Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 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 14165272 162 IGKGCSAAVYEATMptlpqnlevtkstgllpgrgpgtsapgegqerapgapaFPLAIKMMWNISAGSSSEAILNTMSQEL 241
Cdd:cd14018   1 IGKGCNAAVYEAAL--------------------------------------FPLAIKMMWNISAGSSSEAILRSMGNEL 42

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 242 VPASRVALAGEYGAVTYRKSKRGPKQLAPHPNIIRVLRAFTSSVPLLPGALVDYPDVLPSRLHPEGLGHGRTLFLVMKNY 321
Cdd:cd14018  43 VPAPNVALLGEYGEVTRLGLQNGRKLLAPHPNIIRVQRAFTDSVPLLPGAIEDYPDVLPARLNPSGLGHNRTLFLVMKNY 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 322 PCTLRQYLCVNTPSPRLAAMMLLQLLEGVDHLVQQGIAHRDLKSDNILVELDPDGCPWLVIADFGCCLADESIGLQLPFS 401
Cdd:cd14018 123 PCTLRQYLWVNTPSYRLARVMILQLLEGVDHLVRHGIAHRDLKSDNILLELDFDGCPWLVIADFGCCLADDSIGLQLPFS 202

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 402 SWYVDRGGNGCLMAPEVSTARPGPRAVIDYSKADAWAVGAIAYEIFGLVNPFYGQGKAHLESRSYQEAQLPALPESVPPD 481
Cdd:cd14018 203 SWYVDRGGNACLMAPEVSTAVPGPGVVINYSKADAWAVGAIAYEIFGLSNPFYGLGDTMLESRSYQESQLPALPSAVPPD 282

                       330       340       350
                ....*....|....*....|....*....|.
gi 14165272 482 VRQLVRALLQREASKRPSARVAANVLHLSLW 512
Cdd:cd14018 283 VRQVVKDLLQRDPNKRVSARVAANVLHLSLW 313

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 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 14165272 162 IGKGCSAAVYEATMptlpqnlevtkstgllpgrgpgtsapgegqerapgapaFPLAIKMMWNISAGSSSEAILNTMSQEL 241
Cdd:cd14018   1 IGKGCNAAVYEAAL--------------------------------------FPLAIKMMWNISAGSSSEAILRSMGNEL 42

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 242 VPASRVALAGEYGAVTYRKSKRGPKQLAPHPNIIRVLRAFTSSVPLLPGALVDYPDVLPSRLHPEGLGHGRTLFLVMKNY 321
Cdd:cd14018  43 VPAPNVALLGEYGEVTRLGLQNGRKLLAPHPNIIRVQRAFTDSVPLLPGAIEDYPDVLPARLNPSGLGHNRTLFLVMKNY 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 322 PCTLRQYLCVNTPSPRLAAMMLLQLLEGVDHLVQQGIAHRDLKSDNILVELDPDGCPWLVIADFGCCLADESIGLQLPFS 401
Cdd:cd14018 123 PCTLRQYLWVNTPSYRLARVMILQLLEGVDHLVRHGIAHRDLKSDNILLELDFDGCPWLVIADFGCCLADDSIGLQLPFS 202

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 402 SWYVDRGGNGCLMAPEVSTARPGPRAVIDYSKADAWAVGAIAYEIFGLVNPFYGQGKAHLESRSYQEAQLPALPESVPPD 481
Cdd:cd14018 203 SWYVDRGGNACLMAPEVSTAVPGPGVVINYSKADAWAVGAIAYEIFGLSNPFYGLGDTMLESRSYQESQLPALPSAVPPD 282

                       330       340       350
                ....*....|....*....|....*....|.
gi 14165272 482 VRQLVRALLQREASKRPSARVAANVLHLSLW 512
Cdd:cd14018 283 VRQVVKDLLQRDPNKRVSARVAANVLHLSLW 313

Serine/threonine protein kinase [Signal transduction mechanisms];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 271 HPNIIRVLRAFTssvpllpgalvdypdvlpsrlhpeglgHGRTLFLVMKNYP-CTLRQYLCVNTP-SPRLAAMMLLQLLE 348
Cdd:COG0515  66 HPNIVRVYDVGE---------------------------EDGRPYLVMEYVEgESLADLLRRRGPlPPAEALRILAQLAE 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 349 GVDHLVQQGIAHRDLKSDNILVelDPDGCPwlVIADFGCCLADESIGLQLPFSSW----YvdrggngclMAPE-VSTARP 423
Cdd:COG0515 119 ALAAAHAAGIVHRDIKPANILL--TPDGRV--KLIDFGIARALGGATLTQTGTVVgtpgY---------MAPEqARGEPV 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 424 GPRavidyskADAWAVGAIAYEIFGLVNPFYGQGKAHLESRSYQEAQLP--ALPESVPPDVRQLVRALLQREASKRP-SA 500
Cdd:COG0515 186 DPR-------SDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPpsELRPDLPPALDAIVLRALAKDPEERYqSA 258

