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Conserved domains on  [gi|1907111721|ref|XP_036015215|]
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triple functional domain protein isoform X4 [Mus musculus]

Protein Classification

triple functional domain protein( domain architecture ID 12213595)

triple functional domain protein (Trio) is a large serine/threonine-protein kinase and Rho guanine nucleotide exchange factor that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates and functions as a GEF for Rac1, RhoG, and RhoA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
2760-3022 0e+00

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio 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: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 581.55  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2760 WKDNFDAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVL 2839
Cdd:cd14113      1 WKDNFDSFYSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQVTHELGVLQSLQHPQLVGLLDTFETPTSYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2840 VLEMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAVQLNTTY 2919
Cdd:cd14113     81 VLEMADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSKPTIKLADFGDAVQLNTTY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2920 YIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFV 2999
Cdd:cd14113    161 YIHQLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPDDYFKGVSQKAKDFV 240
                          250       260
                   ....*....|....*....|...
gi 1907111721 3000 CFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14113    241 CFLLQMDPAKRPSAALCLQEQWL 263
SH3-RhoG_link super family cl24983
SH3-RhoGEF linking unstructured region; This family of natively unstructured but conserved ...
1683-1940 1.36e-150

SH3-RhoGEF linking unstructured region; This family of natively unstructured but conserved residues from higher eukaryotes is found to lie between an SH3 pfam00018 and the RhoGEF, pfam00621, domains. It is serine-rich and likely to be acidic and natively unstructured.


The actual alignment was detected with superfamily member pfam16609:

Pssm-ID: 465196  Cd Length: 261  Bit Score: 468.13  E-value: 1.36e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1683 SLCIAHSRSSMEMEGIFNHKDSLSVSSNDASPPASVASLQP-HMIGAQSSPGPKRPGNTLRKWLTSPVRRLSSGKADGHA 1761
Cdd:pfam16609    1 MLCIAHSRSSMEMEGIFNHKDTLSVYSNDSIMPGSSATLQPgHGISSHASPGPKRPGNTLRKWLTSPVRRLSSGKADGHV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1762 KKLAHKHKKSREVRKS--ADAGSQKDSDDSAATPQDETIEERGRNEGLSSGTLSKSSSSGMQSCGEEEGEEGADAVPLPP 1839
Cdd:pfam16609   81 KKLAHKHKKSREVRKSreITAGSQKDSDDSAATPQDETVEERVRNEGLSSGTLSKSSSSGMQSCGEEEGEEGADSVPLPP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1840 PMAIQQHSLLQPDSQDDKASSRLLVRPTSSETPSAAELVSAIEELVKSKMALEDRPSSLLVDQGDSSSPSFNPSDNSLLS 1919
Cdd:pfam16609  161 PMAIQQHSLLQPDSQDDKTSSRLFVRPSSSETPSAAELVSAIEELVKSKMALEDRPSSLSVDQGDSSSPSFNPSDNSLLS 240
                          250       260
                   ....*....|....*....|.
gi 1907111721 1920 SSSPIDEMEERKCSSLKRRHY 1940
Cdd:pfam16609  241 SSSPISEMDERRSSFLKKRHY 261
PH2_Kalirin_Trio_p63RhoGEF cd13241
p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor ...
2116-2254 1.19e-79

p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor p63RhoGEF is an effector of the heterotrimeric G protein, Galphaq and linking Galphaq-coupled receptors (GPCRs) to the activation of RhoA. The Dbl(DH) and PH domains of p63RhoGEF interact with the effector-binding site and the C-terminal region of Galphaq and appear to relieve autoinhibition of the catalytic DH domain by the PH domain. Trio, Duet, and p63RhoGEF are shown to constitute a family of Galphaq effectors that appear to activate RhoA both in vitro and in intact cells. Dbs is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a rhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Trio is a multidomain signaling protein that contains two RhoGEF(DH)-PH domains in tandem. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 270061  Cd Length: 140  Bit Score: 259.50  E-value: 1.19e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2116 VGRLQGFDGKIVAQGKLLLQDTFLVTDQDAGLLPRCKERRVFLFEQIVIFSEPLDKKKGFSMPGFLFKNSIKVSCLCLEE 2195
Cdd:cd13241      1 VGRLQGFDGKITAQGKLLLQGTLLVSEPSAGLLQKGKERRVFLFEQIIIFSEILGKKTQFSNPGYIYKNHIKVNKMSLEE 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2196 NVESDPCKFALTSRTG-DAVETFVLHSSSPSVRQTWIHEINQILENQRNFLNALTSPIEY 2254
Cdd:cd13241     81 NVDGDPLRFALKSRDPnNPSETFILQAASPEVRQEWVDTINQILDTQRDFLKALQSPIAY 140
PH1_Kalirin_Trio_like cd13240
Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; ...
1440-1562 6.08e-72

Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; RhoGEFs, Kalirin and Trio, the mammalian homologs of Drosophila Trio and Caenorhabditis elegans UNC-73 regulate a novel step in secretory granule maturation. Their signaling modulates the extent to which regulated cargo enter and remain in the regulated secretory pathway. This allows for fine tuning of peptides released by a single secretory cell type with impaired signaling leading to pathological states. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Kalirin and Trio are encoded by separate genes in mammals and by a single one in invertebrates. Kalirin and Trio share the same complex multidomain structure and display several splice variants. The longest Kalirin and Trio proteins have a Sec14 domain, a stretch of spectrin repeats, a RhoGEF(DH)/PH cassette (also called GEF1), an SH3 domain, a second RhoGEF(DH)/PH cassette (also called GEF2), a second SH3 domain, Ig/FNIII domains, and a kinase domain. The first RhoGEF(DH)/PH cassette catalyzes exchange on Rac1 and RhoG while the second RhoGEF(DH)/PH cassette is specific for RhoA. Kalirin and Trio are closely related to p63RhoGEF and have PH domains of similar function. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains.


:

Pssm-ID: 270060  Cd Length: 123  Bit Score: 236.51  E-value: 6.08e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1440 MLEGFDENIESQGELILQESFQVWDPKTLIRKGRERHLFLFEMSLVFSKEVKDSSGRSKYLYKSKLFTSELGVTEHVEGD 1519
Cdd:cd13240      1 LLEGCDEDLDSLGEVILQDSFQVWDPKQLIRKGRERHVFLFELCLVFSKEVKDSNGKSKYIYKSRLMTSEIGVTEHIEGD 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1907111721 1520 PCKFALWVGRTPTSDNKIVLKASSIENKQDWIKHIREVIQERT 1562
Cdd:cd13240     81 PCKFALWTGRVPTSDNKIVLKASSLEVKQTWVKKLREVIQERI 123
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
1938-2111 1.01e-50

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


:

Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 178.26  E-value: 1.01e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1938 RHYVLQELVETERDYVRDLGCVVEGYMALMKEDGVPDDmKGKDKIVFGNIHQIYDWHRDFFLGELEKCLED---PEKLGS 2014
Cdd:cd00160      1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLS-PEEVELLFGNIEEIYEFHRIFLKSLEERVEEWdksGPRIGD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2015 LFVKHERRLHMYIVYCQNKPKSEHIVSEYI--DTFFEDLKQRLG---HRLQLTDLLIKPVQRIMKYQLLLKDFLKYSKKA 2089
Cdd:cd00160     80 VFLKLAPFFKIYSEYCSNHPDALELLKKLKkfNKFFQEFLEKAEsecGRLKLESLLLKPVQRLTKYPLLLKELLKHTPDG 159
                          170       180
                   ....*....|....*....|..
gi 1907111721 2090 SLDTSELEKAVEVMCIVPKRCN 2111
Cdd:cd00160    160 HEDREDLKKALEAIKEVASQVN 181
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
1263-1433 1.75e-44

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


:

Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 160.16  E-value: 1.75e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1263 FIMAELIQTEKAYVRDLRECMDTYLWEMTSGVEEIPPGIVNkelIIFGNMQEIYEFHNnIFLKELEKY----EQLPEDVG 1338
Cdd:cd00160      3 EVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSPEEVE---LLFGNIEEIYEFHR-IFLKSLEERveewDKSGPRIG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1339 HCFVTWADKFQMYVTYCKNKPDSTQLILEHAG--SYFDEIQQRHGLAN---SISSYLIKPVQRITKYQLLLKELLTCCEE 1413
Cdd:cd00160     79 DVFLKLAPFFKIYSEYCSNHPDALELLKKLKKfnKFFQEFLEKAESECgrlKLESLLLKPVQRLTKYPLLLKELLKHTPD 158
                          170       180
                   ....*....|....*....|...
gi 1907111721 1414 G---KGEIKDGLEVMLSVPKRAN 1433
Cdd:cd00160    159 GhedREDLKKALEAIKEVASQVN 181
SH3_Kalirin_2 cd11853
Second Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
2527-2585 1.47e-34

Second Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or TRAD, is a large neuronal dual Rho guanine nucleotide exchange factor (RhoGEF) that activates Rac1, RhoA, and RhoG using two RhoGEF domains. Kalirin exists in many isoforms generated by alternative splicing and the use of multiple promoters; the major isoforms are kalirin-7, -9, and -12, which differ at their C-terminal ends. Kalirin-12, the longest isoform, contains an N-terminal Sec14p domain, spectrin-like repeats, two RhoGEF domains, two SH3 domains, as well as Ig, FNIII, and kinase domains at the C-terminal end. Kalirin-7 contains only a single RhoGEF domain and does not contain an SH3 domain. Kalirin, through its many isoforms, interacts with many different proteins and is able to localize to different locations within the cell. It influences neurite initiation, axon growth, dendritic morphogenesis, vesicle trafficking, neuronal maintenance, and neurodegeneration. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


:

Pssm-ID: 212787  Cd Length: 59  Bit Score: 127.17  E-value: 1.47e-34
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907111721 2527 TMLVTHEYTAVKEDEINVYQGEVVQILASNQQNMFLVFRAATDQCPAAEGWIPGFVLGH 2585
Cdd:cd11853      1 TMPVIQDYYALKEDEICVSQGEVVQILAANQQNMFLVYRPATDQSPAAEGWIPGSVLGH 59
SH3_Kalirin_1 cd11852
First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
1627-1686 7.15e-32

First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or TRAD, is a large neuronal dual Rho guanine nucleotide exchange factor (RhoGEF) that activates Rac1, RhoA, and RhoG using two RhoGEF domains. Kalirin exists in many isoforms generated by alternative splicing and the use of multiple promoters; the major isoforms are kalirin-7, -9, and -12, which differ at their C-terminal ends. Kalirin-12, the longest isoform, contains an N-terminal Sec14p domain, spectrin-like repeats, two RhoGEF domains, two SH3 domains, as well as Ig, FNIII, and kinase domains at the C-terminal end. Kalirin-7 contains only a single RhoGEF domain and does not contain an SH3 domain. Kalirin, through its many isoforms, interacts with many different proteins and is able to localize to different locations within the cell. It influences neurite initiation, axon growth, dendritic morphogenesis, vesicle trafficking, neuronal maintenance, and neurodegeneration. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


:

Pssm-ID: 212786  Cd Length: 62  Bit Score: 119.81  E-value: 7.15e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907111721 1627 ELTVVIHDFTACNSNELTIRRGQTVEVLERPHDKPDWCLVRTT--DRSPAAEGLVPCGSLCI 1686
Cdd:cd11852      1 ELTVVIEDFEATSSQELTVSKGQTVEVLERPSSRPDWCLVRTLeqDNSPPQEGLVPSSILCI 62
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
535-751 3.74e-25

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 105.99  E-value: 3.74e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  535 QLCVFQQDVQQVLDWIENHGEAFLSkhTGVGKSLHRARALQKRHEDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIY 614
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  615 QAAHQLEDRIQDFVRRVEQRKILLDMSV---SFHTHVKELWTWLEELQKELLDDVYAESVEAVQDLIKRFgqqqqttlQV 691
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALdlqQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKH--------KE 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  692 TVNVIKEGEDLIQQLRDSAISSNKTPHNSSINHIETVLQQLDEAQSQMEELFQERKIKLE 751
Cdd:cd00176    151 LEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
I-set pfam07679
Immunoglobulin I-set domain;
2657-2748 4.44e-22

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 92.71  E-value: 4.44e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2657 PEFVIPLSEVTCETGETVVFRCRVCGRPKASITWKGPEHnTLNNDDHYSISYSDiGEATLKIIGVSTEDDGIYTCIAVND 2736
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQ-PLRSSDRFKVTYEG-GTYTLTISNVQPDDSGKYTCVATNS 78
                           90
                   ....*....|..
gi 1907111721 2737 MGSASSSASLRV 2748
Cdd:pfam07679   79 AGEAEASAELTV 90
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
37-172 5.81e-22

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


:

Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 95.06  E-value: 5.81e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721    37 LKEKVAYLSGGR--DKRGGPILTFPARS--NHDRIRQEDLRRLISYLACIPSEE---VCKRGFTVIVDMRGSK-----WD 104
Cdd:smart00516    2 LELLKAYIPGGRgyDKDGRPVLIERAGRfdLKSVTLEELLRYLVYVLEKILQEEkktGGIEGFTVIFDLKGLSmsnpdLS 81
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907111721   105 SIKPLLKILQESFPCCIHIALIIKPDNFWQ---KQRTNFGSSKFEFETNMVSL---EGLTKVVDPSQLTPEFDG 172
Cdd:smart00516   82 VLRKILKILQDHYPERLGKVYIINPPWFFRvlwKIIKPFLDEKTREKIRFVGNdskEELLEYIDKEQLPEELGG 155
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
876-1105 8.89e-19

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 87.50  E-value: 8.89e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  876 QLRHLQAEVKQVLGWIRNGESMLNAGLiTASSLQEAEQLQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDMIRD 955
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  956 CAEKVASHWQQLMLKMEDRLKLVNASVAFYKTSEQVCSVlesleqeykreEDWCGGADKLGPNSETDHVTPMISKHLEQK 1035
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL-----------EQWLEEKEAALASEDLGKDLESVEELLKKH 148
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1036 EAFLKACTlarrNADVFLKYLHRNSVSMPGmvTHIKAPEQQVKNILNELFQRENRVLHYWTMRKRRLDQC 1105
Cdd:cd00176    149 KELEEELE----AHEPRLKSLNELAEELLE--EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
309-534 1.08e-17

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 84.42  E-value: 1.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  309 QLRLFEQDAEKMFDWITHnKGLFLNSyTEIGTSHPHAMELQTQHNHFAMNCMNVYVNINRIMSVANRLVESGHYASQQIK 388
Cdd:cd00176      1 KLQQFLRDADELEAWLSE-KEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  389 QIANQLEQEWKAFAAALDERSTLLDMSSIFHQKAEKyMSNVDSWCKACGEV----DLPSELQDLEDAIHHHQGIYEHITL 464
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAAlaseDLGKDLESVEELLKKHKELEEELEA 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  465 AysevSQDGKSLLDKLQRPLTPGSSDSLTasanyskavhHVLDVIHEVLHHQRQLENIWQHRKVRLHQRL 534
Cdd:cd00176    158 H----EPRLKSLNELAEELLEEGHPDADE----------EIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
755-982 1.79e-16

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 80.95  E-value: 1.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  755 QLRIFERDAidiiSDLESWNDELSQQMNDFDT-EDLTIAEQRLQHHADKALTMNNltfdviHQGQdllqyVNEVQASGvE 833
Cdd:cd00176      1 KLQQFLRDA----DELEAWLSEKEELLSSTDYgDDLESVEALLKKHEALEAELAA------HEER-----VEALNELG-E 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  834 LLCDRDVDMATRVQDLLEFLHEKQQELDLAAEQHRKHLEQCVQLRHLQAEVKQVLGWIRNGESMLNAGLITaSSLQEAEQ 913
Cdd:cd00176     65 QLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLG-KDLESVEE 143
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  914 LQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDM-IRDCAEKVASHWQQLMLKMEDRLKLVNASV 982
Cdd:cd00176    144 LLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
188-413 3.64e-15

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 77.10  E-value: 3.64e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  188 FEEYISNAAHMLSRLEELQDVLAKKELPQDLEGARNMIDEHSQLKK--KVIKAPIEDLDLEGQKLLQriqssdsfpkknS 265
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAelAAHEERVEALNELGEQLIE------------E 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  266 GSGNADlqnllpKVSTMLDRLHSTRQHLHQMWHVRKLKLDQCFQLRLFEQDAEKMFDWIThNKGLFLNSyTEIGTSHPHA 345
Cdd:cd00176     70 GHPDAE------EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLE-EKEAALAS-EDLGKDLESV 141
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907111721  346 MELQTQHNHFAMNCMNVYVNINRIMSVANRLVESGHYASQ-QIKQIANQLEQEWKAFAAALDERSTLLD 413
Cdd:cd00176    142 EELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC smart00150
Spectrin repeats;
1111-1211 9.08e-14

Spectrin repeats;


:

Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 69.67  E-value: 9.08e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  1111 FERSAKQALEWIHDNGEfyLSTHTSTGSSIQHTQELLKEHEEFQITAKQTKERVKLLIQLADGFCEKGHAHAAEIKKCVT 1190
Cdd:smart00150    3 FLRDADELEAWLEEKEQ--LLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 1907111721  1191 AVDKRYRDFSLRMEKYRTSLE 1211
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
 
Name Accession Description Interval E-value
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
2760-3022 0e+00

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio 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: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 581.55  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2760 WKDNFDAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVL 2839
Cdd:cd14113      1 WKDNFDSFYSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQVTHELGVLQSLQHPQLVGLLDTFETPTSYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2840 VLEMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAVQLNTTY 2919
Cdd:cd14113     81 VLEMADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSKPTIKLADFGDAVQLNTTY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2920 YIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFV 2999
Cdd:cd14113    161 YIHQLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPDDYFKGVSQKAKDFV 240
                          250       260
                   ....*....|....*....|...
gi 1907111721 3000 CFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14113    241 CFLLQMDPAKRPSAALCLQEQWL 263
SH3-RhoG_link pfam16609
SH3-RhoGEF linking unstructured region; This family of natively unstructured but conserved ...
1683-1940 1.36e-150

SH3-RhoGEF linking unstructured region; This family of natively unstructured but conserved residues from higher eukaryotes is found to lie between an SH3 pfam00018 and the RhoGEF, pfam00621, domains. It is serine-rich and likely to be acidic and natively unstructured.


Pssm-ID: 465196  Cd Length: 261  Bit Score: 468.13  E-value: 1.36e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1683 SLCIAHSRSSMEMEGIFNHKDSLSVSSNDASPPASVASLQP-HMIGAQSSPGPKRPGNTLRKWLTSPVRRLSSGKADGHA 1761
Cdd:pfam16609    1 MLCIAHSRSSMEMEGIFNHKDTLSVYSNDSIMPGSSATLQPgHGISSHASPGPKRPGNTLRKWLTSPVRRLSSGKADGHV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1762 KKLAHKHKKSREVRKS--ADAGSQKDSDDSAATPQDETIEERGRNEGLSSGTLSKSSSSGMQSCGEEEGEEGADAVPLPP 1839
Cdd:pfam16609   81 KKLAHKHKKSREVRKSreITAGSQKDSDDSAATPQDETVEERVRNEGLSSGTLSKSSSSGMQSCGEEEGEEGADSVPLPP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1840 PMAIQQHSLLQPDSQDDKASSRLLVRPTSSETPSAAELVSAIEELVKSKMALEDRPSSLLVDQGDSSSPSFNPSDNSLLS 1919
Cdd:pfam16609  161 PMAIQQHSLLQPDSQDDKTSSRLFVRPSSSETPSAAELVSAIEELVKSKMALEDRPSSLSVDQGDSSSPSFNPSDNSLLS 240
                          250       260
                   ....*....|....*....|.
gi 1907111721 1920 SSSPIDEMEERKCSSLKRRHY 1940
Cdd:pfam16609  241 SSSPISEMDERRSSFLKKRHY 261
PH2_Kalirin_Trio_p63RhoGEF cd13241
p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor ...
2116-2254 1.19e-79

p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor p63RhoGEF is an effector of the heterotrimeric G protein, Galphaq and linking Galphaq-coupled receptors (GPCRs) to the activation of RhoA. The Dbl(DH) and PH domains of p63RhoGEF interact with the effector-binding site and the C-terminal region of Galphaq and appear to relieve autoinhibition of the catalytic DH domain by the PH domain. Trio, Duet, and p63RhoGEF are shown to constitute a family of Galphaq effectors that appear to activate RhoA both in vitro and in intact cells. Dbs is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a rhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Trio is a multidomain signaling protein that contains two RhoGEF(DH)-PH domains in tandem. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270061  Cd Length: 140  Bit Score: 259.50  E-value: 1.19e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2116 VGRLQGFDGKIVAQGKLLLQDTFLVTDQDAGLLPRCKERRVFLFEQIVIFSEPLDKKKGFSMPGFLFKNSIKVSCLCLEE 2195
Cdd:cd13241      1 VGRLQGFDGKITAQGKLLLQGTLLVSEPSAGLLQKGKERRVFLFEQIIIFSEILGKKTQFSNPGYIYKNHIKVNKMSLEE 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2196 NVESDPCKFALTSRTG-DAVETFVLHSSSPSVRQTWIHEINQILENQRNFLNALTSPIEY 2254
Cdd:cd13241     81 NVDGDPLRFALKSRDPnNPSETFILQAASPEVRQEWVDTINQILDTQRDFLKALQSPIAY 140
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
2768-3022 8.65e-75

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 250.14  E-value: 8.65e-75
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMK--RDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMAD 2845
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKkdRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  2846 QGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQLNTTYYIHQLL 2925
Cdd:smart00220   81 GGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDE---DGHVKLADFGLARQLDPGEKLTTFV 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  2926 GNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQE 3005
Cdd:smart00220  158 GTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLLVK 237
                           250
                    ....*....|....*..
gi 1907111721  3006 DPAKRPSAALALQEQWL 3022
Cdd:smart00220  238 DPEKRLTAEEALQHPFF 254
PH1_Kalirin_Trio_like cd13240
Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; ...
1440-1562 6.08e-72

Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; RhoGEFs, Kalirin and Trio, the mammalian homologs of Drosophila Trio and Caenorhabditis elegans UNC-73 regulate a novel step in secretory granule maturation. Their signaling modulates the extent to which regulated cargo enter and remain in the regulated secretory pathway. This allows for fine tuning of peptides released by a single secretory cell type with impaired signaling leading to pathological states. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Kalirin and Trio are encoded by separate genes in mammals and by a single one in invertebrates. Kalirin and Trio share the same complex multidomain structure and display several splice variants. The longest Kalirin and Trio proteins have a Sec14 domain, a stretch of spectrin repeats, a RhoGEF(DH)/PH cassette (also called GEF1), an SH3 domain, a second RhoGEF(DH)/PH cassette (also called GEF2), a second SH3 domain, Ig/FNIII domains, and a kinase domain. The first RhoGEF(DH)/PH cassette catalyzes exchange on Rac1 and RhoG while the second RhoGEF(DH)/PH cassette is specific for RhoA. Kalirin and Trio are closely related to p63RhoGEF and have PH domains of similar function. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains.


Pssm-ID: 270060  Cd Length: 123  Bit Score: 236.51  E-value: 6.08e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1440 MLEGFDENIESQGELILQESFQVWDPKTLIRKGRERHLFLFEMSLVFSKEVKDSSGRSKYLYKSKLFTSELGVTEHVEGD 1519
Cdd:cd13240      1 LLEGCDEDLDSLGEVILQDSFQVWDPKQLIRKGRERHVFLFELCLVFSKEVKDSNGKSKYIYKSRLMTSEIGVTEHIEGD 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1907111721 1520 PCKFALWVGRTPTSDNKIVLKASSIENKQDWIKHIREVIQERT 1562
Cdd:cd13240     81 PCKFALWTGRVPTSDNKIVLKASSLEVKQTWVKKLREVIQERI 123
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
1938-2111 1.01e-50

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 178.26  E-value: 1.01e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1938 RHYVLQELVETERDYVRDLGCVVEGYMALMKEDGVPDDmKGKDKIVFGNIHQIYDWHRDFFLGELEKCLED---PEKLGS 2014
Cdd:cd00160      1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLS-PEEVELLFGNIEEIYEFHRIFLKSLEERVEEWdksGPRIGD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2015 LFVKHERRLHMYIVYCQNKPKSEHIVSEYI--DTFFEDLKQRLG---HRLQLTDLLIKPVQRIMKYQLLLKDFLKYSKKA 2089
Cdd:cd00160     80 VFLKLAPFFKIYSEYCSNHPDALELLKKLKkfNKFFQEFLEKAEsecGRLKLESLLLKPVQRLTKYPLLLKELLKHTPDG 159
                          170       180
                   ....*....|....*....|..
gi 1907111721 2090 SLDTSELEKAVEVMCIVPKRCN 2111
Cdd:cd00160    160 HEDREDLKKALEAIKEVASQVN 181
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
1941-2111 1.73e-47

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 168.63  E-value: 1.73e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1941 VLQELVETERDYVRDLGCVVEGYMALMKE--DGVPDDMKgkdkIVFGNIHQIYDWHRDFFLGELEKCLEDPEKLGSLFVK 2018
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKplSESEEEIK----TIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIFLK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2019 HERRLHMYIVYCQNKPKSEHIVSEY------IDTFFEDLKQRLG-HRLQLTDLLIKPVQRIMKYQLLLKDFLKYSKKASL 2091
Cdd:pfam00621   77 FAPGFKVYSTYCSNYPKALKLLKKLlkknpkFRAFLEELEANPEcRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPPDHP 156
                          170       180
                   ....*....|....*....|
gi 1907111721 2092 DTSELEKAVEVMCIVPKRCN 2111
Cdd:pfam00621  157 DYEDLKKALEAIKEVAKQIN 176
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
1941-2112 1.29e-46

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 166.32  E-value: 1.29e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  1941 VLQELVETERDYVRDLGCVVEGYMALMKEDGVPDDMKGKDKIvFGNIHQIYDWHRDFfLGELEKCLED----PEKLGSLF 2016
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKLLSPNELETL-FGNIEEIYEFHRDF-LDELEERIEEwddsVERIGDVF 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  2017 VKHERRLHMYIVYCQNKPKSEHIVSE--YIDTFFEDLKQRLGH----RLQLTDLLIKPVQRIMKYQLLLKDFLKYSKKAS 2090
Cdd:smart00325   79 LKLEEFFKIYSEYCSNHPDALELLKKlkKNPRFQKFLKEIESSpqcrRLTLESLLLKPVQRLTKYPLLLKELLKHTPEDH 158
                           170       180
                    ....*....|....*....|..
gi 1907111721  2091 LDTSELEKAVEVMCIVPKRCND 2112
Cdd:smart00325  159 EDREDLKKALKAIKELANQVNE 180
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
1263-1433 1.75e-44

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 160.16  E-value: 1.75e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1263 FIMAELIQTEKAYVRDLRECMDTYLWEMTSGVEEIPPGIVNkelIIFGNMQEIYEFHNnIFLKELEKY----EQLPEDVG 1338
Cdd:cd00160      3 EVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSPEEVE---LLFGNIEEIYEFHR-IFLKSLEERveewDKSGPRIG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1339 HCFVTWADKFQMYVTYCKNKPDSTQLILEHAG--SYFDEIQQRHGLAN---SISSYLIKPVQRITKYQLLLKELLTCCEE 1413
Cdd:cd00160     79 DVFLKLAPFFKIYSEYCSNHPDALELLKKLKKfnKFFQEFLEKAESECgrlKLESLLLKPVQRLTKYPLLLKELLKHTPD 158
                          170       180
                   ....*....|....*....|...
gi 1907111721 1414 G---KGEIKDGLEVMLSVPKRAN 1433
Cdd:cd00160    159 GhedREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
1264-1434 4.12e-42

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 153.61  E-value: 4.12e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  1264 IMAELIQTEKAYVRDLRECMDTYLWEMTSGVEEIPPgivNKELIIFGNMQEIYEFHNnIFLKELEKY----EQLPEDVGH 1339
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKLLSP---NELETLFGNIEEIYEFHR-DFLDELEERieewDDSVERIGD 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  1340 CFVTWADKFQMYVTYCKNKPDSTQLI--LEHAGSYFDEIQQRHGLAN----SISSYLIKPVQRITKYQLLLKELLTCCEE 1413
Cdd:smart00325   77 VFLKLEEFFKIYSEYCSNHPDALELLkkLKKNPRFQKFLKEIESSPQcrrlTLESLLLKPVQRLTKYPLLLKELLKHTPE 156
                           170       180
                    ....*....|....*....|....
gi 1907111721  1414 G---KGEIKDGLEVMLSVPKRAND 1434
Cdd:smart00325  157 DhedREDLKKALKAIKELANQVNE 180
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
1264-1433 8.12e-41

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 149.76  E-value: 8.12e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1264 IMAELIQTEKAYVRDLRECMDTYLWEMTSGVEEIPpgivnKEL-IIFGNMQEIYEFHNNIFLKELEKYEQLPEDVGHCFV 1342
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESE-----EEIkTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIFL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1343 TWADKFQMYVTYCKNKPDSTQLI------LEHAGSYFDEIQQR---HGLanSISSYLIKPVQRITKYQLLLKELLTCCEE 1413
Cdd:pfam00621   76 KFAPGFKVYSTYCSNYPKALKLLkkllkkNPKFRAFLEELEANpecRGL--DLNSFLIKPVQRIPRYPLLLKELLKHTPP 153
                          170       180
                   ....*....|....*....|...
gi 1907111721 1414 G---KGEIKDGLEVMLSVPKRAN 1433
Cdd:pfam00621  154 DhpdYEDLKKALEAIKEVAKQIN 176
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
2771-3029 1.03e-40

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 159.02  E-value: 1.03e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2771 VAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMK----RDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQ 2846
Cdd:COG0515     12 LRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAAdpeaRERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEG 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2847 GRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTYYIH--QL 2924
Cdd:COG0515     92 ESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPD---GRVKLIDFGIARALGGATLTQtgTV 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2925 LGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQ 3004
Cdd:COG0515    169 VGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDLPPALDAIVLRALA 248
                          250       260
                   ....*....|....*....|....*
gi 1907111721 3005 EDPAKRPSAALALQEQWLQAGNGSG 3029
Cdd:COG0515    249 KDPEERYQSAAELAAALRAVLRSLA 273
Pkinase pfam00069
Protein kinase domain;
2768-3022 2.85e-40

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 149.70  E-value: 2.85e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNK---KLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMA 2844
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKekiKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 DQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVrylhncriahldlkpenilvdqslaKPTIKLADFgdavqlnttyyihql 2924
Cdd:pfam00069   81 EGGSLFDLLSEKGAFSEREAKFIMKQILEGL-------------------------ESGSSLTTF--------------- 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2925 LGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRlDFSFPEDYFQGVSQKAKEFVCFLLQ 3004
Cdd:pfam00069  121 VGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIID-QPYAFPELPSNLSEEAKDLLKKLLK 199
                          250
                   ....*....|....*...
gi 1907111721 3005 EDPAKRPSAALALQEQWL 3022
Cdd:pfam00069  200 KDPSKRLTATQALQHPWF 217
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
2774-3010 1.30e-35

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 139.95  E-value: 1.30e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTH---ELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:PTZ00263    26 LGTGSFGRVRIAKHKGTGEYYAIKCLKKReILKMKQVQHvaqEKSILMELSHPFIVNMMCSFQDENRVYFLLEFVVGGEL 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQLNTTYYihQLLGNPE 2929
Cdd:PTZ00263   106 FTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDN---KGHVKVTDFGFAKKVPDRTF--TLCGTPE 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2930 FAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPedyfQGVSQKAKEFVCFLLQEDPAK 3009
Cdd:PTZ00263   181 YLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFP----NWFDGRARDLVKGLLQTDHTK 256

                   .
gi 1907111721 3010 R 3010
Cdd:PTZ00263   257 R 257
SH3_Kalirin_2 cd11853
Second Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
2527-2585 1.47e-34

Second Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or TRAD, is a large neuronal dual Rho guanine nucleotide exchange factor (RhoGEF) that activates Rac1, RhoA, and RhoG using two RhoGEF domains. Kalirin exists in many isoforms generated by alternative splicing and the use of multiple promoters; the major isoforms are kalirin-7, -9, and -12, which differ at their C-terminal ends. Kalirin-12, the longest isoform, contains an N-terminal Sec14p domain, spectrin-like repeats, two RhoGEF domains, two SH3 domains, as well as Ig, FNIII, and kinase domains at the C-terminal end. Kalirin-7 contains only a single RhoGEF domain and does not contain an SH3 domain. Kalirin, through its many isoforms, interacts with many different proteins and is able to localize to different locations within the cell. It influences neurite initiation, axon growth, dendritic morphogenesis, vesicle trafficking, neuronal maintenance, and neurodegeneration. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212787  Cd Length: 59  Bit Score: 127.17  E-value: 1.47e-34
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907111721 2527 TMLVTHEYTAVKEDEINVYQGEVVQILASNQQNMFLVFRAATDQCPAAEGWIPGFVLGH 2585
Cdd:cd11853      1 TMPVIQDYYALKEDEICVSQGEVVQILAANQQNMFLVYRPATDQSPAAEGWIPGSVLGH 59
SH3_Kalirin_1 cd11852
First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
1627-1686 7.15e-32

First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or TRAD, is a large neuronal dual Rho guanine nucleotide exchange factor (RhoGEF) that activates Rac1, RhoA, and RhoG using two RhoGEF domains. Kalirin exists in many isoforms generated by alternative splicing and the use of multiple promoters; the major isoforms are kalirin-7, -9, and -12, which differ at their C-terminal ends. Kalirin-12, the longest isoform, contains an N-terminal Sec14p domain, spectrin-like repeats, two RhoGEF domains, two SH3 domains, as well as Ig, FNIII, and kinase domains at the C-terminal end. Kalirin-7 contains only a single RhoGEF domain and does not contain an SH3 domain. Kalirin, through its many isoforms, interacts with many different proteins and is able to localize to different locations within the cell. It influences neurite initiation, axon growth, dendritic morphogenesis, vesicle trafficking, neuronal maintenance, and neurodegeneration. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212786  Cd Length: 62  Bit Score: 119.81  E-value: 7.15e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907111721 1627 ELTVVIHDFTACNSNELTIRRGQTVEVLERPHDKPDWCLVRTT--DRSPAAEGLVPCGSLCI 1686
Cdd:cd11852      1 ELTVVIEDFEATSSQELTVSKGQTVEVLERPSSRPDWCLVRTLeqDNSPPQEGLVPSSILCI 62
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
535-751 3.74e-25

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 105.99  E-value: 3.74e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  535 QLCVFQQDVQQVLDWIENHGEAFLSkhTGVGKSLHRARALQKRHEDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIY 614
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  615 QAAHQLEDRIQDFVRRVEQRKILLDMSV---SFHTHVKELWTWLEELQKELLDDVYAESVEAVQDLIKRFgqqqqttlQV 691
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALdlqQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKH--------KE 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  692 TVNVIKEGEDLIQQLRDSAISSNKTPHNSSINHIETVLQQLDEAQSQMEELFQERKIKLE 751
Cdd:cd00176    151 LEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
I-set pfam07679
Immunoglobulin I-set domain;
2657-2748 4.44e-22

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 92.71  E-value: 4.44e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2657 PEFVIPLSEVTCETGETVVFRCRVCGRPKASITWKGPEHnTLNNDDHYSISYSDiGEATLKIIGVSTEDDGIYTCIAVND 2736
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQ-PLRSSDRFKVTYEG-GTYTLTISNVQPDDSGKYTCVATNS 78
                           90
                   ....*....|..
gi 1907111721 2737 MGSASSSASLRV 2748
Cdd:pfam07679   79 AGEAEASAELTV 90
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
37-172 5.81e-22

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 95.06  E-value: 5.81e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721    37 LKEKVAYLSGGR--DKRGGPILTFPARS--NHDRIRQEDLRRLISYLACIPSEE---VCKRGFTVIVDMRGSK-----WD 104
Cdd:smart00516    2 LELLKAYIPGGRgyDKDGRPVLIERAGRfdLKSVTLEELLRYLVYVLEKILQEEkktGGIEGFTVIFDLKGLSmsnpdLS 81
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907111721   105 SIKPLLKILQESFPCCIHIALIIKPDNFWQ---KQRTNFGSSKFEFETNMVSL---EGLTKVVDPSQLTPEFDG 172
Cdd:smart00516   82 VLRKILKILQDHYPERLGKVYIINPPWFFRvlwKIIKPFLDEKTREKIRFVGNdskEELLEYIDKEQLPEELGG 155
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
876-1105 8.89e-19

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 87.50  E-value: 8.89e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  876 QLRHLQAEVKQVLGWIRNGESMLNAGLiTASSLQEAEQLQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDMIRD 955
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  956 CAEKVASHWQQLMLKMEDRLKLVNASVAFYKTSEQVCSVlesleqeykreEDWCGGADKLGPNSETDHVTPMISKHLEQK 1035
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL-----------EQWLEEKEAALASEDLGKDLESVEELLKKH 148
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1036 EAFLKACTlarrNADVFLKYLHRNSVSMPGmvTHIKAPEQQVKNILNELFQRENRVLHYWTMRKRRLDQC 1105
Cdd:cd00176    149 KELEEELE----AHEPRLKSLNELAEELLE--EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
309-534 1.08e-17

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 84.42  E-value: 1.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  309 QLRLFEQDAEKMFDWITHnKGLFLNSyTEIGTSHPHAMELQTQHNHFAMNCMNVYVNINRIMSVANRLVESGHYASQQIK 388
Cdd:cd00176      1 KLQQFLRDADELEAWLSE-KEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  389 QIANQLEQEWKAFAAALDERSTLLDMSSIFHQKAEKyMSNVDSWCKACGEV----DLPSELQDLEDAIHHHQGIYEHITL 464
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAAlaseDLGKDLESVEELLKKHKELEEELEA 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  465 AysevSQDGKSLLDKLQRPLTPGSSDSLTasanyskavhHVLDVIHEVLHHQRQLENIWQHRKVRLHQRL 534
Cdd:cd00176    158 H----EPRLKSLNELAEELLEEGHPDADE----------EIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
755-982 1.79e-16

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 80.95  E-value: 1.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  755 QLRIFERDAidiiSDLESWNDELSQQMNDFDT-EDLTIAEQRLQHHADKALTMNNltfdviHQGQdllqyVNEVQASGvE 833
Cdd:cd00176      1 KLQQFLRDA----DELEAWLSEKEELLSSTDYgDDLESVEALLKKHEALEAELAA------HEER-----VEALNELG-E 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  834 LLCDRDVDMATRVQDLLEFLHEKQQELDLAAEQHRKHLEQCVQLRHLQAEVKQVLGWIRNGESMLNAGLITaSSLQEAEQ 913
Cdd:cd00176     65 QLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLG-KDLESVEE 143
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  914 LQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDM-IRDCAEKVASHWQQLMLKMEDRLKLVNASV 982
Cdd:cd00176    144 LLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEAL 213
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2664-2748 5.23e-16

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 75.23  E-value: 5.23e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  2664 SEVTCETGETVVFRCRVCGRPKASITWKGPEHNTLNNDDHYSISYSDiGEATLKIIGVSTEDDGIYTCIAVNDMGSASSS 2743
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSG-STSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                    ....*
gi 1907111721  2744 ASLRV 2748
Cdd:smart00410   81 TTLTV 85
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
2790-2960 1.01e-15

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 84.51  E-value: 1.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2790 TKRAVATKFVN----KKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVL-VLEMADQGRLLDCVVRWGSLTEGKV 2864
Cdd:TIGR03903    2 TGHEVAIKLLRtdapEEEHQRARFRRETALCARLYHPNIVALLDSGEAPPGLLFaVFEYVPGRTLREVLAADGALPAGET 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2865 RAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFG-----------DAVQLNTTyyiHQLLGNPEFAAP 2933
Cdd:TIGR03903   82 GRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPHAKVLDFGigtllpgvrdaDVATLTRT---TEVLGTPTYCAP 158
                          170       180
                   ....*....|....*....|....*..
gi 1907111721 2934 EIILGNPVSLTADTWSVGVLTYVLLSG 2960
Cdd:TIGR03903  159 EQLRGEPVTPNSDLYAWGLIFLECLTG 185
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
42-172 3.25e-15

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 75.45  E-value: 3.25e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721   42 AYLSGGRDKRGGPILTFPAR-SNHDRIRQEDLRRLISYL--ACIPSEEVCKRGFTVIVDMRGSKW------DSIKPLLKI 112
Cdd:cd00170     11 IGYLGGRDKEGRPVLVFRAGwDPPKLLDLEELLRYLVYLleKALRELEEQVEGFVVIIDLKGFSLsnlsdlSLLKKLLKI 90
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  113 LQESFPCCIHIALIIKPDNF----WQ------KQRTnfgSSKFEFETNmvSLEGLTKVVDPSQLTPEFDG 172
Cdd:cd00170     91 LQDHYPERLKKIYIVNAPWIfsalWKivkpflSEKT---RKKIVFLGS--DLEELLEYIDPDQLPKELGG 155
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
188-413 3.64e-15

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 77.10  E-value: 3.64e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  188 FEEYISNAAHMLSRLEELQDVLAKKELPQDLEGARNMIDEHSQLKK--KVIKAPIEDLDLEGQKLLQriqssdsfpkknS 265
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAelAAHEERVEALNELGEQLIE------------E 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  266 GSGNADlqnllpKVSTMLDRLHSTRQHLHQMWHVRKLKLDQCFQLRLFEQDAEKMFDWIThNKGLFLNSyTEIGTSHPHA 345
Cdd:cd00176     70 GHPDAE------EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLE-EKEAALAS-EDLGKDLESV 141
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907111721  346 MELQTQHNHFAMNCMNVYVNINRIMSVANRLVESGHYASQ-QIKQIANQLEQEWKAFAAALDERSTLLD 413
Cdd:cd00176    142 EELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC smart00150
Spectrin repeats;
1111-1211 9.08e-14

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 69.67  E-value: 9.08e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  1111 FERSAKQALEWIHDNGEfyLSTHTSTGSSIQHTQELLKEHEEFQITAKQTKERVKLLIQLADGFCEKGHAHAAEIKKCVT 1190
Cdd:smart00150    3 FLRDADELEAWLEEKEQ--LLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 1907111721  1191 AVDKRYRDFSLRMEKYRTSLE 1211
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
539-639 1.39e-13

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 68.90  E-value: 1.39e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721   539 FQQDVQQVLDWIENHgEAFLSkHTGVGKSLHRARALQKRHEDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYQAAH 618
Cdd:smart00150    3 FLRDADELEAWLEEK-EQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 1907111721   619 QLEDRIQDFVRRVEQRKILLD 639
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
2662-2748 2.15e-13

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 67.80  E-value: 2.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2662 PLSEVTCETGETVVFRCRVCGRPKASITWkgpehntLNNDDHYSISY--SDIGEATLKIIGVSTEDDGIYTCIAVNDMGS 2739
Cdd:cd20978      7 PEKNVVVKGGQDVTLPCQVTGVPQPKITW-------LHNGKPLQGPMerATVEDGTLTIINVQPEDTGYYGCVATNEIGD 79

                   ....*....
gi 1907111721 2740 ASSSASLRV 2748
Cdd:cd20978     80 IYTETLLHV 88
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1107-1214 5.33e-13

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 70.55  E-value: 5.33e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1107 QYVVFERSAKQALEWIHDNGEFYLSThtSTGSSIQHTQELLKEHEEFQITAKQTKERVKLLIQLADGFCEKGHAHAAEIK 1186
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSST--DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                           90       100
                   ....*....|....*....|....*...
gi 1907111721 1187 KCVTAVDKRYRDFSLRMEKYRTSLEKAL 1214
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEAL 106
SPEC smart00150
Spectrin repeats;
878-976 1.58e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 63.12  E-value: 1.58e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721   878 RHLQAEVKQVLGWIRNGESMLNAgLITASSLQEAEQLQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDMIRDCA 957
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79
                            90
                    ....*....|....*....
gi 1907111721   958 EKVASHWQQLMLKMEDRLK 976
Cdd:smart00150   80 EELNERWEELKELAEERRQ 98
SPEC smart00150
Spectrin repeats;
313-413 1.86e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 62.73  E-value: 1.86e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721   313 FEQDAEKMFDWITHNKGLFlnSYTEIGTSHPHAMELQTQHNHFAMNCMNVYVNINRIMSVANRLVESGHYASQQIKQIAN 392
Cdd:smart00150    3 FLRDADELEAWLEEKEQLL--ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 1907111721   393 QLEQEWKAFAAALDERSTLLD 413
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
2819-2968 3.77e-10

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 65.59  E-value: 3.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2819 LQHPLLVSLLDTFETPTSYVLVLEMADqGRLLDCVVRwgslTEGKVRAH-----LGEVLEAVRYLHNCRIAHLDLKPENI 2893
Cdd:NF033483    64 LSHPNIVSVYDVGEDGGIPYIVMEYVD-GRTLKDYIR----EHGPLSPEeaveiMIQILSALEHAHRNGIVHRDIKPQNI 138
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907111721 2894 LVDQSlakPTIKLADFGDAVQLN--TTYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDS 2968
Cdd:NF033483   139 LITKD---GRVKVTDFGIARALSstTMTQTNSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDS 212
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
52-179 4.60e-10

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 60.03  E-value: 4.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721   52 GGPILTFPARS-NHDRIRQEDLRRLISYLACIPSEEVCKRGFTVIVDMRGSKWDS------IKPLLKILQESFPCCIHIA 124
Cdd:pfam13716    1 GRPVLVFISKLlPSRPASLDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTGVTSENfpslsfLKKAYDLLPRAFKKNLKAV 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  125 LIIKPDNFWQKQ----RTNFGSSKFEFETNMVS-LEGLTKVVDPSQLTPEFDGCLEYNHE 179
Cdd:pfam13716   81 YVVHPSTFLRTFlktlGSLLGSKKLRKKVHYVSsLSELWEGIDREQLPTELPGVLSYDEE 140
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
876-967 7.42e-08

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 52.71  E-value: 7.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  876 QLRHLQAEVKQVLGWIRNGESMLNAGLItASSLQEAEQLQREHEQFQHAIEkTHQSALQ-VQQKAEAMLQANHYDMDMIR 954
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEALLSSEDY-GKDLESVQALLKKHKALEAELA-AHQDRVEaLNELAEKLIDEGHYASEEIQ 79
                           90
                   ....*....|...
gi 1907111721  955 DCAEKVASHWQQL 967
Cdd:pfam00435   80 ERLEELNERWEQL 92
PH pfam00169
PH domain; PH stands for pleckstrin homology.
1473-1558 1.07e-07

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 52.56  E-value: 1.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1473 RERHLFLFEMSLVFSKevkDSSGRSKYLYKSKLFTSELGVTEHVEGD----PCKFALWVGrTPTSDNKIVLKASSIENKQ 1548
Cdd:pfam00169   19 KKRYFVLFDGSLLYYK---DDKSGKSKEPKGSISLSGCEVVEVVASDspkrKFCFELRTG-ERTGKRTYLLQAESEEERK 94
                           90
                   ....*....|
gi 1907111721 1549 DWIKHIREVI 1558
Cdd:pfam00169   95 DWIKAIQSAI 104
SPEC smart00150
Spectrin repeats;
189-305 1.46e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.95  E-value: 1.46e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721   189 EEYISNAAHMLSRLEELQDVLAKKELPQDLEGARNMIDEHSQLKKKV--IKAPIEDLDLEGQKLLQriqssdsfpkknSG 266
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELeaHEERVEALNELGEQLIE------------EG 68
                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 1907111721   267 SGNAdlqnllPKVSTMLDRLHSTRQHLHQMWHVRKLKLD 305
Cdd:smart00150   69 HPDA------EEIEERLEELNERWEELKELAEERRQKLE 101
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
1451-1559 1.58e-07

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 51.78  E-value: 1.58e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  1451 QGELILQEsfqvwdpKTLIRKGRERHLFLFEMSLVFSKevkDSSGRSKYLYKSKLFTSELGVTEHVEGD----PCKFALW 1526
Cdd:smart00233    4 EGWLYKKS-------GGGKKSWKKRYFVLFNSTLLYYK---SKKDKKSYKPKGSIDLSGCTVREAPDPDsskkPHCFEIK 73
                            90       100       110
                    ....*....|....*....|....*....|...
gi 1907111721  1527 VGRTPTsdnkIVLKASSIENKQDWIKHIREVIQ 1559
Cdd:smart00233   74 TSDRKT----LLLQAESEEEREKWVEALRKAIA 102
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
1937-2103 2.18e-07

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 57.21  E-value: 2.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1937 RRHYVLQELVETERDYVRDLGCVVEGYMALMKE-DGVPDDMKGK-DKIVFGNIHQIYDWHRDFfLGELEK--CLED-PEK 2011
Cdd:COG5422    484 KRQEAIYEVIYTERDFVKDLEYLRDTWIKPLEEsNIIPENARRNfIKHVFANINEIYAVNSKL-LKALTNrqCLSPiVNG 562
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2012 LGSLFVKHERRLHMYIVYCQNKP------KSEHIVSEYIDTFFED-LKQRLGHRLQLTDLLIKPVQRIMKYQLLLKDFLK 2084
Cdd:COG5422    563 IADIFLDYVPKFEPFIKYGASQPyakyefEREKSVNPNFARFDHEvERLDESRKLELDGYLTKPTTRLARYPLLLEEVLK 642
                          170
                   ....*....|....*....
gi 1907111721 2085 YSKKASLDTSELEKAVEVM 2103
Cdd:COG5422    643 FTDPDNPDTEDIPKVIDML 661
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
1630-1681 2.56e-07

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 49.46  E-value: 2.56e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1907111721  1630 VVIHDFTACNSNELTIRRGQTVEVLERPHDkpDWCLVRTTDRspaAEGLVPC 1681
Cdd:smart00326    6 RALYDYTAQDPDELSFKKGDIITVLEKSDD--GWWKGRLGRG---KEGLFPS 52
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1111-1211 6.37e-07

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 50.01  E-value: 6.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1111 FERSAKQALEWIHDNGEFYLSThtSTGSSIQHTQELLKEHEEFQITAKQTKERVKLLIQLADGFCEKGHAHAAEIKKCVT 1190
Cdd:pfam00435    6 FFRDADDLESWIEEKEALLSSE--DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83
                           90       100
                   ....*....|....*....|.
gi 1907111721 1191 AVDKRYRDFSLRMEKYRTSLE 1211
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLE 104
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
1248-1425 1.03e-06

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 54.90  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1248 HELNEEKRKSARRKEFIMAELIQTEKAYVRDLRECMDTY---LWEMTsgveeIPPGIVNKELI--IFGNMQEIYEFhNNI 1322
Cdd:COG5422    472 KEVWESLPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWikpLEESN-----IIPENARRNFIkhVFANINEIYAV-NSK 545
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1323 FLKELEK---YEQLPEDVGHCFVTWADKFQMYVTYCKNKPDSTQLIlEHAGS-------YFDEIQ-----QRHGlansIS 1387
Cdd:COG5422    546 LLKALTNrqcLSPIVNGIADIFLDYVPKFEPFIKYGASQPYAKYEF-EREKSvnpnfarFDHEVErldesRKLE----LD 620
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1907111721 1388 SYLIKPVQRITKYQLLLKELLTCCEEGKGEIKDGLEVM 1425
Cdd:COG5422    621 GYLTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVI 658
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
309-412 3.05e-06

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 48.08  E-value: 3.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  309 QLRLFEQDAEKMFDWIThNKGLFLNSyTEIGTSHPHAMELQTQHNHFAMNcMNVY-VNINRIMSVANRLVESGHYASQQI 387
Cdd:pfam00435    2 LLQQFFRDADDLESWIE-EKEALLSS-EDYGKDLESVQALLKKHKALEAE-LAAHqDRVEALNELAEKLIDEGHYASEEI 78
                           90       100
                   ....*....|....*....|....*
gi 1907111721  388 KQIANQLEQEWKAFAAALDERSTLL 412
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKL 103
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
2143-2238 9.08e-06

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 46.77  E-value: 9.08e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  2143 QDAGLLPRCKERRVFLFEQIVIFSEPLDKKKGFSMPGFLFKNSIKVSClCLEENVESDPCKFALTSRTGdavETFVLHSS 2222
Cdd:smart00233   10 KSGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKGSIDLSGCTVRE-APDPDSSKKPHCFEIKTSDR---KTLLLQAE 85
                            90
                    ....*....|....*.
gi 1907111721  2223 SPSVRQTWIHEINQIL 2238
Cdd:smart00233   86 SEEEREKWVEALRKAI 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
539-638 1.03e-05

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 46.54  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  539 FQQDVQQVLDWIENHgEAFLSKhTGVGKSLHRARALQKRHEDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYQAAH 618
Cdd:pfam00435    6 FFRDADDLESWIEEK-EALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83
                           90       100
                   ....*....|....*....|
gi 1907111721  619 QLEDRIQDFVRRVEQRKILL 638
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKL 103
PH pfam00169
PH domain; PH stands for pleckstrin homology.
2143-2239 1.36e-05

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 46.40  E-value: 1.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2143 QDAGLLPRCKERRVFLFEQIVIFSepldkKKGFSMPGFLFKNSIKVSCLCLEENVESD----PCKFALTSRTGDAVETFV 2218
Cdd:pfam00169   10 KGGGKKKSWKKRYFVLFDGSLLYY-----KDDKSGKSKEPKGSISLSGCEVVEVVASDspkrKFCFELRTGERTGKRTYL 84
                           90       100
                   ....*....|....*....|.
gi 1907111721 2219 LHSSSPSVRQTWIHEINQILE 2239
Cdd:pfam00169   85 LQAESEEERKDWIKAIQSAIR 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
188-306 5.83e-04

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 41.54  E-value: 5.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  188 FEEYISNAAHMLSRLEELQDVLAKKELPQDLEGARNMIDEHSQLKK--KVIKAPIEDLDLEGQKLLQRiQSSDSfpkkns 265
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAelAAHQDRVEALNELAEKLIDE-GHYAS------ 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1907111721  266 gsgnadlqnllPKVSTMLDRLHSTRQHLHQMWHVRKLKLDQ 306
Cdd:pfam00435   76 -----------EEIQERLEELNERWEQLLELAAERKQKLEE 105
 
Name Accession Description Interval E-value
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
2760-3022 0e+00

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio 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: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 581.55  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2760 WKDNFDAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVL 2839
Cdd:cd14113      1 WKDNFDSFYSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQVTHELGVLQSLQHPQLVGLLDTFETPTSYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2840 VLEMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAVQLNTTY 2919
Cdd:cd14113     81 VLEMADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSKPTIKLADFGDAVQLNTTY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2920 YIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFV 2999
Cdd:cd14113    161 YIHQLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPDDYFKGVSQKAKDFV 240
                          250       260
                   ....*....|....*....|...
gi 1907111721 3000 CFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14113    241 CFLLQMDPAKRPSAALCLQEQWL 263
SH3-RhoG_link pfam16609
SH3-RhoGEF linking unstructured region; This family of natively unstructured but conserved ...
1683-1940 1.36e-150

SH3-RhoGEF linking unstructured region; This family of natively unstructured but conserved residues from higher eukaryotes is found to lie between an SH3 pfam00018 and the RhoGEF, pfam00621, domains. It is serine-rich and likely to be acidic and natively unstructured.


