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Conserved domains on  [gi|42567114|ref|NP_194212|]
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Protein kinase superfamily protein [Arabidopsis thaliana]

Protein Classification

AarF/ABC1/UbiB kinase family protein( domain architecture ID 10142146)

AarF/ABC1/UbiB kinase family protein belonging to the protein kinase superfamily, similar to Triticum aestivum ABC1 protein kinase (TaABC1)

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

Graphical summary

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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 ...
60-316 1.47e-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: 292.48  E-value: 1.47e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114  60 LCDQAPATPFDAVRVVLEKELGKSIEQVFETFDEKPLGSASIAQVHRARVKgDKRDVVVKVQHPGVEKLMMVDIRNLQIF 139
Cdd:cd05121   2 LQDDVPPFPFEEVRKIIEEELGRPLEEVFAEFDPEPLAAASIAQVHRARLK-DGREVAVKVQRPGIEEIIEADLRILRRL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 140 ALYMQK---TDIKFDLFSMTKEIEKQIGYEFDFKREANAMEKIRRFLYDNNRkspVLVPRVFPNLVTRKVLVMEFMNGIP 216
Cdd:cd05121  81 ARLLERlspLLRRLDLVAIVDEFARSLLEELDFRREARNAERFRKNLKDSPD---VYVPKVYPELSTRRVLVMEYIDGVK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 217 ILSLgDEMAKRGINPHgkmaeaakfNILHSLSQAYGQMILKSGFFHADPHPGNILIGKGSEVALLDYGQVKELPDHLRLG 296
Cdd:cd05121 158 LTDL-EALRAAGIDRK---------ELARRLVDAYLKQIFEDGFFHADPHPGNILVLPDGRIALLDFGMVGRLDPETREA 227
                       250       260
                ....*....|....*....|
gi 42567114 297 YANLVIAIADNNASLALQSF 316
Cdd:cd05121 228 LADLLLALVNGDAEGLAEAL 247
 
Name Accession Description Interval E-value
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
60-316 1.47e-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: 292.48  E-value: 1.47e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114  60 LCDQAPATPFDAVRVVLEKELGKSIEQVFETFDEKPLGSASIAQVHRARVKgDKRDVVVKVQHPGVEKLMMVDIRNLQIF 139
Cdd:cd05121   2 LQDDVPPFPFEEVRKIIEEELGRPLEEVFAEFDPEPLAAASIAQVHRARLK-DGREVAVKVQRPGIEEIIEADLRILRRL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 140 ALYMQK---TDIKFDLFSMTKEIEKQIGYEFDFKREANAMEKIRRFLYDNNRkspVLVPRVFPNLVTRKVLVMEFMNGIP 216
Cdd:cd05121  81 ARLLERlspLLRRLDLVAIVDEFARSLLEELDFRREARNAERFRKNLKDSPD---VYVPKVYPELSTRRVLVMEYIDGVK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 217 ILSLgDEMAKRGINPHgkmaeaakfNILHSLSQAYGQMILKSGFFHADPHPGNILIGKGSEVALLDYGQVKELPDHLRLG 296
Cdd:cd05121 158 LTDL-EALRAAGIDRK---------ELARRLVDAYLKQIFEDGFFHADPHPGNILVLPDGRIALLDFGMVGRLDPETREA 227
                       250       260
                ....*....|....*....|
gi 42567114 297 YANLVIAIADNNASLALQSF 316
Cdd:cd05121 228 LADLLLALVNGDAEGLAEAL 247
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
14-393 1.20e-94

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: 293.26  E-value: 1.20e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114  14 WERQHELAAHKVYSMCSDLGGFFLKIAQILG-KPDLAPAAWVRKLVTLCDQAPATPFDAVRVVLEKELGKSIEQVFETFD 92
Cdd:COG0661  44 REELRRRRAERLRLALEELGPTFIKLGQLLStRPDLLPPEYAEELAKLQDRVPPFPFEEVRAVIEEELGRPLEELFAEFD 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114  93 EKPLGSASIAQVHRARVKgDKRDVVVKVQHPGVEKLMMVDIRNLQIFALYMQKTD---IKFDLFSMTKEIEKQIGYEFDF 169
Cdd:COG0661 124 PEPLAAASIGQVHRARLK-DGREVAVKVQRPGIEEAIEADLRILRRLARLLERLSpegRRLDPVEVVDEFARSLLEELDY 202
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 170 KREANAMEKIRRFLYDNNRkspVLVPRVFPNLVTRKVLVMEFMNGIPILSLgDEMAKRGINPHgKMAEAakfnilhsLSQ 249
Cdd:COG0661 203 RREAANAERFRRNFADDPD---VYVPKVYWELSTRRVLTMEWIDGIKISDL-EALDAAGIDRK-RLAER--------LVR 269
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 250 AYGQMILKSGFFHADPHPGNILIGKGSEVALLDYGQVKELPDHLRLGYANLVIAIADNNASLALQSFRELGIATVakcKN 329
Cdd:COG0661 270 AFLRQVFRDGFFHADPHPGNIFVLPDGRLVLLDFGMVGRLDPETREGLAELLLALLNRDYDRVAEALLELGFVPP---DT 346
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42567114 330 EQQELLQLAKTMFDtemppgtttlqPFSEDsSIKKISVEAFPEELFSVLR---------TVVLLRGLSVGIGI 393
Cdd:COG0661 347 DVDELERALRAVLE-----------PYFGK-PLKDISFGELLLELFELARrfplrlppeLVLLQRTLLTLEGV 407
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
62-315 3.33e-73

