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Conserved domains on  [gi|116620331|ref|YP_822487|]
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serine/threonin protein kinase [Candidatus Solibacter usitatus Ellin6076]

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List of domain hits

Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
82-374 3.70e-79

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: 258.29  E-value: 3.70e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331  82 PYRIVQLIAEGGMGAVYQAVrvDDLYRKVVAVKVIRRGVFG-EFALRRFDIERQILAHLDHPNIAKLLDGGATpDGRPFF 160
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRAR--DTLLGRPVAIKVLRPELAEdEEFRERFLREARALARLSHPNIVRVYDVGED-DGRPYI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 161 VMDFIAGTPIDEYCDHHK-LGIRERLDFFLKVCSAVHYAHQNLVIHRDLKPGNILVTEEGALKLLDFGIAKLLDpdalag 239
Cdd:cd14014   78 VMEYVEGGSLADLLRERGpLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALG------ 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 240 EDEPTLTTVHAMTPEYASPEQLHGLQVTTASDVYSLGVLLYRLMTGHRPYAGDSrSIEELWEHIRSRPPRrpstviaand 319
Cdd:cd14014  152 DSGLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDS-PAAVLAKHLQEAPPP---------- 220
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 116620331 320 dgvtpetvcsarstkPERLQRQLSGDLDNILMMALRKEPERRYCSVEQFANDLRR 374
Cdd:cd14014  221 ---------------PSPLNPDVPPALDAIILRALAKDPEERPQSAAELLAALRA 260
TPR cd00189
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2) ...
600-725 8.53e-07

Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here


:

Pssm-ID: 238112 [Multi-domain]  Cd Length: 100  Bit Score: 48.15  E-value: 8.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 600 YGNMAGAYLALGDYAhteeqrsQVLREFQELHRLEPDNESFLYGLANAYHRMANLQEqtkhyaaaranvlqAIELFDQIS 679
Cdd:cd00189    3 LLNLGNLYYKLGDYD-------EALEYYEKALELDPDNADAYYNLAAAYYKLGKYEE--------------ALEDYEKAL 61
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 116620331 680 ARHPKDILKRSdwtfaqqRLGSILISTGDLKGALAAFEQVLPIREQ 725
Cdd:cd00189   62 ELDPDNAKAYY-------NLGLAYYKLGKYEEALEAYEKALELDPN 100
TPR cd00189
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2) ...
699-818 1.11e-05

Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here


:

Pssm-ID: 238112 [Multi-domain]  Cd Length: 100  Bit Score: 44.68  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 699 LGSILISTGDLKGALAAFEQVLpireqlqHLDPKDARARLNLANshasvgfVLLELGQAREARGHFEQqrrldeeLIRLD 778
Cdd:cd00189    6 LGNLYYKLGDYDEALEYYEKAL-------ELDPDNADAYYNLAA-------AYYKLGKYEEALEDYEK-------ALELD 64
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 116620331 779 PmgvayqySLSEALENLGRVAQRLGERERGKTYLREALKI 818
Cdd:cd00189   65 P-------DNAKAYYNLGLAYYKLGKYEEALEAYEKALEL 97
TPR cd00189
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2) ...
513-625 1.60e-04

Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here


:

Pssm-ID: 238112 [Multi-domain]  Cd Length: 100  Bit Score: 40.83  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 513 LGQSAEALASYHRALEierqladhdyanitvLRRDMARIYNHICRVEQETGKFKESLENCRESsriqeeqLRLHPDDvvl 592
Cdd:cd00189   13 LGDYDEALEYYEKALE---------------LDPDNADAYYNLAAAYYKLGKYEEALEDYEKA-------LELDPDN--- 67
                         90       100       110
                 ....*....|....*....|....*....|...
gi 116620331 593 radlATTYGNMAGAYLALGDYAHTEEQRSQVLR 625
Cdd:cd00189   68 ----AKAYYNLGLAYYKLGKYEEALEAYEKALE 96
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
83-375 2.21e-56

