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 1398130412   1 MKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHS 80
Cdd:cd14126    35 MKSRAPQLHLEYRFYKLLGQAEGLPQVYYFGPCGKYNAMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRIEYVHS 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130412  81 KNLIYRDVKPENFLIGRPGNKTQQVIHIIDFGLAKEYIDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEAL 160
Cdd:cd14126   115 KHLIYRDVKPENFLIGRQSTKKQHVIHIIDFGLAKEYIDPETNKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEAL 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130412 161 GHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFP-EMATYLRYVRRLDFFEKPDYDYLRKLFTDLFDR 239
Cdd:cd14126   195 GHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFPeEMATYLRYVRRLDFFETPDYDYLRKLFTDLFDR 274

                         250
                  ....*....|....
gi 1398130412 240 KGYMFDYEYDWIGK 253
Cdd:cd14126   275 KGYTDDYEFDWTGK 288

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. CK1gamma proteins are unique within the CK1 subfamily in that they are palmitoylated at the C-termini and are anchored to the plasma membrane. CK1gamma is involved in transducing the signaling of LDL-receptor-related protein 6 (LRP6) through direct phosphorylation following Wnt stimulation, resulting in the recruitment of the scaffold protein Axin. In Xenopus embryos, CK1gamma is required during anterio-posterior patterning. In higher vertebrates, three CK1gamma (gamma1-3) isoforms exist. In mammalian cells, CK1gamma2 has been implicated in regulating the synthesis of sphingomyelin, a phospholipid that is found in the outer leaflet of the plasma membrane, by hyperphosphorylating and inactivating the ceramide transfer protein CERT. CK1gamma2 also phosphorylates the transcription factor Smad-3 resulting in its ubiquitination and degradation. It inhibits Smad-3 mediated responses of Transforming Growth Factor-beta (TGF-beta) including cell growth arrest. The CK1 gamma 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 1398130412   1 MKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHS 80
Cdd:cd14126    35 MKSRAPQLHLEYRFYKLLGQAEGLPQVYYFGPCGKYNAMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRIEYVHS 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130412  81 KNLIYRDVKPENFLIGRPGNKTQQVIHIIDFGLAKEYIDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEAL 160
Cdd:cd14126   115 KHLIYRDVKPENFLIGRQSTKKQHVIHIIDFGLAKEYIDPETNKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEAL 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130412 161 GHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFP-EMATYLRYVRRLDFFEKPDYDYLRKLFTDLFDR 239
Cdd:cd14126   195 GHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFPeEMATYLRYVRRLDFFETPDYDYLRKLFTDLFDR 274

                         250
                  ....*....|....
gi 1398130412 240 KGYMFDYEYDWIGK 253
Cdd:cd14126   275 KGYTDDYEFDWTGK 288

putative serine/threonine kinase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130412  23 GIPQvyYFGpCG--KYNAM-----VLELLGPSLEDLFDLCdRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLI 95
Cdd:PHA02882   84 GIPK--YYG-CGsfKRCRMyyrfiLLEKLVENTKEIFKRI-KCKNKKLIKNIMKDMLTTLEYIHEHGISHGDIKPENIMV 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130412  96 grpgnKTQQVIHIIDFGLAKEYIdpETKKHIPY-REHKSL-TGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLP 173
Cdd:PHA02882  160 -----DGNNRGYIIDYGIASHFI--IHGKHIEYsKEQKDLhRGTLYYAGLDAHNGACVTRRGDLESLGYCMLKWAGIKLP 232

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398130412 174 WQGLKADTLKERYQKIGDTKRATPIEVLCENFPE-MATYLRYVRRLDFFEKPDYDYLRKLF 233
Cdd:PHA02882  233 WKGFGHNGNLIHAAKCDFIKRLHEGKIKIKNANKfIYDFIECVTKLSYEEKPDYDALIKIF 293

