Tudor domain found in Tudor domain-containing protein 8 (TDRD8) and similar proteins; TDRD8, also called serine/threonine-protein kinase (EC 2.7.11.1) 31 (STK31), serine/threonine-protein kinase NYD-SPK, or Sugen kinase 396 (SgK396), is a germ cell-specific factor expressed in embryonic gonocytes of both sexes, and in postnatal spermatocytes and round spermatids in males. It acts as a cell-cycle regulated protein that contributes to the tumorigenicity of epithelial cancer cells. TDRD8 contains a Tudor domain and a serine/threonine kinase domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034656310  65 IGCSLSEVCPQASSVLGNLDPNKIYGGLFSEDQCWYRCKVLKIISVEKCLVRYIDYGNTEILNRSDIVEIPLELQ 139
Cdd:cd20430     1 LSDELAEVCPTAPPLFGTPDPNKIYGGKFSEDNCWYRCKVKSILSDEKCTVQYIDYGNTETVSRSSIVELPPDLQ 75

Protein kinase domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656310 703 KSVSQRASVNMMVGDLSLMSPELKMGKPASPGSDLYAYGCLL---------LWLSVQNQEFEINKDGIPKVDQF--HLDD 771
Cdd:pfam00069 109 EGLESGSSLTTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILyelltgkppFPGINGNEIYELIIDQPYAFPELpsNLSE 188

                          90       100
                  ....*....|....*....|....*
gi 1034656310 772 KVKSLLCSLICYRSS--MTAEQVLN 794
Cdd:pfam00069 189 EAKDLLKKLLKKDPSkrLTATQALQ 213

Tudor domain found in Tudor domain-containing protein 8 (TDRD8) and similar proteins; TDRD8, also called serine/threonine-protein kinase (EC 2.7.11.1) 31 (STK31), serine/threonine-protein kinase NYD-SPK, or Sugen kinase 396 (SgK396), is a germ cell-specific factor expressed in embryonic gonocytes of both sexes, and in postnatal spermatocytes and round spermatids in males. It acts as a cell-cycle regulated protein that contributes to the tumorigenicity of epithelial cancer cells. TDRD8 contains a Tudor domain and a serine/threonine kinase domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034656310  65 IGCSLSEVCPQASSVLGNLDPNKIYGGLFSEDQCWYRCKVLKIISVEKCLVRYIDYGNTEILNRSDIVEIPLELQ 139
Cdd:cd20430     1 LSDELAEVCPTAPPLFGTPDPNKIYGGKFSEDNCWYRCKVKSILSDEKCTVQYIDYGNTETVSRSSIVELPPDLQ 75

Serine/threonine protein kinase [Signal transduction mechanisms];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656310 628 DPMAYLMVPYYPRANLNA-VQANMPLNSEETLKVMKGVAQGLHTLHKADIIHGSLHQNNVFaLNREQGI-VGDFDFTKSV 705
Cdd:COG0515    79 DGRPYLVMEYVEGESLADlLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANIL-LTPDGRVkLIDFGIARAL 157

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1034656310 706 --SQRASVNMMVGDLSLMSPELKMGKPASPGSDLYAYGCLLLWL 747
Cdd:COG0515   158 ggATLTQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYEL 201

Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in the Drosophila Tudor protein. Initial proposal that the survival motor neuron gene product contain a Tudor domain are corroborated by more recent database search techniques such as PSI-BLAST (unpublished).

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1034656310   93 FSEDQCWYRCKVLKIISVEKCLVRYIDYGNTEILNRSDIVEIPLEL 138
Cdd:smart00333  12 RWEDGEWYRARIVKVDGEQLYEVFFIDYGNEEVVPPSDLRQLPEEL 57

Stk1 family PASTA domain-containing Ser/Thr kinase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656310 646 VQANMPLNSEETLKVMKGVAQGLHTLHKADIIHGSLHQNNVfaLNREQGI--VGDFDFTKSVSQrASV---NMMVGDLSL 720
Cdd:NF033483   98 IREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNI--LITKDGRvkVTDFGIARALSS-TTMtqtNSVLGTVHY 174

