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 20071571  33 LAPEIITAT-------QYKKCDEFQTGILIYEMLHLPNPF--DENPELKEKEYTRTDLPRIPLRSPYSwgLQQLASCLLN 103
Cdd:cd14018 215 MAPEVSTAVpgpgvviNYSKADAWAVGAIAYEIFGLSNPFygLGDTMLESRSYQESQLPALPSAVPPD--VRQVVKDLLQ 292

                        90       100
                ....*....|....*....|.
gi 20071571 104 PNPSERILISDAKGILQCLLW 124
Cdd:cd14018 293 RDPNKRVSARVAANVLHLSLW 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 20071571  33 LAPEIITAT-------QYKKCDEFQTGILIYEMLHLPNPF--DENPELKEKEYTRTDLPRIPLRSPYSwgLQQLASCLLN 103
Cdd:cd14018 215 MAPEVSTAVpgpgvviNYSKADAWAVGAIAYEIFGLSNPFygLGDTMLESRSYQESQLPALPSAVPPD--VRQVVKDLLQ 292

                        90       100
                ....*....|....*....|.
gi 20071571 104 PNPSERILISDAKGILQCLLW 124
Cdd:cd14018 293 RDPNKRVSARVAANVLHLSLW 313

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071571     33 LAPEIITATQY-KKCDEFQTGILIYEMLHLPNPFDENPELKE--KEYTRTDLPRIPLRSPYSWGLQQLASCLLNPNPSER 109
Cdd:smart00220 163 MAPEVLLGKGYgKAVDIWSLGVILYELLTGKPPFPGDDQLLElfKKIGKPKPPFPPPEWDISPEAKDLIRKLLVKDPEKR 242

                           90
                   ....*....|.
gi 20071571    110 IlisDAKGILQ 120
Cdd:smart00220 243 L---TAEEALQ 250

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 20071571  33 LAPEIITAT-------QYKKCDEFQTGILIYEMLHLPNPF--DENPELKEKEYTRTDLPRIPLRSPYSwgLQQLASCLLN 103
Cdd:cd14018 215 MAPEVSTAVpgpgvviNYSKADAWAVGAIAYEIFGLSNPFygLGDTMLESRSYQESQLPALPSAVPPD--VRQVVKDLLQ 292

                        90       100
                ....*....|....*....|.
gi 20071571 104 PNPSERILISDAKGILQCLLW 124
Cdd:cd14018 293 RDPNKRVSARVAANVLHLSLW 313

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071571     33 LAPEIITATQY-KKCDEFQTGILIYEMLHLPNPFDENPELKE--KEYTRTDLPRIPLRSPYSWGLQQLASCLLNPNPSER 109
Cdd:smart00220 163 MAPEVLLGKGYgKAVDIWSLGVILYELLTGKPPFPGDDQLLElfKKIGKPKPPFPPPEWDISPEAKDLIRKLLVKDPEKR 242

                           90
                   ....*....|.
gi 20071571    110 IlisDAKGILQ 120
Cdd:smart00220 243 L---TAEEALQ 250

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. 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 20071571  33 LAPEIITATQYK-KCDEFQTGILIYEMLHLPNPF--DENPELKEKeYTRTDLPRIPLRspYSWGLQQLASCLLNPNPSER 109
Cdd:cd08530 168 AAPEVWKGRPYDyKSDIWSLGCLLYEMATFRPPFeaRTMQELRYK-VCRGKFPPIPPV--YSQDLQQIIRSLLQVNPKKR 244

                        90
                ....*....|.
gi 20071571 110 ILISDakgILQ 120
Cdd:cd08530 245 PSCDK---LLQ 252

NIMA-related protein kinase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071571   33 LAPEIITATQY-KKCDEFQTGILIYEMLHLPNPF---DENPELKEKEYTRTDlpriPLRSPYSWGLQQLASCLLNPNPSE 108
Cdd:PTZ00267 238 LAPELWERKRYsKKADMWSLGVILYELLTLHRPFkgpSQREIMQQVLYGKYD----PFPCPVSSGMKALLDPLLSKNPAL 313

                 .
gi 20071571  109 R 109
Cdd:PTZ00267 314 R 314

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. 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 MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE 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 20071571  33 LAPEIITATQY-KKCDEFQTGILIYEMLHLPNPFDENPELKEKEYTRTDLPrIPLRSPYSWG--LQQLASCLLNPNPSER 109
Cdd:cd05122 164 MAPEVIQGKPYgFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNGP-PGLRNPKKWSkeFKDFLKKCLQKDPEKR 242

serine/threonine protein kinase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071571   33 LAPEIITATQY-KKCDEFQTGILIYEMLHLPNPFD-EN-PELKEKEYT-RTDlpriPLRSPYSWGLQQLASCLLNPNPSE 108
Cdd:PTZ00283 212 VAPEIWRRKPYsKKADMFSLGVLLYELLTLKRPFDgENmEEVMHKTLAgRYD----PLPPSISPEMQEIVTALLSSDPKR 287

                 .
gi 20071571  109 R 109
Cdd:PTZ00283 288 R 288

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 20071571  33 LAPEIITATQY-KKCDEFQTGILIYEMLHLPNPFdENPELKEKeYTRTDLPRIPLRSPYSWGLQQLASCLLNPNPSERIL 111
Cdd:cd14007 165 LPPEMVEGKEYdYKVDIWSLGVLCYELLVGKPPF-ESKSHQET-YKRIQNVDIKFPSSVSPEAKDLISKLLQKDPSKRLS 242