Casein kinase 1 gamma C terminal; This domain family is found in eukaryotes, and is typically between 54 and 99 amino acids in length. The family is found in association with pfam00069. CK1gamma is a membrane-bound member of the CK1 family. Gain-of-function and loss-of-function experiments show that CK1gamma is both necessary and sufficient to transduce LRP6 signalling in vertebrates and Drosophila cells.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130412 253 KQLPTPVGAVQ-QDPALSSNREAHQHRDKM----------QQSKN------------------------------QVVSS 291
Cdd:pfam12605   1 KPMPTPVGSLQtSESAVSPSREAHIGVSRPplpqprrvsqQGSKGrkgawppptpqtnaetlgshlpadrhggsvQVVSS 80

                          90
                  ....*....|....*....
gi 1398130412 292 TNGELNTDDPTAGRSNAPI 310
Cdd:pfam12605  81 TNGELNTDDPTAGHSNAPI 99

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 1398130412  39 MVLELL-GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKE- 116
Cdd:pfam07714  78 IVTEYMpGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENL-----VVKISDFGLSRDi 152

                  ....*....
gi 1398130412 117 YIDPETKKH 125
Cdd:pfam07714 153 YDDDYYRKR 161

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. CK1gamma proteins are unique within the CK1 subfamily in that they are palmitoylated at the C-termini and are anchored to the plasma membrane. CK1gamma is involved in transducing the signaling of LDL-receptor-related protein 6 (LRP6) through direct phosphorylation following Wnt stimulation, resulting in the recruitment of the scaffold protein Axin. In Xenopus embryos, CK1gamma is required during anterio-posterior patterning. In higher vertebrates, three CK1gamma (gamma1-3) isoforms exist. In mammalian cells, CK1gamma2 has been implicated in regulating the synthesis of sphingomyelin, a phospholipid that is found in the outer leaflet of the plasma membrane, by hyperphosphorylating and inactivating the ceramide transfer protein CERT. CK1gamma2 also phosphorylates the transcription factor Smad-3 resulting in its ubiquitination and degradation. It inhibits Smad-3 mediated responses of Transforming Growth Factor-beta (TGF-beta) including cell growth arrest. The CK1 gamma 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 1398130412   1 MKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHS 80
Cdd:cd14126    35 MKSRAPQLHLEYRFYKLLGQAEGLPQVYYFGPCGKYNAMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRIEYVHS 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130412  81 KNLIYRDVKPENFLIGRPGNKTQQVIHIIDFGLAKEYIDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEAL 160
Cdd:cd14126   115 KHLIYRDVKPENFLIGRQSTKKQHVIHIIDFGLAKEYIDPETNKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEAL 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130412 161 GHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFP-EMATYLRYVRRLDFFEKPDYDYLRKLFTDLFDR 239
Cdd:cd14126   195 GHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFPeEMATYLRYVRRLDFFETPDYDYLRKLFTDLFDR 274

                         250
                  ....*....|....
gi 1398130412 240 KGYMFDYEYDWIGK 253
Cdd:cd14126   275 KGYTDDYEFDWTGK 288

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. The delta and epsilon isoforms of CK1 play important roles in circadian rhythm and cell growth. They phosphorylate PERIOD proteins (PER1-3), which are circadian clock proteins that fulfill negative regulatory functions. PER phosphorylation leads to its degradation. However, CRY proteins form a complex with PER and CK1delta/epsilon that protects PER from degradation and leads to nuclear accummulation of the complex, which inhibits BMAL1-CLOCK dependent transcription activation. CK1delta/epsilon also phosphorylate the tumor suppressor p53 and the cellular oncogene Mdm2, which are key regulators of cell growth, genome integrity, and the development of cancer. This subfamily also includes the CK1 fungal proteins Saccharomyces cerevisiae HRR25 and Schizosaccharomyces pombe HHP1. These fungal proteins are involved in DNA repair. The CK1 delta/epsilon 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 1398130412   2 KSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSK 81
Cdd:cd14125    36 KTKHPQLLYESKLYKILQGGVGIPNVRWYGVEGDYNVMVMDLLGPSLEDLFNFCSRKFSLKTVLMLADQMISRIEYVHSK 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130412  82 NLIYRDVKPENFLIGRpGNKTQQViHIIDFGLAKEYIDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALG 161
Cdd:cd14125   116 NFIHRDIKPDNFLMGL-GKKGNLV-YIIDFGLAKKYRDPRTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLG 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130412 162 HMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFP-EMATYLRYVRRLDFFEKPDYDYLRKLFTDLFDRK 240
Cdd:cd14125   194 YVLMYFNRGSLPWQGLKAATKKQKYEKISEKKMSTPIEVLCKGFPsEFATYLNYCRSLRFDDKPDYSYLRRLFRDLFHRE 273