                ....*...
gi 14165272 501 RVAANVLH 508
Cdd:COG0515 259 AELAAALR 266

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272   348 EGVDHLVQQGIAHRDLKSDNILVELDPdgcpwLV-IADFGccLADesigLQLPFSSWYVDRGGNGCL--MAPEvstarpg 424
Cdd:pfam07714 113 KGMEYLESKNFVHRDLAARNCLVSENL-----VVkISDFG--LSR----DIYDDDYYRKRGGGKLPIkwMAPE------- 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272   425 praVIDY----SKADAWAVGAIAYEIFGL-VNPFYGQGKAHLESRSYQEAQLPAlPESVPPDVRQLVRALLQREASKRPS 499
Cdd:pfam07714 175 ---SLKDgkftSKSDVWSFGVLLWEIFTLgEQPYPGMSNEEVLEFLEDGYRLPQ-PENCPDELYDLMKQCWAYDPEDRPT 250

                  ..
gi 14165272   500 AR 501
Cdd:pfam07714 251 FS 252

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 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 14165272 162 IGKGCSAAVYEATMptlpqnlevtkstgllpgrgpgtsapgegqerapgapaFPLAIKMMWNISAGSSSEAILNTMSQEL 241
Cdd:cd14018   1 IGKGCNAAVYEAAL--------------------------------------FPLAIKMMWNISAGSSSEAILRSMGNEL 42

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 242 VPASRVALAGEYGAVTYRKSKRGPKQLAPHPNIIRVLRAFTSSVPLLPGALVDYPDVLPSRLHPEGLGHGRTLFLVMKNY 321
Cdd:cd14018  43 VPAPNVALLGEYGEVTRLGLQNGRKLLAPHPNIIRVQRAFTDSVPLLPGAIEDYPDVLPARLNPSGLGHNRTLFLVMKNY 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 322 PCTLRQYLCVNTPSPRLAAMMLLQLLEGVDHLVQQGIAHRDLKSDNILVELDPDGCPWLVIADFGCCLADESIGLQLPFS 401
Cdd:cd14018 123 PCTLRQYLWVNTPSYRLARVMILQLLEGVDHLVRHGIAHRDLKSDNILLELDFDGCPWLVIADFGCCLADDSIGLQLPFS 202

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 402 SWYVDRGGNGCLMAPEVSTARPGPRAVIDYSKADAWAVGAIAYEIFGLVNPFYGQGKAHLESRSYQEAQLPALPESVPPD 481
Cdd:cd14018 203 SWYVDRGGNACLMAPEVSTAVPGPGVVINYSKADAWAVGAIAYEIFGLSNPFYGLGDTMLESRSYQESQLPALPSAVPPD 282

                       330       340       350
                ....*....|....*....|....*....|.
gi 14165272 482 VRQLVRALLQREASKRPSARVAANVLHLSLW 512
Cdd:cd14018 283 VRQVVKDLLQRDPNKRVSARVAANVLHLSLW 313

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 14165272 271 HPNIIRVLRAFTSsvpllpgalvdypdvlpsrlhpeglghGRTLFLVMKNYP-CTLRQYLCVN--TPSPRLAAMMLLQLL 347
Cdd:cd00180  50 HPNIVKLYDVFET---------------------------ENFLYLVMEYCEgGSLKDLLKENkgPLSEEEALSILRQLL 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 348 EGVDHLVQQGIAHRDLKSDNILVeldpDGCPWLVIADFGCCLADESIGLQLPFSSWyvdrGGNGCLMAPEVSTARPgpra 427
Cdd:cd00180 103 SALEYLHSNGIIHRDLKPENILL----DSDGTVKLADFGLAKDLDSDDSLLKTTGG----TTPPYYAPPELLGGRY---- 170

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14165272 428 viDYSKADAWAVGAIAYEIfglvnpfygqgkahlesrsyqeaqlpalpesvpPDVRQLVRALLQREASKRPSAR 501
Cdd:cd00180 171 --YGPKVDIWSLGVILYEL---------------------------------EELKDLIRRMLQYDPKKRPSAK 209