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 194.29  E-value: 2.21e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331    83 YRIVQLIAEGGMGAVYQAVRVDDlyRKVVAVKVIRRGVFGEFaLRRFDIERQILAHLDHPNIAKLLDGGATPDgRPFFVM 162
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKT--GKLVAIKVIKKKKIKKD-RERILREIKILKKLKHPNIVRLYDVFEDED-KLYLVM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331   163 DFIAGTPIDEY-CDHHKLGIRERLDFFLKVCSAVHYAHQNLVIHRDLKPGNILVTEEGALKLLDFGIAKLLDPDalaged 241
Cdd:smart00220  77 EYCEGGDLFDLlKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPG------ 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331   242 ePTLTTVhAMTPEYASPEQLHGLQVTTASDVYSLGVLLYRLMTGHRPYAGDSrSIEELWEHIRSRPPRRPStviaanddg 321
Cdd:smart00220 151 -EKLTTF-VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDD-QLLELFKKIGKPKPPFPP--------- 218
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 116620331   322 vtPETVCSArstkperlqrqlsgDLDNILMMALRKEPERRYCsveqfANDLRRH 375
Cdd:smart00220 219 --PEWDISP--------------EAKDLIRKLLVKDPEKRLT-----AEEALQH 251
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
82-374 3.70e-79

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: 258.29  E-value: 3.70e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331  82 PYRIVQLIAEGGMGAVYQAVrvDDLYRKVVAVKVIRRGVFG-EFALRRFDIERQILAHLDHPNIAKLLDGGATpDGRPFF 160
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRAR--DTLLGRPVAIKVLRPELAEdEEFRERFLREARALARLSHPNIVRVYDVGED-DGRPYI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 161 VMDFIAGTPIDEYCDHHK-LGIRERLDFFLKVCSAVHYAHQNLVIHRDLKPGNILVTEEGALKLLDFGIAKLLDpdalag 239
Cdd:cd14014   78 VMEYVEGGSLADLLRERGpLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALG------ 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 240 EDEPTLTTVHAMTPEYASPEQLHGLQVTTASDVYSLGVLLYRLMTGHRPYAGDSrSIEELWEHIRSRPPRrpstviaand 319
Cdd:cd14014  152 DSGLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDS-PAAVLAKHLQEAPPP---------- 220
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 116620331 320 dgvtpetvcsarstkPERLQRQLSGDLDNILMMALRKEPERRYCSVEQFANDLRR 374
Cdd:cd14014  221 ---------------PSPLNPDVPPALDAIILRALAKDPEERPQSAAELLAALRA 260
TPR cd00189
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2) ...
600-725 8.53e-07

Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here


Pssm-ID: 238112 [Multi-domain]  Cd Length: 100  Bit Score: 48.15  E-value: 8.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 600 YGNMAGAYLALGDYAhteeqrsQVLREFQELHRLEPDNESFLYGLANAYHRMANLQEqtkhyaaaranvlqAIELFDQIS 679
Cdd:cd00189    3 LLNLGNLYYKLGDYD-------EALEYYEKALELDPDNADAYYNLAAAYYKLGKYEE--------------ALEDYEKAL 61
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 116620331 680 ARHPKDILKRSdwtfaqqRLGSILISTGDLKGALAAFEQVLPIREQ 725
Cdd:cd00189   62 ELDPDNAKAYY-------NLGLAYYKLGKYEEALEAYEKALELDPN 100
TPR cd00189
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2) ...
699-818 1.11e-05

Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here


Pssm-ID: 238112 [Multi-domain]  Cd Length: 100  Bit Score: 44.68  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 699 LGSILISTGDLKGALAAFEQVLpireqlqHLDPKDARARLNLANshasvgfVLLELGQAREARGHFEQqrrldeeLIRLD 778
Cdd:cd00189    6 LGNLYYKLGDYDEALEYYEKAL-------ELDPDNADAYYNLAA-------AYYKLGKYEEALEDYEK-------ALELD 64
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 116620331 779 PmgvayqySLSEALENLGRVAQRLGERERGKTYLREALKI 818
Cdd:cd00189   65 P-------DNAKAYYNLGLAYYKLGKYEEALEAYEKALEL 97
TPR cd00189
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2) ...
513-625 1.60e-04

Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here


Pssm-ID: 238112 [Multi-domain]  Cd Length: 100  Bit Score: 40.83  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 513 LGQSAEALASYHRALEierqladhdyanitvLRRDMARIYNHICRVEQETGKFKESLENCRESsriqeeqLRLHPDDvvl 592
Cdd:cd00189   13 LGDYDEALEYYEKALE---------------LDPDNADAYYNLAAAYYKLGKYEEALEDYEKA-------LELDPDN--- 67
                         90       100       110
                 ....*....|....*....|....*....|...
gi 116620331 593 radlATTYGNMAGAYLALGDYAHTEEQRSQVLR 625
Cdd:cd00189   68 ----AKAYYNLGLAYYKLGKYEEALEAYEKALE 96
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
83-375 2.21e-56

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 194.29  E-value: 2.21e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331    83 YRIVQLIAEGGMGAVYQAVRVDDlyRKVVAVKVIRRGVFGEFaLRRFDIERQILAHLDHPNIAKLLDGGATPDgRPFFVM 162
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKT--GKLVAIKVIKKKKIKKD-RERILREIKILKKLKHPNIVRLYDVFEDED-KLYLVM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331   163 DFIAGTPIDEY-CDHHKLGIRERLDFFLKVCSAVHYAHQNLVIHRDLKPGNILVTEEGALKLLDFGIAKLLDPDalaged 241
Cdd:smart00220  77 EYCEGGDLFDLlKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPG------ 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331   242 ePTLTTVhAMTPEYASPEQLHGLQVTTASDVYSLGVLLYRLMTGHRPYAGDSrSIEELWEHIRSRPPRRPStviaanddg 321
Cdd:smart00220 151 -EKLTTF-VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDD-QLLELFKKIGKPKPPFPP--------- 218
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 116620331   322 vtPETVCSArstkperlqrqlsgDLDNILMMALRKEPERRYCsveqfANDLRRH 375
Cdd:smart00220 219 --PEWDISP--------------EAKDLIRKLLVKDPEKRLT-----AEEALQH 251
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
83-377 7.91e-50

Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair]


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 180.32  E-value: 7.91e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331  83 YRIVQLIAEGGMGAVYQAVRvddlyRKVVAVKVIRRGVFGE-FALRRFDIERQILAHLDHP-NIAKLLDGGaTPDGRPFF 160
Cdd:COG0515    2 YRILRKLGEGSFGEVYLARD-----RKLVALKVLAKKLESKsKEVERFLREIQILASLNHPpNIVKLYDFF-QDEGSLYL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 161 VMDFIAGTPIDEYCDHHKLGIR----ERLDFFLKVCSAVHYAHQNLVIHRDLKPGNILVTEEG-ALKLLDFGIAKLLDPD 235
Cdd:COG0515   76 VMEYVDGGSLEDLLKKIGRKGPlsesEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGrVVKLIDFGLAKLLPDP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 236 ALAGEDEPTLTTVHAmTPEYASPEQLHGL---QVTTASDVYSLGVLLYRLMTGHRPYAGDSRS--IEELWEHIRSRPPRr 310
Cdd:COG0515  156 GSTSSIPALPSTSVG-TPGYMAPEVLLGLslaYASSSSDIWSLGITLYELLTGLPPFEGEKNSsaTSQTLKIILELPTP- 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116620331 311 pstviaanddgvtpetvcSARSTKPERLQRQLSGDLDNILMMALRKEPERRYCSVEQFANDLRRHLQ 377
Cdd:COG0515  234 ------------------SLASPLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLK 282
Pkinase pfam00069
Protein kinase domain;
83-312 1.04e-48