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: 229.81  E-value: 3.33e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114    62 DQAPATPFDAVRVVLEKELGKSIEQVFETFDEKPLGSASIAQVHRARVKgDKRDVVVKVQHPGVEKLMMVDIRNLQIFAl 141
Cdd:pfam03109   4 DRAPPFPFEQAKKVIEEELGAPVEEIFAEFDEEPIAAASIAQVHRARLK-DGEEVAVKVQRPGVKKRIRSDLLLLRFLA- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114   142 ymQKTDIKF-DLFSMT---KEIEKQIGYEFDFKREANAMEKIRrflyDNNRKSP-VLVPRVFPNLVTRKVLVMEFMNGIP 216
Cdd:pfam03109  82 --KVAKRFFpGFRRLDwlvDEFRKSLPQELDFLREAANAEKFR----ENFADDPdVYVPKVYWELTTERVLTMEYVDGIK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114   217 ILSLgDEMAKRGINPHgkmaeaakfNILHSLSQAYGQMILKSGFFHADPHPGNILIGKGSEVALLDYGQVKELPDHLRLG 296
Cdd:pfam03109 156 IDDL-DALSEAGIDRK---------EIARRLVELFLEQIFRDGFFHADPHPGNILVRKDGRIVLLDFGLMGRLDEKFRRL 225
                         250
                  ....*....|....*....
gi 42567114   297 YANLVIAIADNNASLALQS 315
Cdd:pfam03109 226 YAELLLALVNRDYKRVAEM 244
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
30-320 1.17e-61

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: 205.99  E-value: 1.17e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114    30 SDLGGFFLKIAQILG-KPDLAPAAWVRKLVTLCDQAPATPFDAVRVVLEKELGKSIEQVFETFDEKPLGSASIAQVHRAR 108
Cdd:TIGR01982  58 EELGPTFIKFGQTLStRADLLPADIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEEKPLAAASIAQVHRAR 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114   109 VKGDKRdVVVKVQHPGVEKLMMVDIRNLQIFALYMQKTD---IKFDLFSMTKEIEKQIGYEFDFKREANAMEKIRRflyd 185
Cdd:TIGR01982 138 LVDGKE-VAVKVLRPGIEKTIAADIALLYRLARIVERLSpdsRRLRPTEVVKEFEKTLRRELDLRREAANASELGE---- 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114   186 NNRKSP-VLVPRVFPNLVTRKVLVMEFMNGIPIlslgDEMAK---RGINPHgKMAEAakfnilhsLSQAYGQMILKSGFF 261
Cdd:TIGR01982 213 NFKNDPgVYVPEVYWDRTSERVLTMEWIDGIPL----SDIAAldeAGLDRK-ALAEN--------LARSFLNQVLRDGFF 279
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 42567114   262 HADPHPGNILIGKGSEVALLDYGQVKELPDHLRLGYANLVIAIADNNASLALQSFRELG 320
Cdd:TIGR01982 280 HADLHPGNIFVLKDGKIIALDFGIVGRLSEEDRRYLAEILYGFLNRDYRRVAEVHFDAG 338
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
31-272 4.85e-41

