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Conserved domains on  [gi|1720419116|ref|XP_030111527|]
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serine/threonine-protein kinase 31 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tudor_TDRD8 cd20430
Tudor domain found in Tudor domain-containing protein 8 (TDRD8) and similar proteins; TDRD8, ...
61-135 1.65e-40

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.


:

Pssm-ID: 410501 [Multi-domain]  Cd Length: 75  Bit Score: 143.20  E-value: 1.65e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720419116  61 IGCSLSEVCPLANSVFGNLDPKKIYGGLFSEDKCWYRCKVLKTISDDKCLVRYIDYGNTEILNRSDIVEIPPELQ 135
Cdd:cd20430     1 LSDELAEVCPTAPPLFGTPDPNKIYGGKFSEDNCWYRCKVKSILSDEKCTVQYIDYGNTETVSRSSIVELPPDLQ 75
SPS1 super family cl43163
Serine/threonine protein kinase [Signal transduction mechanisms];
625-744 3.89e-12

Serine/threonine protein kinase [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG0515:

Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 69.66  E-value: 3.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 625 DPVAYLMVPYYPKANLSA-VQASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFaLNREQGI-VGDYDFTK-- 700
Cdd:COG0515    79 DGRPYLVMEYVEGESLADlLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANIL-LTPDGRVkLIDFGIARal 157
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1720419116 701 SESQRASVNAMVGGLSLLSPELKTGKPPSASSDLYAYGCLFLWL 744
Cdd:COG0515   158 GGATLTQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYEL 201
235kDa-fam super family cl31124
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
231-540 8.07e-04

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


The actual alignment was detected with superfamily member TIGR01612:

Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 43.50  E-value: 8.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116  231 NELEKIWAEYNVAQEKIQtclneNEGNILIAERNEVQQklfvavdvfiLEVDDlpldkrlktlQDLATSLE-SVYGKAKE 309
Cdd:TIGR01612 1997 NELKDTLSDLKYKKEKIL-----NDVKLLLHKFDELNK----------LSCDS----------QNYDTILElSKQDKIKE 2051
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116  310 GTNNSEETLRKF-YDWQCTKREE-FASIRSETEaSLQHLVAWFQSSQKVFDLSLDEPLTSEDLIGNIDEILeKTEscvCK 387
Cdd:TIGR01612 2052 KIDNYEKEKEKFgIDFDVKAMEEkFDNDIKDIE-KFENNYKHSEKDNHDFSEEKDNIIQSKKKLKELTEAF-NTE---IK 2126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116  388 ELELSLIEQ-GVID------KEIILSTYSQVLQKIHSE----EKFIATLLSKYKDSVEFKKQMIDCLNKnpNVDYL---L 453
Cdd:TIGR01612 2127 IIEDKIIEKnDLIDkliemrKECLLFSYATLVETLKSKvinhSEFITSAAKFSKDFFEFIEDISDSLND--DIDALqikY 2204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116  454 SIKKTLKGLKAQLRWKLVEKSNLEESDdhdgTEIEKIKQEITQLRNSVFQEIYHEREEYEKL-----NSLTQKWFPELPL 528
Cdd:TIGR01612 2205 NLNQTKKHMISILADATKDHNNLIEKE----KEATKIINNLTELFTIDFNNADADILHNNKIqiiyfNSELHKSIESIKK 2280
                          330
                   ....*....|..
gi 1720419116  529 LYPEIGLLKYMN 540
Cdd:TIGR01612 2281 LYKKINAFKLLN 2292
 
Name Accession Description Interval E-value
Tudor_TDRD8 cd20430
Tudor domain found in Tudor domain-containing protein 8 (TDRD8) and similar proteins; TDRD8, ...
61-135 1.65e-40

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.


Pssm-ID: 410501 [Multi-domain]  Cd Length: 75  Bit Score: 143.20  E-value: 1.65e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720419116  61 IGCSLSEVCPLANSVFGNLDPKKIYGGLFSEDKCWYRCKVLKTISDDKCLVRYIDYGNTEILNRSDIVEIPPELQ 135
Cdd:cd20430     1 LSDELAEVCPTAPPLFGTPDPNKIYGGKFSEDNCWYRCKVKSILSDEKCTVQYIDYGNTETVSRSSIVELPPDLQ 75
TUDOR pfam00567
Tudor domain;
32-147 1.84e-29

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 113.22  E-value: 1.84e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116  32 KVEDVVGSHVEDAVTFWAQNVSKNKDIMKIGCSLSEVCPLANSVFGNLDPKKIYGGLFSEDKCWYRCKVLKTISDDKCLV 111
Cdd:pfam00567   1 STIDVVVSHIESPSTFYIQPKSDSKKLEKLTEELQEYYASKPPESLPPAVGDGCVAAFSEDGKWYRAKITESLDDGLVEV 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1720419116 112 RYIDYGNTEILNRSDIVEIPPELQF-SSIAKKYRLWG 147
Cdd:pfam00567  81 LFIDYGNTETVPLSDLRPLPPELESlPPQAIKCQLAG 117
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
625-744 3.89e-12

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 69.66  E-value: 3.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 625 DPVAYLMVPYYPKANLSA-VQASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFaLNREQGI-VGDYDFTK-- 700
Cdd:COG0515    79 DGRPYLVMEYVEGESLADlLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANIL-LTPDGRVkLIDFGIARal 157
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1720419116 701 SESQRASVNAMVGGLSLLSPELKTGKPPSASSDLYAYGCLFLWL 744
Cdd:COG0515   158 GGATLTQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYEL 201
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
625-744 2.60e-11

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.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 64.92  E-value: 2.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 625 DPVAYLMVPYYPKANLSAV-QASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFALNREQGIVGDYDFTK--S 701
Cdd:cd14014    72 DGRPYIVMEYVEGGSLADLlRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARalG 151
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1720419116 702 ESQRASVNAMVGGLSLLSPELKTGKPPSASSDLYAYGCLFLWL 744
Cdd:cd14014   152 DSGLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYEL 194
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
89-134 4.91e-10

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).


Pssm-ID: 197660  Cd Length: 57  Bit Score: 55.74  E-value: 4.91e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1720419116   89 FSEDKCWYRCKVLKTISDDKCLVRYIDYGNTEILNRSDIVEIPPEL 134
Cdd:smart00333  12 RWEDGEWYRARIVKVDGEQLYEVFFIDYGNEEVVPPSDLRQLPEEL 57
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
648-741 4.78e-07

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 53.26  E-value: 4.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 648 PLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVfaLNREQGIVGDYDF----TKSESQRASVNAMVGGLSLLSPELK 723
Cdd:NF033483  103 PLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNI--LITKDGRVKVTDFgiarALSSTTMTQTNSVLGTVHYLSPEQA 180
                          90
                  ....*....|....*...
gi 1720419116 724 TGKPPSASSDLYAYGCLF 741
Cdd:NF033483  181 RGGTVDARSDIYSLGIVL 198
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
629-795 5.89e-07

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 51.76  E-value: 5.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116  629 YLMVPYYPKANLSAV-QASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFaLNrEQGIV--GDYDFTKSESQR 705
Cdd:smart00220  73 YLVMEYCEGGDLFDLlKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENIL-LD-EDGHVklADFGLARQLDPG 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116  706 ASVNAMVGGLSLLSPELKTGKPPSASSDLYAYGCLF--------LWLSVQNQE--FETNEDGIPKVDQFH--LDDNVKSL 773
Cdd:smart00220 151 EKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILyelltgkpPFPGDDQLLelFKKIGKPKPPFPPPEwdISPEAKDL 230
                          170       180
                   ....*....|....*....|....
gi 1720419116  774 LCSLIYFRSS--MTAEQVLNAECF 795
Cdd:smart00220 231 IRKLLVKDPEkrLTAEEALQHPFF 254
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
231-540 8.07e-04

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 43.50  E-value: 8.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116  231 NELEKIWAEYNVAQEKIQtclneNEGNILIAERNEVQQklfvavdvfiLEVDDlpldkrlktlQDLATSLE-SVYGKAKE 309
Cdd:TIGR01612 1997 NELKDTLSDLKYKKEKIL-----NDVKLLLHKFDELNK----------LSCDS----------QNYDTILElSKQDKIKE 2051
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116  310 GTNNSEETLRKF-YDWQCTKREE-FASIRSETEaSLQHLVAWFQSSQKVFDLSLDEPLTSEDLIGNIDEILeKTEscvCK 387
Cdd:TIGR01612 2052 KIDNYEKEKEKFgIDFDVKAMEEkFDNDIKDIE-KFENNYKHSEKDNHDFSEEKDNIIQSKKKLKELTEAF-NTE---IK 2126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116  388 ELELSLIEQ-GVID------KEIILSTYSQVLQKIHSE----EKFIATLLSKYKDSVEFKKQMIDCLNKnpNVDYL---L 453
Cdd:TIGR01612 2127 IIEDKIIEKnDLIDkliemrKECLLFSYATLVETLKSKvinhSEFITSAAKFSKDFFEFIEDISDSLND--DIDALqikY 2204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116  454 SIKKTLKGLKAQLRWKLVEKSNLEESDdhdgTEIEKIKQEITQLRNSVFQEIYHEREEYEKL-----NSLTQKWFPELPL 528
Cdd:TIGR01612 2205 NLNQTKKHMISILADATKDHNNLIEKE----KEATKIINNLTELFTIDFNNADADILHNNKIqiiyfNSELHKSIESIKK 2280
                          330
                   ....*....|..
gi 1720419116  529 LYPEIGLLKYMN 540
Cdd:TIGR01612 2281 LYKKINAFKLLN 2292
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
626-751 1.02e-03

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 42.52  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 626 PVAYLMVPYYPKANLSAVQASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFALNREQGIVGDYDF---TKSE 702
Cdd:PHA03207  159 STVCMVMPKYKCDLFTYVDRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAackLDAH 238
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1720419116 703 SQRASVNAMVGGLSLLSPELKTGKPPSASSDLYAYGCLFLWLSVQNQEF 751
Cdd:PHA03207  239 PDTPQCYGWSGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKNVTL 287
 
Name Accession Description Interval E-value
Tudor_TDRD8 cd20430
Tudor domain found in Tudor domain-containing protein 8 (TDRD8) and similar proteins; TDRD8, ...
61-135 1.65e-40

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.


Pssm-ID: 410501 [Multi-domain]  Cd Length: 75  Bit Score: 143.20  E-value: 1.65e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720419116  61 IGCSLSEVCPLANSVFGNLDPKKIYGGLFSEDKCWYRCKVLKTISDDKCLVRYIDYGNTEILNRSDIVEIPPELQ 135
Cdd:cd20430     1 LSDELAEVCPTAPPLFGTPDPNKIYGGKFSEDNCWYRCKVKSILSDEKCTVQYIDYGNTETVSRSSIVELPPDLQ 75
TUDOR pfam00567
Tudor domain;
32-147 1.84e-29

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 113.22  E-value: 1.84e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116  32 KVEDVVGSHVEDAVTFWAQNVSKNKDIMKIGCSLSEVCPLANSVFGNLDPKKIYGGLFSEDKCWYRCKVLKTISDDKCLV 111
Cdd:pfam00567   1 STIDVVVSHIESPSTFYIQPKSDSKKLEKLTEELQEYYASKPPESLPPAVGDGCVAAFSEDGKWYRAKITESLDDGLVEV 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1720419116 112 RYIDYGNTEILNRSDIVEIPPELQF-SSIAKKYRLWG 147
Cdd:pfam00567  81 LFIDYGNTETVPLSDLRPLPPELESlPPQAIKCQLAG 117
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
83-130 1.42e-13

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.


Pssm-ID: 410450  Cd Length: 50  Bit Score: 65.61  E-value: 1.42e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1720419116  83 KIYGGLFSEDKCWYRCKVLKTISDDKCLVRYIDYGNTEILNRSDIVEI 130
Cdd:cd20379     3 DLCAAKYEEDGKWYRARVLEVLSNDKVEVFFVDYGNTETVPLSDLRPL 50
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
625-744 3.89e-12

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 69.66  E-value: 3.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 625 DPVAYLMVPYYPKANLSA-VQASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFaLNREQGI-VGDYDFTK-- 700
Cdd:COG0515    79 DGRPYLVMEYVEGESLADlLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANIL-LTPDGRVkLIDFGIARal 157
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1720419116 701 SESQRASVNAMVGGLSLLSPELKTGKPPSASSDLYAYGCLFLWL 744
Cdd:COG0515   158 GGATLTQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYEL 201
Tudor_TDRD11 cd20433
Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, ...
81-134 1.99e-11

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.


Pssm-ID: 410504 [Multi-domain]  Cd Length: 84  Bit Score: 60.78  E-value: 1.99e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720419116  81 PKK--IYGGLFSEDKCWYRCKVLKTISDDKCLVRYIDYGNTEILNRSDIVEIPPEL 134
Cdd:cd20433    28 PRKgdLCAAKFVEDGEWYRAKVEKVEGDKKVHVLYIDYGNREVLPSTRLAALPPAF 83
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
625-744 2.60e-11

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.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 64.92  E-value: 2.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 625 DPVAYLMVPYYPKANLSAV-QASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFALNREQGIVGDYDFTK--S 701
Cdd:cd14014    72 DGRPYIVMEYVEGGSLADLlRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARalG 151
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1720419116 702 ESQRASVNAMVGGLSLLSPELKTGKPPSASSDLYAYGCLFLWL 744
Cdd:cd14014   152 DSGLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYEL 194
Tudor_TDRD1_rpt2 cd20409
second Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
88-134 1.09e-10

second Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four 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.


Pssm-ID: 410480  Cd Length: 82  Bit Score: 58.62  E-value: 1.09e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1720419116  88 LFSEDKCWYRCKVLKTISDDKCLVRYIDYGNTEILNRSDIVEIPPEL 134
Cdd:cd20409    35 QFTEDNQWYRASVLAYSSEDSVLVGYIDFGNSEEVALSRLRPIPPSL 81
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
618-745 1.25e-10

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.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 61.90  E-value: 1.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 618 FLFLCKSDPVAYLMVPYYPKANLSAV--QASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFaLNREQGIV-G 694
Cdd:cd00180    56 LYDVFETENFLYLVMEYCEGGSLKDLlkENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENIL-LDSDGTVKlA 134
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720419116 695 DYDFTK---SESQRASVNAMVGGLSLLSPELKTGKPPSASSDLYAYGCLFLWLS 745
Cdd:cd00180   135 DFGLAKdldSDDSLLKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYELE 188
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
649-752 2.29e-10

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 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.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 62.06  E-value: 2.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 649 LTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFaLNREQGIV--GDYDFTKSESQRASVNAMVGGLSLLSPELKTGK 726
Cdd:cd08220    98 LSEEEILHFFVQILLALHHVHSKQILHRDLKTQNIL-LNKKRTVVkiGDFGISKILSSKSKAYTVVGTPCYISPELCEGK 176
                          90       100
                  ....*....|....*....|....*.
gi 1720419116 727 PPSASSDLYAYGCLFLWLSVQNQEFE 752
Cdd:cd08220   177 PYNQKSDIWALGCVLYELASLKRAFE 202
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
89-134 4.91e-10

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).


Pssm-ID: 197660  Cd Length: 57  Bit Score: 55.74  E-value: 4.91e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1720419116   89 FSEDKCWYRCKVLKTISDDKCLVRYIDYGNTEILNRSDIVEIPPEL 134
Cdd:smart00333  12 RWEDGEWYRARIVKVDGEQLYEVFFIDYGNEEVVPPSDLRQLPEEL 57
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
629-757 1.64e-09

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.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 59.35  E-value: 1.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 629 YLMVPYYPKANLSAV---QASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFALNREQGIVGDYDFTKSESQR 705
Cdd:cd08529    75 NIVMEYAENGDLHSLiksQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDT 154
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720419116 706 AS-VNAMVGGLSLLSPELKTGKPPSASSDLYAYGCLFLWLSVQNQEFETNEDG 757
Cdd:cd08529   155 TNfAQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQG 207
Tudor_TDRD6_rpt5 cd20424
fifth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
34-135 4.90e-09

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.


Pssm-ID: 410495  Cd Length: 126  Bit Score: 55.20  E-value: 4.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116  34 EDVVGSHVEDAVTFWAQnVSKNKDIM-KIGCSLSEVCPLANSVFGNLDPKKIYGGLFSeDKCWYRCKVLKTISDDKclVR 112
Cdd:cd20424    14 EEVYITYVNDPWTFYCQ-LARNAGVLdQLASAISRLSSEIRKLELSVNPGTLCLAKYS-DQHWYRGIIITNKNSTE--VF 89
                          90       100
                  ....*....|....*....|...
gi 1720419116 113 YIDYGNTEILNRSDIVEIPPELQ 135
Cdd:cd20424    90 FVDYGNTEKVEKEDMLPIPSDAY 112
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
618-743 1.55e-08

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 56.39  E-value: 1.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 618 FLFLCKSDPVAYLMVPYYPKANLSAV--QASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFALNREQGIVGD 695
Cdd:cd13999    55 FIGACLSPPPLCIVTEYMPGGSLYDLlhKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIAD 134
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1720419116 696 YDFTKSESQRASV-NAMVGGLSLLSPELKTGKPPSASSDLYAYGCLfLW 743
Cdd:cd13999   135 FGLSRIKNSTTEKmTGVVGTPRWMAPEVLRGEPYTEKADVYSFGIV-LW 182
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
629-832 1.83e-08

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK 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.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 56.51  E-value: 1.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 629 YLMV-PYYPKANLS----AVQASMPLTSEEALKVMKGVARGLHTLHSAN---IIHGSLHQNNVFaLNRE-QGIVGDY--- 696
Cdd:cd14066    65 KLLVyEYMPNGSLEdrlhCHKGSPPLPWPQRLKIAKGIARGLEYLHEECpppIIHGDIKSSNIL-LDEDfEPKLTDFgla 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 697 -DFTKSESQrASVNAMVGGLSLLSPELKTGKPPSASSDLYAYGCLFLwlsvqnqEFETnedGIPKVDQFHLDDNVKSLlc 775
Cdd:cd14066   144 rLIPPSESV-SKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLL-------ELLT---GKPAVDENRENASRKDL-- 210
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720419116 776 sliyfRSSMTAEQVLNAECFLLPK-GKSVPIPEKEIE--------CTQHSREDESKMESLDRYSEK 832
Cdd:cd14066   211 -----VEWVESKGKEELEDILDKRlVDDDGVEEEEVEallrlallCTRSDPSLRPSMKEVVQMLEK 271
Tudor_TDRD6_rpt6 cd20425
sixth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
89-134 1.13e-07

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.


Pssm-ID: 410496  Cd Length: 115  Bit Score: 50.92  E-value: 1.13e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1720419116  89 FSEDKCWYRCKVLKTISDDKCLVRYIDYGNTEILNRSDIVEIPPEL 134
Cdd:cd20425    58 YPEDGLWYRAVVKEKIPNNLVSVQFIDYGNTSVVQPSKIHRLPKEL 103
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
616-767 1.33e-07

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK 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.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 53.63  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 616 LIFLFLCKSDPVAYLMVPYYPKANLSA-VQASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFALNREQG--- 691
Cdd:cd14155    51 LRFMGVCVHQGQLHALTEYINGGNLEQlLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDENGyta 130
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720419116 692 IVGDYDFTK---SESQRASVNAMVGGLSLLSPELKTGKPPSASSDLYAYGCLFLWLSVQnqeFETNEDGIPKVDQFHLD 767
Cdd:cd14155   131 VVGDFGLAEkipDYSDGKEKLAVVGSPYWMAPEVLRGEPYNEKADVFSYGIILCEIIAR---IQADPDYLPRTEDFGLD 206
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
618-743 1.82e-07

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.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 52.88  E-value: 1.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 618 FLFLCKSDPVAYLMVPYYPKANLSAV-QASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFALNREQGIVGDY 696
Cdd:cd14059    46 FKGVCTQAPCYCILMEYCPYGQLYEVlRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDF 125
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1720419116 697 DFTKSESQRASVNAMVGGLSLLSPELKTGKPPSASSDLYAYGCLfLW 743
Cdd:cd14059   126 GTSKELSEKSTKMSFAGTVAWMAPEVIRNEPCSEKVDIWSFGVV-LW 171
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
648-741 4.78e-07

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 53.26  E-value: 4.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 648 PLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVfaLNREQGIVGDYDF----TKSESQRASVNAMVGGLSLLSPELK 723
Cdd:NF033483  103 PLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNI--LITKDGRVKVTDFgiarALSSTTMTQTNSVLGTVHYLSPEQA 180
                          90
                  ....*....|....*...
gi 1720419116 724 TGKPPSASSDLYAYGCLF 741
Cdd:NF033483  181 RGGTVDARSDIYSLGIVL 198
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
629-795 5.89e-07

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 51.76  E-value: 5.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116  629 YLMVPYYPKANLSAV-QASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFaLNrEQGIV--GDYDFTKSESQR 705
Cdd:smart00220  73 YLVMEYCEGGDLFDLlKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENIL-LD-EDGHVklADFGLARQLDPG 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116  706 ASVNAMVGGLSLLSPELKTGKPPSASSDLYAYGCLF--------LWLSVQNQE--FETNEDGIPKVDQFH--LDDNVKSL 773
Cdd:smart00220 151 EKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILyelltgkpPFPGDDQLLelFKKIGKPKPPFPPPEwdISPEAKDL 230
                          170       180
                   ....*....|....*....|....
gi 1720419116  774 LCSLIYFRSS--MTAEQVLNAECF 795
Cdd:smart00220 231 IRKLLVKDPEkrLTAEEALQHPFF 254
Tudor_SF cd04508
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
87-128 1.16e-06

Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally identified in the Tudor protein of Drosophila, that adopts a beta-barrel-like core structure containing four short beta-strands followed by an alpha-helical region. It binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Tudor domain-containing proteins may mediate protein-protein interactions required for various DNA-templated biological processes, such as RNA metabolism, as well as histone modification and the DNA damage response. Members of this superfamily contain one or more copies of the Tudor domain.


Pssm-ID: 410449 [Multi-domain]  Cd Length: 47  Bit Score: 46.04  E-value: 1.16e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1720419116  87 GLFSEDKCWYRCKVLKTISDDKCLVRYiDYGNTEILNRSDIV 128
Cdd:cd04508     6 AKWSDDGQWYPATVVAVNDDGKYTVLF-DDGNEEEVSEDDIR 46
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
618-738 1.60e-06

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.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 50.18  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 618 FLFLCKSDPVAYLMVPYYPKANLSAVQASM--PLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNN--VFALNREQ-GI 692
Cdd:cd14065    53 FIGVCVKDNKLNFITEYVNGGTLEELLKSMdeQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNclVREANRGRnAV 132
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720419116 693 VGDY-------DFTKSESQRASVNAMVGGLSLLSPELKTGKPPSASSDLYAYG 738
Cdd:cd14065   133 VADFglarempDEKTKKPDRKKRLTVVGSPYWMAPEMLRGESYDEKVDVFSFG 185
Tudor_TDRD1_rpt4 cd20411
fourth Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
89-134 1.90e-06

fourth Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four 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.


Pssm-ID: 410482  Cd Length: 116  Bit Score: 47.44  E-value: 1.90e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1720419116  89 FSEDKCWYRCKVLKTiSDDKCLVRYIDYGNTEILNRSDIVEIPPEL 134
Cdd:cd20411    58 FTGDKNWYRAVVLET-SDSEVKVLYADYGNTETLPLSRILPITKSH 102
Tudor_TDRD6_rpt4 cd20423
fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
89-154 2.69e-06

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.


