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 372622371  23 PEEVFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVESDLQEIIKEISIMQQCDSPYVVKYYGSYFKNTDLWIVMEYC 102
Cdd:cd06612    1 PEEVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371 103 GAGSVSDIIRLRNKT----------------------------------------------------------------- 117
Cdd:cd06612   81 GAGSVSDIMKITNKTlteeeiaailyqtlkgleylhsnkkihrdikagnillneegqakladfgvsgqltdtmakrntvi 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371 118 ----------------------------------------------AIFMIPTNPPPTFRKPELWSDDFTDFVKKCLVKN 151
Cdd:cd06612  161 gtpfwmapeviqeigynnkadiwslgitaiemaegkppysdihpmrAIFMIPNKPPPTLSDPEKWSPEFNDFVKKCLVKD 240

                        250
                 ....*....|....*.
gi 372622371 152 PEQRATATQLLQHPFI 167
Cdd:cd06612  241 PEERPSAIQLLQHPFI 256

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 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 372622371  23 PEEVFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVESDLQEIIKEISIMQQCDSPYVVKYYGSYFKNTDLWIVMEYC 102
Cdd:cd06612    1 PEEVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371 103 GAGSVSDIIRLRNKT----------------------------------------------------------------- 117
Cdd:cd06612   81 GAGSVSDIMKITNKTlteeeiaailyqtlkgleylhsnkkihrdikagnillneegqakladfgvsgqltdtmakrntvi 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371 118 ----------------------------------------------AIFMIPTNPPPTFRKPELWSDDFTDFVKKCLVKN 151
Cdd:cd06612  161 gtpfwmapeviqeigynnkadiwslgitaiemaegkppysdihpmrAIFMIPNKPPPTLSDPEKWSPEFNDFVKKCLVKD 240

                        250
                 ....*....|....*.
gi 372622371 152 PEQRATATQLLQHPFI 167
Cdd:cd06612  241 PEERPSAIQLLQHPFI 256

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371    27 FDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVE---SDLQEIIKEISIMQQCDSPYVVKYYGSYFKNTDLWIVMEYCG 103
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKkikKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371   104 AGSVSDIIRLR--------------------------------------------------------------------- 114
Cdd:smart00220  81 GGDLFDLLKKRgrlsedearfylrqilsaleylhskgivhrdlkpenilldedghvkladfglarqldpgeklttfvgtp 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371   115 ----------------------------------------NKTAIFMIPTNPPPTFRKPE-LWSDDFTDFVKKCLVKNPE 153
Cdd:smart00220 161 eymapevllgkgygkavdiwslgvilyelltgkppfpgddQLLELFKKIGKPKPPFPPPEwDISPEAKDLIRKLLVKDPE 240

                          250
                   ....*....|....
gi 372622371   154 QRATATQLLQHPFI 167
Cdd:smart00220 241 KRLTAEEALQHPFF 254

C-terminal SARAH domain of mammalian STE20-like protein kinase 2 (MST2); MST2, also called serine/threonine-protein kinase 3, MST-2, STE20-like kinase MST2, or serine/threonine-protein kinase (STK) Krs-1, is a STE20 family stress-activated, pro-apoptotic STK which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. It is a key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. This model corresponds to the C-terminal SARAH (Salvador-RassF-Hippo) domain, which mediates homodimerization of MST2. Similar to MST1, MST2 may also form heterodimers with other SARAH domain-containing proteins.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 372622371 325 DFDFLKNLSLEELQMRLKALDPMMEREIEELRQRYTAKRQPILDAMDAK 373
Cdd:cd21888    1 DFDFLKNLSLEELQMRLKALDPMMEREIEELRQRYTAKRQPILDAMDAK 49