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 153.14  E-value: 4.85e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114   31 DLGGFFLKIAQILG-KPDLAPAAWVRKLVTLCDQAPATPFDAVRVVLEKELGKSIEQVFETFDEKPLGSASIAQVHRARV 109
Cdd:PRK04750  61 ELGPIFVKFGQMLStRRDLFPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQVHFARL 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114  110 KGDKRDVVVKVQHPGVEKLMMVDIRNLQIFALYMQKtdikfdLFSMTK---------EIEKQIGYEFDFKRE-ANAMEkI 179
Cdd:PRK04750 141 KDNGREVVVKVLRPDILPVIDADLALMYRLARWVER------LLPDGRrlkprevvaEFEKTLHDELDLMREaANASQ-L 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114  180 RRFLYDnnrKSPVLVPRVFPNLVTRKVLVMEFMNGIPIlSLGDEMAKRGINPHgKMAEAAkFNILhslsqaYGQmILKSG 259
Cdd:PRK04750 214 RRNFED---SDMLYVPEVYWDYCSETVMVMERMYGIPV-SDVAALRAAGTDMK-LLAERG-VEVF------FTQ-VFRDG 280
                        250
                 ....*....|...
gi 42567114  260 FFHADPHPGNILI 272
Cdd:PRK04750 281 FFHADMHPGNIFV 293
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
94-295 6.70e-04

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 41.36  E-value: 6.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114     94 KPLGSASIAQVHRARVKGDKRDVVVKVQHpgveklmmvdirnlqifalymqktdikfdlfsmtkeIEKQIGYEFDFKREA 173
Cdd:smart00220   5 EKLGEGSFGKVYLARDKKTGKLVAIKVIK------------------------------------KKKIKKDRERILREI 48
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114    174 NAMEKIrrflydnnrKSPVLVpRVFPNLVTRK--VLVMEFMNGIPILSLgdemakrgINPHGKMAEA-AKF--------- 241
Cdd:smart00220  49 KILKKL---------KHPNIV-RLYDVFEDEDklYLVMEYCEGGDLFDL--------LKKRGRLSEDeARFylrqilsal 110
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 42567114    242 NILHSLsqaygqmilksGFFHADPHPGNILIGKGSEVALLDYGQVKELPDHLRL 295
Cdd:smart00220 111 EYLHSK-----------GIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKL 153
 
Name Accession Description Interval E-value
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
60-316 1.47e-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: 292.48  E-value: 1.47e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114  60 LCDQAPATPFDAVRVVLEKELGKSIEQVFETFDEKPLGSASIAQVHRARVKgDKRDVVVKVQHPGVEKLMMVDIRNLQIF 139
Cdd:cd05121   2 LQDDVPPFPFEEVRKIIEEELGRPLEEVFAEFDPEPLAAASIAQVHRARLK-DGREVAVKVQRPGIEEIIEADLRILRRL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 140 ALYMQK---TDIKFDLFSMTKEIEKQIGYEFDFKREANAMEKIRRFLYDNNRkspVLVPRVFPNLVTRKVLVMEFMNGIP 216
Cdd:cd05121  81 ARLLERlspLLRRLDLVAIVDEFARSLLEELDFRREARNAERFRKNLKDSPD---VYVPKVYPELSTRRVLVMEYIDGVK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 217 ILSLgDEMAKRGINPHgkmaeaakfNILHSLSQAYGQMILKSGFFHADPHPGNILIGKGSEVALLDYGQVKELPDHLRLG 296
Cdd:cd05121 158 LTDL-EALRAAGIDRK---------ELARRLVDAYLKQIFEDGFFHADPHPGNILVLPDGRIALLDFGMVGRLDPETREA 227
                       250       260
                ....*....|....*....|
gi 42567114 297 YANLVIAIADNNASLALQSF 316
Cdd:cd05121 228 LADLLLALVNGDAEGLAEAL 247
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
14-393 1.20e-94

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: 293.26  E-value: 1.20e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114  14 WERQHELAAHKVYSMCSDLGGFFLKIAQILG-KPDLAPAAWVRKLVTLCDQAPATPFDAVRVVLEKELGKSIEQVFETFD 92
Cdd:COG0661  44 REELRRRRAERLRLALEELGPTFIKLGQLLStRPDLLPPEYAEELAKLQDRVPPFPFEEVRAVIEEELGRPLEELFAEFD 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114  93 EKPLGSASIAQVHRARVKgDKRDVVVKVQHPGVEKLMMVDIRNLQIFALYMQKTD---IKFDLFSMTKEIEKQIGYEFDF 169
Cdd:COG0661 124 PEPLAAASIGQVHRARLK-DGREVAVKVQRPGIEEAIEADLRILRRLARLLERLSpegRRLDPVEVVDEFARSLLEELDY 202
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 170 KREANAMEKIRRFLYDNNRkspVLVPRVFPNLVTRKVLVMEFMNGIPILSLgDEMAKRGINPHgKMAEAakfnilhsLSQ 249
Cdd:COG0661 203 RREAANAERFRRNFADDPD---VYVPKVYWELSTRRVLTMEWIDGIKISDL-EALDAAGIDRK-RLAER--------LVR 269
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 250 AYGQMILKSGFFHADPHPGNILIGKGSEVALLDYGQVKELPDHLRLGYANLVIAIADNNASLALQSFRELGIATVakcKN 329
Cdd:COG0661 270 AFLRQVFRDGFFHADPHPGNIFVLPDGRLVLLDFGMVGRLDPETREGLAELLLALLNRDYDRVAEALLELGFVPP---DT 346
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42567114 330 EQQELLQLAKTMFDtemppgtttlqPFSEDsSIKKISVEAFPEELFSVLR---------TVVLLRGLSVGIGI 393
Cdd:COG0661 347 DVDELERALRAVLE-----------PYFGK-PLKDISFGELLLELFELARrfplrlppeLVLLQRTLLTLEGV 407
ADCK1-like cd13969
aarF domain containing kinase 1 and similar proteins; This subfamily is composed of ...
59-320 1.11e-78

