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Conserved domains on  [gi|17559152|ref|NP_505980|]
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ABC1 atypical kinase-like domain-containing protein [Caenorhabditis elegans]

Protein Classification

ABC1 kinase family protein( domain architecture ID 10195500)

ABC1 (activator of bc1 complex) kinase family protein is an atypical protein kinase, similar to Saccharomyces cerevisiae ABC1 family protein MCP2 and to vertebrate AarF domain-containing protein kinase 1 (ADCK1), which appears to be essential for maintaining mitochondrial cristae formation and mitochondrial function

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ADCK1-like cd13969
aarF domain containing kinase 1 and similar proteins; This subfamily is composed of ...
123-375 2.52e-130

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: 378.75  E-value: 2.52e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 123 ILTSQAPQASKEDVIYVVESELNAKVGDLFSEFSEKPVGAASLAQVHKAKLKEsGETVAVKVQHKRVYKNSRTDVNTMEF 202
Cdd:cd13969   1 VLQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVHKAKLKD-GEEVAVKVQHPDLRKQFAGDLATMEF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 203 LVKVADAVFPEFRLMWLVDEIKKNLPNELDFLHEAKNADEAAQRFKHLKFLRIPKIKYDLTTTRVLTMEFCEGAHVDDVE 282
Cdd:cd13969  80 LVNLVEKLFPDFPFSWLVDELKKNLPKELDFLNEARNAERCAKLFKHRPDVYVPKVYWDLSSKRVLTMEFIDGIKIDDVE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 283 YLKKNNIDPHDVCMKIGKTISEMIFLQGYLHSDPHPGNVLINSL-GNGKYEIVLLDHGLYLNISDHIRKLYSDLWLAILK 361
Cdd:cd13969 160 ALKKLGIDPKEVARLLSEAFAEMIFVHGFVHCDPHPGNLLVRKNpGPGKPQIVLLDHGLYRELDEEFRLNYCRLWKALIL 239
                       250
                ....*....|....
gi 17559152 362 PDLQEIRKVASQMG 375
Cdd:cd13969 240 GDEKKIKKYSKALG 253
 
Name Accession Description Interval E-value
ADCK1-like cd13969
aarF domain containing kinase 1 and similar proteins; This subfamily is composed of ...
123-375 2.52e-130

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: 378.75  E-value: 2.52e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 123 ILTSQAPQASKEDVIYVVESELNAKVGDLFSEFSEKPVGAASLAQVHKAKLKEsGETVAVKVQHKRVYKNSRTDVNTMEF 202
Cdd:cd13969   1 VLQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVHKAKLKD-GEEVAVKVQHPDLRKQFAGDLATMEF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 203 LVKVADAVFPEFRLMWLVDEIKKNLPNELDFLHEAKNADEAAQRFKHLKFLRIPKIKYDLTTTRVLTMEFCEGAHVDDVE 282
Cdd:cd13969  80 LVNLVEKLFPDFPFSWLVDELKKNLPKELDFLNEARNAERCAKLFKHRPDVYVPKVYWDLSSKRVLTMEFIDGIKIDDVE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 283 YLKKNNIDPHDVCMKIGKTISEMIFLQGYLHSDPHPGNVLINSL-GNGKYEIVLLDHGLYLNISDHIRKLYSDLWLAILK 361
Cdd:cd13969 160 ALKKLGIDPKEVARLLSEAFAEMIFVHGFVHCDPHPGNLLVRKNpGPGKPQIVLLDHGLYRELDEEFRLNYCRLWKALIL 239
                       250
                ....*....|....
gi 17559152 362 PDLQEIRKVASQMG 375
Cdd:cd13969 240 GDEKKIKKYSKALG 253
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
124-371 4.12e-109