mitogen-activated protein kinase kinase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371   4 PPAPKSKLKKLSEDSLTKQPEE--VFDVLEK---LGEGSYGSVFKAIHKESGQVVAIKQV---PVESDLQEIIKEISIMQ 75
Cdd:PLN00034  48 PPPSSSSSSSSSSSASGSAPSAakSLSELERvnrIGSGAGGTVYKVIHRPTGRLYALKVIygnHEDTVRRQICREIEILR 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371  76 QCDSPYVVKYYGSYFKNTDLWIVMEYCGAGS-----------VSDIIRL-----------------------------RN 115
Cdd:PLN00034 128 DVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSlegthiadeqfLADVARQilsgiaylhrrhivhrdikpsnllinsakNV 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371 116 KTAIF---------MIPTNPPP---TFRKPE-----------------LW------------------------------ 136
Cdd:PLN00034 208 KIADFgvsrilaqtMDPCNSSVgtiAYMSPErintdlnhgaydgyagdIWslgvsilefylgrfpfgvgrqgdwaslmca 287

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 372622371 137 -------------SDDFTDFVKKCLVKNPEQRATATQLLQHPFIKNAKP 172
Cdd:PLN00034 288 icmsqppeapataSREFRHFISCCLQREPAKRWSAMQLLQHPFILRAQP 336

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 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 372622371  23 PEEVFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVESDLQEIIKEISIMQQCDSPYVVKYYGSYFKNTDLWIVMEYC 102
Cdd:cd06612    1 PEEVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371 103 GAGSVSDIIRLRNKT----------------------------------------------------------------- 117
Cdd:cd06612   81 GAGSVSDIMKITNKTlteeeiaailyqtlkgleylhsnkkihrdikagnillneegqakladfgvsgqltdtmakrntvi 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371 118 ----------------------------------------------AIFMIPTNPPPTFRKPELWSDDFTDFVKKCLVKN 151
Cdd:cd06612  161 gtpfwmapeviqeigynnkadiwslgitaiemaegkppysdihpmrAIFMIPNKPPPTLSDPEKWSPEFNDFVKKCLVKD 240

                        250
                 ....*....|....*.
gi 372622371 152 PEQRATATQLLQHPFI 167
Cdd:cd06612  241 PEERPSAIQLLQHPFI 256

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 372622371  25 EVFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVES---DLQEIIKEISIMQQCDSPYVVKYYGSYFKNTDLWIVMEY 101
Cdd:cd06609    1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEEaedEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIMEY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371 102 CGAGSVSDIIR-------------------------------------------------------------LRNKT--- 117
Cdd:cd06609   81 CGGGSVLDLLKpgpldetyiafilrevllgleylhsegkihrdikaanillseegdvkladfgvsgqltstmSKRNTfvg 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371 118 ---------------------------------------------AIFMIPTNPPPTFRKPElWSDDFTDFVKKCLVKNP 152
Cdd:cd06609  161 tpfwmapevikqsgydekadiwslgitaielakgepplsdlhpmrVLFLIPKNNPPSLEGNK-FSKPFKDFVELCLNKDP 239

                        250       260
                 ....*....|....*....|....*...
gi 372622371 153 EQRATATQLLQHPFIKNAKPVSILRDLI 180
Cdd:cd06609  240 KERPSAKELLKHKFIKKAKKTSYLTLLI 267

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 372622371  26 VFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVESDLQE-IIKEISIMQQCDSPYVVKYYGSYFKNTDLWIVMEYCGA 104
Cdd:cd06614    1 LYKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQNKElIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371 105 GSVSDIIRLRNKT------------------------------------------------------------------- 117
Cdd:cd06614   81 GSLTDIITQNPVRmnesqiayvcrevlqgleylhsqnvihrdiksdnillskdgsvkladfgfaaqltkekskrnsvvgt 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371 118 --------------------------------------------AIFMIPTNPPPTFRKPELWSDDFTDFVKKCLVKNPE 153
Cdd:cd06614  161 pywmapevikrkdygpkvdiwslgimciemaegeppyleepplrALFLITTKGIPPLKNPEKWSPEFKDFLNKCLVKDPE 240