Pssm-ID: 410494  Cd Length: 80  Bit Score: 45.93  E-value: 2.69e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720419116  89 FSEDKCWYRCKVLKTISD-DKCLVRYIDYGNTEILNRSDIVEIPPE-LQFSSIAKKYRLWGLQIPSGQ 154
Cdd:cd20423    13 YSEDGKWCRALIDNVYEPvEMVEVTYVDYGNKELVSLKNLRSISEEfLKLKAQAFRCSLYNLIQPSGQ 80
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
648-740 2.91e-06

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.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 49.70  E-value: 2.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 648 PLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFALNREQGIVGDYDFTKSeSQRASVNAMVGGLSLLSPELKTGKP 727
Cdd:cd08530    99 LFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKV-LKKNLAKTQIGTPLYAAPEVWKGRP 177
                          90
                  ....*....|...
gi 1720419116 728 PSASSDLYAYGCL 740
Cdd:cd08530   178 YDYKSDIWSLGCL 190
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
649-744 3.06e-06

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty 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.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 49.41  E-value: 3.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 649 LTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFALNREQGIVGDYDFTKSESQRASvnAMVGGLSLLSPELKTGKPP 728
Cdd:cd13975    99 LSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKPEAMMSG--SIVGTPIHMAPELFSGKYD 176
                          90
                  ....*....|....*.
gi 1720419116 729 SaSSDLYAYGCLFLWL 744
Cdd:cd13975   177 N-SVDVYAFGILFWYL 191
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
645-743 3.14e-06

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos 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.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 49.69  E-value: 3.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 645 ASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVfaLNREQGIVGDYDFTKSEsQRASVNAMVGGLSLL------ 718
Cdd:cd13979    96 GSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANI--LISEQGVCKLCDFGCSV-KLGEGNEVGTPRSHIggtyty 172
                          90       100
                  ....*....|....*....|....*.
gi 1720419116 719 -SPELKTGKPPSASSDLYAYGcLFLW 743
Cdd:cd13979   173 rAPELLKGERVTPKADIYSFG-ITLW 197
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
87-135 3.53e-06

second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; TDRD12, also called ES cell-associated transcript 8 protein (ECAT8), is a putative ATP-dependent DEAD-like RNA helicase that is essential for germ cell development and maintenance. It acts as a unique piRNA biogenesis factor essential for secondary PIWI interacting RNA (piRNA) biogenesis. TDRD12 contains two Tudor domains, one at the N-terminus and the other at the C-terminal end. The model corresponds to the second/C-terminal 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.


Pssm-ID: 410506  Cd Length: 134  Bit Score: 47.25  E-value: 3.53e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720419116  87 GLFSEDKCWYRCKVLK-TISDDKC-----LVRYIDYGNTEILNRSDIVEIPPELQ 135
Cdd:cd20435    57 AVEDENNLYHRVKVLEiTEKDDKTkprevLVKFIDEGRVETVVVSQLLELPEELK 111
Tudor_AtTudor1-like cd20443
Tudor domain found in Arabidopsis thaliana ribonuclease Tudor 1 (AtTudor1), ribonuclease Tudor ...
47-151 4.24e-06

Tudor domain found in Arabidopsis thaliana ribonuclease Tudor 1 (AtTudor1), ribonuclease Tudor 2 (AtTudor2), and similar proteins; The family includes AtTudor1 (also called Tudor-SN protein 1) and AtTudor2 (also called Tudor-SN protein 2 or 100 kDa coactivator-like protein). They are cytoprotective ribonucleases (RNases) required for resistance to abiotic stresses, acting as positive regulators of mRNA decapping during stress. Members of this family contain one 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.


Pssm-ID: 410514 [Multi-domain]  Cd Length: 117  Bit Score: 46.31  E-value: 4.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116  47 FWAQNVSkNKDIMKI-----GCSLSEVCPLAnsvfGNLDPKK--IYGGLFSEDKCWYRCKVLKTISD------DKCLVRY 113
Cdd:cd20443     4 FYVQVVS-DQRLSSIqqqleGLSLKDKANPP----GGFNPKKgeLVLAQFSADNSWNRAMVVNAPRQgtqspkDEYEVFY 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1720419116 114 IDYGNTEILNRSDIVEIPPELQ-FSSIAKKYRLWGLQIP 151
Cdd:cd20443    79 IDYGNQETVPLSALRPLDPSVSsAPGLAQLCSLAHIKVP 117
Tudor_TDRD6_rpt7 cd20426
seventh Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
89-134 4.31e-06

seventh 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 seventh 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.


Pssm-ID: 410497  Cd Length: 140  Bit Score: 47.11  E-value: 4.31e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1720419116  89 FSEDKCWYRCKVlKTISDDKCLVRYIDYGNTEILNRSDIVEIPPEL 134
Cdd:cd20426    57 YSEDNHWYRALV-TKINDNLVSVRFVDYGNEEDVVREQVRALPSEL 101
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
648-754 4.48e-06

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; 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. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 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.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 49.09  E-value: 4.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 648 PLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFaLNREQGI-VGDYDF-TKSESQRASVNAMVGGLSLLSPELKTG 725
Cdd:cd14186    98 PFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLL-LTRNMNIkIADFGLaTQLKMPHEKHFTMCGTPNYISPEIATR 176
                          90       100
                  ....*....|....*....|....*....
gi 1720419116 726 KPPSASSDLYAYGCLFLWLSVQNQEFETN 754
Cdd:cd14186   177 SAHGLESDVWSLGCMFYTLLVGRPPFDTD 205
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
620-739 5.32e-06

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.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 48.74  E-value: 5.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 620 FLCKSDPvaYLMVPYYPKANLSAV--QASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVfALNREQGI-VGDY 696
Cdd:cd05122    66 YLKKDEL--WIVMEFCSGGSLKDLlkNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANI-LLTSDGEVkLIDF 142
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1720419116 697 DFTKSESQRASVNAMVGGLSLLSPELKTGKPPSASSDLYAYGC 739
Cdd:cd05122   143 GLSAQLSDGKTRNTFVGTPYWMAPEVIQGKPYGFKADIWSLGI 185
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
661-741 5.55e-06

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. 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. The ULK4 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.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 48.83  E-value: 5.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 661 VARGLHTLHSANIIHGSLHQNNV------------FALNREQG-----IVGDYDFTKSESQRASVNAMVGGLSLLSPELK 723
Cdd:cd14010   103 LVRGLHYIHSKGIIYCDLKPSNIlldgngtlklsdFGLARREGeilkeLFGQFSDEGNVNKVSKKQAKRGTPYYMAPELF 182
                          90
                  ....*....|....*...
gi 1720419116 724 TGKPPSASSDLYAYGCLF 741
Cdd:cd14010   183 QGGVHSFASDLWALGCVL 200
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
649-795 5.62e-06

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; 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. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 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.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 48.78  E-value: 5.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 649 LTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFaLNREQGI-VGDYDF-TKSESQRASVNAMVGGLSLLSPELKTGK 726
Cdd:cd14187   104 LTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLF-LNDDMEVkIGDFGLaTKVEYDGERKKTLCGTPNYIAPEVLSKK 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 727 PPSASSDLYAYGCLFLWLSVQNQEFET------------NEDGIPKvdqfHLDDNVKSLLCSLIYFRSSM--TAEQVLNA 792
Cdd:cd14187   183 GHSFEVDIWSIGCIMYTLLVGKPPFETsclketylrikkNEYSIPK----HINPVAASLIQKMLQTDPTArpTINELLND 258

                  ...
gi 1720419116 793 ECF 795
Cdd:cd14187   259 EFF 261
Tudor_TDRD1_rpt3 cd20410
third Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
88-134 6.00e-06

third Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the third 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.


Pssm-ID: 410481 [Multi-domain]  Cd Length: 59  Bit Score: 44.25  E-value: 6.00e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1720419116  88 LFSEDKCWYRCKVLKTISDDKCLVRYIDYGNTEILNRSDIVEIPPEL 134
Cdd:cd20410    12 FFSGDGNWYRAMVKEILPGGAVKVHFVDYGNVEEVTLDKLRKITSTF 58
Tudor_TDRD4_rpt5 cd20418
fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
92-152 9.40e-06

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.