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: 324.57  E-value: 4.12e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152   124 LTSQAPQASKEDVIYVVESELNAKVGDLFSEFSEKPVGAASLAQVHKAKLKeSGETVAVKVQHKRVYKNSRTDVNTMEFL 203
Cdd:pfam03109   2 LQDRAPPFPFEQAKKVIEEELGAPVEEIFAEFDEEPIAAASIAQVHRARLK-DGEEVAVKVQRPGVKKRIRSDLLLLRFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152   204 VKVADAVFPEFR-LMWLVDEIKKNLPNELDFLHEAKNADEAAQRFKHLKFLRIPKIKYDLTTTRVLTMEFCEGAHVDDVE 282
Cdd:pfam03109  81 AKVAKRFFPGFRrLDWLVDEFRKSLPQELDFLREAANAEKFRENFADDPDVYVPKVYWELTTERVLTMEYVDGIKIDDLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152   283 YLKKNNIDPHDVCMKIGKTISEMIFLQGYLHSDPHPGNVLINSLGngkyEIVLLDHGLYLNISDHIRKLYSDLWLAILKP 362
Cdd:pfam03109 161 ALSEAGIDRKEIARRLVELFLEQIFRDGFFHADPHPGNILVRKDG----RIVLLDFGLMGRLDEKFRRLYAELLLALVNR 236

                  ....*....
gi 17559152   363 DLQEIRKVA 371
Cdd:pfam03109 237 DYKRVAEML 245
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
42-375 1.28e-77

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: 251.66  E-value: 1.28e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152  42 LLRFGRAASTVGKIVIDYKTSLRGLPEPSSEY--DDAIKKCHQRSAEH----LLELacvnGGVFIKVGQHISGMEYLIPP 115
Cdd:COG0661   7 LRRLARIARVLLRYGLGELLDRLGLPRLRRLLtgEERREELRRRRAERlrlaLEEL----GPTFIKLGQLLSTRPDLLPP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 116 EYTQTLSILTSQAPQASKEDVIYVVESELNAKVGDLFSEFSEKPVGAASLAQVHKAKLKeSGETVAVKVQHKRVYKNSRT 195
Cdd:COG0661  83 EYAEELAKLQDRVPPFPFEEVRAVIEEELGRPLEELFAEFDPEPLAAASIGQVHRARLK-DGREVAVKVQRPGIEEAIEA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 196 DVNTMEFLVKVADAVFPE---FRLMWLVDEIKKNLPNELDFLHEAKNADEAAQRFKHLKFLRIPKIKYDLTTTRVLTMEF 272
Cdd:COG0661 162 DLRILRRLARLLERLSPEgrrLDPVEVVDEFARSLLEELDYRREAANAERFRRNFADDPDVYVPKVYWELSTRRVLTMEW 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 273 CEGAHVDDVEYLKKNNIDPHDVCMKIGKTISEMIFLQGYLHSDPHPGNVLInsLGNGKyeIVLLDHGLYLNISDHIRKLY 352
Cdd:COG0661 242 IDGIKISDLEALDAAGIDRKRLAERLVRAFLRQVFRDGFFHADPHPGNIFV--LPDGR--LVLLDFGMVGRLDPETREGL 317
                       330       340
                ....*....|....*....|...
gi 17559152 353 SDLWLAILKPDLQEIRKVASQMG 375
Cdd:COG0661 318 AELLLALLNRDYDRVAEALLELG 340
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
79-375 9.69e-62

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: 208.69  E-value: 9.69e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152    79 KCHQRSAEHLLELACVN-GGVFIKVGQHISGMEYLIPPEYTQTLSILTSQAPQASKEDVIYVVESELNAKVGDLFSEFSE 157
Cdd:TIGR01982  43 ENRLMSRGERLRLALEElGPTFIKFGQTLSTRADLLPADIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEE 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152   158 KPVGAASLAQVHKAKLKEsGETVAVKVQHKRVYKNSRTDVNTMEFLVKVADAVFPEFRLM---WLVDEIKKNLPNELDFL 234
Cdd:TIGR01982 123 KPLAAASIAQVHRARLVD-GKEVAVKVLRPGIEKTIAADIALLYRLARIVERLSPDSRRLrptEVVKEFEKTLRRELDLR 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152   235 HEAKNADEAAQRFKHLKFLRIPKIKYDLTTTRVLTMEFCEGAHVDDVEYLKKNNIDPHdvcmKIGKTISEMIFLQ----G 310
Cdd:TIGR01982 202 REAANASELGENFKNDPGVYVPEVYWDRTSERVLTMEWIDGIPLSDIAALDEAGLDRK----ALAENLARSFLNQvlrdG 277
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17559152   311 YLHSDPHPGNVLINSLGNgkyeIVLLDHGLYLNISDHIRKLYSDLWLAILKPDLQEIRKVASQMG 375
Cdd:TIGR01982 278 FFHADLHPGNIFVLKDGK----IIALDFGIVGRLSEEDRRYLAEILYGFLNRDYRRVAEVHFDAG 338
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
96-339 6.50e-38