                        250
                 ....*....|....*
gi 372622371 154 QRATATQLLQHPFIK 168
Cdd:cd06614  241 KRPSAEELLQHPFLK 255

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 372622371  21 KQPEEVFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVESDLQEIIK-EISIMQQ-CDSPYVVKYYGSYFKNTD---- 94
Cdd:cd06608    2 PDPAGIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEEEIKlEINILRKfSNHPNIATFYGAFIKKDPpggd 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371  95 --LWIVMEYCGAGSVSDIIR-LRNK------------------------------------------------------- 116
Cdd:cd06608   82 dqLWLVMEYCGGGSVTDLVKgLRKKgkrlkeewiayilretlrglaylhenkvihrdikgqnillteeaevklvdfgvsa 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371 117 ---------------------------------------------TAI------------------FMIPTNPPPTFRKP 133
Cdd:cd06608  162 qldstlgrrntfigtpywmapeviacdqqpdasydarcdvwslgiTAIeladgkpplcdmhpmralFKIPRNPPPTLKSP 241

                        250       260       270
                 ....*....|....*....|....*....|....
gi 372622371 134 ELWSDDFTDFVKKCLVKNPEQRATATQLLQHPFI 167
Cdd:cd06608  242 EKWSKEFNDFISECLIKNYEQRPFTEELLEHPFI 275

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371  27 FDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVESDL---QEIIKEISIMQQCDSPYVVKYYGSYFKNTDLWIVMEYCG 103
Cdd:cd06623    3 LERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEefrKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371 104 AGSVSDIIR----------------------------------------LRNK--------------------------- 116
Cdd:cd06623   83 GGSLADLLKkvgkipepvlayiarqilkgldylhtkrhiihrdikpsnlLINSkgevkiadfgiskvlentldqcntfvg 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371 117 TAIFMIP---------------------------TNP-------------------PPTFRKPELWSDDFTDFVKKCLVK 150
Cdd:cd06623  163 TVTYMSPeriqgesysyaadiwslgltllecalgKFPflppgqpsffelmqaicdgPPPSLPAEEFSPEFRDFISACLQK 242

                        250       260
                 ....*....|....*....|
gi 372622371 151 NPEQRATATQLLQHPFIKNA 170
Cdd:cd06623  243 DPKKRPSAAELLQHPFIKKA 262

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 372622371  23 PEEVFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQV-PVESDLQEIIKEISIMQQ-CDSPYVVKYYGSYFK----NTD-L 95
Cdd:cd06638   16 PSDTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILdPIHDIDEEIEAEYNILKAlSDHPNVVKFYGMYYKkdvkNGDqL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371  96 WIVMEYCGAGSVSDII---------------------------------------------------------------- 111
Cdd:cd06638   96 WLVLELCNGGSVTDLVkgflkrgermeepiiayilhealmglqhlhvnktihrdvkgnnilltteggvklvdfgvsaqlt 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371 112 --RLRNKT-----------------------------------------------------AIFMIPTNPPPTFRKPELW 136
Cdd:cd06638  176 stRLRRNTsvgtpfwmapeviaceqqldstydarcdvwslgitaielgdgdppladlhpmrALFKIPRNPPPTLHQPELW 255

                        250       260       270
                 ....*....|....*....|....*....|.
gi 372622371 137 SDDFTDFVKKCLVKNPEQRATATQLLQHPFI 167
Cdd:cd06638  256 SNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286

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 372622371  27 FDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVESDLQE---IIKEISIMQQCDSPYVVKYYGSYFKNTDLWIVMEYCG 103
Cdd:cd06605    3 LEYLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLEIDEALqkqILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371 104 AGSVSDIIR-----------------------LRNK------------------------------------------TA 118
Cdd:cd06605   83 GGSLDKILKevgriperilgkiavavvkgliyLHEKhkiihrdvkpsnilvnsrgqvklcdfgvsgqlvdslaktfvgTR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371 119 IFMIPTN-----------------------------PPPTFRKP--------------------ELWSDDFTDFVKKCLV 149
Cdd:cd06605  163 SYMAPERisggkytvksdiwslglslvelatgrfpyPPPNAKPSmmifellsyivdepppllpsGKFSPDFQDFVSQCLQ 242

                        250
                 ....*....|....*....
gi 372622371 150 KNPEQRATATQLLQHPFIK 168
Cdd:cd06605  243 KDPTERPSYKELMEHPFIK 261