                  ..
gi 1398130412 241 GY 242
Cdd:cd14125   274 GF 275

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. CK1alpha plays a role in cell cycle progression, spindle dynamics, and chromosome segregation. It is also involved in regulating apoptosis mediated by Fas or the retinoid X receptor (RXR), and is a positive regulator of Wnt signaling. CK1alpha phosphorylates the NS5A protein of flaviviruses such as the Hepatitis C virus (HCV) and yellow fever virus (YFV), and influences flaviviral replication. The CK1 alpha 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 1398130412   1 MKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHS 80
Cdd:cd14128    35 QKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMIGRIEYVHN 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130412  81 KNLIYRDVKPENFL--IGRPGNKtqqvIHIIDFGLAKEYIDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLE 158
Cdd:cd14128   115 KNFIHRDIKPDNFLmgIGRHCNK----LFLIDFGLAKKYRDSRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDME 190

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130412 159 ALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFP-EMATYLRYVRRLDFFEKPDYDYLRKLF 233
Cdd:cd14128   191 SLGYVLMYFNRGSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPaEFAMYLNYCRGLRFEEAPDYMYLRQLF 266

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins (VRK1, VRK2, and VRK3) while invertebrates, specifically fruit flies and nematodes, seem to carry only a single ortholog. Mutations of VRK in Drosophila and Caenorhabditis elegans showed varying phenotypes ranging from embryonic lethality to mitotic and meiotic defects resulting in sterility. In vertebrates, VRK1 is implicated in cell cycle progression and proliferation, nuclear envelope assembly, and chromatin condensation. VRK2 is involved in modulating JNK signaling. VRK3 is an inactive pseudokinase that inhibits ERK signaling. The VRK 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 1398130412  23 GIPQVYYFG----PCGKYNAMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrp 98
Cdd:cd14015    84 GIPRYIGSGsheyKGEKYRFLVMPRFGRDLQKIFEKNGKRFPEKTVLQLALRILDVLEYIHENGYVHADIKASNLLLG-- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130412  99 GNKTQQVIHIIDFGLAKEYIDpeTKKHIPYRE--HKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQG 176
Cdd:cd14015   162 FGKNKDQVYLVDYGLASRYCP--NGKHKEYKEdpRKAHNGTIEFTSRDAHKGVAPSRRGDLEILGYNMLQWLCGKLPWED 239

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1398130412 177 LKADTLKERYQKIgdtKRATPI-EVLCENFP------EMATYLRYVRRLDFFEKPDYDYLRKLF 233
Cdd:cd14015   240 NLKNPEYVQKQKE---KYMDDIpLLLKKCFPgkdvpeELQKYLKYVASLEYEEKPDYEKLRKIL 300

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Genetic variations in TTBK1 are linked to Alzheimer's disease (AD). Hyperphosphorylated tau is a major component of paired helical filaments that accumulate in the brain of AD patients. Studies in transgenic mice show that TTBK1 is involved in the phosphorylation-dependent pathogenic aggregation of tau. The TTBK1 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 1398130412   8 LHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLGPSLEDLFDLCDR-TFSLKTVLMIAIQLISRMEYVHSKNLIYR 86
Cdd:cd14130    42 LKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGRNLADLRRSQPRgTFTLSTTLRLGKQILESIEAIHSVGFLHR 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130412  87 DVKPENFLIGRPGNkTQQVIHIIDFGLAKEYIDpETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMY 166
Cdd:cd14130   122 DIKPSNFAMGRLPS-TYRKCYMLDFGLARQYTN-TTGEVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVE 199