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 145.82  E-value: 6.50e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152   96 GGVFIKVGQHISGMEYLIPPEYTQTLSILTSQAPQASKEDVIYVVESELNAKVGDLFSEFSEKPVGAASLAQVHKAKLKE 175
Cdd:PRK04750  63 GPIFVKFGQMLSTRRDLFPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQVHFARLKD 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152  176 SGETVAVKVQHKRVYKNSRTDVNTMEFLVKVADAVFPEFR---LMWLVDEIKKNLPNELDFLHEAKNADEAAQRFKHLKF 252
Cdd:PRK04750 143 NGREVVVKVLRPDILPVIDADLALMYRLARWVERLLPDGRrlkPREVVAEFEKTLHDELDLMREAANASQLRRNFEDSDM 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152  253 LRIPKIKYDLTTTRVLTMEFCEGAHVDDVEYLKKNNIDPHdvcmKIGKTISEMIFLQ----GYLHSDPHPGNVLINSLG- 327
Cdd:PRK04750 223 LYVPEVYWDYCSETVMVMERMYGIPVSDVAALRAAGTDMK----LLAERGVEVFFTQvfrdGFFHADMHPGNIFVSYDPp 298
                        250
                 ....*....|...
gi 17559152  328 -NGKYeiVLLDHG 339
Cdd:PRK04750 299 eNPRY--IALDFG 309
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
158-340 7.38e-05

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 44.44  E-value: 7.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152    158 KPVGAASLAQVHKAKLKESGETVAVKVQHKRvyknsrtdvntmeflvkvadavfpefrlmwLVDEIKKNLPNELDFLhea 237
Cdd:smart00220   5 EKLGEGSFGKVYLARDKKTGKLVAIKVIKKK------------------------------KIKKDRERILREIKIL--- 51
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152    238 knadeaaQRFKH---LKFLRIpkikYDLTTTRVLTMEFCEGAHVDDveYLKKNNIDPHDVCMKIGKTISE-MIFL--QGY 311
Cdd:smart00220  52 -------KKLKHpniVRLYDV----FEDEDKLYLVMEYCEGGDLFD--LLKKRGRLSEDEARFYLRQILSaLEYLhsKGI 118
                          170       180
                   ....*....|....*....|....*....
gi 17559152    312 LHSDPHPGNVLINSLGNgkyeIVLLDHGL 340
Cdd:smart00220 119 VHRDLKPENILLDEDGH----VKLADFGL 143
 
Name Accession Description Interval E-value
ADCK1-like cd13969
aarF domain containing kinase 1 and similar proteins; This subfamily is composed of ...
123-375 2.52e-130

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: 378.75  E-value: 2.52e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 123 ILTSQAPQASKEDVIYVVESELNAKVGDLFSEFSEKPVGAASLAQVHKAKLKEsGETVAVKVQHKRVYKNSRTDVNTMEF 202
Cdd:cd13969   1 VLQDKAPQSPYEEVRRVFKEDLGKPPEELFSEFDEEPIASASLAQVHKAKLKD-GEEVAVKVQHPDLRKQFAGDLATMEF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 203 LVKVADAVFPEFRLMWLVDEIKKNLPNELDFLHEAKNADEAAQRFKHLKFLRIPKIKYDLTTTRVLTMEFCEGAHVDDVE 282
Cdd:cd13969  80 LVNLVEKLFPDFPFSWLVDELKKNLPKELDFLNEARNAERCAKLFKHRPDVYVPKVYWDLSSKRVLTMEFIDGIKIDDVE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 283 YLKKNNIDPHDVCMKIGKTISEMIFLQGYLHSDPHPGNVLINSL-GNGKYEIVLLDHGLYLNISDHIRKLYSDLWLAILK 361
Cdd:cd13969 160 ALKKLGIDPKEVARLLSEAFAEMIFVHGFVHCDPHPGNLLVRKNpGPGKPQIVLLDHGLYRELDEEFRLNYCRLWKALIL 239
                       250
                ....*....|....
gi 17559152 362 PDLQEIRKVASQMG 375
Cdd:cd13969 240 GDEKKIKKYSKALG 253
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
124-371 4.12e-109

