELLRRRFSVRFLwRALTENLASGWEVMQSLPRQFQHLLDLAERGELTLRVEplhlrGLVRQID 488
Cdd:COG0661 416 QLDPRFNLWAVAQPLLAKWLKKQLSPKLL-RELKDEAVAVLNALPLLPRLLRDLLDNDREELSLRSSE-----ELALLLL 489
                       490       500
                ....*....|....*....|....*.
gi 83572016 489 RIINKLTM-SVVLLAFSIIMASLIIS 513
Cdd:COG0661 490 KAVARLSIgSILLVVLAVTVLLIAIL 515
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
1-518 6.08e-100

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310  Cd Length: 537  Bit Score: 315.31  E-value: 6.08e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016    1 MSLRRRYihlnryrQVVNVLARYGfgylLDQVGLGELILRRSREEAPL-----------SLGQRLRLALEELGPTFIKLG 69
Cdd:PRK04750   2 MELFRLY-------KIIRVFLRYG----LDELILSHRLTRPLRLWRRSlfwmpnrhkdkPRGERLRLALEELGPIFVKFG 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016   70 QLLSTRPDLLPADIISELTRLQDRVPPFPFADVRKAVEEELGQPLEELFASFDPEPLAVASIGQVHLATLPD-GSQVIVK 148
Cdd:PRK04750  71 QMLSTRRDLFPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQVHFARLKDnGREVVVK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016  149 VQRPGIARQVRVDLEILFDLARLAQRHTPYGKIYDFNQMAAEFARALTEELDYTREGRNADRFRENFAGDASVYFPAVYW 228
Cdd:PRK04750 151 VLRPDILPVIDADLALMYRLARWVERLLPDGRRLKPREVVAEFEKTLHDELDLMREAANASQLRRNFEDSDMLYVPEVYW 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016  229 DYTTRGVLTQEYVEAVKLNNLEEIDRRGYSRRRIAVNLARAVYQQVLVDGFFHGDPHPGNLAVLP-----GEVIVfMDFG 303
Cdd:PRK04750 231 DYCSETVMVMERMYGIPVSDVAALRAAGTDMKLLAERGVEVFFTQVFRDGFFHADMHPGNIFVSYdppenPRYIA-LDFG 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016  304 LTGTLTEELKEQFVNLVLGIIRRRSQDVLRTIIAMGMVPAEVDRGALRREIEALRDKYYHLSFRQISLGQAIEELLQLAF 383
Cdd:PRK04750 310 IVGSLNKEDKRYLAENFLAFFNRDYRRVAELHVESGWVPPDTRVEELEFAIRAVCEPIFDKPLAEISFGHVLLRLFNTAR 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016  384 RYHLRMPPELTLLGKTLLTLEGLVRKLDPELELAELAEPYGRELLRRRFSVRFLWRALTENLASGWEVMQSLPRQFQHLL 463
Cdd:PRK04750 390 RFNVEIQPQLVLLQKTLLNVEGLGRQLDPQLDLWKTAKPFLERWMKEQVGPRALVRALKEEAPFWAEKLPELPRLVHDSL 469
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 83572016  464 DLAERGELT--LRVEPLHLRGLVRQIDR-IINKLTMSVVLLAFSIIMASLIISTALGA 518
Cdd:PRK04750 470 RQGKLLQHSvdLLAEQLRTNRLRQGQSRyLLGVGATLLLAGTLLLLSRPELMPGAAGL 527
ABC1 pfam03109
ABC1 family; This family includes ABC1 from yeast and AarF from Escherichia coli. These ...
108-227 3.09e-46

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: 158.91  E-value: 3.09e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016   108 EELGQPLEELFASFDPEPLAVASIGQVHLATLPDGSQVIVKVQRPGIARQVRVDLEILFDLARLAQRhtpYGKIYDFNQM 187
Cdd:pfam03109   1 EELGAPVEEVFAEFDEEPIAAASIAQVHRAVLKDGEEVAVKVQRPGVKKRIRSDLKLLKFLAKILKK---FFPGFDLDWL 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 83572016   188 AAEFARALTEELDYTREGRNADRFRENFAGDASVYFPAVY 227
Cdd:pfam03109  78 VDEFRKSLPQELDFLREAANAEKFRENFADLPWVYVPKVY 117
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase (APH) and Choline Kinase (ChoK) family. The APH/ChoK ...
224-303 1.27e-05

Aminoglycoside 3'-phosphotransferase (APH) and Choline Kinase (ChoK) family. 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). The 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.