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398130412 167 FLRGSLPWQGLKADtlkeryQKIGDTKRATPIEVLCENFP-EMATYLRYVRRLDFFEKPDYDYLRKLF 233
Cdd:cd14130   200 FAVGQLPWRKIKDK------EQVGMIKEKYEHRMLLKHMPsEFHLFLDHIASLDYFTKPDYQLIMSVF 261

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 1398130412  11 EYRFYKQLgSGDGIPQVYYFGPCGKYNAMVLELL-GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVK 89
Cdd:cd00180    41 EIEILKKL-NHPNIVKLYDVFETENFLYLVMEYCeGGSLKDLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLK 119

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398130412  90 PENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKHIPYRehkslTGTARYMSINTHLGKEQSRRDDLEALGHMFMYF 167
Cdd:cd00180   120 PENILLDSDGT-----VKLADFGLAKDLDSDDSLLKTTGG-----TTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL 187

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 1398130412  11 EYRFYKQLgSGDGIPQVYYFGPCGKYNAMVLELL-GPSLEDLFDLcDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVK 89
Cdd:cd14014    50 EARALARL-SHPNIVRVYDVGEDDGRPYIVMEYVeGGSLADLLRE-RGPLPPREALRILAQIADALAAAHRAGIVHRDIK 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130412  90 PENFLIGRPGNktqqvIHIIDFGLAKEyIDPETKKHIpyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLR 169
Cdd:cd14014   128 PANILLTEDGR-----VKLTDFGIARA-LGDSGLTQT-----GSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLT 196

                  ....*..
gi 1398130412 170 GSLPWQG 176
Cdd:cd14014   197 GRPPFDG 203

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins. VRK2 exists as two alternative splice forms, A and B, which differ in their C-terminal regions. VRK2A, the predominant isoform, contains a hydrophobic tail and is anchored to the ER and mitochondria. It is expressed in all cell types. VRK2B lacks a membrane-anchor tail and is detected in the cytosol and the nucleus. Like VRK1, it can stabilize p53. VRK2B functionally replaces VRK1 in the nucleus of cell types where VRK1 is absent. VRK2 modulates hypoxia-induced stress responses by interacting with TAK1, an atypical MAPK kinase kinase which triggers cascades that activate JNK following oxidative stress. VRK2 also interacts with JIP1, a scaffold protein that assembles three consecutive members of a MAPK pathway. This interaction prevents the association of JNK with the signaling complex, leading to reduced phosphorylation and AP1-dependent transcription. The VRK2 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 1398130412  35 KYNAMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnKTQQVIHIIDFGLA 114
Cdd:cd14123   102 SYRFMVMDRLGTDLQKILIDNGGQFKKTTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGY---RNPNEVYLADYGLS 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130412 115 KEYIdpETKKHIPYREH--KSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW----------QGLKADTL 182
Cdd:cd14123   179 YRYC--PNGNHKEYKENprKGHNGTIEFTSLDAHKGVAPSRRGDLEILGYCMLHWLCGKLPWeqnlknpvavQEAKAKLL 256

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1398130412 183 KERYQKIgdTKRATPIEVLCenfpEMATYLRYVRRLDFFEKPDYDYLRKLFT 234
Cdd:cd14123   257 SNLPDSV--LKWSTGGSSSM----EIAQFLSRVKDLAYDEKPDYQALKKILS 302

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130412    1 MKSRAPQLHLEYRFYKQLGSgDGIPQVYYFGPCGKYNAMVLELLgpSLEDLFDLCDR--TFSLKTVLMIAIQLISRMEYV 78
Cdd:smart00220  37 IKKDRERILREIKILKKLKH-PNIVRLYDVFEDEDKLYLVMEYC--EGGDLFDLLKKrgRLSEDEARFYLRQILSALEYL 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130412   79 HSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETkkhipyreHKSLTGTARYMSINTHLGKEQSRRDDLE 158
Cdd:smart00220 114 HSKGIVHRDLKPENILLDEDGH-----VKLADFGLARQLDPGEK--------LTTFVGTPEYMAPEVLLGKGYGKAVDIW 180

