Serine/threonine protein kinase [Signal transduction mechanisms];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314926067   9 RQSFWAELN-AARLDHSNVVRVIAASTsvpahQDSLGTIIMEYVGNSTLHHVIygtgsmaaKEREKLSIAQSLGYSCNIV 87
Cdd:COG0515    51 RERFRREARaLARLNHPNIVRVYDVGE-----EDGRPYLVMEYVEGESLADLL--------RRRGPLPPAEALRILAQLA 117

                          90       100
                  ....*....|....*....|....*...
gi 1314926067  88 AGLVFLHSQLIVHLDLKPANVFITEQNV 115
Cdd:COG0515   118 EALAAAHAAGIVHRDIKPANILLTPDGR 145

Stk1 family PASTA domain-containing Ser/Thr kinase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314926067  17 NAARLDHSNVVRVIAASTsvpahQDSLGTIIMEYVGNSTLHHVIygtgsmaaKEREKLSIAQSLGYSCNIVAGLVFLHSQ 96
Cdd:NF033483   60 SAASLSHPNIVSVYDVGE-----DGGIPYIVMEYVDGRTLKDYI--------REHGPLSPEEAVEIMIQILSALEHAHRN 126

                          90
                  ....*....|....*....
gi 1314926067  97 LIVHLDLKPANVFITEQNV 115
Cdd:NF033483  127 GIVHRDIKPQNILITKDGR 145

cyclin-dependent protein kinase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314926067  21 LDHSNVVRVIAastsVPAHQDSLgTIIMEYVgNSTLHHVIygtgsmaaKEREKLSIAQSLGYSCNIVAGLVFLHSQLIVH 100
Cdd:PTZ00024   77 IKHENIMGLVD----VYVEGDFI-NLVMDIM-ASDLKKVV--------DRKIRLTESQVKCILLQILNGLNVLHKWYFMH 142

                          90
                  ....*....|....*.
gi 1314926067 101 LDLKPANVFITEQNVC 116
Cdd:PTZ00024  143 RDLSPANIFINSKGIC 158

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314926067   3 KNCLASRQSFWAELNA-ARLDHSNVVRVIAASTSVPAHQdslgtIIMEYVGNSTLHHVIygtgsmaAKEREKLSIAQSLG 81
Cdd:cd00180    29 EKLKKLLEELLREIEIlKKLNHPNIVKLYDVFETENFLY-----LVMEYCEGGSLKDLL-------KENKGPLSEEEALS 96

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1314926067  82 YSCNIVAGLVFLHSQLIVHLDLKPANVFITEQNVC 116
Cdd:cd00180    97 ILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTV 131

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314926067    3 KNCLASRQSFWAELNA-ARLDHSNVVRVIAASTsvpaHQDSLgTIIMEYVGNSTLHHVIygtgsmaaKEREKLSIAQSLG 81
Cdd:smart00220  35 KKIKKDRERILREIKIlKKLKHPNIVRLYDVFE----DEDKL-YLVMEYCEGGDLFDLL--------KKRGRLSEDEARF 101

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1314926067   82 YSCNIVAGLVFLHSQLIVHLDLKPANVFITEQNV 115
Cdd:smart00220 102 YLRQILSALEYLHSKGIVHRDLKPENILLDEDGH 135

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 1314926067   9 RQSFWAELNA-ARLDHSNVVRVIAASTSVPahqdSLgTIIMEYVGNSTLHHVIygtgsmaAKEREKLSIAQSLGYSCNIV 87
Cdd:cd13999    34 LKEFRREVSIlSKLRHPNIVQFIGACLSPP----PL-CIVTEYMPGGSLYDLL-------HKKKIPLSWSLRLKIALDIA 101

                          90       100
                  ....*....|....*....|....*....
gi 1314926067  88 AGLVFLHSQLIVHLDLKPANVFITEQNVC 116
Cdd:cd13999   102 RGMNYLHSPPIIHRDLKSLNILLDENFTV 130

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 1314926067  20 RLDHSNVVRVIAASTSvpahQDSLgTIIMEYVGNSTLHHVIYGTGSMAakerEKLSIAqslgYSCNIVAGLVFLHSQLIV 99
Cdd:cd06627    55 KLNHPNIVKYIGSVKT----KDSL-YIILEYVENGSLASIIKKFGKFP----ESLVAV----YIYQVLEGLAYLHEQGVI 121

