Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015 575 HHFKPIKPLGSGDTGSVHLVELKGTGELYAMKAMEKTMMLNRNKAHRACIEREIISLLDHPFLPTLYASFQTSTHVCLIT 654
Cdd:cd05574   1 DHFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKVKRVLTEREILATLDHPFLPTLYASFQTSTHLCFVM 80

                        90       100
                ....*....|....*....|....*..
gi 30697015 655 DFCPGGELFALLDRQPMKILTEDSARF 681
Cdd:cd05574  81 DYCPGGELFRLLQKQPGKRLPEEVARF 107

hypothetical protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015  128 LSTLQQT---FVVSDATQPHCPIVYASSGFFTMTGYSSKEIVGRNCRFLQGPDTDKNEVAKIRDCVKNGKSYCGRLLNYK 204
Cdd:PRK13559  46 EQAMEQTrmaMCITDPHQPDLPIVLANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYR 125

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 30697015  205 KDGTPFWNLLTVTPIKDDQGNTIKFIGMQVEVSKYTE 241
Cdd:PRK13559 126 KDGEPFWNALHLGPVYGEDGRLLYFFGSQWDVTDIRA 162

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015 575 HHFKPIKPLGSGDTGSVHLVELKGTGELYAMKAMEKTMMLNRNKAHRACIEREIISLLDHPFLPTLYASFQTSTHVCLIT 654
Cdd:cd05574   1 DHFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKVKRVLTEREILATLDHPFLPTLYASFQTSTHLCFVM 80

                        90       100
                ....*....|....*....|....*..
gi 30697015 655 DFCPGGELFALLDRQPMKILTEDSARF 681
Cdd:cd05574  81 DYCPGGELFRLLQKQPGKRLPEEVARF 107

hypothetical protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015  128 LSTLQQT---FVVSDATQPHCPIVYASSGFFTMTGYSSKEIVGRNCRFLQGPDTDKNEVAKIRDCVKNGKSYCGRLLNYK 204
Cdd:PRK13559  46 EQAMEQTrmaMCITDPHQPDLPIVLANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYR 125

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 30697015  205 KDGTPFWNLLTVTPIKDDQGNTIKFIGMQVEVSKYTE 241
Cdd:PRK13559 126 KDGEPFWNALHLGPVYGEDGRLLYFFGSQWDVTDIRA 162

PAS domain [Signal transduction mechanisms];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015 119 RVSQELKTALSTLQQTFVVSDATQPHCPIVYASSGFFTMTGYSSKEIVGRNCRFLQGPDTDKNEVAKIRDCVKNGKSYCG 198
Cdd:COG2202   5 ALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRG 84

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 30697015 199 RLLNYKKDGTPFWNLLTVTPIKDDQGNTIKFIGMQVEVS 237
Cdd:COG2202  85 ELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDIT 123

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015   400 DNPIIFASDSFLELTEYSREEILGRNCRFLQGPETDQATVQKIRDAIRDQREitVQLINYTKSGKKFWNLFHLQPMRDQK 479
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKAVRE--FEVVLYRKDGEPFPVLVSLAPIRDDG 78

                          90
                  ....*....|..
gi 30697015   480 GELQYFIGVQLD 491
Cdd:pfam13426  79 GELVGIIAILRD 90

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015   144 HCPIVYASSGFFTMTGYSSKEIVGRNCRFLQGpdtDKNEVAKIRDCVKNGKS-YCGRLLNYKKDGTPFWNLLTVTPIKDD 222
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFA---EPEDSERLREALREGKAvREFEVVLYRKDGEPFPVLVSLAPIRDD 77

                          90
                  ....*....|....*.
gi 30697015   223 QGNTIKFIGMQVEVSK 238
Cdd:pfam13426  78 GGELVGIIAILRDITE 93

protein kinase A catalytic subunit; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015  554 KESTSWKaikkiqasgetvgLHHFKPIKPLGSGDTGSVHLVELKGTGELYAMKAMEKTMMLNRNKAHRACIEREIISLLD 633
Cdd:PTZ00263  10 PDTSSWK-------------LSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELS 76

                         90       100       110
                 ....*....|....*....|....*....|...
gi 30697015  634 HPFLPTLYASFQTSTHVCLITDFCPGGELFALL 666
Cdd:PTZ00263  77 HPFIVNMMCSFQDENRVYFLLEFVVGGELFTHL 109

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015   403 IIFASDSFLELTEYSREEILGRNCRFLQGPETDQATVQKIRDAIRDQREITVQLINY-TKSGKKFWNLFHLQPMRDQKGE 481
Cdd:TIGR00229  25 ILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRVrRKDGSEIWVEVSVSPIRTNGGE 104

                          90       100
                  ....*....|....*....|..
gi 30697015   482 LqYFIGVQLDGSDHVEpLQNRL 503
Cdd:TIGR00229 105 L-GVVGIVRDITERKE-AEEAL 124

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015 147 IVYASSGFFTMTGYSSKEIVGRNCRFLQGPDTDKNEVAKIRDCVKNGKSYCGRLLNYKKDGTPFWNLLTVTPIKDDQGNT 226
Cdd:cd00130  14 ILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGGEV 93