                          90       100
                  ....*....|....*....|....
gi 1034656310 721 MSPELKMGKPASPGSDLYAYGCLL 744
Cdd:NF033483  175 LSPEQARGGTVDARSDIYSLGIVL 198

serine/threonine kinase US3; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656310 630 MAYLMVPYYpRANLN---AVQANMPLNseETLKVMKGVAQGLHTLHKADIIHGSLHQNNVFALNREQGIVGDFD---FTK 703
Cdd:PHA03212  157 FTCLILPRY-KTDLYcylAAKRNIAIC--DILAIERSVLRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGaacFPV 233

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034656310 704 SVSQRASVNmMVGDLSLMSPELKMGKPASPGSDLYAYGCLLLWLSV-QNQEFEinKDGI 761
Cdd:PHA03212  234 DINANKYYG-WAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATcHDSLFE--KDGL 289

Tudor domain found in Tudor domain-containing protein 8 (TDRD8) and similar proteins; TDRD8, also called serine/threonine-protein kinase (EC 2.7.11.1) 31 (STK31), serine/threonine-protein kinase NYD-SPK, or Sugen kinase 396 (SgK396), is a germ cell-specific factor expressed in embryonic gonocytes of both sexes, and in postnatal spermatocytes and round spermatids in males. It acts as a cell-cycle regulated protein that contributes to the tumorigenicity of epithelial cancer cells. TDRD8 contains a Tudor domain and a serine/threonine kinase domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034656310  65 IGCSLSEVCPQASSVLGNLDPNKIYGGLFSEDQCWYRCKVLKIISVEKCLVRYIDYGNTEILNRSDIVEIPLELQ 139
Cdd:cd20430     1 LSDELAEVCPTAPPLFGTPDPNKIYGGKFSEDNCWYRCKVKSILSDEKCTVQYIDYGNTETVSRSSIVELPPDLQ 75

Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar proteins; dTUD is required during oogenesis for the formation of primordial germ cells and for normal abdominal segmentation. It contains 11 Tudor domains. The family also includes mitochondrial A-kinase anchor protein 1 (AKAP1) and Tudor domain-containing proteins (TDRDs). AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), or dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), or protein kinase A-anchoring protein 1 (PRKA1), or Spermatid A-kinase anchor protein 84 (S-AKAP84), is found in mitochondria and in the endoplasmic reticulum-nuclear envelope where it anchors protein kinases, phosphatases, and a phosphodiesterase. It regulates multiple cellular processes governing mitochondrial homeostasis and cell viability. AKAP1 binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane. TDRDs have diverse biological functions and may contain one or more copies of the Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034656310  85 PNKIYGGLFSEDQCWYRCKVLKIISVEKCLVRYIDYGNTEILNRSDIVEI 134
Cdd:cd20379     1 VGDLCAAKYEEDGKWYRARVLEVLSNDKVEVFFVDYGNTETVPLSDLRPL 50

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 1034656310 628 DPMAYLMVPYYPRANLNAV-QANMPLNSEETLKVMKGVAQGLHTLHKADIIHGSLHQNNVFALNREQGIVGDFDFTKSV- 705
Cdd:cd14014    72 DGRPYIVMEYVEGGSLADLlRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALg 151

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1034656310 706 -SQRASVNMMVGDLSLMSPELKMGKPASPGSDLYAYGCLLLWL 747
Cdd:cd14014   152 dSGLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYEL 194

Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, also called Staphylococcal nuclease domain-containing protein 1 (SND1), 100 kDa coactivator, EBNA2 coactivator p100, or p100 co-activator, is a multifunctional protein that is reportedly associated with different types of RNA molecules, including mRNA, miRNA, pre-miRNA, and dsRNA. It has been implicated in a number of biological processes in eukaryotic cells, including the cell cycle, DNA damage repair, proliferation, and apoptosis. TDRD11 is overexpressed in multiple cancers and functions as an oncogene. It contains multiple Staphylococcal nuclease (SN) domains and a C-terminal Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1034656310  93 FSEDQCWYRCKVLKIISVEKCLVRYIDYGNTEILNRSDIVEIPLEL 138
Cdd:cd20433    38 FVEDGEWYRAKVEKVEGDKKVHVLYIDYGNREVLPSTRLAALPPAF 83

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 1034656310 623 FLCKSDPmaYLMVPYYPRANLNAV--QANMPLNSEETLKVMKGVAQGLHTLHKADIIHGSLHQNNVfALNREQGI-VGDF 699
Cdd:cd05122    66 YLKKDEL--WIVMEFCSGGSLKDLlkNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANI-LLTSDGEVkLIDF 142