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 173.20  E-value: 1.04e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331   83 YRIVQLIAEGGMGAVYQAVRVDDlyRKVVAVKVIRRGVFGEFALRRFDIERQILAHLDHPNIAKLLDGGATPDgRPFFVM 162
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGT--GKIVAVKILKKRSEKSKKDQTARREIRILRRLSHPNIVRLIDAFEDKD-HLYLVM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331  163 DFIAGTPIDEYC-DHHKLGIRERLDFFLKVCSAVHYAHQNLVIHRDLKPGNILVTEEGALKLLDFGIAKLLDPDAlaged 241
Cdd:pfam00069  78 EYCEGGDLFDYLsRGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGVVKIADFGLAKKLTKSS----- 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116620331  242 ePTLTTVhAMTPEYASPEQL-HGLQVTTASDVYSLGVLLYRLMTGHRPYAGDS-RSIEELWEHIRSRPPRRPS 312
Cdd:pfam00069 153 -SSLTTF-VGTPEYMAPEVLlGGNGYGPKVDVWSLGVILYELLTGKPPFSGESiLDQLQLIRRILGPPLEFDE 223
pknD PRK13184
serine/threonine-protein kinase; Reviewed
80-380 1.57e-32

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 134.51  E-value: 1.57e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331  80 LGPYRIVQLIAEGGMGAVYQAVrvDDLYRKVVAVKVIRRGVfGEFAL--RRFDIERQILAHLDHPNIAKLLDggATPDGR 157
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYLAY--DPVCSRRVALKKIREDL-SENPLlkKRFLREAKIAADLIHPGIVPVYS--ICSDGD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 158 P-FFVMDFIAGTPIDEY------CD------HHKLGIRERLDFFLKVCSAVHYAHQNLVIHRDLKPGNILVTEEGALKLL 224
Cdd:PRK13184  76 PvYYTMPYIEGYTLKSLlksvwqKEslskelAEKTSVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVIL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 225 DFG--IAKLLDPDALAGEDEPTLTTVHAM---------TPEYASPEQLHGLQVTTASDVYSLGVLLYRLMTGHRPYagds 293
Cdd:PRK13184 156 DWGaaIFKKLEEEDLLDIDVDERNICYSSmtipgkivgTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPY---- 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 294 rsieelwehiRSRPPRRpstvIAANDDGVTPETVCSARSTKPErlqrqlsgdLDNILMMALRKEPERRYCSVEQFANDLR 373
Cdd:PRK13184 232 ----------RRKKGRK----ISYRDVILSPIEVAPYREIPPF---------LSQIAMKALAVDPAERYSSVQELKQDLE 288

                 ....*..
gi 116620331 374 RHLQGHP 380
Cdd:PRK13184 289 PHLQGSP 295
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
111-373 1.00e-27

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 119.56  E-value: 1.00e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331   111 VAVKVIRR-GVFGEFALRRFDIERQILAHLDHPNIAKLLDGGATPDGRPFFVMDFIAG-TPIDEYCDHHKLGIRERLDFF 188
Cdd:TIGR03903    6 VAIKLLRTdAPEEEHQRARFRRETALCARLYHPNIVALLDSGEAPPGLLFAVFEYVPGrTLREVLAADGALPAGETGRLM 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331   189 LKVCSAVHYAHQNLVIHRDLKPGNILVTEEGA---LKLLDFGIAKLLdPDALAGeDEPTLTTVHAM--TPEYASPEQLHG 263
Cdd:TIGR03903   86 LQVLDALACAHNQGIVHRDLKPQNIMVSQTGVrphAKVLDFGIGTLL-PGVRDA-DVATLTRTTEVlgTPTYCAPEQLRG 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331   264 LQVTTASDVYSLGVLLYRLMTGHRPYAGDSRSiEELWEHIRSRPPRRPStVIAANddgvtpetvcsarstkperlqrqls 343
Cdd:TIGR03903  164 EPVTPNSDLYAWGLIFLECLTGQRVVQGASVA-EILYQQLSPVDVSLPP-WIAGH------------------------- 216
                          250       260       270
                   ....*....|....*....|....*....|
gi 116620331   344 gDLDNILMMALRKEPERRYCSVEQFANDLR 373
Cdd:TIGR03903  217 -PLGQVLRKALNKDPRQRAASAPALAERFR 245
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
52-293 3.19e-19