Pssm-ID: 240159  Cd Length: 155  Bit Score: 44.32  E-value: 1.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016 224 PAVYWDYTTRG--VLTQEYVEAVKLNNLEEIDRRgYSRRRIAVNLARavYQQVLVDGFFHGDPHPGNLAVLPGEVIVFMD 301
Cdd:cd05120  56 PKVLASGESDGwsYLLMEWIEGETLDEVSEEEKE-DIAEQLAELLAK--LHQLPLLVLCHGDLHPGNILVDDGKILGIID 132

                ..
gi 83572016 302 FG 303
Cdd:cd05120 133 WE 134
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
216-304 5.08e-04

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


Pssm-ID: 234331  Cd Length: 199  Bit Score: 40.28  E-value: 5.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016   216 AGDASVYFPAVYWDYTTRGVLTQEYVEAVKLNnlEEIDRRGYSR-RRIAVNLAR---AvyqqvlvdGFFHGDPHPGNLaV 291
Cdd:TIGR03724  54 ARKAGVNTPVVYDVDPDNKTIVMEYIEGKPLK--DVIEEGNDELlREIGRLVGKlhkA--------GIVHGDLTTSNI-I 122
                          90
                  ....*....|...
gi 83572016   292 LPGEVIVFMDFGL 304
Cdd:TIGR03724 123 VRDDKLYLIDFGL 135
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
12-438 1.69e-151

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: 233667 [Multi-domain]  Cd Length: 437  Bit Score: 444.82  E-value: 1.69e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016    12 RYRQVVNVLARYGFGYLLD-QVGLGELILRR-------SREEAPLSLGQRLRLALEELGPTFIKLGQLLSTRPDLLPADI 83
Cdd:TIGR01982   3 RLRRIIRVLIRYGFLALVEsPIGPLSLRLLRrlllpfsNRENRLMSRGERLRLALEELGPTFIKFGQTLSTRADLLPADI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016    84 ISELTRLQDRVPPFPFADVRKAVEEELGQPLEELFASFDPEPLAVASIGQVHLATLPDGSQVIVKVQRPGIARQVRVDLE 163
Cdd:TIGR01982  83 AEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEEKPLAAASIAQVHRARLVDGKEVAVKVLRPGIEKTIAADIA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016   164 ILFDLARLAQRHTPYGKIYDFNQMAAEFARALTEELDYTREGRNADRFRENFAGDASVYFPAVYWDYTTRGVLTQEYVEA 243
Cdd:TIGR01982 163 LLYRLARIVERLSPDSRRLRPTEVVKEFEKTLRRELDLRREAANASELGENFKNDPGVYVPEVYWDRTSERVLTMEWIDG 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016   244 VKLNNLEEIDRRGYSRRRIAVNLARAVYQQVLVDGFFHGDPHPGNLAVLPGEVIVFMDFGLTGTLTEELKEQFVNLVLGI 323
Cdd:TIGR01982 243 IPLSDIAALDEAGLDRKALAENLARSFLNQVLRDGFFHADLHPGNIFVLKDGKIIALDFGIVGRLSEEDRRYLAEILYGF 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016   324 IRRRSQDVLRTIIAMGMVPAEVDRGALRREIEALRDKYYHLSFRQISLGQAIEELLQLAFRYHLRMPPELTLLGKTLLTL 403
Cdd:TIGR01982 323 LNRDYRRVAEVHFDAGYVPSDTDMAEFEQAIRAIGEPIFGQPLKEISVGRLLAGLFKITRDFNMELQPQLLLLQKTLLTV 402
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 83572016   404 EGLVRKLDPELELAELAEPYGRELLRRRFSVRFLW 438
Cdd:TIGR01982 403 EGVGRQLDPDLNMWKVAEPFVKRWIRKRLGPKAKI 437
 
Name Accession Description Interval E-value
AarF COG0661
Predicted unusual protein kinase [General function prediction only]
19-513 1.05e-155

Predicted unusual protein kinase [General function prediction only]