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1034656310 700 DFTKSVSQRASVNMMVGDLSLMSPELKMGKPASPGSDLYAYGCLLL 745
Cdd:cd05122   143 GLSAQLSDGKTRNTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAI 188

fifth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the fifth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656310  38 EDVVGSHIEDAVTFWAQsINRNKDIM-KIGCSLSEVCPQASSVLGNLDPNKIYGGLFSeDQCWYRCKVLKIISVEKclVR 116
Cdd:cd20424    14 EEVYITYVNDPWTFYCQ-LARNAGVLdQLASAISRLSSEIRKLELSVNPGTLCLAKYS-DQHWYRGIIITNKNSTE--VF 89

                          90       100
                  ....*....|....*....|...
gi 1034656310 117 YIDYGNTEILNRSDIVEIPLELQ 139
Cdd:cd20424    90 FVDYGNTEKVEKEDMLPIPSDAY 112

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656310  632 YLMVPYYPRANLNAV-QANMPLNSEETLKVMKGVAQGLHTLHKADIIHGSLHQNNVFaLNrEQGIV--GDFDFTKSVSQR 708
Cdd:smart00220  73 YLVMEYCEGGDLFDLlKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENIL-LD-EDGHVklADFGLARQLDPG 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656310  709 ASVNMMVGDLSLMSPELKMGKPASPGSDLYAYGCLL--------LWLSVQNQE--FEINKDGIPKVDQFH--LDDKVKSL 776
Cdd:smart00220 151 EKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILyelltgkpPFPGDDQLLelFKKIGKPKPPFPPPEwdISPEAKDL 230

                          170       180
                   ....*....|....*....|....
gi 1034656310  777 LCSLICYRSS--MTAEQVLNAECF 798
Cdd:smart00220 231 IRKLLVKDPEkrLTAEEALQHPFF 254

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. 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 1034656310 647 QANMPLNSEETLKVMKGVAQGLHTLHKADIIHGSLHQNNVFALNREQGIVGDFDFTKSVSQRASVNM-MVGDLSLMSPEL 725
Cdd:cd08529    93 QRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTNFAQtIVGTPYYLSPEL 172

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1034656310 726 KMGKPASPGSDLYAYGCLLLWLSVQNQEFEINKDG 760
Cdd:cd08529   173 CEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQG 207

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 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 1034656310 621 FLFLCKSDPMAYLMVPYYPRANL-NAVQANMPLNSEETLKVMKGVAQGLHTLHKADIIHGSLHQNNVFALNREQGIVGDF 699
Cdd:cd14059    46 FKGVCTQAPCYCILMEYCPYGQLyEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDF 125

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1034656310 700 DFTKSVSQRASVNMMVGDLSLMSPELKMGKPASPGSDLYAYGcLLLW 746
Cdd:cd14059   126 GTSKELSEKSTKMSFAGTVAWMAPEVIRNEPCSEKVDIWSFG-VVLW 171

fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the fifth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656310  96 DQCWYRCKVLKIISVE--KCLVRYIDYGNTEILNRSDIVEIPLEL-QFSSVAKKYKLWGLHIPSDQEVTQ 162
Cdd:cd20418    16 DGKWYRAKLLSILEFNpvKILVRHVDYGSTAALPTSRLRQIPAELmQYPCQAIKVKLAGFKPPLNDSETE 85

Stk1 family PASTA domain-containing Ser/Thr kinase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656310 646 VQANMPLNSEETLKVMKGVAQGLHTLHKADIIHGSLHQNNVfaLNREQGI--VGDFDFTKSVSQrASV---NMMVGDLSL 720
Cdd:NF033483   98 IREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNI--LITKDGRvkVTDFGIARALSS-TTMtqtNSVLGTVHY 174

                          90       100
                  ....*....|....*....|....
gi 1034656310 721 MSPELKMGKPASPGSDLYAYGCLL 744
Cdd:NF033483  175 LSPEQARGGTVDARSDIYSLGIVL 198

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 1034656310 651 PLNSEETLKVMKGVAQGLHTLHKADIIHGSLHQNNVFALNREQGIVGDFDFTKsVSQRASVNMMVGDLSLMSPELKMGKP 730
Cdd:cd08530    99 LFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISK-VLKKNLAKTQIGTPLYAAPEVWKGRP 177