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: 244.32  E-value: 1.11e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114  59 TLCDQAPATPFDAVRVVLEKELGKSIEQVFETFDEKPLGSASIAQVHRARVKgDKRDVVVKVQHPGVEKLMMVDIRNLQI 138
Cdd:cd13969   1 VLQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVHKAKLK-DGEEVAVKVQHPDLRKQFAGDLATMEF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 139 FALYMQKTDIKFDLFSMTKEIEKQIGYEFDFKREANAMEKIRRFLYDNNRkspVLVPRVFPNLVTRKVLVMEFMNGIPIL 218
Cdd:cd13969  80 LVNLVEKLFPDFPFSWLVDELKKNLPKELDFLNEARNAERCAKLFKHRPD---VYVPKVYWDLSSKRVLTMEFIDGIKID 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 219 SLgDEMAKRGINPHGkmaeaakfnILHSLSQAYGQMILKSGFFHADPHPGNILI----GKGS-EVALLDYGQVKELPDHL 293
Cdd:cd13969 157 DV-EALKKLGIDPKE---------VARLLSEAFAEMIFVHGFVHCDPHPGNLLVrknpGPGKpQIVLLDHGLYRELDEEF 226
                       250       260
                ....*....|....*....|....*..
gi 42567114 294 RLGYANLVIAIADNNASLALQSFRELG 320
Cdd:cd13969 227 RLNYCRLWKALILGDEKKIKKYSKALG 253
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
62-315 3.33e-73

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: 229.81  E-value: 3.33e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114    62 DQAPATPFDAVRVVLEKELGKSIEQVFETFDEKPLGSASIAQVHRARVKgDKRDVVVKVQHPGVEKLMMVDIRNLQIFAl 141
Cdd:pfam03109   4 DRAPPFPFEQAKKVIEEELGAPVEEIFAEFDEEPIAAASIAQVHRARLK-DGEEVAVKVQRPGVKKRIRSDLLLLRFLA- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114   142 ymQKTDIKF-DLFSMT---KEIEKQIGYEFDFKREANAMEKIRrflyDNNRKSP-VLVPRVFPNLVTRKVLVMEFMNGIP 216
Cdd:pfam03109  82 --KVAKRFFpGFRRLDwlvDEFRKSLPQELDFLREAANAEKFR----ENFADDPdVYVPKVYWELTTERVLTMEYVDGIK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114   217 ILSLgDEMAKRGINPHgkmaeaakfNILHSLSQAYGQMILKSGFFHADPHPGNILIGKGSEVALLDYGQVKELPDHLRLG 296
Cdd:pfam03109 156 IDDL-DALSEAGIDRK---------EIARRLVELFLEQIFRDGFFHADPHPGNILVRKDGRIVLLDFGLMGRLDEKFRRL 225
                         250
                  ....*....|....*....
gi 42567114   297 YANLVIAIADNNASLALQS 315
Cdd:pfam03109 226 YAELLLALVNRDYKRVAEM 244
ABC1_ADCK3 cd13970
Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This ...
56-320 1.41e-64

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: 207.75  E-value: 1.41e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114  56 KLVTLCDQAPATPFDAVRVVLEKELGKSIEQVFETFDEKPLGSASIAQVHRARVKgDKRDVVVKVQHPGVEKLMMVDIRN 135
Cdd:cd13970   2 ALARLRDSAPPMPWAQLEKVLEAELGEDWRELFAEFDEEPFAAASIGQVHRATLK-DGREVAVKVQYPGVAESIDSDLNN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 136 LQIFALYMQKTDIKFDLFSMTKEIEKQIGYEFDFKREANAMEKIRRFLYDNNRkspVLVPRVFPNLVTRKVLVMEFMNGI 215
Cdd:cd13970  81 LRRLLKLTGLLPKGLDLDALIAELREELLEECDYEREAANQRRFRELLADDPR---FVVPEVIPELSTKRVLTTEFVDGV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 216 PIlslgDEMAkrginphgKMAEAAKFNILHSLSQAYGQMILKSGFFHADPHPGNILIGKGS-EVALLDYGQVKELPDHLR 294
Cdd:cd13970 158 PL----DEAA--------DLSQEERNRIGELLLRLCLRELFEFGFMQTDPNPGNFLYDPEDgRLGLLDFGAVREYPPEFV 225
                       250       260
                ....*....|....*....|....*.
gi 42567114 295 LGYANLVIAIADNNASLALQSFRELG 320
Cdd:cd13970 226 DGYRRLVRAALEGDREALLEASVELG 251
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
30-320 1.17e-61