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 14165272 349 GVDHLVQQGIAHRDLKSDNILveLDPDGcpWLVIADFGccLADESIglqlpfsswyvdRGGNGC--------LMAPEVST 420
Cdd:cd05123 105 ALEYLHSLGIIYRDLKPENIL--LDSDG--HIKLTDFG--LAKELS------------SDGDRTytfcgtpeYLAPEVLL 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 421 ARPgpravidYSKA-DAWAVGAIAYE-IFGLVnPFYGQGKAHLEsRSYQEAQLpALPESVPPDVRQLVRALLQREASKRP 498
Cdd:cd05123 167 GKG-------YGKAvDWWSLGVLLYEmLTGKP-PFYAENRKEIY-EKILKSPL-KFPEYVSPEAKSLISGLLQKDPTKRL 236

                ....*
gi 14165272 499 SARVA 503
Cdd:cd05123 237 GSGGA 241

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 271 HPNIIRVLRAFTssvpllpgalvdypdvlpsrlhpeglgHGRTLFLVMKNYP-CTLRQYLCVNTP-SPRLAAMMLLQLLE 348
Cdd:cd14014  59 HPNIVRVYDVGE---------------------------DDGRPYIVMEYVEgGSLADLLRERGPlPPREALRILAQIAD 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 349 GVDHLVQQGIAHRDLKSDNILveLDPDGcpWLVIADFGCCLADESIGLQlpfsswyvdRGGNGCL----MAPE-VSTARP 423
Cdd:cd14014 112 ALAAAHRAGIVHRDIKPANIL--LTEDG--RVKLTDFGIARALGDSGLT---------QTGSVLGtpayMAPEqARGGPV 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 424 GPRavidyskADAWAVGAIAYEIFGLVNPFYGQGKAHLESRSYQEA--QLPALPESVPPDVRQLVRALLQREASKRP-SA 500
Cdd:cd14014 179 DPR-------SDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAppPPSPLNPDVPPALDAIILRALAKDPEERPqSA 251

                ....*...
gi 14165272 501 RVAANVLH 508
Cdd:cd14014 252 AELLAALR 259

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 14165272 349 GVDHLVQQGIAHRDLKSDNILveLDPDGCpwLVIADFGccladesIGLQL----PFSSWYVdrgGNGCLMAPEVSTARPg 424
Cdd:cd08215 115 ALKYLHSRKILHRDLKTQNIF--LTKDGV--VKLGDFG-------ISKVLesttDLAKTVV---GTPYYLSPELCENKP- 179

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 425 pravidYS-KADAWAVGAIAYEIFGLVNPFYGQgkaHLESRSYQ--EAQLPALPESVPPDVRQLVRALLQREASKRPSAR 501
Cdd:cd08215 180 ------YNyKSDIWALGCVLYELCTLKHPFEAN---NLPALVYKivKGQYPPIPSQYSSELRDLVNSMLQKDPEKRPSAN 250

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 348 EGVDHLVQQGIAHRDLKSDNILVElDPDGCPWLVIADFGccLA---DESIGLQLPFSSWYvdrggngcLMAPEVSTARPg 424
Cdd:cd05117 110 SAVAYLHSQGIVHRDLKPENILLA-SKDPDSPIKIIDFG--LAkifEEGEKLKTVCGTPY--------YVAPEVLKGKG- 177

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 425 pravidYSKA-DAWAVGAIAYEIFGLVNPFYG-----------QGKAHLESRSYQeaqlpalpeSVPPDVRQLVRALLQR 492
Cdd:cd05117 178 ------YGKKcDIWSLGVILYILLCGYPPFYGeteqelfekilKGKYSFDSPEWK---------NVSEEAKDLIKRLLVV 242

                ....*....
gi 14165272 493 EASKRPSAR 501
Cdd:cd05117 243 DPKKRLTAA 251

Serine/threonine protein kinase [Signal transduction mechanisms];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 271 HPNIIRVLRAFTssvpllpgalvdypdvlpsrlhpeglgHGRTLFLVMKNYP-CTLRQYLCVNTP-SPRLAAMMLLQLLE 348
Cdd:COG0515  66 HPNIVRVYDVGE---------------------------EDGRPYLVMEYVEgESLADLLRRRGPlPPAEALRILAQLAE 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 349 GVDHLVQQGIAHRDLKSDNILVelDPDGCPwlVIADFGCCLADESIGLQLPFSSW----YvdrggngclMAPE-VSTARP 423
Cdd:COG0515 119 ALAAAHAAGIVHRDIKPANILL--TPDGRV--KLIDFGIARALGGATLTQTGTVVgtpgY---------MAPEqARGEPV 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 424 GPRavidyskADAWAVGAIAYEIFGLVNPFYGQGKAHLESRSYQEAQLP--ALPESVPPDVRQLVRALLQREASKRP-SA 500
Cdd:COG0515 186 DPR-------SDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPpsELRPDLPPALDAIVLRALAKDPEERYqSA 258