                          90
                  ....*....|....
gi 1034656310 731 ASPGSDLYAYGCLL 744
Cdd:cd08530   178 YDYKSDIWSLGCLL 191

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656310 647 QANMPLNSEETLKVMKGVAQGLHTLHKADIIHGSLHQNNVFaLNREQGI-VGDFDFTKSVSQRASV-NMMVGDLSLMSPE 724
Cdd:cd08215    95 KKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIF-LTKDGVVkLGDFGISKVLESTTDLaKTVVGTPYYLSPE 173

                          90       100
                  ....*....|....*....|
gi 1034656310 725 LKMGKPASPGSDLYAYGCLL 744
Cdd:cd08215   174 LCENKPYNYKSDIWALGCVL 193

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK 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 1034656310 633 LMVPYYPRANLNAVQANM--PLNSEETLKVMKGVAQGLHTLHKADIIHGSLHQNNVFALNREQGIVGDFDFTKS-VSQRA 709
Cdd:cd14154    67 LITEYIPGGTLKDVLKDMarPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLiVEERL 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656310 710 SVNMM--------------------VGDLSLMSPELKMGKPASPGSDLYAYGCLLLWLSVQnqeFEINKDGIPKVDQFHL 769
Cdd:cd14154   147 PSGNMspsetlrhlkspdrkkrytvVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEIIGR---VEADPDYLPRTKDFGL 223

                  ....
gi 1034656310 770 DDKV 773
Cdd:cd14154   224 NVDS 227

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-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 1034656310 621 FLFLCKSDPMAYLMVPYYPRANLNAVQANM--PLNSEETLKVMKGVAQGLHTLHKADIIHGSLHQNN--VFALNREQ-GI 695
Cdd:cd14065    53 FIGVCVKDNKLNFITEYVNGGTLEELLKSMdeQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNclVREANRGRnAV 132

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034656310 696 VGDF-------DFTKSVSQRASVNMMVGDLSLMSPELKMGKPASPGSDLYAYGCLL 744
Cdd:cd14065   133 VADFglarempDEKTKKPDRKKRLTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVL 188

sixth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the sixth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1034656310  93 FSEDQCWYRCKVLKIISVEKCLVRYIDYGNTEILNRSDIVEIPLEL 138
Cdd:cd20425    58 YPEDGLWYRAVVKEKIPNNLVSVQFIDYGNTSVVQPSKIHRLPKEL 103

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 1034656310 632 YLMVPYYPRANL-NAVQANMPLNSEETLKVMKGVAQGLHTLHKADIIHGSLHQNNVfaLNREQGIVGDFDFTKSVSQRAS 710
Cdd:cd14007    76 YLILEYAPNGELyKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENI--LLGSNGELKLADFGWSVHAPSN 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656310 711 VNM-MVGDLSLMSPELKMGKPASPGSDLYAYGCLLLWLSVQNQEFEIN-----KDGIPKVDqFHLDDKV----KSLLCSL 780
Cdd:cd14007   154 RRKtFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKshqetYKRIQNVD-IKFPSSVspeaKDLISKL 232

                         170
                  ....*....|....*.
gi 1034656310 781 ICYRSS--MTAEQVLN 794
Cdd:cd14007   233 LQKDPSkrLSLEQVLN 248

fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the fourth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034656310  85 PNKIYGGLFSEDQCWYRCKVLKIIS-VEKCLVRYIDYGNTEILNRSDIVEIPLE-LQFSSVAKKYKLWGLHIPSDQ 158
Cdd:cd20423     5 PNPVCLAKYSEDGKWCRALIDNVYEpVEMVEVTYVDYGNKELVSLKNLRSISEEfLKLKAQAFRCSLYNLIQPSGQ 80

second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1034656310  95 EDQCWYRCKVLKIISVEKCLVRYIDYGNTEILNRSDIVEIP 135
Cdd:cd20415    36 EDGAWYRARIIGLPGHREVEVKYVDFGNTATVTIKHVRKIK 76

Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing factor 30 (SPF30), and similar proteins; This group contains SMN, SPF30, Tudor domain-containing protein 3 (TDRD3), DNA excision repair protein ERCC-6-like 2 (ERCC6L2), and similar proteins. SMN, also called component of gems 1, or Gemin-1, is part of a multimeric SMN complex that includes spliceosomal Sm core proteins and plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. SPF30, also called 30 kDa splicing factor SMNrp, SMN-related protein, or survival motor neuron domain-containing protein 1 (SMNDC1), is an essential pre-mRNA splicing factor required for assembly of the U4/U5/U6 tri-small nuclear ribonucleoprotein into the spliceosome. TDRD3 is a scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. ERCC6L2, also called DNA repair and recombination protein RAD26-like (RAD26L), may be involved in early DNA damage response. It regulates RNA Pol II-mediated transcription via its interaction with DNA-dependent protein kinase (DNA-PK) to resolve R loops and minimize transcription-associated genome instability. Members of this group contain a single Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1034656310  92 LFSEDQCWYRCKVLKI-ISVEKCLVRYIDYGNTEILNRSDIVEI 134
Cdd:cd21182     7 PYSDDGKYYEATIEEItEESDTATVVFDGYGNSEEVPLSDLKPL 50

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; 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. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. 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. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B 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 1034656310 597 IERAATYHRAWREAEGDSGLL-PLIFLFL--CKSDPMAYLMVPYYPRANL-NAVQANMPLNSEETLKVMKGVAQGLHTLH 672
Cdd:cd14117    44 IEKEGVEHQLRREIEIQSHLRhPNILRLYnyFHDRKRIYLILEYAPRGELyKELQKHGRFDEQRTATFMEELADALHYCH 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034656310 673 KADIIHGSLHQNNVFALNREQGIVGDFDF---TKSVSQRAsvnmMVGDLSLMSPELKMGKPASPGSDLYAYGCLLLWLSV 749
Cdd:cd14117   124 EKKVIHRDIKPENLLMGYKGELKIADFGWsvhAPSLRRRT----MCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLV 199

                  ....*.
gi 1034656310 750 QNQEFE 755
Cdd:cd14117   200 GMPPFE 205

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates 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. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf 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 1034656310 658 LKVMKGVAQGLHTLHKADIIHGSLHQNNVFALNREQGIVGDFDFTkSVSQRAS----VNMMVGDLSLMSPE---LKMGKP 730
Cdd:cd14151   107 IDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLA-TVKSRWSgshqFEQLSGSILWMAPEvirMQDKNP 185

                          90
                  ....*....|....
gi 1034656310 731 ASPGSDLYAYGCLL 744
Cdd:cd14151   186 YSFQSDVYAFGIVL 199

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They 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. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK 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 1034656310 664 VAQGLHTLHKADIIHGSLHQNNVfaLNREQGIV--GDFDFTKSVSQRASVNM---MVGDLSLMSPELKMGKPASPGSDLY 738
Cdd:cd06606   108 ILEGLEYLHSNGIVHRDIKGANI--LVDSDGVVklADFGCAKRLAEIATGEGtksLRGTPYWMAPEVIRGEGYGRAADIW 185

                  ....*..
gi 1034656310 739 AYGCLLL 745
Cdd:cd06606   186 SLGCTVI 192

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha 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 1034656310 652 LNSEETLKVMKGVAQGLHTLHKADIIHGSLHQNNVfALNREQG-----IVgDFDFTKSVSQRASVNMMVGDLSLMSPELK 726
Cdd:cd14039    96 LKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENI-VLQEINGkivhkII-DLGYAKDLDQGSLCTSFVGTLQYLAPELF 173

                          90
                  ....*....|....*....
gi 1034656310 727 MGKPASPGSDLYAYGCLLL 745
Cdd:cd14039   174 ENKSYTVTVDYWSFGTMVF 192

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC 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 1034656310 659 KVMKGVAQGLHTLHKADIIHGSLHQNNV-FALNREQGIVGDFDFTKSVSQRASVNmMVGDLSLMSPELKMG-KPASPGSD 736
Cdd:cd05118   105 SYLYQLLQALDFLHSNGIIHRDLKPENIlINLELGQLKLADFGLARSFTSPPYTP-YVATRWYRAPEVLLGaKPYGSSID 183

                  ....*....
gi 1034656310 737 LYAYGCLLL 745
Cdd:cd05118   184 IWSLGCILA 192