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: 324.57  E-value: 4.12e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152   124 LTSQAPQASKEDVIYVVESELNAKVGDLFSEFSEKPVGAASLAQVHKAKLKeSGETVAVKVQHKRVYKNSRTDVNTMEFL 203
Cdd:pfam03109   2 LQDRAPPFPFEQAKKVIEEELGAPVEEIFAEFDEEPIAAASIAQVHRARLK-DGEEVAVKVQRPGVKKRIRSDLLLLRFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152   204 VKVADAVFPEFR-LMWLVDEIKKNLPNELDFLHEAKNADEAAQRFKHLKFLRIPKIKYDLTTTRVLTMEFCEGAHVDDVE 282
Cdd:pfam03109  81 AKVAKRFFPGFRrLDWLVDEFRKSLPQELDFLREAANAEKFRENFADDPDVYVPKVYWELTTERVLTMEYVDGIKIDDLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152   283 YLKKNNIDPHDVCMKIGKTISEMIFLQGYLHSDPHPGNVLINSLGngkyEIVLLDHGLYLNISDHIRKLYSDLWLAILKP 362
Cdd:pfam03109 161 ALSEAGIDRKEIARRLVELFLEQIFRDGFFHADPHPGNILVRKDG----RIVLLDFGLMGRLDEKFRRLYAELLLALVNR 236

                  ....*....
gi 17559152   363 DLQEIRKVA 371
Cdd:pfam03109 237 DYKRVAEML 245
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
42-375 1.28e-77

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: 251.66  E-value: 1.28e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152  42 LLRFGRAASTVGKIVIDYKTSLRGLPEPSSEY--DDAIKKCHQRSAEH----LLELacvnGGVFIKVGQHISGMEYLIPP 115
Cdd:COG0661   7 LRRLARIARVLLRYGLGELLDRLGLPRLRRLLtgEERREELRRRRAERlrlaLEEL----GPTFIKLGQLLSTRPDLLPP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 116 EYTQTLSILTSQAPQASKEDVIYVVESELNAKVGDLFSEFSEKPVGAASLAQVHKAKLKeSGETVAVKVQHKRVYKNSRT 195
Cdd:COG0661  83 EYAEELAKLQDRVPPFPFEEVRAVIEEELGRPLEELFAEFDPEPLAAASIGQVHRARLK-DGREVAVKVQRPGIEEAIEA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 196 DVNTMEFLVKVADAVFPE---FRLMWLVDEIKKNLPNELDFLHEAKNADEAAQRFKHLKFLRIPKIKYDLTTTRVLTMEF 272
Cdd:COG0661 162 DLRILRRLARLLERLSPEgrrLDPVEVVDEFARSLLEELDYRREAANAERFRRNFADDPDVYVPKVYWELSTRRVLTMEW 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 273 CEGAHVDDVEYLKKNNIDPHDVCMKIGKTISEMIFLQGYLHSDPHPGNVLInsLGNGKyeIVLLDHGLYLNISDHIRKLY 352
Cdd:COG0661 242 IDGIKISDLEALDAAGIDRKRLAERLVRAFLRQVFRDGFFHADPHPGNIFV--LPDGR--LVLLDFGMVGRLDPETREGL 317
                       330       340
                ....*....|....*....|...
gi 17559152 353 SDLWLAILKPDLQEIRKVASQMG 375
Cdd:COG0661 318 AELLLALLNRDYDRVAEALLELG 340
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
124-370 1.06e-76

