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 343175990   1 MAPEVMEQVRGYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETGVEdkemMKKYGKSFRKLLSLCL 80
Cdd:cd06610  173 MAPEVMEQVRGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNDPPSLETGAD----YKKYSKSFRKMISLCL 248

                         90
                 ....*....|....*....
gi 343175990  81 QKDPSKRPTAAELLKCKFF 99
Cdd:cd06610  249 QKDPSKRPTAEELLKHKFF 267

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343175990   1 MAPEVMEQVRGYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETGVEdkemMKKYGKSFRKLLSLCL 80
Cdd:cd06610  173 MAPEVMEQVRGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNDPPSLETGAD----YKKYSKSFRKMISLCL 248

                         90
                 ....*....|....*....
gi 343175990  81 QKDPSKRPTAAELLKCKFF 99
Cdd:cd06610  249 QKDPSKRPTAEELLKHKFF 267

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343175990     1 MAPEVMEQvRGYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLEtgvedkEMMKKYGKSFRKLLSLCL 80
Cdd:smart00220 163 MAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFP------PPEWDISPEAKDLIRKLL 235

                           90
                   ....*....|....*....
gi 343175990    81 QKDPSKRPTAAELLKCKFF 99
Cdd:smart00220 236 VKDPEKRLTAEEALQHPFF 254

Serine/threonine protein kinase [Signal transduction mechanisms];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343175990   1 MAPEvmeQVRG--YDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETGVEDkemmkkYGKSFRKLLSL 78
Cdd:COG0515  175 MAPE---QARGepVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPD------LPPALDAIVLR 245

                         90
                 ....*....|....*...
gi 343175990  79 CLQKDPSKRP-TAAELLK 95
Cdd:COG0515  246 ALAKDPEERYqSAAELAA 263

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343175990   1 MAPEVMEQVRGYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETGVEdkemMKKYGKSFRKLLSLCL 80
Cdd:cd06610  173 MAPEVMEQVRGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNDPPSLETGAD----YKKYSKSFRKMISLCL 248

                         90
                 ....*....|....*....
gi 343175990  81 QKDPSKRPTAAELLKCKFF 99
Cdd:cd06610  249 QKDPSKRPTAEELLKHKFF 267

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-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 343175990   1 MAPEVMEQvRGYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETGvedkemmkKYGKSFRKLLSLCL 80
Cdd:cd06609  165 MAPEVIKQ-SGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNNPPSLEGN--------KFSKPFKDFVELCL 235

                         90       100       110
                 ....*....|....*....|....*....|
gi 343175990  81 QKDPSKRPTAAELLKCKFFQKAKNREYLIE 110
Cdd:cd06609  236 NKDPKERPSAKELLKHKFIKKAKKTSYLTL 265

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-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 343175990   1 MAPEVM----EQVRGYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETGvedkemmKKYGKSFRKLL 76
Cdd:cd06611  170 MAPEVVacetFKDNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEPPTLDQP-------SKWSSSFNDFL 242

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 343175990  77 SLCLQKDPSKRPTAAELLKCKFFQKAKNREYLIEKLL 113
Cdd:cd06611  243 KSCLVKDPDDRPTAAELLKHPFVSDQSDNKAIKDLLA 279

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK 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 343175990   1 MAPEVmeqVRG--YDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETGvedkemmKKYGKSFRKLLSL 78
Cdd:cd06614  164 MAPEV---IKRkdYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITTKGIPPLKNP-------EKWSPEFKDFLNK 233

                         90       100
                 ....*....|....*....|..
gi 343175990  79 CLQKDPSKRPTAAELLKCKFFQ 100
Cdd:cd06614  234 CLVKDPEKRPSAEELLQHPFLK 255