                ....*...
gi 14165272 501 RVAANVLH 508
Cdd:COG0515 259 AELAAALR 266

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in 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 14165272 349 GVDHLVQQGIAHRDLKSDNILVELDpdgcpWLVIADFG-CCLADESIGLQLPFSswyvdrgGNGCLMAPEVSTARpgpra 427
Cdd:cd08222 118 AVQYMHERRILHRDLKAKNIFLKNN-----VIKVGDFGiSRILMGTSDLATTFT-------GTPYYMSPEVLKHE----- 180

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14165272 428 viDY-SKADAWAVGAIAYEIFGLVNPFYGQGkahLESRSYQ--EAQLPALPESVPPDVRQLVRALLQREASKRPSA 500
Cdd:cd08222 181 --GYnSKSDIWSLGCILYEMCCLKHAFDGQN---LLSVMYKivEGETPSLPDKYSKELNAIYSRMLNKDPALRPSA 251

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 14165272 355 QQGIAHRDLKSDNILveLDPDGCPWLviADFGCC--LADESIglqlpFSSWYVdrgGNGCLMAPEVSTARPgpravidYS 432
Cdd:cd08217 128 GGKILHRDLKPANIF--LDSDNNVKL--GDFGLArvLSHDSS-----FAKTYV---GTPYYMSPELLNEQS-------YD 188

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14165272 433 -KADAWAVGAIAYEIFGLVNPFYGQGKAHLESRsYQEAQLPALPESVPPDVRQLVRALLQREASKRPSA 500
Cdd:cd08217 189 eKSDIWSLGCLIYELCALHPPFQAANQLELAKK-IKEGKFPRIPSRYSSELNEVIKSMLNVDPDKRPSV 256

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 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 14165272 356 QGIAHRDLKSDNILVELDPDGCP-----WLVIADFGCC--LADESIGLQLPFSSWYvdrggngclMAPEVSTARpgprav 428
Cdd:cd14120 111 KGIVHRDLKPQNILLSHNSGRKPspndiRLKIADFGFArfLQDGMMAATLCGSPMY---------MAPEVIMSL------ 175

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14165272 429 iDY-SKADAWAVGAIAYEIFGLVNPFYGQGKAHLESRSYQEAQL-PALPESVPPDVRQLVRALLQREASKR 497
Cdd:cd14120 176 -QYdAKADLWSIGTIVYQCLTGKAPFQAQTPQELKAFYEKNANLrPNIPSGTSPALKDLLLGLLKRNPKDR 245

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK 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 14165272 350 VDHLVQQGIAHRDLKSDNILveLDPDGcpWLVIADFGccLADEsiglqlpFSSWYVDRGGNGC----LMAPEVstARPGP 425
Cdd:cd05583 112 LEHLHKLGIIYRDIKLENIL--LDSEG--HVVLTDFG--LSKE-------FLPGENDRAYSFCgtieYMAPEV--VRGGS 176

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14165272 426 RAvidYSKA-DAWAVGAIAYEIFGLVNPFYGQGKAHLE---SRSYQEAQlPALPESVPPDVRQLVRALLQREASKR 497
Cdd:cd05583 177 DG---HDKAvDWWSLGVLTYELLTGASPFTVDGERNSQseiSKRILKSH-PPIPKTFSAEAKDFILKLLEKDPKKR 248

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 349 GVDHLVQQGIAHRDLKSDNILveLDPDGcpWLVIADFGCClaDESIglqlpfssWYVDRGGNGC----LMAPEVSTARPG 424
Cdd:cd05570 108 ALQFLHERGIIYRDLKLDNVL--LDAEG--HIKIADFGMC--KEGI--------WGGNTTSTFCgtpdYIAPEILREQDY 173