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 88.72  E-value: 3.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331  52 AGTFIEEPVASAPKLTP-PMPENLGIGSdLGPYRIVQLIAEGgmgavyqavrvddlyrKVVAVKVIR-RGVFGEFALRRF 129
Cdd:PTZ00263   3 AAYMFTKPDTSSWKLSDfEMGETLGTGS-FGRVRIAKHKGTG----------------EYYAIKCLKkREILKMKQVQHV 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 130 DIERQILAHLDHPNIAKLLDGgATPDGRPFFVMDFIAGtpiDEYCDHHKLGIRERLD----FFLKVCSAVHYAHQNLVIH 205
Cdd:PTZ00263  66 AQEKSILMELSHPFIVNMMCS-FQDENRVYFLLEFVVG---GELFTHLRKAGRFPNDvakfYHAELVLAFEYLHSKDIIY 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 206 RDLKPGNILVTEEGALKLLDFGIAKLLdpdalagedePTLTTVHAMTPEYASPEQLHGLQVTTASDVYSLGVLLYRLMTG 285
Cdd:PTZ00263 142 RDLKPENLLLDNKGHVKVTDFGFAKKV----------PDRTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAG 211

                 ....*...
gi 116620331 286 HRPYAGDS 293
Cdd:PTZ00263 212 YPPFFDDT 219
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
86-393 3.10e-12

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 67.54  E-value: 3.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331  86 VQLIAEGGMGAVYQAVrvddlYR---KVVAVKVIRrGVFGEFALRRFDIERQILAHLDHPNIAKLLDGgATPDGRPFFVM 162
Cdd:PLN00034  79 VNRIGSGAGGTVYKVI-----HRptgRLYALKVIY-GNHEDTVRRQICREIEILRDVNHPNVVKCHDM-FDHNGEIQVLL 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 163 DFIAGTPIDeycDHHKLGIRERLDFFLKVCSAVHYAHQNLVIHRDLKPGNILVTEEGALKLLDFGIAKLL----DPdala 238
Cdd:PLN00034 152 EFMDGGSLE---GTHIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILaqtmDP---- 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 239 geDEPTLTTVHAMTPEYASPEQLHGLQVTTASDVYSLGVLLYRLMTGHRPYA----GDSRSIeeLWEHIRSRPPRRPSTV 314
Cdd:PLN00034 225 --CNSSVGTIAYMSPERINTDLNHGAYDGYAGDIWSLGVSILEFYLGRFPFGvgrqGDWASL--MCAICMSQPPEAPATA 300
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116620331 315 iaanddgvtpetvcsarstkperlqrqlSGDLDNILMMALRKEPERRYCSVEqfandlrrhLQGHPVTARPDTIRYRAG 393
Cdd:PLN00034 301 ----------------------------SREFRHFISCCLQREPAKRWSAMQ---------LLQHPFILRAQPGQGQGG 342
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
140-319 1.19e-11