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: 205.99  E-value: 1.17e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114    30 SDLGGFFLKIAQILG-KPDLAPAAWVRKLVTLCDQAPATPFDAVRVVLEKELGKSIEQVFETFDEKPLGSASIAQVHRAR 108
Cdd:TIGR01982  58 EELGPTFIKFGQTLStRADLLPADIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEEKPLAAASIAQVHRAR 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114   109 VKGDKRdVVVKVQHPGVEKLMMVDIRNLQIFALYMQKTD---IKFDLFSMTKEIEKQIGYEFDFKREANAMEKIRRflyd 185
Cdd:TIGR01982 138 LVDGKE-VAVKVLRPGIEKTIAADIALLYRLARIVERLSpdsRRLRPTEVVKEFEKTLRRELDLRREAANASELGE---- 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114   186 NNRKSP-VLVPRVFPNLVTRKVLVMEFMNGIPIlslgDEMAK---RGINPHgKMAEAakfnilhsLSQAYGQMILKSGFF 261
Cdd:TIGR01982 213 NFKNDPgVYVPEVYWDRTSERVLTMEWIDGIPL----SDIAAldeAGLDRK-ALAEN--------LARSFLNQVLRDGFF 279
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 42567114   262 HADPHPGNILIGKGSEVALLDYGQVKELPDHLRLGYANLVIAIADNNASLALQSFRELG 320
Cdd:TIGR01982 280 HADLHPGNIFVLKDGKIIALDFGIVGRLSEEDRRYLAEILYGFLNRDYRRVAEVHFDAG 338
UbiB cd13972
Ubiquinone biosynthetic protein UbiB; UbiB is the prokaryotic homolog of yeast Abc1p and human ...
60-304 2.51e-47

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: 162.76  E-value: 2.51e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114  60 LCDQAPATPFDAVRVVLEKELGKSIEQVFETFDEKPLGSASIAQVHRARVKgDKRDVVVKVQHPGVEKLMMVDIRNL--- 136
Cdd:cd13972   2 LQDRVPPFSGKEARAIIEAELGKPLDALFSDFDEEPVAAASIAQVHKARLL-DGREVAVKVLRPGIEKRIERDLELLrfl 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 137 -QIFALYMQKTDiKFDLFSMTKEIEKQIGYEFDFKREANAMEKIRRFLYDNNRkspVLVPRVFPNLVTRKVLVMEFMNGI 215
Cdd:cd13972  81 aRLAERLLPEAR-RLRPVEVVKEFARSLLLELDLRLEAANASELRENFLDDPG---FYVPEVYWELTSKNVLTMEWIDGI 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 216 PILSLgDEMAKRGINPhgkMAEAAKFnILHSLSQAYGQmilksGFFHADPHPGNILIGKGSEVALLDYGQVKELPDHLRL 295
Cdd:cd13972 157 PISDI-EALDAAGIDR---KALAERL-VEIFFRQVFRD-----GFFHADMHPGNIFVDPNGRIIAVDFGIMGRLDKKDRR 226

                ....*....
gi 42567114 296 GYANLVIAI 304
Cdd:cd13972 227 YLAEILYGF 235
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
31-272 4.85e-41

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 153.14  E-value: 4.85e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114   31 DLGGFFLKIAQILG-KPDLAPAAWVRKLVTLCDQAPATPFDAVRVVLEKELGKSIEQVFETFDEKPLGSASIAQVHRARV 109
Cdd:PRK04750  61 ELGPIFVKFGQMLStRRDLFPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQVHFARL 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114  110 KGDKRDVVVKVQHPGVEKLMMVDIRNLQIFALYMQKtdikfdLFSMTK---------EIEKQIGYEFDFKRE-ANAMEkI 179
Cdd:PRK04750 141 KDNGREVVVKVLRPDILPVIDADLALMYRLARWVER------LLPDGRrlkprevvaEFEKTLHDELDLMREaANASQ-L 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114  180 RRFLYDnnrKSPVLVPRVFPNLVTRKVLVMEFMNGIPIlSLGDEMAKRGINPHgKMAEAAkFNILhslsqaYGQmILKSG 259
Cdd:PRK04750 214 RRNFED---SDMLYVPEVYWDYCSETVMVMERMYGIPV-SDVAALRAAGTDMK-LLAERG-VEVF------FTQ-VFRDG 280
                        250
                 ....*....|...
gi 42567114  260 FFHADPHPGNILI 272
Cdd:PRK04750 281 FFHADMHPGNIFV 293
ADCK2-like cd13971
aarF domain containing kinase 2 and similar proteins; This subfamily is composed of ...
59-295 1.27e-39