                ....*
gi 20071571 112 ISDAK 116
Cdd:cd14007 243 LEQVL 247

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta 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 20071571  33 LAPEIITATQYK-KCDEFQTGILIYEMLHLPNPFD---ENPELKEKEYTRTDLPRIPLRSPYSWGLQ--QLASCLLNPNP 106
Cdd:cd05617 183 IAPEILRGEEYGfSVDWWALGVLMFEMMAGRSPFDiitDNPDMNTEDYLFQVILEKPIRIPRFLSVKasHVLKGFLNKDP 262

                ....
gi 20071571 107 SERI 110
Cdd:cd05617 263 KERL 266

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20071571  33 LAPEIITATQY-KKCDEFQTGILIYEMLHLPNPF-DENPE-----LKEKEYTRTDLPRIplrspySWGLQQLASCLLNPN 105
Cdd:cd05579 175 LAPEILLGQGHgKTVDWWSLGVILYEFLVGIPPFhAETPEeifqnILNGKIEWPEDPEV------SDEAKDLISKLLTPD 248

                        90
                ....*....|...
gi 20071571 106 PSERIlisDAKGI 118
Cdd:cd05579 249 PEKRL---GAKGI 258

Catalytic domain of Yeast Protein Kinase 1-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 fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-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 20071571  33 LAPEIITATQYKKCDEFQT-GILIYEMLH-LPNPFDEN-PELKEKEYTRtdlpriPLRSP--YSWGLQQLASCLLNPNPS 107
Cdd:cd05585 161 LAPELLLGHGYTKAVDWWTlGVLLYEMLTgLPPFYDENtNEMYRKILQE------PLRFPdgFDRDAKDLLIGLLNRDPT 234

                        90
                ....*....|.
gi 20071571 108 ERILISDAKGI 118
Cdd:cd05585 235 KRLGYNGAQEI 245

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; 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. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 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 20071571  33 LAPEIITATQY-KKCDEFQTGILIYEMLHLPNPFDENP--ELKEKeyTRTDLP-RIPLRSPYSWGLQQLASCLLNPNPSE 108
Cdd:cd14121 163 MAPEMILKKKYdARVDLWSVGVILYECLFGRAPFASRSfeELEEK--IRSSKPiEIPTRPELSADCRDLLLRLLQRDPDR 240

                ..
gi 20071571 109 RI 110
Cdd:cd14121 241 RI 242

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 20071571  33 LAPEIITATQY-KKCDEFQTGILIYEMLHLPNPFDE--NPELKEKEYTRTDLPRIPLRSPYSWGlQQLASClLNPNPSER 109
Cdd:cd13999 158 MAPEVLRGEPYtEKADVYSFGIVLWELLTGEVPFKElsPIQIAAAVVQKGLRPPIPPDCPPELS-KLIKRC-WNEDPEKR 235

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 20071571  33 LAPEIITATQYK-KCDEFQTGILIYEMLHLPNPF-DENPELKE--KEYTRTDLPriPLRSP-YSWGLQQLASCLLNPNPS 107
Cdd:cd08224 171 MSPERIREQGYDfKSDIWSLGCLLYEMAALQSPFyGEKMNLYSlcKKIEKCEYP--PLPADlYSQELRDLVAACIQPDPE 248

                ....*...
gi 20071571 108 ERILISDA 115
Cdd:cd08224 249 KRPDISYV 256

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta 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
                ....*....|....*....|....*....|....*....|....*....|....
gi 20071571  33 LAPEIITATQYK-KCDEFQTGILIYEMLHLPNPFDENPELKEKEYTRTDLPRIP 85
Cdd:cd05620 163 IAPEILQGLKYTfSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYP 216

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 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 20071571  33 LAPEIITATQYK-KCDEFQTGILIYEMLHLPNPFDENPELKEKEYTRTDLPRIPLRSPYsW-----GLQQLASCLLNPNP 106
Cdd:cd14184 167 VAPEIIAETGYGlKVDIWAAGVITYILLCGFPPFRSENNLQEDLFDQILLGKLEFPSPY-WdnitdSAKELISHMLQVNV 245

                ...
gi 20071571 107 SER 109
Cdd:cd14184 246 EAR 248

Catalytic domain of Numb-Associated Kinase (NAK)-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 Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It 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. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-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 20071571  14 QAKQKSHLVDPQILRD---QSRlAPEIITATQYK----KCDEFQTGILIYEMLHLPNPFDENPEL--KEKEYTrtdlprI 84
Cdd:cd14037 165 QTKQGVTYVEEDIKKYttlQYR-APEMIDLYRGKpiteKSDIWALGCLLYKLCFYTTPFEESGQLaiLNGNFT------F 237

                        90       100
                ....*....|....*....|....*
gi 20071571  85 PLRSPYSWGLQQLASCLLNPNPSER 109
Cdd:cd14037 238 PDNSRYSKRLHKLIRYMLEEDPEKR 262

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. 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 20071571  33 LAPEIITATQYK-KCDEFQTGILIYEMLHLPNPF---DENPELKEKEYTRTDLPRIPlRSPYSWGLQQLASCLLNPNPSE 108
Cdd:cd08229 195 MSPERIHENGYNfKSDIWSLGCLLYEMAALQSPFygdKMNLYSLCKKIEQCDYPPLP-SDHYSEELRQLVNMCINPDPEK 273

                .
gi 20071571 109 R 109
Cdd:cd08229 274 R 274