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 64.49  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 140 DHPNIAKLLDGGATPDGRpFFVMDFIAGTPIDEYC-DHHKLGIRERLDFFLKVCSAVHYAHQNLVIHRDLKPGNILVTE- 217
Cdd:PHA03390  67 DNPNFIKLYYSVTTLKGH-VLIMDYIKDGDLFDLLkKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRa 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 218 EGALKLLDFGIAKLLDpdalagedeptLTTVHAMTPEYASPEQLHGLQVTTASDVYSLGVLLYRLMTGHRPYAGDSR--- 294
Cdd:PHA03390 146 KDRIYLCDYGLCKIIG-----------TPSCYDGTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDeel 214
                        170       180
                 ....*....|....*....|....*
gi 116620331 295 SIEELWEHIRSRPPRRPSTVIAAND 319
Cdd:PHA03390 215 DLESLLKRQQKKLPFIKNVSKNAND 239
Uncharacterized_protein_HI_0366 TIGR02521
type IV pilus biogenesis/stability protein PilW; Members of this family are designated PilF ...
660-818 3.08e-05

type IV pilus biogenesis/stability protein PilW; Members of this family are designated PilF and PilW. This outer membrane protein is required both for pilus stability and for pilus function such as adherence to human cells. Members of this family contain copies of the TPR (tetratricopeptide repeat) domain.


Pssm-ID: 131573 [Multi-domain]  Cd Length: 234  Bit Score: 45.02  E-value: 3.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331  660 HYAAARANVLQAIELfdqisarHPKDILkrsdwtfAQQRLGSILISTGDLKGALAAFEQVLpireqlqHLDPKDARARLN 739
Cdd:TIGR02521  46 DLEVAKENLDKALEH-------DPDDYL-------AYLALALYYQQLGELEKAEDSFRRAL-------TLNPNNGDVLNN 104
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116620331  740 LanshasvGFVLLELGQAREARGHFEQQRRldeelirlDPmgvaYQYSLSEALENLGRVAQRLGERERGKTYLREALKI 818
Cdd:TIGR02521 105 Y-------GTFLCQQGKYEQAMQQFEQAIE--------DP----LYPQPARSLENAGLCALKAGDFDKAEKYLTRALQI 164
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
82-374 3.70e-79

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: 258.29  E-value: 3.70e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331  82 PYRIVQLIAEGGMGAVYQAVrvDDLYRKVVAVKVIRRGVFG-EFALRRFDIERQILAHLDHPNIAKLLDGGATpDGRPFF 160
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRAR--DTLLGRPVAIKVLRPELAEdEEFRERFLREARALARLSHPNIVRVYDVGED-DGRPYI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 161 VMDFIAGTPIDEYCDHHK-LGIRERLDFFLKVCSAVHYAHQNLVIHRDLKPGNILVTEEGALKLLDFGIAKLLDpdalag 239
Cdd:cd14014   78 VMEYVEGGSLADLLRERGpLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALG------ 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 240 EDEPTLTTVHAMTPEYASPEQLHGLQVTTASDVYSLGVLLYRLMTGHRPYAGDSrSIEELWEHIRSRPPRrpstviaand 319
Cdd:cd14014  152 DSGLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDS-PAAVLAKHLQEAPPP---------- 220
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 116620331 320 dgvtpetvcsarstkPERLQRQLSGDLDNILMMALRKEPERRYCSVEQFANDLRR 374
Cdd:cd14014  221 ---------------PSPLNPDVPPALDAIILRALAKDPEERPQSAAELLAALRA 260
TPR cd00189
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2) ...
600-725 8.53e-07

Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here


Pssm-ID: 238112 [Multi-domain]  Cd Length: 100  Bit Score: 48.15  E-value: 8.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 600 YGNMAGAYLALGDYAhteeqrsQVLREFQELHRLEPDNESFLYGLANAYHRMANLQEqtkhyaaaranvlqAIELFDQIS 679
Cdd:cd00189    3 LLNLGNLYYKLGDYD-------EALEYYEKALELDPDNADAYYNLAAAYYKLGKYEE--------------ALEDYEKAL 61
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 116620331 680 ARHPKDILKRSdwtfaqqRLGSILISTGDLKGALAAFEQVLPIREQ 725
Cdd:cd00189   62 ELDPDNAKAYY-------NLGLAYYKLGKYEEALEAYEKALELDPN 100
TPR cd00189
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2) ...
699-818 1.11e-05

Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here


Pssm-ID: 238112 [Multi-domain]  Cd Length: 100  Bit Score: 44.68  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 699 LGSILISTGDLKGALAAFEQVLpireqlqHLDPKDARARLNLANshasvgfVLLELGQAREARGHFEQqrrldeeLIRLD 778
Cdd:cd00189    6 LGNLYYKLGDYDEALEYYEKAL-------ELDPDNADAYYNLAA-------AYYKLGKYEEALEDYEK-------ALELD 64
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 116620331 779 PmgvayqySLSEALENLGRVAQRLGERERGKTYLREALKI 818
Cdd:cd00189   65 P-------DNAKAYYNLGLAYYKLGKYEEALEAYEKALEL 97
TPR cd00189
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2) ...
513-625 1.60e-04

Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here


Pssm-ID: 238112 [Multi-domain]  Cd Length: 100  Bit Score: 40.83  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 513 LGQSAEALASYHRALEierqladhdyanitvLRRDMARIYNHICRVEQETGKFKESLENCRESsriqeeqLRLHPDDvvl 592
Cdd:cd00189   13 LGDYDEALEYYEKALE---------------LDPDNADAYYNLAAAYYKLGKYEEALEDYEKA-------LELDPDN--- 67
                         90       100       110
                 ....*....|....*....|....*....|...
gi 116620331 593 radlATTYGNMAGAYLALGDYAHTEEQRSQVLR 625
Cdd:cd00189   68 ----AKAYYNLGLAYYKLGKYEEALEAYEKALE 96
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
82-314 2.59e-41

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-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: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 152.29  E-value: 2.59e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331  82 PYRIVQLIAEGGMGAVYQAVrvDDLYRKVVAVKVIRRGVFGEFALRRFDIERQILAHLDHPNIAKLLDGGATPDgRPFFV 161
Cdd:cd14003    1 NYELGKTLGEGSFGKVKLAR--HKLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETEN-KIYLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 162 MdfiagtpidEYCD----HHKLGIRERLD------FFLKVCSAVHYAHQNLVIHRDLKPGNILVTEEGALKLLDFGIAKL 231
Cdd:cd14003   78 M---------EYASggelFDYIVNNGRLSedearrFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNE 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 232 LDPDALAGedeptlTTVHamTPEYASPEQLHG-LQVTTASDVYSLGVLLYRLMTGHRPYagDSRSIEELWEHIRSRPPRR 310
Cdd:cd14003  149 FRGGSLLK------TFCG--TPAYAAPEVLLGrKYDGPKADVWSLGVILYAMLTGYLPF--DDDNDSKLFRKILKGKYPI 218

                 ....
gi 116620331 311 PSTV 314
Cdd:cd14003  219 PSHL 222
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
89-312 3.27e-40

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: 148.19  E-value: 3.27e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331  89 IAEGGMGAVYQAVRVDDlyRKVVAVKVIRRGVFGEFaLRRFDIERQILAHLDHPNIAKLLDGGATPDgRPFFVMDFIAGT 168
Cdd:cd00180    1 LGKGSFGKVYKARDKET--GKKVAVKVIPKEKLKKL-LEELLREIEILKKLNHPNIVKLYDVFETEN-FLYLVMEYCEGG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 169 PIDEY-CDH-HKLGIRERLDFFLKVCSAVHYAHQNLVIHRDLKPGNILVTEEGALKLLDFGIAKLLDPDalageDEPTLT 246
Cdd:cd00180   77 SLKDLlKENkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSD-----DSLLKT 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331 247 TVHAMTPEYASPEQLHGLQVTTASDVYSLGVLLYRLmtghrpyagdsrsiEELWEHIRS----RPPRRPS 312
Cdd:cd00180  152 TGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL--------------EELKDLIRRmlqyDPKKRPS 207
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
89-311 4.47e-40

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase 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 mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 148.84  E-value: 4.47e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116620331  89 IAEGGMGAVYQAVrvddlYR-KVVAV