Oxidative-stress-responsive kinase 1 C-terminal domain; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with pfam00069. There is a single completely conserved residue F that may be functionally important. OSR1 is involved in the signalling cascade which activates Na/K/2Cl cotransporter during osmotic stress. This domain is the C terminal domain of OSR1 which recognizes a motif (Arg-Phe-Xaa-Val) on the OSR1-activating protein WNK1.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343175990  213 VNLVLRLRN----SRKELNDIRFEFTPGRDTADGVSQELFSAGLVDGHDVVIVAANLQKIVD 270
Cdd:pfam12202   1 INLVLRVRDpkkkKHKELNAIRFEFTLGKDTAEGVAQEMVKAGLVDEEDVKVVAANLRKRVD 62

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-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 343175990   1 MAPEV---MEQV-RGYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETGvedkemmKKYGKSFRKLL 76
Cdd:cd06608  180 MAPEViacDQQPdASYDARCDVWSLGITAIELADGKPPLCDMHPMRALFKIPRNPPPTLKSP-------EKWSKEFNDFI 252

                         90       100
                 ....*....|....*....|..
gi 343175990  77 SLCLQKDPSKRPTAAELLKCKF 98
Cdd:cd06608  253 SECLIKNYEQRPFTEELLEHPF 274

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 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 343175990   1 MAPEVMEQvRGYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLetgvedkemMKKYGKSFRKLLSLCL 80
Cdd:cd06640  168 MAPEVIQQ-SAYDSKADIWSLGITAIELAKGEPPNSDMHPMRVLFLIPKNNPPTL---------VGDFSKPFKEFIDACL 237

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 343175990  81 QKDPSKRPTAAELLKCKFFQKAKNREYLIEKLLTR 115
Cdd:cd06640  238 NKDPSFRPTAKELLKHKFIVKNAKKTSYLTELIDR 272

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-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 343175990   1 MAPEVMEqVRGYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETGVEDkemmkkygkSFRKLLSLCL 80
Cdd:cd06627  166 MAPEVIE-MSGVTTASDIWSVGCTVIELLTGNPPYYDLQPMAALFRIVQDDHPPLPENISP---------ELRDFLLQCF 235

                         90
                 ....*....|....*....
gi 343175990  81 QKDPSKRPTAAELLKCKFF 99
Cdd:cd06627  236 QKDPTLRPSAKELLKHPWL 254

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO 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 343175990   1 MAPEV---MEQVRgYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETGvedkemmkKYGKSFRKLLS 77
Cdd:cd06607  164 MAPEVilaMDEGQ-YDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNDSPTLSSG--------EWSDDFRNFVD 234

                         90       100
                 ....*....|....*....|....
gi 343175990  78 LCLQKDPSKRPTAAELLKCKFFQK 101
Cdd:cd06607  235 SCLQKIPQDRPSAEDLLKHPFVTR 258

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 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 343175990   1 MAPEV---MEQVRgYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETgvedkemmKKYGKSFRKLLS 77
Cdd:cd06633  184 MAPEVilaMDEGQ-YDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHIAQNDSPTLQS--------NEWTDSFRGFVD 254

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 343175990  78 LCLQKDPSKRPTAAELLKCKFFQKAKNREYLIEkLLTRTPD 118
Cdd:cd06633  255 YCLQKIPQERPSSAELLRHDFVRRERPPRVLID-LIQRTKD 294

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343175990   1 MAPEVMeQVRGYDFKADMWSFGITAIELATGAAPY---HKYPPMKVLML---TLQNDPPTLETGvedkemmkKYGKSFRK 74
Cdd:cd06605  165 MAPERI-SGGKYTVKSDIWSLGLSLVELATGRFPYpppNAKPSMMIFELlsyIVDEPPPLLPSG--------KFSPDFQD 235

                         90       100       110
                 ....*....|....*....|....*....|
gi 343175990  75 LLSLCLQKDPSKRPTAAELLKCKFFQKAKN 104
Cdd:cd06605  236 FVSQCLQKDPTERPSYKELMEHPFIKRYEY 265