                          90
                  ....*....|....*..
gi 1314926067 100 HLDLKPANVFITEQNVC 116
Cdd:cd06627   122 HRDIKGANILTTKDGLV 138

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK 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 1314926067  20 RLDHSNVVR---VIaastSVPaHQDSLgTIIMEYVGNSTLHHVIYGTgsmaakEREKLSIAQSLGYSCNIVAGLVFLHSQ 96
Cdd:cd14008    60 KLDHPNIVRlyeVI----DDP-ESDKL-YLVLEYCEGGPVMELDSGD------RVPPLPEETARKYFRDLVLGLEYLHEN 127

                          90       100
                  ....*....|....*....|
gi 1314926067  97 LIVHLDLKPANVFITEQNVC 116
Cdd:cd14008   128 GIVHRDIKPENLLLTADGTV 147

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They 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. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK 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 1314926067  20 RLDHSNVVRVIAASTSvpahQDSLgTIIMEYVGNSTLHHVIYGTGSMaakeREKLsIAQslgYSCNIVAGLVFLHSQLIV 99
Cdd:cd06606    55 SLKHPNIVRYLGTERT----ENTL-NIFLEYVPGGSLASLLKKFGKL----PEPV-VRK---YTRQILEGLEYLHSNGIV 121

                          90
                  ....*....|....*..
gi 1314926067 100 HLDLKPANVFITEQNVC 116
Cdd:cd06606   122 HRDIKGANILVDSDGVV 138

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314926067    9 RQSFWAELNA-ARLDHSNVVRVIAASTSVPAHQdslgtIIMEYVGNSTLHHVIygtgsmAAKEREKLSIAQSLGYSCNIV 87
Cdd:smart00221  45 IEEFLREARImRKLDHPNIVKLLGVCTEEEPLM-----IVMEYMPGGDLLDYL------RKNRPKELSLSDLLSFALQIA 113

                           90       100
                   ....*....|....*....|....*....
gi 1314926067   88 AGLVFLHSQLIVHLDLKPANVFITEQNVC 116
Cdd:smart00221 114 RGMEYLESKNFIHRDLAARNCLVGENLVV 142

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314926067   9 RQSFWAELNA-ARLDHSNVVRVIAASTSvpahQDSLgTIIMEYVGNSTLHHVIYGTGSMAAKEREK-LSIAQSLGYSCNI 86
Cdd:cd00192    40 RKDFLKEARVmKKLGHPNVVRLLGVCTE----EEPL-YLVMEYMEGGDLLDFLRKSRPVFPSPEPStLSLKDLLSFAIQI 114

                          90       100       110
                  ....*....|....*....|....*....|
gi 1314926067  87 VAGLVFLHSQLIVHLDLKPANVFITEQNVC 116
Cdd:cd00192   115 AKGMEYLASKKFVHRDLAARNCLVGEDLVV 144

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 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 1314926067   6 LASRQSFWAELNA-ARLDHSNVVRVIAASTSVPAhqDSLgtiIMEYVGNSTLHHVIYGtgsmaAKEREKLSIAQSLGYSC 84
Cdd:cd14058    27 ESEKKAFEVEVRQlSRVDHPNIIKLYGACSNQKP--VCL---VMEYAEGGSLYNVLHG-----KEPKPIYTAAHAMSWAL 96

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1314926067  85 NIVAGLVFLHS---QLIVHLDLKPANVFITEQ 113
Cdd:cd14058    97 QCAKGVAYLHSmkpKALIHRDLKPPNLLLTNG 128

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 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 1314926067  20 RLDHSNVVRVIAastsVPAHQDSLgTIIMEYVGNSTLHHVI-YGTGsmaakEREKLSIAqslgYSCNIVAGLVFLHSQLI 98
Cdd:cd06626    55 GLDHPNLVRYYG----VEVHREEV-YIFMEYCQEGTLEELLrHGRI-----LDEAVIRV----YTLQLLEGLAYLHENGI 120

                          90
                  ....*....|....*..
gi 1314926067  99 VHLDLKPANVFITEQNV 115
Cdd:cd06626   121 VHRDIKPANIFLDSNGL 137

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like 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 1314926067  23 HSNVVRVIAaSTSVPAHQDSLGTIIMEYVGNSTLHHviygtgsMAAKEREKLSIAQSLGYSCNIVAGLVFLHSQL--IVH 100
Cdd:cd13985    57 HPNIVQYYD-SAILSSEGRKEVLLLMEYCPGSLVDI-------LEKSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIH 128