                        90
                ....*....|
gi 30697015 227 IKFIGMQVEV 236
Cdd:cd00130  94 IGLLGVVRDI 103

Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 30697015    202 NYKKDGTPFWNLLTVTPIKDDQGNTIKFIGMQVEVS 237
Cdd:smart00086   6 LRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDIT 41

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015 575 HHFKPIKPLGSGDTGSVHLVELKGTGELYAMKAMEKTMMLNRNKAHRACIEREIISLLDHPFLPTLYASFQTSTHVCLIT 654
Cdd:cd05574   1 DHFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKVKRVLTEREILATLDHPFLPTLYASFQTSTHLCFVM 80

                        90       100
                ....*....|....*....|....*..
gi 30697015 655 DFCPGGELFALLDRQPMKILTEDSARF 681
Cdd:cd05574  81 DYCPGGELFRLLQKQPGKRLPEEVARF 107

hypothetical protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015  377 GIDLATTLERIEKNFVISDPRLPDNPIIFASDSFLELTEYSREEILGRNCRFLQGPETDQATVQKIRDAIRDQREITVQL 456
Cdd:PRK13559  42 GRLFEQAMEQTRMAMCITDPHQPDLPIVLANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIAVAKIRAAIAAEREIVVEL 121

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30697015  457 INYTKSGKKFWNLFHLQPMRDQKGELQYFIGVQLDGSDHVEPlqnRLSERTEMQSSKLVKATATNV 522
Cdd:PRK13559 122 LNYRKDGEPFWNALHLGPVYGEDGRLLYFFGSQWDVTDIRAV---RALEAHERRLAREVDHRSKNV 184

histidine kinase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015  127 ALSTLQQTFVVSDATQPHCPIVYASSGFFTMTGYSSKEIVGRNCRFLQGPDTDKNEVAKIRDCVKNGKSYCGRLLNYKKD 206
Cdd:PRK13557  35 AVETTRMPMIVTDPNQPDNPIVFANRAFLEMTGYAAEEIIGNNCRFLQGPETDRATVAEVRDAIAERREIATEILNYRKD 114

                         90       100       110
                 ....*....|....*....|....*....|..
gi 30697015  207 GTPFWNLLTVTPIKDDQGNTIKFIGMQVEVSK 238
Cdd:PRK13557 115 GSSFWNALFVSPVYNDAGDLVYFFGSQLDVSR 146

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015 583 LGSGDTGSVHLVELKGTGELYAMKAMEKTMMLNRNKAHRACIEREIISLLDHPFLPTLYASFQTSTHVCLITDFCPGGEL 662
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80

                        90
                ....*....|....*....
gi 30697015 663 FALLDRQPMkiLTEDSARF 681
Cdd:cd05123  81 FSHLSKEGR--FPEERARF 97

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015    577 FKPIKPLGSGDTGSVHLVELKGTGELYAMKAMEKTMMlnRNKAHRACIEREIISLLDHPFLPTLYASFQTSTHVCLITDF 656
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI--KKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78

                           90       100
                   ....*....|....*....|....*
gi 30697015    657 CPGGELFALLDRQpmKILTEDSARF 681
Cdd:smart00220  79 CEGGDLFDLLKKR--GRLSEDEARF 101

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015 577 FKPIKPLGSGDTGSVHLVELKGTGELYAMKAMEKTMMLNRNK-AH-RAciEREIISLLDHPFLPTLYASFQTSTHVCLIT 654
Cdd:cd05599   3 FEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQvAHvRA--ERDILAEADNPWVVKLYYSFQDEENLYLIM 80

                        90       100
                ....*....|....*....|....*....
gi 30697015 655 DFCPGGELFALLdrqpMK--ILTEDSARF 681
Cdd:cd05599  81 EFLPGGDMMTLL----MKkdTLTEEETRF 105

PAS domain [Signal transduction mechanisms];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015 119 RVSQELKTALSTLQQTFVVSDATQPHCPIVYASSGFFTMTGYSSKEIVGRNCRFLQGPDTDKNEVAKIRDCVKNGKSYCG 198
Cdd:COG2202   5 ALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRG 84

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 30697015 199 RLLNYKKDGTPFWNLLTVTPIKDDQGNTIKFIGMQVEVS 237
Cdd:COG2202  85 ELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDIT 123

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015   400 DNPIIFASDSFLELTEYSREEILGRNCRFLQGPETDQATVQKIRDAIRDQREitVQLINYTKSGKKFWNLFHLQPMRDQK 479
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKAVRE--FEVVLYRKDGEPFPVLVSLAPIRDDG 78

                          90
                  ....*....|..
gi 30697015   480 GELQYFIGVQLD 491
Cdd:pfam13426  79 GELVGIIAILRD 90

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015 575 HHFKPIKPLGSGDTGSVHLVELKGTGELYAMKAMEKTMMLNRNKAHRACIEREIISLLDHPFLPTLYASFQTSTHVCLIT 654
Cdd:cd05581   1 NDFKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIKEKKVKYVTIEKEVLSRLAHPGIVKLYYTFQDESKLYFVL 80