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 372622371  23 PEEVFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVES---DLQEIIKEISIMQQCDSPYVVKYYGSYFKNTDLWIVM 99
Cdd:cd06640    2 PEELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEaedEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371 100 EYCGAGSVSDIIRL--------------------------------------------------------------RNK- 116
Cdd:cd06640   82 EYLGGGSALDLLRAgpfdefqiatmlkeilkgldylhsekkihrdikaanvllseqgdvkladfgvagqltdtqikRNTf 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371 117 ----------------------------TAI------------------FMIPTNPPPTFRKPelWSDDFTDFVKKCLVK 150
Cdd:cd06640  162 vgtpfwmapeviqqsaydskadiwslgiTAIelakgeppnsdmhpmrvlFLIPKNNPPTLVGD--FSKPFKEFIDACLNK 239

                        250       260       270
                 ....*....|....*....|....*....|.
gi 372622371 151 NPEQRATATQLLQHPFI-KNAKPVSILRDLI 180
Cdd:cd06640  240 DPSFRPTAKELLKHKFIvKNAKKTSYLTELI 270

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 372622371  23 PEEVFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPV--ESDLQEIIKEISIMQQCDSPYVVKYYGSYFKNTDLWIVME 100
Cdd:cd06643    3 PEDFWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTksEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371 101 YCGAGSVSDI------------IRL-------------RNK--------------------------------------- 116
Cdd:cd06643   83 FCAGGAVDAVmlelerpltepqIRVvckqtlealvylhENKiihrdlkagnilftldgdikladfgvsakntrtlqrrds 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371 117 ---TAIFMIPT--------------------------------------NP-----------PPTFRKPELWSDDFTDFV 144
Cdd:cd06643  163 figTPYWMAPEvvmcetskdrpydykadvwslgvtliemaqiepphhelNPmrvllkiaksePPTLAQPSRWSPEFKDFL 242

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 372622371 145 KKCLVKNPEQRATATQLLQHPFIKNAKPVSILRDLITEA 183
Cdd:cd06643  243 RKCLEKNVDARWTTSQLLQHPFVSVLVSNKPLRELIAEA 281

C terminal SARAH domain of Mst1; This family of proteins represents the C terminal SARAH domain of Mst1. SARAH controls apoptosis and cell cycle arrest via the Ras, RASSF, MST pathway. The Mst1 SARAH domain interacts with Rassf1 and Rassf5 by forming a heterodimer which mediates the apoptosis process.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 372622371  326 FDFLKNLSLEELQMRLKALDPMMEREIEELRQRYTAKRQPILDAMDAK 373
Cdd:pfam11629   1 FEFLKFLSVDELQQRLANLDPEMEREIEELRKRYQAKRQPILDAIDAK 48

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. 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 372622371  27 FDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPV----ESDLQEIIKEISIMQQCDSPYVVKYYGSYFKNTDLWIVMEYC 102
Cdd:cd08215    2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLsnmsEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEYA 81

                         90
                 ....*....|....*....
gi 372622371 103 GAGSVSDIIRLRNKTAIFM 121
Cdd:cd08215   82 DGGDLAQKIKKQKKKGQPF 100

C-terminal SARAH domain found in the mammalian STE20-like protein kinase (MST) subfamily; The MST subfamily includes MST1 and MST2, as well as Drosophila melanogaster homolog protein, Hippo (Hpo). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 and MST2 are STE20 family stress-activated, pro-apoptotic serine/threonine-protein kinases which, following caspase-cleavage, enter the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. They are key components of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. Hpo, also called STE20-like kinase MST (dMST), is the Drosophila homolog of STE20-like protein kinases, MST1 and MST2. It is a STE20 family serine/threonine-protein kinase that functions as a tumor suppressor by restricting cell proliferation, and promotes apoptosis in conjunction with salvador and warts. Hpo plays a key role in the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. This model corresponds to the C-terminal SARAH (Salvador-RassF-Hippo) domain of mammalian STE20-like protein kinases and the Drosophila melanogaster homolog Hippo.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 372622371 326 FDFLKNLSLEELQMRLKALDPMMEREIEELRQRYTAKRQPILDAMDAK 373
Cdd:cd21884    1 FEFLKSLSYEELQERLALLDPEMEREIEELRKRYQAKRQPILDAIEAK 48