                          90
                  ....*....|....*.
gi 1314926067 101 LDLKPANVFITEQNVC 116
Cdd:cd13985   129 RDIKIENILFSNTGRF 144

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-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 1314926067  20 RLDHSNVVR---VIAASTSVpahqdslgTIIMEYVgNSTLHHVIygtgsmaAKEREKLSIAQSLGYSCNIVAGLVFLHSQ 96
Cdd:cd07829    54 ELKHPNIVKlldVIHTENKL--------YLVFEYC-DQDLKKYL-------DKRPGPLPPNLIKSIMYQLLRGLAYCHSH 117

                          90
                  ....*....|....*....
gi 1314926067  97 LIVHLDLKPANVFITEQNV 115
Cdd:cd07829   118 RILHRDLKPQNLLINRDGV 136

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 1314926067  20 RLDHSNVVR---VIAASTSVpahqdslgTIIMEYVGNSTLHHVIYGTGSMAAKEREKLsIAQslgyscnIVAGLVFLHSQ 96
Cdd:cd14003    55 LLNHPNIIKlyeVIETENKI--------YLVMEYASGGELFDYIVNNGRLSEDEARRF-FQQ-------LISAVDYCHSN 118

                          90
                  ....*....|....*...
gi 1314926067  97 LIVHLDLKPANVFITEQN 114
Cdd:cd14003   119 GIVHRDLKLENILLDKNG 136

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 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 1314926067  20 RLDHSNVVRVIAASTSVPAHqdslgTIIMEYVGNSTLHHVIygtgsmaaKEREKLSIAQSLGYSCNIVAGLVFLHSQLIV 99
Cdd:cd14059    37 KLNHPNIIKFKGVCTQAPCY-----CILMEYCPYGQLYEVL--------RAGREITPSLLVDWSKQIASGMNYLHLHKII 103

                          90
                  ....*....|....*.
gi 1314926067 100 HLDLKPANVFITEQNV 115
Cdd:cd14059   104 HRDLKSPNVLVTYNDV 119

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314926067  23 HSNVVRVIAAStsvpAHQDSLgTIIMEYVGNSTLHHviygtgsmaAKEREKLSIAQSLGYSCNIVAGLVFLHSQLIVHLD 102
Cdd:cd14050    60 HPNCVRFIKAW----EEKGIL-YIQTELCDTSLQQY---------CEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLD 125

                          90
                  ....*....|....
gi 1314926067 103 LKPANVFITEQNVC 116
Cdd:cd14050   126 IKPANIFLSKDGVC 139

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 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 1314926067  20 RLDHSNVVRV----------IAASTSVPAHQDSLgTIIMEYVgNSTLHHVIygtgsmaakEREKLSIAQSLGYSCNIVAG 89
Cdd:cd07854    58 RLDHDNIVKVyevlgpsgsdLTEDVGSLTELNSV-YIVQEYM-ETDLANVL---------EQGPLSEEHARLFMYQLLRG 126

                          90       100
                  ....*....|....*....|....*..
gi 1314926067  90 LVFLHSQLIVHLDLKPANVFI-TEQNV 115
Cdd:cd07854   127 LKYIHSANVLHRDLKPANVFInTEDLV 153

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314926067   1 CSKNCLASRQSFWAELNAA-RLDHSNVVRVIAASTSVPAHQDSLGT-IIMEYVGNSTLHHVIYGTGSmaakerekLSIAQ 78
Cdd:cd14012    34 KTSNGKKQIQLLEKELESLkKLRHPNLVSYLAFSIERRGRSDGWKVyLLTEYAPGGSLSELLDSVGS--------VPLDT 105

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1314926067  79 SLGYSCNIVAGLVFLHSQLIVHLDLKPANVFI 110
Cdd:cd14012   106 ARRWTLQLLEALEYLHRNGVVHKSLHAGNVLL 137

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK 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 1314926067  20 RLDHSNVVRVIaasTSVPAHQDSLGTIiMEYVGNSTLHHVIYGTGSMAakEREKLSIAqslgysCNIVAGLVFL--HSQL 97
Cdd:cd13990    60 SLDHPRIVKLY---DVFEIDTDSFCTV-LEYCDGNDLDFYLKQHKSIP--EREARSII------MQVVSALKYLneIKPP 127