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: 241.25  E-value: 1.06e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 124 LTSQAPQASKEDVIYVVESELNAKVGDLFSEFSEKPVGAASLAQVHKAKLKeSGETVAVKVQHKRVYKNSRTDVNTMEFL 203
Cdd:cd05121   2 LQDDVPPFPFEEVRKIIEEELGRPLEEVFAEFDPEPLAAASIAQVHRARLK-DGREVAVKVQRPGIEEIIEADLRILRRL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 204 VKVADAVFPEFR---LMWLVDEIKKNLPNELDFLHEAKNADEAAQRFKHLKFLRIPKIKYDLTTTRVLTMEFCEGAHVDD 280
Cdd:cd05121  81 ARLLERLSPLLRrldLVAIVDEFARSLLEELDFRREARNAERFRKNLKDSPDVYVPKVYPELSTRRVLVMEYIDGVKLTD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 281 VEYLKKNNIDPHDVCMKIGKTISEMIFLQGYLHSDPHPGNVLInsLGNGKyeIVLLDHGLYLNISDHIRKLYSDLWLAIL 360
Cdd:cd05121 161 LEALRAAGIDRKELARRLVDAYLKQIFEDGFFHADPHPGNILV--LPDGR--IALLDFGMVGRLDPETREALADLLLALV 236
                       250
                ....*....|
gi 17559152 361 KPDLQEIRKV 370
Cdd:cd05121 237 NGDAEGLAEA 246
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
79-375 9.69e-62

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: 208.69  E-value: 9.69e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152    79 KCHQRSAEHLLELACVN-GGVFIKVGQHISGMEYLIPPEYTQTLSILTSQAPQASKEDVIYVVESELNAKVGDLFSEFSE 157
Cdd:TIGR01982  43 ENRLMSRGERLRLALEElGPTFIKFGQTLSTRADLLPADIAEELSLLQDRVPPFDFKVARKVIEAALGGPLEELFAEFEE 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152   158 KPVGAASLAQVHKAKLKEsGETVAVKVQHKRVYKNSRTDVNTMEFLVKVADAVFPEFRLM---WLVDEIKKNLPNELDFL 234
Cdd:TIGR01982 123 KPLAAASIAQVHRARLVD-GKEVAVKVLRPGIEKTIAADIALLYRLARIVERLSPDSRRLrptEVVKEFEKTLRRELDLR 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152   235 HEAKNADEAAQRFKHLKFLRIPKIKYDLTTTRVLTMEFCEGAHVDDVEYLKKNNIDPHdvcmKIGKTISEMIFLQ----G 310
Cdd:TIGR01982 202 REAANASELGENFKNDPGVYVPEVYWDRTSERVLTMEWIDGIPLSDIAALDEAGLDRK----ALAENLARSFLNQvlrdG 277
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17559152   311 YLHSDPHPGNVLINSLGNgkyeIVLLDHGLYLNISDHIRKLYSDLWLAILKPDLQEIRKVASQMG 375
Cdd:TIGR01982 278 FFHADLHPGNIFVLKDGK----IIALDFGIVGRLSEEDRRYLAEILYGFLNRDYRRVAEVHFDAG 338
ABC1_ADCK3 cd13970
Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This ...
119-375 1.86e-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: 183.48  E-value: 1.86e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 119 QTLSILTSQAPQASKEDVIYVVESELNAKVGDLFSEFSEKPVGAASLAQVHKAKLKeSGETVAVKVQHKRVYKNSRTDVN 198
Cdd:cd13970   1 EALARLRDSAPPMPWAQLEKVLEAELGEDWRELFAEFDEEPFAAASIGQVHRATLK-DGREVAVKVQYPGVAESIDSDLN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 199 TMEFLVKVADAVFPEFRLMWLVDEIKKNLPNELDFLHEAKNADEAAQRFKHLKFLRIPKIKYDLTTTRVLTMEFCEGAHV 278
Cdd:cd13970  80 NLRRLLKLTGLLPKGLDLDALIAELREELLEECDYEREAANQRRFRELLADDPRFVVPEVIPELSTKRVLTTEFVDGVPL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 279 DDVEYLKKNNIDphdvcmKIGKTISEMIFLQ----GYLHSDPHPGNVLINSlGNGKyeIVLLDHGLYLNISDHIRKLYSD 354
Cdd:cd13970 160 DEAADLSQEERN------RIGELLLRLCLRElfefGFMQTDPNPGNFLYDP-EDGR--LGLLDFGAVREYPPEFVDGYRR 230
                       250       260
                ....*....|....*....|.
gi 17559152 355 LWLAILKPDLQEIRKVASQMG 375
Cdd:cd13970 231 LVRAALEGDREALLEASVELG 251
UbiB cd13972
Ubiquinone biosynthetic protein UbiB; UbiB is the prokaryotic homolog of yeast Abc1p and human ...
123-371 1.06e-49