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14165272 425 PRAVidyskaDAWAVGAIAYEIFGLVNPFYGQGKAHL-ESRSYQEaqlPALPESVPPDVRQLVRALLQREASKR 497
Cdd:cd05570 174 GFSV------DWWALGVLLYEMLAGQSPFEGDDEDELfEAILNDE---VLYPRWLSREAVSILKGLLTKDPARR 238

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 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 14165272 357 GIAHRDLKSDNILveLDPDGCPwlVIADFG-CCLAD---ESIGLQLPFSSWYVDRggngCLM---APEVSTARPGprAVI 429
Cdd:cd13986 129 PYAHRDIKPGNVL--LSEDDEP--ILMDLGsMNPARieiEGRREALALQDWAAEH----CTMpyrAPELFDVKSH--CTI 198

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 430 DySKADAWAVGAIAYEIFGLVNPF---YGQGKahlesrSYQEAQLPAL-----PESVPPDVRQLVRALLQREASKRPSAR 501
Cdd:cd13986 199 D-EKTDIWSLGCTLYALMYGESPFeriFQKGD------SLALAVLSGNysfpdNSRYSEELHQLVKSMLVVNPAERPSID 271

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK 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 14165272 352 HLVQQGIAHRDLKSDNILveLDPDGcpWLVIADFGCCLADESIGlqlpfsswyvDRGGNGC----LMAPEVSTARPGPRA 427
Cdd:cd05575 111 YLHSLNIIYRDLKPENIL--LDSQG--HVVLTDFGLCKEGIEPS----------DTTSTFCgtpeYLAPEVLRKQPYDRT 176

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14165272 428 VidyskaDAWAVGAIAYE-IFGLvNPFYGQGKAHLESRSYQEaQLpALPESVPPDVRQLVRALLQREASKR 497
Cdd:cd05575 177 V------DWWCLGAVLYEmLYGL-PPFYSRDTAEMYDNILHK-PL-RLRTNVSPSARDLLEGLLQKDRTKR 238

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (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. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 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 14165272 348 EGVDHLVQQGIAHRDLKSDNILVELDPDgcpwLVIADFGccLADEsigLQLpFSSWYVDRGGNGC--LMAPEVStarpgp 425
Cdd:cd14119 108 DGLEYLHSQGIIHKDIKPGNLLLTTDGT----LKISDFG--VAEA---LDL-FAEDDTCTTSQGSpaFQPPEIA------ 171

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14165272 426 RAVIDYS--KADAWAVGAIAYEIFGLVNPFYGQGKAHL-ESRSYQEAQlpaLPESVPPDVRQLVRALLQREASKRPS 499
Cdd:cd14119 172 NGQDSFSgfKVDIWSAGVTLYNMTTGKYPFEGDNIYKLfENIGKGEYT---IPDDVDPDLQDLLRGMLEKDPEKRFT 245

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK 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 14165272 350 VDHLVQQGIAHRDLKSDNILVElDPDGCP-WLVIADFGccLADesiglQLpfsswyvdRGGNGCLM---------APEVs 419
Cdd:cd14091 107 VEYLHSQGVVHRDLKPSNILYA-DESGDPeSLRICDFG--FAK-----QL--------RAENGLLMtpcytanfvAPEV- 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 420 TARPGpravidYSKA-DAWAVGAIAYEIFGLVNPF--------------YGQGKAHLESRSYqeaqlpalpESVPPDVRQ 484
Cdd:cd14091 170 LKKQG------YDAAcDIWSLGVLLYTMLAGYTPFasgpndtpevilarIGSGKIDLSGGNW---------DHVSDSAKD 234

                       170
                ....*....|....*.
gi 14165272 485 LVRALLQREASKRPSA 500
Cdd:cd14091 235 LVRKMLHVDPSQRPTA 250

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 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 14165272 348 EGVDHLVQQGIAHRDLKSDNILVELDPdgcPWLV-IADFGccLADESIGlqlpfSSWYVDRGGNGCLMAPEV--STARPG 424
Cdd:cd14098 112 EAMAYTHSMGITHRDLKPENILITQDD---PVIVkISDFG--LAKVIHT-----GTFLVTFCGTMAYLAPEIlmSKEQNL 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14165272 425 PRAvidYS-KADAWAVGAIAYEIFGLVNPFYGQGKAHLESR----SYQEAqlPALPESVPPDVRQLVRALLQREASKRPS 499
Cdd:cd14098 182 QGG---YSnLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRirkgRYTQP--PLVDFNISEEAIDFILRLLDVDPEKRMT 256

                ....*.
gi 14165272 500 ARVAAN 505
Cdd:cd14098 257 AAQALD 262