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: 143.90  E-value: 1.27e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114  59 TLCDQAPATPFDAVRVVLEKELGKSIEQVFETFDEKPLGSASIAQVHRARVKGDK-------RDVVVKVQHPGVEKLMMV 131
Cdd:cd13971   1 KLHSNAPPHSWAHTERALEAAFGKDWEDIFEEFDEEPIGSGSIAQVHRAKLKPDYggdgggpRVVAVKVLHPGVREQIER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 132 DIRNLQIFA---------LYMQKTDIKfDLFS--MTKEIekqigyefDFKREANAMEkirRFLYDNNRKSPVLVPRVFPN 200
Cdd:cd13971  81 DLAILRLFAklleaipplRWLSLPESV-EQFAslMLRQL--------DLRVEAANLE---RFRENFKDRKDVSFPKPLYP 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 201 LVTRKVLVMEFMNGIPILSLGDEMakrginphgkMAEAAKFNILHSLSQAYGQMILKSGFFHADPHPGNILIGKGSEVAL 280
Cdd:cd13971 149 LVTEEVLVETFEEGVPISRTVLAH----------GGEPLKRKLARIGLDAFLKMLFVDNFVHGDLHPGNILVRFNDSNRP 218
                       250
                ....*....|....*
gi 42567114 281 LDYGQVKELPDHLRL 295
Cdd:cd13971 219 SLLVSLDARGSPPRL 233
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
96-292 9.54e-09

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 55.35  E-value: 9.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114  96 LGSASIAQVHRARVKGDKRDVVVKVqhpgveklmmvdirnlqifalymqktdIKFDLFSMTKEiekqigyefDFKREANA 175
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAVKV---------------------------IPKEKLKKLLE---------ELLREIEI 44
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 176 MEKIRRflydnnrkspvlvprvfPNLVT---------RKVLVMEFMNGIpilSLGDEMAKRGinphGKMAEAAKFNILHS 246
Cdd:cd00180  45 LKKLNH-----------------PNIVKlydvfetenFLYLVMEYCEGG---SLKDLLKENK----GPLSEEEALSILRQ 100
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 42567114 247 LSQAYgQMILKSGFFHADPHPGNILIGKGSEVALLDYGQVKELPDH 292
Cdd:cd00180 101 LLSAL-EYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSD 145
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
93-291 2.49e-08

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 55.79  E-value: 2.49e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114  93 EKPLGSASIAQVHRARVKGDKRDVVVKVQHPGveklmmvdirnlqifalymqktdikfdlFSMTKEIEKQigyefdFKRE 172
Cdd:COG0515  12 LRLLGRGGMGVVYLARDLRLGRPVALKVLRPE----------------------------LAADPEARER------FRRE 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 173 ANAMEKIRRflydnnrkspvlvprvfPNLVT---------RKVLVMEFMNGIpilSLGDEMAKRGINPhgkMAEAAKF-- 241
Cdd:COG0515  58 ARALARLNH-----------------PNIVRvydvgeedgRPYLVMEYVEGE---SLADLLRRRGPLP---PAEALRIla 114
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 42567114 242 NILHSLSQAYGQmilksGFFHADPHPGNILIGKGSEVALLDYGQVKELPD 291
Cdd:COG0515 115 QLAEALAAAHAA-----GIVHRDIKPANILLTPDGRVKLIDFGIARALGG 159
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
93-291 2.06e-07

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 51.82  E-value: 2.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114  93 EKPLGSASIAQVHRARVKGDKRDVVVKVQHPGveklmmvdirnlqifalymqktdikfdlFSMTKEIEKQigyefdFKRE 172
Cdd:cd14014   5 VRLLGRGGMGEVYRARDTLLGRPVAIKVLRPE----------------------------LAEDEEFRER------FLRE 50
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 173 ANAMEKIRrflydnnrkSPvLVPRVFPNLVTRKV--LVMEFMNGIpilSLGDEMAKRGINPHGKMAEAAKfNILHSLSQA 250
Cdd:cd14014  51 ARALARLS---------HP-NIVRVYDVGEDDGRpyIVMEYVEGG---SLADLLRERGPLPPREALRILA-QIADALAAA 116
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 42567114 251 YGQmilksGFFHADPHPGNILIGKGSEVALLDYGQVKELPD 291
Cdd:cd14014 117 HRA-----GIVHRDIKPANILLTEDGRVKLTDFGIARALGD 152
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
170-285 8.54e-05