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: 170.85  E-value: 1.06e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 123 ILTSQAPQASKEDVIYVVESELNAKVGDLFSEFSEKPVGAASLAQVHKAKLKEsGETVAVKVQHKRVYKNSRTDVNTMEF 202
Cdd:cd13972   1 KLQDRVPPFSGKEARAIIEAELGKPLDALFSDFDEEPVAAASIAQVHKARLLD-GREVAVKVLRPGIEKRIERDLELLRF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 203 LVKVADAVFPE---FRLMWLVDEIKKNLPNELDFLHEAKNADEAAQRFKHLKFLRIPKIKYDLTTTRVLTMEFCEGAHVD 279
Cdd:cd13972  80 LARLAERLLPEarrLRPVEVVKEFARSLLLELDLRLEAANASELRENFLDDPGFYVPEVYWELTSKNVLTMEWIDGIPIS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 280 DVEYLKKNNIDPhdvcmkigKTISE---MIFL-----QGYLHSDPHPGNVLINSLGNgkyeIVLLDHGLYLNISDHIRKL 351
Cdd:cd13972 160 DIEALDAAGIDR--------KALAErlvEIFFrqvfrDGFFHADMHPGNIFVDPNGR----IIAVDFGIMGRLDKKDRRY 227
                       250       260
                ....*....|....*....|
gi 17559152 352 YSDLWLAILKPDLqeiRKVA 371
Cdd:cd13972 228 LAEILYGFLTRDY---RRVA 244
ubiB PRK04750
putative ubiquinone biosynthesis protein UbiB; Reviewed
96-339 6.50e-38

putative ubiquinone biosynthesis protein UbiB; Reviewed


Pssm-ID: 235310 [Multi-domain]  Cd Length: 537  Bit Score: 145.82  E-value: 6.50e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152   96 GGVFIKVGQHISGMEYLIPPEYTQTLSILTSQAPQASKEDVIYVVESELNAKVGDLFSEFSEKPVGAASLAQVHKAKLKE 175
Cdd:PRK04750  63 GPIFVKFGQMLSTRRDLFPPDIADELALLQDRVPPFDGALARAIIEKALGGPVEEWFDDFDIKPLASASIAQVHFARLKD 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152  176 SGETVAVKVQHKRVYKNSRTDVNTMEFLVKVADAVFPEFR---LMWLVDEIKKNLPNELDFLHEAKNADEAAQRFKHLKF 252
Cdd:PRK04750 143 NGREVVVKVLRPDILPVIDADLALMYRLARWVERLLPDGRrlkPREVVAEFEKTLHDELDLMREAANASQLRRNFEDSDM 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152  253 LRIPKIKYDLTTTRVLTMEFCEGAHVDDVEYLKKNNIDPHdvcmKIGKTISEMIFLQ----GYLHSDPHPGNVLINSLG- 327
Cdd:PRK04750 223 LYVPEVYWDYCSETVMVMERMYGIPVSDVAALRAAGTDMK----LLAERGVEVFFTQvfrdGFFHADMHPGNIFVSYDPp 298
                        250
                 ....*....|...
gi 17559152  328 -NGKYeiVLLDHG 339
Cdd:PRK04750 299 eNPRY--IALDFG 309
ADCK2-like cd13971
aarF domain containing kinase 2 and similar proteins; This subfamily is composed of ...
123-363 3.73e-33