                          90
                  ....*....|....*....
gi 1314926067  98 IVHLDLKPANVFITEQNVC 116
Cdd:cd13990   128 IIHYDLKPGNILLHSGNVS 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 1314926067  19 ARLDHSNVVRVIAASTSvpahQDSLGtIIMEYVGNSTLHHVIygtgsmaaKEREKLSIAQSLGYSCNIVAGLVFLHSQLI 98
Cdd:cd05123    48 ERVNHPFIVKLHYAFQT----EEKLY-LVLDYVPGGELFSHL--------SKEGRFPEERARFYAAEIVLALEYLHSLGI 114

                          90
                  ....*....|....*
gi 1314926067  99 VHLDLKPANVFITEQ 113
Cdd:cd05123   115 IYRDLKPENILLDSD 129

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 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 1314926067  20 RLDHSNVVRVIAASTSVPAHQDslgTIIMEYVGNSTLHHVI-YGTGSMAAKEREKLSIAQslgyscNIVAGLVFLHSQLI 98
Cdd:cd13988    47 KLNHKNIVKLFAIEEELTTRHK---VLVMELCPCGSLYTVLeEPSNAYGLPESEFLIVLR------DVVAGMNHLRENGI 117

                          90
                  ....*....|
gi 1314926067  99 VHLDLKPANV 108
Cdd:cd13988   118 VHRDIKPGNI 127

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek 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 1314926067  14 AELNAAR-LDHSNVVR-----VIAASTSVpahqdslgTIIMEYVGNSTLHHVIygtgSMAAKEREKLSIAQSLGYSCNIV 87
Cdd:cd08217    48 SEVNILReLKHPNIVRyydriVDRANTTL--------YIVMEYCEGGDLAQLI----KKCKKENQYIPEEFIWKIFTQLL 115

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1314926067  88 AGLVFLH-----SQLIVHLDLKPANVFITEQNV 115
Cdd:cd08217   116 LALYECHnrsvgGGKILHRDLKPANIFLDSDNN 148

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314926067   8 SRQSFWAELNAAR-LDHSNVVRVIAASTSV-PAHqdslgtIIMEYVGNSTLHHViygtgsMAAKEREKLSIAQSLGYSCN 85
Cdd:cd05072    45 SVQAFLEEANLMKtLQHDKLVRLYAVVTKEePIY------IITEYMAKGSLLDF------LKSDEGGKVLLPKLIDFSAQ 112

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1314926067  86 IVAGLVFLHSQLIVHLDLKPANVFITEQNVC 116
Cdd:cd05072   113 IAEGMAYIERKNYIHRDLRAANVLVSESLMC 143

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314926067  15 ELNAARLDHS-NVVRVIAASTsvpAHQDSLGTIIMEYVGNSTLHhVIYG---TGSMAAKEREKLSIAQSlgyscnIVAGL 90
Cdd:cd06621    49 ELEINKSCASpYIVKYYGAFL---DEQDSSIGIAMEYCEGGSLD-SIYKkvkKKGGRIGEKVLGKIAES------VLKGL 118

                          90       100
                  ....*....|....*....|...
gi 1314926067  91 VFLHSQLIVHLDLKPANVFITEQ 113
Cdd:cd06621   119 SYLHSRKIIHRDIKPSNILLTRK 141

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 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 1314926067  20 RLDHSNVVRVIAA--STSVPAHQDSLgTIIMEYVgNSTLHHVIygtgSMAAKEREKLSIAQSLGYSCNIVAGLVFLHSQL 97
Cdd:cd14137    53 RLKHPNIVKLKYFfySSGEKKDEVYL-NLVMEYM-PETLYRVI----RHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLG 126

                          90
                  ....*....|...
gi 1314926067  98 IVHLDLKPANVFI 110
Cdd:cd14137   127 ICHRDIKPQNLLV 139

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek 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 1314926067  20 RLDHSNVVRVIAASTSvpahQDSLgTIIMEYVGNSTLHHVIygtgSMAAKEREKLSIAQSLGYSCNIVAGLVFLHSQLIV 99
Cdd:cd08224    56 QLNHPNIIKYLASFIE----NNEL-NIVLELADAGDLSRLI----KHFKKQKRLIPERTIWKYFVQLCSALEHMHSKRIM 126

                          90
                  ....*....|....*.
gi 1314926067 100 HLDLKPANVFITEQNV 115
Cdd:cd08224   127 HRDIKPANVFITANGV 142