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 1799901130 253 RGTLLYSPPEWIHHQRYHGKAATIWSLGLLLYHLVVGKHPFKRGQEIIWGQIPFPRRLSLECQDVLKRCLSMQPLARPSL 332
Cdd:cd14005   167 DGTRVYSPPEWIRHGRYHGRPATVWSLGILLYDMLCGDIPFENDEQILRGNVLFRPRLSKECCDLISRCLQFDPSKRPSL 246

                  ....*....
gi 1799901130 333 EVLFSEPWL 341
Cdd:cd14005   247 EQILSHPWF 255

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM 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 1799901130 253 RGTLLYSPPEWIHHQRYHGKAATIWSLGLLLYHLVVGKHPFKRGQEIIWGQIPFPRRLSLECQDVLKRCLSMQPLARPSL 332
Cdd:cd14005   167 DGTRVYSPPEWIRHGRYHGRPATVWSLGILLYDMLCGDIPFENDEQILRGNVLFRPRLSKECCDLISRCLQFDPSKRPSL 246

                  ....*....
gi 1799901130 333 EVLFSEPWL 341
Cdd:cd14005   247 EQILSHPWF 255

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799901130  254 GTLLYSPPEWIHHQRYhGKAATIWSLGLLLYHLVVGKHPF----------KRGQEIIWGQIPFPRRLSLECQDVLKRCLS 323
Cdd:smart00220 158 GTPEYMAPEVLLGKGY-GKAVDIWSLGVILYELLTGKPPFpgddqllelfKKIGKPKPPFPPPEWDISPEAKDLIRKLLV 236

                           90
                   ....*....|....*...
gi 1799901130  324 MQPLARPSLEVLFSEPWL 341
Cdd:smart00220 237 KDPEKRLTAEEALQHPFF 254

Serine/threonine protein kinase [Signal transduction mechanisms];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799901130 238 ASIQLDQTLSELERRRGTLLYSPPEwihhqRYHGKAAT----IWSLGLLLYHLVVGKHPFKRG------QEIIWGQIPFP 307
Cdd:COG0515   154 ARALGGATLTQTGTVVGTPGYMAPE-----QARGEPVDprsdVYSLGVTLYELLTGRPPFDGDspaellRAHLREPPPPP 228

                          90       100
                  ....*....|....*....|....*...
gi 1799901130 308 RR----LSLECQDVLKRCLSMQPLARPS 331
Cdd:COG0515   229 SElrpdLPPALDAIVLRALAKDPEERYQ 256

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM 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 1799901130 253 RGTLLYSPPEWIHHQRYHGKAATIWSLGLLLYHLVVGKHPFKRGQEIIWGQIPFPRRLSLECQDVLKRCLSMQPLARPSL 332
Cdd:cd14005   167 DGTRVYSPPEWIRHGRYHGRPATVWSLGILLYDMLCGDIPFENDEQILRGNVLFRPRLSKECCDLISRCLQFDPSKRPSL 246

                  ....*....
gi 1799901130 333 EVLFSEPWL 341
Cdd:cd14005   247 EQILSHPWF 255

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 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 1799901130 254 GTLLYSPPEWIHHQRYHGKAATIWSLGLLLYHLVVGKHPFKRGQEIIWGQIPFPRRLSLECQDVLKRCLSMQPLARPSLE 333
Cdd:cd14100   167 GTRVYSPPEWIRFHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIRGQVFFRQRVSSECQHLIKWCLALRPSDRPSFE 246

                  ....*...
gi 1799901130 334 VLFSEPWL 341
Cdd:cd14100   247 DIQNHPWM 254

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 1799901130 247 SELERRRGTLLYSPPEWIHHQRYHGKAATIWSLGLLLYHLVVGKHPF------KRGQEIIWGQIPFPRRLSLECQDVLKR 320
Cdd:cd14003   153 SLLKTFCGTPAYAAPEVLLGRKYDGPKADVWSLGVILYAMLTGYLPFdddndsKLFRKILKGKYPIPSHLSPDARDLIRR 232

                          90       100
                  ....*....|....*....|
gi 1799901130 321 CLSMQPLARPSLEVLFSEPW 340
Cdd:cd14003   233 MLVVDPSKRITIEEILNHPW 252

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK 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 1799901130 253 RGTLLYSPPEWIHHQRYHGKAATIWSLGLLLYHLVVGKHPFKRGQEIIWGQIPFPRRLSLECQDVLKRCLSMQPLARPSL 332
Cdd:cd14004   168 VGTIDYAAPEVLRGNPYGGKEQDIWALGVLLYTLVFKENPFYNIEEILEADLRIPYAVSEDLIDLISRMLNRDVGDRPTI 247