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1398130412  159 ALGHMFMYFLRGSLPWQGlkADTLKERYQKIGDTKRATPIE 199
Cdd:smart00220 181 SLGVILYELLTGKPPFPG--DDQLLELFKKIGKPKPPFPPP 219

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 1398130412  39 MVLELL--GpsleDLFDLCDR--TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLA 114
Cdd:cd05123    70 LVLDYVpgG----ELFSHLSKegRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGH-----IKLTDFGLA 140

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398130412 115 KEYIDPETKKHipyrehkSLTGTARYMSINTHLGKEQSRRDDLEALGHMfMY-FLRGSLPWQglkADTLKERYQKI 189
Cdd:cd05123   141 KELSSDGDRTY-------TFCGTPEYLAPEVLLGKGYGKAVDWWSLGVL-LYeMLTGKPPFY---AENRKEIYEKI 205

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-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 1398130412  57 RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDpetkkhipyrEHKSLTG 136
Cdd:cd05612    96 GRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGH-----IKLTDFGFAKKLRD----------RTWTLCG 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130412 137 TARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKERYQKIgdtkratpievlcenfpeMATYLRYVR 216
Cdd:cd05612   161 TPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFD---DNPFGIYEKI------------------LAGKLEFPR 219

                         170       180
                  ....*....|....*....|....*...
gi 1398130412 217 RLDFFEKpdyDYLRKLFT-DLFDRKGYM 243
Cdd:cd05612   220 HLDLYAK---DLIKKLLVvDRTRRLGNM 244

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 1398130412  50 DLFDLCDRT--FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKeYIDPETkkhip 127
Cdd:cd05580    87 ELFSLLRRSgrFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGH-----IKITDFGFAK-RVKDRT----- 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130412 128 yrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWqglKADTLKERYQKI--GDTKratpievlcenF 205
Cdd:cd05580   156 ----YTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPF---FDENPMKIYEKIleGKIR-----------F 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398130412 206 PEmatylryvrrldFFEKPDYDYLRKLFT-DLFDRKGYM-----------FDYEYDWIG---KQLPTPVGAVQQDPALSS 270
Cdd:cd05580   218 PS------------FFDPDAKDLIKRLLVvDLTKRLGNLkngvediknhpWFAGIDWDAllqRKIPAPYVPKVRGPGDTS 285

                  .
gi 1398130412 271 N 271
Cdd:cd05580   286 N 286

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK 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 1398130412  35 KYNAMVLEL-LGpslEDLFD-LCDR-TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDF 111
Cdd:cd05572    66 KYLYMLMEYcLG---GELWTiLRDRgLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNG-----YVKLVDF 137

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398130412 112 GLAKeYIDPETKKHipyrehkSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKeRYQKI 189
Cdd:cd05572   138 GFAK-KLGSGRKTW-------TFCGTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDPMK-IYNII 206

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 1398130412  39 MVLELLgpSLEDLFDLCDRT--FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrpgnkTQQVIHIIDFGLAke 116
Cdd:cd14007    77 LILEYA--PNGELYKELKKQkrFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLG-----SNGELKLADFGWS-- 147

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1398130412 117 yidpetkKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGhMFMY-FLRGSLPWqglKADTLKERYQKI 189
Cdd:cd14007   148 -------VHAPSNRRKTFCGTLDYLPPEMVEGKEYDYKVDIWSLG-VLCYeLLVGKPPF---ESKSHQETYKRI 210

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; 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. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 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 1398130412  53 DLCD-----RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLI----GRPGNKTQQVIHIIDFGLAKeYIDPETK 123
Cdd:cd14202    87 DLADylhtmRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLsysgGRKSNPNNIRIKIADFGFAR-YLQNNMM 165

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398130412 124 KhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLC 202
Cdd:cd14202   166 A-------ATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKNKSLSPNIPRETSS 237