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Conserved domains on  [gi|1534350390|gb|RSG57709|]
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AarF/ABC1/UbiB kinase family protein [Acinetobacter baumannii]

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 ...
10-431 1.05e-119

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: 357.59  E-value: 1.05e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390  10 LRSVARIGETAVVAAKAGIKYATD--------------------KPSNAKLMRETFESLGSTYIKLGQFIASTPSLFPRE 69
Cdd:COG0661     4 LRRLRRLARIARVLLRYGLGELLDrlglprlrrlltgeerreelRRRRAERLRLALEELGPTFIKLGQLLSTRPDLLPPE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390  70 YVEEFQGCLDQTPTLPFSYIQGVLASEFeGRDLSQIFSYIDETPLASASIAQVHAAKLTTGEDVVIKVQKPGVETILYTD 149
Cdd:COG0661    84 YAEELAKLQDRVPPFPFEEVRAVIEEEL-GRPLEELFAEFDPEPLAAASIGQVHRARLKDGREVAVKVQRPGIEEAIEAD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 150 LNVVHWAAKLLERAVPKIKFAALSEIVDEIKTRMVREVDFIEEAQNLDDFVEylNISQNQAATAPKVYHQFSTRRVLTMQ 229
Cdd:COG0661   163 LRILRRLARLLERLSPEGRRLDPVEVVDEFARSLLEELDYRREAANAERFRR--NFADDPDVYVPKVYWELSTRRVLTME 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 230 RLYGVPLTDFSVVKQYAKDPSQVLITAMNTWFGSLMLCKSFHADLHAGNLMLLEDGRIGFIDFGIVGQLKPEVWTACIAF 309
Cdd:COG0661   241 WIDGIKISDLEALDAAGIDRKRLAERLVRAFLRQVFRDGFFHADPHPGNIFVLPDGRLVLLDFGMVGRLDPETREGLAEL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 310 MDALQKTDYQAMAENMLKMGMTHNKIDVQVLAQDLERLFNGVLMADPQQIlasnpaDLNDIMMDMVAVGERHGIKFPRDF 389
Cdd:COG0661   321 LLALLNRDYDRVAEALLELGFVPPDTDVDELERALRAVLEPYFGKPLKDI------SFGELLLELFELARRFPLRLPPEL 394
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1534350390 390 ALLFKQMLYFDRFMRVLAPYTDIYAD-----QRLkMVQNMEPASLLK 431
Cdd:COG0661   395 VLLQRTLLTLEGVGRQLDPDFDLWEVakpflERL-LRERLGPRALLK 440
 
Name Accession Description Interval E-value
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
10-431 1.05e-119

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: 357.59  E-value: 1.05e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390  10 LRSVARIGETAVVAAKAGIKYATD--------------------KPSNAKLMRETFESLGSTYIKLGQFIASTPSLFPRE 69
Cdd:COG0661     4 LRRLRRLARIARVLLRYGLGELLDrlglprlrrlltgeerreelRRRRAERLRLALEELGPTFIKLGQLLSTRPDLLPPE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390  70 YVEEFQGCLDQTPTLPFSYIQGVLASEFeGRDLSQIFSYIDETPLASASIAQVHAAKLTTGEDVVIKVQKPGVETILYTD 149
Cdd:COG0661    84 YAEELAKLQDRVPPFPFEEVRAVIEEEL-GRPLEELFAEFDPEPLAAASIGQVHRARLKDGREVAVKVQRPGIEEAIEAD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 150 LNVVHWAAKLLERAVPKIKFAALSEIVDEIKTRMVREVDFIEEAQNLDDFVEylNISQNQAATAPKVYHQFSTRRVLTMQ 229
Cdd:COG0661   163 LRILRRLARLLERLSPEGRRLDPVEVVDEFARSLLEELDYRREAANAERFRR--NFADDPDVYVPKVYWELSTRRVLTME 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 230 RLYGVPLTDFSVVKQYAKDPSQVLITAMNTWFGSLMLCKSFHADLHAGNLMLLEDGRIGFIDFGIVGQLKPEVWTACIAF 309
Cdd:COG0661   241 WIDGIKISDLEALDAAGIDRKRLAERLVRAFLRQVFRDGFFHADPHPGNIFVLPDGRLVLLDFGMVGRLDPETREGLAEL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 310 MDALQKTDYQAMAENMLKMGMTHNKIDVQVLAQDLERLFNGVLMADPQQIlasnpaDLNDIMMDMVAVGERHGIKFPRDF 389
Cdd:COG0661   321 LLALLNRDYDRVAEALLELGFVPPDTDVDELERALRAVLEPYFGKPLKDI------SFGELLLELFELARRFPLRLPPEL 394
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1534350390 390 ALLFKQMLYFDRFMRVLAPYTDIYAD-----QRLkMVQNMEPASLLK 431
Cdd:COG0661   395 VLLQRTLLTLEGVGRQLDPDFDLWEVakpflERL-LRERLGPRALLK 440
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
77-325 8.86e-90

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: 272.45  E-value: 8.86e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390  77 CLDQTPTLPFSYIQGVLASEFeGRDLSQIFSYIDETPLASASIAQVHAAKLTTGEDVVIKVQKPGVETILYTDLNVVHWA 156
Cdd:cd05121     2 LQDDVPPFPFEEVRKIIEEEL-GRPLEEVFAEFDPEPLAAASIAQVHRARLKDGREVAVKVQRPGIEEIIEADLRILRRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 157 AKLLERAVPKIKFAALSEIVDEIKTRMVREVDFIEEAQNLDDFVEylNISQNQAATAPKVYHQFSTRRVLTMQRLYGVPL 236
Cdd:cd05121    81 ARLLERLSPLLRRLDLVAIVDEFARSLLEELDFRREARNAERFRK--NLKDSPDVYVPKVYPELSTRRVLVMEYIDGVKL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 237 TDFSVVKQYAKDPSQVLITAMNTWFGSLMLCKSFHADLHAGNLMLLEDGRIGFIDFGIVGQLKPEVWTACIAFMDALQKT 316
Cdd:cd05121   159 TDLEALRAAGIDRKELARRLVDAYLKQIFEDGFFHADPHPGNILVLPDGRIALLDFGMVGRLDPETREALADLLLALVNG 238

                  ....*....
gi 1534350390 317 DYQAMAENM 325
Cdd:cd05121   239 DAEGLAEAL 247
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
41-414 9.49e-77

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: 245.28  E-value: 9.49e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390  41 MRETFESLGSTYIKLGQFIASTPSLFPREYVEEFQGCLDQTPTLPFSYIQGVLASEFeGRDLSQIFSYIDETPLASASIA 120
Cdd:TIGR01982  53 LRLALEELGPTFIKFGQTLSTRADLLPADIAEELSLLQDRVPPFDFKVARKVIEAAL-GGPLEELFAEFEEKPLAAASIA 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 121 QVHAAKLTTGEDVVIKVQKPGVETILYTDLNVVHWAAKLLERAVPKIKFAALSEIVDEIKTRMVREVDFIEEAQNLDDFV 200
Cdd:TIGR01982 132 QVHRARLVDGKEVAVKVLRPGIEKTIAADIALLYRLARIVERLSPDSRRLRPTEVVKEFEKTLRRELDLRREAANASELG 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 201 EylNISQNQAATAPKVYHQFSTRRVLTMQRLYGVPLTDFSVVKQYAKDPSQVLITAMNTWFGSLMLCKSFHADLHAGNLM 280
Cdd:TIGR01982 212 E--NFKNDPGVYVPEVYWDRTSERVLTMEWIDGIPLSDIAALDEAGLDRKALAENLARSFLNQVLRDGFFHADLHPGNIF 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 281 LLEDGRIGFIDFGIVGQLKPEVWTACIAFMDALQKTDYQAMAENMLKMGMTHNKIDVQVLAQDLERLFNGVLMADPQQIl 360
Cdd:TIGR01982 290 VLKDGKIIALDFGIVGRLSEEDRRYLAEILYGFLNRDYRRVAEVHFDAGYVPSDTDMAEFEQAIRAIGEPIFGQPLKEI- 368
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1534350390 361 asnpaDLNDIMMDMVAVGERHGIKFPRDFALLFKQMLYFDRFMRVLAPYTDIYA 414
Cdd:TIGR01982 369 -----SVGRLLAGLFKITRDFNMELQPQLLLLQKTLLTVEGVGRQLDPDLNMWK 417
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
79-325 2.12e-62

ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. These proteins have a nuclear or mitochondrial subcellular location in eukaryotes. The exact molecular functions of these proteins is not clear, however yeast ABC1 suppresses a cytochrome b mRNA translation defect and is essential for the electron transfer in the bc 1 complex and E. coli AarF is required for ubiquinone production. It has been suggested that members of the ABC1 family are novel chaperonins. These proteins are unrelated to the ABC transporter proteins.


Pssm-ID: 427143 [Multi-domain]  Cd Length: 245  Bit Score: 201.69  E-value: 2.12e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390  79 DQTPTLPFSYIQGVLASEFeGRDLSQIFSYIDETPLASASIAQVHAAKLTTGEDVVIKVQKPGVETILYTDLNVVHWAAK 158
Cdd:pfam03109   4 DRAPPFPFEQAKKVIEEEL-GAPVEEIFAEFDEEPIAAASIAQVHRARLKDGEEVAVKVQRPGVKKRIRSDLLLLRFLAK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 159 LLERAVPkiKFAALSEIVDEIKTRMVREVDFIEEAQNLDDFVEylNISQNQAATAPKVYHQFSTRRVLTMQRLYGVPLTD 238
Cdd:pfam03109  83 VAKRFFP--GFRRLDWLVDEFRKSLPQELDFLREAANAEKFRE--NFADDPDVYVPKVYWELTTERVLTMEYVDGIKIDD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 239 FSVVKQYAKDPSQVLITAMNTWFGSLMLCKSFHADLHAGNLMLLEDGRIGFIDFGIVGQLKP-------EVWTACIafmd 311
Cdd:pfam03109 159 LDALSEAGIDRKEIARRLVELFLEQIFRDGFFHADPHPGNILVRKDGRIVLLDFGLMGRLDEkfrrlyaELLLALV---- 234
                         250
                  ....*....|....
gi 1534350390 312 alqKTDYQAMAENM 325
Cdd:pfam03109 235 ---NRDYKRVAEML 245
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
32-298 2.44e-39

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 148.13  E-value: 2.44e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390  32 TDKPSNAKLmRETFESLGSTYIKLGQFIASTPSLFPREYVEEFQGCLDQTPtlPFSYIQGVLASE-FEGRDLSQIFSYID 110
Cdd:PRK04750   47 KDKPRGERL-RLALEELGPIFVKFGQMLSTRRDLFPPDIADELALLQDRVP--PFDGALARAIIEkALGGPVEEWFDDFD 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 111 ETPLASASIAQVHAAKL-TTGEDVVIKVQKPGVETILYTDLNVVHWAAKLLERAVPKIKFAALSEIVDEIKTRMVREVDF 189
Cdd:PRK04750  124 IKPLASASIAQVHFARLkDNGREVVVKVLRPDILPVIDADLALMYRLARWVERLLPDGRRLKPREVVAEFEKTLHDELDL 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 190 IEEAQN---LDDFVEYLNISQnqaatAPKVYHQFSTRRVLTMQRLYGVPLTDFSV-------VKQYAKDPSQVLITAM-N 258
Cdd:PRK04750  204 MREAANasqLRRNFEDSDMLY-----VPEVYWDYCSETVMVMERMYGIPVSDVAAlraagtdMKLLAERGVEVFFTQVfR 278
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1534350390 259 TWFgslmlcksFHADLHAGNLML----LEDGR-IGfIDFGIVGQL 298
Cdd:PRK04750  279 DGF--------FHADMHPGNIFVsydpPENPRyIA-LDFGIVGSL 314
 
Name Accession Description Interval E-value
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
10-431 1.05e-119

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: 357.59  E-value: 1.05e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390  10 LRSVARIGETAVVAAKAGIKYATD--------------------KPSNAKLMRETFESLGSTYIKLGQFIASTPSLFPRE 69
Cdd:COG0661     4 LRRLRRLARIARVLLRYGLGELLDrlglprlrrlltgeerreelRRRRAERLRLALEELGPTFIKLGQLLSTRPDLLPPE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390  70 YVEEFQGCLDQTPTLPFSYIQGVLASEFeGRDLSQIFSYIDETPLASASIAQVHAAKLTTGEDVVIKVQKPGVETILYTD 149
Cdd:COG0661    84 YAEELAKLQDRVPPFPFEEVRAVIEEEL-GRPLEELFAEFDPEPLAAASIGQVHRARLKDGREVAVKVQRPGIEEAIEAD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 150 LNVVHWAAKLLERAVPKIKFAALSEIVDEIKTRMVREVDFIEEAQNLDDFVEylNISQNQAATAPKVYHQFSTRRVLTMQ 229
Cdd:COG0661   163 LRILRRLARLLERLSPEGRRLDPVEVVDEFARSLLEELDYRREAANAERFRR--NFADDPDVYVPKVYWELSTRRVLTME 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 230 RLYGVPLTDFSVVKQYAKDPSQVLITAMNTWFGSLMLCKSFHADLHAGNLMLLEDGRIGFIDFGIVGQLKPEVWTACIAF 309
Cdd:COG0661   241 WIDGIKISDLEALDAAGIDRKRLAERLVRAFLRQVFRDGFFHADPHPGNIFVLPDGRLVLLDFGMVGRLDPETREGLAEL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 310 MDALQKTDYQAMAENMLKMGMTHNKIDVQVLAQDLERLFNGVLMADPQQIlasnpaDLNDIMMDMVAVGERHGIKFPRDF 389
Cdd:COG0661   321 LLALLNRDYDRVAEALLELGFVPPDTDVDELERALRAVLEPYFGKPLKDI------SFGELLLELFELARRFPLRLPPEL 394
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1534350390 390 ALLFKQMLYFDRFMRVLAPYTDIYAD-----QRLkMVQNMEPASLLK 431
Cdd:COG0661   395 VLLQRTLLTLEGVGRQLDPDFDLWEVakpflERL-LRERLGPRALLK 440
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
77-325 8.86e-90

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: 272.45  E-value: 8.86e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390  77 CLDQTPTLPFSYIQGVLASEFeGRDLSQIFSYIDETPLASASIAQVHAAKLTTGEDVVIKVQKPGVETILYTDLNVVHWA 156
Cdd:cd05121     2 LQDDVPPFPFEEVRKIIEEEL-GRPLEEVFAEFDPEPLAAASIAQVHRARLKDGREVAVKVQRPGIEEIIEADLRILRRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 157 AKLLERAVPKIKFAALSEIVDEIKTRMVREVDFIEEAQNLDDFVEylNISQNQAATAPKVYHQFSTRRVLTMQRLYGVPL 236
Cdd:cd05121    81 ARLLERLSPLLRRLDLVAIVDEFARSLLEELDFRREARNAERFRK--NLKDSPDVYVPKVYPELSTRRVLVMEYIDGVKL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 237 TDFSVVKQYAKDPSQVLITAMNTWFGSLMLCKSFHADLHAGNLMLLEDGRIGFIDFGIVGQLKPEVWTACIAFMDALQKT 316
Cdd:cd05121   159 TDLEALRAAGIDRKELARRLVDAYLKQIFEDGFFHADPHPGNILVLPDGRIALLDFGMVGRLDPETREALADLLLALVNG 238

                  ....*....
gi 1534350390 317 DYQAMAENM 325
Cdd:cd05121   239 DAEGLAEAL 247
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
41-414 9.49e-77

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: 245.28  E-value: 9.49e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390  41 MRETFESLGSTYIKLGQFIASTPSLFPREYVEEFQGCLDQTPTLPFSYIQGVLASEFeGRDLSQIFSYIDETPLASASIA 120
Cdd:TIGR01982  53 LRLALEELGPTFIKFGQTLSTRADLLPADIAEELSLLQDRVPPFDFKVARKVIEAAL-GGPLEELFAEFEEKPLAAASIA 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 121 QVHAAKLTTGEDVVIKVQKPGVETILYTDLNVVHWAAKLLERAVPKIKFAALSEIVDEIKTRMVREVDFIEEAQNLDDFV 200
Cdd:TIGR01982 132 QVHRARLVDGKEVAVKVLRPGIEKTIAADIALLYRLARIVERLSPDSRRLRPTEVVKEFEKTLRRELDLRREAANASELG 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 201 EylNISQNQAATAPKVYHQFSTRRVLTMQRLYGVPLTDFSVVKQYAKDPSQVLITAMNTWFGSLMLCKSFHADLHAGNLM 280
Cdd:TIGR01982 212 E--NFKNDPGVYVPEVYWDRTSERVLTMEWIDGIPLSDIAALDEAGLDRKALAENLARSFLNQVLRDGFFHADLHPGNIF 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 281 LLEDGRIGFIDFGIVGQLKPEVWTACIAFMDALQKTDYQAMAENMLKMGMTHNKIDVQVLAQDLERLFNGVLMADPQQIl 360
Cdd:TIGR01982 290 VLKDGKIIALDFGIVGRLSEEDRRYLAEILYGFLNRDYRRVAEVHFDAGYVPSDTDMAEFEQAIRAIGEPIFGQPLKEI- 368
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1534350390 361 asnpaDLNDIMMDMVAVGERHGIKFPRDFALLFKQMLYFDRFMRVLAPYTDIYA 414
Cdd:TIGR01982 369 -----SVGRLLAGLFKITRDFNMELQPQLLLLQKTLLTVEGVGRQLDPDLNMWK 417
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
79-325 2.12e-62

ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. These proteins have a nuclear or mitochondrial subcellular location in eukaryotes. The exact molecular functions of these proteins is not clear, however yeast ABC1 suppresses a cytochrome b mRNA translation defect and is essential for the electron transfer in the bc 1 complex and E. coli AarF is required for ubiquinone production. It has been suggested that members of the ABC1 family are novel chaperonins. These proteins are unrelated to the ABC transporter proteins.


Pssm-ID: 427143 [Multi-domain]  Cd Length: 245  Bit Score: 201.69  E-value: 2.12e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390  79 DQTPTLPFSYIQGVLASEFeGRDLSQIFSYIDETPLASASIAQVHAAKLTTGEDVVIKVQKPGVETILYTDLNVVHWAAK 158
Cdd:pfam03109   4 DRAPPFPFEQAKKVIEEEL-GAPVEEIFAEFDEEPIAAASIAQVHRARLKDGEEVAVKVQRPGVKKRIRSDLLLLRFLAK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 159 LLERAVPkiKFAALSEIVDEIKTRMVREVDFIEEAQNLDDFVEylNISQNQAATAPKVYHQFSTRRVLTMQRLYGVPLTD 238
Cdd:pfam03109  83 VAKRFFP--GFRRLDWLVDEFRKSLPQELDFLREAANAEKFRE--NFADDPDVYVPKVYWELTTERVLTMEYVDGIKIDD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 239 FSVVKQYAKDPSQVLITAMNTWFGSLMLCKSFHADLHAGNLMLLEDGRIGFIDFGIVGQLKP-------EVWTACIafmd 311
Cdd:pfam03109 159 LDALSEAGIDRKEIARRLVELFLEQIFRDGFFHADPHPGNILVRKDGRIVLLDFGLMGRLDEkfrrlyaELLLALV---- 234
                         250
                  ....*....|....
gi 1534350390 312 alqKTDYQAMAENM 325
Cdd:pfam03109 235 ---NRDYKRVAEML 245
ABC1_ADCK3 cd13970
Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This ...
79-329 3.44e-54

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: 180.79  E-value: 3.44e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390  79 DQTPTLPFSYIQGVLASEFeGRDLSQIFSYIDETPLASASIAQVHAAKLTTGEDVVIKVQKPGVETILYTDLNVVHWAAK 158
Cdd:cd13970     8 DSAPPMPWAQLEKVLEAEL-GEDWRELFAEFDEEPFAAASIGQVHRATLKDGREVAVKVQYPGVAESIDSDLNNLRRLLK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 159 LLeRAVPKIKFaaLSEIVDEIKTRMVREVDFIEEAQNLDDFVEYLnisQNQAATA-PKVYHQFSTRRVLTMQRLYGVPLT 237
Cdd:cd13970    87 LT-GLLPKGLD--LDALIAELREELLEECDYEREAANQRRFRELL---ADDPRFVvPEVIPELSTKRVLTTEFVDGVPLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 238 DfsvvkqyAKDPSQVLI-----TAMNTWFGSLMLCKSFHADLHAGNLMLLE-DGRIGFIDFGIVGQLKPEVWTACIAFMD 311
Cdd:cd13970   161 E-------AADLSQEERnrigeLLLRLCLRELFEFGFMQTDPNPGNFLYDPeDGRLGLLDFGAVREYPPEFVDGYRRLVR 233
                         250
                  ....*....|....*...
gi 1534350390 312 ALQKTDYQAMAENMLKMG 329
Cdd:cd13970   234 AALEGDREALLEASVELG 251
UbiB cd13972
Ubiquinone biosynthetic protein UbiB; UbiB is the prokaryotic homolog of yeast Abc1p and human ...
79-298 8.07e-54

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: 179.70  E-value: 8.07e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390  79 DQTPTLPFSYIQGVLASEFeGRDLSQIFSYIDETPLASASIAQVHAAKLTTGEDVVIKVQKPGVETILYTDLNVVHWAAK 158
Cdd:cd13972     4 DRVPPFSGKEARAIIEAEL-GKPLDALFSDFDEEPVAAASIAQVHKARLLDGREVAVKVLRPGIEKRIERDLELLRFLAR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 159 LLERAVPKIKFAALSEIVDEIKTRMVREVDFIEEAQNLDDFVEylNISQNQAATAPKVYHQFSTRRVLTMQRLYGVPLTD 238
Cdd:cd13972    83 LAERLLPEARRLRPVEVVKEFARSLLLELDLRLEAANASELRE--NFLDDPGFYVPEVYWELTSKNVLTMEWIDGIPISD 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 239 FSVVKQYAKDPSQVLITAMNTWFGSLMLCKSFHADLHAGNLMLLEDGRIGFIDFGIVGQL 298
Cdd:cd13972   161 IEALDAAGIDRKALAERLVEIFFRQVFRDGFFHADMHPGNIFVDPNGRIIAVDFGIMGRL 220
ADCK1-like cd13969
aarF domain containing kinase 1 and similar proteins; This subfamily is composed of ...
77-280 9.61e-48

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: 163.81  E-value: 9.61e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390  77 CLDQTPTLPFSYIQGVLASEFeGRDLSQIFSYIDETPLASASIAQVHAAKLTTGEDVVIKVQKPGVETILYTDLNVVHWA 156
Cdd:cd13969     2 LQDKAPQSPYEEVRRVFKEDL-GKPPEELFSEFDEEPIASASLAQVHKAKLKDGEEVAVKVQHPDLRKQFAGDLATMEFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 157 AKLLERAVPKIKFAALseiVDEIKTRMVREVDFIEEAQNLDDFVEYLNISQNqaATAPKVYHQFSTRRVLTMQRLYGVPL 236
Cdd:cd13969    81 VNLVEKLFPDFPFSWL---VDELKKNLPKELDFLNEARNAERCAKLFKHRPD--VYVPKVYWDLSSKRVLTMEFIDGIKI 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1534350390 237 TDFSVVKQYAKDPSQVLITAMNTwFGSLMLCKSF-HADLHAGNLM 280
Cdd:cd13969   156 DDVEALKKLGIDPKEVARLLSEA-FAEMIFVHGFvHCDPHPGNLL 199
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
32-298 2.44e-39

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 148.13  E-value: 2.44e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390  32 TDKPSNAKLmRETFESLGSTYIKLGQFIASTPSLFPREYVEEFQGCLDQTPtlPFSYIQGVLASE-FEGRDLSQIFSYID 110
Cdd:PRK04750   47 KDKPRGERL-RLALEELGPIFVKFGQMLSTRRDLFPPDIADELALLQDRVP--PFDGALARAIIEkALGGPVEEWFDDFD 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 111 ETPLASASIAQVHAAKL-TTGEDVVIKVQKPGVETILYTDLNVVHWAAKLLERAVPKIKFAALSEIVDEIKTRMVREVDF 189
Cdd:PRK04750  124 IKPLASASIAQVHFARLkDNGREVVVKVLRPDILPVIDADLALMYRLARWVERLLPDGRRLKPREVVAEFEKTLHDELDL 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 190 IEEAQN---LDDFVEYLNISQnqaatAPKVYHQFSTRRVLTMQRLYGVPLTDFSV-------VKQYAKDPSQVLITAM-N 258
Cdd:PRK04750  204 MREAANasqLRRNFEDSDMLY-----VPEVYWDYCSETVMVMERMYGIPVSDVAAlraagtdMKLLAERGVEVFFTQVfR 278
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1534350390 259 TWFgslmlcksFHADLHAGNLML----LEDGR-IGfIDFGIVGQL 298
Cdd:PRK04750  279 DGF--------FHADMHPGNIFVsydpPENPRyIA-LDFGIVGSL 314
ADCK2-like cd13971
aarF domain containing kinase 2 and similar proteins; This subfamily is composed of ...
79-349 9.07e-36

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: 133.50  E-value: 9.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390  79 DQTPTLPFSYIQGVLASEFeGRDLSQIFSYIDETPLASASIAQVHAAKL--------TTGEDVVIKVQKPGVETILYTDL 150
Cdd:cd13971     4 SNAPPHSWAHTERALEAAF-GKDWEDIFEEFDEEPIGSGSIAQVHRAKLkpdyggdgGGPRVVAVKVLHPGVREQIERDL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 151 NVVHWAAKLLERaVPKIKFAALSEIVDEIKTRMVREVDFIEEAQNLDDFVEylNISQNQAATAPKVYHQFSTRRVLTMQR 230
Cdd:cd13971    83 AILRLFAKLLEA-IPPLRWLSLPESVEQFASLMLRQLDLRVEAANLERFRE--NFKDRKDVSFPKPLYPLVTEEVLVETF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 231 LYGVPLTDFSVVKQYAKDPSQVLITAMNTWFGSLMLCKSFHADLHAGNLMLLEDG-----------------RIGFIDFG 293
Cdd:cd13971   160 EEGVPISRTVLAHGGEPLKRKLARIGLDAFLKMLFVDNFVHGDLHPGNILVRFNDsnrpsllvsldargsppRLVFLDAG 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1534350390 294 IVGQLKPEVWTACIAFMDALQKTDYQAMAENMLKMGMT-HNKIDVQVLAQDLERLFN 349
Cdd:cd13971   240 LVTELSPQDRRNFIDLFKAVARGDGYKAAELMLERSRSsQTCPDPEGFKSEMEELVN 296
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
181-325 1.33e-06

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


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 48.03  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 181 TRMVREVDFIEEAQNLDdfveylnisqnqaATAPKVYHQFSTRRVLTMQRLYGVPLTDfsVVKQYAKDPSqvLITAMNTW 260
Cdd:COG3642     1 ERTRREARLLRELREAG-------------VPVPKVLDVDPDDADLVMEYIEGETLAD--LLEEGELPPE--LLRELGRL 63
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1534350390 261 FGSLMLCKSFHADLHAGNlMLLEDGRIGFIDFGIVGQLKPEVWTA--CIAFMDALQKTDYQAMAENM 325
Cdd:COG3642    64 LARLHRAGIVHGDLTTSN-ILVDDGGVYLIDFGLARYSDPLEDKAvdLAVLKRSLESTHPDPAEELW 129
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
270-296 5.95e-05

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: 44.15  E-value: 5.95e-05
                          10        20
                  ....*....|....*....|....*...
gi 1534350390 270 FHADLHAGNLmLLEDGRI-GFIDFGIVG 296
Cdd:cd05155   166 LHGDLHPGNL-LVRDGRLsAVIDFGDLG 192
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
164-311 1.37e-04

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


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 42.29  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 164 VPKIKFAALSEivdeiktRMVREVDFIEEAQnlddfvEYLNISqnqaatAPKVYHQF--STRRVLTMQRLYGVPLTDFSV 241
Cdd:cd05120    24 VLKIGPPRLKK-------DLEKEAAMLQLLA------GKLSLP------VPKVYGFGesDGWEYLLMERIEGETLSEVWP 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1534350390 242 VKQYAKDPS--QVLITAMNTWFGSLMLCkSFHADLHAGNLMLLEDGRI-GFIDFGIVGqLKPEVWTACIAFMD 311
Cdd:cd05120    85 RLSEEEKEKiaDQLAEILAALHRIDSSV-LTHGDLHPGNILVKPDGKLsGIIDWEFAG-YGPPAFDYAAALRD 155
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
271-293 4.77e-04

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: 41.83  E-value: 4.77e-04
                          10        20
                  ....*....|....*....|...
gi 1534350390 271 HADLHAGNLMLLEDGRIGFIDFG 293
Cdd:COG2334   183 HGDLHPDNVLFDGDGVSGLIDFD 205
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
223-292 5.73e-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 [Multi-domain]  Cd Length: 183  Bit Score: 40.57  E-value: 5.73e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 223 RRVLTMQRLYGVPLTDFSVVKqyakDPSQVLITAMNTwFGSLMLCKSFHADLHAGNLMLLEDGRIGFIDF 292
Cdd:cd05144    90 RHAVVMELIDGYPLYQVRLLE----DPEEVLDEILEL-IVKLAKHGLIHGDFSEFNILVDEDEKITVIDF 154
COG3178 COG3178
Predicted phosphotransferase, aminoglycoside/choline kinase (APH/ChoK) family [General ...
271-292 5.83e-04

Predicted phosphotransferase, aminoglycoside/choline kinase (APH/ChoK) family [General function prediction only];


Pssm-ID: 442411  Cd Length: 327  Bit Score: 41.72  E-value: 5.83e-04
                          10        20
                  ....*....|....*....|..
gi 1534350390 271 HADLHAGNLMLLEDGRIGFIDF 292
Cdd:COG3178   186 HRDFHSRNLMVLPDGRPGLIDF 207
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
271-293 7.72e-04

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: 40.95  E-value: 7.72e-04
                          10        20
                  ....*....|....*....|....
gi 1534350390 271 HADLHAGNLMLLEDGRI-GFIDFG 293
Cdd:pfam01636 171 HGDLHPGNLLVDPGGRVsGVIDFE 194
ChoK-like_euk cd14021
Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline ...
213-292 2.61e-03

Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline kinase, ethanolamine kinase, and similar proteins. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270923 [Multi-domain]  Cd Length: 229  Bit Score: 39.17  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534350390 213 APKVYHQFSTRRVltMQRLYGVPLT-----DFSVVKQYAKDPSQVLITAMNtwfgSLMLCksfHADLHAGNLMLLEDG-R 286
Cdd:cd14021    62 GPKLIYKFDGGRI--EEYIDGRPLTtdelrNPSVLTSIAKLLAKFHKIKTP----PVVFC---HNDLQENNILLTNDQdG 132

                  ....*.
gi 1534350390 287 IGFIDF 292
Cdd:cd14021   133 LRLIDF 138
 
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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