Pssm-ID: 465196  Cd Length: 261  Bit Score: 468.13  E-value: 1.36e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1683 SLCIAHSRSSMEMEGIFNHKDSLSVSSNDASPPASVASLQP-HMIGAQSSPGPKRPGNTLRKWLTSPVRRLSSGKADGHA 1761
Cdd:pfam16609    1 MLCIAHSRSSMEMEGIFNHKDTLSVYSNDSIMPGSSATLQPgHGISSHASPGPKRPGNTLRKWLTSPVRRLSSGKADGHV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1762 KKLAHKHKKSREVRKS--ADAGSQKDSDDSAATPQDETIEERGRNEGLSSGTLSKSSSSGMQSCGEEEGEEGADAVPLPP 1839
Cdd:pfam16609   81 KKLAHKHKKSREVRKSreITAGSQKDSDDSAATPQDETVEERVRNEGLSSGTLSKSSSSGMQSCGEEEGEEGADSVPLPP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1840 PMAIQQHSLLQPDSQDDKASSRLLVRPTSSETPSAAELVSAIEELVKSKMALEDRPSSLLVDQGDSSSPSFNPSDNSLLS 1919
Cdd:pfam16609  161 PMAIQQHSLLQPDSQDDKTSSRLFVRPSSSETPSAAELVSAIEELVKSKMALEDRPSSLSVDQGDSSSPSFNPSDNSLLS 240
                          250       260
                   ....*....|....*....|.
gi 1907111721 1920 SSSPIDEMEERKCSSLKRRHY 1940
Cdd:pfam16609  241 SSSPISEMDERRSSFLKKRHY 261
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
2774-3021 1.16e-117

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 372.76  E-value: 1.16e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDCV 2853
Cdd:cd14006      1 LGRGRFGVVKRCIEKATGREFAAKFIPKRDKKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELLDRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2854 VRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdQSLAKPTIKLADFGDAVQLNTTYYIHQLLGNPEFAAP 2933
Cdd:cd14006     81 AERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILL-ADRPSPQIKIIDFGLARKLNPGEELKEIFGTPEFVAP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2934 EIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNI--CRLDFSFPedYFQGVSQKAKEFVCFLLQEDPAKRP 3011
Cdd:cd14006    160 EIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANIsaCRVDFSEE--YFSSVSQEAKDFIRKLLVKEPRKRP 237
                          250
                   ....*....|
gi 1907111721 3012 SAALALQEQW 3021
Cdd:cd14006    238 TAQEALQHPW 247
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
2774-3021 1.20e-111

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin 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: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 355.81  E-value: 1.20e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDCV 2853
Cdd:cd14115      1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLLDYL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2854 VRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAVQLNTTYYIHQLLGNPEFAAP 2933
Cdd:cd14115     81 MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHRHVHHLLGNPEFAAP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2934 EIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQEDPAKRPSA 3013
Cdd:cd14115    161 EVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEYFGDVSQAARDFINVILQEDPRRRPTA 240

                   ....*...
gi 1907111721 3014 ALALQEQW 3021
Cdd:cd14115    241 ATCLQHPW 248
PH2_Kalirin_Trio_p63RhoGEF cd13241
p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor ...
2116-2254 1.19e-79

p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor p63RhoGEF is an effector of the heterotrimeric G protein, Galphaq and linking Galphaq-coupled receptors (GPCRs) to the activation of RhoA. The Dbl(DH) and PH domains of p63RhoGEF interact with the effector-binding site and the C-terminal region of Galphaq and appear to relieve autoinhibition of the catalytic DH domain by the PH domain. Trio, Duet, and p63RhoGEF are shown to constitute a family of Galphaq effectors that appear to activate RhoA both in vitro and in intact cells. Dbs is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a rhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Trio is a multidomain signaling protein that contains two RhoGEF(DH)-PH domains in tandem. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270061  Cd Length: 140  Bit Score: 259.50  E-value: 1.19e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2116 VGRLQGFDGKIVAQGKLLLQDTFLVTDQDAGLLPRCKERRVFLFEQIVIFSEPLDKKKGFSMPGFLFKNSIKVSCLCLEE 2195
Cdd:cd13241      1 VGRLQGFDGKITAQGKLLLQGTLLVSEPSAGLLQKGKERRVFLFEQIIIFSEILGKKTQFSNPGYIYKNHIKVNKMSLEE 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2196 NVESDPCKFALTSRTG-DAVETFVLHSSSPSVRQTWIHEINQILENQRNFLNALTSPIEY 2254
Cdd:cd13241     81 NVDGDPLRFALKSRDPnNPSETFILQAASPEVRQEWVDTINQILDTQRDFLKALQSPIAY 140
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
2773-3021 7.13e-76

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 253.55  E-value: 7.13e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTH---ELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd05117      7 VLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMlrrEIEILKRLDHPNIVKLYEVFEDDKNLYLVMELCTGGEL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAVQLNTTYYIHQLLGNPE 2929
Cdd:cd05117     87 FDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIFEEGEKLKTVCGTPY 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2930 FAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQEDPAK 3009
Cdd:cd05117    167 YVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEEAKDLIKRLLVVDPKK 246
                          250
                   ....*....|..
gi 1907111721 3010 RPSAALALQEQW 3021
Cdd:cd05117    247 RLTAAEALNHPW 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
2768-3022 8.65e-75

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 250.14  E-value: 8.65e-75
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMK--RDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMAD 2845
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKkdRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  2846 QGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQLNTTYYIHQLL 2925
Cdd:smart00220   81 GGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDE---DGHVKLADFGLARQLDPGEKLTTFV 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  2926 GNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQE 3005
Cdd:smart00220  158 GTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLLVK 237
                           250
                    ....*....|....*..
gi 1907111721  3006 DPAKRPSAALALQEQWL 3022
Cdd:smart00220  238 DPEKRLTAEEALQHPFF 254
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
2774-3022 1.07e-73

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK 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: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 246.75  E-value: 1.07e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVN-KKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDC 2852
Cdd:cd14103      1 LGRGKFGTVYRCVEKATGKELAAKFIKcRKAKDREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGELFER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2853 VVRWGS-LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENIL-VDQSLAKptIKLADFGDAVQLNTTYYIHQLLGNPEF 2930
Cdd:cd14103     81 VVDDDFeLTERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNQ--IKIIDFGLARKYDPDKKLKVLFGTPEF 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2931 AAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQEDPAKR 3010
Cdd:cd14103    159 VAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWDFDDEAFDDISDEAKDFISKLLVKDPRKR 238
                          250
                   ....*....|..
gi 1907111721 3011 PSAALALQEQWL 3022
Cdd:cd14103    239 MSAAQCLQHPWL 250
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
2762-3022 5.08e-72

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 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: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 243.00  E-value: 5.08e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2762 DNFDAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMK-------RDQVTHELGILQNLQHPLLVSLLDTFETP 2834
Cdd:cd14194      1 ENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKssrrgvsREDIEREVSILKEIQHPNVITLHEVYENK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2835 TSYVLVLEMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENI-LVDQSLAKPTIKLADFGDAV 2913
Cdd:cd14194     81 TDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENImLLDRNVPKPRIKIIDFGLAH 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2914 QLNTTYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQ 2993
Cdd:cd14194    161 KIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTSA 240
                          250       260
                   ....*....|....*....|....*....
gi 1907111721 2994 KAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14194    241 LAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
PH1_Kalirin_Trio_like cd13240
Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; ...
1440-1562 6.08e-72

Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; RhoGEFs, Kalirin and Trio, the mammalian homologs of Drosophila Trio and Caenorhabditis elegans UNC-73 regulate a novel step in secretory granule maturation. Their signaling modulates the extent to which regulated cargo enter and remain in the regulated secretory pathway. This allows for fine tuning of peptides released by a single secretory cell type with impaired signaling leading to pathological states. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Kalirin and Trio are encoded by separate genes in mammals and by a single one in invertebrates. Kalirin and Trio share the same complex multidomain structure and display several splice variants. The longest Kalirin and Trio proteins have a Sec14 domain, a stretch of spectrin repeats, a RhoGEF(DH)/PH cassette (also called GEF1), an SH3 domain, a second RhoGEF(DH)/PH cassette (also called GEF2), a second SH3 domain, Ig/FNIII domains, and a kinase domain. The first RhoGEF(DH)/PH cassette catalyzes exchange on Rac1 and RhoG while the second RhoGEF(DH)/PH cassette is specific for RhoA. Kalirin and Trio are closely related to p63RhoGEF and have PH domains of similar function. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains.


Pssm-ID: 270060  Cd Length: 123  Bit Score: 236.51  E-value: 6.08e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1440 MLEGFDENIESQGELILQESFQVWDPKTLIRKGRERHLFLFEMSLVFSKEVKDSSGRSKYLYKSKLFTSELGVTEHVEGD 1519
Cdd:cd13240      1 LLEGCDEDLDSLGEVILQDSFQVWDPKQLIRKGRERHVFLFELCLVFSKEVKDSNGKSKYIYKSRLMTSEIGVTEHIEGD 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1907111721 1520 PCKFALWVGRTPTSDNKIVLKASSIENKQDWIKHIREVIQERT 1562
Cdd:cd13240     81 PCKFALWTGRVPTSDNKIVLKASSLEVKQTWVKKLREVIQERI 123
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
2762-3022 6.47e-72

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK 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: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 242.78  E-value: 6.47e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2762 DNFDAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMK-------RDQVTHELGILQNLQHPLLVSLLDTFETP 2834
Cdd:cd14105      1 ENVEDFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKasrrgvsREDIEREVSILRQVLHPNIITLHDVFENK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2835 TSYVLVLEMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENI-LVDQSLAKPTIKLADFGDAV 2913
Cdd:cd14105     81 TDVVLILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENImLLDKNVPIPRIKLIDFGLAH 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2914 QLNTTYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQ 2993
Cdd:cd14105    161 KIEDGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFDDEYFSNTSE 240
                          250       260
                   ....*....|....*....|....*....
gi 1907111721 2994 KAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14105    241 LAKDFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
2761-3022 3.71e-70

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: 237.63  E-value: 3.71e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2761 KDNFDAFYS-EVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQ---VTHELGIL-QNLQHPLLVSLLDTFETPT 2835
Cdd:cd14106      2 TENINEVYTvESTPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCrneILHEIAVLeLCKDCPRVVNLHEVYETRS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2836 SYVLVLEMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAVQL 2915
Cdd:cd14106     82 ELILILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPLGDIKLCDFGISRVI 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2916 NTTYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKA 2995
Cdd:cd14106    162 GEGEEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEELFKDVSPLA 241
                          250       260
                   ....*....|....*....|....*..
gi 1907111721 2996 KEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14106    242 IDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
2762-3024 1.79e-69

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 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: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 235.67  E-value: 1.79e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2762 DNFDAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMK-------RDQVTHELGILQNLQHPLLVSLLDTFETP 2834
Cdd:cd14195      1 SMVEDHYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSssrrgvsREEIEREVNILREIQHPNIITLHDIFENK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2835 TSYVLVLEMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENI-LVDQSLAKPTIKLADFGDAV 2913
Cdd:cd14195     81 TDVVLILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENImLLDKNVPNPRIKLIDFGIAH 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2914 QLNTTYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQ 2993
Cdd:cd14195    161 KIEAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSNTSE 240
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1907111721 2994 KAKEFVCFLLQEDPAKRPSAALALQEQWLQA 3024
Cdd:cd14195    241 LAKDFIRRLLVKDPKKRMTIAQSLEHSWIKA 271
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
2763-3022 1.04e-65

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 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: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 224.84  E-value: 1.04e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2763 NFDAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKL-------MKRDQVTHELGILQNLQHPLLVSLLDTFETPT 2835
Cdd:cd14196      2 KVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQsrasrrgVSREEIEREVSILRQVLHPNIITLHDVYENRT 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2836 SYVLVLEMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENI-LVDQSLAKPTIKLADFGDAVQ 2914
Cdd:cd14196     82 DVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIPIPHIKLIDFGLAHE 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2915 LNTTYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQK 2994
Cdd:cd14196    162 IEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSHTSEL 241
                          250       260
                   ....*....|....*....|....*...
gi 1907111721 2995 AKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14196    242 AKDFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
2773-3022 2.28e-61

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs 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 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 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: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 212.49  E-value: 2.28e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRD---QVTHELGILQNLQ-HPLLVSLLDTFETPTSYVLVLEMADQGR 2848
Cdd:cd14197     16 ELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDcrmEIIHEIAVLELAQaNPWVINLHEVYETASEMILVLEYAAGGE 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLD-CVV-RWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAVQLNTTYYIHQLLG 2926
Cdd:cd14197     96 IFNqCVAdREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLGDIKIVDFGLSRILKNSEELREIMG 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2927 NPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQED 3006
Cdd:cd14197    176 TPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEEEFEHLSESAIDFIKTLLIKK 255
                          250
                   ....*....|....*.
gi 1907111721 3007 PAKRPSAALALQEQWL 3022
Cdd:cd14197    256 PENRATAEDCLKHPWL 271
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
2762-3022 1.49e-59

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs 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 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 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: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 207.08  E-value: 1.49e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2762 DNFDAFYS-EVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRD---QVTHELGILQNLQ-HPLLVSLLDTFETPTS 2836
Cdd:cd14198      3 DNFNNFYIlTSKELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDcraEILHEIAVLELAKsNPRVVNLHEVYETTSE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2837 YVLVLEMADQGRLLD-CVVRWGS-LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAVQ 2914
Cdd:cd14198     83 IILILEYAAGGEIFNlCVPDLAEmVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPLGDIKIVDFGMSRK 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2915 LNTTYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQK 2994
Cdd:cd14198    163 IGHACELREIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDYSEETFSSVSQL 242
                          250       260
                   ....*....|....*....|....*...
gi 1907111721 2995 AKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14198    243 ATDFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
2766-3022 1.25e-55

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: 195.49  E-value: 1.25e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2766 AFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMAD 2845
Cdd:cd14107      2 SVYEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSSTRARAFQERDILARLSHRRLTCLLDQFETRKTLILILELCS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2846 QGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdQSLAKPTIKLADFGDAVQLNTTYYIHQLL 2925
Cdd:cd14107     82 SEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILM-VSPTREDIKICDFGFAQEITPSEHQFSKY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2926 GNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQE 3005
Cdd:cd14107    161 GSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWDTPEITHLSEDAKDFIKRVLQP 240
                          250
                   ....*....|....*..
gi 1907111721 3006 DPAKRPSAALALQEQWL 3022
Cdd:cd14107    241 DPEKRPSASECLSHEWF 257
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
2767-3022 3.87e-55

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: 193.95  E-value: 3.87e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2767 FYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKL-MKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMAD 2845
Cdd:cd14114      3 HYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHeSDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFLS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2846 QGRLLDCVVRWG-SLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdQSLAKPTIKLADFGDAVQLNTTYYIHQL 2924
Cdd:cd14114     83 GGELFERIAAEHyKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMC-TTKRSNEVKLIDFGLATHLDPKESVKVT 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2925 LGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQ 3004
Cdd:cd14114    162 TGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDDSAFSGISEEAKDFIRKLLL 241
                          250
                   ....*....|....*...
gi 1907111721 3005 EDPAKRPSAALALQEQWL 3022
Cdd:cd14114    242 ADPNKRMTIHQALEHPWL 259
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
2774-3021 2.26e-54

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 191.58  E-value: 2.26e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTH---ELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLL 2850
Cdd:cd14003      8 LGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKikrEIEIMKLLNHPNIIKLYEVIETENKIYLVMEYASGGELF 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2851 DCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGdavqLNTTYYIHQLL----G 2926
Cdd:cd14003     88 DYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLD---KNGNLKIIDFG----LSNEFRGGSLLktfcG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2927 NPEFAAPEIILGNPV-SLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDyfqgVSQKAKEFVCFLLQE 3005
Cdd:cd14003    161 TPAYAAPEVLLGRKYdGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSH----LSPDARDLIRRMLVV 236
                          250
                   ....*....|....*.
gi 1907111721 3006 DPAKRPSAALALQEQW 3021
Cdd:cd14003    237 DPSKRITIEEILNHPW 252
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
2774-3023 3.53e-54

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: 190.76  E-value: 3.53e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKR----DQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd14007      8 LGKGKFGNVYLAREKKSGFIVALKVISKSQLQKsgleHQLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILEYAPNGEL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQLN----TTyyihqLL 2925
Cdd:cd14007     88 YKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLG---SNGELKLADFGWSVHAPsnrrKT-----FC 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2926 GNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDyfqgVSQKAKEFVCFLLQE 3005
Cdd:cd14007    160 GTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFPSS----VSPEAKDLISKLLQK 235
                          250
                   ....*....|....*...
gi 1907111721 3006 DPAKRPSAALALQEQWLQ 3023
Cdd:cd14007    236 DPSKRLSLEQVLNHPWIK 253
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
2766-3022 6.38e-53

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 187.74  E-value: 6.38e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2766 AFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMAD 2845
Cdd:cd14087      1 AKYDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMELAT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2846 QGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAVQLNTT--YYIHQ 2923
Cdd:cd14087     81 GGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPDSKIMITDFGLASTRKKGpnCLMKT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2924 LLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLL 3003
Cdd:cd14087    161 TCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGEPWPSVSNLAKDFIDRLL 240
                          250
                   ....*....|....*....
gi 1907111721 3004 QEDPAKRPSAALALQEQWL 3022
Cdd:cd14087    241 TVNPGERLSATQALKHPWI 259
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2764-3048 4.02e-52

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 186.57  E-value: 4.02e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2764 FDAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVnKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEM 2843
Cdd:cd14085      1 LEDFFEIESELGRGATSVVYRCRQKGTQKPYAVKKL-KKTVDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAVQLNTTYYIHQ 2923
Cdd:cd14085     80 VTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAPLKIADFGLSKIVDQQVTMKT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2924 LLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLN-ICRLDFSFPEDYFQGVSQKAKEFVCFL 3002
Cdd:cd14085    160 VCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQYMFKrILNCDYDFVSPWWDDVSLNAKDLVKKL 239
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1907111721 3003 LQEDPAKRPSAALALQEQWLQagnGSGKGTGVLDTSR--LTSFIERRK 3048
Cdd:cd14085    240 IVLDPKKRLTTQQALQHPWVT---GKAANFAHMDTAQkkLQEFNARRK 284
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
2774-3022 4.12e-52

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 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: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 185.55  E-value: 4.12e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMK-RDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDC 2852
Cdd:cd14192     12 LGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKeREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGELFDR 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2853 VVRWG-SLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKpTIKLADFGDAVQLNTTYYIHQLLGNPEFA 2931
Cdd:cd14192     92 ITDESyQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNSTGN-QIKIIDFGLARRYKPREKLKVNFGTPEFL 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2932 APEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQEDPAKRP 3011
Cdd:cd14192    171 APEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDAEAFENLSEEAKDFISRLLVKEKSCRM 250
                          250
                   ....*....|.
gi 1907111721 3012 SAALALQEQWL 3022
Cdd:cd14192    251 SATQCLKHEWL 261
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
2768-3021 1.13e-51

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 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: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 184.22  E-value: 1.13e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNK---KLMKR--DQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLE 2842
Cdd:cd14098      2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKrkvAGNDKnlQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 MADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKpTIKLADFGDAVQLNTTYYIH 2922
Cdd:cd14098     82 YVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPV-IVKISDFGLAKVIHTGTFLV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2923 QLLGNPEFAAPEIILGNPVSL------TADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAK 2996
Cdd:cd14098    161 TFCGTMAYLAPEILMSKEQNLqggysnLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYTQPPLVDFNISEEAI 240
                          250       260
                   ....*....|....*....|....*
gi 1907111721 2997 EFVCFLLQEDPAKRPSAALALQEQW 3021
Cdd:cd14098    241 DFILRLLDVDPEKRMTAAQALDHPW 265
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
2767-3022 1.77e-51

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 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: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 183.67  E-value: 1.77e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2767 FYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMK-RDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMAD 2845
Cdd:cd14191      3 FYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKeKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMVS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2846 QGRLLDCVVRWG-SLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENIL-VDQSLAKptIKLADFGDAVQLNTTYYIHQ 2923
Cdd:cd14191     83 GGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTK--IKLIDFGLARRLENAGSLKV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2924 LLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLL 3003
Cdd:cd14191    161 LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLL 240
                          250
                   ....*....|....*....
gi 1907111721 3004 QEDPAKRPSAALALQEQWL 3022
Cdd:cd14191    241 KKDMKARLTCTQCLQHPWL 259
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2774-3021 5.66e-51

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 182.19  E-value: 5.66e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKR--DQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLD 2851
Cdd:cd14083     11 LGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGkeDSLENEIAVLRKIKHPNIVQLLDIYESKSHLYLVMELVTGGELFD 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2852 CVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFG-----DAVQLNTTyyihqlLG 2926
Cdd:cd14083     91 RIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSPDEDSKIMISDFGlskmeDSGVMSTA------CG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2927 NPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQED 3006
Cdd:cd14083    165 TPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFDSPYWDDISDSAKDFIRHLMEKD 244
                          250
                   ....*....|....*
gi 1907111721 3007 PAKRPSAALALQEQW 3021
Cdd:cd14083    245 PNKRYTCEQALEHPW 259
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
2774-3016 7.54e-51

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 181.18  E-value: 7.54e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLM-KRDQVTH---ELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd05123      1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIiKRKEVEHtlnERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQL-NTTYYIHQLLGNP 2928
Cdd:cd05123     81 FSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSD---GHIKLTDFGLAKELsSDGDRTYTFCGTP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2929 EFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEdyfqGVSQKAKEFVCFLLQEDPA 3008
Cdd:cd05123    158 EYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPE----YVSPEAKSLISGLLQKDPT 233

                   ....*...
gi 1907111721 3009 KRPSAALA 3016
Cdd:cd05123    234 KRLGSGGA 241
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
1938-2111 1.01e-50

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 178.26  E-value: 1.01e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1938 RHYVLQELVETERDYVRDLGCVVEGYMALMKEDGVPDDmKGKDKIVFGNIHQIYDWHRDFFLGELEKCLED---PEKLGS 2014
Cdd:cd00160      1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLS-PEEVELLFGNIEEIYEFHRIFLKSLEERVEEWdksGPRIGD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2015 LFVKHERRLHMYIVYCQNKPKSEHIVSEYI--DTFFEDLKQRLG---HRLQLTDLLIKPVQRIMKYQLLLKDFLKYSKKA 2089
Cdd:cd00160     80 VFLKLAPFFKIYSEYCSNHPDALELLKKLKkfNKFFQEFLEKAEsecGRLKLESLLLKPVQRLTKYPLLLKELLKHTPDG 159
                          170       180
                   ....*....|....*....|..
gi 1907111721 2090 SLDTSELEKAVEVMCIVPKRCN 2111
Cdd:cd00160    160 HEDREDLKKALEAIKEVASQVN 181
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
2774-3022 1.06e-50

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 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: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 181.27  E-value: 1.06e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMK-RDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDC 2852
Cdd:cd14190     12 LGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKdKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGGELFER 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2853 VVRWGS-LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKpTIKLADFGDAVQLNTTYYIHQLLGNPEFA 2931
Cdd:cd14190     92 IVDEDYhLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTGH-QVKIIDFGLARRYNPREKLKVNFGTPEFL 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2932 APEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQEDPAKRP 3011
Cdd:cd14190    171 SPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFDEETFEHVSDEAKDFVSNLIIKERSARM 250
                          250
                   ....*....|.
gi 1907111721 3012 SAALALQEQWL 3022
Cdd:cd14190    251 SATQCLKHPWL 261
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
2768-3021 1.09e-50

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL 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: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 180.98  E-value: 1.09e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNK-KLM-KRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMAD 2845
Cdd:cd14095      2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKaKCKgKEHMIENEVAILRRVKHPNIVQLIEEYDTDTELYLVMELVK 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2846 QGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILV-DQSLAKPTIKLADFGDAVQLntTYYIHQL 2924
Cdd:cd14095     82 GGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVvEHEDGSKSLKLADFGLATEV--KEPLFTV 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2925 LGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFL--DDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFL 3002
Cdd:cd14095    160 CGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRspDRDQEELFDLILAGEFEFLSPYWDNISDSAKDLISRM 239
                          250
                   ....*....|....*....
gi 1907111721 3003 LQEDPAKRPSAALALQEQW 3021
Cdd:cd14095    240 LVVDPEKRYSAGQVLDHPW 258
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2765-3025 3.26e-50

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 180.47  E-value: 3.26e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2765 DAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLM--KRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLE 2842
Cdd:cd14169      2 NSVYELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALrgKEAMVENEIAVLRRINHENIVSLEDIYESPTHLYLAME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 MADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAvQLNTTYYIH 2922
Cdd:cd14169     82 LVTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATPFEDSKIMISDFGLS-KIEAQGMLS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2923 QLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFL 3002
Cdd:cd14169    161 TACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEFDSPYWDDISESAKDFIRHL 240
                          250       260
                   ....*....|....*....|...
gi 1907111721 3003 LQEDPAKRPSAALALQEQWLQAG 3025
Cdd:cd14169    241 LERDPEKRFTCEQALQHPWISGD 263
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
2774-3022 5.73e-50

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 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: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 179.34  E-value: 5.73e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMK-RDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDC 2852
Cdd:cd14193     12 LGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKeKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGGELFDR 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2853 VVRWG-SLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKpTIKLADFGDAVQLNTTYYIHQLLGNPEFA 2931
Cdd:cd14193     92 IIDENyNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSREAN-QVKIIDFGLARRYKPREKLRVNFGTPEFL 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2932 APEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQEDPAKRP 3011
Cdd:cd14193    171 APEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEDEEFADISEEAKDFISKLLIKEKSWRM 250
                          250
                   ....*....|.
gi 1907111721 3012 SAALALQEQWL 3022
Cdd:cd14193    251 SASEALKHPWL 261
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2761-3022 2.18e-48

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 174.83  E-value: 2.18e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2761 KDNFDafYSEVaeLGRGRFAVVKKCDQKGTKRAVATKFVNKKLM--KRDQVTHELGILQNLQHPLLVSLLDTFETPTSYV 2838
Cdd:cd14167      2 RDIYD--FREV--LGTGAFSEVVLAEEKRTQKLVAIKCIAKKALegKETSIENEIAVLHKIKHPNIVALDDIYESGGHLY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2839 LVLEMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAVQLNTT 2918
Cdd:cd14167     78 LIMQLVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLDEDSKIMISDFGLSKIEGSG 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2919 YYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEF 2998
Cdd:cd14167    158 SVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSPYWDDISDSAKDF 237
                          250       260
                   ....*....|....*....|....
gi 1907111721 2999 VCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14167    238 IQHLMEKDPEKRFTCEQALQHPWI 261
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
1941-2111 1.73e-47

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 168.63  E-value: 1.73e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1941 VLQELVETERDYVRDLGCVVEGYMALMKE--DGVPDDMKgkdkIVFGNIHQIYDWHRDFFLGELEKCLEDPEKLGSLFVK 2018
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKplSESEEEIK----TIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIFLK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2019 HERRLHMYIVYCQNKPKSEHIVSEY------IDTFFEDLKQRLG-HRLQLTDLLIKPVQRIMKYQLLLKDFLKYSKKASL 2091
Cdd:pfam00621   77 FAPGFKVYSTYCSNYPKALKLLKKLlkknpkFRAFLEELEANPEcRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPPDHP 156
                          170       180
                   ....*....|....*....|
gi 1907111721 2092 DTSELEKAVEVMCIVPKRCN 2111
Cdd:pfam00621  157 DYEDLKKALEAIKEVAKQIN 176
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
2767-3022 2.40e-47

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG 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: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 171.62  E-value: 2.40e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2767 FYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQ 2846
Cdd:cd14108      3 YYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTSARRELALLAELDHKSIVRFHDAFEKRRVVIIVTELCHE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2847 GRLLDcVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILV-DQSLAKptIKLADFGDAVQLNTTYYIHQLL 2925
Cdd:cd14108     83 ELLER-ITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMaDQKTDQ--VRICDFGNAQELTPNEPQYCKY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2926 GNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQE 3005
Cdd:cd14108    160 GTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAFEESMFKDLCREAKGFIIKVLVS 239
                          250
                   ....*....|....*..
gi 1907111721 3006 DPAkRPSAALALQEQWL 3022
Cdd:cd14108    240 DRL-RPDAEETLEHPWF 255
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
2768-3022 2.45e-47

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


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 171.58  E-value: 2.45e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMK----RDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEM 2843
Cdd:cd14099      3 YRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTkpkqREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLEL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQLN------T 2917
Cdd:cd14099     83 CSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENM---NVKIGDFGLAARLEydgerkK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2918 TyyihqLLGNPEFAAPEIILG-NPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDyfQGVSQKAK 2996
Cdd:cd14099    160 T-----LCGTPNYIAPEVLEKkKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSH--LSISDEAK 232
                          250       260
                   ....*....|....*....|....*.
gi 1907111721 2997 EFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14099    233 DLIRSMLQPDPTKRPSLDEILSHPFF 258
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
1941-2112 1.29e-46

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 166.32  E-value: 1.29e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  1941 VLQELVETERDYVRDLGCVVEGYMALMKEDGVPDDMKGKDKIvFGNIHQIYDWHRDFfLGELEKCLED----PEKLGSLF 2016
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKLLSPNELETL-FGNIEEIYEFHRDF-LDELEERIEEwddsVERIGDVF 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  2017 VKHERRLHMYIVYCQNKPKSEHIVSE--YIDTFFEDLKQRLGH----RLQLTDLLIKPVQRIMKYQLLLKDFLKYSKKAS 2090
Cdd:smart00325   79 LKLEEFFKIYSEYCSNHPDALELLKKlkKNPRFQKFLKEIESSpqcrRLTLESLLLKPVQRLTKYPLLLKELLKHTPEDH 158
                           170       180
                    ....*....|....*....|..
gi 1907111721  2091 LDTSELEKAVEVMCIVPKRCND 2112
Cdd:smart00325  159 EDREDLKKALKAIKELANQVNE 180
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
2776-3013 1.02e-45

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


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 167.39  E-value: 1.02e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2776 RGRFAVVKKCDQKGTKRAVATKFVNKKLMKR----DQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMA---DQGR 2848
Cdd:cd05579      3 RGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRknqvDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLpggDLYS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVvrwGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFG----------------DA 2912
Cdd:cd05579     83 LLENV---GALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDAN---GHLKLTDFGlskvglvrrqiklsiqKK 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2913 VQLNTTYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDyfQGVS 2992
Cdd:cd05579    157 SNGAPEKEDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPED--PEVS 234
                          250       260
                   ....*....|....*....|.
gi 1907111721 2993 QKAKEFVCFLLQEDPAKRPSA 3013
Cdd:cd05579    235 DEAKDLISKLLTPDPEKRLGA 255
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
2774-3021 1.97e-45

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 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: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 165.89  E-value: 1.97e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLM--KRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLD 2851
Cdd:cd14185      8 IGDGNFAVVKECRHWNENQEYAMKIIDKSKLkgKEDMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYVRGGDLFD 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2852 CVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKP-TIKLADFGDAVQLntTYYIHQLLGNPEF 2930
Cdd:cd14185     88 AIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPDKStTLKLADFGLAKYV--TGPIFTVCGTPTY 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2931 AAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLD-DSVEETCLNICRL-DFSFPEDYFQGVSQKAKEFVCFLLQEDPA 3008
Cdd:cd14185    166 VAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSpERDQEELFQIIQLgHYEFLPPYWDNISEAAKDLISRLLVVDPE 245
                          250
                   ....*....|...
gi 1907111721 3009 KRPSAALALQEQW 3021
Cdd:cd14185    246 KRYTAKQVLQHPW 258
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
2774-3022 3.17e-45

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 165.43  E-value: 3.17e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKC--DQKGTKRAVATKFVNKKLMKRDQVT----HELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQG 2847
Cdd:cd14080      8 IGEGSYSKVKLAeyTKSGLKEKVACKIIDKKKAPKDFLEkflpRELEILRKLRHPNIIQVYSIFERGSKVFIFMEYAEHG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2848 RLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFG--------DAVQLNTTY 2919
Cdd:cd14080     88 DLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLD---SNNNVKLSDFGfarlcpddDGDVLSKTF 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2920 yihqlLGNPEFAAPEIILGNPVS-LTADTWSVGVLTYVLLSGVSPFlDDSveetclNICRL-------DFSFPEDYfQGV 2991
Cdd:cd14080    165 -----CGSAAYAAPEILQGIPYDpKKYDIWSLGVILYIMLCGSMPF-DDS------NIKKMlkdqqnrKVRFPSSV-KKL 231
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1907111721 2992 SQKAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14080    232 SPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2774-3026 8.09e-45

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 165.17  E-value: 8.09e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQ-VTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDC 2852
Cdd:cd14166     11 LGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSsLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQLVSGGELFDR 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2853 VVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAvQLNTTYYIHQLLGNPEFAA 2932
Cdd:cd14166     91 ILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTPDENSKIMITDFGLS-KMEQNGIMSTACGTPGYVA 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2933 PEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQEDPAKRPS 3012
Cdd:cd14166    170 PEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESPFWDDISESAKDFIRHLLEKNPSKRYT 249
                          250
                   ....*....|....
gi 1907111721 3013 AALALQEQWLqAGN 3026
Cdd:cd14166    250 CEKALSHPWI-IGN 262
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
1263-1433 1.75e-44

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 160.16  E-value: 1.75e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1263 FIMAELIQTEKAYVRDLRECMDTYLWEMTSGVEEIPPGIVNkelIIFGNMQEIYEFHNnIFLKELEKY----EQLPEDVG 1338
Cdd:cd00160      3 EVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSPEEVE---LLFGNIEEIYEFHR-IFLKSLEERveewDKSGPRIG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1339 HCFVTWADKFQMYVTYCKNKPDSTQLILEHAG--SYFDEIQQRHGLAN---SISSYLIKPVQRITKYQLLLKELLTCCEE 1413
Cdd:cd00160     79 DVFLKLAPFFKIYSEYCSNHPDALELLKKLKKfnKFFQEFLEKAESECgrlKLESLLLKPVQRLTKYPLLLKELLKHTPD 158
                          170       180
                   ....*....|....*....|...
gi 1907111721 1414 G---KGEIKDGLEVMLSVPKRAN 1433
Cdd:cd00160    159 GhedREDLKKALEAIKEVASQVN 181
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
2774-3022 7.40e-44

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


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 162.18  E-value: 7.40e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKR---------DQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMA 2844
Cdd:cd14084     14 LGSGACGEVKLAYDKSTCKKVAIKIINKRKFTIgsrreinkpRNIETEIEILKKLSHPCIIKIEDFFDAEDDYYIVLELM 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 DQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAVQLNTTYYIHQL 2924
Cdd:cd14084     94 EGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEECLIKITDFGLSKILGETSLMKTL 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2925 LGNPEFAAPEIIL---GNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLN-ICRLDFSFPEDYFQGVSQKAKEFVC 3000
Cdd:cd14084    174 CGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEEYTQMSLKEqILSGKYTFIPKAWKNVSEEAKDLVK 253
                          250       260
                   ....*....|....*....|..
gi 1907111721 3001 FLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14084    254 KMLVVDPSRRPSIEEALEHPWL 275
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
2774-3010 1.08e-43

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 160.85  E-value: 1.08e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFV-----NKKLmkRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGR 2848
Cdd:cd14009      1 IGRGSFATVWKGRHKQTGEVVAIKEIsrkklNKKL--QENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGD 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAVQLNTTYYIHQLLGNP 2928
Cdd:cd14009     79 LSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDDPVLKIADFGFARSLQPASMAETLCGSP 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2929 EFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQEDPA 3008
Cdd:cd14009    159 LYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAVIPFPIAAQLSPDCKDLLRRLLRRDPA 238

                   ..
gi 1907111721 3009 KR 3010
Cdd:cd14009    239 ER 240
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
2773-3026 1.22e-43

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK 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: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 162.03  E-value: 1.22e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRAVATKFVNKKlmKRDqVTHELGILQNL-QHPLLVSLLDTFETPTSYVLVLEMADQGRLLD 2851
Cdd:cd14091      7 EIGKGSYSVCKRCIHKATGKEYAVKIIDKS--KRD-PSEEIEILLRYgQHPNIITLRDVYDDGNSVYLVTELLRGGELLD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2852 CVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENIL-VDQSLAKPTIKLADFGDAVQLNTTyyiHQLLGNP-- 2928
Cdd:cd14091     84 RILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILyADESGDPESLRICDFGFAKQLRAE---NGLLMTPcy 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2929 --EFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFL---DDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLL 3003
Cdd:cd14091    161 taNFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFAsgpNDTPEVILARIGSGKIDLSGGNWDHVSDSAKDLVRKML 240
                          250       260
                   ....*....|....*....|...
gi 1907111721 3004 QEDPAKRPSAALALQEQWLQAGN 3026
Cdd:cd14091    241 HVDPSQRPTAAQVLQHPWIRNRD 263
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
2773-3013 1.47e-43

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 161.23  E-value: 1.47e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRAVATKFVNKKL----MKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGR 2848
Cdd:cd05581      8 PLGEGSYSTVVLAKEKETGKEYAIKVLDKRHiikeKKVKYVTIEKEVLSRLAHPGIVKLYYTFQDESKLYFVLEYAPNGD 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQLNTTYYIHQLL--- 2925
Cdd:cd05581     88 LLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDE---DMHIKITDFGTAKVLGPDSSPESTKgda 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2926 ---------------GNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEdyfqG 2990
Cdd:cd05581    165 dsqiaynqaraasfvGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEFPE----N 240
                          250       260
                   ....*....|....*....|...
gi 1907111721 2991 VSQKAKEFVCFLLQEDPAKRPSA 3013
Cdd:cd05581    241 FPPDAKDLIQKLLVLDPSKRLGV 263
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2773-3022 3.02e-43

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 161.05  E-value: 3.02e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRAVATKFVN-KKLMKRD--QVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd14086      8 ELGKGAFSVVRRCVQKSTGQEFAAKIINtKKLSARDhqKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGEL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAVQL---NTTYYihQLLG 2926
Cdd:cd14086     88 FEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVqgdQQAWF--GFAG 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2927 NPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNI--CRLDFSFPEdyFQGVSQKAKEFVCFLLQ 3004
Cdd:cd14086    166 TPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIkaGAYDYPSPE--WDTVTPEAKDLINQMLT 243
                          250
                   ....*....|....*...
gi 1907111721 3005 EDPAKRPSAALALQEQWL 3022
Cdd:cd14086    244 VNPAKRITAAEALKHPWI 261
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
2774-3022 4.48e-43

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK 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: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 158.97  E-value: 4.48e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKR----DQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd14079     10 LGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSldmeEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMVMEYVSGGEL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFG------DAVQLNTTyyihq 2923
Cdd:cd14079     90 FDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNM---NVKIADFGlsnimrDGEFLKTS----- 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2924 lLGNPEFAAPEIILGnpvSLTA----DTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDyfqgVSQKAKEFV 2999
Cdd:cd14079    162 -CGSPNYAAPEVISG---KLYAgpevDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSGIYTIPSH----LSPGARDLI 233
                          250       260
                   ....*....|....*....|...
gi 1907111721 3000 CFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14079    234 KRMLVVDPLKRITIPEIRQHPWF 256
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
2774-3022 5.92e-43

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 158.57  E-value: 5.92e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNK-KLMKRDQ---VTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd14081      9 LGKGQTGLVKLAKHCVTGQKVAIKIVNKeKLSKESVlmkVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEYVSGGEL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDA-VQLNTTyYIHQLLGNP 2928
Cdd:cd14081     89 FDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLD---EKNNIKIADFGMAsLQPEGS-LLETSCGSP 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2929 EFAAPEIILGNPV-SLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDyfqgVSQKAKEFVCFLLQEDP 3007
Cdd:cd14081    165 HYACPEVIKGEKYdGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHF----ISPDAQDLLRRMLEVNP 240
                          250
                   ....*....|....*
gi 1907111721 3008 AKRPSAALALQEQWL 3022
Cdd:cd14081    241 EKRITIEEIKKHPWF 255
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
2773-3025 6.14e-43

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin 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: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 159.64  E-value: 6.14e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDC 2852
Cdd:cd14104      7 ELGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQVLVKKEISILNIARHRNILRLHESFESHEELVMIFEFISGVDIFER 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2853 VVRWG-SLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdQSLAKPTIKLADFGDAVQLNTTYYIHQLLGNPEFA 2931
Cdd:cd14104     87 ITTARfELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIY-CTRRGSYIKIIEFGQSRQLKPGDKFRLQYTSAEFY 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2932 APEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQEDPAKRP 3011
Cdd:cd14104    166 APEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDDEAFKNISIEALDFVDRLLVKERKSRM 245
                          250
                   ....*....|....
gi 1907111721 3012 SAALALQEQWLQAG 3025
Cdd:cd14104    246 TAQEALNHPWLKQG 259
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
2768-3017 6.20e-43

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: 158.90  E-value: 6.20e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVT----HELGILQNLQHPLLVSLLDTFETPTSYVLVLEM 2843
Cdd:cd14014      2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRerflREARALARLSHPNIVRVYDVGEDDGRPYIVMEY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFG--DAVQLNTTYYI 2921
Cdd:cd14014     82 VEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLT---EDGRVKLTDFGiaRALGDSGLTQT 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2922 HQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCF 3001
Cdd:cd14014    159 GSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILR 238
                          250
                   ....*....|....*.
gi 1907111721 3002 LLQEDPAKRPSAALAL 3017
Cdd:cd14014    239 ALAKDPEERPQSAAEL 254
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
2764-3022 7.14e-43

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG 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: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 159.06  E-value: 7.14e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2764 FDAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRD--------QVTH-ELGILQNLQ-HPLLVSLLDTFET 2833
Cdd:cd14093      1 FYAKYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIDITGEKSSeneaeelrEATRrEIEILRQVSgHPNIIELHDVFES 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2834 PTSYVLVLEMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAV 2913
Cdd:cd14093     81 PTFIFLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNL---NVKISDFGFAT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2914 QLNTTYYIHQLLGNPEFAAPEII-----LGNP-VSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDY 2987
Cdd:cd14093    158 RLDEGEKLRELCGTPGYLAPEVLkcsmyDNAPgYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYEFGSPE 237
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1907111721 2988 FQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14093    238 WDDISDTAKDLISKLLVVDPKKRLTAEEALEHPFF 272
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
2774-3022 3.11e-42

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 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: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 157.08  E-value: 3.11e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLM--KRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLD 2851
Cdd:cd14183     14 IGDGNFAVVKECVERSTGREYALKIINKSKCrgKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVMELVKGGDLFD 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2852 CVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILV-DQSLAKPTIKLADFGDAVQLNTTYYihQLLGNPEF 2930
Cdd:cd14183     94 AITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyEHQDGSKSLKLGDFGLATVVDGPLY--TVCGTPTY 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2931 AAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCL--NICRLDFSFPEDYFQGVSQKAKEFVCFLLQEDPA 3008
Cdd:cd14183    172 VAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEVLfdQILMGQVDFPSPYWDNVSDSAKELITMMLQVDVD 251
                          250
                   ....*....|....
gi 1907111721 3009 KRPSAALALQEQWL 3022
Cdd:cd14183    252 QRYSALQVLEHPWV 265
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
2774-3022 3.84e-42

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 156.53  E-value: 3.84e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATK---FVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLL 2850
Cdd:cd06606      8 LGKGSFGSVYLALNLDTGELMAVKeveLSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVPGGSLA 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2851 DCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQLNTTYYI---HQLLGN 2927
Cdd:cd06606     88 SLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDG---VVKLADFGCAKRLAEIATGegtKSLRGT 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2928 PEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPF--LDDSVEetclNICRLDFS-----FPEDyfqgVSQKAKEFV- 2999
Cdd:cd06606    165 PYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWseLGNPVA----ALFKIGSSgepppIPEH----LSEEAKDFLr 236
                          250       260
                   ....*....|....*....|....
gi 1907111721 3000 -CFllQEDPAKRPSAALALQEQWL 3022
Cdd:cd06606    237 kCL--QRDPKKRPTADELLQHPFL 258
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
1264-1434 4.12e-42

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 153.61  E-value: 4.12e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  1264 IMAELIQTEKAYVRDLRECMDTYLWEMTSGVEEIPPgivNKELIIFGNMQEIYEFHNnIFLKELEKY----EQLPEDVGH 1339
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKLLSP---NELETLFGNIEEIYEFHR-DFLDELEERieewDDSVERIGD 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  1340 CFVTWADKFQMYVTYCKNKPDSTQLI--LEHAGSYFDEIQQRHGLAN----SISSYLIKPVQRITKYQLLLKELLTCCEE 1413
Cdd:smart00325   77 VFLKLEEFFKIYSEYCSNHPDALELLkkLKKNPRFQKFLKEIESSPQcrrlTLESLLLKPVQRLTKYPLLLKELLKHTPE 156
                           170       180
                    ....*....|....*....|....
gi 1907111721  1414 G---KGEIKDGLEVMLSVPKRAND 1434
Cdd:smart00325  157 DhedREDLKKALKAIKELANQVNE 180
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
2774-3018 1.46e-41

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: 153.20  E-value: 1.46e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMK--RDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLD 2851
Cdd:cd00180      1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKklLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLKD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2852 CVVRW-GSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQL---NTTYYIHQLLGN 2927
Cdd:cd00180     81 LLKENkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLD---SDGTVKLADFGLAKDLdsdDSLLKTTGGTTP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2928 PEFAAPEIILGNPVSLTADTWSVGVLTYVLlsgvspflddsveetclnicrldfsfpedyfqgvsQKAKEFVCFLLQEDP 3007
Cdd:cd00180    158 PYYAPPELLGGRYYGPKVDIWSLGVILYEL-----------------------------------EELKDLIRRMLQYDP 202
                          250
                   ....*....|.
gi 1907111721 3008 AKRPSAALALQ 3018
Cdd:cd00180    203 KKRPSAKELLE 213
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
2774-3021 3.88e-41

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 153.65  E-value: 3.88e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLM--KRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLD 2851
Cdd:cd14184      9 IGDGNFAVVKECVERSTGKEFALKIIDKAKCcgKEHLIENEVSILRRVKHPNIIMLIEEMDTPAELYLVMELVKGGDLFD 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2852 CVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILV-DQSLAKPTIKLADFGDAVQLNTTYYihQLLGNPEF 2930
Cdd:cd14184     89 AITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVcEYPDGTKSLKLGDFGLATVVEGPLY--TVCGTPTY 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2931 AAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFL-DDSVEETCLN-ICRLDFSFPEDYFQGVSQKAKEFVCFLLQEDPA 3008
Cdd:cd14184    167 VAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRsENNLQEDLFDqILLGKLEFPSPYWDNITDSAKELISHMLQVNVE 246
                          250
                   ....*....|...
gi 1907111721 3009 KRPSAALALQEQW 3021
Cdd:cd14184    247 ARYTAEQILSHPW 259
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
2768-3022 4.78e-41

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-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: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 154.52  E-value: 4.78e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRF-AVVKKCDQKGTKRAVATKFVNK--------KLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYV 2838
Cdd:cd14096      3 YRLINKIGEGAFsNVYKAVPLRNTGKPVAIKVVRKadlssdnlKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYYY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2839 LVLEMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVD-----QSLAKPT---------- 2903
Cdd:cd14096     83 IVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEpipfiPSIVKLRkadddetkvd 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2904 ---------------IKLADFGDAVQL--NTTyyiHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLD 2966
Cdd:cd14096    163 egefipgvggggigiVKLADFGLSKQVwdSNT---KTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPFYD 239
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907111721 2967 DSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14096    240 ESIETLTEKISRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
1264-1433 8.12e-41

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 149.76  E-value: 8.12e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1264 IMAELIQTEKAYVRDLRECMDTYLWEMTSGVEEIPpgivnKEL-IIFGNMQEIYEFHNNIFLKELEKYEQLPEDVGHCFV 1342
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESE-----EEIkTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIFL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1343 TWADKFQMYVTYCKNKPDSTQLI------LEHAGSYFDEIQQR---HGLanSISSYLIKPVQRITKYQLLLKELLTCCEE 1413
Cdd:pfam00621   76 KFAPGFKVYSTYCSNYPKALKLLkkllkkNPKFRAFLEELEANpecRGL--DLNSFLIKPVQRIPRYPLLLKELLKHTPP 153
                          170       180
                   ....*....|....*....|...
gi 1907111721 1414 G---KGEIKDGLEVMLSVPKRAN 1433
Cdd:pfam00621  154 DhpdYEDLKKALEAIKEVAKQIN 176
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2760-3022 9.15e-41

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 154.05  E-value: 9.15e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2760 WK---DNFDAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMK--RDQVTHELGILQNLQHPLLVSLLDTFETP 2834
Cdd:cd14168      1 WKkqvEDIKKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKgkESSIENEIAVLRKIKHENIVALEDIYESP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2835 TSYVLVLEMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAVQ 2914
Cdd:cd14168     81 NHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQDEESKIMISDFGLSKM 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2915 LNTTYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQK 2994
Cdd:cd14168    161 EGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSPYWDDISDS 240
                          250       260
                   ....*....|....*....|....*...
gi 1907111721 2995 AKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14168    241 AKDFIRNLMEKDPNKRYTCEQALRHPWI 268
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
2771-3029 1.03e-40

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 159.02  E-value: 1.03e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2771 VAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMK----RDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQ 2846
Cdd:COG0515     12 LRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAAdpeaRERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEG 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2847 GRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTYYIH--QL 2924
Cdd:COG0515     92 ESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPD---GRVKLIDFGIARALGGATLTQtgTV 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2925 LGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQ 3004
Cdd:COG0515    169 VGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDLPPALDAIVLRALA 248
                          250       260
                   ....*....|....*....|....*
gi 1907111721 3005 EDPAKRPSAALALQEQWLQAGNGSG 3029
Cdd:COG0515    249 KDPEERYQSAAELAAALRAVLRSLA 273
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
2771-3010 2.29e-40

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 152.35  E-value: 2.29e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2771 VAELGRGRFAVVKKCDQKGTKRAVATKFVNK-KLMKRDQVTH---ELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQ 2846
Cdd:cd05580      6 LKTLGTGSFGRVRLVKHKDSGKYYALKILKKaKIIKLKQVEHvlnEKRILSEVRHPFIVNLLGSFQDDRNLYMVMEYVPG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2847 GRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQL-NTTYyihQLL 2925
Cdd:cd05580     86 GELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLD---SDGHIKITDFGFAKRVkDRTY---TLC 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2926 GNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPedyfQGVSQKAKEFVCFLLQE 3005
Cdd:cd05580    160 GTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFP----SFFDPDAKDLIKRLLVV 235

                   ....*
gi 1907111721 3006 DPAKR 3010
Cdd:cd05580    236 DLTKR 240
Pkinase pfam00069
Protein kinase domain;
2768-3022 2.85e-40

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 149.70  E-value: 2.85e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNK---KLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMA 2844
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKekiKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 DQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVrylhncriahldlkpenilvdqslaKPTIKLADFgdavqlnttyyihql 2924
Cdd:pfam00069   81 EGGSLFDLLSEKGAFSEREAKFIMKQILEGL-------------------------ESGSSLTTF--------------- 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2925 LGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRlDFSFPEDYFQGVSQKAKEFVCFLLQ 3004
Cdd:pfam00069  121 VGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIID-QPYAFPELPSNLSEEAKDLLKKLLK 199
                          250
                   ....*....|....*...
gi 1907111721 3005 EDPAKRPSAALALQEQWL 3022
Cdd:pfam00069  200 KDPSKRLTATQALQHPWF 217
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
2768-3022 6.07e-40

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG 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: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 150.36  E-value: 6.07e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQG 2847
Cdd:cd14111      5 YTFLDEKARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAEFCSGK 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2848 RLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTyYIHQL--- 2924
Cdd:cd14111     85 ELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNL---NAIKIVDFGSAQSFNPL-SLRQLgrr 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2925 LGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSfPEDYFQGVSQKAKEFVCFLLQ 3004
Cdd:cd14111    161 TGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKFD-AFKLYPNVSQSASLFLKKVLS 239
                          250
                   ....*....|....*...
gi 1907111721 3005 EDPAKRPSAALALQEQWL 3022
Cdd:cd14111    240 SYPWSRPTTKDCFAHAWL 257
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
2769-3026 9.65e-40

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK 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: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 151.30  E-value: 9.65e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2769 SEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLmkrdQVTHELGILQNLQ-HPLLVSLLDTFETPTSYVLVLEMADQG 2847
Cdd:cd14092      9 LREEALGDGSFSVCRKCVHKKTGQEFAVKIVSRRL----DTSREVQLLRLCQgHPNIVKLHEVFQDELHTYLVMELLRGG 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2848 RLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFG------DAVQLNTTYYI 2921
Cdd:cd14092     85 ELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDAEIKIVDFGfarlkpENQPLKTPCFT 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2922 HQllgnpeFAAPEIILgnpVSLTA-------DTWSVGVLTYVLLSGVSPF----LDDSVEETCLNICRLDFSFPEDYFQG 2990
Cdd:cd14092    165 LP------YAAPEVLK---QALSTqgydescDLWSLGVILYTMLSGQVPFqspsRNESAAEIMKRIKSGDFSFDGEEWKN 235
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1907111721 2991 VSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQAGN 3026
Cdd:cd14092    236 VSSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQGSS 271
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
2768-3022 1.09e-39