                  ....*....
gi 1799901130 333 EVLFSEPWL 341
Cdd:cd14004   248 EELLTDPWL 256

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 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 1799901130 238 ASIQLDQTLseLERRRGTLLYSPPEWIHHQRYHGKAATIWSLGLLLYHLVVGKHPF------------KRGQEIIwgqip 305
Cdd:cd14081   148 ASLQPEGSL--LETSCGSPHYACPEVIKGEKYDGRKADIWSCGVILYALLVGALPFdddnlrqllekvKRGVFHI----- 220

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1799901130 306 fPRRLSLECQDVLKRCLSMQPLARPSLEVLFSEPWL 341
Cdd:cd14081   221 -PHFISPDAQDLLRRMLEVNPEKRITIEEIKKHPWF 255

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799901130  254 GTLLYSPPEWIHHQRYhGKAATIWSLGLLLYHLVVGKHPF----------KRGQEIIWGQIPFPRRLSLECQDVLKRCLS 323
Cdd:smart00220 158 GTPEYMAPEVLLGKGY-GKAVDIWSLGVILYELLTGKPPFpgddqllelfKKIGKPKPPFPPPEWDISPEAKDLIRKLLV 236

                           90
                   ....*....|....*...
gi 1799901130  324 MQPLARPSLEVLFSEPWL 341
Cdd:smart00220 237 KDPEKRLTAEEALQHPFF 254

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. 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. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK 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 1799901130 244 QTLSELERRRGTLLYSPPEWIHHQRYHGKAaTIWSLGLLLYHLVVGKHPF------------KRGQEIIwgQIPFPRRLS 311
Cdd:cd14009   146 QPASMAETLCGSPLYMAPEILQFQKYDAKA-DLWSVGAILFEMLVGKPPFrgsnhvqllrniERSDAVI--PFPIAAQLS 222

                          90       100
                  ....*....|....*....|....*....
gi 1799901130 312 LECQDVLKRCLSMQPLARPSLEVLFSEPW 340
Cdd:cd14009   223 PDCKDLLRRLLRRDPAERISFEEFFAHPF 251

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-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 1799901130 254 GTLLYSPPEWIHHQRYHGKAATIWSLGLLLYHLVVGKHPFKRG--QEIIWGQ----IPFPRR---LSLECQDVLKRCLSM 324
Cdd:cd14080   166 GSAAYAAPEILQGIPYDPKKYDIWSLGVILYIMLCGSMPFDDSniKKMLKDQqnrkVRFPSSvkkLSPECKDLIDQLLEP 245

                          90
                  ....*....|....*..
gi 1799901130 325 QPLARPSLEVLFSEPWL 341
Cdd:cd14080   246 DPTKRATIEEILNHPWL 262

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 1799901130 254 GTLLYSPPEWIHHQRYhGKAATIWSLGLLLYHLVVGKHPF--KRGQEIIW----GQIPFPRR----LSLECQDVLKRCLS 323
Cdd:cd05117   163 GTPYYVAPEVLKGKGY-GKKCDIWSLGVILYILLCGYPPFygETEQELFEkilkGKYSFDSPewknVSEEAKDLIKRLLV 241

                          90
                  ....*....|....*..
gi 1799901130 324 MQPLARPSLEVLFSEPW 340
Cdd:cd05117   242 VDPKKRLTAAEALNHPW 258

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799901130 248 ELERRRGTLLYSPPEWIHHQRYHGK--AATIWSLGLLLYHLVVGKHP-----------FKRGQeiiwG---QIPFPRRLS 311
Cdd:cd06626   160 EVNSLVGTPAYMAPEVITGNKGEGHgrAADIWSLGCVVLEMATGKRPwseldnewaimYHVGM----GhkpPIPDSLQLS 235

                          90       100       110
                  ....*....|....*....|....*....|
gi 1799901130 312 LECQDVLKRCLSMQPLARPSLEVLFSEPWL 341
Cdd:cd06626   236 PEGKDFLSRCLESDPKKRPTASELLDHPFI 265

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799901130 219 RRGPLRRKNKPRGDTKSLEASIQLDQTLSELERRRGTLLYSPPEWIHHQ-RYHGKAATIWSLGLLLYHLVVGKHPFKRGQ 297
Cdd:cd14022   113 RKFVFKDEERTRVKLESLEDAYILRGHDDSLSDKHGCPAYVSPEILNTSgSYSGKAADVWSLGVMLYTMLVGRYPFHDIE 192

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1799901130 298 ------EIIWGQIPFPRRLSLECQDVLKRCLSMQPLARPSLEVLFSEPWL 341
Cdd:cd14022   193 psslfsKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPWF 242