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


Pssm-ID: 270873 [Multi-domain]  Cd Length: 298  Bit Score: 127.72  E-value: 3.73e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 123 ILTSQAPQASKEDVIYVVESELNAKVGDLFSEFSEKPVGAASLAQVHKAKLKES-------GETVAVKVQHKRVYKNSRT 195
Cdd:cd13971   1 KLHSNAPPHSWAHTERALEAAFGKDWEDIFEEFDEEPIGSGSIAQVHRAKLKPDyggdgggPRVVAVKVLHPGVREQIER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 196 DVNTMEFLVKVADAVFPefrLMWL-----VDEIKKNLPNELDFLHEAKNADEAAQRFKHLKFLRIPKIKYDLTTTRVLTM 270
Cdd:cd13971  81 DLAILRLFAKLLEAIPP---LRWLslpesVEQFASLMLRQLDLRVEAANLERFRENFKDRKDVSFPKPLYPLVTEEVLVE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 271 EFCEGAHVDDVEylkkNNIDPHDVCMKIGKTISE----MIFLQGYLHSDPHPGNVLI-------------NSLGNGKYEI 333
Cdd:cd13971 158 TFEEGVPISRTV----LAHGGEPLKRKLARIGLDaflkMLFVDNFVHGDLHPGNILVrfndsnrpsllvsLDARGSPPRL 233
                       250       260       270
                ....*....|....*....|....*....|
gi 17559152 334 VLLDHGLYLNISDHIRKLYSDLWLAILKPD 363
Cdd:cd13971 234 VFLDAGLVTELSPQDRRNFIDLFKAVARGD 263
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
157-340 3.92e-06

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 49.24  E-value: 3.92e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 157 EKPVGAASLAQVHKAKLKESGETVAVKVQHKRVYKNsrtdvntmeflvkvadavfPEFRLMwlvdeikknlpneldFLHE 236
Cdd:COG0515  12 LRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAAD-------------------PEARER---------------FRRE 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 237 AknadEAAQRFKHLkflRIPKIkYDLTTTR---VLTMEFCEGAHVDDveYLKKNN-IDPHDVcMKIGKTISE-MIFL--Q 309
Cdd:COG0515  58 A----RALARLNHP---NIVRV-YDVGEEDgrpYLVMEYVEGESLAD--LLRRRGpLPPAEA-LRILAQLAEaLAAAhaA 126
                       170       180       190
                ....*....|....*....|....*....|.
gi 17559152 310 GYLHSDPHPGNVLINSLGngkyEIVLLDHGL 340
Cdd:COG0515 127 GIVHRDIKPANILLTPDG----RVKLIDFGI 153
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
229-357 2.22e-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: 44.56  E-value: 2.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 229 NELDFLHEAKNADeaaqrfkhlkfLRIPKIkYDLTTTR-VLTMEFCEGAHVDDVeylKKNNIDPHDVCMKIGKTISEMiF 307
Cdd:COG3642   5 REARLLRELREAG-----------VPVPKV-LDVDPDDaDLVMEYIEGETLADL---LEEGELPPELLRELGRLLARL-H 68
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 17559152 308 LQGYLHSDPHPGNVLINslgNGKyeIVLLDHGLYLnISDHIRKLYSDLWL 357
Cdd:COG3642  69 RAGIVHGDLTTSNILVD---DGG--VYLIDFGLAR-YSDPLEDKAVDLAV 112
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
158-340 7.38e-05

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 44.44  E-value: 7.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152    158 KPVGAASLAQVHKAKLKESGETVAVKVQHKRvyknsrtdvntmeflvkvadavfpefrlmwLVDEIKKNLPNELDFLhea 237
Cdd:smart00220   5 EKLGEGSFGKVYLARDKKTGKLVAIKVIKKK------------------------------KIKKDRERILREIKIL--- 51
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152    238 knadeaaQRFKH---LKFLRIpkikYDLTTTRVLTMEFCEGAHVDDveYLKKNNIDPHDVCMKIGKTISE-MIFL--QGY 311
Cdd:smart00220  52 -------KKLKHpniVRLYDV----FEDEDKLYLVMEYCEGGDLFD--LLKKRGRLSEDEARFYLRQILSaLEYLhsKGI 118
                          170       180
                   ....*....|....*....|....*....
gi 17559152    312 LHSDPHPGNVLINSLGNgkyeIVLLDHGL 340
Cdd:smart00220 119 VHRDLKPENILLDEDGH----VKLADFGL 143
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
161-369 7.44e-05