Pssm-ID: 410489  Cd Length: 105  Bit Score: 45.09  E-value: 9.40e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720419116  92 DKCWYRCKVL--KTISDDKCLVRYIDYGNTEILNRSDIVEIPPEL-QFSSIAKKYRLWGLQIPS 152
Cdd:cd20418    16 DGKWYRAKLLsiLEFNPVKILVRHVDYGSTAALPTSRLRQIPAELmQYPCQAIKVKLAGFKPPL 79
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
648-740 1.32e-05

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.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 47.46  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 648 PLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFaLNREQGI-VGDYDFTKS-ESQRASVNAMVGGLSLLSPELKTG 725
Cdd:cd08215    99 PFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIF-LTKDGVVkLGDFGISKVlESTTDLAKTVVGTPYYLSPELCEN 177
                          90
                  ....*....|....*
gi 1720419116 726 KPPSASSDLYAYGCL 740
Cdd:cd08215   178 KPYNYKSDIWALGCV 192
Tudor_TDRD15_rpt6 cd20441
sixth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
72-133 1.99e-05

sixth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that 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.


Pssm-ID: 410512  Cd Length: 108  Bit Score: 44.35  E-value: 1.99e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720419116  72 ANSVFGNLDPKKIYGGL----FSEDKCWYRCKVLKTISDDKCLVRYIDYGNTEILNRSDIVEIPPE 133
Cdd:cd20441    27 SEKSRENAAVKLKVGDLvaaeYDEDLALYRAVITAVLPGKSFKVEFIDYGNTAVVDKSNIYTLQEK 92
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
629-753 2.45e-05

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; 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. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 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.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 46.93  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 629 YLMVPYYPKANLSAV-QASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFALNREQGIVGDYDF-TKSESQRA 706
Cdd:cd14188    77 YILLEYCSRRSMAHIlKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLaARLEPLEH 156
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1720419116 707 SVNAMVGGLSLLSPELKTGKPPSASSDLYAYGCLFLWLSVQNQEFET 753
Cdd:cd14188   157 RRRTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFET 203
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
630-767 2.65e-05

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.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 46.73  E-value: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 630 LMVPYYPKANLSAVQASM--PLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFALNREQGIVGDY----------- 696
Cdd:cd14154    67 LITEYIPGGTLKDVLKDMarPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFglarliveerl 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 697 ----------DFTKSESQRASVNAMVGGLSLLSPELKTGKPPSASSDLYAYGCLFLWLSVQnqeFETNEDGIPKVDQFHL 766
Cdd:cd14154   147 psgnmspsetLRHLKSPDRKKRYTVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEIIGR---VEADPDYLPRTKDFGL 223

                  .
gi 1720419116 767 D 767
Cdd:cd14154   224 N 224
Tudor_SMN cd20398
Tudor domain found in survival motor neuron protein (SMN) and similar proteins; SMN, also ...
89-132 4.24e-05

Tudor domain found in survival motor neuron protein (SMN) 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. Mutations in human SMN lead to motor neuron degeneration and spinal muscular atrophy. SMN contains a central, highly conserved Tudor domain that is required for U snRNP assembly and Sm protein binding and has been shown to bind arginine-glycine-rich motifs in an methylarginine-dependent manner.


Pssm-ID: 410469  Cd Length: 56  Bit Score: 41.87  E-value: 4.24e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1720419116  89 FSEDKCWYRCKVLKTI-SDDKCLVRYIDYGNTEILNRSDIveIPP 132
Cdd:cd20398    11 YSEDGIIYEATIVSIDaERGTCVVRYTGYGNEEEQNLSDL--LPP 53
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
582-744 4.49e-05

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 45.95  E-value: 4.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 582 GYSVDVDTEGRVIQRAASYHRACgyakeesgllpliflflCKSDPVAYLMVPYYPKANL-----SAVQASMPLTSEEALK 656
Cdd:cd14664    36 GFQAEIQTLGMIRHRNIVRLRGY-----------------CSNPTTNLLVYEYMPNGSLgellhSRPESQPPLDWETRQR 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 657 VMKGVARGLHTLH---SANIIHGSLHQNNVFALNREQGIVGDYDFTK--SESQRASVNAMVGGLSLLSPE-LKTGKPpSA 730
Cdd:cd14664    99 IALGSARGLAYLHhdcSPLIIHRDVKSNNILLDEEFEAHVADFGLAKlmDDKDSHVMSSVAGSYGYIAPEyAYTGKV-SE 177
                         170
                  ....*....|....
gi 1720419116 731 SSDLYAYGCLFLWL 744
Cdd:cd14664   178 KSDVYSYGVVLLEL 191
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
644-739 4.75e-05

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks 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. Nek4 is one in a family of 11 different Neks (Nek1-11). 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.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 45.89  E-value: 4.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 644 QASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFaLNREQGI-VGDYDFTKS-ESQRASVNAMVGGLSLLSPE 721
Cdd:cd08223    94 QKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIF-LTKSNIIkVGDLGIARVlESSSDMATTLIGTPYYMSPE 172
                          90
                  ....*....|....*...
gi 1720419116 722 LKTGKPPSASSDLYAYGC 739
Cdd:cd08223   173 LFSNKPYNHKSDVWALGC 190
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
629-742 6.04e-05

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 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.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 45.43  E-value: 6.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 629 YLMVPYYPKANLSA-VQASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFALNREQGI---VGDY-------D 697
Cdd:cd14012    80 YLLTEYAPGGSLSElLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAGTGivkLTDYslgktllD 159
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720419116 698 FTKSESQRASVNAMVgglslLSPEL-KTGKPPSASSDLYAYGCLFL 742
Cdd:cd14012   160 MCSRGSLDEFKQTYW-----LPPELaQGSKSPTRKTDVWDLGLLFL 200
Tudor_TDRD15_rpt4 cd20439
fourth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
33-133 6.23e-05

fourth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that 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.


Pssm-ID: 410510  Cd Length: 125  Bit Score: 43.25  E-value: 6.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116  33 VEDVVGSHVEDAVTFWAQNVSKNKDIMKIGCSLSEVCPLANsvfgnlDPKKIyGGL-----FSEDKCWYRCKVLKTISDD 107
Cdd:cd20439    11 VVDVKCSYVNSPGDFWCQLQTKSSELKSLMKQIQSYYLIHN------DPYKH-GQIacvakYSKDGKWYRAAVLKQVSAK 83
                          90       100
                  ....*....|....*....|....*.
gi 1720419116 108 KCLVRYIDYGNTEILNRSDIVEIPPE 133
Cdd:cd20439    84 EVDVIFVDYGNQERVLISDLRAIKPQ 109
Tudor_TDRD9 cd20431
Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is ...
90-134 6.64e-05

Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is an ATP-dependent DEAD-like RNA helicase required during spermatogenesis. It is involved in the biosynthesis of PIWI-interacting RNAs (piRNAs). A recessive deleterious mutation mutation in TDRD9 causes non-obstructive azoospermia in infertile men. TDRD9 contains an N-terminal HrpA-like RNA helicase module and a 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.


Pssm-ID: 410502  Cd Length: 101  Bit Score: 42.76  E-value: 6.64e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1720419116  90 SEDKCWYRCKVLKtISDDKCLVRYIDYGNTEILNRSDIVEIPPEL 134
Cdd:cd20431    54 ADMKKYYRAKILY-VSGSSAEVFFVDYGNTSQVPSSLLREIPETL 97
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
650-761 7.54e-05

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK 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.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 45.49  E-value: 7.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 650 TSEEAL-KVMKGVARGLHTLHSANIIHGSLHQNNVfaLNREQGIVGDYDFTKSESQRASVNAMVGGLSL-LSPELKTGKP 727
Cdd:cd06621   102 IGEKVLgKIAESVLKGLSYLHSRKIIHRDIKPSNI--LLTRKGQVKLCDFGVSGELVNSLAGTFTGTSYyMAPERIQGGP 179
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1720419116 728 PSASSDLYAYGcLFLwLSVQNQEFETNEDGIPKV 761
Cdd:cd06621   180 YSITSDVWSLG-LTL-LEVAQNRFPFPPEGEPPL 211
Tudor_SMN_SPF30-like cd21182
Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing ...
88-130 7.66e-05

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.


Pssm-ID: 410549  Cd Length: 50  Bit Score: 40.70  E-value: 7.66e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1720419116  88 LFSEDKCWYRCKVLK-TISDDKCLVRYIDYGNTEILNRSDIVEI 130
Cdd:cd21182     7 PYSDDGKYYEATIEEiTEESDTATVVFDGYGNSEEVPLSDLKPL 50
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
649-740 1.24e-04

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.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 44.91  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 649 LTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVfALNREQGI----VGDYDFTKSESQRASVNAMVGGLSLLSPELKT 724
Cdd:cd14039    96 LKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENI-VLQEINGKivhkIIDLGYAKDLDQGSLCTSFVGTLQYLAPELFE 174
                          90
                  ....*....|....*.
gi 1720419116 725 GKPPSASSDLYAYGCL 740
Cdd:cd14039   175 NKSYTVTVDYWSFGTM 190
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
655-738 1.42e-04

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-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. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-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.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 44.62  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 655 LKVMKGVARGLHTLHSANIIHGSLHQNNVFALNREQGIVGDYDFTKSESQRAS---VNAMVGGLSLLSPE---LKTGKPP 728
Cdd:cd14150    99 IDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTRWSGsqqVEQPSGSILWMAPEvirMQDTNPY 178
                          90
                  ....*....|
gi 1720419116 729 SASSDLYAYG 738
Cdd:cd14150   179 SFQSDVYAYG 188
Agenet pfam05641
Agenet domain; This domain is related to the TUDOR domain pfam00567. The function of the ...
94-132 1.57e-04

Agenet domain; This domain is related to the TUDOR domain pfam00567. The function of the agenet domain is unknown. This family now matches both the two Agenet domains in the FMR proteins.


Pssm-ID: 461700  Cd Length: 61  Bit Score: 40.37  E-value: 1.57e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1720419116  94 CWYRCKVLKTISDDKCLVRYIDYGN-------TEILNRSDIVEIPP 132
Cdd:pfam05641  16 AWFRAKVIKVLKGDKYLVEYDDLLDedgggplEEWVPASDIRPCPP 61
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
645-754 2.23e-04

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 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.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 44.05  E-value: 2.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 645 ASMPLTSEEALKVMKGVARGLHTLH--SANIIHGSLHQNNVF---ALNREQGIVGDYDFTKSESQrASVNAMV------- 712
Cdd:cd14159    88 SCPCLSWSQRLHVLLGTARAIQYLHsdSPSLIHGDVKSSNILldaALNPKLGDFGLARFSRRPKQ-PGMSSTLartqtvr 166
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1720419116 713 GGLSLLSPE-LKTGKpPSASSDLYAYGCLFLWLSVQNQEFETN 754
Cdd:cd14159   167 GTLAYLPEEyVKTGT-LSVEIDVYSFGVVLLELLTGRRAMEVD 208
Tudor_TDRD4_rpt2 cd20415
second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
91-145 2.55e-04

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.


Pssm-ID: 410486  Cd Length: 96  Bit Score: 40.88  E-value: 2.55e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720419116  91 EDKCWYRCKVLKTISDDKCLVRYIDYGNTEILNRSDIVEIPPE-LQFSSIAKKYRL 145
Cdd:cd20415    36 EDGAWYRARIIGLPGHREVEVKYVDFGNTATVTIKHVRKIKDDfLSLPEKARECRL 91
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
640-742 2.56e-04

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 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.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 44.03  E-value: 2.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 640 LSAVQASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFALNREQGIVGDYDFTKSE---SQRASVNAMVGGLS 716
Cdd:cd14158   105 LACLNDTPPLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLARASekfSQTIMTERIVGTTA 184
                          90       100
                  ....*....|....*....|....*.
gi 1720419116 717 LLSPELKTGKpPSASSDLYAYGCLFL 742
Cdd:cd14158   185 YMAPEALRGE-ITPKSDIFSFGVVLL 209
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
652-745 2.69e-04

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which 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. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The 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.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 43.54  E-value: 2.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 652 EEALKVMKGVARGLHTLHSANIIHGSLHQNNVFALnrEQGIV--GDYDFTKSESQRAS---VNAMVGGLSLLSPE---LK 723
Cdd:cd14062    89 LQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLH--EDLTVkiGDFGLATVKTRWSGsqqFEQPTGSILWMAPEvirMQ 166
                          90       100
                  ....*....|....*....|...
gi 1720419116 724 TGKPPSASSDLYAYG-CLFLWLS 745
Cdd:cd14062   167 DENPYSFQSDVYAFGiVLYELLT 189
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
640-740 4.31e-04

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of 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. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK 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 (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 43.21  E-value: 4.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 640 LSAVQASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFALNREQGIVG---DYDFTKSESQRASVNAMVGGLS 716
Cdd:cd13989    90 LNQPENCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRVIYkliDLGYAKELDQGSLCTSFVGTLQ 169
                          90       100
                  ....*....|....*....|....
gi 1720419116 717 LLSPELKTGKPPSASSDLYAYGCL 740
Cdd:cd13989   170 YLAPELFESKKYTCTVDYWSFGTL 193
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
655-738 4.33e-04

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.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 43.13  E-value: 4.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 655 LKVMKGVARGLHTLHSANIIHGSLHQNNVFALNREQGIVGDYDFTKSESQRA---SVNAMVGGLSLLSPE---LKTGKPP 728
Cdd:cd14151   107 IDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSgshQFEQLSGSILWMAPEvirMQDKNPY 186
                          90
                  ....*....|
gi 1720419116 729 SASSDLYAYG 738
Cdd:cd14151   187 SFQSDVYAFG 196
Tudor_TDRD15_rpt5 cd20440
fifth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
34-133 4.64e-04

fifth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that 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.


Pssm-ID: 410511  Cd Length: 127  Bit Score: 40.90  E-value: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116  34 EDVVGSHVEDAVTFWAQNVSKNKDIMKIGCSLSEVCPLANSVFGNLDPKKIYGGLFSEDKCWYRCKVLKTISDDKCLVRY 113
Cdd:cd20440    12 EEVYITHVYSPAKFYCQLDRNTEILEALMEKIAEISKLFNSQILDNCKTRLCLAKYFEDGQWYRALAHPVESSSHLSVYF 91
                          90       100
                  ....*....|....*....|
gi 1720419116 114 IDYGNTEILNRSDIVEIPPE 133
Cdd:cd20440    92 VDYGNKQIVEKNEVLPIPDT 111
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
644-764 5.56e-04

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 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.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 42.71  E-value: 5.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 644 QASMPLTSEEALK-VMKGVARGLHTLHSANIIHGSLHQNNVFALNREQGIVGDYDFTKSESQRASVNAMVGGLSLLSPEL 722
Cdd:cd07862   101 KVPEPGVPTETIKdMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIYSFQMALTSVVVTLWYRAPEV 180
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1720419116 723 KTGKPPSASSDLYAYGCLFLWLSVQNQEFETNEDgipkVDQF 764
Cdd:cd07862   181 LLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSD----VDQL 218
Tudor_TDRD6_rpt2 cd20421
second Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
92-133 6.03e-04

second 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 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.


Pssm-ID: 410492  Cd Length: 130  Bit Score: 40.48  E-value: 6.03e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1720419116  92 DKCWYRCKVLKTISDDKC-LVRYIDYGNTEILNRSDIVEIPPE 133
Cdd:cd20421    73 DGRWYRAVLQQVFSANRVvEVLHVDYGRKEVVSVSNLRYLAPE 115
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
653-744 6.51e-04

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-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. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-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.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 42.71  E-value: 6.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 653 EALKVMKGVARGLHTLHSANIIHGSLHQNNVFALNREQGIVGDYDFTKSESQRA---SVNAMVGGLSLLSPE---LKTGK 726
Cdd:cd14149   109 QLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSgsqQVEQPTGSILWMAPEvirMQDNN 188
                          90
                  ....*....|....*...
gi 1720419116 727 PPSASSDLYAYGCLFLWL 744
Cdd:cd14149   189 PFSFQSDVYSYGIVLYEL 206
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
231-540 8.07e-04

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 43.50  E-value: 8.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116  231 NELEKIWAEYNVAQEKIQtclneNEGNILIAERNEVQQklfvavdvfiLEVDDlpldkrlktlQDLATSLE-SVYGKAKE 309
Cdd:TIGR01612 1997 NELKDTLSDLKYKKEKIL-----NDVKLLLHKFDELNK----------LSCDS----------QNYDTILElSKQDKIKE 2051
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116  310 GTNNSEETLRKF-YDWQCTKREE-FASIRSETEaSLQHLVAWFQSSQKVFDLSLDEPLTSEDLIGNIDEILeKTEscvCK 387
Cdd:TIGR01612 2052 KIDNYEKEKEKFgIDFDVKAMEEkFDNDIKDIE-KFENNYKHSEKDNHDFSEEKDNIIQSKKKLKELTEAF-NTE---IK 2126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116  388 ELELSLIEQ-GVID------KEIILSTYSQVLQKIHSE----EKFIATLLSKYKDSVEFKKQMIDCLNKnpNVDYL---L 453
Cdd:TIGR01612 2127 IIEDKIIEKnDLIDkliemrKECLLFSYATLVETLKSKvinhSEFITSAAKFSKDFFEFIEDISDSLND--DIDALqikY 2204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116  454 SIKKTLKGLKAQLRWKLVEKSNLEESDdhdgTEIEKIKQEITQLRNSVFQEIYHEREEYEKL-----NSLTQKWFPELPL 528
Cdd:TIGR01612 2205 NLNQTKKHMISILADATKDHNNLIEKE----KEATKIINNLTELFTIDFNNADADILHNNKIqiiyfNSELHKSIESIKK 2280
                          330
                   ....*....|..
gi 1720419116  529 LYPEIGLLKYMN 540
Cdd:TIGR01612 2281 LYKKINAFKLLN 2292
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
617-753 8.87e-04

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; 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. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 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.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 41.84  E-value: 8.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 617 IFLFLCKSDPVAYLMvpyypkanlsavQASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFALNREQGIVGDY 696
Cdd:cd14189    78 IFLELCSRKSLAHIW------------KARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDF 145
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 697 DF-TKSESQRASVNAMVGGLSLLSPE--LKTGKPPsaSSDLYAYGCLFLWLSVQNQEFET 753
Cdd:cd14189   146 GLaARLEPPEQRKKTICGTPNYLAPEvlLRQGHGP--ESDVWSLGCVMYTLLCGNPPFET 203
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
629-791 9.67e-04

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.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 41.69  E-value: 9.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 629 YLMVPYYPKANL-SAVQASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVfaLNREQGIVGDYDFTKS----ES 703
Cdd:cd14007    76 YLILEYAPNGELyKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENI--LLGSNGELKLADFGWSvhapSN 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 704 QRasvNAMVGGLSLLSPELKTGKPPSASSDLYAYGCLFLWLSVQNQEFETNEDG-----IPKVDqFHLDDNV----KSLL 774
Cdd:cd14007   154 RR---KTFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQetykrIQNVD-IKFPSSVspeaKDLI 229
                         170
                  ....*....|....*....
gi 1720419116 775 CSLIYFRSS--MTAEQVLN 791
Cdd:cd14007   230 SKLLQKDPSkrLSLEQVLN 248
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
626-751 1.02e-03

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 42.52  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 626 PVAYLMVPYYPKANLSAVQASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFALNREQGIVGDYDF---TKSE 702
Cdd:PHA03207  159 STVCMVMPKYKCDLFTYVDRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAackLDAH 238
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1720419116 703 SQRASVNAMVGGLSLLSPELKTGKPPSASSDLYAYGCLFLWLSVQNQEF 751
Cdd:PHA03207  239 PDTPQCYGWSGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKNVTL 287
Tudor_vreteno-like_rpt1 cd20444
first Tudor domain found in Drosophila melanogaster protein vreteno and similar proteins; ...
92-134 1.04e-03

first Tudor domain found in Drosophila melanogaster protein vreteno and similar proteins; Vreteno is a gonad-specific protein essential for germline development to repress transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process in both germline and somatic gonadal tissues by mediating the repression of transposable elements during meiosis. Vreteno contains two Tudor domains. The model corresponds to the first 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.


Pssm-ID: 410515  Cd Length: 55  Bit Score: 37.67  E-value: 1.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1720419116  92 DKCWYRCKVLKTIS-DDKCLVRYIDYGNTEILNRSDIVEIPPEL 134
Cdd:cd20444    12 DGNHYRAIVLRVLNpDLKILVRFVDFGNVEVMKLENLYECPEYL 55
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
622-778 1.07e-03

Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 41.77  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 622 CKSDPVAYLMVPYYPKANLSAVQAS--MPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFALNREQGIVGDYDFT 699
Cdd:cd14045    71 CIEVPNVAIITEYCPKGSLNDVLLNedIPLNWGFRFSFATDIARGMAYLHQHKIYHGRLKSSNCVIDDRWVCKIADYGLT 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 700 KSESQRASVNAmvGGLS------LLSPELK--TGKPPSASSDLYAYGCLFLwlsvqnqEFETNEDGIPKvDQFHLDDNVK 771
Cdd:cd14045   151 TYRKEDGSENA--SGYQqrlmqvYLPPENHsnTDTEPTQATDVYSYAIILL-------EIATRNDPVPE-DDYSLDEAWC 220

                  ....*..
gi 1720419116 772 SLLCSLI 778
Cdd:cd14045   221 PPLPELI 227
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
629-784 1.11e-03

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.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 41.77  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 629 YLMVPYYPKANL-SAVQASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFALNREQGIVGDYDFT-KSESQRA 706
Cdd:cd14117    82 YLILEYAPRGELyKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSvHAPSLRR 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 707 svNAMVGGLSLLSPELKTGKPPSASSDLYAYGCLFLWLSVQNQEFETNEDG-----IPKVD-QF--HLDDNVKSLLCSLI 778
Cdd:cd14117   162 --RTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTetyrrIVKVDlKFppFLSDGSRDLISKLL 239

                  ....*.
gi 1720419116 779 YFRSSM 784
Cdd:cd14117   240 RYHPSE 245
Tudor_vreteno-like_rpt2 cd20445
second Tudor domain found in Drosophila melanogaster protein vreteno and similar proteins; ...
91-136 1.19e-03

second Tudor domain found in Drosophila melanogaster protein vreteno and similar proteins; Vreteno is a gonad-specific protein essential for germline development to repress transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process in both germline and somatic gonadal tissues by mediating the repression of transposable elements during meiosis. Vreteno contains two Tudor domains. The 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.


Pssm-ID: 410516  Cd Length: 56  Bit Score: 37.79  E-value: 1.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1720419116  91 EDKcWYRCKVLKTISDDKCLVRYIDYGNTEILNRSDIVEIPPELQF 136
Cdd:cd20445    10 MDK-WYRAVCLESVGDGRPTVLFCDYGNILMARLTDIRPFPPTFAT 54
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
661-740 1.51e-03

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 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.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 41.26  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 661 VARGLHTLHSANIIHGSLHQNNVFALNREQGIVGDYDFTK---SESQRAsvNAMVGGLSLLSPELKTGKPPSASSDLYAY 737
Cdd:cd08221   110 IVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKvldSESSMA--ESIVGTPYYMSPELVQGVKYNFKSDIWAV 187

                  ...
gi 1720419116 738 GCL 740
Cdd:cd08221   188 GCV 190
Tudor_TDRD1_rpt1 cd20408
first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
89-132 1.94e-03

first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the first 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.


Pssm-ID: 410479  Cd Length: 130  Bit Score: 39.28  E-value: 1.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720419116  89 FSEDKCWYRCKVLKT-ISDDKCLVRYIDYGNTEI--LNR-----SDIVEIPP 132
Cdd:cd20408    57 YSEDQNWYRALVQTVdVQQKKAGVFYIDYGNEETvpLNRiqplkKDIELFPP 108
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
649-771 2.20e-03

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 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.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 40.70  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 649 LTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVfaLNREQGIVG--DYDFTKSESQRASVNAMVGGLSL-LSPELKTG 725
Cdd:cd14002    96 LPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNI--LIGKGGVVKlcDFGFARAMSCNTLVLTSIKGTPLyMAPELVQE 173
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720419116 726 KPPSASSDLYAYGCLFLWLSVQNQEFETNEdgIPKVDQFHLDDNVK 771
Cdd:cd14002   174 QPYDHTADLWSLGCILYELFVGQPPFYTNS--IYQLVQMIVKDPVK 217
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
631-741 2.81e-03

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 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.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 40.92  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 631 MVPYYPKANLSAVQASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFaLNREQGI--VGDYDFTKSESQRASV 708
Cdd:cd07854    93 IVQEYMETDLANVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVF-INTEDLVlkIGDFGLARIVDPHYSH 171
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720419116 709 NamvGGLS-------------LLSPELKTgkppsASSDLYAYGCLF 741
Cdd:cd07854   172 K---GYLSeglvtkwyrsprlLLSPNNYT-----KAIDMWAAGCIF 209
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
661-754 3.54e-03

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks 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 specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). 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.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 39.94  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 661 VARGLHTLHSANIIHGSLHQNNVF-ALNREQGIVGDYDFTKSESQRASV-NAMVGGLSLLSPELKTGKPPSASSDLYAYG 738
Cdd:cd08225   110 ISLGLKHIHDRKILHRDIKSQNIFlSKNGMVAKLGDFGIARQLNDSMELaYTCVGTPYYLSPEICQNRPYNNKTDIWSLG 189
                          90
                  ....*....|....*.
gi 1720419116 739 CLFLWLSVQNQEFETN 754
Cdd:cd08225   190 CVLYELCTLKHPFEGN 205
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
622-743 3.81e-03

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 40.02  E-value: 3.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 622 CKSDPVAYLMVPYYPKANL------SAVQASMP-----------LTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVf 684
Cdd:cd05047    65 CEHRGYLYLAIEYAPHGNLldflrkSRVLETDPafaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNI- 143
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720419116 685 aLNREQGIVGDYDFTKSESQRASVNAMVGGLSL--LSPELKTGKPPSASSDLYAYGCLfLW 743
Cdd:cd05047   144 -LVGENYVAKIADFGLSRGQEVYVKKTMGRLPVrwMAIESLNYSVYTTNSDVWSYGVL-LW 202
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
649-740 3.99e-03

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 39.87  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 649 LTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFALNREQGIVGDYDF--TKSESQRASVNAMVGGLSLLSPELKTGK 726
Cdd:cd14114    97 MSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRSNEVKLIDFglATHLDPKESVKVTTGTAEFAAPEIVERE 176
                          90
                  ....*....|....
gi 1720419116 727 PPSASSDLYAYGCL 740
Cdd:cd14114   177 PVGFYTDMWAVGVL 190
Tudor_TDRD15_rpt3 cd20438
third Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
24-133 4.25e-03

third Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the third 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.


Pssm-ID: 410509  Cd Length: 141  Bit Score: 38.61  E-value: 4.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116  24 MDEDTHYnkvedvVG--SHVEDAVTFWAQNVSKNKD---IMKIGCSLSEVCPLANSVFGNLDPKKIYGGLFSEDKCWYRC 98
Cdd:cd20438     1 MEVDAAY------VAfvEYVLNPSNFWIRTDEYNNEfqaLMKNIADIYNLCGNDEELLKKPEPGLLCCARYSKDRHYYRA 74
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1720419116  99 kVLKTISDDKCLVRYIDYGNTEILNRSDIVEIPPE 133
Cdd:cd20438    75 -VITEVLDLKVSVYFLDFGNTDTVPFYDVKTLLPE 108
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
629-741 4.99e-03

Catalytic domain of fungal Rim15-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 Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-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.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 39.77  E-value: 4.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 629 YLMVPYYPKANL-SAVQASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFALNREQGIVGDYDFTKSESQRAS 707
Cdd:cd05611    73 YLVMEYLNGGDCaSLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGLEKRH 152
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1720419116 708 VNAMVGGLSLLSPELKTGKPPSASSDLYAYGCLF 741
Cdd:cd05611   153 NKKFVGTPDYLAPETILGVGDDKMSDWWSLGCVI 186
Tudor_SPF30 cd20399
Tudor domain found in survival of motor neuron-related-splicing factor 30 (SPF30) and similar ...
87-121 5.37e-03

Tudor domain found in survival of motor neuron-related-splicing factor 30 (SPF30) and similar proteins; 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. Overexpression of SPF30 causes apoptosis. It contains one 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.


Pssm-ID: 410470 [Multi-domain]  Cd Length: 55  Bit Score: 35.75  E-value: 5.37e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1720419116  87 GLFSEDKCWYRCKVLKTISDDKCLVRYIDYGNTEI 121
Cdd:cd20399     9 AVWSEDGQYYEATIEEISEDGTCTVTFDGYGNTEV 43
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
661-740 6.02e-03

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 39.61  E-value: 6.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 661 VARGLHTLH-SANIIHGSLHQNNVFaLNrEQG--IVGDYDFTKSESQRASVNAMVGG------------LSLLSPELKTG 725
Cdd:cd14011   123 ISEALSFLHnDVKLVHGNICPESVV-IN-SNGewKLAGFDFCISSEQATDQFPYFREydpnlpplaqpnLNYLAPEYILS 200
                          90
                  ....*....|....*
gi 1720419116 726 KPPSASSDLYAYGCL 740
Cdd:cd14011   201 KTCDPASDMFSLGVL 215
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
649-740 6.66e-03

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK 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.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 39.26  E-value: 6.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 649 LTSEEALKVMKGVARGLHTLHSANIIHGSLH-QNNVFALNREQG--IVGDYDFTKSESQRASVNAMVGGLSLLSPELKTG 725
Cdd:cd14106   105 LTEADVRRLMRQILEGVQYLHERNIVHLDLKpQNILLTSEFPLGdiKLCDFGISRVIGEGEEIREILGTPDYVAPEILSY 184
                          90
                  ....*....|....*
gi 1720419116 726 KPPSASSDLYAYGCL 740
Cdd:cd14106   185 EPISLATDMWSIGVL 199
Tudor_AKAP1 cd20407
Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; ...
95-130 6.74e-03

Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), 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. It contains 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.


Pssm-ID: 410478  Cd Length: 76  Bit Score: 36.03  E-value: 6.74e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1720419116  95 WYRCKVLKTISD-DKCLVRYIDYGNTEILNRSDIVEI 130
Cdd:cd20407    19 WYRAQVVGVFEEtDEVEIKYLDYGGYERVPVDDLRQI 55
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
649-738 9.13e-03

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin 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.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 38.72  E-value: 9.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 649 LTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFALN--REQGIVGDYDFTKSESQRASVNAMVGGLSLLSPELKTGK 726
Cdd:cd14107    95 VTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSptREDIKICDFGFAQEITPSEHQFSKYGSPEFVAPEIVHQE 174
                          90
                  ....*....|..
gi 1720419116 727 PPSASSDLYAYG 738
Cdd:cd14107   175 PVSAATDIWALG 186
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
648-744 9.48e-03

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates 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. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK 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.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 38.69  E-value: 9.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419116 648 PLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFaLNREqGIVGDYDFTKSE---SQRASVNAMVGGLSLLSPELKT 724
Cdd:cd14008   104 PLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLL-LTAD-GTVKISDFGVSEmfeDGNDTLQKTAGTPAFLAPELCD 181
                          90       100
                  ....*....|....*....|....
gi 1720419116 725 GKPPSASS---DLYAYG-CLFLWL 744
Cdd:cd14008   182 GDSKTYSGkaaDIWALGvTLYCLV 205
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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