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799901130 240 IQLDQTLSELERRRGTLLYSPPEWIHHQRYH---------GKAATIWSLGLLLYHLVVGKHPFKRGQEII---------W 301
Cdd:cd14131   152 IQNDTTSIVRDSQVGTLNYMSPEAIKDTSASgegkpkskiGRPSDVWSLGCILYQMVYGKTPFQHITNPIaklqaiidpN 231

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1799901130 302 GQIPFPRRLSLECQDVLKRCLSMQPLARPSLEVLFSEPWL 341
Cdd:cd14131   232 HEIEFPDIPNPDLIDVMKRCLQRDPKKRPSIPELLNHPFL 271

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799901130 235 SLEASIQLDQTLSELERRRGTLLYSPPEWIHHQR-YHGKAATIWSLGLLLYHLVVGKHPFKRGQ------EIIWGQIPFP 307
Cdd:cd13976   129 SLEDAVILEGEDDSLSDKHGCPAYVSPEILNSGAtYSGKAADVWSLGVILYTMLVGRYPFHDSEpaslfaKIRRGQFAIP 208

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1799901130 308 RRLSLECQDVLKRCLSMQPLARPSLEVLFSEPWL 341
Cdd:cd13976   209 ETLSPRARCLIRSLLRREPSERLTAEDILLHPWL 242

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-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 1799901130 254 GTLLYSPPEWIHHQRyHGKAATIWSLGLLLYHLVVGKHPF------KRGQEIIWGQIPFPRRLSLECQDVLKRCLSMQPL 327
Cdd:cd05580   160 GTPEYLAPEIILSKG-HGKAVDWWALGILIYEMLAGYPPFfdenpmKIYEKILEGKIRFPSFFDPDAKDLIKRLLVVDLT 238

                          90       100
                  ....*....|....*....|..
gi 1799901130 328 AR-----PSLEVLFSEPWLQGV 344
Cdd:cd05580   239 KRlgnlkNGVEDIKNHPWFAGI 260

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799901130 247 SELERRRGTLLYSPPEWIHH--QRYHGKAATIWSLGLLLYHLVVGKHPFKR-------GQEIIWGQIPF----PRRLSLE 313
Cdd:cd14084   168 SLMKTLCGTPTYLAPEVLRSfgTEGYTRAVDCWSLGVILFICLSGYPPFSEeytqmslKEQILSGKYTFipkaWKNVSEE 247

                          90       100
                  ....*....|....*....|....*...
gi 1799901130 314 CQDVLKRCLSMQPLARPSLEVLFSEPWL 341
Cdd:cd14084   248 AKDLVKKMLVVDPSRRPSIEEALEHPWL 275

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-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 1799901130 230 RGDTKSLEASIQLDQTLSelerrrGTLLYSPPEWIHHQRYHGKAATIWSLGLLLYHLVVGKHPF-KRGQEIIWGQIP--- 305
Cdd:cd14162   148 RGVMKTKDGKPKLSETYC------GSYAYASPEILRGIPYDPFLSDIWSMGVVLYTMVYGRLPFdDSNLKVLLKQVQrrv 221

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1799901130 306 -FPRR--LSLECQDVLKRCLSMQPlARPSLEVLFSEPWL 341
Cdd:cd14162   222 vFPKNptVSEECKDLILRMLSPVK-KRITIEEIKRDPWF 259

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 1799901130 254 GTLLYSPPEWIHHQRYhGKAATIWSLGLLLYHLVVGK------HPFKRGQEIiwGQIPFPR-----RLSLECQDVLKRCL 322
Cdd:cd05122   159 GTPYWMAPEVIQGKPY-GFKADIWSLGITAIEMAEGKppyselPPMKALFLI--ATNGPPGlrnpkKWSKEFKDFLKKCL 235

                          90
                  ....*....|....*....
gi 1799901130 323 SMQPLARPSLEVLFSEPWL 341
Cdd:cd05122   236 QKDPEKRPTAEQLLKHPFI 254

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 1799901130 251 RRRGTLLYSPPEWIHHQR-YHGKAATIWSLGLLLYHLVVGKHPFKrGQEII-------WGQIPFPRRLSLECQDVLKRCL 322
Cdd:cd14119   158 TSQGSPAFQPPEIANGQDsFSGFKVDIWSAGVTLYNMTTGKYPFE-GDNIYklfenigKGEYTIPDDVDPDLQDLLRGML 236

                          90
                  ....*....|....*....
gi 1799901130 323 SMQPLARPSLEVLFSEPWL 341
Cdd:cd14119   237 EKDPEKRFTIEQIRQHPWF 255