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: 44.18  E-value: 7.44e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 161 GAASLAQVHKAKLKESGETVAVKVQHKRvyknsrtdvntmeflvkvadavfpefrlmwLVDEIKKNLPNELDFLheakna 240
Cdd:cd00180   2 GKGSFGKVYKARDKETGKKVAVKVIPKE------------------------------KLKKLLEELLREIEIL------ 45
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 241 deaaqrfKHLKFLRIPKIKYDLTTTR--VLTMEFCEGahVDDVEYLKKNN-IDPHDVCMKIGKTISEMI-FL--QGYLHS 314
Cdd:cd00180  46 -------KKLNHPNIVKLYDVFETENflYLVMEYCEG--GSLKDLLKENKgPLSEEEALSILRQLLSALeYLhsNGIIHR 116
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17559152 315 DPHPGNVLINSLGNgkyeIVLLDHGL---YLNISDHIRKLYSDLWLAILKPDLQEIRK 369
Cdd:cd00180 117 DLKPENILLDSDGT----VKLADFGLakdLDSDDSLLKTTGGTTPPYYAPPELLGGRY 170
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
157-340 1.72e-04

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: 43.34  E-value: 1.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 157 EKPVGAASLAQVHKAKLKESGETVAVKVqhkrvyknsrtdvntmeflVKVADAVFPEFRLmwlvdeikknlpnelDFLHE 236
Cdd:cd14014   5 VRLLGRGGMGEVYRARDTLLGRPVAIKV-------------------LRPELAEDEEFRE---------------RFLRE 50
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 237 AknadEAAQRFKHLkflRIPKIkYD---LTTTRVLTMEFCEGAHVDDveYLKKNNIDPHDVCMKIGKTISE-MIFL--QG 310
Cdd:cd14014  51 A----RALARLSHP---NIVRV-YDvgeDDGRPYIVMEYVEGGSLAD--LLRERGPLPPREALRILAQIADaLAAAhrAG 120
                       170       180       190
                ....*....|....*....|....*....|
gi 17559152 311 YLHSDPHPGNVLINSLGngkyEIVLLDHGL 340
Cdd:cd14014 121 IVHRDIKPANILLTEDG----RVKLTDFGI 146
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
158-340 1.12e-03

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family 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: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 40.65  E-value: 1.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 158 KPVGAASLAQVHKAKLKESGETVAVKVQHKRVyknsrtdvntmeflvkvadavfpefrlmwlvDEIKKNLPNELDFLHEa 237
Cdd:cd05122   6 EKIGKGGFGVVYKARHKKTGQIVAIKKINLES-------------------------------KEKKESILNEIAILKK- 53
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559152 238 knadeaaqrFKHlkflriPKI-----KYDLTTTRVLTMEFCEGAHVDDVEYLKKNNIDPHDvcmkIGKTISEMifLQG-- 310
Cdd:cd05122  54 ---------CKH------PNIvkyygSYLKKDELWIVMEFCSGGSLKDLLKNTNKTLTEQQ----IAYVCKEV--LKGle 112
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 17559152 311 YLHS------DPHPGNVLINSlgngKYEIVLLDHGL 340
Cdd:cd05122 113 YLHShgiihrDIKAANILLTS----DGEVKLIDFGL 144
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
267-339 3.15e-03

Catalytic domain of fungal Byr1-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 Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 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: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 39.73  E-value: 3.15e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17559152 267 VLTMEFCEGAHVDDVeyLKKNNIDPHDVCMKIGKTISE-MIFLqgY-----LHSDPHPGNVLINSLGngkyEIVLLDHG 339
Cdd:cd06620  80 IICMEYMDCGSLDKI--LKKKGPFPEEVLGKIAVAVLEgLTYL--YnvhriIHRDIKPSNILVNSKG----QIKLCDFG 150
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
268-330 4.82e-03

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; 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 MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. 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: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 38.73  E-value: 4.82e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17559152 268 LTMEFCEGAHVDDVeyLKKNNIDPHDVCMKIGKTIsemifLQG--YLHSDPH-------PGNVLINSLGNGK 330
Cdd:cd06623  76 IVLEYMDGGSLADL--LKKVGKIPEPVLAYIARQI-----LKGldYLHTKRHiihrdikPSNLLINSKGEVK 140
 
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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