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 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 343175990   1 MAPEV-MEQVRGYDFKADMWSFGITAIELATGAAPYHKYPPMKVlMLTLQNDP--PTLETGVEDKemmkkyGKSFrklLS 77
Cdd:cd06632  168 MAPEViMQKNSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAA-IFKIGNSGelPPIPDHLSPD------AKDF---IR 237

                         90       100
                 ....*....|....*....|.
gi 343175990  78 LCLQKDPSKRPTAAELLKCKF 98
Cdd:cd06632  238 LCLQRDPEDRPTASQLLEHPF 258

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK 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 343175990   1 MAPEVM----EQVRGYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETGvedkemmKKYGKSFRKLL 76
Cdd:cd06643  170 MAPEVVmcetSKDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLAQP-------SRWSPEFKDFL 242

                         90       100
                 ....*....|....*....|..
gi 343175990  77 SLCLQKDPSKRPTAAELLKCKF 98
Cdd:cd06643  243 RKCLEKNVDARWTTSQLLQHPF 264

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 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 343175990   1 MAPEVMEQVRG----YDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETgvedkemmKKYGKSFRKLL 76
Cdd:cd06636  188 MAPEVIACDENpdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPKLKS--------KKWSKKFIDFI 259

                         90       100
                 ....*....|....*....|..
gi 343175990  77 SLCLQKDPSKRPTAAELLKCKF 98
Cdd:cd06636  260 EGCLVKNYLSRPSTEQLLKHPF 281

Protein kinase domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343175990    1 MAPEVMEQvRGYDFKADMWSFGITAIELATGAAPYHkyppmkvlmltLQNDPPTLETGVEDKEMMKK----YGKSFRKLL 76
Cdd:pfam00069 127 MAPEVLGG-NPYGPKVDVWSLGCILYELLTGKPPFP-----------GINGNEIYELIIDQPYAFPElpsnLSEEAKDLL 194

                          90       100
                  ....*....|....*....|...
gi 343175990   77 SLCLQKDPSKRPTAAELLKCKFF 99
Cdd:pfam00069 195 KKLLKKDPSKRLTATQALQHPWF 217

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin 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 343175990   1 MAPEVM--EQV--RGYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLetgvEDKEMmkkYGKSFRKLL 76
Cdd:cd06638  191 MAPEVIacEQQldSTYDARCDVWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPTL----HQPEL---WSNEFNDFI 263

                         90       100
                 ....*....|....*....|..
gi 343175990  77 SLCLQKDPSKRPTAAELLKCKF 98
Cdd:cd06638  264 RKCLTKDYEKRPTVSDLLQHVF 285

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343175990   1 MAPEVMEQvRGYDFKADMWSFGITAIELATGAAPYHKYPPMKVLML-TLQNDPPTLETGVedkemmkkyGKSFRKLLSLC 79
Cdd:cd13999  158 MAPEVLRG-EPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAvVQKGLRPPIPPDC---------PPELSKLIKRC 227

                         90
                 ....*....|....*.
gi 343175990  80 LQKDPSKRPTAAELLK 95
Cdd:cd13999  228 WNEDPEKRPSFSEIVK 243

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-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 343175990   1 MAPEVMEQvRGYDFKADMWSFGITAIELATGAAPYHKYPPMKVLM-LTLQNDPPTLETGVEDkemmkkygkSFRKLLSLC 79
Cdd:cd06625  171 MSPEVING-EGYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFkIATQPTNPQLPPHVSE---------DARDFLSLI 240

                         90       100
                 ....*....|....*....|
gi 343175990  80 LQKDPSKRPTAAELLKCKFF 99
Cdd:cd06625  241 FVRNKKQRPSAEELLSHSFV 260