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to 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 1799901130 254 GTLLYSPPEWIHHQRYHGKAATIWSLGLLLYHLVVGKHPF----------KRGQEIIWGQ--IPFPRRLSLECQDVLKRC 321
Cdd:cd14665   159 GTPAYIAPEVLLKKEYDGKIADVWSCGVTLYVMLVGAYPFedpeeprnfrKTIQRILSVQysIPDYVHISPECRHLISRI 238

                          90
                  ....*....|....*....
gi 1799901130 322 LSMQPLARPSLEVLFSEPW 340
Cdd:cd14665   239 FVADPATRITIPEIRNHEW 257

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-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 1799901130 254 GTLLYSPPEWIHHQRYHGKAATIWSLGLLLYHLVVGKHPF------KRGQEIIWGQIPFPRR--LSLECQDVLKRCLSMQ 325
Cdd:cd14165   168 GSAAYAAPEVLQGIPYDPRIYDIWSLGVILYIMVCGSMPYddsnvkKMLKIQKEHRVRFPRSknLTSECKDLIYRLLQPD 247

                          90
                  ....*....|....*.
gi 1799901130 326 PLARPSLEVLFSEPWL 341
Cdd:cd14165   248 VSQRLCIDEVLSHPWL 263

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. 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 1799901130 254 GTLLYSPPEWIHHQRYHGKAaTIWSLGLLLYHLVVGKHPFKRGQ------EIIWGQI-PFPRRLSLECQDVLKRCLSMQP 326
Cdd:cd08219   162 GTPYYVPPEIWENMPYNNKS-DIWSLGCILYELCTLKHPFQANSwknlilKVCQGSYkPLPSHYSYELRSLIKQMFKRNP 240

                          90
                  ....*....|.
gi 1799901130 327 LARPSLEVLFS 337
Cdd:cd08219   241 RSRPSATTILS 251

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799901130 250 ERRR---GTLLYSPPEWIHHQRYHGKAATIWSLGLLLYHLVVGKHPF-KRGQEIIWGQI-----PFPRRL--SLECQDVL 318
Cdd:cd14099   156 ERKKtlcGTPNYIAPEVLEKKKGHSFEVDIWSLGVILYTLLVGKPPFeTSDVKETYKRIkkneySFPSHLsiSDEAKDLI 235

                          90       100
                  ....*....|....*....|...
gi 1799901130 319 KRCLSMQPLARPSLEVLFSEPWL 341
Cdd:cd14099   236 RSMLQPDPTKRPSLDEILSHPFF 258

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to 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 1799901130 254 GTLLYSPPEWIHHQRYHGKAATIWSLGLLLYHLVVGKHPF----------KRGQEIIWGQ--IPFPRRLSLECQDVLKRC 321
Cdd:cd14662   159 GTPAYIAPEVLSRKEYDGKVADVWSCGVTLYVMLVGAYPFedpddpknfrKTIQRIMSVQykIPDYVRVSQDCRHLLSRI 238

                          90
                  ....*....|....*....
gi 1799901130 322 LSMQPLARPSLEVLFSEPW 340
Cdd:cd14662   239 FVANPAKRITIPEIKNHPW 257

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-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 1799901130 254 GTLLYSPPEWIHHQRYHGKAATIWSLGLLLYHLVVGKHPFK-------RGQEiiwGQIPFPRRLSLE--CQDVLKRCLSM 324
Cdd:cd14164   163 GSRAYTPPEVILGTPYDPKKYDVWSLGVVLYVMVTGTMPFDetnvrrlRLQQ---RGVLYPSGVALEepCRALIRTLLQF 239

                          90
                  ....*....|....*..
gi 1799901130 325 QPLARPSLEVLFSEPWL 341
Cdd:cd14164   240 NPSTRPSIQQVAGNSWL 256

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 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 1799901130 232 DTKSLEASIQLDQTLSELERRR----GTLLYSPPEWIHHQRYhGKAATIWSLGLLLYHLVVGKHPFKRG------QEIIW 301
Cdd:cd05581   154 DSSPESTKGDADSQIAYNQARAasfvGTAEYVSPELLNEKPA-GKSSDLWALGCIIYQMLTGKPPFRGSneyltfQKIVK 232

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1799901130 302 GQIPFPRRLSLECQDVLKRCLSMQPLARPSLEVLFS 337
Cdd:cd05581   233 LEYEFPENFPPDAKDLIQKLLVLDPSKRLGVNENGG 268

NIMA-related protein kinase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799901130 231 GDTKSLEASIQLDQTLSELerrrGTLLYSPPEWIHHQRYhGKAATIWSLGLLLYHLVVGKHPFKRG------QEIIWGQI 304
Cdd:PTZ00267  214 GFSKQYSDSVSLDVASSFC----GTPYYLAPELWERKRY-SKKADMWSLGVILYELLTLHRPFKGPsqreimQQVLYGKY 288