Pssm-ID: 223733  Cd Length: 517  Bit Score: 458.31  E-value: 1.05e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016  19 VLARYGFGYLLDQVGLGELILRR----------SREEAPLSLGQRLRLALEELGPTFIKLGQLLSTRPDLLPADIISELT 88
Cdd:COG0661  16 VRLRYLLGRLLRLTGRLALLLRLlswlgksklaSSEELREKRAERLRLALEELGPTFIKLGQILSTRPDLVPPEYAEELA 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016  89 RLQDRVPPFPFADVRKAVEEELGQPLEELFASFDPEPLAVASIGQVHLATLPDGSQVIVKVQRPGIARQVRVDLEILFDL 168
Cdd:COG0661  96 KLQDRVPPFPFEEAERIIEEELGRPIEELFSEFEPEPIASASIAQVHRAVLKSGEEVAVKVQRPGIRERIEADLKLLRRL 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016 169 ARLAQRHTPYGKIYDFNQMAAEFARALTEELDYTREGRNADRFRENFAGDASVYFPAVYWDYTTRGVLTQEYVEAVKLNN 248
Cdd:COG0661 176 ARLIKRLPPGGRRLDLVEVVDEFEKRLREELDYRREAANAERFRENFKDDPDVYVPKVYWEYTTRRVLTMEWIDGIKISD 255
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016 249 LEEIDRRGYSRRRIAVNLARAVYQQVLVDGFFHGDPHPGNLAVLPGEVIVFMDFGLTGTLTEELKEQFVNLVLGIIRRRS 328
Cdd:COG0661 256 IAALKSAGIDRKELAELLVRAFLRQLLRDGFFHADPHPGNILVRSDGRIVLLDFGIVGRLDPKFRRYLAELLLAFLNRDY 335
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016 329 QDVLRTIIAMGMVPAEVDRGALRREIEALRDKYYHLSFRQISLGQAIEELLQLAFRYHLRMPPELTLLGKTLLTLEGLVR 408
Cdd:COG0661 336 DRVAELHVELGYVPPDTDRDPLAAAIRAVLEPIYGKPLEEISFGEILDKLFEVARRFPMRLPPELVLLQRTLLLVEGVGR 415
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016 409 KLDPELELAELAEPYGRELLRRRFSVRFLwRALTENLASGWEVMQSLPRQFQHLLDLAERGELTLRVEplhlrGLVRQID 488
Cdd:COG0661 416 QLDPRFNLWAVAQPLLAKWLKKQLSPKLL-RELKDEAVAVLNALPLLPRLLRDLLDNDREELSLRSSE-----ELALLLL 489
                       490       500
                ....*....|....*....|....*.
gi 83572016 489 RIINKLTM-SVVLLAFSIIMASLIIS 513
Cdd:COG0661 490 KAVARLSIgSILLVVLAVTVLLIAIL 515
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
1-518 6.08e-100

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310  Cd Length: 537  Bit Score: 315.31  E-value: 6.08e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016    1 MSLRRRYihlnryrQVVNVLARYGfgylLDQVGLGELILRRSREEAPL-----------SLGQRLRLALEELGPTFIKLG 69
Cdd:PRK04750   2 MELFRLY-------KIIRVFLRYG----LDELILSHRLTRPLRLWRRSlfwmpnrhkdkPRGERLRLALEELGPIFVKFG 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016   70 QLLSTRPDLLPADIISELTRLQDRVPPFPFADVRKAVEEELGQPLEELFASFDPEPLAVASIGQVHLATLPD-GSQVIVK 148
Cdd:PRK04750  71 QMLSTRRDLFPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQVHFARLKDnGREVVVK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016  149 VQRPGIARQVRVDLEILFDLARLAQRHTPYGKIYDFNQMAAEFARALTEELDYTREGRNADRFRENFAGDASVYFPAVYW 228
Cdd:PRK04750 151 VLRPDILPVIDADLALMYRLARWVERLLPDGRRLKPREVVAEFEKTLHDELDLMREAANASQLRRNFEDSDMLYVPEVYW 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016  229 DYTTRGVLTQEYVEAVKLNNLEEIDRRGYSRRRIAVNLARAVYQQVLVDGFFHGDPHPGNLAVLP-----GEVIVfMDFG 303
Cdd:PRK04750 231 DYCSETVMVMERMYGIPVSDVAALRAAGTDMKLLAERGVEVFFTQVFRDGFFHADMHPGNIFVSYdppenPRYIA-LDFG 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016  304 LTGTLTEELKEQFVNLVLGIIRRRSQDVLRTIIAMGMVPAEVDRGALRREIEALRDKYYHLSFRQISLGQAIEELLQLAF 383
Cdd:PRK04750 310 IVGSLNKEDKRYLAENFLAFFNRDYRRVAELHVESGWVPPDTRVEELEFAIRAVCEPIFDKPLAEISFGHVLLRLFNTAR 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016  384 RYHLRMPPELTLLGKTLLTLEGLVRKLDPELELAELAEPYGRELLRRRFSVRFLWRALTENLASGWEVMQSLPRQFQHLL 463
Cdd:PRK04750 390 RFNVEIQPQLVLLQKTLLNVEGLGRQLDPQLDLWKTAKPFLERWMKEQVGPRALVRALKEEAPFWAEKLPELPRLVHDSL 469
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 83572016  464 DLAERGELT--LRVEPLHLRGLVRQIDR-IINKLTMSVVLLAFSIIMASLIISTALGA 518
Cdd:PRK04750 470 RQGKLLQHSvdLLAEQLRTNRLRQGQSRyLLGVGATLLLAGTLLLLSRPELMPGAAGL 527
ABC1 pfam03109
ABC1 family; This family includes ABC1 from yeast and AarF from Escherichia coli. These ...
108-227 3.09e-46

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: 158.91  E-value: 3.09e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016   108 EELGQPLEELFASFDPEPLAVASIGQVHLATLPDGSQVIVKVQRPGIARQVRVDLEILFDLARLAQRhtpYGKIYDFNQM 187
Cdd:pfam03109   1 EELGAPVEEVFAEFDEEPIAAASIAQVHRAVLKDGEEVAVKVQRPGVKKRIRSDLKLLKFLAKILKK---FFPGFDLDWL 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 83572016   188 AAEFARALTEELDYTREGRNADRFRENFAGDASVYFPAVY 227
Cdd:pfam03109  78 VDEFRKSLPQELDFLREAANAEKFRENFADLPWVYVPKVY 117
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase (APH) and Choline Kinase (ChoK) family. The APH/ChoK ...
224-303 1.27e-05

Aminoglycoside 3'-phosphotransferase (APH) and Choline Kinase (ChoK) family. 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). The 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.


Pssm-ID: 240159  Cd Length: 155  Bit Score: 44.32  E-value: 1.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016 224 PAVYWDYTTRG--VLTQEYVEAVKLNNLEEIDRRgYSRRRIAVNLARavYQQVLVDGFFHGDPHPGNLAVLPGEVIVFMD 301
Cdd:cd05120  56 PKVLASGESDGwsYLLMEWIEGETLDEVSEEEKE-DIAEQLAELLAK--LHQLPLLVLCHGDLHPGNILVDDGKILGIID 132

                ..
gi 83572016 302 FG 303
Cdd:cd05120 133 WE 134
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
216-304 5.08e-04

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


Pssm-ID: 234331  Cd Length: 199  Bit Score: 40.28  E-value: 5.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016   216 AGDASVYFPAVYWDYTTRGVLTQEYVEAVKLNnlEEIDRRGYSR-RRIAVNLAR---AvyqqvlvdGFFHGDPHPGNLaV 291
Cdd:TIGR03724  54 ARKAGVNTPVVYDVDPDNKTIVMEYIEGKPLK--DVIEEGNDELlREIGRLVGKlhkA--------GIVHGDLTTSNI-I 122
                          90
                  ....*....|...
gi 83572016   292 LPGEVIVFMDFGL 304
Cdd:TIGR03724 123 VRDDKLYLIDFGL 135
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
224-304 5.15e-04

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 40.28  E-value: 5.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016  224 PAVYWDYTTRGVLTQEYVEAVKLNNLeeIDRRGYSRRriavNLARAVYQQVLV---DGFFHGDPHPGNLaVLPGEVIVFM 300
Cdd:PRK14879  64 PAVYFVDPENFIIVMEYIEGEPLKDL--INSNGMEEL----ELSREIGRLVGKlhsAGIIHGDLTTSNM-ILSGGKIYLI 136

                 ....
gi 83572016  301 DFGL 304
Cdd:PRK14879 137 DFGL 140
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3' ...
189-306 1.60e-03

Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase (APH) and Choline kinase (ChoK) family members. The APH/ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K). 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.


Pssm-ID: 240176  Cd Length: 235  Bit Score: 38.88  E-value: 1.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016 189 AEFARALTEELDYTREGRNADRFR----ENFAGDasvyfPAVYWDYTTRGVLtqeyveavkLNNLEEIDrrgysrrriaV 264
Cdd:cd05155  90 SEFAEDLADFLAALRQIDPSGGPPagrhNFLRGG-----DLAVRDAETREAI---------EALEGVID----------V 145
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 83572016 265 NLARAVYQQVL------VDGFFHGDPHPGNLAVLPGEVIVFMDFGLTG 306
Cdd:cd05155 146 DAARALWEAALrapwwgPPVWFHGDLAPGNLLVQDGRLSAVIDFGCLG 193
COG3642 COG3642
Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]
197-319 6.13e-03

Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]


Pssm-ID: 226168  Cd Length: 204  Bit Score: 36.88  E-value: 6.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016 197 EELDYT-REGRNADRFRE-NFAGDASVYFPAVYWDYTTRGVLTQEYVEAVKLNNLeeIDRRGYSR-RRIAVNLARavyqq 273
Cdd:COG3642  35 PELDEKlRRERTRREARIlAKAREAGVPVPIVYDVDPDNGLIVMEYIEGELLKDA--LEEARPDLlREVGRLVGK----- 107
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 83572016 274 VLVDGFFHGDPHPGNLaVLPGEVIVFMDFGLtGTLTEELKEQFVNL 319
Cdd:COG3642 108 LHKAGIVHGDLTTSNI-ILSGGRIYFIDFGL-GEFSDEVEDKAVDL 151
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
12-438 1.69e-151

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: 233667 [Multi-domain]  Cd Length: 437  Bit Score: 444.82  E-value: 1.69e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016    12 RYRQVVNVLARYGFGYLLD-QVGLGELILRR-------SREEAPLSLGQRLRLALEELGPTFIKLGQLLSTRPDLLPADI 83
Cdd:TIGR01982   3 RLRRIIRVLIRYGFLALVEsPIGPLSLRLLRrlllpfsNRENRLMSRGERLRLALEELGPTFIKFGQTLSTRADLLPADI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016    84 ISELTRLQDRVPPFPFADVRKAVEEELGQPLEELFASFDPEPLAVASIGQVHLATLPDGSQVIVKVQRPGIARQVRVDLE 163
Cdd:TIGR01982  83 AEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEEKPLAAASIAQVHRARLVDGKEVAVKVLRPGIEKTIAADIA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016   164 ILFDLARLAQRHTPYGKIYDFNQMAAEFARALTEELDYTREGRNADRFRENFAGDASVYFPAVYWDYTTRGVLTQEYVEA 243
Cdd:TIGR01982 163 LLYRLARIVERLSPDSRRLRPTEVVKEFEKTLRRELDLRREAANASELGENFKNDPGVYVPEVYWDRTSERVLTMEWIDG 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016   244 VKLNNLEEIDRRGYSRRRIAVNLARAVYQQVLVDGFFHGDPHPGNLAVLPGEVIVFMDFGLTGTLTEELKEQFVNLVLGI 323
Cdd:TIGR01982 243 IPLSDIAALDEAGLDRKALAENLARSFLNQVLRDGFFHADLHPGNIFVLKDGKIIALDFGIVGRLSEEDRRYLAEILYGF 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83572016   324 IRRRSQDVLRTIIAMGMVPAEVDRGALRREIEALRDKYYHLSFRQISLGQAIEELLQLAFRYHLRMPPELTLLGKTLLTL 403
Cdd:TIGR01982 323 LNRDYRRVAEVHFDAGYVPSDTDMAEFEQAIRAIGEPIFGQPLKEISVGRLLAGLFKITRDFNMELQPQLLLLQKTLLTV 402
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 83572016   404 EGLVRKLDPELELAELAEPYGRELLRRRFSVRFLW 438
Cdd:TIGR01982 403 EGVGRQLDPDLNMWKVAEPFVKRWIRKRLGPKAKI 437
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • 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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