                        90       100
                ....*....|....*....|....*..
gi 30697015 655 DFCPGGELFALLDRqpMKILTEDSARF 681
Cdd:cd05581  81 EYAPNGDLLEYIRK--YGSLDEKCTRF 105

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015 577 FKPIKPLGSGDTGSVHLVELKGTGELYAMKAMEKTMMLNRNKAHRACIEREIISLLDHPFLPTLYASFQTSTHVCLITDF 656
Cdd:cd05609   2 FETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRNQIQQVFVERDILTFAENPFVVSMYCSFETKRHLCMVMEY 81

                        90       100
                ....*....|....*....|....*
gi 30697015 657 CPGGELFALLdrQPMKILTEDSARF 681
Cdd:cd05609  82 VEGGDCATLL--KNIGPLPVDMARM 104

Protein kinase domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015   577 FKPIKPLGSGDTGSVHLVELKGTGELYAMKAMEKTMMLNRNKAHrACIEREIISLLDHPFLPTLYASFQTSTHVCLITDF 656
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKN-ILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79

                          90       100
                  ....*....|....*....|....*
gi 30697015   657 CPGGELFALLdrQPMKILTEDSARF 681
Cdd:pfam00069  80 VEGGSLFDLL--SEKGAFSEREAKF 102

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB 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 PI3K.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015 581 KPLGSGDTGSVHLVELKGTGELYAMKAMEKTMMLNRNKAHRACIEREIISLLDHPFLPTLYASFQTSTHVCLITDFCPGG 660
Cdd:cd05571   1 KVLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHTLTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGG 80

                        90       100
                ....*....|....*....|.
gi 30697015 661 ELFALLDRQpmKILTEDSARF 681
Cdd:cd05571  81 ELFFHLSRE--RVFSEDRTRF 99

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015 583 LGSGDTGSVHLVELKGTGELYAMKAMEKTMMLNRNKAHRACIEREIISLLDHPFLPTLYASFQTSTHVCLITDFCPGGEL 662
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80

                        90       100
                ....*....|....*....|
gi 30697015 663 F-ALLDRqpmKILTEDSARF 681
Cdd:cd05572  81 WtILRDR---GLFDEYTARF 97

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015   144 HCPIVYASSGFFTMTGYSSKEIVGRNCRFLQGpdtDKNEVAKIRDCVKNGKS-YCGRLLNYKKDGTPFWNLLTVTPIKDD 222
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFA---EPEDSERLREALREGKAvREFEVVLYRKDGEPFPVLVSLAPIRDD 77

                          90
                  ....*....|....*.
gi 30697015   223 QGNTIKFIGMQVEVSK 238
Cdd:pfam13426  78 GGELVGIIAILRDITE 93

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015 576 HFKPIKPLGSGDTGSVHLVELKGTGELYAMKAMEKTMMLNRNkahRACIERE--IISLLDHPFLPTLYASFQTSTHVCLI 653
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSED---EEMLRREieILKRLDHPNIVKLYEVFEDDKNLYLV 77

                        90       100
                ....*....|....*....|....*....
gi 30697015 654 TDFCPGGELF-ALLDRqpmKILTEDSARF 681
Cdd:cd05117  78 MELCTGGELFdRIVKK---GSFSEREAAK 103

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015 580 IKPLGSGDTGSVHLVELKGTGELYAMKAMEKTMMLNRNKAHracIEREII--SLLDHPFLPTLYASFQTSTHVCLITDFC 657
Cdd:cd14003   5 GKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEK---IKREIEimKLLNHPNIIKLYEVIETENKIYLVMEYA 81

                        90       100
                ....*....|....*....|...
gi 30697015 658 PGGELFALLDRQpmKILTEDSAR 680
Cdd:cd14003  82 SGGELFDYIVNN--GRLSEDEAR 102

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015 581 KPLGSGDTGSVHLVELKGTGELYAMKAMEKTMMLNRNKAHRACIEREIISL-LDHPFLPTLYASFQTSTHVCLITDFCPG 659
Cdd:cd05570   1 KVLGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDVECTMTEKRVLALaNRHPFLTGLHACFQTEDRLYFVMEYVNG 80

                        90       100
                ....*....|....*....|..
gi 30697015 660 GELfaLLDRQPMKILTEDSARF 681
Cdd:cd05570  81 GDL--MFHIQRARRFTEERARF 100

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697015 576 HFKPIKPLGSGDTGSVHLVELKGTGELYAMKAMEKTMMLNRNKAHRACIEREIISLLDHPFLPTLYASFQTSTHVCLITD 655
Cdd:cd05600  12 DFQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLNEVNHVLTERDILTTTNSPWLVKLLYAFQDPENVYLAME 91

                        90       100
                ....*....|....*....|....*.
gi 30697015 656 FCPGGELFALLDRQpmKILTEDSARF 681
Cdd:cd05600  92 YVPGGDFRTLLNNS--GILSEEHARF 115