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


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 42.64  E-value: 8.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 170 KREANAMEKIRRFlydnnrksPVLVPRVFPNLVTRKVLVMEFMNGIPilsLGDEMAKRGINPhgkmaeaakfnilhSLSQ 249
Cdd:COG3642   4 RREARLLRELREA--------GVPVPKVLDVDPDDADLVMEYIEGET---LADLLEEGELPP--------------ELLR 58
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 42567114 250 AYGQMILK---SGFFHADPHPGNILIGKGsEVALLDYGQ 285
Cdd:COG3642  59 ELGRLLARlhrAGIVHGDLTTSNILVDDG-GVYLIDFGL 96
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
168-284 2.44e-04

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


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 41.52  E-value: 2.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 168 DFKREANAMekirRFLydnNRKSPVLVPRVFP--NLVTRKVLVMEFMNGIpilSLGDEmakrginpHGKMAEAAKFNILH 245
Cdd:cd05120  35 DLEKEAAML----QLL---AGKLSLPVPKVYGfgESDGWEYLLMERIEGE---TLSEV--------WPRLSEEEKEKIAD 96
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 42567114 246 SLSQAYGQM--ILKSGFFHADPHPGNILIGKGSEV-ALLDYG 284
Cdd:cd05120  97 QLAEILAALhrIDSSVLTHGDLHPGNILVKPDGKLsGIIDWE 138
RIO1_like cd05145
Catalytic domain of the atypical protein serine kinases, RIO1 and RIO3 kinases and similar ...
192-292 4.72e-04

Catalytic domain of the atypical protein serine kinases, RIO1 and RIO3 kinases and similar proteins; RIO1 is present in archaea, bacteria and eukaryotes. In addition, RIO3 is present in multicellular eukaryotes. Both RIO1 and RIO3 are associated with precursors of 40S ribosomal subunits, just like RIO2. RIO1 is essential for survival and is required for 18S rRNA processing, proper cell cycle progression and chromosome maintenance. Although depletion of either RIO1 and RIO2 results in similar effects, the two kinases are not fully interchangeable. The specific function of RIO3 is unknown. 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 RIO 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: 270696 [Multi-domain]  Cd Length: 189  Bit Score: 41.00  E-value: 4.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 192 VLVPRvfPNLVTRKVLVMEFM--NGIPILSLGDemakrgINPHGKMAEAAKFNILHSLSQAYgqmiLKSGFFHADPHPGN 269
Cdd:cd05145  80 VRVPE--PIAVYRNVLVMEFIgdDGSPAPRLKD------VELEEEDAEELYEQVVEQMRRMY----CKAGLVHGDLSEYN 147
                        90       100
                ....*....|....*....|...
gi 42567114 270 ILIGKGsEVALLDYGQVKELpDH 292
Cdd:cd05145 148 ILYYDG-KPVIIDVSQAVTL-DH 168
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
94-295 6.70e-04

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 41.36  E-value: 6.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114     94 KPLGSASIAQVHRARVKGDKRDVVVKVQHpgveklmmvdirnlqifalymqktdikfdlfsmtkeIEKQIGYEFDFKREA 173
Cdd:smart00220   5 EKLGEGSFGKVYLARDKKTGKLVAIKVIK------------------------------------KKKIKKDRERILREI 48
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114    174 NAMEKIrrflydnnrKSPVLVpRVFPNLVTRK--VLVMEFMNGIPILSLgdemakrgINPHGKMAEA-AKF--------- 241
Cdd:smart00220  49 KILKKL---------KHPNIV-RLYDVFEDEDklYLVMEYCEGGDLFDL--------LKKRGRLSEDeARFylrqilsal 110
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 42567114    242 NILHSLsqaygqmilksGFFHADPHPGNILIGKGSEVALLDYGQVKELPDHLRL 295
Cdd:smart00220 111 EYLHSK-----------GIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKL 153
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
207-289 7.00e-04

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 41.37  E-value: 7.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 207 LVMEFMNGipilSLGDEMAKRGINPhgkMAEAAKFNILHSLSQAYgQMILKSGFFHADPHPGNILIGKGSEVALLDYGQV 286
Cdd:cd07830  75 FVFEYMEG----NLYQLMKDRKGKP---FSESVIRSIIYQILQGL-AHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLA 146