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343175990   1 MAPEVMeQVRGYDFKADMWSFGITAIELATGAAPYHKYP--------PMKVLML---TLQNDPPTLETGvedkemmKKYG 69
Cdd:cd06620  170 MSPERI-QGGKYSVKSDVWSLGLSIIELALGEFPFAGSNddddgyngPMGILDLlqrIVNEPPPRLPKD-------RIFP 241

                         90       100       110
                 ....*....|....*....|....*....|...
gi 343175990  70 KSFRKLLSLCLQKDPSKRPTAAELLKCKFFQKA 102
Cdd:cd06620  242 KDLRDFVDRCLLKDPRERPSPQLLLDHDPFIQA 274

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha, stabilized through ATP and MO25, may be needed to activate LKB1. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. The STRAD alpha subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343175990   1 MAPEVMEQ-VRGYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTL--ETGVEDKEMMKKYGKS------ 71
Cdd:cd08227  175 LSPEVLQQnLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLldTTTIPAEELTMKPSRSgansgl 254

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343175990  72 ----------------------------FRKLLSLCLQKDPSKRPTAAELLKCKFFQKAKNR--EYLIEKLL 113
Cdd:cd08227  255 gesttvstprpsngessshpynrtfsphFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRasEALPELLR 326

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK 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 343175990   1 MAPEVMEQVRgYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETgvedkemMKKYGKSFRKLLSLCL 80
Cdd:cd06648  170 MAPEVISRLP-YGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEPPKLKN-------LHKVSPRLRSFLDRML 241

                         90
                 ....*....|....*....
gi 343175990  81 QKDPSKRPTAAELLKCKFF 99
Cdd:cd06648  242 VRDPAQRATAAELLNHPFL 260

Catalytic domain of fungal PBS2-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 Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343175990   1 MAPE-----VMEQVRGYDFKADMWSFGITAIELATGAAPYhkyPP------MKVLMLTLQNDPPTLETGvedkemmkkYG 69
Cdd:cd06622  168 MAPEriksgGPNQNPTYTVQSDVWSLGLSILEMALGRYPY---PPetyaniFAQLSAIVDGDPPTLPSG---------YS 235

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 343175990  70 KSFRKLLSLCLQKDPSKRPTAAELLKCKFFQKAKNRE 106
Cdd:cd06622  236 DDAQDFVAKCLNKIPNRRPTYAQLLEHPWLVKYKNAD 272

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343175990   1 MAPEVMEQVRgYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETgvedkemMKKYGKSFRKLLSLCL 80
Cdd:cd06657  183 MAPELISRLP-YGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPKLKN-------LHKVSPSLKGFLDRLL 254

                         90       100
                 ....*....|....*....|..
gi 343175990  81 QKDPSKRPTAAELLKCKFFQKA 102
Cdd:cd06657  255 VRDPAQRATAAELLKHPFLAKA 276

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343175990   1 MAPEvmeQVRG--YDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLetgvedKEMMKKYGKSFRKLLSL 78
Cdd:cd14014  168 MAPE---QARGgpVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPP------SPLNPDVPPALDAIILR 238

                         90
                 ....*....|....*..
gi 343175990  79 CLQKDPSKRP-TAAELL 94
Cdd:cd14014  239 ALAKDPEERPqSAAELL 255

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343175990   1 MAPEVMEQvRGYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETGvedkemmKKYGKSFRKLLSLCL 80
Cdd:cd06655  182 MAPEVVTR-KAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNP-------EKLSPIFRDFLNRCL 253

                         90       100
                 ....*....|....*....|...
gi 343175990  81 QKDPSKRPTAAELLKCKFFQKAK 103
Cdd:cd06655  254 EMDVEKRGSAKELLQHPFLKLAK 276

Serine/threonine protein kinase [Signal transduction mechanisms];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343175990   1 MAPEvmeQVRG--YDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETGVEDkemmkkYGKSFRKLLSL 78
Cdd:COG0515  175 MAPE---QARGepVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPD------LPPALDAIVLR 245