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK 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: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 149.46  E-value: 1.09e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAE-LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRD--QVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMA 2844
Cdd:cd14078      4 YYELHEtIGSGGFAKVKLATHILTGEKVAIKIMDKKALGDDlpRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVLEYC 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 DQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAV--QLNTTYYIH 2922
Cdd:cd14078     84 PGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQ---NLKLIDFGLCAkpKGGMDHHLE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2923 QLLGNPEFAAPEIILGNP-VSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEdyfqGVSQKAKEFVCF 3001
Cdd:cd14078    161 TCCGSPAYAAPELIQGKPyIGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYEEPE----WLSPSSKLLLDQ 236
                          250       260
                   ....*....|....*....|.
gi 1907111721 3002 LLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14078    237 MLQVDPKKRITVKELLNHPWV 257
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
2764-3022 2.98e-39

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 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: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 150.94  E-value: 2.98e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2764 FDAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKlmKRDQvTHELGILQNL-QHPLLVSLLDTFETPTSYVLVLE 2842
Cdd:cd14176     17 FTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKS--KRDP-TEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTE 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 MADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENIL-VDQSLAKPTIKLADFGDAVQLNTTyyi 2921
Cdd:cd14176     94 LMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNPESIRICDFGFAKQLRAE--- 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2922 HQLLGNP----EFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFL---DDSVEETCLNICRLDFSFPEDYFQGVSQK 2994
Cdd:cd14176    171 NGLLMTPcytaNFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGYWNSVSDT 250
                          250       260
                   ....*....|....*....|....*...
gi 1907111721 2995 AKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14176    251 AKDLVSKMLHVDPHQRLTAALVLRHPWI 278
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
2774-3021 3.85e-39

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD 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: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 147.94  E-value: 3.85e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLM---KRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADqGRLL 2850
Cdd:cd14082     11 LGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFptkQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKLH-GDML 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2851 DCVV--RWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAVQLNTTYYIHQLLGNP 2928
Cdd:cd14082     90 EMILssEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPFPQVKLCDFGFARIIGEKSFRRSVVGTP 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2929 EFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDsvEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQEDPA 3008
Cdd:cd14082    170 AYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED--EDINDQIQNAAFMYPPNPWKEISPDAIDLINNLLQVKMR 247
                          250
                   ....*....|...
gi 1907111721 3009 KRPSAALALQEQW 3021
Cdd:cd14082    248 KRYSVDKSLSHPW 260
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
2768-3022 1.03e-38

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 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: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 146.92  E-value: 1.03e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKK---LMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMA 2844
Cdd:cd14097      3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREkagSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMELC 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 DQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPT----IKLADFGDAVQLN--TT 2918
Cdd:cd14097     83 EDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIIDNNdklnIKVTDFGLSVQKYglGE 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2919 YYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEF 2998
Cdd:cd14097    163 DMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTQSVWQSVSDAAKNV 242
                          250       260
                   ....*....|....*....|....
gi 1907111721 2999 VCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14097    243 LQQLLKVDPAHRMTASELLDNPWI 266
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
2770-3010 1.10e-38

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: 146.24  E-value: 1.10e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2770 EVAEL-GRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVT---HELGILQNLQHPLLVSLLDTFETPTSYVLVLEMAd 2845
Cdd:cd14002      4 HVLELiGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKELRnlrQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEYA- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2846 QGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQLNT-TYYIHQL 2924
Cdd:cd14002     83 QGELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIG---KGGVVKLCDFGFARAMSCnTLVLTSI 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2925 LGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEdyfqGVSQKAKEFVCFLLQ 3004
Cdd:cd14002    160 KGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKWPS----NMSPEFKSFLQGLLN 235

                   ....*.
gi 1907111721 3005 EDPAKR 3010
Cdd:cd14002    236 KDPSKR 241
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
2768-3022 1.26e-38

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: 146.19  E-value: 1.26e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVN-KKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQ 2846
Cdd:cd05122      2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKINlESKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFCSG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2847 GRLLDCV-VRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlAKptIKLADFGDAVQLNTTYYIHQLL 2925
Cdd:cd05122     82 GSLKDLLkNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSD-GE--VKLIDFGLSAQLSDGKTRNTFV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2926 GNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDF-SFPEDYFqgVSQKAKEFVCFLLQ 3004
Cdd:cd05122    159 GTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNGPpGLRNPKK--WSKEFKDFLKKCLQ 236
                          250
                   ....*....|....*...
gi 1907111721 3005 EDPAKRPSAALALQEQWL 3022
Cdd:cd05122    237 KDPEKRPTAEQLLKHPFI 254
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
2774-3010 1.57e-38

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 146.22  E-value: 1.57e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTH---ELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd05572      1 LGVGGFGRVELVQLKSKGRTFALKCVKKRhIVQTRQQEHifsEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTYYIHQLLGNPE 2929
Cdd:cd05572     81 WTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSN---GYVKLVDFGFAKKLGSGRKTWTFCGTPE 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2930 FAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPF--LDDSVEETCLNIcrLDFSFPEDYFQGVSQKAKEFVCFLLQEDP 3007
Cdd:cd05572    158 YVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFggDDEDPMKIYNII--LKGIDKIEFPKYIDKNAKNLIKQLLRRNP 235

                   ...
gi 1907111721 3008 AKR 3010
Cdd:cd05572    236 EER 238
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
2768-3022 2.84e-38

Catalytic kinase domain, second 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: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 145.45  E-value: 2.84e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQG 2847
Cdd:cd14110      5 YAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYKPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGP 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2848 RLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQLNT---------T 2918
Cdd:cd14110     85 ELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITE---KNLLKIVDLGNAQPFNQgkvlmtdkkG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2919 YYIhqllgnpEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYfQGVSQKAKEF 2998
Cdd:cd14110    162 DYV-------ETMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQLSRCY-AGLSGGAVNF 233
                          250       260
                   ....*....|....*....|....
gi 1907111721 2999 VCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14110    234 LKSTLCAKPWGRPTASECLQNPWL 257
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
2774-3022 3.19e-38

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK 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: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 145.25  E-value: 3.19e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNK-KL--MKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLL 2850
Cdd:cd14074     11 LGRGHFAVVKLARHVFTGEKVAVKVIDKtKLddVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLILELGDGGDMY 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2851 DCVVRWGS-LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAkpTIKLADFGDAVQLNTTYYIHQLLGNPE 2929
Cdd:cd14074     91 DYIMKHENgLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQG--LVKLTDFGFSNKFQPGEKLETSCGSLA 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2930 FAAPEIILGNPVSLTA-DTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDyfqgVSQKAKEFVCFLLQEDPA 3008
Cdd:cd14074    169 YSAPEILLGDEYDAPAvDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPAH----VSPECKDLIRRMLIRDPK 244
                          250
                   ....*....|....
gi 1907111721 3009 KRPSAALALQEQWL 3022
Cdd:cd14074    245 KRASLEEIENHPWL 258
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
2790-3022 3.72e-38

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 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: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 144.96  E-value: 3.72e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2790 TKRAVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLL--DCVVRW-GSLTEGKVRA 2866
Cdd:cd14109     24 TERSTGRNFLAQLRYGDPFLMREVDIHNSLDHPNIVQMHDAYDDEKLAVTVIDNLASTIELvrDNLLPGkDYYTERQVAV 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2867 HLGEVLEAVRYLHNCRIAHLDLKPENILvdqsLAKPTIKLADFGDAVQLNTTYYIHQLLGNPEFAAPEIILGNPVSLTAD 2946
Cdd:cd14109    104 FVRQLLLALKHMHDLGIAHLDLRPEDIL----LQDDKLKLADFGQSRRLLRGKLTTLIYGSPEFVSPEIVNSYPVTLATD 179
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907111721 2947 TWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14109    180 MWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSFDSSPLGNISDDARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
2762-3010 4.73e-38

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA 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: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 146.01  E-value: 4.73e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2762 DNFDafysEVAELGRGRFAVVKKCDQKGTKRAVATKFVNK-KLMKRDQVTH---ELGILQNLQHPLLVSLLDTFETPTSY 2837
Cdd:cd14209      1 DDFD----RIKTLGTGSFGRVMLVRHKETGNYYAMKILDKqKVVKLKQVEHtlnEKRILQAINFPFLVKLEYSFKDNSNL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2838 VLVLEMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQLNT 2917
Cdd:cd14209     77 YMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQ---QGYIKVTDFGFAKRVKG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2918 TYYihQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEdYFqgvSQKAKE 2997
Cdd:cd14209    154 RTW--TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPS-HF---SSDLKD 227
                          250
                   ....*....|...
gi 1907111721 2998 FVCFLLQEDPAKR 3010
Cdd:cd14209    228 LLRNLLQVDLTKR 240
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
2774-3021 3.86e-37

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 142.16  E-value: 3.86e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKR----DQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd14663      8 LGEGTFAKVKFARNTKTGESVAIKIIDKEQVARegmvEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVMELVTGGEL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAV---QLNTTYYIHQLLG 2926
Cdd:cd14663     88 FSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLD---EDGNLKISDFGLSAlseQFRQDGLLHTTCG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2927 NPEFAAPEIILGNP-VSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEdYFqgvSQKAKEFVCFLLQE 3005
Cdd:cd14663    165 TPNYVAPEVLARRGyDGAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYPR-WF---SPGAKSLIKRILDP 240
                          250
                   ....*....|....*.
gi 1907111721 3006 DPAKRPSAALALQEQW 3021
Cdd:cd14663    241 NPSTRITVEQIMASPW 256
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
2774-3022 7.31e-37

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 141.28  E-value: 7.31e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVT----HELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd14162      8 LGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDYLQkflpREIEVIKGLKHPNLICFYEAIETTSRVYIIMELAENGDL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDA----------VQLNTTY 2919
Cdd:cd14162     88 LDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLD---KNNNLKITDFGFArgvmktkdgkPKLSETY 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2920 yihqlLGNPEFAAPEIILGNPVSLT-ADTWSVGVLTYVLLSGVSPFlDDSVEETCLNICRLDFSFPEDyfQGVSQKAKEF 2998
Cdd:cd14162    165 -----CGSYAYASPEILRGIPYDPFlSDIWSMGVVLYTMVYGRLPF-DDSNLKVLLKQVQRRVVFPKN--PTVSEECKDL 236
                          250       260
                   ....*....|....*....|....
gi 1907111721 2999 VCFLLQEDPaKRPSAALALQEQWL 3022
Cdd:cd14162    237 ILRMLSPVK-KRITIEEIKRDPWF 259
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
2774-3022 1.03e-36

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 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: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 142.09  E-value: 1.03e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKlmKRDQvTHELGILQNL-QHPLLVSLLDTFETPTSYVLVLEMADQGRLLDC 2852
Cdd:cd14175      9 IGVGSYSVCKRCVHKATNMEYAVKVIDKS--KRDP-SEEIEILLRYgQHPNIITLKDVYDDGKHVYLVTELMRGGELLDK 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2853 VVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENIL-VDQSLAKPTIKLADFGDAVQLNTTyyiHQLLGNP--- 2928
Cdd:cd14175     86 ILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESGNPESLRICDFGFAKQLRAE---NGLLMTPcyt 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2929 -EFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPF---LDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQ 3004
Cdd:cd14175    163 aNFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFangPSDTPEEILTRIGSGKFTLSGGNWNTVSDAAKDLVSKMLH 242
                          250
                   ....*....|....*...
gi 1907111721 3005 EDPAKRPSAALALQEQWL 3022
Cdd:cd14175    243 VDPHQRLTAKQVLQHPWI 260
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
2773-3022 2.52e-36

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-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: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 139.67  E-value: 2.52e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQ---VTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd06627      7 LIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDlksVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYVENGSL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILvdqsLAKP-TIKLADFGDAVQLN-TTYYIHQLLGN 2927
Cdd:cd06627     87 ASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANIL----TTKDgLVKLADFGVATKLNeVEKDENSVVGT 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2928 PEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFS-FPEdyfqGVSQKAKEFV--CFllQ 3004
Cdd:cd06627    163 PYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDLQPMAALFRIVQDDHPpLPE----NISPELRDFLlqCF--Q 236
                          250
                   ....*....|....*...
gi 1907111721 3005 EDPAKRPSAALALQEQWL 3022
Cdd:cd06627    237 KDPTLRPSAKELLKHPWL 254
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
2764-3048 3.59e-36

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK 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: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 140.75  E-value: 3.59e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2764 FDAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKR------DQVTHELGILQNLQHPLLVSLLDTFETPTSY 2837
Cdd:cd14094      1 FEDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSspglstEDLKREASICHMLKHPHIVELLETYSSDGML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2838 VLVLEMADQGRLLDCVVRWGS----LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAV 2913
Cdd:cd14094     81 YMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2914 QL-NTTYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLdDSVEETCLNICRLDFSFPEDYFQGVS 2992
Cdd:cd14094    161 QLgESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFY-GTKERLFEGIIKGKYKMNPRQWSHIS 239
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907111721 2993 QKAKEFVCFLLQEDPAKRPSAALALQEQWLQAGNGSGKGTGVLDT-SRLTSFIERRK 3048
Cdd:cd14094    240 ESAKDLVRRMLMLDPAERITVYEALNHPWIKERDRYAYRIHLPETvEQLRKFNARRK 296
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
2774-2964 3.70e-36

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK 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: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 139.06  E-value: 3.70e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd14073      9 LGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQdmvrIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEYASGGEL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGdavqLNTTYYIHQLL---- 2925
Cdd:cd14073     89 YDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNG---NAKIADFG----LSNLYSKDKLLqtfc 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1907111721 2926 GNPEFAAPEIILGNP-VSLTADTWSVGVLTYVLLSGVSPF 2964
Cdd:cd14073    162 GSPLYASPEIVNGTPyQGPEVDCWSLGVLLYTLVYGTMPF 201
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
2773-3022 7.38e-36

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 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: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 139.76  E-value: 7.38e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRAVATKFVNKKlmKRDQvTHELGILQNL-QHPLLVSLLDTFETPTSYVLVLEMADQGRLLD 2851
Cdd:cd14178     10 DIGIGSYSVCKRCVHKATSTEYAVKIIDKS--KRDP-SEEIEILLRYgQHPNIITLKDVYDDGKFVYLVMELMRGGELLD 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2852 CVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENIL-VDQSLAKPTIKLADFGDAVQLNTTyyiHQLLGNP-- 2928
Cdd:cd14178     87 RILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILyMDESGNPESIRICDFGFAKQLRAE---NGLLMTPcy 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2929 --EFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFL---DDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLL 3003
Cdd:cd14178    164 taNFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFAngpDDTPEEILARIGSGKYALSGGNWDSISDAAKDIVSKML 243
                          250
                   ....*....|....*....
gi 1907111721 3004 QEDPAKRPSAALALQEQWL 3022
Cdd:cd14178    244 HVDPHQRLTAPQVLRHPWI 262
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
2774-3022 7.44e-36

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: 138.84  E-value: 7.44e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKR---------------DQVTHELGILQNLQHPLLVSLLDTFETPTS-- 2836
Cdd:cd14008      1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRLRKrregkndrgkiknalDDVRREIAIMKKLDHPNIVRLYEVIDDPESdk 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2837 -YvLVLEMADQGrlldCVVRWGS------LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADF 2909
Cdd:cd14008     81 lY-LVLEYCEGG----PVMELDSgdrvppLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTAD---GTVKISDF 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2910 GDAVQL-NTTYYIHQLLGNPEFAAPEIILGNPVSLT---ADTWSVGVLTYVLLSGVSPFLDDSVEETCLNI--CRLDFSF 2983
Cdd:cd14008    153 GVSEMFeDGNDTLQKTAGTPAFLAPELCDGDSKTYSgkaADIWALGVTLYCLVFGRLPFNGDNILELYEAIqnQNDEFPI 232
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1907111721 2984 PEDyfqgVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14008    233 PPE----LSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
2766-3022 1.16e-35

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 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: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 137.85  E-value: 1.16e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2766 AFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKlmKRDQVTH-----ELGILQNLQHPLLVSLLDTFETPTSYVLV 2840
Cdd:cd14075      2 GFYRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKT--KLDQKTQrllsrEISSMEKLHHPNIIRLYEVVETLSKLHLV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2841 LEMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdqsLAKPTIKLADFGDAVQLNTTYY 2920
Cdd:cd14075     80 MEYASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFY---ASNNCVKVGDFGFSTHAKRGET 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2921 IHQLLGNPEFAAPEII-----LGNPVsltaDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPeDYfqgVSQKA 2995
Cdd:cd14075    157 LNTFCGSPPYAAPELFkdehyIGIYV----DIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYTIP-SY---VSEPC 228
                          250       260
                   ....*....|....*....|....*..
gi 1907111721 2996 KEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14075    229 QELIRGILQPVPSDRYSIDEIKNSEWL 255
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
2767-3023 1.16e-35

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK 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: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 137.73  E-value: 1.16e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2767 FYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQ 2846
Cdd:cd06614      1 LYKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2847 GRLLDcVVRW--GSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQLNT-TYYIHQ 2923
Cdd:cd06614     81 GSLTD-IITQnpVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSK---DGSVKLADFGFAAQLTKeKSKRNS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2924 LLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEE-----TCLNICRLDFSfpedyfQGVSQKAKEF 2998
Cdd:cd06614    157 VVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRalfliTTKGIPPLKNP------EKWSPEFKDF 230
                          250       260
                   ....*....|....*....|....*
gi 1907111721 2999 VCFLLQEDPAKRPSAALALQEQWLQ 3023
Cdd:cd06614    231 LNKCLVKDPEKRPSAEELLQHPFLK 255
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
2774-3010 1.30e-35

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 139.95  E-value: 1.30e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTH---ELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:PTZ00263    26 LGTGSFGRVRIAKHKGTGEYYAIKCLKKReILKMKQVQHvaqEKSILMELSHPFIVNMMCSFQDENRVYFLLEFVVGGEL 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQLNTTYYihQLLGNPE 2929
Cdd:PTZ00263   106 FTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDN---KGHVKVTDFGFAKKVPDRTF--TLCGTPE 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2930 FAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPedyfQGVSQKAKEFVCFLLQEDPAK 3009
Cdd:PTZ00263   181 YLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFP----NWFDGRARDLVKGLLQTDHTK 256

                   .
gi 1907111721 3010 R 3010
Cdd:PTZ00263   257 R 257
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
2768-3022 2.64e-35

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 136.75  E-value: 2.64e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKK-----LMKRDQ----VTHELGILQNLQ---HPLLVSLLDTFETPT 2835
Cdd:cd14004      2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKErilvdTWVRDRklgtVPLEIHILDTLNkrsHPNIVKLLDFFEDDE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2836 SYVLVLEMADQG-RLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQ 2914
Cdd:cd14004     82 FYYLVMEKHGSGmDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNG---TIKLIDFGSAAY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2915 LNT----TYYihqllGNPEFAAPEIILGNP-VSLTADTWSVGVLTYVLLSGVSPFLDdsVEETCLNICRLDFSfpedyfq 2989
Cdd:cd14004    159 IKSgpfdTFV-----GTIDYAAPEVLRGNPyGGKEQDIWALGVLLYTLVFKENPFYN--IEEILEADLRIPYA------- 224
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1907111721 2990 gVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14004    225 -VSEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
2801-3022 2.78e-35

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 137.08  E-value: 2.78e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2801 KKLMKRD------QVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEA 2874
Cdd:cd14088     32 KKFLKRDgrkvrkAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLELATGREVFDWILDQGYYSERDTSNVIRQVLEA 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2875 VRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAVQLNTtyYIHQLLGNPEFAAPEII----LGNPVsltaDTWSV 2950
Cdd:cd14088    112 VAYLHSLKIVHRNLKLENLVYYNRLKNSKIVISDFHLAKLENG--LIKEPCGTPEYLAPEVVgrqrYGRPV----DCWAI 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2951 GVLTYVLLSGVSPFLDDSVEETCLN--------ICRLDFSFPEDYFQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14088    186 GVIMYILLSGNPPFYDEAEEDDYENhdknlfrkILAGDYEFDSPYWDDISQAAKDLVTRLMEVEQDQRITAEEAISHEWI 265
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
2771-3023 2.95e-35

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; 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 MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. 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: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 136.95  E-value: 2.95e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2771 VAELGRGRFAVVKKCDQKGTKRAVATKF--VNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGR 2848
Cdd:cd06623      6 VKVLGQGSSGVVYKVRHKPTGKIYALKKihVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDGGS 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCR-IAHLDLKPENILVDQslaKPTIKLADFGDAVQLNTTYYIHQ-LLG 2926
Cdd:cd06623     86 LADLLKKVGKIPEPVLAYIARQILKGLDYLHTKRhIIHRDIKPSNLLINS---KGEVKIADFGISKVLENTLDQCNtFVG 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2927 NPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDD---SVEETCLNICRLDFSFPEDyfQGVSQKAKEFVCFLL 3003
Cdd:cd06623    163 TVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPgqpSFFELMQAICDGPPPSLPA--EEFSPEFRDFISACL 240
                          250       260
                   ....*....|....*....|
gi 1907111721 3004 QEDPAKRPSAALALQEQWLQ 3023
Cdd:cd06623    241 QKDPKKRPSAAELLQHPFIK 260
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
2767-3022 3.00e-35

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK 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: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 136.37  E-value: 3.00e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2767 FYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRD---QVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEM 2843
Cdd:cd14071      1 FYDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEEnlkKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQLNTTYYIHQ 2923
Cdd:cd14071     81 ASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANM---NIKIADFGFSNFFKPGELLKT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2924 LLGNPEFAAPEIILGNP-VSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPedYFqgVSQKAKEFVCFL 3002
Cdd:cd14071    158 WCGSPPYAAPEVFEGKEyEGPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIP--FF--MSTDCEHLIRRM 233
                          250       260
                   ....*....|....*....|
gi 1907111721 3003 LQEDPAKRPSAALALQEQWL 3022
Cdd:cd14071    234 LVLDPSKRLTIEQIKKHKWM 253
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
2774-3018 4.14e-35

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 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: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 137.02  E-value: 4.14e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMK---------RDQVTHELGILQNLQ-HPLLVSLLDTFETPTSYVLVLEM 2843
Cdd:cd14181     18 IGRGVSSVVRRCVHRHTGQEFAVKIIEVTAERlspeqleevRSSTLKEIHILRQVSgHPSIITLIDSYESSTFIFLVFDL 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQLNTTYYIHQ 2923
Cdd:cd14181     98 MRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQL---HIKLSDFGFSCHLEPGEKLRE 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2924 LLGNPEFAAPEII----------LGNPVsltaDTWSVGVLTYVLLSGVSPFLDDSVEETCLNIC--RLDFSFPEdyFQGV 2991
Cdd:cd14181    175 LCGTPGYLAPEILkcsmdethpgYGKEV----DLWACGVILFTLLAGSPPFWHRRQMLMLRMIMegRYQFSSPE--WDDR 248
                          250       260
                   ....*....|....*....|....*..
gi 1907111721 2992 SQKAKEFVCFLLQEDPAKRPSAALALQ 3018
Cdd:cd14181    249 SSTVKDLISRLLVVDPEIRLTAEQALQ 275
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
2764-3022 5.29e-35

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 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: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 137.07  E-value: 5.29e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2764 FDAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKlmKRDQvTHELGILQNL-QHPLLVSLLDTFETPTSYVLVLE 2842
Cdd:cd14177      2 FTDVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKS--KRDP-SEEIEILMRYgQHPNIITLKDVYDDGRYVYLVTE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 MADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENIL-VDQSLAKPTIKLADFGDAVQLNTTyyi 2921
Cdd:cd14177     79 LMKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILyMDDSANADSIRICDFGFAKQLRGE--- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2922 HQLLGNP----EFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFL---DDSVEETCLNICRLDFSFPEDYFQGVSQK 2994
Cdd:cd14177    156 NGLLLTPcytaNFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFAngpNDTPEEILLRIGSGKFSLSGGNWDTVSDA 235
                          250       260
                   ....*....|....*....|....*...
gi 1907111721 2995 AKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14177    236 AKDLLSHMLHVDPHQRYTAEQVLKHSWI 263
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
2768-3022 8.79e-35

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


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 135.05  E-value: 8.79e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFV-NKKLMKRdQVTHELGILQNL----QHPLLVSLLDTFETPTS--YVLV 2840
Cdd:cd05118      1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIkNDFRHPK-AALREIKLLKHLndveGHPNIVKLLDVFEHRGGnhLCLV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2841 LEMADQGrLLDcVVRWGS--LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakPTIKLADFGDAVQLNTT 2918
Cdd:cd05118     80 FELMGMN-LYE-LIKDYPrgLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLEL--GQLKLADFGLARSFTSP 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2919 YYIHQlLGNPEFAAPEIILG-NPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLdfsfpedyfQGVSQkAKE 2997
Cdd:cd05118    156 PYTPY-VATRWYRAPEVLLGaKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRL---------LGTPE-ALD 224
                          250       260
                   ....*....|....*....|....*
gi 1907111721 2998 FVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd05118    225 LLSKMLKYDPAKRITASQALAHPYF 249
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
2774-3003 1.13e-34

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-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: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 137.80  E-value: 1.13e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLM-KRDQVTH---ELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd05573      9 IGRGAFGEVWLVRDKDTGQVYAMKILRKSDMlKREQIAHvraERDILADADSPWIVRLHYAFQDEDHLYLVMEYMPGGDL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQLN----TTYYIHQLL 2925
Cdd:cd05573     89 MNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLD---ADGHIKLADFGLCTKMNksgdRESYLNDSV 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2926 --------------------------GNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNI--C 2977
Cdd:cd05573    166 ntlfqdnvlarrrphkqrrvraysavGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVETYSKImnW 245
                          250       260
                   ....*....|....*....|....*.
gi 1907111721 2978 RLDFSFPEDyfQGVSQKAKEFVCFLL 3003
Cdd:cd05573    246 KESLVFPDD--PDVSPEAIDLIRRLL 269
SH3_Kalirin_2 cd11853
Second Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
2527-2585 1.47e-34

Second Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or TRAD, is a large neuronal dual Rho guanine nucleotide exchange factor (RhoGEF) that activates Rac1, RhoA, and RhoG using two RhoGEF domains. Kalirin exists in many isoforms generated by alternative splicing and the use of multiple promoters; the major isoforms are kalirin-7, -9, and -12, which differ at their C-terminal ends. Kalirin-12, the longest isoform, contains an N-terminal Sec14p domain, spectrin-like repeats, two RhoGEF domains, two SH3 domains, as well as Ig, FNIII, and kinase domains at the C-terminal end. Kalirin-7 contains only a single RhoGEF domain and does not contain an SH3 domain. Kalirin, through its many isoforms, interacts with many different proteins and is able to localize to different locations within the cell. It influences neurite initiation, axon growth, dendritic morphogenesis, vesicle trafficking, neuronal maintenance, and neurodegeneration. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212787  Cd Length: 59  Bit Score: 127.17  E-value: 1.47e-34
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907111721 2527 TMLVTHEYTAVKEDEINVYQGEVVQILASNQQNMFLVFRAATDQCPAAEGWIPGFVLGH 2585
Cdd:cd11853      1 TMPVIQDYYALKEDEICVSQGEVVQILAANQQNMFLVYRPATDQSPAAEGWIPGSVLGH 59
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
2768-3022 1.59e-34

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK 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: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 134.57  E-value: 1.59e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMK---RDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMA 2844
Cdd:cd14072      2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNpssLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 DQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQLNTTYYIHQL 2924
Cdd:cd14072     82 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADM---NIKIADFGFSNEFTPGNKLDTF 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2925 LGNPEFAAPEIILGNPVS-LTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPedYFqgVSQKAKEFVCFLL 3003
Cdd:cd14072    159 CGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIP--FY--MSTDCENLLKKFL 234
                          250
                   ....*....|....*....
gi 1907111721 3004 QEDPAKRPSAALALQEQWL 3022
Cdd:cd14072    235 VLNPSKRGTLEQIMKDRWM 253
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
2768-2964 1.99e-34

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 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: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 134.31  E-value: 1.99e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKC-DQKGtkRAVATKFVNKKLMKRDQ-VTH---ELGILQNLQHPLLVSLLDTFETPTSYVLVLE 2842
Cdd:cd14161      5 YEFLETLGKGTYGRVKKArDSSG--RLVAIKSIRKDRIKDEQdLLHirrEIEIMSSLNHPHIISVYEVFENSSKIVIVME 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 MADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQLNTTYYIH 2922
Cdd:cd14161     83 YASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLD---ANGNIKIADFGLSNLYNQDKFLQ 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1907111721 2923 QLLGNPEFAAPEIILGNP-VSLTADTWSVGVLTYVLLSGVSPF 2964
Cdd:cd14161    160 TYCGSPLYASPEIVNGRPyIGPEVDSWSLGVLLYILVHGTMPF 202
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
2768-3021 1.34e-33

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk 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: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 132.92  E-value: 1.34e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAE-LGRGRFAVVKKCDQKGTKRAVATKFVNKKL-MKRDQVTHELGILQNLQ-HPLLVSLLDTFETPTSYVLVLEMA 2844
Cdd:cd14090      3 YKLTGElLGEGAYASVQTCINLYTGKEYAVKIIEKHPgHSRSRVFREVETLHQCQgHPNILQLIEYFEDDERFYLVFEKM 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 DQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADF--GDAVQLNTTY--- 2919
Cdd:cd14090     83 RGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVSPVKICDFdlGSGIKLSSTSmtp 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2920 -YIHQLL---GNPEFAAPEII---LGNPVSL--TADTWSVGVLTYVLLSGVSPFLDDSVEE----------TCLN----- 2975
Cdd:cd14090    163 vTTPELLtpvGSAEYMAPEVVdafVGEALSYdkRCDLWSLGVILYIMLCGYPPFYGRCGEDcgwdrgeacqDCQEllfhs 242
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1907111721 2976 ICRLDFSFPEDYFQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQW 3021
Cdd:cd14090    243 IQEGEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPW 288
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
2774-3026 1.36e-33

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 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: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 133.63  E-value: 1.36e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQvtHELGILQNLQ-HPLLVSLLDTFETPTSYVLVLEMADQGRLLDC 2852
Cdd:cd14179     15 LGEGSFSICRKCLHKKTNQEYAVKIVSKRMEANTQ--REIAALKLCEgHPNIVKLHEVYHDQLHTFLVMELLKGGELLER 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2853 VVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAvQLNTTYyiHQLLGNP---- 2928
Cdd:cd14179     93 IKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDNSEIKIIDFGFA-RLKPPD--NQPLKTPcftl 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2929 EFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPF-------LDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCF 3001
Cdd:cd14179    170 HYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFqchdkslTCTSAEEIMKKIKQGDFSFEGEAWKNVSQEAKDLIQG 249
                          250       260
                   ....*....|....*....|....*
gi 1907111721 3002 LLQEDPAKRPSAALALQEQWLQAGN 3026
Cdd:cd14179    250 LLTVDPNKRIKMSGLRYNEWLQDGS 274
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
2771-3010 1.85e-33

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-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: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 133.13  E-value: 1.85e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2771 VAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLM-KRDQVTH---ELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQ 2846
Cdd:cd05574      6 IKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMiKRNKVKRvltEREILATLDHPFLPTLYASFQTSTHLCFVMDYCPG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2847 G---RLLDcvVRWGS-LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTT---- 2918
Cdd:cd05574     86 GelfRLLQ--KQPGKrLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHES---GHIMLTDFDLSKQSSVTpppv 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2919 ----------YYIHQLL----------------GNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEET 2972
Cdd:cd05574    161 rkslrkgsrrSSVKSIEketfvaepsarsnsfvGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRDET 240
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1907111721 2973 CLNICRLDFSFPEDyfQGVSQKAKEFVCFLLQEDPAKR 3010
Cdd:cd05574    241 FSNILKKELTFPES--PPVSSEAKDLIRKLLVKDPSKR 276
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
2774-3012 2.24e-33

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 130.87  E-value: 2.24e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQK-GTKRAVATKFVNKKLMKR---DQVTHELGILQNLQHPLLVSLLDtFETPTSYV-LVLEMADQGR 2848
Cdd:cd14121      3 LGSGTYATVYKAYRKsGAREVVAVKCVSKSSLNKastENLLTEIELLKKLKHPHIVELKD-FQWDEEHIyLIMEYCSGGD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdQSLAKPTIKLADFGDAVQLNTTYYIHQLLGNP 2928
Cdd:cd14121     82 LSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLL-SSRYNPVLKLADFGFAQHLKPNDEAHSLRGSP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2929 EFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLD----FSFPEdyfqgVSQKAKEFVCFLLQ 3004
Cdd:cd14121    161 LYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKpieiPTRPE-----LSADCRDLLLRLLQ 235

                   ....*...
gi 1907111721 3005 EDPAKRPS 3012
Cdd:cd14121    236 RDPDRRIS 243
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
2765-2971 5.42e-33

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 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: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 130.51  E-value: 5.42e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2765 DAFYSEVAELGRGRFAVV-KKCDQKGTKRAVATKFVNKKLMKRDQVT--HELGILQNLQHPLLVSLLDTFETPTSYVLVL 2841
Cdd:cd14201      5 DFEYSRKDLVGHGAFAVVfKGRHRKKTDWEVAIKSINKKNLSKSQILlgKEIKILKELQHENIVALYDVQEMPNSVFLVM 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2842 EMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPT------IKLADFGDAVQL 2915
Cdd:cd14201     85 EYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRKKSsvsgirIKIADFGFARYL 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907111721 2916 NTTYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEE 2971
Cdd:cd14201    165 QSNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQD 220
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
2774-3022 1.73e-32

Catalytic domain of the Serine/Threonine kinase, Aurora-A 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. 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, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. 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: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 128.54  E-value: 1.73e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHEL----GILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd14116     13 LGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLrrevEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTV 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQLNTTYYiHQLLGNPE 2929
Cdd:cd14116     93 YRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLG---SAGELKIADFGWSVHAPSSRR-TTLCGTLD 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2930 FAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPeDYfqgVSQKAKEFVCFLLQEDPAK 3009
Cdd:cd14116    169 YLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFP-DF---VTEGARDLISRLLKHNPSQ 244
                          250
                   ....*....|...
gi 1907111721 3010 RPSAALALQEQWL 3022
Cdd:cd14116    245 RPMLREVLEHPWI 257
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
2774-3023 1.76e-32

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 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: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 129.26  E-value: 1.76e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVN---KKLMKRDQVTH-------ELGILQNLQ-HPLLVSLLDTFETPTSYVLVLE 2842
Cdd:cd14182     11 LGRGVSSVVRRCIHKPTRQEYAVKIIDitgGGSFSPEEVQElreatlkEIDILRKVSgHPNIIQLKDTYETNTFFFLVFD 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 MADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQLNTTYYIH 2922
Cdd:cd14182     91 LMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDM---NIKLTDFGFSCQLDPGEKLR 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2923 QLLGNPEFAAPEII----------LGNPVsltaDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVS 2992
Cdd:cd14182    168 EVCGTPGYLAPEIIecsmddnhpgYGKEV----DMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFGSPEWDDRS 243
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1907111721 2993 QKAKEFVCFLLQEDPAKRPSAALALQEQWLQ 3023
Cdd:cd14182    244 DTVKDLISRFLVVQPQKRYTAEEALAHPFFQ 274
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
2768-3022 2.27e-32

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 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: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 128.22  E-value: 2.27e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRD---QVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMA 2844
Cdd:cd14069      3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDcpeNIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEYA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 DQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQL---NTTYYI 2921
Cdd:cd14069     83 SGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLD---ENDNLKISDFGLATVFrykGKERLL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2922 HQLLGNPEFAAPEIIL-----GNPVsltaDTWSVGVLTYVLLSGVSPFldDSVEETCLNIC--RLDFSFPEDYFQGVSQK 2994
Cdd:cd14069    160 NKMCGTLPYVAPELLAkkkyrAEPV----DVWSCGIVLFAMLAGELPW--DQPSDSCQEYSdwKENKKTYLTPWKKIDTA 233
                          250       260
                   ....*....|....*....|....*...
gi 1907111721 2995 AKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14069    234 ALSLLRKILTENPNKRITIEDIKKHPWY 261
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
2774-2964 2.54e-32

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 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: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 128.26  E-value: 2.54e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVV-KKCDQKGTKRAVATKFVNKKLMKRDQ--VTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLL 2850
Cdd:cd14120      1 IGHGAFAVVfKGRHRKKPDLPVAIKCITKKNLSKSQnlLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGDLA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2851 DCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQ------SLAKPTIKLADFGDAVQLNTTYYIHQL 2924
Cdd:cd14120     81 DYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHnsgrkpSPNDIRLKIADFGFARFLQDGMMAATL 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1907111721 2925 LGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPF 2964
Cdd:cd14120    161 CGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPF 200
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
2774-3022 3.66e-32

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-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: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 127.80  E-value: 3.66e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVT----HELGILQNLQHPLLVSLLDTFETPTSYV-LVLEMADQGR 2848
Cdd:cd14163      8 IGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEEFIQrflpRELQIVERLDHKNIIHVYEMLESADGKIyLVMELAEDGD 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILvdqsLAKPTIKLADFGDAVQL--NTTYYIHQLLG 2926
Cdd:cd14163     88 VFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENAL----LQGFTLKLTDFGFAKQLpkGGRELSQTFCG 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2927 NPEFAAPEIILGNPV-SLTADTWSVGVLTYVLLSGVSPFLDDSVEETclnICRLD--FSFPEDYfqGVSQKAKEFVCFLL 3003
Cdd:cd14163    164 STAYAAPEVLQGVPHdSRKGDIWSMGVVLYVMLCAQLPFDDTDIPKM---LCQQQkgVSLPGHL--GVSRTCQDLLKRLL 238
                          250
                   ....*....|....*....
gi 1907111721 3004 QEDPAKRPSAALALQEQWL 3022
Cdd:cd14163    239 EPDMVLRPSIEEVSWHPWL 257
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
2768-3018 6.35e-32

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: 126.81  E-value: 6.35e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMK---RDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMA 2844
Cdd:cd08215      2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSekeREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEYA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 DQGRLLDCVVRWGS----LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQLNTTY- 2919
Cdd:cd08215     82 DGGDLAQKIKKQKKkgqpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLT---KDGVVKLGDFGISKVLESTTd 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2920 YIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFS-FPEDYfqgvSQKAKEF 2998
Cdd:cd08215    159 LAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPpIPSQY----SSELRDL 234
                          250       260
                   ....*....|....*....|
gi 1907111721 2999 VCFLLQEDPAKRPSAALALQ 3018
Cdd:cd08215    235 VNSMLQKDPEKRPSANEILS 254
SH3_Kalirin_1 cd11852
First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
1627-1686 7.15e-32

First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or TRAD, is a large neuronal dual Rho guanine nucleotide exchange factor (RhoGEF) that activates Rac1, RhoA, and RhoG using two RhoGEF domains. Kalirin exists in many isoforms generated by alternative splicing and the use of multiple promoters; the major isoforms are kalirin-7, -9, and -12, which differ at their C-terminal ends. Kalirin-12, the longest isoform, contains an N-terminal Sec14p domain, spectrin-like repeats, two RhoGEF domains, two SH3 domains, as well as Ig, FNIII, and kinase domains at the C-terminal end. Kalirin-7 contains only a single RhoGEF domain and does not contain an SH3 domain. Kalirin, through its many isoforms, interacts with many different proteins and is able to localize to different locations within the cell. It influences neurite initiation, axon growth, dendritic morphogenesis, vesicle trafficking, neuronal maintenance, and neurodegeneration. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212786  Cd Length: 62  Bit Score: 119.81  E-value: 7.15e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907111721 1627 ELTVVIHDFTACNSNELTIRRGQTVEVLERPHDKPDWCLVRTT--DRSPAAEGLVPCGSLCI 1686
Cdd:cd11852      1 ELTVVIEDFEATSSQELTVSKGQTVEVLERPSSRPDWCLVRTLeqDNSPPQEGLVPSSILCI 62
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
2774-3022 9.00e-32

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK 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: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 126.86  E-value: 9.00e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRD-----QVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGR 2848
Cdd:cd14070     10 LGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDsyvtkNLRREGRIQQMIRHPNITQLLDILETENSYYLVMELCPGGN 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQLNTTYYIHQLL--- 2925
Cdd:cd14070     90 LMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDEND---NIKLIDFGLSNCAGILGYSDPFStqc 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2926 GNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFS---FPEDyfqgVSQKAKEFVCFL 3002
Cdd:cd14070    167 GSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEPFSLRALHQKMVDKEmnpLPTD----LSPGAISFLRSL 242
                          250       260
                   ....*....|....*....|
gi 1907111721 3003 LQEDPAKRPSAALALQEQWL 3022
Cdd:cd14070    243 LEPDPLKRPNIKQALANRWL 262
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
2774-3017 1.84e-31

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: 125.74  E-value: 1.84e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKR----DQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQG-- 2847
Cdd:cd14186      9 LGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKagmvQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLEMCHNGem 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2848 -RLLDCVVRwgSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQLNTTYYIH-QLL 2925
Cdd:cd14186     89 sRYLKNRKK--PFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNM---NIKIADFGLATQLKMPHEKHfTMC 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2926 GNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDyfqgVSQKAKEFVCFLLQE 3005
Cdd:cd14186    164 GTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPAF----LSREAQDLIHQLLRK 239
                          250
                   ....*....|..
gi 1907111721 3006 DPAKRPSAALAL 3017
Cdd:cd14186    240 NPADRLSLSSVL 251
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
2774-2971 2.08e-31

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 125.89  E-value: 2.08e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKR-AVATKFVNKKLMKRDQ--VTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLL 2850
Cdd:cd14202     10 IGHGAFAVVFKGRHKEKHDlEVAVKCINKKNLAKSQtlLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNGGDLA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2851 DCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPT------IKLADFGDAVQLNTTYYIHQL 2924
Cdd:cd14202     90 DYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGGRKSnpnnirIKIADFGFARYLQNNMMAATL 169
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1907111721 2925 LGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEE 2971
Cdd:cd14202    170 CGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQD 216
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
2774-3010 3.02e-31

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 126.92  E-value: 3.02e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTHELG---ILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd05585      2 IGKGSFGKVMQVRKKDTSRIYALKTIRKAhIVSRSEVTHTLAertVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGEL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGdAVQLN--TTYYIHQLLGN 2927
Cdd:cd05585     82 FHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYT---GHIALCDFG-LCKLNmkDDDKTNTFCGT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2928 PEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEdyfqGVSQKAKEFVCFLLQEDP 3007
Cdd:cd05585    158 PEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPD----GFDRDAKDLLIGLLNRDP 233

                   ...
gi 1907111721 3008 AKR 3010
Cdd:cd05585    234 TKR 236
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
2774-3022 4.73e-31

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 124.51  E-value: 4.73e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVT----HELGILQNLQHPLLVSLLDTFETPTSYV-LVLEMADQGR 2848
Cdd:cd14165      9 LGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDFVEkflpRELEILARLNHKSIIKTYEIFETSDGKVyIVMELGVQGD 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQLNTTYYIHQLL--- 2925
Cdd:cd14165     89 LLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDF---NIKLTDFGFSKRCLRDENGRIVLskt 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2926 --GNPEFAAPEIILGNPVS-LTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDyfQGVSQKAKEFVCFL 3002
Cdd:cd14165    166 fcGSAAYAAPEVLQGIPYDpRIYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRS--KNLTSECKDLIYRL 243
                          250       260
                   ....*....|....*....|
gi 1907111721 3003 LQEDPAKRPSAALALQEQWL 3022
Cdd:cd14165    244 LQPDVSQRLCIDEVLSHPWL 263
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
2774-3010 7.25e-31

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB 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 PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 125.93  E-value: 7.25e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTHELG---ILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd05571      3 LGKGTFGKVILCREKATGELYAIKILKKEvIIAKDEVAHTLTenrVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGGEL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFG----DAVQLNTTyyiHQLL 2925
Cdd:cd05571     83 FFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDK---DGHIKITDFGlckeEISYGATT---KTFC 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2926 GNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPedyfQGVSQKAKEFVCFLLQE 3005
Cdd:cd05571    157 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFP----STLSPEAKSLLAGLLKK 232

                   ....*
gi 1907111721 3006 DPAKR 3010
Cdd:cd05571    233 DPKKR 237
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
2768-3022 9.50e-31

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-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: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 124.52  E-value: 9.50e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKfvnkkLMKRDQ------VT--HELGILQNLQHPLLVSLLDTFETPTSYVL 2839
Cdd:cd07829      1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALK-----KIRLDNeeegipSTalREISLLKELKHPNIVKLLDVIHTENKLYL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2840 VLEMADQ--GRLLDcvVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDA--VQL 2915
Cdd:cd07829     76 VFEYCDQdlKKYLD--KRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLIN---RDGVLKLADFGLAraFGI 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2916 NTTYYIHQLLgNPEFAAPEIILGNPV-SLTADTWSVGVLTYVLLSGVSPFLDDSV---------------EETCLNICRL 2979
Cdd:cd07829    151 PLRTYTHEVV-TLWYRAPEILLGSKHySTAVDIWSVGCIFAELITGKPLFPGDSEidqlfkifqilgtptEESWPGVTKL 229
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907111721 2980 ---DFSFP-------EDYFQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd07829    230 pdyKPTFPkwpkndlEKVLPRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
2773-3010 1.22e-30

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: 123.56  E-value: 1.22e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRAVATKFVNKKlmKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDC 2852
Cdd:cd14010      7 EIGRGKHSVVYKGRRKGTIEFVAIKCVDKS--KRPEVLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYCTGGDLETL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2853 VVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFG-----------------DAVQL 2915
Cdd:cd14010     85 LRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGN---GTLKLSDFGlarregeilkelfgqfsDEGNV 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2916 NTTYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPedyFQGVSQKA 2995
Cdd:cd14010    162 NKVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPP---PPKVSSKP 238
                          250
                   ....*....|....*....
gi 1907111721 2996 ----KEFVCFLLQEDPAKR 3010
Cdd:cd14010    239 spdfKSLLKGLLEKDPAKR 257
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
2775-3010 2.04e-30

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 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: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 122.75  E-value: 2.04e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2775 GRGRFAVVKKCDQKGTKRAVATKFVNK-KLMKRDQVTH---ELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLL 2850
Cdd:cd05578      9 GKGSFGKVCIVQKKDTKKMFAMKYMNKqKCIEKDSVRNvlnELEILQELEHPFLVNLWYSFQDEEDMYMVVDLLLGGDLR 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2851 DCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQLNTTYYIHQLLGNPEF 2930
Cdd:cd05578     89 YHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDE---QGHVHITDFNIATKLTDGTLATSTSGTKPY 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2931 AAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLnICRLDFSFPEDYFQGVSQKAKEFVCFLLQEDPAKR 3010
Cdd:cd05578    166 MAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRTSIEE-IRAKFETASVLYPAGWSEEAIDLINKLLERDPQKR 244
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
2774-3010 2.22e-30

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK 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: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 124.35  E-value: 2.22e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTHELG----ILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGR 2848
Cdd:cd05575      3 IGKGSFGKVLLARHKAEGKLYAVKVLQKKaILKRNEVKHIMAernvLLKNVKHPFLVGLHYSFQTKDKLYFVLDYVNGGE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFG----DAVQLNTTyyiHQL 2924
Cdd:cd05575     83 LFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLD---SQGHVVLTDFGlckeGIEPSDTT---STF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2925 LGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEdyfqGVSQKAKEFVCFLLQ 3004
Cdd:cd05575    157 CGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRT----NVSPSARDLLEGLLQ 232

                   ....*.
gi 1907111721 3005 EDPAKR 3010
Cdd:cd05575    233 KDRTKR 238
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
2768-3021 2.27e-30

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 122.40  E-value: 2.27e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQG 2847
Cdd:cd14665      2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKIDENVQREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYAAGG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2848 RLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAkPTIKLADFGDAVQLNTTYYIHQLLGN 2927
Cdd:cd14665     82 ELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPA-PRLKICDFGYSKSSVLHSQPKSTVGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2928 PEFAAPEIILGNPVS-LTADTWSVGVLTYVLLSGVSPFLD----DSVEETCLNICRLDFSFPEDYFqgVSQKAKEFVCFL 3002
Cdd:cd14665    161 PAYIAPEVLLKKEYDgKIADVWSCGVTLYVMLVGAYPFEDpeepRNFRKTIQRILSVQYSIPDYVH--ISPECRHLISRI 238
                          250
                   ....*....|....*....
gi 1907111721 3003 LQEDPAKRPSAALALQEQW 3021
Cdd:cd14665    239 FVADPATRITIPEIRNHEW 257
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
2774-3025 3.74e-30

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: 121.96  E-value: 3.74e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLM----KRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd14187     15 LGKGGFAKCYEITDADTKEVFAGKIVPKSLLlkphQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRRSL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQLNTTYYIHQLL-GNP 2928
Cdd:cd14187     95 LELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDM---EVKIGDFGLATKVEYDGERKKTLcGTP 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2929 EFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDyfqgVSQKAKEFVCFLLQEDPA 3008
Cdd:cd14187    172 NYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKH----INPVAASLIQKMLQTDPT 247
                          250
                   ....*....|....*..
gi 1907111721 3009 KRPSAALALQEQWLQAG 3025
Cdd:cd14187    248 ARPTINELLNDEFFTSG 264
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
2768-3022 3.78e-30

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 122.17  E-value: 3.78e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVN---------------KKLMKRDQ-VTHELGILQNLQHPLLVSLLDTF 2831
Cdd:cd14077      3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPrasnaglkkerekrlEKEISRDIrTIREAALSSLLNHPHICRLRDFL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2832 ETPTSYVLVLEMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGD 2911
Cdd:cd14077     83 RTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKS---GNIKIIDFGL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2912 AVQLNTTYYIHQLLGNPEFAAPEIILGNP-VSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPedyfQG 2990
Cdd:cd14077    160 SNLYDPRRLLRTFCGSLYFAAPELLQAQPyTGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYP----SY 235
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1907111721 2991 VSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14077    236 LSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
2774-3020 6.66e-30

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC 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: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 123.09  E-value: 6.66e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKL-MKRDQV----THELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGR 2848
Cdd:cd05570      3 LGKGSFGKVMLAERKKTDELYAIKVLKKEViIEDDDVectmTEKRVLALANRHPFLTGLHACFQTEDRLYFVMEYVNGGD 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFG----DAVQLNTTyyiHQL 2924
Cdd:cd05570     83 LMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLD---AEGHIKIADFGmckeGIWGGNTT---STF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2925 LGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPedyfQGVSQKAKEFVCFLLQ 3004
Cdd:cd05570    157 CGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYP----RWLSREAVSILKGLLT 232
                          250       260
                   ....*....|....*....|
gi 1907111721 3005 EDPAKR----PSAALALQEQ 3020
Cdd:cd05570    233 KDPARRlgcgPKGEADIKAH 252
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
2774-3010 8.08e-30

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK 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: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 121.48  E-value: 8.08e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd05577      1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKgetmALNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGS--LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTYYIHQLLGN 2927
Cdd:cd05577     81 KYHIYNVGTrgFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDH---GHVRISDLGLAVEFKGGKKIKGRVGT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2928 PEFAAPEIILGN-PVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQED 3006
Cdd:cd05577    158 HGYMAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEELKRRTLEMAVEYPDSFSPEARSLCEGLLQKD 237

                   ....
gi 1907111721 3007 PAKR 3010
Cdd:cd05577    238 PERR 241
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
2776-3018 1.38e-29

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 120.97  E-value: 1.38e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2776 RGRFAVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTH---ELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGrllD 2851
Cdd:cd05609     10 NGAYGAVYLVRHRETRQRFAMKKINKQnLILRNQIQQvfvERDILTFAENPFVVSMYCSFETKRHLCMVMEYVEGG---D 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2852 C---VVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdQSLAKptIKLADFGDA----VQLNTTYYIH-- 2922
Cdd:cd05609     87 CatlLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLI-TSMGH--IKLTDFGLSkiglMSLTTNLYEGhi 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2923 ----------QLLGNPEFAAPEIIL----GNPVsltaDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYf 2988
Cdd:cd05609    164 ekdtrefldkQVCGTPEYIAPEVILrqgyGKPV----DWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEGD- 238
                          250       260       270
                   ....*....|....*....|....*....|
gi 1907111721 2989 QGVSQKAKEFVCFLLQEDPAKRPSAALALQ 3018
Cdd:cd05609    239 DALPDDAQDLITRLLQQNPLERLGTGGAEE 268
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
2773-3010 1.46e-29

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: 120.28  E-value: 1.46e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRAVATKFVNKKLM-KRDQVTH---ELGILQNLQH-PLLVSLLDTFETPTSYVLVLEMADQG 2847
Cdd:cd05611      3 PISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMiAKNQVTNvkaERAIMMIQGEsPYVAKLYYSFQSKDYLYLVMEYLNGG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2848 RLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGdavqLNTTYYIHQ---- 2923
Cdd:cd05611     83 DCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQT---GHLKLTDFG----LSRNGLEKRhnkk 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2924 LLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLL 3003
Cdd:cd05611    156 FVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPEEVKEFCSPEAVDLINRLL 235

                   ....*..
gi 1907111721 3004 QEDPAKR 3010
Cdd:cd05611    236 CMDPAKR 242
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
2774-3010 1.53e-29

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta 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: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 122.04  E-value: 1.53e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTH---ELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd05595      3 LGKGTFGKVILVREKATGRYYAMKILRKEvIIAKDEVAHtvtESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGEL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFG---DAVQLNTTyyIHQLLG 2926
Cdd:cd05595     83 FFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKD---GHIKITDFGlckEGITDGAT--MKTFCG 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2927 NPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPedyfQGVSQKAKEFVCFLLQED 3006
Cdd:cd05595    158 TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFP----RTLSPEAKSLLAGLLKKD 233

                   ....
gi 1907111721 3007 PAKR 3010
Cdd:cd05595    234 PKQR 237
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
2774-3013 2.44e-29

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 119.29  E-value: 2.44e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNkklMKRD--QVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLD 2851
Cdd:cd06612     11 LGEGSYGSVYKAIHKETGQVVAIKVVP---VEEDlqEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYCGAGSVSD 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2852 CV-VRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQLNTTY-YIHQLLGNPE 2929
Cdd:cd06612     88 IMkITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNE---EGQAKLADFGVSGQLTDTMaKRNTVIGTPF 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2930 FAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDdsveetcLNICRLDFSFPEDYFQGVS---QKAKEFVCFL---L 3003
Cdd:cd06612    165 WMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSD-------IHPMRAIFMIPNKPPPTLSdpeKWSPEFNDFVkkcL 237
                          250
                   ....*....|
gi 1907111721 3004 QEDPAKRPSA 3013
Cdd:cd06612    238 VKDPEERPSA 247
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
2774-3022 4.62e-29

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk 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: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 119.75  E-value: 4.62e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKL-MKRDQVTHELGILQNLQ-HPLLVSLLDTFETPTSYVLVLEMADQGRLLD 2851
Cdd:cd14173     10 LGEGAYARVQTCINLITNKEYAVKIIEKRPgHSRSRVFREVEMLYQCQgHRNVLELIEFFEEEDKFYLVFEKMRGGSILS 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2852 CVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADF--GDAVQLN------TTYYIHQ 2923
Cdd:cd14173     90 HIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVSPVKICDFdlGSGIKLNsdcspiSTPELLT 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2924 LLGNPEFAAPEII--LGNPVSL---TADTWSVGVLTYVLLSGVSPFLD--------DSVE--ETCLN-----ICRLDFSF 2983
Cdd:cd14173    170 PCGSAEYMAPEVVeaFNEEASIydkRCDLWSLGVILYIMLSGYPPFVGrcgsdcgwDRGEacPACQNmlfesIQEGKYEF 249
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1907111721 2984 PEDYFQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14173    250 PEKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
2773-3018 5.17e-29

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 118.53  E-value: 5.17e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRAVATKFVNKKLM----KRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQG- 2847
Cdd:cd08224      7 KIGKGQFSVVYRARCLLDGRLVALKKVQIFEMmdakARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIVLELADAGd 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2848 --RLLDCVVRWGSL-TEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQLNT-TYYIHQ 2923
Cdd:cd08224     87 lsRLIKHFKKQKRLiPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFIT---ANGVVKLGDLGLGRFFSSkTTAAHS 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2924 LLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDD--SVEETCLNICRLDFS-FPEDYFqgvSQKAKEFVC 3000
Cdd:cd08224    164 LVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEkmNLYSLCKKIEKCEYPpLPADLY---SQELRDLVA 240
                          250
                   ....*....|....*...
gi 1907111721 3001 FLLQEDPAKRPSAALALQ 3018
Cdd:cd08224    241 ACIQPDPEKRPDISYVLD 258
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
2774-3025 6.56e-29

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 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: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 119.98  E-value: 6.56e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQvtHELGILQNLQ-HPLLVSLLDTFETPTSYVLVLEMADQGRLLDC 2852
Cdd:cd14180     14 LGEGSFSVCRKCRHRQSGQEYAVKIISRRMEANTQ--REVAALRLCQsHPNIVALHEVLHDQYHTYLVMELLRGGELLDR 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2853 VVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDA-VQLNTTYYIHQLLGNPEFA 2931
Cdd:cd14180     92 IKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDGAVLKVIDFGFArLRPQGSRPLQTPCFTLQYA 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2932 APEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDS-------VEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQ 3004
Cdd:cd14180    172 APELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRgkmfhnhAADIMHKIKEGDFSLEGEAWKGVSEEAKDLVRGLLT 251
                          250       260
                   ....*....|....*....|.
gi 1907111721 3005 EDPAKRPSAALALQEQWLQAG 3025
Cdd:cd14180    252 VDPAKRLKLSELRESDWLQGG 272
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
2774-3021 1.03e-28

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-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: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 117.84  E-value: 1.03e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFV-----NKKLMKR-DQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQG 2847
Cdd:cd06625      8 LGQGAFGQVYLCYDADTGRELAVKQVeidpiNTEASKEvKALECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPGG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2848 RLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNT---TYYIHQL 2924
Cdd:cd06625     88 SVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSN---GNVKLGDFGASKRLQTicsSTGMKSV 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2925 LGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNIC--RLDFSFPedyfQGVSQKAKEFVCFL 3002
Cdd:cd06625    165 TGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIAtqPTNPQLP----PHVSEDARDFLSLI 240
                          250
                   ....*....|....*....
gi 1907111721 3003 LQEDPAKRPSAALALQEQW 3021
Cdd:cd06625    241 FVRNKKQRPSAEELLSHSF 259
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
2775-3019 1.20e-28

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K 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: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 119.43  E-value: 1.20e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2775 GRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQ--VTH---ELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd05584      8 GYGKVFQVRKTTGSDKGKIFAMKVLKKASIVRNQkdTAHtkaERNILEAVKHPFIVDLHYAFQTGGKLYLILEYLSGGEL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFG---DAVQLNTTyyIHQLLG 2926
Cdd:cd05584     88 FMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLD---AQGHVKLTDFGlckESIHDGTV--THTFCG 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2927 NPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEdYfqgVSQKAKEFVCFLLQED 3006
Cdd:cd05584    163 TIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPP-Y---LTNEARDLLKKLLKRN 238
                          250
                   ....*....|....*..
gi 1907111721 3007 PAKR----PSAALALQE 3019
Cdd:cd05584    239 VSSRlgsgPGDAEEIKA 255
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
2774-3010 1.63e-28

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK 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: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 119.34  E-value: 1.63e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKK-LMKRDQVT---HELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd05601      9 IGRGHFGEVQVVKEKATGDIYAMKVLKKSeTLAQEEVSffeEERDIMAKANSPWITKLQYAFQDSENLYLVMEYHPGGDL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRW-GSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTYYIHQLL--G 2926
Cdd:cd05601     89 LSLLSRYdDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRT---GHIKLADFGSAAKLSSDKTVTSKMpvG 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2927 NPEFAAPEIIL---GNPVS---LTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNIcrLDF----SFPEDyfQGVSQKAK 2996
Cdd:cd05601    166 TPDYIAPEVLTsmnGGSKGtygVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNI--MNFkkflKFPED--PKVSESAV 241
                          250
                   ....*....|....
gi 1907111721 2997 EFVCFLLqEDPAKR 3010
Cdd:cd05601    242 DLIKGLL-TDAKER 254
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
2768-3022 3.01e-28

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The Unc-89 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: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 116.48  E-value: 3.01e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTK--RAVATKfVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMAd 2845
Cdd:cd14112      5 FSFGSEIFRGRFSVIVKAVDSTTEtdAHCAVK-IFEVSDEASEAVREFESLRTLQHENVQRLIAAFKPSNFAYLVMEKL- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2846 QGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdQSLAKPTIKLADFGDAVQLNTTYYIhQLL 2925
Cdd:cd14112     83 QEDVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMF-QSVRSWQVKLVDFGRAQKVSKLGKV-PVD 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2926 GNPEFAAPEIILGN-PVSLTADTWSVGVLTYVLLSGVSPFL--DDSVEETCLNICRLDFSfPEDYFQGVSQKAKEFVCFL 3002
Cdd:cd14112    161 GDTDWASPEFHNPEtPITVQSDIWGLGVLTFCLLSGFHPFTseYDDEEETKENVIFVKCR-PNLIFVEATQEALRFATWA 239
                          250       260
                   ....*....|....*....|
gi 1907111721 3003 LQEDPAKRPSAALALQEQWL 3022
Cdd:cd14112    240 LKKSPTRRMRTDEALEHRWL 259
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
2774-3022 3.12e-28

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 116.11  E-value: 3.12e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVT----HELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd14164      8 IGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPDFVQkflpRELSILRRVNHPNIVQMFECIEVANGRLYIVMEAAATDL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdqSLAKPTIKLADFG------DAVQLNTTYyihq 2923
Cdd:cd14164     88 LQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILL--SADDRKIKIADFGfarfveDYPELSTTF---- 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2924 lLGNPEFAAPEIILGNPVSLTA-DTWSVGVLTYVLLSGVSPFLDDSVeetclNICRLDfSFPEDYFQGVS--QKAKEFVC 3000
Cdd:cd14164    162 -CGSRAYTPPEVILGTPYDPKKyDVWSLGVVLYVMVTGTMPFDETNV-----RRLRLQ-QRGVLYPSGVAleEPCRALIR 234
                          250       260
                   ....*....|....*....|..
gi 1907111721 3001 FLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14164    235 TLLQFNPSTRPSIQQVAGNSWL 256
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
2768-3022 3.82e-28

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


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 115.80  E-value: 3.82e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVV----KKCDQkgtkRAVATKFVNKKLMKR-------DQVTHELGIL---QNLQHPLLVSLLDTFET 2833
Cdd:cd14005      2 YEVGDLLGKGGFGTVysgvRIRDG----LPVAVKFVPKSRVTEwamingpVPVPLEIALLlkaSKPGVPGVIRLLDWYER 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2834 PTSYVLVLEMA----DqgrLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslaKPT--IKLA 2907
Cdd:cd14005     78 PDGFLLIMERPepcqD---LFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLIN----LRTgeVKLI 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2908 DFGDAVQLNTTYYiHQLLGNPEFAAPEIIL-----GNPvsltADTWSVGVLTYVLLSGVSPFLDDsveetcLNICRLDFS 2982
Cdd:cd14005    151 DFGCGALLKDSVY-TDFDGTRVYSPPEWIRhgryhGRP----ATVWSLGILLYDMLCGDIPFEND------EQILRGNVL 219
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1907111721 2983 FPedyfQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14005    220 FR----PRLSKECCDLISRCLQFDPSKRPSLEQILSHPWF 255
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
2774-3022 3.96e-28

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-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: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 116.25  E-value: 3.96e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQK--GTKRAVATKFVNKKLMK------RDQVTHELGILQNLQHPLLVSLLDTFETPTS-YVLVLEMA 2844
Cdd:cd13994      1 IGKGATSVVRIVTKKnpRSGVLYAVKEYRRRDDEskrkdyVKRLTSEYIISSKLHHPNIVKVLDLCQDLHGkWCLVMEYC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 DQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQL-----NTTY 2919
Cdd:cd13994     81 PGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDG---VLKLTDFGTAEVFgmpaeKESP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2920 YIHQLLGNPEFAAPEIILGNPVS-LTADTWSVGVLTYVLLSGVSPF----LDDSVEETCLNICRLDFSFPEDYFQGVSQK 2994
Cdd:cd13994    158 MSAGLCGSEPYMAPEVFTSGSYDgRAVDVWSCGIVLFALFTGRFPWrsakKSDSAYKAYEKSGDFTNGPYEPIENLLPSE 237
                          250       260
                   ....*....|....*....|....*...
gi 1907111721 2995 AKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd13994    238 CRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
2774-3023 6.39e-28

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk 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: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 116.28  E-value: 6.39e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKL-MKRDQVTHELGILQNLQ-HPLLVSLLDTFETPTSYVLVLEMADQGRLLD 2851
Cdd:cd14174     10 LGEGAYAKVQGCVSLQNGKEYAVKIIEKNAgHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLRGGSILA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2852 CVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADF--GDAVQLN------TTYYIHQ 2923
Cdd:cd14174     90 HIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVSPVKICDFdlGSGVKLNsactpiTTPELTT 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2924 LLGNPEFAAPEI--ILGNPVSL---TADTWSVGVLTYVLLSGVSPFLDD----------SVEETCLN-----ICRLDFSF 2983
Cdd:cd14174    170 PCGSAEYMAPEVveVFTDEATFydkRCDLWSLGVILYIMLSGYPPFVGHcgtdcgwdrgEVCRVCQNklfesIQEGKYEF 249
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1907111721 2984 PEDYFQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQ 3023
Cdd:cd14174    250 PDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
2768-3049 6.70e-28

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-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: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 115.81  E-value: 6.70e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVN--KKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMAD 2845
Cdd:cd06609      3 FTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDleEAEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIMEYCG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2846 QGRLLDcVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQL-NTTYYIHQL 2924
Cdd:cd06609     83 GGSVLD-LLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLS---EEGDVKLADFGVSGQLtSTMSKRNTF 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2925 LGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDF-SFPEDYFqgvSQKAKEFVCFLL 3003
Cdd:cd06609    159 VGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNNPpSLEGNKF---SKPFKDFVELCL 235
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1907111721 3004 QEDPAKRPSAALALQEQWLQAgngSGKgtgvldTSRLTSFIERRKH 3049
Cdd:cd06609    236 NKDPKERPSAKELLKHKFIKK---AKK------TSYLTLLIERIKK 272
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
2771-2976 7.44e-28

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group 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: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 118.60  E-value: 7.44e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2771 VAELGRGRFAVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTH---ELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQ 2846
Cdd:cd05600     16 LTQVGQGGYGSVFLARKKDTGEICALKIMKKKvLFKLNEVNHvltERDILTTTNSPWLVKLLYAFQDPENVYLAMEYVPG 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2847 G--RLLDCVVrwGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDA------------ 2912
Cdd:cd05600     96 GdfRTLLNNS--GILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSS---GHIKLTDFGLAsgtlspkkiesm 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2913 -VQLN-------------------------TTYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLD 2966
Cdd:cd05600    171 kIRLEevkntafleltakerrniyramrkeDQNYANSVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFSG 250
                          250
                   ....*....|
gi 1907111721 2967 DSVEETCLNI 2976
Cdd:cd05600    251 STPNETWANL 260
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
2768-3010 8.11e-28

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 115.25  E-value: 8.11e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQG 2847
Cdd:cd14662      2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKIDENVQREIINHRSLRHPNIIRFKEVVLTPTHLAIVMEYAAGG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2848 RLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAkPTIKLADFGdavqLNTTYYIHQ---- 2923
Cdd:cd14662     82 ELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPA-PRLKICDFG----YSKSSVLHSqpks 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2924 LLGNPEFAAPEIILGNPVS-LTADTWSVGVLTYVLLSGVSPFLDDS----VEETCLNICRLDFSFPeDYFQgVSQKAKEF 2998
Cdd:cd14662    157 TVGTPAYIAPEVLSRKEYDgKVADVWSCGVTLYVMLVGAYPFEDPDdpknFRKTIQRIMSVQYKIP-DYVR-VSQDCRHL 234
                          250
                   ....*....|..
gi 1907111721 2999 VCFLLQEDPAKR 3010
Cdd:cd14662    235 LSRIFVANPAKR 246
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
2774-3024 9.29e-28

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: 115.35  E-value: 9.29e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTH----ELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd14117     14 LGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGVEHqlrrEIEIQSHLRHPNILRLYNYFHDRKRIYLILEYAPRGEL 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQlNTTYYIHQLLGNPE 2929
Cdd:cd14117     94 YKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMG---YKGELKIADFGWSVH-APSLRRRTMCGTLD 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2930 FAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPedyfQGVSQKAKEFVCFLLQEDPAK 3009
Cdd:cd14117    170 YLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFP----PFLSDGSRDLISKLLRYHPSE 245
                          250
                   ....*....|....*
gi 1907111721 3010 RPSAALALQEQWLQA 3024
Cdd:cd14117    246 RLPLKGVMEHPWVKA 260
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
2774-3013 1.88e-27

Catalytic domain of Suppressor of loss of cAMP-dependent protein 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 of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-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: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 116.13  E-value: 1.88e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLM-KRDQVTHELG---ILQNL---QHPLLVSLLDTFETPTSYVLVLEMADQ 2846
Cdd:cd05586      1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIvAKKEVAHTIGernILVRTaldESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2847 GRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFG-DAVQLNTTYYIHQLL 2925
Cdd:cd05586     81 GELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLD---ANGHIALCDFGlSKADLTDNKTTNTFC 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2926 GNPEFAAPEIILGNP-VSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYfqgVSQKAKEFVCFLLQ 3004
Cdd:cd05586    158 GTTEYLAPEVLLDEKgYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKDV---LSDEGRSFVKGLLN 234

                   ....*....
gi 1907111721 3005 EDPAKRPSA 3013
Cdd:cd05586    235 RNPKHRLGA 243
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
2774-3019 2.47e-27

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 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: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 113.65  E-value: 2.47e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKK--CDQKGTKRAVA-TKFVNKKLMKRD---QVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQG 2847
Cdd:cd06632      8 LGSGSFGSVYEgfNGDTGDFFAVKeVSLVDDDKKSREsvkQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVPGG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2848 RLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAkptIKLADFGDAVQLNTTYYIHQLLGN 2927
Cdd:cd06632     88 SIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGV---VKLADFGMAKHVEAFSFAKSFKGS 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2928 PEFAAPEIIL--GNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDF--SFPEDyfqgVSQKAKEFVCFLL 3003
Cdd:cd06632    165 PYWMAPEVIMqkNSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGElpPIPDH----LSPDAKDFIRLCL 240
                          250
                   ....*....|....*.
gi 1907111721 3004 QEDPAKRPSAALALQE 3019
Cdd:cd06632    241 QRDPEDRPTASQLLEH 256
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
2770-3022 2.78e-27

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-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: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 113.52  E-value: 2.78e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2770 EVAE-LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQ------HPLLVSLLDTFETPTSYVLVLE 2842
Cdd:cd14133      2 EVLEvLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDQSLDEIRLLELLNkkdkadKYHIVRLKDVFYFKNHLCIVFE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 MADQGrLLDCV--VRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdQSLAKPTIKLADFGDAVQLN--TT 2918
Cdd:cd14133     82 LLSQN-LYEFLkqNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILL-ASYSRCQIKIIDFGSSCFLTqrLY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2919 YYIHQLLgnpeFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEF 2998
Cdd:cd14133    160 SYIQSRY----YRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPAHMLDQGKADDELF 235
                          250       260
                   ....*....|....*....|....*..
gi 1907111721 2999 VCFL---LQEDPAKRPSAALALQEQWL 3022
Cdd:cd14133    236 VDFLkklLEIDPKERPTASQALSHPWL 262
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
2774-3010 2.84e-27

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma 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: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 115.95  E-value: 2.84e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTHELG---ILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd05593     23 LGKGTFGKVILVREKASGKYYAMKILKKEvIIAKDEVAHTLTesrVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFG-------DAVQLNTtyyih 2922
Cdd:cd05593    103 FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKD---GHIKITDFGlckegitDAATMKT----- 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2923 qLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPedyfQGVSQKAKEFVCFL 3002
Cdd:cd05593    175 -FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFP----RTLSADAKSLLSGL 249

                   ....*...
gi 1907111721 3003 LQEDPAKR 3010
Cdd:cd05593    250 LIKDPNKR 257
PH2_Kalirin_Trio_p63RhoGEF cd13241
p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor ...
1438-1573 3.25e-27

p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor p63RhoGEF is an effector of the heterotrimeric G protein, Galphaq and linking Galphaq-coupled receptors (GPCRs) to the activation of RhoA. The Dbl(DH) and PH domains of p63RhoGEF interact with the effector-binding site and the C-terminal region of Galphaq and appear to relieve autoinhibition of the catalytic DH domain by the PH domain. Trio, Duet, and p63RhoGEF are shown to constitute a family of Galphaq effectors that appear to activate RhoA both in vitro and in intact cells. Dbs is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a rhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Trio is a multidomain signaling protein that contains two RhoGEF(DH)-PH domains in tandem. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270061  Cd Length: 140  Bit Score: 109.27  E-value: 3.25e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1438 LSMLEGFDENIESQGELILQESFQVWDPK-TLIRKGRERHLFLFEMSLVFSKEVKDSSGRSK--YLYKSKLFTSELGVTE 1514
Cdd:cd13241      1 VGRLQGFDGKITAQGKLLLQGTLLVSEPSaGLLQKGKERRVFLFEQIIIFSEILGKKTQFSNpgYIYKNHIKVNKMSLEE 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1515 HVEGDPCKFALWvGRTP-TSDNKIVLKASSIENKQDWIKHIREVIQERTVHLRgALKEPI 1573
Cdd:cd13241     81 NVDGDPLRFALK-SRDPnNPSETFILQAASPEVRQEWVDTINQILDTQRDFLK-ALQSPI 138
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
2768-3020 3.39e-27

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: 113.26  E-value: 3.39e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLM---KRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMA 2844
Cdd:cd08530      2 FKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLsqkEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEYA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 DQGRLLDCVVRWGS----LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdqsLAKPTIKLADFGDAVQLNTTYY 2920
Cdd:cd08530     82 PFGDLSKLISKRKKkrrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILL---SAGDLVKIGDLGISKVLKKNLA 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2921 IHQLlGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFqgvSQKAKEFVC 3000
Cdd:cd08530    159 KTQI-GTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKFPPIPPVY---SQDLQQIIR 234
                          250       260
                   ....*....|....*....|
gi 1907111721 3001 FLLQEDPAKRPSAALALQEQ 3020
Cdd:cd08530    235 SLLQVNPKKRPSCDKLLQSP 254
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
2773-3010 7.83e-27

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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 AMP-activated protein kinase (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 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: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 112.84  E-value: 7.83e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRAVATKFVNK-KLMKR-----------------------DQVTHELGILQNLQHPLLVSLL 2828
Cdd:cd14118      1 EIGKGSYGIVKLAYNEEDNTLYAMKILSKkKLLKQagffrrppprrkpgalgkpldplDRVYREIAILKKLDHPNVVKLV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2829 DTFETPT--SYVLVLEMADQGRLLDcVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKL 2906
Cdd:cd14118     81 EVLDDPNedNLYMVFELVDKGAVME-VPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDD---GHVKI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2907 ADFG--------DAVQLNTTyyihqllGNPEFAAPEIILGNPVSLT---ADTWSVGVLTYVLLSGVSPFLDDSVEETCLN 2975
Cdd:cd14118    157 ADFGvsnefegdDALLSSTA-------GTPAFMAPEALSESRKKFSgkaLDIWAMGVTLYCFVFGRCPFEDDHILGLHEK 229
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1907111721 2976 ICRLDFSFPEDYFqgVSQKAKEFVCFLLQEDPAKR 3010
Cdd:cd14118    230 IKTDPVVFPDDPV--VSEQLKDLILRMLDKNPSER 262
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
2774-3019 9.22e-27

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 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: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 113.91  E-value: 9.22e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTHELG----ILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGR 2848
Cdd:cd05603      3 IGKGSFGKVLLAKRKCDGKFYAVKVLQKKtILKKKEQNHIMAernvLLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNGGE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFG---DAVQLNTTyyIHQLL 2925
Cdd:cd05603     83 LFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLD---CQGHVVLTDFGlckEGMEPEET--TSTFC 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2926 GNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPedyfQGVSQKAKEFVCFLLQE 3005
Cdd:cd05603    158 GTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLP----GGKTVAACDLLQGLLHK 233
                          250
                   ....*....|....
gi 1907111721 3006 DPAKRPSAALALQE 3019
Cdd:cd05603    234 DQRRRLGAKADFLE 247
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
2774-3010 1.35e-26

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 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: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 113.96  E-value: 1.35e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTHELG----ILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGR 2848
Cdd:cd05602     15 IGKGSFGKVLLARHKSDEKFYAVKVLQKKaILKKKEEKHIMSernvLLKNVKHPFLVGLHFSFQTTDKLYFVLDYINGGE 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFG---DAVQLNTTyyIHQLL 2925
Cdd:cd05602     95 LFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLD---SQGHIVLTDFGlckENIEPNGT--TSTFC 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2926 GNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNIcrldFSFPEDYFQGVSQKAKEFVCFLLQE 3005
Cdd:cd05602    170 GTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNI----LNKPLQLKPNITNSARHLLEGLLQK 245

                   ....*
gi 1907111721 3006 DPAKR 3010
Cdd:cd05602    246 DRTKR 250
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
2774-3023 1.81e-26

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 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: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 111.09  E-value: 1.81e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNK-------KLMKRDQVTHELGILQNL----QHPLLVSLLDTFETPTSYVLVLE 2842
Cdd:cd14101      8 LGKGGFGTVYAGHRISDGLQVAIKQISRnrvqqwsKLPGVNPVPNEVALLQSVgggpGHRGVIRLLDWFEIPEGFLLVLE 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 MADQGR-LLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqsLAKPTIKLADFGDAVQLNTTYYI 2921
Cdd:cd14101     88 RPQHCQdLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVD--LRTGDIKLIDFGSGATLKDSMYT 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2922 hQLLGNPEFAAPEIILGNPV-SLTADTWSVGVLTYVLLSGVSPFLDDSveetclNICRLDFSFPEDyfqgVSQKAKEFVC 3000
Cdd:cd14101    166 -DFDGTRVYSPPEWILYHQYhALPATVWSLGILLYDMVCGDIPFERDT------DILKAKPSFNKR----VSNDCRSLIR 234
                          250       260
                   ....*....|....*....|...
gi 1907111721 3001 FLLQEDPAKRPSAALALQEQWLQ 3023
Cdd:cd14101    235 SCLAYNPSDRPSLEQILLHPWMM 257
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
2774-3010 2.24e-26

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK 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: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 111.33  E-value: 2.24e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFA---VVKKCDQKGTKRAVATKFVNKK--LMKRDQVTH---ELGILQNL-QHPLLVSLLDTFETPTSYVLVLEMA 2844
Cdd:cd05583      2 LGTGAYGkvfLVRKVGGHDAGKLYAMKVLKKAtiVQKAKTAEHtmtERQVLEAVrQSPFLVTLHYAFQTDAKLHLILDYV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 DQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQL--NTTYYIH 2922
Cdd:cd05583     82 NGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDS---EGHVVLTDFGLSKEFlpGENDRAY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2923 QLLGNPEFAAPEIILGNPV--SLTADTWSVGVLTYVLLSGVSPFLDD----SVEETCLNICRLDFSFPEDYfqgvSQKAK 2996
Cdd:cd05583    159 SFCGTIEYMAPEVVRGGSDghDKAVDWWSLGVLTYELLTGASPFTVDgernSQSEISKRILKSHPPIPKTF----SAEAK 234
                          250
                   ....*....|....
gi 1907111721 2997 EFVCFLLQEDPAKR 3010
Cdd:cd05583    235 DFILKLLEKDPKKR 248
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
2768-3021 3.72e-26

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. 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 CDK7 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: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 111.51  E-value: 3.72e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATK--FVNKKLMKRDQVT----HELGILQNLQHPLLVSLLDTFETPTSYVLVL 2841
Cdd:cd07841      2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKkiKLGERKEAKDGINftalREIKLLQELKHPNIIGLLDVFGHKSNINLVF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2842 EMADQGrlLDCVVRWGS--LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQLNT-- 2917
Cdd:cd07841     82 EFMETD--LEKVIKDKSivLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIA---SDGVLKLADFGLARSFGSpn 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2918 TYYIHQLLgNPEFAAPEIILG-NPVSLTADTWSVGVLTYVLLSGVsPFLDDSVEETCLN-ICRL---------------- 2979
Cdd:cd07841    157 RKMTHQVV-TRWYRAPELLFGaRHYGVGVDMWSVGCIFAELLLRV-PFLPGDSDIDQLGkIFEAlgtpteenwpgvtslp 234
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2980 ---DFS-FP----EDYFQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQW 3021
Cdd:cd07841    235 dyvEFKpFPptplKQIFPAASDDALDLLQRLLTLNPNKRITARQALEHPY 284
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
2775-3003 3.91e-26

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 111.94  E-value: 3.91e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2775 GRGRFAVVKKCDQKGTKRAVATKFVNKKLM-KRDQVTH---ELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLL 2850
Cdd:cd05599     10 GRGAFGEVRLVRKKDTGHVYAMKKLRKSEMlEKEQVAHvraERDILAEADNPWVVKLYYSFQDEENLYLIMEFLPGGDMM 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2851 DCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQLNTTYYIHQLLGNPEF 2930
Cdd:cd05599     90 TLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLD---ARGHIKLSDFGLCTGLKKSHLAYSTVGTPDY 166
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907111721 2931 AAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNI--CRLDFSFPEDyfQGVSQKAKEFVCFLL 3003
Cdd:cd05599    167 IAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKImnWRETLVFPPE--VPISPEAKDLIERLL 239
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
2774-3010 3.94e-26

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 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: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 111.98  E-value: 3.94e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTHELG----ILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGR 2848
Cdd:cd05604      4 IGKGSFGKVLLAKRKRDGKYYAVKVLQKKvILNRKEQKHIMAernvLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVNGGE 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFG----DAVQLNTTYyihQL 2924
Cdd:cd05604     84 LFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLD---SQGHIVLTDFGlckeGISNSDTTT---TF 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2925 LGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNIcrldFSFPEDYFQGVSQKAKEFVCFLLQ 3004
Cdd:cd05604    158 CGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENI----LHKPLVLRPGISLTAWSILEELLE 233

                   ....*.
gi 1907111721 3005 EDPAKR 3010
Cdd:cd05604    234 KDRQLR 239
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
2773-3018 8.11e-26

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 109.73  E-value: 8.11e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRAVATKFVNKKLM----KRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGR 2848
Cdd:cd08228      9 KIGRGQFSEVYRATCLLDRKPVALKKVQIFEMmdakARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLELADAGD 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVVRWGS----LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQLNT-TYYIHQ 2923
Cdd:cd08228     89 LSQMIKYFKKqkrlIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFIT---ATGVVKLGDLGLGRFFSSkTTAAHS 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2924 LLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVE--ETCLNICRLDF-SFPEDYFqgvSQKAKEFVC 3000
Cdd:cd08228    166 LVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNlfSLCQKIEQCDYpPLPTEHY---SEKLRELVS 242
                          250
                   ....*....|....*...
gi 1907111721 3001 FLLQEDPAKRPSAALALQ 3018
Cdd:cd08228    243 MCIYPDPDQRPDIGYVHQ 260
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
2767-3023 1.60e-25

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-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: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 109.06  E-value: 1.60e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2767 FYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKlmKRDQVTH---ELGILQNLQHPLLVSLLDTFETPTSYVLVLEM 2843
Cdd:cd06611      6 IWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIE--SEEELEDfmvEIDILSECKHPNIVGLYEAYFYENKLWILIEF 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQGRLLDCVVRWGS-LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFG-DAVQLNTTYYI 2921
Cdd:cd06611     84 CDGGALDSIMLELERgLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLD---GDVKLADFGvSAKNKSTLQKR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2922 HQLLGNPEFAAPEIIL-----GNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLD---FSFPedyfQGVSQ 2993
Cdd:cd06611    161 DTFIGTPYWMAPEVVAcetfkDNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEpptLDQP----SKWSS 236
                          250       260       270
                   ....*....|....*....|....*....|
gi 1907111721 2994 KAKEFVCFLLQEDPAKRPSAALALQEQWLQ 3023
Cdd:cd06611    237 SFNDFLKSCLVKDPDDRPTAAELLKHPFVS 266
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
2774-3010 2.78e-25

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha 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: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 110.50  E-value: 2.78e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTHELG---ILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd05594     33 LGKGTFGKVILVKEKATGRYYAMKILKKEvIVAKDEVAHTLTenrVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCR-IAHLDLKPENILVDQSlakPTIKLADFG---DAVQLNTTyyIHQLL 2925
Cdd:cd05594    113 FFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKD---GHIKITDFGlckEGIKDGAT--MKTFC 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2926 GNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPedyfQGVSQKAKEFVCFLLQE 3005
Cdd:cd05594    188 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFP----RTLSPEAKSLLSGLLKK 263

                   ....*
gi 1907111721 3006 DPAKR 3010
Cdd:cd05594    264 DPKQR 268
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
2774-3010 3.48e-25

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-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: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 109.01  E-value: 3.48e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTH----ELGILQ-NLQHPLLVSLLDTFETPTSYVLVLEMADQGR 2848
Cdd:cd05592      3 LGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDDDVEctmiERRVLAlASQHPFLTHLFCTFQTESHLFFVMEYLNGGD 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAV-QLNTTYYIHQLLGN 2927
Cdd:cd05592     83 LMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDR---EGHIKIADFGMCKeNIYGENKASTFCGT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2928 PEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPedyfQGVSQKAKEFVCFLLQEDP 3007
Cdd:cd05592    160 PDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHYP----RWLTKEAASCLSLLLERNP 235

                   ...
gi 1907111721 3008 AKR 3010
Cdd:cd05592    236 EKR 238
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
2774-3010 3.73e-25

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 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: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 108.19  E-value: 3.73e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd05630      8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKgeamALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGGDL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGS--LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTYYIHQLLGN 2927
Cdd:cd05630     88 KFHIYHMGQagFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDH---GHIRISDLGLAVHVPEGQTIKGRVGT 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2928 PEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQEDP 3007
Cdd:cd05630    165 VGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPEEYSEKFSPQARSLCSMLLCKDP 244

                   ...
gi 1907111721 3008 AKR 3010
Cdd:cd05630    245 AER 247
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
535-751 3.74e-25

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 105.99  E-value: 3.74e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  535 QLCVFQQDVQQVLDWIENHGEAFLSkhTGVGKSLHRARALQKRHEDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIY 614
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  615 QAAHQLEDRIQDFVRRVEQRKILLDMSV---SFHTHVKELWTWLEELQKELLDDVYAESVEAVQDLIKRFgqqqqttlQV 691
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALdlqQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKH--------KE 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  692 TVNVIKEGEDLIQQLRDSAISSNKTPHNSSINHIETVLQQLDEAQSQMEELFQERKIKLE 751
Cdd:cd00176    151 LEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
2774-3012 4.33e-25

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 106.96  E-value: 4.33e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKR-----DQVTHELGILQNLQHPLLVSLLDTFETPTS---YvLVLEMAD 2845
Cdd:cd14119      1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLRRipngeANVKREIQILRRLNHRNVIKLVDVLYNEEKqklY-MVMEYCV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2846 QG--RLLDCVVRwGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILV--DQslakpTIKLADFGDAVQLN---TT 2918
Cdd:cd14119     80 GGlqEMLDSAPD-KRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLttDG-----TLKISDFGVAEALDlfaED 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2919 YYIHQLLGNPEFAAPEIILGNPV--SLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDyfqgVSQKAK 2996
Cdd:cd14119    154 DTCTTSQGSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIPDD----VDPDLQ 229
                          250
                   ....*....|....*.
gi 1907111721 2997 EFVCFLLQEDPAKRPS 3012
Cdd:cd14119    230 DLLRGMLEKDPEKRFT 245
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
2774-3022 7.65e-25

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK 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: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 107.55  E-value: 7.65e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCdqkgTKRAVATKFVNKKLMKRDQVTHELGILQNLQ-HPLLVSLLDTF---------ETPTSYVL-VLE 2842
Cdd:cd14171     14 LGTGISGPVRVC----VKKSTGERFALKILLDRPKARTEVRLHMMCSgHPNIVQIYDVYansvqfpgeSSPRARLLiVME 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 MADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFG----DAVQLNTT 2918
Cdd:cd14171     90 LMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEDAPIKLCDFGfakvDQGDLMTP 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2919 YYihqllgNPEFAAPEII----------LGNPVSLT-------ADTWSVGVLTYVLLSGVSPFLDDSVEETCLN-----I 2976
Cdd:cd14171    170 QF------TPYYVAPQVLeaqrrhrkerSGIPTSPTpytydksCDMWSLGVIIYIMLCGYPPFYSEHPSRTITKdmkrkI 243
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1907111721 2977 CRLDFSFPEDYFQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14171    244 MTGSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
2774-3010 7.93e-25

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK 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: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 107.87  E-value: 7.93e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFA---VVKKCDQKGTKRAVATKFVNKKLMK-RDQV--THELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQG 2847
Cdd:cd05582      3 LGQGSFGkvfLVRKITGPDAGTLYAMKVLKKATLKvRDRVrtKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFLRGG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2848 RLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFG---DAV-QLNTTYyihQ 2923
Cdd:cd05582     83 DLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLD---EDGHIKLTDFGlskESIdHEKKAY---S 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2924 LLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPedyfQGVSQKAKEFVCFLL 3003
Cdd:cd05582    157 FCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMP----QFLSPEAQSLLRALF 232

                   ....*..
gi 1907111721 3004 QEDPAKR 3010
Cdd:cd05582    233 KRNPANR 239
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
2774-3022 8.34e-25

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 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: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 106.80  E-value: 8.34e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRD---------QVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMA 2844
Cdd:cd14076      9 LGEGEFGKVKLGWPLPKANHRSGVQVAIKLIRRDtqqencqtsKIMREINILKGLTHPNIVRLLDVLKTKKYIGIVLEFV 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 DQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQ--LNTTYYIH 2922
Cdd:cd14076     89 SGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKN---RNLVITDFGFANTfdHFNGDLMS 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2923 QLLGNPEFAAPEIILGNPV--SLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRL-------DFSFPEDyfqgVSQ 2993
Cdd:cd14076    166 TSCGSPCYAAPELVVSDSMyaGRKADIWSCGVILYAMLAGYLPFDDDPHNPNGDNVPRLyryicntPLIFPEY----VTP 241
                          250       260
                   ....*....|....*....|....*....
gi 1907111721 2994 KAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14076    242 KARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
2774-3011 1.10e-24

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK 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: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 106.63  E-value: 1.10e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKF--VN------KKLMKRDQVTHELGILQNLQHPLLVSLLDTFET-PTSYVLVLEMA 2844
Cdd:cd13990      8 LGKGGFSEVYKAFDLVEQRYVACKIhqLNkdwseeKKQNYIKHALREYEIHKSLDHPRIVKLYDVFEIdTDSFCTVLEYC 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 DqGRLLDCVV-RWGSLTEGKVRAHLGEVLEAVRYLHNCR--IAHLDLKPENILVDQSLAKPTIKLADFGDAVQLNTTYYI 2921
Cdd:cd13990     88 D-GNDLDFYLkQHKSIPEREARSIIMQVVSALKYLNEIKppIIHYDLKPGNILLHSGNVSGEIKITDFGLSKIMDDESYN 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2922 H-------QLLGNPEFAAPEIILGNP----VSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCL--NICR--LDFSFPED 2986
Cdd:cd13990    167 SdgmeltsQGAGTYWYLPPECFVVGKtppkISSKVDVWSVGVIFYQMLYGRKPFGHNQSQEAILeeNTILkaTEVEFPSK 246
                          250       260
                   ....*....|....*....|....*
gi 1907111721 2987 yfQGVSQKAKEFVCFLLQEDPAKRP 3011
Cdd:cd13990    247 --PVVSSEAKDFIRRCLTYRKEDRP 269
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
2768-3010 1.27e-24

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 106.75  E-value: 1.27e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVN-KKLMKRDQVTH---ELGILQNLQHPLLVSLLDTFETPTSYVLVLEM 2843
Cdd:cd05612      3 FERIKTIGTGTFGRVHLVRDRISEHYYALKVMAiPEVIRLKQEQHvhnEKRVLKEVSHPFIIRLFWTEHDQRFLYMLMEY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQLNTTYYihQ 2923
Cdd:cd05612     83 VPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDK---EGHIKLTDFGFAKKLRDRTW--T 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2924 LLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNIC--RLDFSFPEDYFqgvsqkAKEFVCF 3001
Cdd:cd05612    158 LCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILagKLEFPRHLDLY------AKDLIKK 231

                   ....*....
gi 1907111721 3002 LLQEDPAKR 3010
Cdd:cd05612    232 LLVVDRTRR 240
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
2774-2976 1.70e-24

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS 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: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 107.40  E-value: 1.70e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTH---ELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd05598      9 IGVGAFGEVSLVRKKDTNALYAMKTLRKKdVLKRNQVAHvkaERDILAEADNEWVVKLYYSFQDKENLYFVMDYIPGGDL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQL----NTTYYI-HQL 2924
Cdd:cd05598     89 MSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRD---GHIKLTDFGLCTGFrwthDSKYYLaHSL 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907111721 2925 LGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNI 2976
Cdd:cd05598    166 VGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKV 217
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
2773-3022 2.03e-24

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: 105.19  E-value: 2.03e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRAVATKFVNKKLM---KRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd08529      7 KLGKGSFGVVYKVVRKVDGRVYALKQIDISRMsrkMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEYAENGDL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGS--LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQLN-TTYYIHQLLG 2926
Cdd:cd08529     87 HSLIKSQRGrpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGD---NVKIGDLGVAKILSdTTNFAQTIVG 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2927 NPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFS-FPEDYFQGVSQkakeFVCFLLQE 3005
Cdd:cd08529    164 TPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPpISASYSQDLSQ----LIDSCLTK 239
                          250
                   ....*....|....*..
gi 1907111721 3006 DPAKRPSAALALQEQWL 3022
Cdd:cd08529    240 DYRQRPDTTELLRNPSL 256
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
2774-3012 2.33e-24

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: 105.01  E-value: 2.33e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNK----KLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd14189      9 LGKGGFARCYEMTDLATNKTYAVKVIPHsrvaKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRKSL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAkptIKLADFGDAVQLNTTYYIHQLL-GNP 2928
Cdd:cd14189     89 AHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENME---LKVGDFGLAARLEPPEQRKKTIcGTP 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2929 EFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPedyfQGVSQKAKEFVCFLLQEDPA 3008
Cdd:cd14189    166 NYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLP----ASLSLPARHLLAGILKRNPG 241

                   ....
gi 1907111721 3009 KRPS 3012
Cdd:cd14189    242 DRLT 245
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
2777-3010 3.73e-24

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 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: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 105.47  E-value: 3.73e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2777 GRFAVVKKCDQKGTKRAVATKFVNK-----KLMKRDQVTHELGILQNL-QHPLLVSLLDTFETPTSYVLVLEMADQGRLL 2850
Cdd:cd05613     14 GKVFLVRKVSGHDAGKLYAMKVLKKativqKAKTAEHTRTERQVLEHIrQSPFLVTLHYAFQTDTKLHLILDYINGGELF 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2851 DCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQ--LNTTYYIHQLLGNP 2928
Cdd:cd05613     94 THLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSS---GHVVLTDFGLSKEflLDENERAYSFCGTI 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2929 EFAAPEIILGNPV--SLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQED 3006
Cdd:cd05613    171 EYMAPEIVRGGDSghDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAKDIIQRLLMKD 250

                   ....
gi 1907111721 3007 PAKR 3010
Cdd:cd05613    251 PKKR 254
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
2774-3012 3.87e-24

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: 104.16  E-value: 3.87e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVatkfvnkKLMKRDQVTH--------ELGILQNLQHPLLVSLLDTFETPTSYVLVLEMAD 2845
Cdd:cd13999      1 IGSGSFGEVYKGKWRGTDVAI-------KKLKVEDDNDellkefrrEVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMP 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2846 QGRLLDCvvrwgsLTEGKVRAHLGEVL-------EAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQLNTT 2918
Cdd:cd13999     74 GGSLYDL------LHKKKIPLSWSLRLkialdiaRGMNYLHSPPIIHRDLKSLNILLDENF---TVKIADFGLSRIKNST 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2919 YYIH-QLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLD-DSVEETCLNICR-----LDFSFPEDYFQGV 2991
Cdd:cd13999    145 TEKMtGVVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKElSPIQIAAAVVQKglrppIPPDCPPELSKLI 224
                          250       260
                   ....*....|....*....|.
gi 1907111721 2992 SQkakefvCflLQEDPAKRPS 3012
Cdd:cd13999    225 KR------C--WNEDPEKRPS 237
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
2768-3018 4.12e-24

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It 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: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 104.55  E-value: 4.12e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLM---KRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEM- 2843
Cdd:cd08217      2 YEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMsekEKQQLVSEVNILRELKHPNIVRYYDRIVDRANTTLYIVMe 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ----ADQGRLL-DCVVRWGSLTEGKVRAHLGEVLEAVRYLHNC-----RIAHLDLKPENILVDqslAKPTIKLADFGDAV 2913
Cdd:cd08217     82 ycegGDLAQLIkKCKKENQYIPEEFIWKIFTQLLLALYECHNRsvgggKILHRDLKPANIFLD---SDNNVKLGDFGLAR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2914 QLNT-TYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSF-PEDYfqgv 2991
Cdd:cd08217    159 VLSHdSSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKFPRiPSRY---- 234
                          250       260
                   ....*....|....*....|....*..
gi 1907111721 2992 SQKAKEFVCFLLQEDPAKRPSAALALQ 3018
Cdd:cd08217    235 SSELNEVIKSMLNVDPDKRPSVEELLQ 261
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
2768-3022 4.81e-24

Catalytic domain of Cyclin-Dependent protein 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 of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. 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 CDKL 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: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 105.09  E-value: 4.81e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVA---------TKFVNKKLMKrdqvthELGILQNLQHPLLVSLLDTFETPTSYV 2838
Cdd:cd07833      3 YEVLGVVGEGAYGVVLKCRNKATGEIVAikkfkesedDEDVKKTALR------EVKVLRQLRHENIVNLKEAFRRKGRLY 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2839 LVLEMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQL--N 2916
Cdd:cd07833     77 LVFEYVERTLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESG---VLKLCDFGFARALtaR 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2917 TTYYIHQLLGNPEFAAPEIILGNP-VSLTADTWSVGVLTYVLLSGVSPF------------------LDDSVEETCLNIC 2977
Cdd:cd07833    154 PASPLTDYVATRWYRAPELLVGDTnYGKPVDVWAIGCIMAELLDGEPLFpgdsdidqlyliqkclgpLPPSHQELFSSNP 233
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907111721 2978 RLD-FSFPE---------DYFQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd07833    234 RFAgVAFPEpsqpeslerRYPGKVSSPALDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
2774-3010 4.98e-24

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-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: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 104.74  E-value: 4.98e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd05605      8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKgeamALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTIMNGGDL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGS--LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTYYIHQLLGN 2927
Cdd:cd05605     88 KFHIYNMGNpgFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDH---GHVRISDLGLAVEIPEGETIRGRVGT 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2928 PEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPF-----------LDDSVEETclnicrldfsfPEDYFQGVSQKAK 2996
Cdd:cd05605    165 VGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFrarkekvkreeVDRRVKED-----------QEEYSEKFSEEAK 233
                          250
                   ....*....|....
gi 1907111721 2997 EFVCFLLQEDPAKR 3010
Cdd:cd05605    234 SICSQLLQKDPKTR 247
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
2768-3022 5.92e-24

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK 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: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 104.72  E-value: 5.92e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKfvnKKLMKR------DQVTHELGILQNLQ-HPLLVSLLDTFETPTSYVLV 2840
Cdd:cd07832      2 YKILGRIGEGAHGIVFKAKDRETGETVALK---KVALRKleggipNQALREIKALQACQgHPYVVKLRDVFPHGTGFVLV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2841 LEMADQG--RLLDCVVRwgSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQLN-- 2916
Cdd:cd07832     79 FEYMLSSlsEVLRDEER--PLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLIS---STGVLKIADFGLARLFSee 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2917 -TTYYIHQlLGNPEFAAPEIILGNP-VSLTADTWSVGVLTYVLLSGvSPFLD--DSVEETCLNICRL------------- 2979
Cdd:cd07832    154 dPRLYSHQ-VATRWYRAPELLYGSRkYDEGVDLWAVGCIFAELLNG-SPLFPgeNDIEQLAIVLRTLgtpnektwpelts 231
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907111721 2980 --DFS---FP-------EDYFQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd07832    232 lpDYNkitFPeskgirlEEIFPDCSPEAIDLLKGLLVYNPKKRLSAEEALRHPYF 286
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
2774-3022 6.07e-24

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


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 103.90  E-value: 6.07e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNK-------KLMKRDQVTHELGILQNLQHPL--LVSLLDTFETPTSYVLVLEMA 2844
Cdd:cd14100      8 LGSGGFGSVYSGIRVADGAPVAIKHVEKdrvsewgELPNGTRVPMEIVLLKKVGSGFrgVIRLLDWFERPDSFVLVLERP 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 DQGR-LLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqsLAKPTIKLADFGDAVQLNTTYYIhQ 2923
Cdd:cd14100     88 EPVQdLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILID--LNTGELKLIDFGSGALLKDTVYT-D 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2924 LLGNPEFAAPEIILGNPV-SLTADTWSVGVLTYVLLSGVSPFLDDsvEEtclnICRLDFSFPedyfQGVSQKAKEFVCFL 3002
Cdd:cd14100    165 FDGTRVYSPPEWIRFHRYhGRSAAVWSLGILLYDMVCGDIPFEHD--EE----IIRGQVFFR----QRVSSECQHLIKWC 234
                          250       260
                   ....*....|....*....|
gi 1907111721 3003 LQEDPAKRPSAALALQEQWL 3022
Cdd:cd14100    235 LALRPSDRPSFEDIQNHPWM 254
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
2774-3021 1.11e-23

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK 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: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 103.14  E-value: 1.11e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVthELGILQNlQHPLLVSLLDTFETPTS----YVLVLEMADQGRL 2849
Cdd:cd14089      9 LGLGINGKVLECFHKKTGEKFALKVLRDNPKARREV--ELHWRAS-GCPHIVRIIDVYENTYQgrkcLLVVMECMEGGEL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGS--LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAVQLNTTYYIHQLLGN 2927
Cdd:cd14089     86 FSRIQERADsaFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAILKLTDFGFAKETTTKKSLQTPCYT 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2928 PEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDsveeTCLNIC-----RL---DFSFPEDYFQGVSQKAKEFV 2999
Cdd:cd14089    166 PYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSN----HGLAISpgmkkRIrngQYEFPNPEWSNVSEEAKDLI 241
                          250       260
                   ....*....|....*....|..
gi 1907111721 3000 CFLLQEDPAKRPSAALALQEQW 3021
Cdd:cd14089    242 RGLLKTDPSERLTIEEVMNHPW 263
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
2774-2963 1.31e-23

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 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: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 102.79  E-value: 1.31e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQ-HPLLVSLLD-TFETPTSYVLVLEMADQGRLLD 2851
Cdd:cd13987      1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDFLREYNISLELSvHPHIIKTYDvAFETEDYYVFAQEYAPYGDLFS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2852 CVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILV-DQSLAKptIKLADFGDAVQLNTTyyIHQLLGNPEF 2930
Cdd:cd13987     81 IIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfDKDCRR--VKLCDFGLTRRVGST--VKRVSGTIPY 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1907111721 2931 AAPEI--------ILGNPVSltaDTWSVGVLTYVLLSGVSP 2963
Cdd:cd13987    157 TAPEVceakknegFVVDPSI---DVWAFGVLLFCCLTGNFP 194
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
2774-3010 4.26e-23

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 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: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 101.99  E-value: 4.26e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd05631      8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKgeamALNEKRILEKVNSRFVVSLAYAYETKDALCLVLTIMNGGDL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRA--HLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQLNTTYYIHQLLGN 2927
Cdd:cd05631     88 KFHIYNMGNPGFDEQRAifYAAELCCGLEDLQRERIVYRDLKPENILLDD---RGHIRISDLGLAVQIPEGETVRGRVGT 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2928 PEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQEDP 3007
Cdd:cd05631    165 VGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKREEVDRRVKEDQEEYSEKFSEDAKSICRMLLTKNP 244

                   ...
gi 1907111721 3008 AKR 3010
Cdd:cd05631    245 KER 247
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
2773-3023 4.47e-23

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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 AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 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: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 101.97  E-value: 4.47e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKR---------------------------DQVTHELGILQNLQHPLLV 2825
Cdd:cd14199      9 EIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLMRqagfprrppprgaraapegctqprgpiERVYQEIAILKKLDHPNVV 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2826 SLLDTFETPTS--YVLVLEMADQGRLLDcVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPT 2903
Cdd:cd14199     89 KLVEVLDDPSEdhLYMVFELVKQGPVME-VPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGED---GH 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2904 IKLADFG--------DAVQLNTtyyihqlLGNPEFAAPEII--LGNPVSLTA-DTWSVGVLTYVLLSGVSPFLDDSVEET 2972
Cdd:cd14199    165 IKIADFGvsnefegsDALLTNT-------VGTPAFMAPETLseTRKIFSGKAlDVWAMGVTLYCFVFGQCPFMDERILSL 237
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907111721 2973 CLNICRLDFSFPEDyfQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQ 3023
Cdd:cd14199    238 HSKIKTQPLEFPDQ--PDISDDLKDLLFRMLDKNPESRISVPEIKLHPWVT 286
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
2807-3014 5.26e-23

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 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: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 101.46  E-value: 5.26e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2807 DQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHL 2886
Cdd:cd06628     51 DALQREIALLRELQHENIVQYLGSSSDANHLNIFLEYVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHR 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2887 DLKPENILVDQslaKPTIKLADFG-----DAVQLNTTYYIHQ--LLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLS 2959
Cdd:cd06628    131 DIKGANILVDN---KGGIKISDFGiskklEANSLSTKNNGARpsLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLT 207
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907111721 2960 GVSPFLDDSVEETCLNICRLDF-SFPEDyfqgVSQKAKEFVCFLLQEDPAKRPSAA 3014
Cdd:cd06628    208 GTHPFPDCTQMQAIFKIGENASpTIPSN----ISSEARDFLEKTFEIDHNKRPTAD 259
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
2768-3011 5.47e-23

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: 100.96  E-value: 5.47e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVT---HELGILQNLQHPLLVSLLDTFETPTSYVLVLEMA 2844
Cdd:cd08220      2 YEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQaalNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 DQGRLLDCVVRWGS--LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlaKPTIKLADFGDAVQLNTTYYIH 2922
Cdd:cd08220     82 PGGTLFEYIQQRKGslLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKK--RTVVKIGDFGISKILSSKSKAY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2923 QLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFqgvSQKAKEFVCFL 3002
Cdd:cd08220    160 TVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFAPISDRY---SEELRHLILSM 236

                   ....*....
gi 1907111721 3003 LQEDPAKRP 3011
Cdd:cd08220    237 LHLDPNKRP 245
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
2774-3022 6.95e-23

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 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: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 101.22  E-value: 6.95e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELgilQNLQHPLLVSLLDTFET----PTSYVLVLEMADQGRL 2849
Cdd:cd14172     12 LGLGVNGKVLECFHRRTGQKCALKLLYDSPKARREVEHHW---RASGGPHIVHILDVYENmhhgKRCLLIIMECMEGGEL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWG--SLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAVQLNTTYYIHQLLGN 2927
Cdd:cd14172     89 FSRIQERGdqAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDAVLKLTDFGFAKETTVQNALQTPCYT 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2928 PEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRL----DFSFPEDYFQGVSQKAKEFVCFLL 3003
Cdd:cd14172    169 PYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISPGMKRRirmgQYGFPNPEWAEVSEEAKQLIRHLL 248
                          250
                   ....*....|....*....
gi 1907111721 3004 QEDPAKRPSAALALQEQWL 3022
Cdd:cd14172    249 KTDPTERMTITQFMNHPWI 267
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
2774-2965 7.31e-23

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: 101.76  E-value: 7.31e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATK---FVNKKLMK-RDQVTHELGILQNLQHPLLVSLLD----TFETPTSYVLVLEM-- 2843
Cdd:cd13989      1 LGSGGFGYVTLWKHQDTGEYVAIKkcrQELSPSDKnRERWCLEVQIMKKLNHPNVVSARDvppeLEKLSPNDLPLLAMey 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ---ADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAVQLNTTYY 2920
Cdd:cd13989     81 csgGDLRKVLNQPENCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRVIYKLIDLGYAKELDQGSL 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907111721 2921 IHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFL 2965
Cdd:cd13989    161 CTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPFL 205
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
2768-3014 1.20e-22

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK 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: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 100.51  E-value: 1.20e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNkkLMKR----DQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEM 2843
Cdd:cd06610      3 YELIEVIGSGATAVVYAAYCLPKKEKVAIKRID--LEKCqtsmDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQGRLLDCV---VRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQL----- 2915
Cdd:cd06610     81 LSGGSLLDIMkssYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGED---GSVKIADFGVSASLatggd 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2916 NTTYYIHQLLGNPEFAAPEII-LGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDF-SFPEDYFQGVSQ 2993
Cdd:cd06610    158 RTRKVRKTFVGTPCWMAPEVMeQVRGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNDPpSLETGADYKKYS 237
                          250       260
                   ....*....|....*....|..
gi 1907111721 2994 KA-KEFVCFLLQEDPAKRPSAA 3014
Cdd:cd06610    238 KSfRKMISLCLQKDPSKRPTAE 259
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
2768-3022 2.13e-22

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 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: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 99.26  E-value: 2.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKklmkrDQVThELGILQNLQHPL--------------LVSLLDTFET 2833
Cdd:cd14102      2 YQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVK-----ERVT-EWGTLNGVMVPLeivllkkvgsgfrgVIKLLDWYER 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2834 PTSYVLVLEMADQGR-LLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqsLAKPTIKLADFGDA 2912
Cdd:cd14102     76 PDGFLIVMERPEPVKdLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVD--LRTGELKLIDFGSG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2913 VQLNTTYYIhQLLGNPEFAAPEIILGNPV-SLTADTWSVGVLTYVLLSGVSPFLDDsvEEtclnICRLDFSFPedyfQGV 2991
Cdd:cd14102    154 ALLKDTVYT-DFDGTRVYSPPEWIRYHRYhGRSATVWSLGVLLYDMVCGDIPFEQD--EE----ILRGRLYFR----RRV 222
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1907111721 2992 SQKAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14102    223 SPECQQLIKWCLSLRPSDRPTLEQIFDHPWM 253
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
2768-3018 2.55e-22

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. 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 CDK4/6-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: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 100.04  E-value: 2.55e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKL--------MKRdqvthELGILQNLQ---HPLLVSLLDTFETP-- 2834
Cdd:cd07838      1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRVPLseegiplsTIR-----EIALLKQLEsfeHPNVVRLLDVCHGPrt 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2835 ---TSYVLVLEMADQ--GRLLDCVVRWGsLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADF 2909
Cdd:cd07838     76 dreLKLTLVFEHVDQdlATYLDKCPKPG-LPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDG---QVKLADF 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2910 GdavqLNTTYYIHQLLgNPE-----FAAPEIILGNPVSLTADTWSVGVLTYVLLS------GVS--------------PF 2964
Cdd:cd07838    152 G----LARIYSFEMAL-TSVvvtlwYRAPEVLLQSSYATPVDMWSVGCIFAELFNrrplfrGSSeadqlgkifdviglPS 226
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907111721 2965 LDDSVEETCLNICRLDFSFP---EDYFQGVSQKAKEFVCFLLQEDPAKRPSAALALQ 3018
Cdd:cd07838    227 EEEWPRNSALPRSSFPSYTPrpfKSFVPEIDEEGLDLLKKMLTFNPHKRISAFEALQ 283
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
2807-3022 2.60e-22

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


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 99.30  E-value: 2.60e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2807 DQVTHELGILQNLQHPLLVSLLDtFETPTSYVLVL----------EMADQGRLLDCVVrwgsltegkVRAHLGEVLEAVR 2876
Cdd:cd06626     44 KEIADEMKVLEGLDHPNLVRYYG-VEVHREEVYIFmeycqegtleELLRHGRILDEAV---------IRVYTLQLLEGLA 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2877 YLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQL--NTTYYIH----QLLGNPEFAAPEIILGNPVS---LTADT 2947
Cdd:cd06626    114 YLHENGIVHRDIKPANIFLDSN---GLIKLGDFGSAVKLknNTTTMAPgevnSLVGTPAYMAPEVITGNKGEghgRAADI 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2948 WSVGVLTYVLLSGVSP--FLDdsveetclNICRLDF--------SFPEDyfQGVSQKAKEFVCFLLQEDPAKRPSAALAL 3017
Cdd:cd06626    191 WSLGCVVLEMATGKRPwsELD--------NEWAIMYhvgmghkpPIPDS--LQLSPEGKDFLSRCLESDPKKRPTASELL 260

                   ....*
gi 1907111721 3018 QEQWL 3022
Cdd:cd06626    261 DHPFI 265
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
2768-3022 4.18e-22

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. 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 CDK1 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: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 99.29  E-value: 4.18e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVnkKLMKRDQ-----VTHELGILQNLQHPLLVSLLDTFETPTSYVLVLE 2842
Cdd:cd07835      1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKI--RLETEDEgvpstAIREISLLKELNHPNIVRLLDVVHSENKLYLVFE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 MADQG--RLLDCVvRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDA----VQLN 2916
Cdd:cd07835     79 FLDLDlkKYMDSS-PLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDT---EGALKLADFGLArafgVPVR 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2917 TtyYIHQLLgNPEFAAPEIILGNPVSLTA-DTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRL---------------- 2979
Cdd:cd07835    155 T--YTHEVV-TLWYRAPEILLGSKHYSTPvDIWSVGCIFAEMVTRRPLFPGDSEIDQLFRIFRTlgtpdedvwpgvtslp 231
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907111721 2980 DF--SFP-------EDYFQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd07835    232 DYkpTFPkwarqdlSKVVPSLDEDGLDLLSQMLVYDPAKRISAKAALQHPYF 283
I-set pfam07679
Immunoglobulin I-set domain;
2657-2748 4.44e-22

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 92.71  E-value: 4.44e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2657 PEFVIPLSEVTCETGETVVFRCRVCGRPKASITWKGPEHnTLNNDDHYSISYSDiGEATLKIIGVSTEDDGIYTCIAVND 2736
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQ-PLRSSDRFKVTYEG-GTYTLTISNVQPDDSGKYTCVATNS 78
                           90
                   ....*....|..
gi 1907111721 2737 MGSASSSASLRV 2748
Cdd:pfam07679   79 AGEAEASAELTV 90
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
2765-3048 4.87e-22

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 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: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 98.98  E-value: 4.87e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2765 DAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRD--QVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLE 2842
Cdd:cd06642      3 EELFTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAEDEieDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIME 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 MADQGRLLDcVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQL-NTTYYI 2921
Cdd:cd06642     83 YLGGGSALD-LLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSE---QGDVKLADFGVAGQLtDTQIKR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2922 HQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDdsveetcLNICRLDFSFPED---YFQGVSQKA-KE 2997
Cdd:cd06642    159 NTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSD-------LHPMRVLFLIPKNsppTLEGQHSKPfKE 231
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907111721 2998 FVCFLLQEDPAKRPSAALALQEQWLQAGNGSgkgtgvldTSRLTSFIERRK 3048
Cdd:cd06642    232 FVEACLNKDPRFRPTAKELLKHKFITRYTKK--------TSFLTELIDRYK 274
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
37-172 5.81e-22

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 95.06  E-value: 5.81e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721    37 LKEKVAYLSGGR--DKRGGPILTFPARS--NHDRIRQEDLRRLISYLACIPSEE---VCKRGFTVIVDMRGSK-----WD 104
Cdd:smart00516    2 LELLKAYIPGGRgyDKDGRPVLIERAGRfdLKSVTLEELLRYLVYVLEKILQEEkktGGIEGFTVIFDLKGLSmsnpdLS 81
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907111721   105 SIKPLLKILQESFPCCIHIALIIKPDNFWQ---KQRTNFGSSKFEFETNMVSL---EGLTKVVDPSQLTPEFDG 172
Cdd:smart00516   82 VLRKILKILQDHYPERLGKVYIINPPWFFRvlwKIIKPFLDEKTREKIRFVGNdskEELLEYIDKEQLPEELGG 155
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
2774-3010 8.63e-22

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-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: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 99.34  E-value: 8.63e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRF---AVVKkcdQKGTKRAVATKFVNK-KLMKRDQVT---HELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQ 2846
Cdd:cd05597      9 IGRGAFgevAVVK---LKSTEKVYAMKILNKwEMLKRAETAcfrEERDVLVNGDRRWITKLHYAFQDENYLYLVMDYYCG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2847 GRLLDCVVRWGS-LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTYYIHQL- 2924
Cdd:cd05597     86 GDLLTLLSKFEDrLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRN---GHIRLADFGSCLKLREDGTVQSSv 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2925 -LGNPEFAAPEIILGNP-----VSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLD--FSFPeDYFQGVSQKAK 2996
Cdd:cd05597    163 aVGTPDYISPEILQAMEdgkgrYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKehFSFP-DDEDDVSEEAK 241
                          250
                   ....*....|....
gi 1907111721 2997 EFVCFLLQeDPAKR 3010
Cdd:cd05597    242 DLIRRLIC-SRERR 254
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
2768-3021 8.68e-22

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. 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 CDK2/3 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: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 98.35  E-value: 8.68e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKR---DQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMA 2844
Cdd:cd07860      2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEgvpSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 DQG--RLLDCVVRWGsLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAkptIKLADFGDA----VQLNTt 2918
Cdd:cd07860     82 HQDlkKFMDASALTG-IPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGA---IKLADFGLArafgVPVRT- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2919 yYIHQLLgNPEFAAPEIILGNPVSLTA-DTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRL----------------DF 2981
Cdd:cd07860    157 -YTHEVV-TLWYRAPEILLGCKYYSTAvDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTlgtpdevvwpgvtsmpDY 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1907111721 2982 --SFP-------EDYFQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQW 3021
Cdd:cd07860    235 kpSFPkwarqdfSKVVPPLDEDGRDLLSQMLHYDPNKRISAKAALAHPF 283
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
2768-3002 1.16e-21

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK 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: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 99.37  E-value: 1.16e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNK-KLMKRDQVT---HELGILQNLQHPLLVSLLDTFETPTSYVLVLEM 2843
Cdd:cd05596     28 FDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKfEMIKRSDSAffwEERDIMAHANSEWIVQLHYAFQDDKYLYMVMDY 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQGRLLDCVVRWgSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQLNTTYYIH- 2922
Cdd:cd05596    108 MPGGDLVNLMSNY-DVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLD---ASGHLKLADFGTCMKMDKDGLVRs 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2923 -QLLGNPEFAAPEIILG----NPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNIcrLD----FSFPEDyfQGVSQ 2993
Cdd:cd05596    184 dTAVGTPDYISPEVLKSqggdGVYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKI--MNhknsLQFPDD--VEISK 259
                          250
                   ....*....|
gi 1907111721 2994 KAKEFVC-FL 3002
Cdd:cd05596    260 DAKSLICaFL 269
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
2768-3010 1.27e-21

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-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: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 97.42  E-value: 1.27e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKK--------LMKRDQVTHELGILQNL-QHPLLVSLLDTFETPTSYV 2838
Cdd:cd13993      2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSgpnskdgnDFQKLPQLREIDLHRRVsRHPNIITLHDVFETEVAIY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2839 LVLEMADQGRLLDCVV--RWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAkpTIKLADFGDAVQLN 2916
Cdd:cd13993     82 IVLEYCPNGDLFEAITenRIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEG--TVKLCDFGLATTEK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2917 TTYYIHqlLGNPEFAAPEIILGNPVSLT------ADTWSVGVLTYVLLSGVSPFLDDSVEEtclNICRLDFSFPEDYFQG 2990
Cdd:cd13993    160 ISMDFG--VGSEFYMAPECFDEVGRSLKgypcaaGDIWSLGIILLNLTFGRNPWKIASESD---PIFYDYYLNSPNLFDV 234
                          250       260
                   ....*....|....*....|...
gi 1907111721 2991 VSQKAKEFVCFL---LQEDPAKR 3010
Cdd:cd13993    235 ILPMSDDFYNLLrqiFTVNPNNR 257
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
2766-3024 1.45e-21

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 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: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 97.55  E-value: 1.45e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2766 AFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRD--QVTHELGILQNLQH---PLLVSLLDTFETPTSYVLV 2840
Cdd:cd06917      1 SLYRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLDTDDDDvsDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSLWII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2841 LEMADQGRLlDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTYY 2920
Cdd:cd06917     81 MDYCEGGSI-RTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNT---GNVKLCDFGVAASLNQNSS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2921 IHQ-LLGNPEFAAPEIIL-GNPVSLTADTWSVGVLTYVLLSGVSPFLD-DSVEETCLNICRLDFSFPEDYFqgvSQKAKE 2997
Cdd:cd06917    157 KRStFVGTPYWMAPEVITeGKYYDTKADIWSLGITTYEMATGNPPYSDvDALRAVMLIPKSKPPRLEGNGY---SPLLKE 233
                          250       260
                   ....*....|....*....|....*..
gi 1907111721 2998 FVCFLLQEDPAKRPSAALALQEQWLQA 3024
Cdd:cd06917    234 FVAACLDEEPKDRLSADELLKSKWIKQ 260
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
2771-3024 1.61e-21

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. 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: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 97.03  E-value: 1.61e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2771 VAELGRGRFAVVKKCDQKGTKRAVATKFV--NKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGR 2848
Cdd:cd06605      6 LGELGEGNGGVVSKVRHRPSGQIMAVKVIrlEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMDGGS 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVVRWGSLTE---GKV-RAhlgeVLEAVRYLHNCR-IAHLDLKPENILVDqslAKPTIKLADFGDAVQL-------- 2915
Cdd:cd06605     86 LDKILKEVGRIPErilGKIaVA----VVKGLIYLHEKHkIIHRDVKPSNILVN---SRGQVKLCDFGVSGQLvdslaktf 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2916 -NTTYYIhqllgnpefaAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFlDDSVEETCLNI-----CRLDFS---FPED 2986
Cdd:cd06605    159 vGTRSYM----------APERISGGKYTVKSDIWSLGLSLVELATGRFPY-PPPNAKPSMMIfellsYIVDEPpplLPSG 227
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1907111721 2987 YFqgvSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQA 3024
Cdd:cd06605    228 KF---SPDFQDFVSQCLQKDPTERPSYKELMEHPFIKR 262
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
2761-2999 1.94e-21

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta 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. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 99.70  E-value: 1.94e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2761 KDNFDAfyseVAELGRGRFAVVKKCDQKGTKRAVATKFVNK-KLMKRDQVT---HELGILQNLQHPLLVSLLDTFETPTS 2836
Cdd:cd05624     71 RDDFEI----IKVIGRGAFGEVAVVKMKNTERIYAMKILNKwEMLKRAETAcfrEERNVLVNGDCQWITTLHYAFQDENY 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2837 YVLVLEMADQGRLLDCVVRW-GSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQL 2915
Cdd:cd05624    147 LYLVMDYYVGGDLLTLLSKFeDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMN---GHIRLADFGSCLKM 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2916 NTTYYIHQ--LLGNPEFAAPEIILGNPVSL-----TADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLD--FSFPEd 2986
Cdd:cd05624    224 NDDGTVQSsvAVGTPDYISPEILQAMEDGMgkygpECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEerFQFPS- 302
                          250
                   ....*....|...
gi 1907111721 2987 YFQGVSQKAKEFV 2999
Cdd:cd05624    303 HVTDVSEEAKDLI 315
PH_puratrophin-1 cd13242
Puratrophin-1 pleckstrin homology (PH) domain; Puratrophin-1 (also called Purkinje cell ...
1430-1566 2.08e-21

Puratrophin-1 pleckstrin homology (PH) domain; Puratrophin-1 (also called Purkinje cell atrophy-associated protein 1 or PLEKHG4/Pleckstrin homology domain-containing family G member 4) contains a spectrin repeat, a RhoGEF (DH) domain, and a PH domain. It is thought to function in intracellular signaling and cytoskeleton dynamics at the Golgi. Puratrophin-1 is expressed in kidney, Leydig cells in the testis, epithelial cells in the prostate gland and Langerhans islet in the pancreas. A single nucleotide substitution in the puratrophin-1 gene were once thought to result in autosomal dominant cerebellar ataxia (ADCA), but now it has been demonstrated that this ataxia is a result of defects in the BEAN gene. Puratrophin contains a domain architecture similar to that of Dbl family members Dbs and Trio. Dbs is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a RhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Trio is a multidomain signaling protein that contains two RhoGEF(DH)-PH domains in tandem. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270062  Cd Length: 136  Bit Score: 92.74  E-value: 2.08e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1430 KRANDAMHLSMLEGFDENIESQGELILQESFQVWDPktliRKGRERHLFLFEMSLVFSKEVKDSSGRSKYLYKSKLFTSE 1509
Cdd:cd13242      5 RHGNDLLAMDSIRGCDVNLKEQGQLLRQDEFLVWQG----RKKCLRHVFLFEDLILFSKPKKTPGGKDVYIYKHSIKTSD 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907111721 1510 LGVTEHVEGDPCKFALWVgRTPTSDNKIVLKASSIENKQDWIKHIREVIQERTVHLR 1566
Cdd:cd13242     81 IGLTENVGDSGLKFEIWF-RRRKARDTYILQATSPEIKQAWTSDIAKLLWKQAIRNR 136
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
2763-2963 2.15e-21

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK 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: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 97.02  E-value: 2.15e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2763 NFDAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKR-DQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVL 2841
Cdd:cd06643      2 NPEDFWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKSEEElEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2842 EMAdQGRLLDCVV----RwgSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFG-DAVQLN 2916
Cdd:cd06643     82 EFC-AGGAVDAVMleleR--PLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFT---LDGDIKLADFGvSAKNTR 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907111721 2917 TTYYIHQLLGNPEFAAPEIIL-----GNPVSLTADTWSVGVlTYVLLSGVSP 2963
Cdd:cd06643    156 TLQRRDSFIGTPYWMAPEVVMcetskDRPYDYKADVWSLGV-TLIEMAQIEP 206
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
2773-3022 2.30e-21

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK 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: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 96.36  E-value: 2.30e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRAVATKFVN-KKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLD 2851
Cdd:cd06648     14 KIGEGSTGIVCIATDKSTGRQVAVKKMDlRKQQRRELLFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGGALTD 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2852 cVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNT-TYYIHQLLGNPEF 2930
Cdd:cd06648     94 -IVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSD---GRVKLSDFGFCAQVSKeVPRRKSLVGTPYW 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2931 AAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQgVSQKAKEFVCFLLQEDPAKR 3010
Cdd:cd06648    170 MAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEPPKLKNLHK-VSPRLRSFLDRMLVRDPAQR 248
                          250
                   ....*....|..
gi 1907111721 3011 PSAALALQEQWL 3022
Cdd:cd06648    249 ATAAELLNHPFL 260
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
2771-3026 2.37e-21

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 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: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 97.41  E-value: 2.37e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2771 VAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKR-DQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd06644     17 IGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEElEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEFCPGGAV 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWG-SLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFG-DAVQLNTTYYIHQLLGN 2927
Cdd:cd06644     97 DAIMLELDrGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLD---GDIKLADFGvSAKNVKTLQRRDSFIGT 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2928 PEFAAPEIIL-----GNPVSLTADTWSVGVlTYVLLSGVSPFLDDsveetcLNICRLDFSFPEDYFQGVSQKAK---EFV 2999
Cdd:cd06644    174 PYWMAPEVVMcetmkDTPYDYKADIWSLGI-TLIEMAQIEPPHHE------LNPMRVLLKIAKSEPPTLSQPSKwsmEFR 246
                          250       260       270
                   ....*....|....*....|....*....|
gi 1907111721 3000 CFL---LQEDPAKRPSAALALQEQWLQAGN 3026
Cdd:cd06644    247 DFLktaLDKHPETRPSAAQLLEHPFVSSVT 276
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
2768-3010 3.04e-21

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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 AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 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: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 96.56  E-value: 3.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKK-LMKR--------------------------DQVTHELGILQNLQ 2820
Cdd:cd14200      2 YKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKkLLKQygfprrppprgskaaqgeqakplaplERVYQEIAILKKLD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2821 HPLLVSLLDTFETPT--SYVLVLEMADQGRLLDcVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQS 2898
Cdd:cd14200     82 HVNIVKLIEVLDDPAedNLYMVFDLLRKGPVME-VPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDD 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2899 lakPTIKLADFGDAVQLN-TTYYIHQLLGNPEFAAPEIILGNPVSLTA---DTWSVGVLTYVLLSGVSPFLDDSVEETCL 2974
Cdd:cd14200    161 ---GHVKIADFGVSNQFEgNDALLSSTAGTPAFMAPETLSDSGQSFSGkalDVWAMGVTLYCFVYGKCPFIDEFILALHN 237
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1907111721 2975 NICRLDFSFPEDyfQGVSQKAKEFVCFLLQEDPAKR 3010
Cdd:cd14200    238 KIKNKPVEFPEE--PEISEELKDLILKMLDKNPETR 271
PH_Dbs cd01227
DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming ...
1443-1558 3.25e-21

DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming sequence-like protein 2) is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a rhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269934 [Multi-domain]  Cd Length: 126  Bit Score: 91.49  E-value: 3.25e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1443 GFDENIESQGELILQESFQVW------DPKTLIR-KGRERHLFLFEMSLVFSKEVKDSSGRSKYLYKSKLFTSELGVTEH 1515
Cdd:cd01227      4 GYDGNLGDLGKLLMQGSFNVWtehkkgHTKKLARfKPMQRHIFLYEKAVLFCKKRGENGEAPSYSYKNSLNTTAVGLTEN 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907111721 1516 VEGDPCKFALWV-GRTPTsdnkIVLKASSIENKQDWIKHIREVI 1558
Cdd:cd01227     84 VKGDTKKFEIWLnGREEV----FIIQAPTPEIKAAWVKAIRQVL 123
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
2774-3010 3.69e-21

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 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: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 96.49  E-value: 3.69e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd05608      9 LGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKgyegAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTIMNGGDL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGS----LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQL-----NTTYY 2920
Cdd:cd05608     89 RYHIYNVDEenpgFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDD---GNVRISDLGLAVELkdgqtKTKGY 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2921 IhqllGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPF--LDDSVE--ETCLNICRLDFSFPEDYfqgvSQKAK 2996
Cdd:cd05608    166 A----GTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFraRGEKVEnkELKQRILNDSVTYSEKF----SPASK 237
                          250
                   ....*....|....
gi 1907111721 2997 EFVCFLLQEDPAKR 3010
Cdd:cd05608    238 SICEALLAKDPEKR 251
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
2774-2965 4.02e-21

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical 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 classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta 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: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 96.57  E-value: 4.02e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKL--MKRDQVTHELGILQNLQHPLLVSLLDTFE-----TPTSY-VLVLEMAD 2845
Cdd:cd14038      2 LGTGGFGNVLRWINQETGEQVAIKQCRQELspKNRERWCLEIQIMKRLNHPNVVAARDVPEglqklAPNDLpLLAMEYCQ 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2846 QGRL---LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAVQLNTTYYIH 2922
Cdd:cd14038     82 GGDLrkyLNQFENCCGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRLIHKIIDLGYAKELDQGSLCT 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1907111721 2923 QLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFL 2965
Cdd:cd14038    162 SFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFL 204
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
2774-3010 4.12e-21

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC 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: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 97.08  E-value: 4.12e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQ------VTHELGILQNlQHPLLVSLLDTFETPTSYVLVLEMADQG 2847
Cdd:cd05587      4 LGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDDdvectmVEKRVLALSG-KPPFLTQLHSCFQTMDRLYFVMEYVNGG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2848 RLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFG----DAVQLNTTyyiHQ 2923
Cdd:cd05587     83 DLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAE---GHIKIADFGmckeGIFGGKTT---RT 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2924 LLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPedyfQGVSQKAKEFVCFLL 3003
Cdd:cd05587    157 FCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYP----KSLSKEAVSICKGLL 232

                   ....*..
gi 1907111721 3004 QEDPAKR 3010
Cdd:cd05587    233 TKHPAKR 239
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
2774-3012 4.90e-21

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 95.81  E-value: 4.90e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVV--KKCDQKGTKRAVATKFVNKK----LMKRdqvthELGILQNLQ-HPLLVSLLDTFETPTSY----VLVL- 2841
Cdd:cd14037     11 LAEGGFAHVylVKTSNGGNRAALKRVYVNDEhdlnVCKR-----EIEIMKRLSgHKNIVGYIDSSANRSGNgvyeVLLLm 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2842 EMADQGRLLDCV---VRWGsLTEGKVRAHLGEVLEAVRYLHNCR--IAHLDLKPENILVDqslAKPTIKLADFGDA---- 2912
Cdd:cd14037     86 EYCKGGGVIDLMnqrLQTG-LTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLIS---DSGNYKLCDFGSAttki 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2913 ---------------VQLNTTyyihqllgnPEFAAPEII---LGNPVSLTADTWSVGVLTYVLLSGVSPFlddsvEETC- 2973
Cdd:cd14037    162 lppqtkqgvtyveedIKKYTT---------LQYRAPEMIdlyRGKPITEKSDIWALGCLLYKLCFYTTPF-----EESGq 227
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1907111721 2974 LNICRLDFSFPEdyFQGVSQKAKEFVCFLLQEDPAKRPS 3012
Cdd:cd14037    228 LAILNGNFTFPD--NSRYSKRLHKLIRYMLEEDPEKRPN 264
PH_puratrophin-1 cd13242
Puratrophin-1 pleckstrin homology (PH) domain; Puratrophin-1 (also called Purkinje cell ...
2111-2241 5.26e-21

Puratrophin-1 pleckstrin homology (PH) domain; Puratrophin-1 (also called Purkinje cell atrophy-associated protein 1 or PLEKHG4/Pleckstrin homology domain-containing family G member 4) contains a spectrin repeat, a RhoGEF (DH) domain, and a PH domain. It is thought to function in intracellular signaling and cytoskeleton dynamics at the Golgi. Puratrophin-1 is expressed in kidney, Leydig cells in the testis, epithelial cells in the prostate gland and Langerhans islet in the pancreas. A single nucleotide substitution in the puratrophin-1 gene were once thought to result in autosomal dominant cerebellar ataxia (ADCA), but now it has been demonstrated that this ataxia is a result of defects in the BEAN gene. Puratrophin contains a domain architecture similar to that of Dbl family members Dbs and Trio. Dbs is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a RhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Trio is a multidomain signaling protein that contains two RhoGEF(DH)-PH domains in tandem. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270062  Cd Length: 136  Bit Score: 91.58  E-value: 5.26e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2111 NDMMNVGRLQGFDGKIVAQGKLLLQDTFLVTDQDagllpRCKERRVFLFEQIVIFSEPLDKKKGFSMpgFLFKNSIKVSC 2190
Cdd:cd13242      8 NDLLAMDSIRGCDVNLKEQGQLLRQDEFLVWQGR-----KKCLRHVFLFEDLILFSKPKKTPGGKDV--YIYKHSIKTSD 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907111721 2191 LCLEENVESDPCKFALTSRTGDAVETFVLHSSSPSVRQTWIHEINQILENQ 2241
Cdd:cd13242     81 IGLTENVGDSGLKFEIWFRRRKARDTYILQATSPEIKQAWTSDIAKLLWKQ 131
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
2770-3024 5.38e-21

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: 95.95  E-value: 5.38e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2770 EVAELGRGRFAVVKKCDQKGTKRAVATKFV----NKKLMKrdQVTHELGILQNLQHPLLVSLLDTF--ETPTSYVLVLEM 2843
Cdd:cd06621      5 ELSSLGEGAGGSVTKCRLRNTKTIFALKTIttdpNPDVQK--QILRELEINKSCASPYIVKYYGAFldEQDSSIGIAMEY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQG---RLLDCVVRWGSLTEGKVRAHLGE-VLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQL---- 2915
Cdd:cd06621     83 CEGGsldSIYKKVKKKGGRIGEKVLGKIAEsVLKGLSYLHSRKIIHRDIKPSNILLTR---KGQVKLCDFGVSGELvnsl 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2916 -----NTTYYIhqllgnpefaAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVE-----ETCLNICRL-DFSFP 2984
Cdd:cd06621    160 agtftGTSYYM----------APERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPplgpiELLSYIVNMpNPELK 229
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1907111721 2985 EDYFQGV--SQKAKEFVCFLLQEDPAKRPSAALALQEQWLQA 3024
Cdd:cd06621    230 DEPENGIkwSESFKDFIEKCLEKDGTRRPGPWQMLAHPWIKA 271
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
2768-3017 5.59e-21

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. 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 CDK1 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: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 95.95  E-value: 5.59e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVnkKLMKRDQ-----VTHELGILQNLQHPLLVSLLDTFETPTSYVLVLE 2842
Cdd:cd07861      2 YTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKI--RLESEEEgvpstAIREISLLKELQHPNIVCLEDVLMQENRLYLVFE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 M--ADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFG--DAVQLNTT 2918
Cdd:cd07861     80 FlsMDLKKYLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDN---KGVIKLADFGlaRAFGIPVR 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2919 YYIHQLLgNPEFAAPEIILGNP-VSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRL----------------DF 2981
Cdd:cd07861    157 VYTHEVV-TLWYRAPEVLLGSPrYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRIlgtptediwpgvtslpDY 235
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1907111721 2982 --SFPE-------DYFQGVSQKAKEFVCFLLQEDPAKRPSAALAL 3017
Cdd:cd07861    236 knTFPKwkkgslrTAVKNLDEDGLDLLEKMLIYDPAKRISAKKAL 280
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
2768-3005 7.02e-21

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 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: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 97.76  E-value: 7.02e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNK-KLMKRDQVT---HELGILQNLQHPLLVSLLDTFETPTSYVLVLEM 2843
Cdd:cd05621     54 YDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKfEMIKRSDSAffwEERDIMAFANSPWVVQLFCAFQDDKYLYMVMEY 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQGRLLDCVVRWgSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTYYIH- 2922
Cdd:cd05621    134 MPGGDLVNLMSNY-DVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKY---GHLKLADFGTCMKMDETGMVHc 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2923 -QLLGNPEFAAPEIILGNP----VSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNIC--RLDFSFPEDYfqGVSQKA 2995
Cdd:cd05621    210 dTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMdhKNSLNFPDDV--EISKHA 287
                          250
                   ....*....|
gi 1907111721 2996 KEFVCFLLQE 3005
Cdd:cd05621    288 KNLICAFLTD 297
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
2777-3014 7.24e-21

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 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: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 96.53  E-value: 7.24e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2777 GRFAVVKKCDQKGTKRAVATKFVNK-KLMKRDQVTH----ELGILQNL-QHPLLVSLLDTFETPTSYVLVLEMADQGRLL 2850
Cdd:cd05614     14 GKVFLVRKVSGHDANKLYAMKVLRKaALVQKAKTVEhtrtERNVLEHVrQSPFLVTLHYAFQTDAKLHLILDYVSGGELF 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2851 DCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQLNT-----TYyihQLL 2925
Cdd:cd05614     94 THLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLD---SEGHVVLTDFGLSKEFLTeekerTY---SFC 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2926 GNPEFAAPEIILGNPVSLTA-DTWSVGVLTYVLLSGVSPFL----DDSVEETCLNICRLDFSFPEDyfqgVSQKAKEFVC 3000
Cdd:cd05614    168 GTIEYMAPEIIRGKSGHGKAvDWWSLGILMFELLTGASPFTlegeKNTQSEVSRRILKCDPPFPSF----IGPVARDLLQ 243
                          250
                   ....*....|....
gi 1907111721 3001 FLLQEDPAKRPSAA 3014
Cdd:cd05614    244 KLLCKDPKKRLGAG 257
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
2768-3005 8.52e-21

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 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: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 97.77  E-value: 8.52e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNK-KLMKRDQVT---HELGILQNLQHPLLVSLLDTFETPTSYVLVLEM 2843
Cdd:cd05622     75 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfEMIKRSDSAffwEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQGRLLDCVVRWgSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTYYIH- 2922
Cdd:cd05622    155 MPGGDLVNLMSNY-DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKS---GHLKLADFGTCMKMNKEGMVRc 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2923 -QLLGNPEFAAPEIILGNP----VSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNIC--RLDFSFPEDyfQGVSQKA 2995
Cdd:cd05622    231 dTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhKNSLTFPDD--NDISKEA 308
                          250
                   ....*....|
gi 1907111721 2996 KEFVCFLLQE 3005
Cdd:cd05622    309 KNLICAFLTD 318
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
2774-3022 9.84e-21

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: 94.31  E-value: 9.84e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVN----KKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd14188      9 LGKGGFAKCYEMTDLTTNKVYAAKIIPhsrvSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSM 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQLNTTYYIHQLL-GNP 2928
Cdd:cd14188     89 AHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENM---ELKVGDFGLAARLEPLEHRRRTIcGTP 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2929 EFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPedyfQGVSQKAKEFVCFLLQEDPA 3008
Cdd:cd14188    166 NYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLP----SSLLAPAKHLIASMLSKNPE 241
                          250
                   ....*....|....
gi 1907111721 3009 KRPSAALALQEQWL 3022
Cdd:cd14188    242 DRPSLDEIIRHDFF 255
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
2820-3022 1.12e-20

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 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: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 95.49  E-value: 1.12e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2820 QHPLLVSLLDTFE----TPTSYVLVLEMADQGRLLDCVVRWG--SLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENI 2893
Cdd:cd14170     53 QCPHIVRIVDVYEnlyaGRKCLLIVMECLDGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENL 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2894 LVDQSLAKPTIKLADFGDAVQLNTTYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDD---SVE 2970
Cdd:cd14170    133 LYTSKRPNAILKLTDFGFAKETTSHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNhglAIS 212
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907111721 2971 ETCLNICRL-DFSFPEDYFQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14170    213 PGMKTRIRMgQYEFPNPEWSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWI 265
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
2768-3014 1.30e-20

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like 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: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 93.99  E-value: 1.30e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKL---MKRDQVTHELGILQNL-QHPLLVSLLDTFETPTSYVLVLEM 2843
Cdd:cd13997      2 FHELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKKPFrgpKERARALREVEAHAALgQHPNIVRYYSSWEEGGHLYIQMEL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQGRLLDCVVRWG---SLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQLNTTYY 2920
Cdd:cd13997     82 CENGSLQDALEELSpisKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISN---KGTCKIGDFGLATRLETSGD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2921 IHQllGNPEFAAPEIILGNPVSLT-ADTWSVGVLTYVLLSGvSPFLDDSveETCLNICRLDFSFPEDyfQGVSQKAKEFV 2999
Cdd:cd13997    159 VEE--GDSRYLAPELLNENYTHLPkADIFSLGVTVYEAATG-EPLPRNG--QQWQQLRQGKLPLPPG--LVLSQELTRLL 231
                          250
                   ....*....|....*
gi 1907111721 3000 CFLLQEDPAKRPSAA 3014
Cdd:cd13997    232 KVMLDPDPTRRPTAD 246
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
2821-3010 1.66e-20

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 94.15  E-value: 1.66e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2821 HPLLVSLLDTFETPTSYVLVLEMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslA 2900
Cdd:PHA03390    68 NPNFIKLYYSVTTLKGHVLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDR--A 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2901 KPTIKLADFGDAVQLNT--TYYihqllGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFlDDSVEEtCLNICR 2978
Cdd:PHA03390   146 KDRIYLCDYGLCKIIGTpsCYD-----GTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPF-KEDEDE-ELDLES 218
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1907111721 2979 L------DFSFPEDyfqgVSQKAKEFVCFLLQEDPAKR 3010
Cdd:PHA03390   219 LlkrqqkKLPFIKN----VSKNANDFVQSMLKYNINYR 252
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
2768-3018 2.25e-20

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. 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 CDKL2/3 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: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 94.03  E-value: 2.25e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATK---------FVNKKLMKrdqvthELGILQNLQHPLLVSLLDTFETPTSYV 2838
Cdd:cd07846      3 YENLGLVGEGSYGMVMKCRHKETGQIVAIKkfleseddkMVKKIAMR------EIKMLKQLRHENLVNLIEVFRRKKRWY 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2839 LVLEMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTT 2918
Cdd:cd07846     77 LVFEFVDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQS---GVVKLCDFGFARTLAAP 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2919 YYIH-QLLGNPEFAAPEIILGNPVSLTA-DTWSVGVLTYVLLSGVSPFLDDS-VEE-----TCL-NIC-RLDFSFPED-Y 2987
Cdd:cd07846    154 GEVYtDYVATRWYRAPELLVGDTKYGKAvDVWAVGCLVTEMLTGEPLFPGDSdIDQlyhiiKCLgNLIpRHQELFQKNpL 233
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1907111721 2988 FQGV------------------SQKAKEFVCFLLQEDPAKRPSAALALQ 3018
Cdd:cd07846    234 FAGVrlpevkeveplerrypklSGVVIDLAKKCLHIDPDKRPSCSELLH 282
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
2768-3023 2.30e-20

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, 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. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK 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: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 93.45  E-value: 2.30e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVN-KKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQ 2846
Cdd:cd06647      9 YTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2847 GRLLDcVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTYYIHQ-LL 2925
Cdd:cd06647     89 GSLTD-VVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMD---GSVKLTDFGFCAQITPEQSKRStMV 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2926 GNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNIC---RLDFSFPEDyfqgVSQKAKEFVCFL 3002
Cdd:cd06647    165 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAtngTPELQNPEK----LSAIFRDFLNRC 240
                          250       260
                   ....*....|....*....|.
gi 1907111721 3003 LQEDPAKRPSAALALQEQWLQ 3023
Cdd:cd06647    241 LEMDVEKRGSAKELLQHPFLK 261
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
2762-3022 4.80e-20

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK 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: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 94.17  E-value: 4.80e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2762 DNFDAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVnKKLMK-RDQVTHELGILQNLQH------PLLVSLLDTFETP 2834
Cdd:cd14134      8 DLLTNRYKILRLLGEGTFGKVLECWDRKRKRYVAVKII-RNVEKyREAAKIEIDVLETLAEkdpngkSHCVQLRDWFDYR 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2835 TSYVLVLEMADQGrLLD--CVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQS-------------- 2898
Cdd:cd14134     87 GHMCIVFELLGPS-LYDflKKNNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDSdyvkvynpkkkrqi 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2899 --LAKPTIKLADFGDAV--------QLNTTYYihqllgnpefAAPEIILGNPVSLTADTWSVGVLTYVLLSGVS------ 2962
Cdd:cd14134    166 rvPKSTDIKLIDFGSATfddeyhssIVSTRHY----------RAPEVILGLGWSYPCDVWSIGCILVELYTGELlfqthd 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2963 -------------PFLDDSVEETCLNICRLDFS-----FPED----------------YFQGVSQKAKEFVCF---LLQE 3005
Cdd:cd14134    236 nlehlammerilgPLPKRMIRRAKKGAKYFYFYhgrldWPEGsssgrsikrvckplkrLMLLVDPEHRLLFDLirkMLEY 315
                          330
                   ....*....|....*..
gi 1907111721 3006 DPAKRPSAALALQEQWL 3022
Cdd:cd14134    316 DPSKRITAKEALKHPFF 332
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
2768-3013 5.84e-20

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 94.18  E-value: 5.84e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNL----QHPLLVSLLDTFETPTSYVLVLEM 2843
Cdd:cd05610      6 FVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMVHQVQAERDAlalsKSPFIVHLYYSLQSANNVYLVMEY 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFG-DAVQLN------ 2916
Cdd:cd05610     86 LIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISN---EGHIKLTDFGlSKVTLNrelnmm 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2917 ----------------------------------TTYYI-------------HQLLGNPEFAAPEIILGNPVSLTADTWS 2949
Cdd:cd05610    163 dilttpsmakpkndysrtpgqvlslisslgfntpTPYRTpksvrrgaarvegERILGTPDYLAPELLLGKPHGPAVDWWA 242
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907111721 2950 VGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYfQGVSQKAKEFVCFLLQEDPAKRPSA 3013
Cdd:cd05610    243 LGVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPEGE-EELSVNAQNAIEILLTMDPTKRAGL 305
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
2771-3010 6.09e-20

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN 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: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 93.90  E-value: 6.09e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2771 VAELGRGRFAVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTH---ELGILQ---NLQHPLLVSLLDTFETPTSYVLVLEM 2843
Cdd:cd05589      4 IAVLGRGHFGKVLLAEYKPTGELFAIKALKKGdIIARDEVESlmcEKRIFEtvnSARHPFLVNLFACFQTPEHVCFVMEY 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQGRLL-----DCvvrwgsLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFG------DA 2912
Cdd:cd05589     84 AAGGDLMmhiheDV------FSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLD---TEGYVKIADFGlckegmGF 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2913 VQLNTTYyihqlLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPedYFqgVS 2992
Cdd:cd05589    155 GDRTSTF-----CGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYP--RF--LS 225
                          250
                   ....*....|....*...
gi 1907111721 2993 QKAKEFVCFLLQEDPAKR 3010
Cdd:cd05589    226 TEAISIMRRLLRKNPERR 243
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
2774-2964 6.47e-20

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC 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: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 93.64  E-value: 6.47e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHELGIL-QNLQHPLLVSLLDTFETPTSYVLVLEMADQGR 2848
Cdd:cd05588      3 IGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDDEdidwVQTEKHVFeTASNHPFLVGLHSCFQTESRLFFVIEFVNGGD 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFG---DAVQLNTTyyIHQLL 2925
Cdd:cd05588     83 LMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDS---EGHIKLTDYGmckEGLRPGDT--TSTFC 157
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1907111721 2926 GNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPF 2964
Cdd:cd05588    158 GTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPF 196
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
2768-2986 6.51e-20

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR 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: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 94.53  E-value: 6.51e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLM-KRDQVTH---ELGILQNLQHPLLVSLLDTFETPTSYVLVLEM 2843
Cdd:cd05629      3 FHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMfKKDQLAHvkaERDVLAESDSPWVVSLYYSFQDAQYLYLIMEF 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQLNTTY---Y 2920
Cdd:cd05629     83 LPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILID---RGGHIKLSDFGLSTGFHKQHdsaY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2921 IHQLL---------------------------------------------GNPEFAAPEIILGNPVSLTADTWSVGVLTY 2955
Cdd:cd05629    160 YQKLLqgksnknridnrnsvavdsinltmsskdqiatwkknrrlmaystvGTPDYIAPEIFLQQGYGQECDWWSLGAIMF 239
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1907111721 2956 VLLSGVSPFLDDSVEETCLNIC--RLDFSFPED 2986
Cdd:cd05629    240 ECLIGWPPFCSENSHETYRKIInwRETLYFPDD 272
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
2774-3010 6.53e-20

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta 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: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 93.53  E-value: 6.53e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNL-----QHPLLVSLLDTFETPTSYVLVLEMADQGR 2848
Cdd:cd05616      8 LGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVlalsgKPPFLTQLHSCFQTMDRLYFVMEYVNGGD 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFG-------DAVQLNTtyyi 2921
Cdd:cd05616     88 LMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLD---SEGHIKIADFGmckeniwDGVTTKT---- 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2922 hqLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPedyfQGVSQKAKEFVCF 3001
Cdd:cd05616    161 --FCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYP----KSMSKEAVAICKG 234

                   ....*....
gi 1907111721 3002 LLQEDPAKR 3010
Cdd:cd05616    235 LMTKHPGKR 243
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
2774-3023 6.82e-20

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. 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 CDK10 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: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 93.20  E-value: 6.82e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVnKKLMKRDQVT----HELGILQNLQHPLLVSLLD--TFETPTSYVLVLEMADQ- 2846
Cdd:cd07845     15 IGEGTYGIVYRARDTTSGEIVALKKV-RMDNERDGIPisslREITLLLNLRHPNIVELKEvvVGKHLDSIFLVMEYCEQd 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2847 -GRLLDCVVRwgSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGdavqLNTTYYIHQLL 2925
Cdd:cd07845     94 lASLLDNMPT--PFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTD---KGCLKIADFG----LARTYGLPAKP 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2926 GNPE-----FAAPEIILGNPVSLTA-DTWSVGVLTYVLLSGvSPFLDDSVEETCLN-ICRL------------------- 2979
Cdd:cd07845    165 MTPKvvtlwYRAPELLLGCTTYTTAiDMWAVGCILAELLAH-KPLLPGKSEIEQLDlIIQLlgtpnesiwpgfsdlplvg 243
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907111721 2980 DFSFPED-Y------FQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQ 3023
Cdd:cd07845    244 KFTLPKQpYnnlkhkFPWLSEAGLRLLNFLLMYDPKKRATAEEALESSYFK 294
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
2774-3010 7.17e-20

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 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: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 93.50  E-value: 7.17e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd05632     10 LGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKgesmALNEKQILEKVNSQFVVNLAYAYETKDALCLVLTIMNGGDL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGS--LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTYYIHQLLGN 2927
Cdd:cd05632     90 KFHIYNMGNpgFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDY---GHIRISDLGLAVKIPEGESIRGRVGT 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2928 PEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQEDP 3007
Cdd:cd05632    167 VGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDRRVLETEEVYSAKFSEEAKSICKMLLTKDP 246

                   ...
gi 1907111721 3008 AKR 3010
Cdd:cd05632    247 KQR 249
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
2774-3022 7.19e-20

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 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: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 92.11  E-value: 7.19e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKkCDQKGTKRAVATKFV-------NKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQ 2846
Cdd:cd06631      9 LGKGAYGTVY-CGLTSTGQLIAVKQVeldtsdkEKAEKEYEKLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEFVPG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2847 GRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdqsLAKPTIKLADFGDAVQL--NTTYYIH-Q 2923
Cdd:cd06631     88 GSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIML---MPNGVIKLIDFGCAKRLciNLSSGSQsQ 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2924 LL----GNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPE--DYFqgvSQKAKE 2997
Cdd:cd06631    165 LLksmrGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIGSGRKPVPRlpDKF---SPEARD 241
                          250       260
                   ....*....|....*....|....*
gi 1907111721 2998 FVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd06631    242 FVHACLTRDQDERPSAEQLLKHPFI 266
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
2768-3018 7.53e-20

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 92.10  E-value: 7.53e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKfVNKKL----MKRD---QVTHELGILQNLQHPLLVSLLDTFETPTSYVLV 2840
Cdd:cd08222      2 YRVVRKLGSGNFGTVYLVSDLKATADEELK-VLKEIsvgeLQPDetvDANREAKLLSKLDHPAIVKFHDSFVEKESFCIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2841 LEMAdQGRLLDCVVRW-----GSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakptIKLADFGDA-VQ 2914
Cdd:cd08222     81 TEYC-EGGDLDDKISEykksgTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNNV----IKVGDFGISrIL 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2915 LNTTYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDF-SFPEDYfqgvSQ 2993
Cdd:cd08222    156 MGTSDLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETpSLPDKY----SK 231
                          250       260
                   ....*....|....*....|....*
gi 1907111721 2994 KAKEFVCFLLQEDPAKRPSAALALQ 3018
Cdd:cd08222    232 ELNAIYSRMLNKDPALRPSAAEILK 256
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
2768-3014 7.63e-20

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-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: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 92.40  E-value: 7.63e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTH-ELGILQNL-QHPLLVSLLDT---FETPTSYVLVLE 2842
Cdd:cd13985      2 YQVTKQLGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEQLRVAIkEIEIMKRLcGHPNIVQYYDSailSSEGRKEVLLLM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 MADQGRLLDCVVRWGS--LTEGKVRAHLGEVLEAVRYLHNC--RIAHLDLKPENILVDQSlakPTIKLADFGDA------ 2912
Cdd:cd13985     82 EYCPGSLVDILEKSPPspLSEEEVLRIFYQICQAVGHLHSQspPIIHRDIKIENILFSNT---GRFKLCDFGSAttehyp 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2913 -------------VQLNTTyyihqllgnPEFAAPEII---LGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVeetcLNI 2976
Cdd:cd13985    159 leraeevniieeeIQKNTT---------PMYRAPEMIdlySKKPIGEKADIWALGCLLYKLCFFKLPFDESSK----LAI 225
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1907111721 2977 CRLDFSFPEdyFQGVSQKAKEFVCFLLQEDPAKRPSAA 3014
Cdd:cd13985    226 VAGKYSIPE--QPRYSPELHDLIRHMLTPDPAERPDIF 261
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
2765-3048 7.98e-20

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 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: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 92.44  E-value: 7.98e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2765 DAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRD--QVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLE 2842
Cdd:cd06641      3 EELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEieDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIME 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 MADQGRLLDcVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQL-NTTYYI 2921
Cdd:cd06641     83 YLGGGSALD-LLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSE---HGEVKLADFGVAGQLtDTQIKR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2922 HQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDdsveetcLNICRLDFSFPED---YFQG-VSQKAKE 2997
Cdd:cd06641    159 N*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSE-------LHPMKVLFLIPKNnppTLEGnYSKPLKE 231
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907111721 2998 FVCFLLQEDPAKRPSAALALQEQWLQAgngSGKgtgvlDTSRLTSFIERRK 3048
Cdd:cd06641    232 FVEACLNKEPSFRPTAKELLKHKFILR---NAK-----KTSYLTELIDRYK 274
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
2773-3025 1.00e-19

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK 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: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 92.74  E-value: 1.00e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRAVATKFVN-KKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLD 2851
Cdd:cd06659     28 KIGEGSTGVVCIAREKHSGRQVAVKMMDlRKQQRRELLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGGALTD 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2852 cVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQLNTTYYIHQ-LLGNPEF 2930
Cdd:cd06659    108 -IVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDG---RVKLSDFGFCAQISKDVPKRKsLVGTPYW 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2931 AAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETclnICRLDFSFPEDY--FQGVSQKAKEFVCFLLQEDPA 3008
Cdd:cd06659    184 MAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQA---MKRLRDSPPPKLknSHKASPVLRDFLERMLVRDPQ 260
                          250
                   ....*....|....*...
gi 1907111721 3009 KRPSAALALQEQW-LQAG 3025
Cdd:cd06659    261 ERATAQELLDHPFlLQTG 278
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
2768-2960 1.36e-19

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 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: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 92.67  E-value: 1.36e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFA-VVKKCDQKGTKRAVATKFV-NKKLMKRDQVThELGILQNL--------QHplLVSLLDTFETPTSY 2837
Cdd:cd14135      2 YRVYGYLGKGVFSnVVRARDLARGNQEVAIKIIrNNELMHKAGLK-ELEILKKLndadpddkKH--CIRLLRHFEHKNHL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2838 VLVLEMADqGRLLDCVVRWGS---LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlaKPTIKLADFGDAVQ 2914
Cdd:cd14135     79 CLVFESLS-MNLREVLKKYGKnvgLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEK--KNTLKLCDFGSASD 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2915 LN----TTYYIHQLlgnpeFAAPEIILGNPVSLTADTWSVGVLTYVLLSG 2960
Cdd:cd14135    156 IGeneiTPYLVSRF-----YRAPEIILGLPYDYPIDMWSVGCTLYELYTG 200
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
2774-3010 1.56e-19

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 92.75  E-value: 1.56e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQ------VTHELGILQNlQHPLLVSLLDTFETPTSYVLVLEMADQG 2847
Cdd:cd05615     18 LGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDdvectmVEKRVLALQD-KPPFLTQLHSCFQTVDRLYFVMEYVNGG 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2848 RLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFG----DAVQLNTTyyiHQ 2923
Cdd:cd05615     97 DLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLD---SEGHIKIADFGmckeHMVEGVTT---RT 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2924 LLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPedyfQGVSQKAKEFVCFLL 3003
Cdd:cd05615    171 FCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYP----KSLSKEAVSICKGLM 246

                   ....*..
gi 1907111721 3004 QEDPAKR 3010
Cdd:cd05615    247 TKHPAKR 253
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
2768-3022 1.59e-19

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: 90.79  E-value: 1.59e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLM---KRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMA 2844
Cdd:cd08225      2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMpvkEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYC 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 DQGRLLDCVVRW-GSL-TEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlaKPTIKLADFGDAVQLN-TTYYI 2921
Cdd:cd08225     82 DGGDLMKRINRQrGVLfSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKN--GMVAKLGDFGIARQLNdSMELA 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2922 HQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFqgvSQKAKEFVCF 3001
Cdd:cd08225    160 YTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFAPISPNF---SRDLRSLISQ 236
                          250       260
                   ....*....|....*....|.
gi 1907111721 3002 LLQEDPAKRPSAALALQEQWL 3022
Cdd:cd08225    237 LFKVSPRDRPSITSILKRPFL 257
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
2765-3010 1.72e-19

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 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: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 91.50  E-value: 1.72e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2765 DAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRD----QVTHELGILQNLQHPLLVSLLDTFETPTSYVLV 2840
Cdd:cd05607      1 DKYFYEFRVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKsgekMALLEKEILEKVNSPFIVSLAYAFETKTHLCLV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2841 LEMADQGRLLDCVVRWGS--LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQLNTT 2918
Cdd:cd05607     81 MSLMNGGDLKYHIYNVGErgIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDD---NGNCRLSDLGLAVEVKEG 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2919 YYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDD----SVEETCLNICRLDFSFPEDYFqgvSQK 2994
Cdd:cd05607    158 KPITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHkekvSKEELKRRTLEDEVKFEHQNF---TEE 234
                          250
                   ....*....|....*.
gi 1907111721 2995 AKEFVCFLLQEDPAKR 3010
Cdd:cd05607    235 AKDICRLFLAKKPENR 250
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
2774-3010 1.81e-19

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon 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: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 92.17  E-value: 1.81e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQ-----VTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGR 2848
Cdd:cd05591      3 LGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQDDdvdctMTEKRILALAAKHPFLTALHSCFQTKDRLFFVMEYVNGGD 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQ------LNTTYyih 2922
Cdd:cd05591     83 LMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLD---AEGHCKLADFGMCKEgilngkTTTTF--- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2923 qlLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPedyfQGVSQKAKEFVCFL 3002
Cdd:cd05591    157 --CGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYP----VWLSKEAVSILKAF 230

                   ....*...
gi 1907111721 3003 LQEDPAKR 3010
Cdd:cd05591    231 MTKNPAKR 238
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
2774-2964 2.69e-19

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC 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: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 92.79  E-value: 2.69e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHELGIL-QNLQHPLLVSLLDTFETPTSYVLVLEMADQGR 2848
Cdd:cd05618     28 IGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEdidwVQTEKHVFeQASNHPFLVGLHSCFQTESRLFFVIEYVNGGD 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQ-LNTTYYIHQLLGN 2927
Cdd:cd05618    108 LMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLD---SEGHIKLTDYGMCKEgLRPGDTTSTFCGT 184
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1907111721 2928 PEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPF 2964
Cdd:cd05618    185 PNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPF 221
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
2774-2964 2.90e-19

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 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: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 90.49  E-value: 2.90e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATK---FVNKKLMKRDQVTH---ELGILQNLQHPLLVS----LLDTFETPTSyvLVLEM 2843
Cdd:cd06652     10 LGQGAFGRVYLCYDADTGRELAVKqvqFDPESPETSKEVNAlecEIQLLKNLLHERIVQyygcLRDPQERTLS--IFMEY 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTYY--- 2920
Cdd:cd06652     88 MPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSV---GNVKLGDFGASKRLQTICLsgt 164
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907111721 2921 -IHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPF 2964
Cdd:cd06652    165 gMKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPW 209
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
2768-3033 3.55e-19

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 92.19  E-value: 3.55e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSE---VAELGRGRFAVVKKCDQKGTKRAVATKFV--NKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLE 2842
Cdd:PLN00034    73 LSElerVNRIGSGAGGTVYKVIHRPTGRLYALKVIygNHEDTVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLE 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 MADQGRLldcvvrwgsltEGKVRAHLG-------EVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQL 2915
Cdd:PLN00034   153 FMDGGSL-----------EGTHIADEQfladvarQILSGIAYLHRRHIVHRDIKPSNLLIN---SAKNVKIADFGVSRIL 218
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2916 NTTY-YIHQLLGNPEFAAPEII-----LGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQ 2989
Cdd:PLN00034   219 AQTMdPCNSSVGTIAYMSPERIntdlnHGAYDGYAGDIWSLGVSILEFYLGRFPFGVGRQGDWASLMCAICMSQPPEAPA 298
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1907111721 2990 GVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLqAGNGSGKGTG 3033
Cdd:PLN00034   299 TASREFRHFISCCLQREPAKRWSAMQLLQHPFI-LRAQPGQGQG 341
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
2774-3010 4.05e-19

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC 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: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 91.52  E-value: 4.05e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTH----ELGILQ-NLQHPLLVSLLDTFETPTSYVLVLEMADQGR 2848
Cdd:cd05619     13 LGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVEctmvEKRVLSlAWEHPFLTHLFCTFQTKENLFFVMEYLNGGD 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQ-LNTTYYIHQLLGN 2927
Cdd:cd05619     93 LMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDK---DGHIKIADFGMCKEnMLGDAKTSTFCGT 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2928 PEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNIcRLDFSFpedYFQGVSQKAKEFVCFLLQEDP 3007
Cdd:cd05619    170 PDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSI-RMDNPF---YPRWLEKEAKDILVKLFVREP 245

                   ...
gi 1907111721 3008 AKR 3010
Cdd:cd05619    246 ERR 248
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
2774-3010 4.60e-19

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta 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: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 91.12  E-value: 4.60e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQ-----VTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGR 2848
Cdd:cd05590      3 LGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDdvectMTEKRILSLARNHPFLTQLYCCFQTPDRLFFVMEFVNGGD 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFG-------DAVQLNTtyyi 2921
Cdd:cd05590     83 LMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDH---EGHCKLADFGmckegifNGKTTST---- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2922 hqLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPedyfQGVSQKAKEFVCF 3001
Cdd:cd05590    156 --FCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYP----TWLSQDAVDILKA 229

                   ....*....
gi 1907111721 3002 LLQEDPAKR 3010
Cdd:cd05590    230 FMTKNPTMR 238
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
2765-3048 5.13e-19

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 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: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 90.11  E-value: 5.13e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2765 DAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRD--QVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLE 2842
Cdd:cd06640      3 EELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEDEieDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIME 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 MADQGRLLDcVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQLNTTYYIH 2922
Cdd:cd06640     83 YLGGGSALD-LLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSE---QGDVKLADFGVAGQLTDTQIKR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2923 Q-LLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRldfsFPEDYFQG-VSQKAKEFVC 3000
Cdd:cd06640    159 NtFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHPMRVLFLIPK----NNPPTLVGdFSKPFKEFID 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1907111721 3001 FLLQEDPAKRPSAALALQEQWLQAGNGSgkgtgvldTSRLTSFIERRK 3048
Cdd:cd06640    235 ACLNKDPSFRPTAKELLKHKFIVKNAKK--------TSYLTELIDRFK 274
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
2768-3018 6.29e-19

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 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: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 89.87  E-value: 6.29e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATK--FVNKKLMKRdqvthELGILQNLQHPLLVSLLDTFETPTS-----YV-L 2839
Cdd:cd14137      6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIKkvLQDKRYKNR-----ELQIMRRLKHPNIVKLKYFFYSSGEkkdevYLnL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2840 VLE-MAD--QGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlaKPTIKLADFGDAVQL- 2915
Cdd:cd14137     81 VMEyMPEtlYRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPE--TGVLKLCDFGSAKRLv 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2916 ----NTTY-----YihqllgnpefAAPEIILGNPVSLTA-DTWSVG------VLTYVLLSGvspflDDSVE--------- 2970
Cdd:cd14137    159 pgepNVSYicsryY----------RAPELIFGATDYTTAiDIWSAGcvlaelLLGQPLFPG-----ESSVDqlveiikvl 223
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907111721 2971 -----ETCLNIC--RLDFSFP-------EDYF-QGVSQKAKEFVCFLLQEDPAKRPSAALALQ 3018
Cdd:cd14137    224 gtptrEQIKAMNpnYTEFKFPqikphpwEKVFpKRTPPDAIDLLSKILVYNPSKRLTALEALA 286
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
2806-3017 6.89e-19

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: 89.03  E-value: 6.89e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2806 RDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDCVVRWGS--LTEGKVRAHLGEVLEAVRYLHNCRI 2883
Cdd:cd08221     43 RRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGNLHDKIAQQKNqlFPEEVVLWYLYQIVSAVSHIHKAGI 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2884 AHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTYYIHQ-LLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVS 2962
Cdd:cd08221    123 LHRDIKTLNIFLTKA---DLVKLGDFGISKVLDSESSMAEsIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKR 199
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907111721 2963 PFLDDSVEETCLNICRLDFsfpEDYFQGVSQKAKEFVCFLLQEDPAKRPSAALAL 3017
Cdd:cd08221    200 TFDATNPLRLAVKIVQGEY---EDIDEQYSEEIIQLVHDCLHQDPEDRPTAEELL 251
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
2768-3004 7.25e-19

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 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: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 89.68  E-value: 7.25e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVT--HELGILQNLQHPLLVSLLDTFETPTSYVLVLEM-- 2843
Cdd:cd07871      7 YVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTaiREVSLLKNLKHANIVTLHDIIHTERCLTLVFEYld 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQGRLLD-CvvrwGSL-TEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFG--DAVQLNTTY 2919
Cdd:cd07871     87 SDLKQYLDnC----GNLmSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINE---KGELKLADFGlaRAKSVPTKT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2920 YIHQLLgNPEFAAPEIILGNP-VSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQ----K 2994
Cdd:cd07871    160 YSNEVV-TLWYRPPDVLLGSTeYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELHLIFRLLGTPTEETWPGVTSneefR 238
                          250
                   ....*....|
gi 1907111721 2995 AKEFVCFLLQ 3004
Cdd:cd07871    239 SYLFPQYRAQ 248
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
2774-3010 7.34e-19

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 90.39  E-value: 7.34e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQ-----VTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGR 2848
Cdd:cd05620      3 LGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDdvectMVEKRVLALAWENPFLTHLYCTFQTKEHLFFVMEFLNGGD 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFG----DAVQLN--TTYyih 2922
Cdd:cd05620     83 LMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRD---GHIKIADFGmckeNVFGDNraSTF--- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2923 qlLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNIcRLDfsfPEDYFQGVSQKAKEFVCFL 3002
Cdd:cd05620    157 --CGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESI-RVD---TPHYPRWITKESKDILEKL 230

                   ....*...
gi 1907111721 3003 LQEDPAKR 3010
Cdd:cd05620    231 FERDPTRR 238
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
2807-3022 7.37e-19

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 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: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 89.36  E-value: 7.37e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2807 DQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHL 2886
Cdd:cd06629     53 DALKSEIDTLKDLDHPNIVQYLGFEETEDYFSIFLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHR 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2887 DLKPENILVDQslaKPTIKLADFGDAVQLNTTYYIHQ---LLGNPEFAAPEIILGNPVSLTA--DTWSVGVLTYVLLSGV 2961
Cdd:cd06629    133 DLKADNILVDL---EGICKISDFGISKKSDDIYGNNGatsMQGSVFWMAPEVIHSQGQGYSAkvDIWSLGCVVLEMLAGR 209
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907111721 2962 SPFLDDSVEETCLNICRLDFS--FPEDYfqGVSQKAKEFV--CFLLqeDPAKRPSAALALQEQWL 3022
Cdd:cd06629    210 RPWSDDEAIAAMFKLGNKRSAppVPEDV--NLSPEALDFLnaCFAI--DPRDRPTAAELLSHPFL 270
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
876-1105 8.89e-19

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 87.50  E-value: 8.89e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  876 QLRHLQAEVKQVLGWIRNGESMLNAGLiTASSLQEAEQLQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDMIRD 955
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  956 CAEKVASHWQQLMLKMEDRLKLVNASVAFYKTSEQVCSVlesleqeykreEDWCGGADKLGPNSETDHVTPMISKHLEQK 1035
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL-----------EQWLEEKEAALASEDLGKDLESVEELLKKH 148
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1036 EAFLKACTlarrNADVFLKYLHRNSVSMPGmvTHIKAPEQQVKNILNELFQRENRVLHYWTMRKRRLDQC 1105
Cdd:cd00176    149 KELEEELE----AHEPRLKSLNELAEELLE--EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
2774-3010 9.09e-19

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 90.85  E-value: 9.09e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHELGIL-QNLQHPLLVSLLDTFETPTSYVLVLEMADQGR 2848
Cdd:cd05617     23 IGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEdidwVQTEKHVFeQASSNPFLVGLHSCFQTTSRLFLVIEYVNGGD 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQ-LNTTYYIHQLLGN 2927
Cdd:cd05617    103 LMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDAD---GHIKLTDYGMCKEgLGPGDTTSTFCGT 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2928 PEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPF---LDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQ 3004
Cdd:cd05617    180 PNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiiTDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLN 259

                   ....*.
gi 1907111721 3005 EDPAKR 3010
Cdd:cd05617    260 KDPKER 265
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
2772-2967 9.19e-19

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: 88.98  E-value: 9.19e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2772 AELGRGRFAVVKKCDQKGtkRAVATKFVN---KKLMKRDQVTHELGILqNLQHPLLVSLL--DTFETPTSYVLVL-EMAD 2845
Cdd:cd13979      9 EPLGSGGFGSVYKATYKG--ETVAVKIVRrrrKNRASRQSFWAELNAA-RLRHENIVRVLaaETGTDFASLGLIImEYCG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2846 QGRLLDCVVR-WGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLN----TTYY 2920
Cdd:cd13979     86 NGTLQQLIYEgSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQ---GVCKLCDFGCSVKLGegneVGTP 162
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1907111721 2921 IHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDD 2967
Cdd:cd13979    163 RSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGL 209
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
2774-3025 1.01e-18

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 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: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 90.47  E-value: 1.01e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGIL-----QNLQHPLLVSLLDTFETPTSYVLVLEMADQGr 2848
Cdd:cd14229      8 LGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQGQIEVGILarlsnENADEFNFVRAYECFQHRNHTCLVFEMLEQN- 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVV--RWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKP-TIKLADFGDAVQLNTTyYIHQLL 2925
Cdd:cd14229     87 LYDFLKqnKFSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLVDPVRQPyRVKVIDFGSASHVSKT-VCSTYL 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2926 GNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGvSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCfllQE 3005
Cdd:cd14229    166 QSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG-WPLYPGALEYDQIRYISQTQGLPGEQLLNVGTKTSRFFC---RE 241
                          250       260
                   ....*....|....*....|.
gi 1907111721 3006 DPAKRPSAAL-ALQEQWLQAG 3025
Cdd:cd14229    242 TDAPYSSWRLkTLEEHEAETG 262
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
2768-3023 1.11e-18

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK 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: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 89.40  E-value: 1.11e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVN-KKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQ 2846
Cdd:cd06654     22 YTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2847 GRLLDcVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTYYIHQ-LL 2925
Cdd:cd06654    102 GSLTD-VVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMD---GSVKLTDFGFCAQITPEQSKRStMV 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2926 GNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNIC---RLDFSFPEDyfqgVSQKAKEFVCFL 3002
Cdd:cd06654    178 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIAtngTPELQNPEK----LSAIFRDFLNRC 253
                          250       260
                   ....*....|....*....|.
gi 1907111721 3003 LQEDPAKRPSAALALQEQWLQ 3023
Cdd:cd06654    254 LEMDVEKRGSAKELLQHQFLK 274
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
2774-2964 1.21e-18

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-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: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 88.54  E-value: 1.21e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFV-----NKKLMKR-DQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVL--EMAD 2845
Cdd:cd06653     10 LGRGAFGEVYLCYDADTGRELAVKQVpfdpdSQETSKEvNALECEIQLLKNLRHDRIVQYYGCLRDPEEKKLSIfvEYMP 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2846 QGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTYY----I 2921
Cdd:cd06653     90 GGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSA---GNVKLGDFGASKRIQTICMsgtgI 166
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1907111721 2922 HQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPF 2964
Cdd:cd06653    167 KSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPW 209
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
2768-3023 1.42e-18

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK 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: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 89.01  E-value: 1.42e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVN-KKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQ 2846
Cdd:cd06655     21 YTRYEKIGQGASGTVFTAIDVATGQEVAIKQINlQKQPKKELIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYLAG 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2847 GRLLDcVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQLNTTYYIHQ-LL 2925
Cdd:cd06655    101 GSLTD-VVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGM---DGSVKLTDFGFCAQITPEQSKRStMV 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2926 GNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNIC---RLDFSFPEDyfqgVSQKAKEFVCFL 3002
Cdd:cd06655    177 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAtngTPELQNPEK----LSPIFRDFLNRC 252
                          250       260
                   ....*....|....*....|.
gi 1907111721 3003 LQEDPAKRPSAALALQEQWLQ 3023
Cdd:cd06655    253 LEMDVEKRGSAKELLQHPFLK 273
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
2774-3013 1.77e-18

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK 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: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 88.44  E-value: 1.77e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGtkRAVATKFVNKK------------LMKRDQVTH----------ELGILQNLQHPLLVSLLDTF 2831
Cdd:cd14000      2 LGDGGFGSVYRASYKG--EPVAVKIFNKHtssnfanvpadtMLRHLRATDamknfrllrqELTVLSHLHHPSIVYLLGIG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2832 ETPTsyVLVLEMADQGRLlDCVVRWGSltegKVRAHLG---------EVLEAVRYLHNCRIAHLDLKPENILVdQSLAKP 2902
Cdd:cd14000     80 IHPL--MLVLELAPLGSL-DHLLQQDS----RSFASLGrtlqqrialQVADGLRYLHSAMIIYRDLKSHNVLV-WTLYPN 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2903 T---IKLADFGDAVQlNTTYYIHQLLGNPEFAAPEIILGNPV-SLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNI-- 2976
Cdd:cd14000    152 SaiiIKIADYGISRQ-CCRMGAKGSEGTPGFRAPEIARGNVIyNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIhg 230
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1907111721 2977 -CRLDFSFPEDYFqgvSQKAKEFVCFLLQEDPAKRPSA 3013
Cdd:cd14000    231 gLRPPLKQYECAP---WPEVEVLMKKCWKENPQQRPTA 265
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
2773-3011 2.28e-18

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 88.55  E-value: 2.28e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRAVATKFVNK-KLMK---RDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGR 2848
Cdd:cd08229     31 KIGRGQFSEVYRATCLLDGVPVALKKVQIfDLMDakaRADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGD 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVVRWGS----LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQLNT-TYYIHQ 2923
Cdd:cd08229    111 LSRMIKHFKKqkrlIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFIT---ATGVVKLGDLGLGRFFSSkTTAAHS 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2924 LLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVE--ETCLNICRLDF-SFPEDYFqgvSQKAKEFVC 3000
Cdd:cd08229    188 LVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNlySLCKKIEQCDYpPLPSDHY---SEELRQLVN 264
                          250
                   ....*....|.
gi 1907111721 3001 FLLQEDPAKRP 3011
Cdd:cd08229    265 MCINPDPEKRP 275
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
2764-3022 2.97e-18

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 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: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 89.27  E-value: 2.97e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2764 FDAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKfvnkKLMKRDQVTH-------ELGILQNLQHPLLVSLLDTFeTPTS 2836
Cdd:cd07851     13 VPDRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIK----KLSRPFQSAIhakrtyrELRLLKHMKHENVIGLLDVF-TPAS 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2837 YV-------LVLEMADQGrlLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADF 2909
Cdd:cd07851     88 SLedfqdvyLVTHLMGAD--LNNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDC---ELKILDF 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2910 GDAVQLN---TTYyihqlLGNPEFAAPEIILgNPVSL--TADTWSVGVLTYVLLSGVSPFL-DDSVEE-TC-LNIC---- 2977
Cdd:cd07851    163 GLARHTDdemTGY-----VATRWYRAPEIML-NWMHYnqTVDIWSVGCIMAELLTGKTLFPgSDHIDQlKRiMNLVgtpd 236
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907111721 2978 -----------------------RLDFSfpeDYFQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd07851    237 eellkkissesarnyiqslpqmpKKDFK---EVFSGANPLAIDLLEKMLVLDPDKRITAAEALAHPYL 301
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
2768-3012 3.03e-18

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 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: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 87.17  E-value: 3.03e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRF--AVVKKCDQKGTKRAVATKFVNKKLMK-RDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMA 2844
Cdd:cd08218      2 YVRIKKIGEGSFgkALLVKSKEDGKQYVIKEINISKMSPKeREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYC 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 DQGRLLDCV--VRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTYYIH 2922
Cdd:cd08218     82 DGGDLYKRInaQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKD---GIIKLGDFGIARVLNSTVELA 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2923 Q-LLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDF-SFPEDYfqgvSQKAKEFVC 3000
Cdd:cd08218    159 RtCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSYpPVPSRY----SYDLRSLVS 234
                          250
                   ....*....|..
gi 1907111721 3001 FLLQEDPAKRPS 3012
Cdd:cd08218    235 QLFKRNPRDRPS 246
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
2774-2965 3.21e-18

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: 88.05  E-value: 3.21e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKL--MKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYV-----LVLEMADQ 2846
Cdd:cd14039      1 LGTGGFGNVCLYQNQETGEKIAIKSCRLELsvKNKDRWCHEIQIMKKLNHPNVVKACDVPEEMNFLVndvplLAMEYCSG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2847 G---RLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAVQLNTTYYIHQ 2923
Cdd:cd14039     81 GdlrKLLNKPENCCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKIVHKIIDLGYAKDLDQGSLCTS 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907111721 2924 LLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFL 2965
Cdd:cd14039    161 FVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPFL 202
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
2762-3022 3.54e-18

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK 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: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 88.40  E-value: 3.54e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2762 DNFDAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQ--------NLQHPLLVSLLDTFET 2833
Cdd:cd14136      6 EVYNGRYHVVRKLGWGHFSTVWLCWDLQNKRFVALKVVKSAQHYTEAALDEIKLLKcvreadpkDPGREHVVQLLDDFKH 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2834 P----TSYVLVLE-MADQgrLLDCVVRWG--SLTEGKVRAHLGEVLEAVRYLHN-CRIAHLDLKPENILVdqSLAKPTIK 2905
Cdd:cd14136     86 TgpngTHVCMVFEvLGPN--LLKLIKRYNyrGIPLPLVKKIARQVLQGLDYLHTkCGIIHTDIKPENVLL--CISKIEVK 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2906 LADFGDAVQLNTTYY--IHQLlgnpEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPF---------LDDS----VE 2970
Cdd:cd14136    162 IADLGNACWTDKHFTedIQTR----QYRSPEVILGAGYGTPADIWSTACMAFELATGDYLFdphsgedysRDEDhlalII 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2971 ETCLNICR---LDFSFPEDYF-----------------QGV--------SQKAKEFVCFL---LQEDPAKRPSAALALQE 3019
Cdd:cd14136    238 ELLGRIPRsiiLSGKYSREFFnrkgelrhisklkpwplEDVlvekykwsKEEAKEFASFLlpmLEYDPEKRATAAQCLQH 317

                   ...
gi 1907111721 3020 QWL 3022
Cdd:cd14136    318 PWL 320
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
2771-3028 3.76e-18

Catalytic domain of fungal Byr1-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 Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 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: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 87.49  E-value: 3.76e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2771 VAELGRGRFAVVKKCDQKGTKRAVATK--FVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTF--ETPTsYVLVLEMADQ 2846
Cdd:cd06620     10 LKDLGAGNGGSVSKVLHIPTGTIMAKKviHIDAKSSVRKQILRELQILHECHSPYIVSFYGAFlnENNN-IIICMEYMDC 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2847 GRLlDCVVRWGSLTEGKVRAHLGE-VLEAVRYLHNC-RIAHLDLKPENILVDqslAKPTIKLADFGDAVQLnTTYYIHQL 2924
Cdd:cd06620     89 GSL-DKILKKKGPFPEEVLGKIAVaVLEGLTYLYNVhRIIHRDIKPSNILVN---SKGQIKLCDFGVSGEL-INSIADTF 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2925 LGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPF----LDDSVEETCLNICRL--------------DFSFPED 2986
Cdd:cd06620    164 VGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFagsnDDDDGYNGPMGILDLlqrivneppprlpkDRIFPKD 243
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1907111721 2987 yfqgvsqkAKEFVCFLLQEDPAKRPSAALALQEQ-WLQAGNGS 3028
Cdd:cd06620    244 --------LRDFVDRCLLKDPRERPSPQLLLDHDpFIQAVRAS 278
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
2768-2961 4.02e-18

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. 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 CDKL1/4 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: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 87.43  E-value: 4.02e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATK-FVN-------KKLMKRdqvthELGILQNLQHPLLVSLLDTFETPTSYVL 2839
Cdd:cd07847      3 YEKLSKIGEGSYGVVFKCRNRETGQIVAIKkFVEseddpviKKIALR-----EIRMLKQLKHPNLVNLIEVFRRKRKLHL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2840 VLEMADQGRL--LDCVVRwgSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNT 2917
Cdd:cd07847     78 VFEYCDHTVLneLEKNPR--GVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQ---GQIKLCDFGFARILTG 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907111721 2918 T--YYIhQLLGNPEFAAPEIILGN-----PVsltaDTWSVGVLTYVLLSGV 2961
Cdd:cd07847    153 PgdDYT-DYVATRWYRAPELLVGDtqygpPV----DVWAIGCVFAELLTGQ 198
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
2768-3018 4.06e-18

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-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: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 86.98  E-value: 4.06e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVnkKLMKRDQVT---HELGILQNLQHPLLVSLLDTFETPTSYVLVLEMA 2844
Cdd:cd06613      2 YELIQRIGSGTYGDVYKARNIATGELAAVKVI--KLEPGDDFEiiqQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 DQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTYYIHQ- 2923
Cdd:cd06613     80 GGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTED---GDVKLADFGVSAQLTATIAKRKs 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2924 LLGNPEFAAPEIILGN---PVSLTADTWSVGVLTYVLLSGVSPFLDdsveetcLNICRLDFSFPEDYFQGVSQKAKE--- 2997
Cdd:cd06613    157 FIGTPYWMAPEVAAVErkgGYDGKCDIWALGITAIELAELQPPMFD-------LHPMRALFLIPKSNFDPPKLKDKEkws 229
                          250       260
                   ....*....|....*....|....*.
gi 1907111721 2998 -----FVCFLLQEDPAKRPSAALALQ 3018
Cdd:cd06613    230 pdfhdFIKKCLTKNPKKRPTATKLLQ 255
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
2768-3013 4.56e-18

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 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: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 87.75  E-value: 4.56e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVT--HELGILQNLQHPLLVSLLDTFETPTSYVLVLEMAD 2845
Cdd:cd07873      4 YIKLDKLGEGTYATVYKGRSKLTDNLVALKEIRLEHEEGAPCTaiREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2846 QG---RLLDCvvrWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFG--DAVQLNTTYY 2920
Cdd:cd07873     84 KDlkqYLDDC---GNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINE---RGELKLADFGlaRAKSIPTKTY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2921 IHQLLgNPEFAAPEIILGNP-VSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKaKEFV 2999
Cdd:cd07873    158 SNEVV-TLWYRPPDILLGSTdYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFRILGTPTEETWPGILSN-EEFK 235
                          250
                   ....*....|....
gi 1907111721 3000 CFllqEDPAKRPSA 3013
Cdd:cd07873    236 SY---NYPKYRADA 246
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
2812-3017 4.90e-18

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 86.57  E-value: 4.90e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2812 ELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDCV-VRWGSL-TEGKVRAHLGEVLEAVRYLHNCRIAHLDLK 2889
Cdd:cd08219     48 EAVLLAKMKHPNIVAFKESFEADGHLYIVMEYCDGGDLMQKIkLQRGKLfPEDTILQWFVQMCLGVQHIHEKRVLHRDIK 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2890 PENILVDQSlakPTIKLADFGDAVQL-NTTYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDS 2968
Cdd:cd08219    128 SKNIFLTQN---GKVKLGDFGSARLLtSPGAYACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANS 204
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2969 VEETCLNICRLDFS-FPEDYfqgvSQKAKEFVCFLLQEDPAKRPSAALAL 3017
Cdd:cd08219    205 WKNLILKVCQGSYKpLPSHY----SYELRSLIKQMFKRNPRSRPSATTIL 250
PH1_Kalirin_Trio_like cd13240
Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; ...
2119-2239 5.09e-18

Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; RhoGEFs, Kalirin and Trio, the mammalian homologs of Drosophila Trio and Caenorhabditis elegans UNC-73 regulate a novel step in secretory granule maturation. Their signaling modulates the extent to which regulated cargo enter and remain in the regulated secretory pathway. This allows for fine tuning of peptides released by a single secretory cell type with impaired signaling leading to pathological states. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Kalirin and Trio are encoded by separate genes in mammals and by a single one in invertebrates. Kalirin and Trio share the same complex multidomain structure and display several splice variants. The longest Kalirin and Trio proteins have a Sec14 domain, a stretch of spectrin repeats, a RhoGEF(DH)/PH cassette (also called GEF1), an SH3 domain, a second RhoGEF(DH)/PH cassette (also called GEF2), a second SH3 domain, Ig/FNIII domains, and a kinase domain. The first RhoGEF(DH)/PH cassette catalyzes exchange on Rac1 and RhoG while the second RhoGEF(DH)/PH cassette is specific for RhoA. Kalirin and Trio are closely related to p63RhoGEF and have PH domains of similar function. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains.


Pssm-ID: 270060  Cd Length: 123  Bit Score: 82.43  E-value: 5.09e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2119 LQGFDGKIVAQGKLLLQDTFLVTDQDAgLLPRCKERRVFLFEQIVIFSEPLDKKKGFSmpGFLFKNSIKVSCLCLEENVE 2198
Cdd:cd13240      2 LEGCDEDLDSLGEVILQDSFQVWDPKQ-LIRKGRERHVFLFELCLVFSKEVKDSNGKS--KYIYKSRLMTSEIGVTEHIE 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1907111721 2199 SDPCKFAL-TSRTGDAVETFVLHSSSPSVRQTWIHEINQILE 2239
Cdd:cd13240     79 GDPCKFALwTGRVPTSDNKIVLKASSLEVKQTWVKKLREVIQ 120
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
2774-3017 5.38e-18

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: 86.94  E-value: 5.38e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCD-QKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDC 2852
Cdd:cd14066      1 IGSGGFGTVYKGVlENGTVVAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLEDR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2853 --------VVRWgsltEGKVRAHLGeVLEAVRYLHN---CRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLN---TT 2918
Cdd:cd14066     81 lhchkgspPLPW----PQRLKIAKG-IARGLEYLHEecpPPIIHGDIKSSNILLDED---FEPKLTDFGLARLIPpseSV 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2919 YYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNIcrldfsfpEDYFQgvSQKAKEF 2998
Cdd:cd14066    153 SKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRKDL--------VEWVE--SKGKEEL 222
                          250       260
                   ....*....|....*....|..
gi 1907111721 2999 VCFL---LQEDPAKRPSAALAL 3017
Cdd:cd14066    223 EDILdkrLVDDDGVEEEEVEAL 244
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
2773-3036 6.10e-18

Catalytic domain of fungal PBS2-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 Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 86.83  E-value: 6.10e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRAVATKFVNKKL--MKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQG--- 2847
Cdd:cd06622      8 ELGKGNYGSVYKVLHRPTGVTMAMKEIRLELdeSKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMDAGsld 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2848 RLLDCVVRWGSLTEGKVRAHLGEVLEAVRYL---HNcrIAHLDLKPENILVDqslAKPTIKLADFGDAVQLNTTYYIHQL 2924
Cdd:cd06622     88 KLYAGGVATEGIPEDVLRRITYAVVKGLKFLkeeHN--IIHRDVKPTNVLVN---GNGQVKLCDFGVSGNLVASLAKTNI 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2925 lGNPEFAAPE-IILGNPV-----SLTADTWSVGVLTYVLLSGVSPF---LDDSVEETCLNICRLDF-SFPEDYfqgvSQK 2994
Cdd:cd06622    163 -GCQSYMAPErIKSGGPNqnptyTVQSDVWSLGLSILEMALGRYPYppeTYANIFAQLSAIVDGDPpTLPSGY----SDD 237
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1907111721 2995 AKEFVCFLLQEDPAKRPSAALALQEQWLQAGNG-----SGKGTGVLD 3036
Cdd:cd06622    238 AQDFVAKCLNKIPNRRPTYAQLLEHPWLVKYKNadvdmAEWVTGALK 284
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
2774-2999 7.84e-18

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 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: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 88.19  E-value: 7.84e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTH---ELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd05627     10 IGRGAFGEVRLVQKKDTGHIYAMKILRKAdMLEKEQVAHiraERDILVEADGAWVVKMFYSFQDKRNLYLIMEFLPGGDM 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQLN----TTYY----- 2920
Cdd:cd05627     90 MTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLD---AKGHVKLSDFGLCTGLKkahrTEFYrnlth 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2921 ---------------------------IHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETC 2973
Cdd:cd05627    167 nppsdfsfqnmnskrkaetwkknrrqlAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETY 246
                          250       260
                   ....*....|....*....|....*...
gi 1907111721 2974 LNIC--RLDFSFPEDYfqGVSQKAKEFV 2999
Cdd:cd05627    247 RKVMnwKETLVFPPEV--PISEKAKDLI 272
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
2809-3018 7.87e-18

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 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: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 86.33  E-value: 7.87e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2809 VTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDL 2888
Cdd:cd06630     50 IREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDL 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2889 KPENILVDQSLAKptIKLADFGDAVQLNTTY-----YIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSP 2963
Cdd:cd06630    130 KGANLLVDSTGQR--LRIADFGAAARLASKGtgageFQGQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPP 207
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907111721 2964 FLDDSVEETCLNICRLDFSF-PEDYFQGVSQKAKEFVCFLLQEDPAKRPSAALALQ 3018
Cdd:cd06630    208 WNAEKISNHLALIFKIASATtPPPIPEHLSPGLRDVTLRCLELQPEDRPPARELLK 263
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
2768-2999 7.95e-18

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 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: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 88.56  E-value: 7.95e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNK-KLMKRDQVTH---ELGILQNLQHPLLVSLLDTFETPTSYVLVLEM 2843
Cdd:cd05628      3 FESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKaDMLEKEQVGHiraERDILVEADSLWVVKMFYSFQDKLNLYLIMEF 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQLN----TTY 2919
Cdd:cd05628     83 LPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLD---SKGHVKLSDFGLCTGLKkahrTEF 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2920 YI---HQL-----------------------------LGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDD 2967
Cdd:cd05628    160 YRnlnHSLpsdftfqnmnskrkaetwkrnrrqlafstVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSE 239
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1907111721 2968 SVEETCLNIC--RLDFSFPEDYfqGVSQKAKEFV 2999
Cdd:cd05628    240 TPQETYKKVMnwKETLIFPPEV--PISEKAKDLI 271
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
2764-3023 8.27e-18

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 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: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 87.81  E-value: 8.27e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2764 FDAFYSEVAELGRGRFAVVKKCDQKGTKRAVATK-----FVNKKLMKRdqvTH-ELGILQNLQHPLLVSLLDTFETPTSY 2837
Cdd:cd07855      3 VGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKkipnaFDVVTTAKR---TLrELKILRHFKHDNIIAIRDILRPKVPY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2838 --------VLVLEMADQGRLLDCVvrwGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADF 2909
Cdd:cd07855     80 adfkdvyvVLDLMESDLHHIIHSD---QPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENC---ELKIGDF 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2910 GDAVQLNT-----TYYIHQLLGNPEFAAPEIILGNPVSLTA-DTWSVGVL--------------TYV--------LLSGV 2961
Cdd:cd07855    154 GMARGLCTspeehKYFMTEYVATRWYRAPELMLSLPEYTQAiDMWSVGCIfaemlgrrqlfpgkNYVhqlqliltVLGTP 233
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907111721 2962 SPFLDDSVEetCLNICRLDFSFP-------EDYFQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQ 3023
Cdd:cd07855    234 SQAVINAIG--ADRVRRYIQNLPnkqpvpwETLYPKADQQALDLLSQMLRFDPSERITVAEALQHPFLA 300
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
2768-3021 8.44e-18

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. 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 Pho85 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: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 86.38  E-value: 8.44e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNkklMKRDQVT-----HELGILQNLQHPLLVSLLDTFETPTSYVLVLE 2842
Cdd:cd07836      2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIH---LDAEEGTpstaiREISLMKELKHENIVRLHDVIHTENKLMLVFE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 MADQG--RLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDA----VQLN 2916
Cdd:cd07836     79 YMDKDlkKYMDTHGVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINK---RGELKLADFGLArafgIPVN 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2917 T------TYYihqllgnpeFAAPEIILGNPV-SLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQ 2989
Cdd:cd07836    156 TfsnevvTLW---------YRAPDVLLGSRTySTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRIMGTPTESTWP 226
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907111721 2990 GVSQKAK-------------------------EFVCFLLQEDPAKRPSAALALQEQW 3021
Cdd:cd07836    227 GISQLPEykptfpryppqdlqqlfphadplgiDLLHRLLQLNPELRISAHDALQHPW 283
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
2768-3022 1.02e-17

Catalytic domain of Male germ cell-Associated 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 of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-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: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 86.43  E-value: 1.02e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTH--ELGILQNLQ-HPLLVSLLDTF-ETPTSYvLVLE- 2842
Cdd:cd07830      1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKKKFYSWEECMNlrEVKSLRKLNeHPNIVKLKEVFrENDELY-FVFEy 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 ---------MADQGRLLdcvvrwgslTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAV 2913
Cdd:cd07830     80 megnlyqlmKDRKGKPF---------SESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPE---VVKIADFGLAR 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2914 QLN-----TTY-----YihqllgnpefAAPEIIL-----GNPVsltaDTWSVGVLTYVLLSgVSPFLDDSVEETCLN-IC 2977
Cdd:cd07830    148 EIRsrppyTDYvstrwY----------RAPEILLrstsySSPV----DIWALGCIMAELYT-LRPLFPGSSEIDQLYkIC 212
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907111721 2978 -------------------RLDFSFPE-------DYFQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd07830    213 svlgtptkqdwpegyklasKLGFRFPQfaptslhQLIPNASPEAIDLIKDMLRWDPKKRPTASQALQHPYF 283
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
309-534 1.08e-17

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 84.42  E-value: 1.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  309 QLRLFEQDAEKMFDWITHnKGLFLNSyTEIGTSHPHAMELQTQHNHFAMNCMNVYVNINRIMSVANRLVESGHYASQQIK 388
Cdd:cd00176      1 KLQQFLRDADELEAWLSE-KEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  389 QIANQLEQEWKAFAAALDERSTLLDMSSIFHQKAEKyMSNVDSWCKACGEV----DLPSELQDLEDAIHHHQGIYEHITL 464
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAAlaseDLGKDLESVEELLKKHKELEEELEA 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  465 AysevSQDGKSLLDKLQRPLTPGSSDSLTasanyskavhHVLDVIHEVLHHQRQLENIWQHRKVRLHQRL 534
Cdd:cd00176    158 H----EPRLKSLNELAEELLEEGHPDADE----------EIEEKLEELNERWEELLELAEERQKKLEEAL 213
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
2774-2999 1.38e-17

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha 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. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 88.15  E-value: 1.38e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNK-KLMKRDQVT---HELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd05623     80 IGRGAFGEVAVVKLKNADKVFAMKILNKwEMLKRAETAcfrEERDVLVNGDSQWITTLHYAFQDDNNLYLVMDYYVGGDL 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRW-GSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQL--NTTYYIHQLLG 2926
Cdd:cd05623    160 LTLLSKFeDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMN---GHIRLADFGSCLKLmeDGTVQSSVAVG 236
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2927 NPEFAAPEIILG-----NPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNIC--RLDFSFPEDyFQGVSQKAKEFV 2999
Cdd:cd05623    237 TPDYISPEILQAmedgkGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMnhKERFQFPTQ-VTDVSENAKDLI 315
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
2768-2964 1.39e-17

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 86.96  E-value: 1.39e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFA-VVKKCDQKGTKRAVATK-FVNKKLMKRDQVTH---ELGILQNLQHPLLVSLLDTFETPTSYVLVLE 2842
Cdd:PTZ00426    32 FNFIRTLGTGSFGrVILATYKNEDFPPVAIKrFEKSKIIKQKQVDHvfsERKILNYINHPFCVNLYGSFKDESYLYLVLE 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 MADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTYYih 2922
Cdd:PTZ00426   112 FVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKD---GFIKMTDFGFAKVVDTRTY-- 186
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907111721 2923 QLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPF 2964
Cdd:PTZ00426   187 TLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPF 228
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
2768-3021 2.02e-17

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. 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 CDK9-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: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 85.69  E-value: 2.02e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKfvnKKLMKRDQ----VT--HELGILQNLQHPLLVSLLD------TFETPT 2835
Cdd:cd07840      1 YEKIAQIGEGTYGQVYKARNKKTGELVALK---KIRMENEKegfpITaiREIKLLQKLDHPNVVRLKEivtskgSAKYKG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2836 SYVLVLEMAD---QGRLLDCVVRwgsLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDA 2912
Cdd:cd07840     78 SIYMVFEYMDhdlTGLLDNPEVK---FTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINN---DGVLKLADFGLA 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2913 VQLNTTyyihqllGNPEFA---------APEIILGNPVSLTA-DTWSVGVLTYVLLSGvSPFLDDSVEETCLN-ICRL-- 2979
Cdd:cd07840    152 RPYTKE-------NNADYTnrvitlwyrPPELLLGATRYGPEvDMWSVGCILAELFTG-KPIFQGKTELEQLEkIFELcg 223
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907111721 2980 -----------------DFSFPE-------DYFQGV-SQKAKEFVCFLLQEDPAKRPSAALALQEQW 3021
Cdd:cd07840    224 spteenwpgvsdlpwfeNLKPKKpykrrlrEVFKNViDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
2768-3023 2.28e-17

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK 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. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 85.54  E-value: 2.28e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVN-KKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQ 2846
Cdd:cd06656     21 YTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2847 GRLLDcVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTYYIHQ-LL 2925
Cdd:cd06656    101 GSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMD---GSVKLTDFGFCAQITPEQSKRStMV 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2926 GNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNIC---RLDFSFPEDyfqgVSQKAKEFVCFL 3002
Cdd:cd06656    177 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAtngTPELQNPER----LSAVFRDFLNRC 252
                          250       260
                   ....*....|....*....|.
gi 1907111721 3003 LQEDPAKRPSAALALQEQWLQ 3023
Cdd:cd06656    253 LEMDVDRRGSAKELLQHPFLK 273
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
2768-3022 6.14e-17

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 84.52  E-value: 6.14e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKC-DQKgTKRAVATKFVNKKLMKRDQVTHELGILQNLQH------PLLVSLLDTFETPTSYVLV 2840
Cdd:cd14210     15 YEVLSVLGKGSFGQVVKClDHK-TGQLVAIKIIRNKKRFHQQALVEVKILKHLNDndpddkHNIVRYKDSFIFRGHLCIV 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2841 LEMADQG--RLLdCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLaKPTIKLADFGDAVQLN-T 2917
Cdd:cd14210     94 FELLSINlyELL-KSNNFQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPS-KSSIKVIDFGSSCFEGeK 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2918 TY-YIHQLLgnpeFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFL-DDSVEETCLnICRLdFSFPEDYFQGVSQKA 2995
Cdd:cd14210    172 VYtYIQSRF----YRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPgENEEEQLAC-IMEV-LGVPPKSLIDKASRR 245
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907111721 2996 KE------------------------------------FVCFL---LQEDPAKRPSAALALQEQWL 3022
Cdd:cd14210    246 KKffdsngkprpttnskgkkrrpgskslaqvlkcddpsFLDFLkkcLRWDPSERMTPEEALQHPWI 311
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
2773-3023 6.20e-17

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK 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: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 84.32  E-value: 6.20e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRAVATKFVN-KKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLD 2851
Cdd:cd06658     29 KIGEGSTGIVCIATEKHTGKQVAVKKMDlRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALTD 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2852 cVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQLNTTYYIHQ-LLGNPEF 2930
Cdd:cd06658    109 -IVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLT---SDGRIKLSDFGFCAQVSKEVPKRKsLVGTPYW 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2931 AAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDdsvEETCLNICRLDFSFPEDY--FQGVSQKAKEFVCFLLQEDPA 3008
Cdd:cd06658    185 MAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFN---EPPLQAMRRIRDNLPPRVkdSHKVSSVLRGFLDLMLVREPS 261
                          250
                   ....*....|....*
gi 1907111721 3009 KRPSAALALQEQWLQ 3023
Cdd:cd06658    262 QRATAQELLQHPFLK 276
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
2774-3019 7.05e-17

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of 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. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK 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: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 83.33  E-value: 7.05e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKrdqvTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDCV 2853
Cdd:cd13991     14 IGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFR----AEELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKEGGSLGQLI 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2854 VRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTikLADFGDAVQLNTTYYIHQLLGNPEFA-- 2931
Cdd:cd13991     90 KEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSDAF--LCDFGHAECLDPDGLGKSLFTGDYIPgt 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2932 ----APEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLD---FSFPEDYFQGVSQKAKEFvcflLQ 3004
Cdd:cd13991    168 ethmAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLCLKIANEPpplREIPPSCAPLTAQAIQAG----LR 243
                          250       260
                   ....*....|....*....|..
gi 1907111721 3005 EDPAKRPSA-------ALALQE 3019
Cdd:cd13991    244 KEPVHRASAaelrrktNRALQE 265
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
2774-3014 7.55e-17

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 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: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 83.08  E-value: 7.55e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKraVATKFVNKKLMKRdQVTHELGILQNLQHPLLVSLLDTFETPTsyVLVLEMADQGRLlDCV 2853
Cdd:cd14068      2 LGDGGFGSVYRAVYRGED--VAVKIFNKHTSFR-LLRQELVVLSHLHHPSLVALLAAGTAPR--MLVMELAPKGSL-DAL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2854 VRW--GSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTI--KLADFGDAvQLNTTYYIHQLLGNPE 2929
Cdd:cd14068     76 LQQdnASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNCAIiaKIADYGIA-QYCCRMGIKTSEGTPG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2930 FAAPEIILGNPV-SLTADTWSVGVLTYVLLSGVSPFLDdsveetclnicrlDFSFPEDY----FQG-VSQKAKEFVCF-- 3001
Cdd:cd14068    155 FRAPEVARGNVIyNQQADVYSFGLLLYDILTCGERIVE-------------GLKFPNEFdelaIQGkLPDPVKEYGCApw 221
                          250       260
                   ....*....|....*....|..
gi 1907111721 3002 ---------LLQEDPAKRPSAA 3014
Cdd:cd14068    222 pgvealikdCLKENPQCRPTSA 243
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
2771-2953 7.94e-17

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 83.63  E-value: 7.94e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2771 VAELGRGRFAVVKKCDQKGTKravATKFVNKKLMK-------RDQVTHELGILQNLQ---HPLLVSLLDTFETPTSYVLV 2840
Cdd:cd14052      5 VELIGSGEFSQVYKVSERVPT---GKVYAVKKLKPnyagakdRLRRLEEVSILRELTldgHDNIVQLIDSWEYHGHLYIQ 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2841 LEMADQGRL---LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQLNT 2917
Cdd:cd14052     82 TELCENGSLdvfLSELGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITF---EGTLKIGDFGMATVWPL 158
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1907111721 2918 TYYIhQLLGNPEFAAPEIILGNPVSLTADTWSVGVL 2953
Cdd:cd14052    159 IRGI-EREGDREYIAPEILSEHMYDKPADIFSLGLI 193
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
2762-3019 8.48e-17

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the 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: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK 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: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 83.50  E-value: 8.48e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2762 DNFDafysEVAELGRGRFAVVKKCDQKGTKRAVATKFV--NKKLMKRDQVTHELGILQNLQHPLLVSLLDTF-ETPTSYV 2838
Cdd:cd13996      6 NDFE----EIELLGSGGFGSVYKVRNKVDGVTYAIKKIrlTEKSSASEKVLREVKALAKLNHPNIVRYYTAWvEEPPLYI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2839 LvLEMADQGRL---LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAkpTIKLADFGDAV-- 2913
Cdd:cd13996     82 Q-MELCEGGTLrdwIDRRNSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDL--QVKIGDFGLATsi 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2914 --QLNTTYYIHQLL-----------GNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSveeTCLNICRlD 2980
Cdd:cd13996    159 gnQKRELNNLNNNNngntsnnsvgiGTPLYASPEQLDGENYNEKADIYSLGIILFEMLHPFKTAMERS---TILTDLR-N 234
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1907111721 2981 FSFPEDYFQGVSQKAKeFVCFLLQEDPAKRPSAALALQE 3019
Cdd:cd13996    235 GILPESFKAKHPKEAD-LIQSLLSKNPEERPSAEQLLRS 272
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
2774-2951 9.41e-17

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 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: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 84.22  E-value: 9.41e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQ-------HPLLVSLLDTFETPTSYVLVLEMADQ 2846
Cdd:cd14212      7 LGQGTFGQVVKCQDLKTNKLVAVKVLKNKPAYFRQAMLEIAILTLLNtkydpedKHHIVRLLDHFMHHGHLCIVFELLGV 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2847 G--RLLDcVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdQSLAKPTIKLADFGDAVQLN-TTY-YI- 2921
Cdd:cd14212     87 NlyELLK-QNQFRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILL-VNLDSPEIKLIDFGSACFENyTLYtYIq 164
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1907111721 2922 --HqllgnpeFAAPEIILGNPVSLTADTWSVG 2951
Cdd:cd14212    165 srF-------YRSPEVLLGLPYSTAIDMWSLG 189
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
2770-2951 1.20e-16

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK 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: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 84.04  E-value: 1.20e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2770 EVAE-LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQHP-----LLVSLLDTFETPTSYVLVLEM 2843
Cdd:cd14211      2 EVLEfLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILSRLSQEnadefNFVRAYECFQHKNHTCLVFEM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQgRLLDCVV--RWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENI-LVDQSLAKPTIKLADFGDAVQLN---- 2916
Cdd:cd14211     82 LEQ-NLYDFLKqnKFSPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENImLVDPVRQPYRVKVIDFGSASHVSkavc 160
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1907111721 2917 TTYyihqlLGNPEFAAPEIILGNPVSLTADTWSVG 2951
Cdd:cd14211    161 STY-----LQSRYYRAPEIILGLPFCEAIDMWSLG 190
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
2794-2968 1.42e-16

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: 81.77  E-value: 1.42e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2794 VATKFVnkklmkRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDCVVRWGSLTEGKVRAHLGEVLE 2873
Cdd:cd14059     19 VAVKKV------RDEKETDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLYEVLRAGREITPSLLVDWSKQIAS 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2874 AVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVL 2953
Cdd:cd14059     93 GMNYLHLHKIIHRDLKSPNVLVTYN---DVLKISDFGTSKELSEKSTKMSFAGTVAWMAPEVIRNEPCSEKVDIWSFGVV 169
                          170
                   ....*....|....*.
gi 1907111721 2954 TYVLLSGVSPFLD-DS 2968
Cdd:cd14059    170 LWELLTGEIPYKDvDS 185
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
2765-3020 1.53e-16

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK 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: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 83.57  E-value: 1.53e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2765 DAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMK--RDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLE 2842
Cdd:cd06650      4 DDDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPaiRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICME 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 MADQGRLLDCVVRWGSLTE---GKVRAHLGEVLEAVRYLHncRIAHLDLKPENILVDqslAKPTIKLADFGDAVQLNTTY 2919
Cdd:cd06650     84 HMDGGSLDQVLKKAGRIPEqilGKVSIAVIKGLTYLREKH--KIMHRDVKPSNILVN---SRGEIKLCDFGVSGQLIDSM 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2920 yIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPF-LDDSVEETCLNICRLDF------SFPEDYFQGVS 2992
Cdd:cd06650    159 -ANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIpPPDAKELELMFGCQVEGdaaetpPRPRTPGRPLS 237
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1907111721 2993 QKAK---------EFVCFLLQEDPAKRPSAALALQEQ 3020
Cdd:cd06650    238 SYGMdsrppmaifELLDYIVNEPPPKLPSGVFSLEFQ 274
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
2774-3010 1.77e-16

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK 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: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 82.49  E-value: 1.77e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHELGILQNLQH----PLLVSLLDTFETPTSYVLVLEMAD 2845
Cdd:cd05606      2 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetlALNERIMLSLVSTggdcPFIVCMTYAFQTPDKLCFILDLMN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2846 QGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTyYIHQLL 2925
Cdd:cd05606     82 GGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEH---GHVRISDLGLACDFSKK-KPHASV 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2926 GNPEFAAPEIIL-GNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETcLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQ 3004
Cdd:cd05606    158 GTHGYMAPEVLQkGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKDK-HEIDRMTLTMNVELPDSFSPELKSLLEGLLQ 236

                   ....*.
gi 1907111721 3005 EDPAKR 3010
Cdd:cd05606    237 RDVSKR 242
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
755-982 1.79e-16

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 80.95  E-value: 1.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  755 QLRIFERDAidiiSDLESWNDELSQQMNDFDT-EDLTIAEQRLQHHADKALTMNNltfdviHQGQdllqyVNEVQASGvE 833
Cdd:cd00176      1 KLQQFLRDA----DELEAWLSEKEELLSSTDYgDDLESVEALLKKHEALEAELAA------HEER-----VEALNELG-E 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  834 LLCDRDVDMATRVQDLLEFLHEKQQELDLAAEQHRKHLEQCVQLRHLQAEVKQVLGWIRNGESMLNAGLITaSSLQEAEQ 913
Cdd:cd00176     65 QLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLG-KDLESVEE 143
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  914 LQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDM-IRDCAEKVASHWQQLMLKMEDRLKLVNASV 982
Cdd:cd00176    144 LLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEEAL 213
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
2656-2735 1.81e-16

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 76.45  E-value: 1.81e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2656 PPEFVIPLSEVTCETGETVVFRCRVCGRPKASITWKGPEHNTLNNddHYSISYSDIGEATLKIIGVSTEDDGIYTCIAVN 2735
Cdd:pfam13927    1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSG--STRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
2768-3049 1.93e-16

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 86.71  E-value: 1.93e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMK---RDQVTHELGILQNLQHPLLVSLLDTFETPTS---YVLvL 2841
Cdd:PTZ00266    15 YEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKereKSQLVIEVNVMRELKHKNIVRYIDRFLNKANqklYIL-M 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2842 EMADQGRL----LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNC-------RIAHLDLKPENILVDQSL----------- 2899
Cdd:PTZ00266    94 EFCDAGDLsrniQKCYKMFGKIEEHAIVDITRQLLHALAYCHNLkdgpngeRVLHRDLKPQNIFLSTGIrhigkitaqan 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2900 ---AKPTIKLADFGDAVQLNTTYYIHQLLGNPEFAAPEIILGNPVSL--TADTWSVGVLTYVLLSGVSPFlddsveETCL 2974
Cdd:PTZ00266   174 nlnGRPIAKIGDFGLSKNIGIESMAHSCVGTPYYWSPELLLHETKSYddKSDMWALGCIIYELCSGKTPF------HKAN 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2975 NICRLDFSF---PEDYFQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQ------AGNGSGKGTGVLDTSRLTSFIE 3045
Cdd:PTZ00266   248 NFSQLISELkrgPDLPIKGKSKELNILIKNLLNLSAKERPSALQCLGYQIIKnvgppvGAAGGGAGVAAAPGAVVARRNP 327

                   ....
gi 1907111721 3046 RRKH 3049
Cdd:PTZ00266   328 SKEH 331
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
2774-3025 2.49e-16

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK 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: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 83.64  E-value: 2.49e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVV-KKCDQKGTKRAVATKFVN--KKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTS------YVLVLEMa 2844
Cdd:cd07853      8 IGYGAFGVVwSVTDPRDGKRVALKKMPNvfQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPHIdpfeeiYVVTELM- 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 dQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDA--VQLNTTYYIH 2922
Cdd:cd07853     87 -QSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNC---VLKICDFGLArvEEPDESKHMT 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2923 QLLGNPEFAAPEIILGNPVSLTA-DTWSVGVLTYVLLSGVSPFLDDS-VEETCLNICRLDFSFPEDYFQ----------- 2989
Cdd:cd07853    163 QEVVTQYYRAPEILMGSRHYTSAvDIWSVGCIFAELLGRRILFQAQSpIQQLDLITDLLGTPSLEAMRSacegarahilr 242
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907111721 2990 ----------------GVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQAG 3025
Cdd:cd07853    243 gphkppslpvlytlssQATHEAVHLLCRMLVFDPDKRISAADALAHPYLDEG 294
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
2768-3022 2.67e-16

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. 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 CDK4 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: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 82.32  E-value: 2.67e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFV----NKKLMKRDQVtHELGILQNLQ---HPLLVSLLDTFET-----PT 2835
Cdd:cd07863      2 YEPVAEIGVGAYGTVYKARDPHSGHFVALKSVrvqtNEDGLPLSTV-REVALLKRLEafdHPNIVRLMDVCATsrtdrET 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2836 SYVLVLEMADQG--RLLDCVVRWGsLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAv 2913
Cdd:cd07863     81 KVTLVFEHVDQDlrTYLDKVPPPG-LPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVT---SGGQVKLADFGLA- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2914 qlntTYYIHQLLGNPE-----FAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRL--------- 2979
Cdd:cd07863    156 ----RIYSCQMALTPVvvtlwYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLiglppeddw 231
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907111721 2980 --DFSFPEDYFQ------------GVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd07863    232 prDVTLPRGAFSprgprpvqsvvpEIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
2766-2976 3.02e-16

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 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: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 83.52  E-value: 3.02e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2766 AFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTH---ELGILQNLQHPLLVSLLDTFETPTSYVLVL 2841
Cdd:cd05626      1 SMFVKIKTLGIGAFGEVCLACKVDTHALYAMKTLRKKdVLNRNQVAHvkaERDILAEADNEWVVKLYYSFQDKDNLYFVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2842 EMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQL----NT 2917
Cdd:cd05626     81 DYIPGGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILID---LDGHIKLTDFGLCTGFrwthNS 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2918 TYY--------------------------------------------IHQLLGNPEFAAPEIILGNPVSLTADTWSVGVL 2953
Cdd:cd05626    158 KYYqkgshirqdsmepsdlwddvsncrcgdrlktleqratkqhqrclAHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVI 237
                          250       260
                   ....*....|....*....|...
gi 1907111721 2954 TYVLLSGVSPFLDDSVEETCLNI 2976
Cdd:cd05626    238 LFEMLVGQPPFLAPTPTETQLKV 260
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
2768-2992 3.66e-16

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 82.35  E-value: 3.66e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVT--HELGILQNLQHPLLVSLLDTFETPTSYVLVLEMAD 2845
Cdd:cd07872      8 YIKLEKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTaiREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLD 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2846 QG---RLLDCvvrwGS-LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFG--DAVQLNTTY 2919
Cdd:cd07872     88 KDlkqYMDDC----GNiMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINE---RGELKLADFGlaRAKSVPTKT 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907111721 2920 YIHQLLgNPEFAAPEIILGNP-VSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVS 2992
Cdd:cd07872    161 YSNEVV-TLWYRPPDVLLGSSeYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRLLGTPTEETWPGIS 233
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
2759-3022 3.93e-16

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK 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: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 81.61  E-value: 3.93e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2759 TWKDNFdafysevAELGRGRFAVVKKCDQKGTKRAVATKFVN-KKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSY 2837
Cdd:cd06657     20 TYLDNF-------IKIGEGSTGIVCIATVKSSGKLVAVKKMDlRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDEL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2838 VLVLEMADQGRLLDcVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNT 2917
Cdd:cd06657     93 WVVMEFLEGGALTD-IVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHD---GRVKLSDFGFCAQVSK 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2918 TYYIHQ-LLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETcLNICRLDFSFPEDYFQGVSQKAK 2996
Cdd:cd06657    169 EVPRRKsLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKA-MKMIRDNLPPKLKNLHKVSPSLK 247
                          250       260
                   ....*....|....*....|....*.
gi 1907111721 2997 EFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd06657    248 GFLDRLLVRDPAQRATAAELLKHPFL 273
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
2774-3023 4.05e-16

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 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: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 81.28  E-value: 4.05e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVN------KKLMKRDQVTHELGILQNLQHPLLVS----LLDTFETptSYVLVLEM 2843
Cdd:cd06651     15 LGQGAFGRVYLCYDVDTGRELAAKQVQfdpespETSKEVSALECEIQLLKNLQHERIVQyygcLRDRAEK--TLTIFMEY 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTYY--- 2920
Cdd:cd06651     93 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSA---GNVKLGDFGASKRLQTICMsgt 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2921 -IHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDyfQGVSQKAKEFV 2999
Cdd:cd06651    170 gIRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLP--SHISEHARDFL 247
                          250       260
                   ....*....|....*....|....
gi 1907111721 3000 CFLLQEdPAKRPSAALALQEQWLQ 3023
Cdd:cd06651    248 GCIFVE-ARHRPSAEELLRHPFAQ 270
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
2774-3022 4.26e-16

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK 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: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 81.30  E-value: 4.26e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHE-LGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLlDC 2852
Cdd:cd06624     16 LGKGTFGVVYAARDLSTQVRIAIKEIPERDSREVQPLHEeIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGGSL-SA 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2853 VVR--WGSLT--EGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlaKPTIKLADFGDAVQL-----NTTYYIhq 2923
Cdd:cd06624     95 LLRskWGPLKdnENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTY--SGVVKISDFGTSKRLaginpCTETFT-- 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2924 llGNPEFAAPEII------LGNPvsltADTWSVGVLTYVLLSGVSPFLDDSVEETCLnicrldfsFPEDYFQ-------G 2990
Cdd:cd06624    171 --GTLQYMAPEVIdkgqrgYGPP----ADIWSLGCTIIEMATGKPPFIELGEPQAAM--------FKVGMFKihpeipeS 236
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1907111721 2991 VSQKAKEFV--CFllQEDPAKRPSAALALQEQWL 3022
Cdd:cd06624    237 LSEEAKSFIlrCF--EPDPDKRATASDLLQDPFL 268
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
2773-3012 4.56e-16

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 80.65  E-value: 4.56e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  2773 ELGRGRFAVVKKCD----QKGTKRAVATKFVNKKLMK--RDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQ 2846
Cdd:smart00219    6 KLGEGAFGEVYKGKlkgkGGKKKVEVAVKTLKEDASEqqIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVMEYMEG 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  2847 GRLLDCVV-RWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQLNTTYYIHQLL 2925
Cdd:smart00219   86 GDLLSYLRkNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENL---VVKISDFGLSRDLYDDDYYRKRG 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  2926 GN-PEF-AAPEIILGNPVSLTADTWSVGVLTYVLLS-GVSPFLDDSVEETCLNI---CRLDF--SFPEDYFQGVSQkake 2997
Cdd:smart00219  163 GKlPIRwMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEYLkngYRLPQppNCPPELYDLMLQ---- 238
                           250
                    ....*....|....*
gi 1907111721  2998 fvCFllQEDPAKRPS 3012
Cdd:smart00219  239 --CW--AEDPEDRPT 249
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
2664-2748 5.23e-16

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 75.23  E-value: 5.23e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  2664 SEVTCETGETVVFRCRVCGRPKASITWKGPEHNTLNNDDHYSISYSDiGEATLKIIGVSTEDDGIYTCIAVNDMGSASSS 2743
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSG-STSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                    ....*
gi 1907111721  2744 ASLRV 2748
Cdd:smart00410   81 TTLTV 85
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
2768-3014 5.72e-16

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 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: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 80.43  E-value: 5.72e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKK--CDQKGTKRAVA---TKFVNKKLMKR--DQV-THElgilQNLQHPLLVSLLDTFETPTSYVL 2839
Cdd:cd14050      3 FTILSKLGEGSFGEVFKvrSREDGKLYAVKrsrSRFRGEKDRKRklEEVeRHE----KLGEHPNCVRFIKAWEEKGILYI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2840 VLEMADQGrLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTY 2919
Cdd:cd14050     79 QTELCDTS-LQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKD---GVCKLGDFGLVVELDKED 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2920 YIHQLLGNPEFAAPEIILGNPvSLTADTWSVGVltyvllsgvspflddsveeTCLNI-CRLDFS-------------FPE 2985
Cdd:cd14050    155 IHDAQEGDPRYMAPELLQGSF-TKAADIFSLGI-------------------TILELaCNLELPsggdgwhqlrqgyLPE 214
                          250       260
                   ....*....|....*....|....*....
gi 1907111721 2986 DYFQGVSQKAKEFVCFLLQEDPAKRPSAA 3014
Cdd:cd14050    215 EFTAGLSPELRSIIKLMMDPDPERRPTAE 243
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
2766-2976 5.81e-16

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 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: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 82.79  E-value: 5.81e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2766 AFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKK-LMKRDQVTH---ELGILQNLQHPLLVSLLDTFETPTSYVLVL 2841
Cdd:cd05625      1 SMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKdVLLRNQVAHvkaERDILAEADNEWVVRLYYSFQDKDNLYFVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2842 EMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQL----NT 2917
Cdd:cd05625     81 DYIPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRD---GHIKLTDFGLCTGFrwthDS 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2918 TYY--------------------------------------------IHQLLGNPEFAAPEIILGNPVSLTADTWSVGVL 2953
Cdd:cd05625    158 KYYqsgdhlrqdsmdfsnewgdpencrcgdrlkplerraarqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVI 237
                          250       260
                   ....*....|....*....|...
gi 1907111721 2954 TYVLLSGVSPFLDDSVEETCLNI 2976
Cdd:cd05625    238 LFEMLVGQPPFLAQTPLETQMKV 260
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
2773-3012 5.91e-16

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 80.29  E-value: 5.91e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  2773 ELGRGRFAVVKKC----DQKGTKRAVATKFVNKKLMK--RDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQ 2846
Cdd:smart00221    6 KLGEGAFGEVYKGtlkgKGDGKEVEVAVKTLKEDASEqqIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVMEYMPG 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  2847 GRLLDCVV--RWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQLNTTYYIHQL 2924
Cdd:smart00221   86 GDLLDYLRknRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENL---VVKISDFGLSRDLYDDDYYKVK 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  2925 LGN-PEF-AAPEIILGNPVSLTADTWSVGVLTYVLLS-GVSPFLDDSVEETCLNI---CRLDF--SFPEDYFQGVSQkak 2996
Cdd:smart00221  163 GGKlPIRwMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEPYPGMSNAEVLEYLkkgYRLPKppNCPPELYKLMLQ--- 239
                           250
                    ....*....|....*.
gi 1907111721  2997 efvCFllQEDPAKRPS 3012
Cdd:smart00221  240 ---CW--AEDPEDRPT 250
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
2790-2960 1.01e-15

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 84.51  E-value: 1.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2790 TKRAVATKFVN----KKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVL-VLEMADQGRLLDCVVRWGSLTEGKV 2864
Cdd:TIGR03903    2 TGHEVAIKLLRtdapEEEHQRARFRRETALCARLYHPNIVALLDSGEAPPGLLFaVFEYVPGRTLREVLAADGALPAGET 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2865 RAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFG-----------DAVQLNTTyyiHQLLGNPEFAAP 2933
Cdd:TIGR03903   82 GRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPHAKVLDFGigtllpgvrdaDVATLTRT---TEVLGTPTYCAP 158
                          170       180
                   ....*....|....*....|....*..
gi 1907111721 2934 EIILGNPVSLTADTWSVGVLTYVLLSG 2960
Cdd:TIGR03903  159 EQLRGEPVTPNSDLYAWGLIFLECLTG 185
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
2774-3024 1.90e-15

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 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: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 80.68  E-value: 1.90e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATK-----FVNKKlmkrD-QVTH-ELGILQNL-QHPLLVSLLDTF--ETPTSYVLVLEM 2843
Cdd:cd07852     15 LGKGAYGIVWKAIDKKTGEVVALKkifdaFRNAT----DaQRTFrEIMFLQELnDHPNIIKLLNVIraENDKDIYLVFEY 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQGrlLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQLNT------ 2917
Cdd:cd07852     91 METD--LHAVIRANILEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLN---SDCRVKLADFGLARSLSQleedde 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2918 ----TYYIhqllgnpefA-----APEIILGNPVSLTA-DTWSVGVLTYVLLSG--------------------------- 2960
Cdd:cd07852    166 npvlTDYV---------AtrwyrAPEILLGSTRYTKGvDMWSVGCILGEMLLGkplfpgtstlnqlekiievigrpsaed 236
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907111721 2961 ----VSPFLDDSVEETClniCRLDFSFPEdYFQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQA 3024
Cdd:cd07852    237 iesiQSPFAATMLESLP---PSRPKSLDE-LFPKASPDALDLLKKLLVFNPNKRLTAEEALRHPYVAQ 300
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
2774-2968 2.21e-15

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. 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 CDKL5 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: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 79.27  E-value: 2.21e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVA-TKFVNKKLMK--RDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLL 2850
Cdd:cd07848      9 VGEGAYGVVLKCRHKETKEIVAiKKFKDSEENEevKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVEKNMLE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2851 DCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQL------NTTYYIhql 2924
Cdd:cd07848     89 LLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLIS---HNDVLKLCDFGFARNLsegsnaNYTEYV--- 162
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1907111721 2925 lGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDS 2968
Cdd:cd07848    163 -ATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGES 205
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
2768-3018 2.65e-15

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK 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: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 79.24  E-value: 2.65e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTH--ELGILQNLQ-HPLLVSLLDT-FETPT-SYVLVLE 2842
Cdd:cd07831      1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKHFKSLEQVNNlrEIQALRRLSpHPNILRLIEVlFDRKTgRLALVFE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 MAD-------QGRLldcvvrwGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakpTIKLADFGDAVQL 2915
Cdd:cd07831     81 LMDmnlyeliKGRK-------RPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD----ILKLADFGSCRGI 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2916 NT----TYYIhqllGNPEFAAPEIILGNPV-SLTADTWSVGVLTYVLLSGVSPF-----LDD-------------SVEET 2972
Cdd:cd07831    150 YSkppyTEYI----STRWYRAPECLLTDGYyGPKMDIWAVGCVFFEILSLFPLFpgtneLDQiakihdvlgtpdaEVLKK 225
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907111721 2973 CLNICRLDFSFPEDYFQG-------VSQKAKEFVCFLLQEDPAKRPSAALALQ 3018
Cdd:cd07831    226 FRKSRHMNYNFPSKKGTGlrkllpnASAEGLDLLKKLLAYDPDERITAKQALR 278
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
2773-2935 2.77e-15

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK 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: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 78.42  E-value: 2.77e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRAVA-TKFVNKKLMK--RDQVTHELGILQNLQHPLLVSLLDTFETP--TSYVLVLEMADQG 2847
Cdd:cd13983      8 VLGRGSFKTVYRAFDTEEGIEVAwNEIKLRKLPKaeRQRFKQEIEILKSLKHPNIIKFYDSWESKskKEVIFITELMTSG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2848 RLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCR--IAHLDLKPENILVDQSLAKptIKLADFGDAVQLNTTYyIHQLL 2925
Cdd:cd13983     88 TLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINGNTGE--VKIGDLGLATLLRQSF-AKSVI 164
                          170
                   ....*....|
gi 1907111721 2926 GNPEFAAPEI 2935
Cdd:cd13983    165 GTPEFMAPEM 174
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
2754-2953 2.91e-15

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 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: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 79.51  E-value: 2.91e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2754 DGIVVTWKDNFDafYSEVAELGRGRFAVVKKCDQKGTKRAVATKF---VNKKLMKRdqvthELGILQNLQ-HPLLVSLLD 2829
Cdd:cd14132      8 ENLNVEWGSQDD--YEIIRKIGRGKYSEVFEGINIGNNEKVVIKVlkpVKKKKIKR-----EIKILQNLRgGPNIVKLLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2830 TFETPTS--YVLVLEMADQgrlLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlaKPTIKLA 2907
Cdd:cd14132     81 VVKDPQSktPSLIFEYVNN---TDFKTLYPTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHE--KRKLRLI 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907111721 2908 DFGDAvqlntTYYIHqllgNPE---------FAAPEIILGNPV---SLtaDTWSVGVL 2953
Cdd:cd14132    156 DWGLA-----EFYHP----GQEynvrvasryYKGPELLVDYQYydySL--DMWSLGCM 202
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
42-172 3.25e-15

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 75.45  E-value: 3.25e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721   42 AYLSGGRDKRGGPILTFPAR-SNHDRIRQEDLRRLISYL--ACIPSEEVCKRGFTVIVDMRGSKW------DSIKPLLKI 112
Cdd:cd00170     11 IGYLGGRDKEGRPVLVFRAGwDPPKLLDLEELLRYLVYLleKALRELEEQVEGFVVIIDLKGFSLsnlsdlSLLKKLLKI 90
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  113 LQESFPCCIHIALIIKPDNF----WQ------KQRTnfgSSKFEFETNmvSLEGLTKVVDPSQLTPEFDG 172
Cdd:cd00170     91 LQDHYPERLKKIYIVNAPWIfsalWKivkpflSEKT---RKKIVFLGS--DLEELLEYIDPDQLPKELGG 155
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
2774-3010 3.34e-15

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 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: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 80.11  E-value: 3.34e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHE---LGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQ 2846
Cdd:cd05633     13 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetlALNErimLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNG 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2847 GRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQLNTTyYIHQLLG 2926
Cdd:cd05633     93 GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDE---HGHVRISDLGLACDFSKK-KPHASVG 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2927 NPEFAAPEIIL-GNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETcLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQE 3005
Cdd:cd05633    169 THGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK-HEIDRMTLTVNVELPDSFSPELKSLLEGLLQR 247

                   ....*
gi 1907111721 3006 DPAKR 3010
Cdd:cd05633    248 DVSKR 252
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
188-413 3.64e-15

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 77.10  E-value: 3.64e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  188 FEEYISNAAHMLSRLEELQDVLAKKELPQDLEGARNMIDEHSQLKK--KVIKAPIEDLDLEGQKLLQriqssdsfpkknS 265
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAelAAHEERVEALNELGEQLIE------------E 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  266 GSGNADlqnllpKVSTMLDRLHSTRQHLHQMWHVRKLKLDQCFQLRLFEQDAEKMFDWIThNKGLFLNSyTEIGTSHPHA 345
Cdd:cd00176     70 GHPDAE------EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLE-EKEAALAS-EDLGKDLESV 141
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907111721  346 MELQTQHNHFAMNCMNVYVNINRIMSVANRLVESGHYASQ-QIKQIANQLEQEWKAFAAALDERSTLLD 413
Cdd:cd00176    142 EELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQKKLE 210
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
2768-3021 4.62e-15

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: 78.54  E-value: 4.62e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKC-DQKGTKRAVATKFVNKKLMKRD---QVTHELGILQNLQ---HPLLVSLLDT-----FETPT 2835
Cdd:cd07862      3 YECVAEIGEGAYGKVFKArDLKNGGRFVALKRVRVQTGEEGmplSTIREVAVLRHLEtfeHPNVVRLFDVctvsrTDRET 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2836 SYVLVLEMADQG--RLLDCVVRWGSLTEgKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDA- 2912
Cdd:cd07862     83 KLTLVFEHVDQDltTYLDKVPEPGVPTE-TIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSS---GQIKLADFGLAr 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2913 ---VQLNTTYYIHQLLgnpeFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDS-VEETCLNICRLDFSFPEDYF 2988
Cdd:cd07862    159 iysFQMALTSVVVTLW----YRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSdVDQLGKILDVIGLPGEEDWP 234
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907111721 2989 Q--GVSQKA--------------------KEFVCFLLQEDPAKRPSAALALQEQW 3021
Cdd:cd07862    235 RdvALPRQAfhsksaqpiekfvtdidelgKDLLLKCLTFNPAKRISAYSALSHPY 289
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
2774-2951 5.13e-15

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 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: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 79.29  E-value: 5.13e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNL-QHP-----LLVSLLDTFETPTSYVLVLEMADQG 2847
Cdd:cd14226     21 IGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMnKHDtenkyYIVRLKRHFMFRNHLCLVFELLSYN 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2848 rLLDCV--VRWGSLTEGKVRAHLGEVLEAVRYLH--NCRIAHLDLKPENILVDQSlAKPTIKLADFGDAVQLNTTyyIHQ 2923
Cdd:cd14226    101 -LYDLLrnTNFRGVSLNLTRKFAQQLCTALLFLStpELSIIHCDLKPENILLCNP-KRSAIKIIDFGSSCQLGQR--IYQ 176
                          170       180
                   ....*....|....*....|....*...
gi 1907111721 2924 LLGNPEFAAPEIILGNPVSLTADTWSVG 2951
Cdd:cd14226    177 YIQSRFYRSPEVLLGLPYDLAIDMWSLG 204
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
2774-3010 5.22e-15

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 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: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 78.94  E-value: 5.22e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQ----VTHE---LGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQ 2846
Cdd:cd14223      8 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetlALNErimLSLVSTGDCPFIVCMSYAFHTPDKLSFILDLMNG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2847 GRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQLNTTyYIHQLLG 2926
Cdd:cd14223     88 GDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDE---FGHVRISDLGLACDFSKK-KPHASVG 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2927 NPEFAAPEIIL-GNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETcLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQE 3005
Cdd:cd14223    164 THGYMAPEVLQkGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK-HEIDRMTLTMAVELPDSFSPELRSLLEGLLQR 242

                   ....*
gi 1907111721 3006 DPAKR 3010
Cdd:cd14223    243 DVNRR 247
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
2774-2966 7.47e-15

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP 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: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 77.49  E-value: 7.47e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNK---KLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLL 2850
Cdd:cd13978      1 LGSGGFGTVSKARHVSWFGMVAIKCLHSspnCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2851 DCVVRWGSLTEGKVRAH-LGEVLEAVRYLHNCR--IAHLDLKPENILVDQSLakpTIKLADFGDAV------QLNTTYYI 2921
Cdd:cd13978     81 SLLEREIQDVPWSLRFRiIHEIALGMNFLHNMDppLLHHDLKPENILLDNHF---HVKISDFGLSKlgmksiSANRRRGT 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1907111721 2922 HQLLGNPEFAAPEIIlgNPV----SLTADTWSVGVLTYVLLSGVSPFLD 2966
Cdd:cd13978    158 ENLGGTPIYMAPEAF--DDFnkkpTSKSDVYSFAIVIWAVLTRKEPFEN 204
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
2771-3023 1.36e-14

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin 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: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 77.34  E-value: 1.36e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2771 VAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNL-QHPLLVSLLDTFETPTSYV-----LVLEMA 2844
Cdd:cd06639     27 IETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVDEEIEAEYNILRSLpNHPNVVKFYGMFYKADQYVggqlwLVLELC 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 DQGRLLDCV---VRWGS-LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQLNTTYY 2920
Cdd:cd06639    107 NGGSVTELVkglLKCGQrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLT---TEGGVKLVDFGVSAQLTSARL 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2921 IHQL-LGNPEFAAPEII-----LGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICR---LDFSFPEDYFQGV 2991
Cdd:cd06639    184 RRNTsVGTPFWMAPEVIaceqqYDYSYDARCDVWSLGITAIELADGDPPLFDMHPVKALFKIPRnppPTLLNPEKWCRGF 263
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1907111721 2992 SQkakeFVCFLLQEDPAKRPSAALALQEQWLQ 3023
Cdd:cd06639    264 SH----FISQCLIKDFEKRPSVTHLLEHPFIK 291
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
2771-3019 1.57e-14

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk 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: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 76.14  E-value: 1.57e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2771 VAELGRGRFAVVKKCDQKgTKRAVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLL 2850
Cdd:cd05112      9 VQEIGSGQFGLVHLGYWL-NKDKVAIKTIREGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGCLS 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2851 DCV-VRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFG-DAVQLNTTYYIHQLLGNP 2928
Cdd:cd05112     88 DYLrTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGEN---QVVKVSDFGmTRFVLDDQYTSSTGTKFP 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2929 -EFAAPEIILGNPVSLTADTWSVGVLTYVLLS-GVSPFLDDSVEETclnICRLDFSFPEDYFQGVSQKAKEFVCFLLQED 3006
Cdd:cd05112    165 vKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYENRSNSEV---VEDINAGFRLYKPRLASTHVYEIMNHCWKER 241
                          250
                   ....*....|...
gi 1907111721 3007 PAKRPSAALALQE 3019
Cdd:cd05112    242 PEDRPSFSLLLRQ 254
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
2768-3021 1.57e-14

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. 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 BUR1 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: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 77.35  E-value: 1.57e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKfvnKKLMKRDQ----VT--HELGILQNLQHPLLVSLLDTF--------ET 2833
Cdd:cd07866     10 YEILGKLGEGTFGEVYKARQIKTGRVVALK---KILMHNEKdgfpITalREIKILKKLKHPNVVPLIDMAverpdkskRK 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2834 PTSYVLVLEMADQ---GRLLDCVVRwgsLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFG 2910
Cdd:cd07866     87 RGSVYMVTPYMDHdlsGLLENPSVK---LTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDN---QGILKIADFG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2911 davqLNTTYY--IHQLLGNPE--------------FAAPEIILGNPVSLTA-DTWSVG-VLTYV-----LLSGVS----- 2962
Cdd:cd07866    161 ----LARPYDgpPPNPKGGGGggtrkytnlvvtrwYRPPELLLGERRYTTAvDIWGIGcVFAEMftrrpILQGKSdidql 236
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907111721 2963 ---------PFLDDSVEETCLNICRLDFSFP------EDYFQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQW 3021
Cdd:cd07866    237 hlifklcgtPTEETWPGWRSLPGCEGVHSFTnyprtlEERFGKLGPEGLDLLSKLLSLDPYKRLTASDALEHPY 310
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
2868-3016 1.73e-14

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 77.15  E-value: 1.73e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2868 LGEVLEAVRYLHNCRIAHLDLKPENILVD-QSLAKPTIKLADFG-----DAVQLNTTYYIHQ--LLGNPEFAAPEIILGN 2939
Cdd:cd14018    144 ILQLLEGVDHLVRHGIAHRDLKSDNILLElDFDGCPWLVIADFGccladDSIGLQLPFSSWYvdRGGNACLMAPEVSTAV 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2940 PVSLT------ADTWSVGVLTYVLLSGVSPF--LDDSVEETClnicrldfSFPEDYFQGVSQK----AKEFVCFLLQEDP 3007
Cdd:cd14018    224 PGPGVvinyskADAWAVGAIAYEIFGLSNPFygLGDTMLESR--------SYQESQLPALPSAvppdVRQVVKDLLQRDP 295

                   ....*....
gi 1907111721 3008 AKRPSAALA 3016
Cdd:cd14018    296 NKRVSARVA 304
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
2768-3022 2.07e-14

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 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: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 77.23  E-value: 2.07e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATK-----FVNKKLMKRdqVTHELGILQNLQHPLLVSLLDTFETPTSYV-LVL 2841
Cdd:cd07856     12 YSDLQPVGMGAFGLVCSARDQLTGQNVAVKkimkpFSTPVLAKR--TYRELKLLKHLRHENIISLSDIFISPLEDIyFVT 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2842 EMadQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDA-VQ------ 2914
Cdd:cd07856     90 EL--LGTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENC---DLKICDFGLArIQdpqmtg 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2915 -LNTTYYihqllgnpefAAPEIILG-NPVSLTADTWSVGVLTYVLLSG---------------VSPFLDDSVEETCLNIC 2977
Cdd:cd07856    165 yVSTRYY----------RAPEIMLTwQKYDVEVDIWSAGCIFAEMLEGkplfpgkdhvnqfsiITELLGTPPDDVINTIC 234
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907111721 2978 R---LDF--SFPEDYFQGVSQK-------AKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd07856    235 SentLRFvqSLPKRERVPFSEKfknadpdAIDLLEKMLVFDPKKRISAAEALAHPYL 291
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
2774-3023 2.29e-14

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK 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: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 77.18  E-value: 2.29e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATK-----FVNKKLMKRdqVTHELGILQNLQHPLLVSLLDTFeTPTSYV------LVLE 2842
Cdd:cd07834      8 IGSGAYGVVCSAYDKRTGRKVAIKkisnvFDDLIDAKR--ILREIKILRHLKHENIIGLLDIL-RPPSPEefndvyIVTE 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 MADQGrlLDCVVRWGS-LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQLNTTYYI 2921
Cdd:cd07834     85 LMETD--LHKVIKSPQpLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNC---DLKICDFGLARGVDPDEDK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2922 HQLlgnPEFA------APEIILGNP-VSLTADTWSVG------VLTYVLLSGVS--------------PFLDDSVEETCL 2974
Cdd:cd07834    160 GFL---TEYVvtrwyrAPELLLSSKkYTKAIDIWSVGcifaelLTRKPLFPGRDyidqlnlivevlgtPSEEDLKFISSE 236
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907111721 2975 NICRLDFSFPE-------DYFQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQ 3023
Cdd:cd07834    237 KARNYLKSLPKkpkkplsEVFPGASPEAIDLLEKMLVFNPKKRITADEALAHPYLA 292
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
2768-3011 2.31e-14

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 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: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 76.00  E-value: 2.31e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFA-VVKKCDQKGTKRAVATKFVN-------KKLMKRDQ----VTHELGIL-QNLQHPLLVSLLDTFETP 2834
Cdd:cd08528      2 YAVLELLGSGAFGcVYKVRKKSNGQTLLALKEINmtnpafgRTEQERDKsvgdIISEVNIIkEQLRHPNIVRYYKTFLEN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2835 TSYVLVLEMADQGRLLDCVV----RWGSLTEGKVRAHLGEVLEAVRYLHNCR-IAHLDLKPENILVDQSlAKPTIklADF 2909
Cdd:cd08528     82 DRLYIVMELIEGAPLGEHFSslkeKNEHFTEDRIWNIFVQMVLALRYLHKEKqIVHRDLKPNNIMLGED-DKVTI--TDF 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2910 GDAVQ-LNTTYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFS-FPEDY 2987
Cdd:cd08528    159 GLAKQkGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEYEpLPEGM 238
                          250       260
                   ....*....|....*....|....
gi 1907111721 2988 FqgvSQKAKEFVCFLLQEDPAKRP 3011
Cdd:cd08528    239 Y---SDDITFVIRSCLTPDPEARP 259
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
2773-3012 2.35e-14

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 75.61  E-value: 2.35e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKC----DQKGTKRAVATKFVNKKLMKRDQV--THELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQ 2846
Cdd:pfam07714    6 KLGEGAFGEVYKGtlkgEGENTKIKVAVKTLKEGADEEEREdfLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEYMPG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2847 GRLLDcvvrwgsltegKVRAHLG------------EVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQ 2914
Cdd:pfam07714   86 GDLLD-----------FLRKHKRkltlkdllsmalQIAKGMEYLESKNFVHRDLAARNCLVSE---NLVVKISDFGLSRD 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2915 LNTTYYIHQLLG---NPEFAAPEIILGNPVSLTADTWSVGVLTYVLLS-GVSPFLDDSVEETCLNI---CRLDFSF--PE 2985
Cdd:pfam07714  152 IYDDDYYRKRGGgklPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEFLedgYRLPQPEncPD 231
                          250       260
                   ....*....|....*....|....*..
gi 1907111721 2986 DYFQGVSQkakefvCflLQEDPAKRPS 3012
Cdd:pfam07714  232 ELYDLMKQ------C--WAYDPEDRPT 250
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
2795-3014 2.40e-14

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated 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. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 76.28  E-value: 2.40e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2795 ATKFVNKKLMK------RDQVTHELGILQNLQHPLLVSLlDTFETPTSYVLVLEMADQGRLLdcvvrwGSLTEGKVRAHL 2868
Cdd:cd14001     32 AVKKINSKCDKgqrslyQERLKEEAKILKSLNHPNIVGF-RAFTKSEDGSLCLAMEYGGKSL------NDLIEERYEAGL 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2869 G------------EVLEAVRYLHN-CRIAHLDLKPENILVDQSLAkpTIKLADFGDAVQLNTTYyihQLLGNPEF----- 2930
Cdd:cd14001    105 GpfpaatilkvalSIARALEYLHNeKKILHGDIKSGNVLIKGDFE--SVKLCDFGVSLPLTENL---EVDSDPKAqyvgt 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2931 ---AAPEIIL-GNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETClnicRLDFSFPEDYFQGVS-------------- 2992
Cdd:cd14001    180 epwKAKEALEeGGVITDKADIFAYGLVLWEMMTLSVPHLNLLDIEDD----DEDESFDEDEEDEEAyygtlgtrpalnlg 255
                          250       260
                   ....*....|....*....|....*...
gi 1907111721 2993 ------QKAKEFVCFLLQEDPAKRPSAA 3014
Cdd:cd14001    256 elddsyQKVIELFYACTQEDPKDRPSAA 283
PH_Obscurin cd13239
Obscurin pleckstrin homology (PH) domain; Obscurin (also called Obscurin-RhoGEF; ...
1440-1561 2.81e-14

Obscurin pleckstrin homology (PH) domain; Obscurin (also called Obscurin-RhoGEF; Obscurin-myosin light chain kinase/Obscurin-MLCK) is a giant muscle protein that is concentrated at the peripheries of Z-disks and M-lines. It binds small ankyrin I, a component of the sarcoplasmic reticulum (SR) membrane. It is associated with the contractile apparatus through binding with titin and sarcomeric myosin. It plays important roles in the organization and assembly of the myofibril and the SR. Obscurin has been observed as alternatively-spliced isoforms. The major isoform in sleletal muscle, approximately 800 kDa in size, is composed of many adhesion modules and signaling domains. It harbors 49 Ig and 2 FNIII repeats at the N-terminues, a complex middle region with additional Ig domains, an IQ motif, and a conserved SH3 domain near RhoGEF and PH domains, and a non-modular C-terminus with phosphorylation motifs. The obscurin gene also encodes two kinase domains, which are not part of the 800 kDa form of the protein, but is part of smaller spliced products that present in heart muscle. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270059  Cd Length: 125  Bit Score: 71.81  E-value: 2.81e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1440 MLEGFDENIESQGELILQESFQVWDPKTLIR---KGRERHLFLFEMSLVFSKEVKDSSGRSK-YLYKSKLFTSELGVTEH 1515
Cdd:cd13239      1 LIENYPAPLQALGEPIRQGHFTVWEEAPEVKtssRGHHRHVFLFKNCVVICKPKRDSRTDTVtYVFKNKMKLSDIDVKDT 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1907111721 1516 VEGDPCKFALWVGRTpTSDNKIVLKASSIENKQDWIKHIREvIQER 1561
Cdd:cd13239     81 VEGDDRSFGLWHEHR-GSVRKYTLQARSAIIKSSWLKDLRD-LQQR 124
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
2773-2964 2.82e-14

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like 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: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 75.46  E-value: 2.82e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKK---CDQKGTKRAVATKFVNKKLMKRDQ--VTHELGILQNLQHPLLVSLLDTFETPtSYVLVLEMADQG 2847
Cdd:cd05060      2 ELGHGNFGSVRKgvyLMKSGKEVEVAVKTLKQEHEKAGKkeFLREASVMAQLDHPCIVRLIGVCKGE-PLMLVMELAPLG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2848 RLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdqsLAKPTIKLADFG--DAVQLNTTYYIHQLL 2925
Cdd:cd05060     81 PLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLL---VNRHQAKISDFGmsRALGAGSDYYRATTA 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907111721 2926 GN-P-EFAAPEIILGNPVSLTADTWSVGVLTYVLLS-GVSPF 2964
Cdd:cd05060    158 GRwPlKWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPY 199
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
2768-2992 2.86e-14

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 76.40  E-value: 2.86e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVnkKLMKRDQ-----VTHELGILQNLQHPLLVSLLDTFETPTSYVLVLE 2842
Cdd:PLN00009     4 YEKVEKIGEGTYGVVYKARDRVTNETIALKKI--RLEQEDEgvpstAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVFE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 MADqgrlLDCVVRWGSLTEGK-----VRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlaKPTIKLADFG--DAVQL 2915
Cdd:PLN00009    82 YLD----LDLKKHMDSSPDFAknprlIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRR--TNALKLADFGlaRAFGI 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907111721 2916 NTTYYIHQLLgNPEFAAPEIILGN-PVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQGVS 2992
Cdd:PLN00009   156 PVRTFTHEVV-TLWYRAPEILLGSrHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILGTPNEETWPGVT 232
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
2776-3022 2.96e-14

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. 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. The MAP3K8 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: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 75.43  E-value: 2.96e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2776 RGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVThelgILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDCVVR 2855
Cdd:cd13995     14 RGAFGKVYLAQDTKTKKRMACKLIPVEQFKPSDVE----IQACFRHENIAELYGALLWEETVHLFMEAGEGGSVLEKLES 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2856 WGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAkptiKLADFGDAVQL-NTTYYIHQLLGNPEFAAPE 2934
Cdd:cd13995     90 CGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKA----VLVDFGLSVQMtEDVYVPKDLRGTEIYMSPE 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2935 IILGNPVSLTADTWSVGVLTYVLLSGVSPFLD---DSVEETCLNICRLDFSFPEDYFQGVSQKAKEFVCFLLQEDPAKRP 3011
Cdd:cd13995    166 VILCRGHNTKADIYSLGATIIHMQTGSPPWVRrypRSAYPSYLYIIHKQAPPLEDIAQDCSPAMRELLEAALERNPNHRS 245
                          250
                   ....*....|.
gi 1907111721 3012 SAALALQEQWL 3022
Cdd:cd13995    246 SAAELLKHEAL 256
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
2760-3023 4.76e-14

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 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: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 75.84  E-value: 4.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2760 WKDNFDAFYSEVAELGRGRFAVVKKCDQKGTKRAVATK---FVNKKLMKRDQ-VTHELGILQNLQHPLLVSLLDTFETPT 2835
Cdd:cd06633     15 YKDDPEEIFVDLHEIGHGSFGAVYFATNSHTNEVVAIKkmsYSGKQTNEKWQdIIKEVKFLQQLKHPNTIEYKGCYLKDH 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2836 SYVLVLE--MADQGRLLDcvVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILvdqsLAKP-TIKLADFGDA 2912
Cdd:cd06633     95 TAWLVMEycLGSASDLLE--VHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNIL----LTEPgQVKLADFGSA 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2913 VQLNTTyyiHQLLGNPEFAAPEIILG---NPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDfsFPEDYFQ 2989
Cdd:cd06633    169 SIASPA---NSFVGTPYWMAPEVILAmdeGQYDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHIAQND--SPTLQSN 243
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1907111721 2990 GVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQ 3023
Cdd:cd06633    244 EWTDSFRGFVDYCLQKIPQERPSSAELLRHDFVR 277
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
2774-2999 6.14e-14

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 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: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 75.48  E-value: 6.14e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQ--------VTHELGILQNLQHPLLVSLLDTFETPT-SYVLVLEMA 2844
Cdd:cd14041     14 LGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEkkenyhkhACREYRIHKELDHPRIVKLYDYFSLDTdSFCTVLEYC 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 dQGRLLDCVVRWGSL-TEGKVRAHLGEVLEAVRYLHNCR--IAHLDLKPENILVDQSLAKPTIKLADFGDAVQLNTTYY- 2920
Cdd:cd14041     94 -EGNDLDFYLKQHKLmSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNGTACGEIKITDFGLSKIMDDDSYn 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2921 -------IHQLLGNPEFAAPE-IILGN---PVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLN----ICRLDFSFPE 2985
Cdd:cd14041    173 svdgmelTSQGAGTYWYLPPEcFVVGKeppKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQentiLKATEVQFPP 252
                          250
                   ....*....|....
gi 1907111721 2986 DyfQGVSQKAKEFV 2999
Cdd:cd14041    253 K--PVVTPEAKAFI 264
SPEC smart00150
Spectrin repeats;
1111-1211 9.08e-14

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 69.67  E-value: 9.08e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  1111 FERSAKQALEWIHDNGEfyLSTHTSTGSSIQHTQELLKEHEEFQITAKQTKERVKLLIQLADGFCEKGHAHAAEIKKCVT 1190
Cdd:smart00150    3 FLRDADELEAWLEEKEQ--LLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 1907111721  1191 AVDKRYRDFSLRMEKYRTSLE 1211
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
2771-3022 1.00e-13

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-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: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 74.26  E-value: 1.00e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2771 VAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNL-QHPLLVSLLDTFETPTSYV------LVLEM 2843
Cdd:cd06608     11 VEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEEEIKLEINILRKFsNHPNIATFYGAFIKKDPPGgddqlwLVMEY 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQGRLLDCV----VRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTY 2919
Cdd:cd06608     91 CGGGSVTDLVkglrKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEE---AEVKLVDFGVSAQLDSTL 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2920 YI-HQLLGNPEFAAPEIILGNPvSLTA------DTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLD---FSFPEDYfq 2989
Cdd:cd06608    168 GRrNTFIGTPYWMAPEVIACDQ-QPDAsydarcDVWSLGITAIELADGKPPLCDMHPMRALFKIPRNPpptLKSPEKW-- 244
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1907111721 2990 gvSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd06608    245 --SKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
2773-2978 1.04e-13

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 74.01  E-value: 1.04e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRaVATKFV-NKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLD 2851
Cdd:cd05148     13 KLGSGYFGEVWEGLWKNRVR-VAIKILkSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITELMEKGSLLA 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2852 CVvrwgSLTEGKVR--AHL----GEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQLNTTYYIHQLL 2925
Cdd:cd05148     92 FL----RSPEGQVLpvASLidmaCQVAEGMAYLEEQNSIHRDLAARNILVGEDL---VCKVADFGLARLIKEDVYLSSDK 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907111721 2926 GNP-EFAAPEIILGNPVSLTADTWSVGVLTYVLLS-GVSPFLDDSVEETCLNICR 2978
Cdd:cd05148    165 KIPyKWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNNHEVYDQITA 219
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
2768-2964 1.10e-13

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta 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: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 75.47  E-value: 1.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNK---KLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTS-------Y 2837
Cdd:cd07878     17 YQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRpfqSLIHARRTYRELRLLKHMKHENVIGLLDVFTPATSienfnevY 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2838 VLVLEMadqGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQLN- 2916
Cdd:cd07878     97 LVTNLM---GADLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDC---ELRILDFGLARQADd 170
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2917 -TTYYIhqllGNPEFAAPEIILG-NPVSLTADTWSVGVLTYVLLSGVSPF 2964
Cdd:cd07878    171 eMTGYV----ATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLKGKALF 216
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
2812-3013 1.18e-13

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: 73.55  E-value: 1.18e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2812 ELGILQNLQHPLLVSLLD--TFETPTSYV----LVLEMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAH 2885
Cdd:cd14012     48 ELESLKKLRHPNLVSYLAfsIERRGRSDGwkvyLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVH 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2886 LDLKPENILVDQSLAKPTIKLADFGDAVQLN--TTYYIHQLLGNPEFAAPEIILGN-PVSLTADTWSVGVLTYVLLSGVS 2962
Cdd:cd14012    128 KSLHAGNVLLDRDAGTGIVKLTDYSLGKTLLdmCSRGSLDEFKQTYWLPPELAQGSkSPTRKTDVWDLGLLFLQMLFGLD 207
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907111721 2963 PFLDDSVEETCLNICRLDFSFpedyfqgvsqkaKEFVCFLLQEDPAKRPSA 3013
Cdd:cd14012    208 VLEKYTSPNPVLVSLDLSASL------------QDFLSKCLSLDPKKRPTA 246
PH_Dbs cd01227
DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming ...
2121-2241 1.30e-13

DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming sequence-like protein 2) is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a rhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269934 [Multi-domain]  Cd Length: 126  Bit Score: 69.92  E-value: 1.30e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2121 GFDGKIVAQGKLLLQDTFLV-TDQDAG---LLPRCK--ERRVFLFEQIVIFSepldKKKG--FSMPGFLFKNSIKVSCLC 2192
Cdd:cd01227      4 GYDGNLGDLGKLLMQGSFNVwTEHKKGhtkKLARFKpmQRHIFLYEKAVLFC----KKRGenGEAPSYSYKNSLNTTAVG 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1907111721 2193 LEENVESDPCKFALTsrTGDAVETFVLHSSSPSVRQTWIHEINQILENQ 2241
Cdd:cd01227     80 LTENVKGDTKKFEIW--LNGREEVFIIQAPTPEIKAAWVKAIRQVLLSQ 126
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
2768-3004 1.36e-13

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha 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: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 75.08  E-value: 1.36e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVkkCDQKGTKRA--VATKFVNK---KLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSY----- 2837
Cdd:cd07877     19 YQNLSPVGSGAYGSV--CAAFDTKTGlrVAVKKLSRpfqSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLeefnd 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2838 -VLVLEMadQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAvqLN 2916
Cdd:cd07877     97 vYLVTHL--MGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDC---ELKILDFGLA--RH 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2917 TTYYIHQLLGNPEFAAPEIILG-NPVSLTADTWSVGVLTYVLLSGVSPFL-DDSVEETCLnICRLDFSFPEDYFQGV-SQ 2993
Cdd:cd07877    170 TDDEMTGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLTGRTLFPgTDHIDQLKL-ILRLVGTPGAELLKKIsSE 248
                          250
                   ....*....|.
gi 1907111721 2994 KAKEFVCFLLQ 3004
Cdd:cd07877    249 SARNYIQSLTQ 259
SPEC smart00150
Spectrin repeats;
539-639 1.39e-13

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 68.90  E-value: 1.39e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721   539 FQQDVQQVLDWIENHgEAFLSkHTGVGKSLHRARALQKRHEDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYQAAH 618
Cdd:smart00150    3 FLRDADELEAWLEEK-EQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 1907111721   619 QLEDRIQDFVRRVEQRKILLD 639
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
2773-2965 1.40e-13

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk 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: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 73.46  E-value: 1.40e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKK--CDQKGTKRAVATKFV----NKKLMKrDQVTHELGILQNLQHPLLVSLLDTFETpTSYVLVLEMADQ 2846
Cdd:cd05116      2 ELGSGNFGTVKKgyYQMKKVVKTVAVKILkneaNDPALK-DELLREANVMQQLDNPYIVRMIGICEA-ESWMLVMEMAEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2847 GRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENI-LVDQSLAkptiKLADFG--DAVQLNTTYYIHQ 2923
Cdd:cd05116     80 GPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVlLVTQHYA----KISDFGlsKALRADENYYKAQ 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907111721 2924 LLGN-P-EFAAPEIILGNPVSLTADTWSVGVLTYVLLS-GVSPFL 2965
Cdd:cd05116    156 THGKwPvKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPYK 200
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
2770-2998 1.57e-13

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 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: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 75.13  E-value: 1.57e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2770 EVAE-LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQHPL-----LVSLLDTFETPTSYVLVLEM 2843
Cdd:cd14227     18 EVLEfLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARLSTESaddynFVRAYECFQHKNHTCLVFEM 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQgRLLDCVV--RWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENI-LVDQSLAKPTIKLADFGDAVQLN---- 2916
Cdd:cd14227     98 LEQ-NLYDFLKqnKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENImLVDPSRQPYRVKVIDFGSASHVSkavc 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2917 TTYyihqlLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGvSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAK 2996
Cdd:cd14227    177 STY-----LQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG-WPLYPGASEYDQIRYISQTQGLPAEYLLSAGTKTT 250

                   ..
gi 1907111721 2997 EF 2998
Cdd:cd14227    251 RF 252
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
2768-3022 1.60e-13

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-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: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 73.95  E-value: 1.60e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVnkklmkrdQVTHELG----------ILQNLQHPLLVSLLDTFETPTSY 2837
Cdd:cd07844      2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEI--------RLEHEEGapftaireasLLKDLKHANIVTLHDIIHTKKTL 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2838 VLVLE---------MADQGRLLDcvvrwgsltEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLAD 2908
Cdd:cd07844     74 TLVFEyldtdlkqyMDDCGGGLS---------MHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLIS---ERGELKLAD 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2909 FG--DAVQLNTTYYIHQ---LLGNPefaaPEIILGNP-VSLTADTWSVGVLTYVLLSGVSPFLDDS-VEETCLNICRLDF 2981
Cdd:cd07844    142 FGlaRAKSVPSKTYSNEvvtLWYRP----PDVLLGSTeYSTSLDMWGVGCIFYEMATGRPLFPGSTdVEDQLHKIFRVLG 217
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907111721 2982 SFPEDYFQGVSQKAK----------------------------EFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd07844    218 TPTEETWPGVSSNPEfkpysfpfypprplinhaprldriphgeELALKFLQYEPKKRISAAEAMKHPYF 286
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
2764-3022 1.66e-13

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin 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: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 73.89  E-value: 1.66e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2764 FDAFYS-----EVAE-LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQ-HPLLVSLLDTF----- 2831
Cdd:cd06638     10 FDSFPDpsdtwEIIEtIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEEIEAEYNILKALSdHPNVVKFYGMYykkdv 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2832 ETPTSYVLVLEMADQGRLLDCV---VRWGSLTEGKVRAH-LGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLA 2907
Cdd:cd06638     90 KNGDQLWLVLELCNGGSVTDLVkgfLKRGERMEEPIIAYiLHEALMGLQHLHVNKTIHRDVKGNNILLT---TEGGVKLV 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2908 DFGDAVQL-NTTYYIHQLLGNPEFAAPEII-----LGNPVSLTADTWSVGVLTYVLLSGVSPFLDdsveetcLNICRLDF 2981
Cdd:cd06638    167 DFGVSAQLtSTRLRRNTSVGTPFWMAPEVIaceqqLDSTYDARCDVWSLGITAIELGDGDPPLAD-------LHPMRALF 239
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1907111721 2982 SFPEDYFQGVSQK---AKEFVCFL---LQEDPAKRPSAALALQEQWL 3022
Cdd:cd06638    240 KIPRNPPPTLHQPelwSNEFNDFIrkcLTKDYEKRPTVSDLLQHVFI 286
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
2662-2748 2.15e-13

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 67.80  E-value: 2.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2662 PLSEVTCETGETVVFRCRVCGRPKASITWkgpehntLNNDDHYSISY--SDIGEATLKIIGVSTEDDGIYTCIAVNDMGS 2739
Cdd:cd20978      7 PEKNVVVKGGQDVTLPCQVTGVPQPKITW-------LHNGKPLQGPMerATVEDGTLTIINVQPEDTGYYGCVATNEIGD 79

                   ....*....
gi 1907111721 2740 ASSSASLRV 2748
Cdd:cd20978     80 IYTETLLHV 88
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
2772-3023 2.89e-13

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 74.03  E-value: 2.89e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2772 AELGRGRFAVVKKCDQKGTKRAVATK---------FVNKKLMKRDQV------THELGILQNLQHPLLVSLLDTFETPTS 2836
Cdd:PTZ00024    15 AHLGEGTYGKVEKAYDTLTGKIVAIKkvkiieisnDVTKDRQLVGMCgihfttLRELKIMNEIKHENIMGLVDVYVEGDF 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2837 YVLVLE-MA-DQGRLLDCVVRwgsLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFG---- 2910
Cdd:PTZ00024    95 INLVMDiMAsDLKKVVDRKIR---LTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINS---KGICKIADFGlarr 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2911 ---------------DAVQLNTTYYIHQLLgnpeFAAPEIILG-NPVSLTADTWSVGVLTYVLLSGV------------- 2961
Cdd:PTZ00024   169 ygyppysdtlskdetMQRREEMTSKVVTLW----YRAPELLMGaEKYHFAVDMWSVGCIFAELLTGKplfpgeneidqlg 244
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907111721 2962 -------SPFLDDSVEETCLNI-CRLDFSFPED---YFQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQ 3023
Cdd:PTZ00024   245 rifellgTPNEDNWPQAKKLPLyTEFTPRKPKDlktIFPNASDDAIDLLQSLLKLNPLERISAKEALKHEYFK 317
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
2807-3019 3.51e-13

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks 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. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 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: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 72.33  E-value: 3.51e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2807 DQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDcvvrwgSLTEGKVRAHL-----GEVLEAVRYLHN- 2880
Cdd:cd14148     38 ENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGALNR------ALAGKKVPPHVlvnwaVQIARGMNYLHNe 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2881 --CRIAHLDLKPENILV-----DQSLAKPTIKLADFGDAVQLNTTYYIhQLLGNPEFAAPEIILGNPVSLTADTWSVGVL 2953
Cdd:cd14148    112 aiVPIIHRDLKSSNILIlepieNDDLSGKTLKITDFGLAREWHKTTKM-SAAGTYAWMAPEVIRLSLFSKSSDVWSFGVL 190
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907111721 2954 TYVLLSGVSPF--LDDSVEETCLNICRLDFSFPedyfqgvSQKAKEFVCfLLQE----DPAKRPSAALALQE 3019
Cdd:cd14148    191 LWELLTGEVPYreIDALAVAYGVAMNKLTLPIP-------STCPEPFAR-LLEEcwdpDPHGRPDFGSILKR 254
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
2776-3019 3.54e-13

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 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. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 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: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 72.38  E-value: 3.54e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2776 RGRFAVVKKCDQKGTKRAVATKfvnkklmkrDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDCVV- 2854
Cdd:cd14146     16 KGQEVAVKAARQDPDEDIKATA---------ESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGTLNRALAa 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2855 ---RWGSLTEGKVRAHL-----GEVLEAVRYLHN---CRIAHLDLKPENILV-----DQSLAKPTIKLADFGDAVQLNTT 2918
Cdd:cd14146     87 anaAPGPRRARRIPPHIlvnwaVQIARGMLYLHEeavVPILHRDLKSSNILLlekieHDDICNKTLKITDFGLAREWHRT 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2919 YYIhQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPF--LDDSVEETCLNICRLDFSFPEDYFQGVSQKAK 2996
Cdd:cd14146    167 TKM-SAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYrgIDGLAVAYGVAVNKLTLPIPSTCPEPFAKLMK 245
                          250       260
                   ....*....|....*....|...
gi 1907111721 2997 EfvCFllQEDPAKRPSAALALQE 3019
Cdd:cd14146    246 E--CW--EQDPHIRPSFALILEQ 264
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
2770-2998 4.17e-13