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 372622371  27 FDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVE---SDLQEIIKEISIMQQCDSPYVVKYYGSYFKNTDLWIVMEYCG 103
Cdd:cd06610    3 YELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEkcqTSMDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPLLS 82

                         90
                 ....*....|....*..
gi 372622371 104 AGSVSDIIRLRNKTAIF 120
Cdd:cd06610   83 GGSLLDIMKSSYPRGGL 99

C-terminal SARAH domain of Drosophila melanogaster protein Hippo (Hpo) and similar proteins; Hpo, also called STE20-like kinase MST (dMST), is the Drosophila homolog of STE20-like protein kinases, MST1 and MST2. It is a STE20 family serine/threonine-protein kinase that functions as a tumor suppressor by restricting cell proliferation, and promotes apoptosis in conjunction with salvador and warts. Hpo plays a key role in the Hippo/SWH (Sav/Wts/Hpo) signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. This model corresponds to the C-terminal SARAH (Salvador-RassF-Hippo) domain of Hpo, which mediates complex formation between Hpo and Sav, as well as homodimerization.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 372622371 324 GDFDFLKNLSLEELQMRLKALDPMMEREIEELRQRYTAKRQPILDAMDAKKRRQQN 379
Cdd:cd21889    1 GEFDFLKFLTYDDLNQRLANIDSEMEREIEELNKRYHAKRQPILDAMDAKRKRQQN 56

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora 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 372622371  27 FDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVP----VESDLQEIIK-EISIMQQCDSPYVVKYYGSYFKNTDLWIVMEY 101
Cdd:cd14007    2 FEIGKPLGKGKFGNVYLAREKKSGFIVALKVISksqlQKSGLEHQLRrEIEIQSHLRHPNILRLYGYFEDKKRIYLILEY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371 102 CGAGSVSDIIRLR-----NKTAIFM-------------------------------------------IPTNPPPTFR-- 131
Cdd:cd14007   82 APNGELYKELKKQkrfdeKEAAKYIyqlalaldylhskniihrdikpenillgsngelkladfgwsvhAPSNRRKTFCgt 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372622371 132 ----KPE------------LW---------------------------------------SDDFTDFVKKCLVKNPEQRA 156
Cdd:cd14007  162 ldylPPEmvegkeydykvdIWslgvlcyellvgkppfeskshqetykriqnvdikfpssvSPEAKDLISKLLQKDPSKRL 241

                        250
                 ....*....|..
gi 372622371 157 TATQLLQHPFIK 168
Cdd:cd14007  242 SLEQVLNHPWIK 253

Catalytic domain of Fungal Nak1-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 Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), 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. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 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 372622371  26 VFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVES---DLQEIIKEISIMQQ---CDSPYVVKYYGSYFKNTDLWIVM 99
Cdd:cd06917    2 LYRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLDTdddDVSDIQKEVALLSQlklGQPKNIIKYYGSYLKGPSLWIIM 81

                         90
                 ....*....|...
gi 372622371 100 EYCGAGSVSDIIR 112
Cdd:cd06917   82 DYCEGGSIRTLMR 94

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 372622371  27 FDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVP----VESDLQEIIKEISIMQQCDSPYVVKYYGSYFKNTDLWIVMEYC 102
Cdd:cd14003    2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDksklKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYA 81

                         90       100
                 ....*....|....*....|....
gi 372622371 103 GAGSVSDII----RLRNKTA--IF 120
Cdd:cd14003   82 SGGELFDYIvnngRLSEDEArrFF 105

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 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 372622371  21 KQPEEVFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVE--SDLQEIIKEISIMQQCDSPYVVKYYGSYFKNTDLWIV 98
Cdd:cd06645    7 RNPQEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEpgEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWIC 86