                ...
gi 42567114 287 KEL 289
Cdd:cd07830 147 REI 149
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
170-284 1.27e-03

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


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 39.89  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114   170 KREANAMEKIRRF------LYDnnrkspvlvprVFPNlvtRKVLVMEFMNGIPilsLGDEMAKRGINPHGKMAEAAkfNI 243
Cdd:TIGR03724  45 RREARLLSRARKAgvntpvIYD-----------VDPD---NKTIVMEYIEGKP---LKDVIEENGDELAREIGRLV--GK 105
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 42567114   244 LHSLsqaygqmilksGFFHADPHPGNILIGkGSEVALLDYG 284
Cdd:TIGR03724 106 LHKA-----------GIVHGDLTTSNIIVR-DDKVYLIDFG 134
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
207-284 2.16e-03

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 39.65  E-value: 2.16e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42567114 207 LVMEFMNGipiLSLGDEMakRGINPHGKMAEAAKFNILHSLSQAYgQMILKSGFFHADPHPGNILIGKGSEVALLDYG 284
Cdd:cd06610  76 LVMPLLSG---GSLLDIM--KSSYPRGGLDEAIIATVLKEVLKGL-EYLHSNGQIHRDVKAGNILLGEDGSVKIADFG 147
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
170-282 2.21e-03

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


Pssm-ID: 440246 [Multi-domain]  Cd Length: 183  Bit Score: 39.12  E-value: 2.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 170 KREANAMEKirrfLYDNNrkspVLVPRvfPNLVTRKVLVMEFMNGIpilslgdEMAKRGINPHGKMAEAakfnILHSLSQ 249
Cdd:COG0478  47 EREFRALER----LYPAG----LPVPR--PIAANRHAIVMERIEGV-------ELARLKLEDPEEVLDK----ILEEIRR 105
                        90       100       110
                ....*....|....*....|....*....|...
gi 42567114 250 AYgqmilKSGFFHADPHPGNILIGKGSEVALLD 282
Cdd:COG0478 106 AH-----DAGIVHADLSEYNILVDDDGGVWIID 133
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
207-318 3.59e-03

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 39.19  E-value: 3.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 207 LVMEFMNGIPILSLgdeMAKRGINPhgkmAEAAKFNI------LHSLSQAygqmilksGFFHADPHPGNILIGKGSEVAL 280
Cdd:cd05573  78 LVMEYMPGGDLMNL---LIKYDVFP----EETARFYIaelvlaLDSLHKL--------GFIHRDIKPDNILLDADGHIKL 142
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 42567114 281 LDYGQVKELPD-HLRLGYANLVIAIADNNASLALQSFRE 318
Cdd:cd05573 143 ADFGLCTKMNKsGDRESYLNDSVNTLFQDNVLARRRPHK 181
PRK14879 PRK14879
Kae1-associated kinase Bud32;
170-284 5.00e-03

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 38.35  E-value: 5.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114  170 KREANAMEKIRRFlydnnrksPVLVPRVFPNLVTRKVLVMEFMNGIPILSLGDEMAKRGINPHGKMAEAAkfNILHSLsq 249
Cdd:PRK14879  47 RREARIMSRARKA--------GVNVPAVYFVDPENFIIVMEYIEGEPLKDLINSNGMEELELSREIGRLV--GKLHSA-- 114
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 42567114  250 aygqmilksGFFHADPHPGNILIgKGSEVALLDYG 284
Cdd:PRK14879 115 ---------GIIHGDLTTSNMIL-SGGKIYLIDFG 139
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
209-289 6.12e-03

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 38.56  E-value: 6.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567114 209 MEFMNGIPILSLGDEMAKRG--INPH--GKMAEaakfNILHSLSQAYGQMILksgffHADPHPGNILIGKGSEVALLDYG 284
Cdd:cd06621  80 MEYCEGGSLDSIYKKVKKKGgrIGEKvlGKIAE----SVLKGLSYLHSRKII-----HRDIKPSNILLTRKGQVKLCDFG 150

                ....*
gi 42567114 285 QVKEL 289
Cdd:cd06621 151 VSGEL 155
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
261-286 8.84e-03

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


Pssm-ID: 270704 [Multi-domain]  Cd Length: 234  Bit Score: 37.60  E-value: 8.84e-03
                        10        20
                ....*....|....*....|....*.
gi 42567114 261 FHADPHPGNILIGKGSEVALLDYGQV 286
Cdd:cd05155 166 LHGDLHPGNLLVRDGRLSAVIDFGDL 191
 
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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