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 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: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 73.58  E-value: 4.17e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2770 EVAE-LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGIL-----QNLQHPLLVSLLDTFETPTSYVLVLEM 2843
Cdd:cd14228     18 EVLEfLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILsrlssENADEYNFVRSYECFQHKNHTCLVFEM 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQGrLLDCVV--RWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKP-TIKLADFGDAVQLN---- 2916
Cdd:cd14228     98 LEQN-LYDFLKqnKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPVRQPyRVKVIDFGSASHVSkavc 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2917 TTYyihqlLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGvSPFLDDSVEETCLNICRLDFSFPEDYFQGVSQKAK 2996
Cdd:cd14228    177 STY-----LQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG-WPLYPGASEYDQIRYISQTQGLPAEYLLSAGTKTS 250

                   ..
gi 1907111721 2997 EF 2998
Cdd:cd14228    251 RF 252
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
2771-2964 4.18e-13

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like 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: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 72.10  E-value: 4.18e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2771 VAELGRGRFAVVKKCDQKGtKRAVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLL 2850
Cdd:cd05059      9 LKELGSGQFGVVHLGKWRG-KIDVAIKMIKEGSMSEDDFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMANGCLL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2851 DCVVRwgslTEGKVRAHL-----GEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDA-VQLNTTYYIHQL 2924
Cdd:cd05059     88 NYLRE----RRGKFQTEQllemcKDVCEAMEYLESNGFIHRDLAARNCLVGEQN---VVKVSDFGLArYVLDDEYTSSVG 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907111721 2925 LGNP-EFAAPEIILGNPVSLTADTWSVGVLTYVLLS-GVSPF 2964
Cdd:cd05059    161 TKFPvKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSeGKMPY 202
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
2875-3018 4.72e-13

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 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: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 72.30  E-value: 4.72e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2875 VRYLHNCRIAHLDLKPENILVDQSLAKPTIK--LADFGDAVQLNT-TYYIHQLLGNPE---FAAPEIILGNP---VSLTA 2945
Cdd:cd13982    112 LAHLHSLNIVHRDLKPQNILISTPNAHGNVRamISDFGLCKKLDVgRSSFSRRSGVAGtsgWIAPEMLSGSTkrrQTRAV 191
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907111721 2946 DTWSVG-VLTYVLLSGVSPFLDDSVEETclNICRLDFSFPEDYFQGV-SQKAKEFVCFLLQEDPAKRPSAALALQ 3018
Cdd:cd13982    192 DIFSLGcVFYYVLSGGSHPFGDKLEREA--NILKGKYSLDKLLSLGEhGPEAQDLIERMIDFDPEKRPSAEEVLN 264
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1107-1214 5.33e-13

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 70.55  E-value: 5.33e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1107 QYVVFERSAKQALEWIHDNGEFYLSThtSTGSSIQHTQELLKEHEEFQITAKQTKERVKLLIQLADGFCEKGHAHAAEIK 1186
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSST--DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                           90       100
                   ....*....|....*....|....*...
gi 1907111721 1187 KCVTAVDKRYRDFSLRMEKYRTSLEKAL 1214
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEAL 106
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
2765-2963 5.94e-13

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK 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: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 72.77  E-value: 5.94e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2765 DAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMK--RDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLE 2842
Cdd:cd06649      4 DDDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPaiRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICME 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 MADQGRLLDCVVRWGSLTE---GKVRAHLGEVLEAVRYLHncRIAHLDLKPENILVDqslAKPTIKLADFGDAVQLNTTY 2919
Cdd:cd06649     84 HMDGGSLDQVLKEAKRIPEeilGKVSIAVLRGLAYLREKH--QIMHRDVKPSNILVN---SRGEIKLCDFGVSGQLIDSM 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1907111721 2920 yIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSP 2963
Cdd:cd06649    159 -ANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYP 201
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
2745-2951 8.84e-13

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK 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: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 72.45  E-value: 8.84e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2745 SLRVLGPGSDGIVVtwkdnfdAFYSEVaelgrgrfavvkkcdqkgTKRAVATK-----FVNKKLMKRdqVTHELGILQNL 2819
Cdd:cd07850      4 NLKPIGSGAQGIVC-------AAYDTV------------------TGQNVAIKklsrpFQNVTHAKR--AYRELVLMKLV 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2820 QHPLLVSLLDTFETPTSY------VLVLEMADQGRlldCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENI 2893
Cdd:cd07850     57 NHKNIIGLLNVFTPQKSLeefqdvYLVMELMDANL---CQVIQMDLDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNI 133
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907111721 2894 LVDqslAKPTIKLADFGDAVQLNTTYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVG 2951
Cdd:cd07850    134 VVK---SDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVG 188
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
2774-3016 9.13e-13

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 73.53  E-value: 9.13e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKfvnKKLMKRDQVTHELGILQNLQHPLLVSLLDTFetptsYVLVLEMADQGRLLDCV 2853
Cdd:PTZ00036    74 IGNGSFGVVYEAICIDTSEKVAIK---KVLQDPQYKNRELLIMKNLNHINIIFLKDYY-----YTECFKKNEKNIFLNVV 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2854 VRWGSLTEGKVRAHLG----------------EVLEAVRYLHNCRIAHLDLKPENILVDQSlaKPTIKLADFGDAVQL-- 2915
Cdd:PTZ00036   146 MEFIPQTVHKYMKHYArnnhalplflvklysyQLCRALAYIHSKFICHRDLKPQNLLIDPN--THTLKLCDFGSAKNLla 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2916 --NTTYYIHQLLgnpeFAAPEIILGNPVSLT-ADTWSVG------VLTYVLLSGVSP---------FLDDSVEETC--LN 2975
Cdd:PTZ00036   224 gqRSVSYICSRF----YRAPELMLGATNYTThIDLWSLGciiaemILGYPIFSGQSSvdqlvriiqVLGTPTEDQLkeMN 299
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907111721 2976 ICRLDFSFPE--------DYFQGVSQKAKEFVCFLLQEDPAKR--PSAALA 3016
Cdd:PTZ00036   300 PNYADIKFPDvkpkdlkkVFPKGTPDDAINFISQFLKYEPLKRlnPIEALA 350
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
2768-3023 1.19e-12

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO 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: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 70.56  E-value: 1.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATK---FVNKKLMKRDQ-VTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEM 2843
Cdd:cd06607      3 FEDLREIGHGSFGAVYYARNKRTSEVVAIKkmsYSGKQSTEKWQdIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVMEY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 AdQGRLLDCV-VRWGSLTEGKVRAHLGEVLEAVRYLHN-CRIaHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTyyi 2921
Cdd:cd06607     83 C-LGSASDIVeVHKKPLQEVEIAAICHGALQGLAYLHShNRI-HRDVKAGNILLTEP---GTVKLADFGSASLVCPA--- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2922 HQLLGNPEFAAPEIILG---NPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDF-SFPEDYFqgvSQKAKE 2997
Cdd:cd06607    155 NSFVGTPYWMAPEVILAmdeGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNDSpTLSSGEW---SDDFRN 231
                          250       260
                   ....*....|....*....|....*.
gi 1907111721 2998 FVCFLLQEDPAKRPSAALALQEQWLQ 3023
Cdd:cd06607    232 FVDSCLQKIPQDRPSAEDLLKHPFVT 257
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
2771-3023 1.44e-12

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 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: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 71.25  E-value: 1.44e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2771 VAELGRGRFAVVKKCDQKGTKRAVATKfvnkkLMKRDQVTHELG-ILQNLQ-----H--PLLVSLLDTFETPTSYVLVLE 2842
Cdd:cd06618     20 LGEIGSGTCGQVYKMRHKKTGHVMAVK-----QMRRSGNKEENKrILMDLDvvlksHdcPYIVKCYGYFITDSDVFICME 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 -MADqgrlldCVVRWGSLTEGKVRAH-LGE----VLEAVRYL---HNcrIAHLDLKPENILVDQSlakPTIKLADFGDAV 2913
Cdd:cd06618     95 lMST------CLDKLLKRIQGPIPEDiLGKmtvsIVKALHYLkekHG--VIHRDVKPSNILLDES---GNVKLCDFGISG 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2914 QLNTTYYIHQLLGNPEFAAPEIILGNPVS---LTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICrLDFSFPE-DYFQ 2989
Cdd:cd06618    164 RLVDSKAKTRSAGCAAYMAPERIDPPDNPkydIRADVWSLGISLVELATGQFPYRNCKTEFEVLTKI-LNEEPPSlPPNE 242
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1907111721 2990 GVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQ 3023
Cdd:cd06618    243 GFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIR 276
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
2671-2748 1.77e-12

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 65.11  E-value: 1.77e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907111721 2671 GETVVFRCRVCGRPKASITWKgpehntlNNDDHYSISYSDI-GEATLKIIGVSTEDDGIYTCIAVNDMGSASSSASLRV 2748
Cdd:cd05725     12 DDSAEFQCEVGGDPVPTVRWR-------KEDGELPKGRYEIlDDHSLKIRKVTAGDMGSYTCVAENMVGKIEASATLTV 83
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
2671-2748 2.03e-12

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 65.17  E-value: 2.03e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907111721 2671 GETVVFRCRVCGRPKASITWKGPEHNTLNNDDhysISYSDIGeaTLKIIGVSTEDDGIYTCIAVNDMGSASSSASLRV 2748
Cdd:cd04969     17 GGDVIIECKPKASPKPTISWSKGTELLTNSSR---ICILPDG--SLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
2768-2999 2.09e-12

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma 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: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 71.52  E-value: 2.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATK-----FVNKKLMKRdqVTHELGILQNLQHPLLVSLLDTFeTP-------T 2835
Cdd:cd07880     17 YRDLKQVGSGAYGTVCSALDRRTGAKVAIKklyrpFQSELFAKR--AYRELRLLKHMKHENVIGLLDVF-TPdlsldrfH 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2836 SYVLVLEM--ADQGRLLdcvvRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAV 2913
Cdd:cd07880     94 DFYLVMPFmgTDLGKLM----KHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDC---ELKILDFGLAR 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2914 QLN---TTYYIHQLlgnpeFAAPEIILG-NPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQ 2989
Cdd:cd07880    167 QTDsemTGYVVTRW-----YRAPEVILNwMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKVTGTPSKEFVQ 241
                          250
                   ....*....|.
gi 1907111721 2990 GV-SQKAKEFV 2999
Cdd:cd07880    242 KLqSEDAKNYV 252
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
2768-3020 2.17e-12

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI 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: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 70.61  E-value: 2.17e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVN-KKLMKRD--QVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMA 2844
Cdd:cd14049      8 FEEIARLGKGGYGKVYKVRNKLDGQYYAIKKILiKKVTKRDcmKVLREVKVLAGLQHPNIVGYHTAWMEHVQLMLYIQMQ 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 DQGR-LLDCVV---RWGSLTEGKVRAH-----------LGEVLEAVRYLHNCRIAHLDLKPENILVdqSLAKPTIKLADF 2909
Cdd:cd14049     88 LCELsLWDWIVernKRPCEEEFKSAPYtpvdvdvttkiLQQLLEGVTYIHSMGIVHRDLKPRNIFL--HGSDIHVRIGDF 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2910 G----DAVQLNTTYYIHQLL---------GNPEFAAPEIILGNPVSLTADTWSVGVltyVLLSGVSPFLDDSVEETCLNI 2976
Cdd:cd14049    166 GlacpDILQDGNDSTTMSRLnglthtsgvGTCLYAAPEQLEGSHYDFKSDMYSIGV---ILLELFQPFGTEMERAEVLTQ 242
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1907111721 2977 CRlDFSFPEDYFQGVSQKAKeFVCFLLQEDPAKRPSAALALQEQ 3020
Cdd:cd14049    243 LR-NGQIPKSLCKRWPVQAK-YIKLLTSTEPSERPSASQLLESE 284
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
2768-3018 2.31e-12

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. 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 CdkB 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: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 70.63  E-value: 2.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKfvnKKLMKRDQ------VTHELGILQNLQH-PLLVSLLD---TFETPTSY 2837
Cdd:cd07837      3 YEKLEKIGEGTYGKVYKARDKNTGKLVALK---KTRLEMEEegvpstALREVSLLQMLSQsIYIVRLLDvehVEENGKPL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2838 V-LVLEMADQG--RLLDCVVRWGS--LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlaKPTIKLADFG-- 2910
Cdd:cd07837     80 LyLVFEYLDTDlkKFIDSYGRGPHnpLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQ--KGLLKIADLGlg 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2911 DAVQLNTTYYIHQLLgNPEFAAPEIILGNP-VSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYFQ 2989
Cdd:cd07837    158 RAFTIPIKSYTHEIV-TLWYRAPEVLLGSThYSTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIFRLLGTPNEEVWP 236
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907111721 2990 GVSQ------------------------KAKEFVCFLLQEDPAKRPSAALALQ 3018
Cdd:cd07837    237 GVSKlrdwheypqwkpqdlsravpdlepEGVDLLTKMLAYDPAKRISAKAALQ 289
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
2766-2964 2.37e-12

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 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: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 71.27  E-value: 2.37e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2766 AFYSEVAE-LGRGRFAVVKKCDQKGTKRAVATKFV-NKKLMKRdQVTHELGILQNL-------QHPLlVSLLD------- 2829
Cdd:cd14225     42 AYRYEILEvIGKGSFGQVVKALDHKTNEHVAIKIIrNKKRFHH-QALVEVKILDALrrkdrdnSHNV-IHMKEyfyfrnh 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2830 ---TFE--TPTSYVLVLEMADQGRLLDCVVRWGSltegkvrahlgEVLEAVRYLHNCRIAHLDLKPENILVDQSlAKPTI 2904
Cdd:cd14225    120 lciTFEllGMNLYELIKKNNFQGFSLSLIRRFAI-----------SLLQCLRLLYRERIIHCDLKPENILLRQR-GQSSI 187
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907111721 2905 KLADFGdavqlnTTYYIHQ----LLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPF 2964
Cdd:cd14225    188 KVIDFG------SSCYEHQrvytYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLF 245
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
2795-3023 2.65e-12

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 72.36  E-value: 2.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2795 ATKFVNKKLMKRD--QVTH---ELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLldcvvrwGSLTEGKVRAHLG 2869
Cdd:PTZ00267    93 KEKVVAKFVMLNDerQAAYarsELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDL-------NKQIKQRLKEHLP 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2870 -----------EVLEAVRYLHNCRIAHLDLKPENILVdqslaKPT--IKLADFG------DAVQLNTTyyiHQLLGNPEF 2930
Cdd:PTZ00267   166 fqeyevgllfyQIVLALDEVHSRKMMHRDLKSANIFL-----MPTgiIKLGDFGfskqysDSVSLDVA---SSFCGTPYY 237
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2931 AAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFS-FPedyfQGVSQKAKEFVCFLLQEDPAK 3009
Cdd:PTZ00267   238 LAPELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKYDpFP----CPVSSGMKALLDPLLSKNPAL 313
                          250
                   ....*....|....
gi 1907111721 3010 RPSAALALQEQWLQ 3023
Cdd:PTZ00267   314 RPTTQQLLHTEFLK 327
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
2768-3018 2.82e-12

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. 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 CDK5 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: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 70.15  E-value: 2.82e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVnkKLMKRDQ-----VTHELGILQNLQHPLLVSLLDTFETPTSYVLVLE 2842
Cdd:cd07839      2 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRV--RLDDDDEgvpssALREICLLKELKHKNIVRLYDVLHSDKKLTLVFE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 MADQG--RLLDCVVrwGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDA-------- 2912
Cdd:cd07839     80 YCDQDlkKYFDSCN--GDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKN---GELKLADFGLArafgipvr 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2913 ---VQLNTTYYihqllgnpefAAPEIILGNPV-SLTADTWSVGVLTYVLLSGVSP-FLDDSVEETCLNICRLDFSFPEDY 2987
Cdd:cd07839    155 cysAEVVTLWY----------RPPDVLFGAKLySTSIDMWSAGCIFAELANAGRPlFPGNDVDDQLKRIFRLLGTPTEES 224
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907111721 2988 FQGVSQ--KAKEFVCF-------------------LLQE----DPAKRPSAALALQ 3018
Cdd:cd07839    225 WPGVSKlpDYKPYPMYpattslvnvvpklnstgrdLLQNllvcNPVQRISAEEALQ 280
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
2768-2963 3.13e-12

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK 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: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 70.16  E-value: 3.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNK--KLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMAD 2845
Cdd:cd06615      3 FEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHLeiKPAIRNQIIRELKVLHECNSPYIVGFYGAFYSDGEISICMEHMD 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2846 QGRLLDCVVRWGSLTE---GKVRAhlgEVLEAVRYLH-NCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQL-----N 2916
Cdd:cd06615     83 GGSLDQVLKKAGRIPEnilGKISI---AVLRGLTYLReKHKIMHRDVKPSNILVN---SRGEIKLCDFGVSGQLidsmaN 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1907111721 2917 TtyyihqLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSP 2963
Cdd:cd06615    157 S------FVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYP 197
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
2773-2935 3.47e-12

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 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: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 69.75  E-value: 3.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRAVA-TKFVNKKLMKRDQ--VTHELGILQNLQHPLLVSLLDTFET----PTSYVLVLEMAD 2845
Cdd:cd14031     17 ELGRGAFKTVYKGLDTETWVEVAwCELQDRKLTKAEQqrFKEEAEMLKGLQHPNIVRFYDSWESvlkgKKCIVLVTELMT 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2846 QGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCR--IAHLDLKPENILVDQSLAkpTIKLADFGDAVQLNTTYyIHQ 2923
Cdd:cd14031     97 SGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTG--SVKIGDLGLATLMRTSF-AKS 173
                          170
                   ....*....|..
gi 1907111721 2924 LLGNPEFAAPEI 2935
Cdd:cd14031    174 VIGTPEFMAPEM 185
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
2767-3012 3.80e-12

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


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 69.55  E-value: 3.80e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2767 FYSEVAELGRGRFAVVKKCdqKGTKRAV-ATKFVNkkLMKRDQVT-----HELGILQNLQH-PLLVSLLD---TFETPTS 2836
Cdd:cd14131      2 PYEILKQLGKGGSSKVYKV--LNPKKKIyALKRVD--LEGADEQTlqsykNEIELLKKLKGsDRIIQLYDyevTDEDDYL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2837 YVlVLEM--ADQGRLLDcvVRWGS-LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPEN-ILVDQSLakptiKLADFG-- 2910
Cdd:cd14131     78 YM-VMECgeIDLATILK--KKRPKpIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANfLLVKGRL-----KLIDFGia 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2911 DAVQLNTTyYIH--QLLGNPEFAAPEIILGN----------PVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLN-IC 2977
Cdd:cd14131    150 KAIQNDTT-SIVrdSQVGTLNYMSPEAIKDTsasgegkpksKIGRPSDVWSLGCILYQMVYGKTPFQHITNPIAKLQaII 228
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1907111721 2978 ----RLDF-SFPEDYFQGVSQKakefvCflLQEDPAKRPS 3012
Cdd:cd14131    229 dpnhEIEFpDIPNPDLIDVMKR-----C--LQRDPKKRPS 261
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
2771-3022 3.99e-12

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. 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 MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 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: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 69.30  E-value: 3.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2771 VAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKR-DQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRL 2849
Cdd:cd06645     16 IQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDfAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEFCGGGSL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTYYIHQ-LLGNP 2928
Cdd:cd06645     96 QDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDN---GHVKLADFGVSAQITATIAKRKsFIGTP 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2929 EFAAPEIIL---GNPVSLTADTWSVGVLTYVLLSGVSPFLDdsveetcLNICRLDFSFPEDYFQGVSQKAK--------E 2997
Cdd:cd06645    173 YWMAPEVAAverKGGYNQLCDIWAVGITAIELAELQPPMFD-------LHPMRALFLMTKSNFQPPKLKDKmkwsnsfhH 245
                          250       260
                   ....*....|....*....|....*
gi 1907111721 2998 FVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd06645    246 FVKMALTKNPKKRPTAEKLLQHPFV 270
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
2774-2999 4.63e-12

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 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: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 69.70  E-value: 4.63e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQ--------VTHELGILQNLQHPLLVSLLDTFETPT-SYVLVLEMA 2844
Cdd:cd14040     14 LGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEkkenyhkhACREYRIHKELDHPRIVKLYDYFSLDTdTFCTVLEYC 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 dQGRLLDCVVRWGSL-TEGKVRAHLGEVLEAVRYLHNCR--IAHLDLKPENILVDQSLAKPTIKLADFG-------DAVQ 2914
Cdd:cd14040     94 -EGNDLDFYLKQHKLmSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITDFGlskimddDSYG 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2915 LNTTYYIHQLLGNPEFAAPE-IILGN---PVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLN----ICRLDFSFPED 2986
Cdd:cd14040    173 VDGMDLTSQGAGTYWYLPPEcFVVGKeppKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQentiLKATEVQFPVK 252
                          250
                   ....*....|...
gi 1907111721 2987 YFqgVSQKAKEFV 2999
Cdd:cd14040    253 PV--VSNEAKAFI 263
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
644-875 5.28e-12

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 67.86  E-value: 5.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  644 FHTHVKELWTWLEELQKELLDDVYAESVEAVQDLIKR---FGQQQQTTLQVTVNVIKEGEDLIQQLRDSAissnktphns 720
Cdd:cd00176      5 FLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKheaLEAELAAHEERVEALNELGEQLIEEGHPDA---------- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  721 siNHIETVLQQLDEAQSQMEELFQERKIKLELFLQLRIFERDAidiiSDLESWNDELSQQMNDFDT-EDLTIAEQRLQHH 799
Cdd:cd00176     75 --EEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA----DDLEQWLEEKEAALASEDLgKDLESVEELLKKH 148
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907111721  800 ADKALTMNNltfdviHQGQdllqyVNEVQASGVELLCDRDVDMATRVQDLLEFLHEKQQELDLAAEQHRKHLEQCV 875
Cdd:cd00176    149 KELEEELEA------HEPR-----LKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
2657-2748 5.33e-12

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 64.36  E-value: 5.33e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2657 PEFVIPLSEVTCETGETVVFRCRVCGRPKASITW--KGPEHNTLNNDDHYSIsYSDIGEATLKIIGVSTEDDGIYTCIAV 2734
Cdd:cd20951      1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWykNGVPIDPSSIPGKYKI-ESEYGVHVLHIRRVTVEDSAVYSAVAK 79
                           90
                   ....*....|....
gi 1907111721 2735 NDMGSASSSASLRV 2748
Cdd:cd20951     80 NIHGEASSSASVVV 93
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
2773-2935 8.13e-12

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 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: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 68.92  E-value: 8.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVV-KKCDQKGTKRAVATKFVNKKLMK--RDQVTHELGILQNLQHPLLVSLLDTFETPTS----YVLVLEMAD 2845
Cdd:cd14030     32 EIGRGSFKTVyKGLDTETTVEVAWCELQDRKLSKseRQRFKEEAGMLKGLQHPNIVRFYDSWESTVKgkkcIVLVTELMT 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2846 QGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCR--IAHLDLKPENILVDQSLAkpTIKLADFGDAVqLNTTYYIHQ 2923
Cdd:cd14030    112 SGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTG--SVKIGDLGLAT-LKRASFAKS 188
                          170
                   ....*....|..
gi 1907111721 2924 LLGNPEFAAPEI 2935
Cdd:cd14030    189 VIGTPEFMAPEM 200
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
2765-3012 8.51e-12

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 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: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 68.75  E-value: 8.51e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2765 DAFYSEVaeLGRGRFAVVKKCDQKGTKRAVATKFV--NKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLE 2842
Cdd:cd06619      2 DIQYQEI--LGHGNGGTVYKAYHLLTRRILAVKVIplDITVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 MADQGRLlDCVVRWGSLTEGKVRAhlgEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQL----NTT 2918
Cdd:cd06619     80 FMDGGSL-DVYRKIPEHVLGRIAV---AVVKGLTYLWSLKILHRDVKPSNMLVN---TRGQVKLCDFGVSTQLvnsiAKT 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2919 YyihqlLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLD-----DSVEETCLNICRLDFSFPEDYFQGVSQ 2993
Cdd:cd06619    153 Y-----VGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYPQiqknqGSLMPLQLLQCIVDEDPPVLPVGQFSE 227
                          250
                   ....*....|....*....
gi 1907111721 2994 KAKEFVCFLLQEDPAKRPS 3012
Cdd:cd06619    228 KFVHFITQCMRKQPKERPA 246
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
2807-2964 9.29e-12

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks 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. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 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: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 68.15  E-value: 9.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2807 DQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQG---RLL-------DCVVRWGSltegkvrahlgEVLEAVR 2876
Cdd:cd14145     50 ENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFARGGplnRVLsgkrippDILVNWAV-----------QIARGMN 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2877 YLHNCRIA---HLDLKPENILVDQ-----SLAKPTIKLADFGDAVQLNTTYYIhQLLGNPEFAAPEIILGNPVSLTADTW 2948
Cdd:cd14145    119 YLHCEAIVpviHRDLKSSNILILEkvengDLSNKILKITDFGLAREWHRTTKM-SAAGTYAWMAPEVIRSSMFSKGSDVW 197
                          170
                   ....*....|....*.
gi 1907111721 2949 SVGVLTYVLLSGVSPF 2964
Cdd:cd14145    198 SYGVLLWELLTGEVPF 213
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
2768-2964 9.95e-12

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 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: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 68.95  E-value: 9.95e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVT--HELGILQNLQHPLLVSLLDTFETPTSYVLVLEM-- 2843
Cdd:cd07869      7 YEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTaiREASLLKGLKHANIVLLHDIIHTKETLTLVFEYvh 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQGRLLDcvVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFG--DAVQLNTTYYI 2921
Cdd:cd07869     87 TDLCQYMD--KHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDT---GELKLADFGlaRAKSVPSHTYS 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1907111721 2922 HQLLgNPEFAAPEIILGNP-VSLTADTWSVGVLTYVLLSGVSPF 2964
Cdd:cd07869    162 NEVV-TLWYRPPDVLLGSTeYSTCLDMWGVGCIFVEMIQGVAAF 204
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
2806-2964 1.23e-11

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs 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. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK 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: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 67.80  E-value: 1.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2806 RDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDCvvrwgsLTEGKVRAHL-----GEVLEAVRYLHN 2880
Cdd:cd14061     37 LENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGGALNRV------LAGRKIPPHVlvdwaIQIARGMNYLHN 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2881 CR---IAHLDLKPENILVDQ-----SLAKPTIKLADFGDAVQLNTTYYIHQLlGNPEFAAPEIILGNPVSLTADTWSVGV 2952
Cdd:cd14061    111 EApvpIIHRDLKSSNILILEaieneDLENKTLKITDFGLAREWHKTTRMSAA-GTYAWMAPEVIKSSTFSKASDVWSYGV 189
                          170
                   ....*....|..
gi 1907111721 2953 LTYVLLSGVSPF 2964
Cdd:cd14061    190 LLWELLTGEVPY 201
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
2760-3023 1.34e-11

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 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: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 68.51  E-value: 1.34e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2760 WKDNFDAFYSEVAELGRGRFAVVKKCDQKGTKRAVATK---FVNKKLMKRDQ-VTHELGILQNLQHPLLVSLLDTFETPT 2835
Cdd:cd06634      9 FKDDPEKLFSDLREIGHGSFGAVYFARDVRNNEVVAIKkmsYSGKQSNEKWQdIIKEVKFLQKLRHPNTIEYRGCYLREH 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2836 SYVLVLE--MADQGRLLDcvVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILvdqsLAKP-TIKLADFGDA 2912
Cdd:cd06634     89 TAWLVMEycLGSASDLLE--VHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNIL----LTEPgLVKLGDFGSA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2913 VQLNTTyyiHQLLGNPEFAAPEIILG---NPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICR-----LDFSFP 2984
Cdd:cd06634    163 SIMAPA---NSFVGTPYWMAPEVILAmdeGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQnespaLQSGHW 239
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1907111721 2985 EDYFqgvsqkaKEFVCFLLQEDPAKRPSAALALQEQWLQ 3023
Cdd:cd06634    240 SEYF-------RNFVDSCLQKIPQDRPTSDVLLKHRFLL 271
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
2746-2960 1.42e-11

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 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: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 68.90  E-value: 1.42e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2746 LRVLGPGSDGIVVTWKDNFDAFYSEVAELGRgrfavvkkcdqkgtkravatKFVNKKLMKRdqVTHELGILQNLQHPLLV 2825
Cdd:cd07876     26 LKPIGSGAQGIVCAAFDTVLGINVAVKKLSR--------------------PFQNQTHAKR--AYRELVLLKCVNHKNII 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2826 SLLDTFeTPTSYV-------LVLEMADQGRlldCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQS 2898
Cdd:cd07876     84 SLLNVF-TPQKSLeefqdvyLVMELMDANL---CQVIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSD 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907111721 2899 LakpTIKLADFGDAVQLNTTYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSG 2960
Cdd:cd07876    160 C---TLKILDFGLARTACTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKG 218
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
2870-3017 1.43e-11

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 69.90  E-value: 1.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2870 EVLEAVRYLHNCRIAHLDLKPENILVdqsLAKPTIKLADFGDAVQLNTTYYI---HQLLGNPEFAAPEIILGNPVSLTAD 2946
Cdd:PTZ00283   151 QVLLAVHHVHSKHMIHRDIKSANILL---CSNGLVKLGDFGFSKMYAATVSDdvgRTFCGTPYYVAPEIWRRKPYSKKAD 227
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907111721 2947 TWSVGVLTYVLLSGVSPFLDDSVEETCLNIC--RLDFSFPEdyfqgVSQKAKEFVCFLLQEDPAKRPSAALAL 3017
Cdd:PTZ00283   228 MFSLGVLLYELLTLKRPFDGENMEEVMHKTLagRYDPLPPS-----ISPEMQEIVTALLSSDPKRRPSSSKLL 295
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
2768-3021 1.49e-11

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. 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 CDK9 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: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 68.16  E-value: 1.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKfvnKKLMKRDQ----VT--HELGILQNLQHPLLVSLLDTFETPT------ 2835
Cdd:cd07865     14 YEKLAKIGQGTFGEVFKARHRKTGQIVALK---KVLMENEKegfpITalREIKILQLLKHENVVNLIEICRTKAtpynry 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2836 --SYVLVLEMADQ---GRLLDCVVRWgslTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFG 2910
Cdd:cd07865     91 kgSIYLVFEFCEHdlaGLLSNKNVKF---TLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKD---GVLKLADFG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2911 davqLNTTYYIHQLLGNPEFA---------APEIILGN-----PVsltaDTWSVGVLTYVLLSGvSPFLDDSVEETCLN- 2975
Cdd:cd07865    165 ----LARAFSLAKNSQPNRYTnrvvtlwyrPPELLLGErdygpPI----DMWGAGCIMAEMWTR-SPIMQGNTEQHQLTl 235
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907111721 2976 ---IC------------RLD----FSFPEDYFQGVSQKAKEFV-----CFLLQE----DPAKRPSAALALQEQW 3021
Cdd:cd07865    236 isqLCgsitpevwpgvdKLElfkkMELPQGQKRKVKERLKPYVkdpyaLDLIDKllvlDPAKRIDADTALNHDF 309
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
2774-3012 1.52e-11

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 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: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 67.71  E-value: 1.52e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFV---NKKlmKRDQVTHELGILQNLQHPLLVSLLD------TFETPTSYvLVLEMA 2844
Cdd:cd13986      8 LGEGGFSFVYLVEDLSTGRLYALKKIlchSKE--DVKEAMREIENYRLFNHPNILRLLDsqivkeAGGKKEVY-LLLPYY 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 DQGRLLD----CVVRWGSLTEGKVRAHLGEVLEAVRYLHNCR---IAHLDLKPENILVDQSlakPTIKLADFGDAVQ--- 2914
Cdd:cd13986     85 KRGSLQDeierRLVKGTFFPEDRILHIFLGICRGLKAMHEPElvpYAHRDIKPGNVLLSED---DEPILMDLGSMNPari 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2915 -LNTTyyiHQLLGNPEFA---------APEiiLGNPVSLT-----ADTWSVGVLTYVLLSGVSPF-----LDDSVEetcL 2974
Cdd:cd13986    162 eIEGR---REALALQDWAaehctmpyrAPE--LFDVKSHCtidekTDIWSLGCTLYALMYGESPFerifqKGDSLA---L 233
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1907111721 2975 NICRLDFSFPEDyfQGVSQKAKEFVCFLLQEDPAKRPS 3012
Cdd:cd13986    234 AVLSGNYSFPDN--SRYSEELHQLVKSMLVVNPAERPS 269
SPEC smart00150
Spectrin repeats;
878-976 1.58e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 63.12  E-value: 1.58e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721   878 RHLQAEVKQVLGWIRNGESMLNAgLITASSLQEAEQLQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDMIRDCA 957
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79
                            90
                    ....*....|....*....
gi 1907111721   958 EKVASHWQQLMLKMEDRLK 976
Cdd:smart00150   80 EELNERWEELKELAEERRQ 98
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
2760-3023 1.61e-11

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 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: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 68.15  E-value: 1.61e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2760 WKDNFDAFYSEVAELGRGRFAVVKKCDQKGTKRAVATK---FVNKKLMKRDQ-VTHELGILQNLQHPLLVSLLDTFETPT 2835
Cdd:cd06635     19 FKEDPEKLFSDLREIGHGSFGAVYFARDVRTSEVVAIKkmsYSGKQSNEKWQdIIKEVKFLQRIKHPNSIEYKGCYLREH 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2836 SYVLVLE--MADQGRLLDcvVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILvdqsLAKP-TIKLADFGDA 2912
Cdd:cd06635     99 TAWLVMEycLGSASDLLE--VHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNIL----LTEPgQVKLADFGSA 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2913 VQLNTTyyiHQLLGNPEFAAPEIILG---NPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICR-----LDFSFP 2984
Cdd:cd06635    173 SIASPA---NSFVGTPYWMAPEVILAmdeGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQnesptLQSNEW 249
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1907111721 2985 EDYFqgvsqkaKEFVCFLLQEDPAKRPSAALALQEQWLQ 3023
Cdd:cd06635    250 SDYF-------RNFVDSCLQKIPQDRPTSEELLKHMFVL 281
SPEC smart00150
Spectrin repeats;
313-413 1.86e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 62.73  E-value: 1.86e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721   313 FEQDAEKMFDWITHNKGLFlnSYTEIGTSHPHAMELQTQHNHFAMNCMNVYVNINRIMSVANRLVESGHYASQQIKQIAN 392
Cdd:smart00150    3 FLRDADELEAWLEEKEQLL--ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 1907111721   393 QLEQEWKAFAAALDERSTLLD 413
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
2662-2748 2.10e-11

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 62.21  E-value: 2.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2662 PLSEVTCETGETVVFRCRVCGRPKASITWKgPEHNTLNNDDHYSISYSDIGEATLKIIGVSTEDDGIYTCIAVNDMGSAS 2741
Cdd:cd20973      3 TLRDKEVVEGSAARFDCKVEGYPDPEVKWM-KDDNPIVESRRFQIDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEAT 81

                   ....*..
gi 1907111721 2742 SSASLRV 2748
Cdd:cd20973     82 CSAELTV 88
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
2768-2999 2.11e-11

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 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: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 68.20  E-value: 2.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRA--VATK-----FVNKKLMKRdqVTHELGILQNLQ-HPLLVSLLDT---FETPTS 2836
Cdd:cd07857      2 YELIKELGQGAYGIVCSARNAETSEEetVAIKkitnvFSKKILAKR--ALRELKLLRHFRgHKNITCLYDMdivFPGNFN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2837 YVLVLEmadqgRLLDC----VVRWGS-LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFG- 2910
Cdd:cd07857     80 ELYLYE-----ELMEAdlhqIIRSGQpLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVN---ADCELKICDFGl 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2911 ----DAVQLNTTYYIHQLLGNPEFAAPEIILGN-PVSLTADTWSVGVLTYVLLsGVSPFL--DDSVEETCLNICRLDfSF 2983
Cdd:cd07857    152 argfSENPGENAGFMTEYVATRWYRAPEIMLSFqSYTKAIDVWSVGCILAELL-GRKPVFkgKDYVDQLNQILQVLG-TP 229
                          250
                   ....*....|....*..
gi 1907111721 2984 PEDYFQGV-SQKAKEFV 2999
Cdd:cd07857    230 DEETLSRIgSPKAQNYI 246
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
2775-2964 2.75e-11

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. 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.The MLTK 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: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 66.52  E-value: 2.75e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2775 GRGRFAVVKKCDQKGTKRAVATKfvnkKLMKRDQVTHelgILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDCVV 2854
Cdd:cd14060      2 GGGSFGSVYRAIWVSQDKEVAVK----KLLKIEKEAE---ILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFDYLN 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2855 RWGS--LTEGKVRAHLGEVLEAVRYLHN---CRIAHLDLKPENILVdqsLAKPTIKLADFGDAVQLNTTYYIhQLLGNPE 2929
Cdd:cd14060     75 SNESeeMDMDQIMTWATDIAKGMHYLHMeapVKVIHRDLKSRNVVI---AADGVLKICDFGASRFHSHTTHM-SLVGTFP 150
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1907111721 2930 FAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPF 2964
Cdd:cd14060    151 WMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPF 185
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
2773-2964 2.76e-11

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 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: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 66.89  E-value: 2.76e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRA--VATKFVNKKLMK--RDQVTHELGILQNLQHPLLVSLLDTFETpTSYVLVLEMADQGR 2848
Cdd:cd05115     11 ELGSGNFGCVKKGVYKMRKKQidVAIKVLKQGNEKavRDEMMREAQIMHQLDNPYIVRMIGVCEA-EALMLVMEMASGGP 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVV-RWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENIL-VDQSLAKptikLADFG--DAVQLNTTYYIHQL 2924
Cdd:cd05115     90 LNKFLSgKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLlVNQHYAK----ISDFGlsKALGADDSYYKARS 165
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1907111721 2925 LGN-P-EFAAPEIILGNPVSLTADTWSVGVLTYVLLS-GVSPF 2964
Cdd:cd05115    166 AGKwPlKWYAPECINFRKFSSRSDVWSYGVTMWEAFSyGQKPY 208
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
2773-2935 2.78e-11

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 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: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 66.57  E-value: 2.78e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRF-AVVKKCDQKGTKRAVATKFVNKKLMK--RDQVTHELGILQNLQHPLLVSLLDTFETPTS----YVLVLEMAD 2845
Cdd:cd14033      8 EIGRGSFkTVYRGLDTETTVEVAWCELQTRKLSKgeRQRFSEEVEMLKGLQHPNIVRFYDSWKSTVRghkcIILVTELMT 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2846 QGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHN--CRIAHLDLKPENILVDQSLAkpTIKLADFGDAVqLNTTYYIHQ 2923
Cdd:cd14033     88 SGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSrcPPILHRDLKCDNIFITGPTG--SVKIGDLGLAT-LKRASFAKS 164
                          170
                   ....*....|..
gi 1907111721 2924 LLGNPEFAAPEI 2935
Cdd:cd14033    165 VIGTPEFMAPEM 176
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
2768-3022 2.98e-11

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 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: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 67.81  E-value: 2.98e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATK-----FVNKKLMKRdqVTHELGILQNLQHPLLVSLLDTFeTPTSYV---- 2838
Cdd:cd07874     19 YQNLKPIGSGAQGIVCAAYDAVLDRNVAIKklsrpFQNQTHAKR--AYRELVLMKCVNHKNIISLLNVF-TPQKSLeefq 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2839 ---LVLEMADQGRlldCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQL 2915
Cdd:cd07874     96 dvyLVMELMDANL---CQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDC---TLKILDFGLARTA 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2916 NTTYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLT------YVLLSGVS----------------PFLDDSVEETC 2973
Cdd:cd07874    170 GTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMgemvrhKILFPGRDyidqwnkvieqlgtpcPEFMKKLQPTV 249
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907111721 2974 LNICR-------LDFS--FPEDYFQGVSQ-------KAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd07874    250 RNYVEnrpkyagLTFPklFPDSLFPADSEhnklkasQARDLLSKMLVIDPAKRISVDEALQHPYI 314
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
2802-3017 3.28e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 68.10  E-value: 3.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2802 KLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLE---------MADQGRLLDCvvrwgsltegKVRAHLGEVL 2872
Cdd:PHA03212   123 KAGQRGGTATEAHILRAINHPSIIQLKGTFTYNKFTCLILPryktdlycyLAAKRNIAIC----------DILAIERSVL 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2873 EAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDA---VQLNTTYYiHQLLGNPEFAAPEIILGNPVSLTADTWS 2949
Cdd:PHA03212   193 RAIQYLHENRIIHRDIKAENIFINHP---GDVCLGDFGAAcfpVDINANKY-YGWAGTIATNAPELLARDPYGPAVDIWS 268
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2950 VGVLTYVLLSGV-SPFLDDSVEETCLN------ICRLDFSFPEDY-----------FQGVSQKAKE-------------- 2997
Cdd:PHA03212   269 AGIVLFEMATCHdSLFEKDGLDGDCDSdrqiklIIRRSGTHPNEFpidaqanldeiYIGLAKKSSRkpgsrplwtnlyel 348
                          250       260
                   ....*....|....*....|....*.
gi 1907111721 2998 ------FVCFLLQEDPAKRPSAALAL 3017
Cdd:PHA03212   349 pidleyLICKMLAFDAHHRPSAEALL 374
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
2768-3022 3.30e-11

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. 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 MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 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: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 66.59  E-value: 3.30e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVnkKLMKRDQ---VTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMA 2844
Cdd:cd06646     11 YELIQRVGSGTYGDVYKARNLHTGELAAVKII--KLEPGDDfslIQQEIFMVKECKHCNIVAYFGSYLSREKLWICMEYC 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 DQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTYYIHQ- 2923
Cdd:cd06646     89 GGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDN---GDVKLADFGVAAKITATIAKRKs 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2924 LLGNPEFAAPEIIL---GNPVSLTADTWSVGVLTYVLLSGVSPFLDdsveetcLNICRLDFSFPEDYFQGVSQKAK---- 2996
Cdd:cd06646    166 FIGTPYWMAPEVAAvekNGGYNQLCDIWAVGITAIELAELQPPMFD-------LHPMRALFLMSKSNFQPPKLKDKtkws 238
                          250       260       270
                   ....*....|....*....|....*....|
gi 1907111721 2997 ----EFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd06646    239 stfhNFVKISLTKNPKKRPTAERLLTHLFV 268
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
418-639 3.34e-11

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 65.54  E-value: 3.34e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  418 FHQKAEKYMSNVDSWCKACGEVDLPSELQDLEDAIHHHQGIYEHITLAYSEVSQdgkslLDKLqrpltpgsSDSLTASAN 497
Cdd:cd00176      5 FLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEA-----LNEL--------GEQLIEEGH 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  498 YSKAVHHvlDVIHEVLHHQRQLENIWQHRKVRLHQRLQLCVFQQDVQQVLDWIENHGEAFLSkhTGVGKSLHRARALQKR 577
Cdd:cd00176     72 PDAEEIQ--ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALAS--EDLGKDLESVEELLKK 147
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907111721  578 HEDFEEVAQNTYTNADKLLEAAEQLAQTGECD-PEEIYQAAHQLEDRIQDFVRRVEQRKILLD 639
Cdd:cd00176    148 HKELEEELEAHEPRLKSLNELAEELLEEGHPDaDEEIEEKLEELNERWEELLELAEERQKKLE 210
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
2773-2964 3.66e-11

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 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: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 66.58  E-value: 3.66e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMK-------RDQVTHELGILQNLQHPLLVSLLD--TFETPTSyvLVLEM 2843
Cdd:cd05091     13 ELGEDRFGKVYKGHLFGTAPGEQTQAVAIKTLKdkaegplREEFRHEAMLRSRLQHPNIVCLLGvvTKEQPMS--MIFSY 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQGRLLDCVVRW------GSLTEGK-VRAHL---------GEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLA 2907
Cdd:cd05091     91 CSHGDLHEFLVMRsphsdvGSTDDDKtVKSTLepadflhivTQIAAGMEYLSSHHVVHKDLATRNVLVFDKL---NVKIS 167
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907111721 2908 DFGDAVQLNTTYYiHQLLGNPEFA----APEIILGNPVSLTADTWSVGVLTYVLLS-GVSPF 2964
Cdd:cd05091    168 DLGLFREVYAADY-YKLMGNSLLPirwmSPEAIMYGKFSIDSDIWSYGVVLWEVFSyGLQPY 228
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
2768-3013 4.19e-11

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR 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: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 66.36  E-value: 4.19e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVnkKLMKRdQVTHELGILQNLQHPLLVSLLDTFETP------------- 2834
Cdd:cd14047      8 FKEIELIGSGGFGQVFKAKHRIDGKTYAIKRV--KLNNE-KAEREVKALAKLDHPNIVRYNGCWDGFdydpetsssnssr 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2835 --TSYVLV-LEMADQGRLLDCVVRWGSLTEGKVRAH--LGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADF 2909
Cdd:cd14047     85 skTKCLFIqMEFCEKGTLESWIEKRNGEKLDKVLALeiFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTG---KVKIGDF 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2910 GDAVQLNTTYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDYfq 2989
Cdd:cd14047    162 GLVTSLKNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCDSAFEKSKFWTDLRNGILPDIFDKRY-- 239
                          250       260
                   ....*....|....*....|....
gi 1907111721 2990 gvsQKAKEFVCFLLQEDPAKRPSA 3013
Cdd:cd14047    240 ---KIEKTIIKKMLSKKPEDRPNA 260
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
2773-2952 4.89e-11

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like 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: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 65.83  E-value: 4.89e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKK---CDQKGTKRAVATKFVNKKLMKR----DQVTHELGILQNLQHPLLVSLLDTFETPtSYVLVLEMAD 2845
Cdd:cd05040      2 KLGDGSFGVVRRgewTTPSGKVIQVAVKCLKSDVLSQpnamDDFLKEVNAMHSLDHPNLIRLYGVVLSS-PLMMVTELAP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2846 QGRLLDCV-VRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdqsLAKPTIKLADFG--DAVQLNTTYYIH 2922
Cdd:cd05040     81 LGSLLDRLrKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILL---ASKDKVKIGDFGlmRALPQNEDHYVM 157
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1907111721 2923 QLLGNPEFA--APEIILGNPVSLTADTWSVGV 2952
Cdd:cd05040    158 QEHRKVPFAwcAPESLKTRKFSHASDVWMFGV 189
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
2774-3023 4.89e-11

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk 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: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 65.77  E-value: 4.89e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVatkfvnkKLMKRDQVTH----ELGILQNLQHPLLVSLLDTF-ETPTSYVLVLEMADQGR 2848
Cdd:cd05082     14 IGKGEFGDVMLGDYRGNKVAV-------KCIKNDATAQaflaEASVMTQLRHSNLVQLLGVIvEEKGGLYIVTEYMAKGS 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVVRWG-SLTEGKVRAHLG-EVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQLNTTYYIHQLlg 2926
Cdd:cd05082     87 LVDYLRSRGrSVLGGDCLLKFSlDVCEAMEYLEGNNFVHRDLAARNVLVSE---DNVAKVSDFGLTKEASSTQDTGKL-- 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2927 nP-EFAAPEIILGNPVSLTADTWSVGVLTYVLLS-GVSPFLDDSVEETclnICRLDFSFPEDYFQGVSQKAKEFV--CFL 3002
Cdd:cd05082    162 -PvKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPYPRIPLKDV---VPRVEKGYKMDAPDGCPPAVYDVMknCWH 237
                          250       260
                   ....*....|....*....|.
gi 1907111721 3003 LqeDPAKRPSaALALQEqWLQ 3023
Cdd:cd05082    238 L--DAAMRPS-FLQLRE-QLE 254
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
2771-3012 6.24e-11

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 65.68  E-value: 6.24e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2771 VAELGRGRFAVVKKCDQKGTKRaVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVlVLEMADQGRLL 2850
Cdd:cd05067     12 VERLGAGQFGEVWMGYYNGHTK-VAIKSLKQGSMSPDAFLAEANLMKQLQHQRLVRLYAVVTQEPIYI-ITEYMENGSLV 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2851 DCV-VRWGS-LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQLNTTYYIHQLLGN- 2927
Cdd:cd05067     90 DFLkTPSGIkLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTL---SCKIADFGLARLIEDNEYTAREGAKf 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2928 P-EFAAPEIILGNPVSLTADTWSVGV-LTYVLLSGVSPFLDDSVEETCLNICRLdFSFPEDyfQGVSQKAKEFVCFLLQE 3005
Cdd:cd05067    167 PiKWTAPEAINYGTFTIKSDVWSFGIlLTEIVTHGRIPYPGMTNPEVIQNLERG-YRMPRP--DNCPEELYQLMRLCWKE 243

                   ....*..
gi 1907111721 3006 DPAKRPS 3012
Cdd:cd05067    244 RPEDRPT 250
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
2773-2964 6.26e-11

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx 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: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 65.67  E-value: 6.26e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGtKRAVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDc 2852
Cdd:cd05113     11 ELGTGQFGVVKYGKWRG-QYDVAIKMIKEGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLN- 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2853 vvrwgSLTEGKVRAHLGEVLE-------AVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQLNTTYYIHQLL 2925
Cdd:cd05113     89 -----YLREMRKRFQTQQLLEmckdvceAMEYLESKQFLHRDLAARNCLVNDQG---VVKVSDFGLSRYVLDDEYTSSVG 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907111721 2926 GN--PEFAAPEIILGNPVSLTADTWSVGVLTYVLLS-GVSPF 2964
Cdd:cd05113    161 SKfpVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPY 202
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
2768-3018 1.09e-10

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) 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-kB 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. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 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: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 65.08  E-value: 1.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVnkKLMKRDQ----VTHELGILQNLQHPLLVSLLDT-FETPTSYVLvLE 2842
Cdd:cd14046      8 FEELQVLGKGAFGQVVKVRNKLDGRYYAIKKI--KLRSESKnnsrILREVMLLSRLNHQHVVRYYQAwIERANLYIQ-ME 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 MADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDAVQLNTTYYIH 2922
Cdd:cd14046     85 YCEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLD---SNGNVKIGDFGLATSNKLNVELA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2923 QLLGNPEFAAPEIILGNpvsltaDTWSVGVLTYV---LLSGVSPFLDDSVE---------ETC------------LNICR 2978
Cdd:cd14046    162 TQDINKSTSAALGSSGD------LTGNVGTALYVapeVQSGTKSTYNEKVDmyslgiiffEMCypfstgmervqiLTALR 235
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1907111721 2979 L-DFSFPEDYFQGVSQKAKEFVCFLLQEDPAKRPSAALALQ 3018
Cdd:cd14046    236 SvSIEFPPDFDDNKHSKQAKLIRWLLNHDPAKRPSAQELLK 276
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
2674-2743 1.28e-10

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 59.65  E-value: 1.28e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2674 VVFRCRVCGRPKASITWKGPehNTLNNDDHYSISYSDIGEATLKIIGVSTEDDGIYTCIAVNDMGSASSS 2743
Cdd:cd00096      1 VTLTCSASGNPPPTITWYKN--GKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASA 68
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
2774-2910 1.35e-10

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 61.69  E-value: 1.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVN-KKLMKRDQVTHELGILQ-NLQHPLLV-SLLDTFETPTSYVLVLEMADQGRLL 2850
Cdd:cd13968      1 MGEGASAKVFWAEGECTTIGVAVKIGDdVNNEEGEDLESEMDILRrLKGLELNIpKVLVTEDVDGPNILLMELVKGGTLI 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2851 DcVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFG 2910
Cdd:cd13968     81 A-YTQEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSE---DGNVKLIDFG 136
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
2773-2935 1.42e-10

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-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: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 64.71  E-value: 1.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRAVA-TKFVNKKLMK--RDQVTHELGILQNLQHPLLVSLLDTFETPTS----YVLVLEMAD 2845
Cdd:cd14032      8 ELGRGSFKTVYKGLDTETWVEVAwCELQDRKLTKveRQRFKEEAEMLKGLQHPNIVRFYDFWESCAKgkrcIVLVTELMT 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2846 QGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCR--IAHLDLKPENILVDQSLAkpTIKLADFGDAVqLNTTYYIHQ 2923
Cdd:cd14032     88 SGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGPTG--SVKIGDLGLAT-LKRASFAKS 164
                          170
                   ....*....|..
gi 1907111721 2924 LLGNPEFAAPEI 2935
Cdd:cd14032    165 VIGTPEFMAPEM 176
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
2774-2960 1.52e-10

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 65.92  E-value: 1.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFA-VVKKCDQKgTKRAVATKFV-NKKLMKRdQVTHELGILQNLQHP------LLVSLLD----------TFE--T 2833
Cdd:cd14224     73 IGKGSFGqVVKAYDHK-THQHVALKMVrNEKRFHR-QAAEEIRILEHLKKQdkdntmNVIHMLEsftfrnhicmTFEllS 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2834 PTSYVLVLEMADQGRLLDCVVRWgsltegkvrAHlgEVLEAVRYLHNCRIAHLDLKPENILVDQSlAKPTIKLADFGDAV 2913
Cdd:cd14224    151 MNLYELIKKNKFQGFSLQLVRKF---------AH--SILQCLDALHRNKIIHCDLKPENILLKQQ-GRSGIKVIDFGSSC 218
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1907111721 2914 QLNTTYYIHqlLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSG 2960
Cdd:cd14224    219 YEHQRIYTY--IQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTG 263
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
2772-3019 1.53e-10

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like 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: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 64.29  E-value: 1.53e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2772 AELGRGRFAVVKKCDQKGTKraVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLD 2851
Cdd:cd05039     12 ELIGKGEFGDVMLGDYRGQK--VAVKCLKDDSTAAQAFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVTEYMAKGSLVD 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2852 CVVRWGsltegkvRAHLG---------EVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQLNTTYYIH 2922
Cdd:cd05039     90 YLRSRG-------RAVITrkdqlgfalDVCEGMEYLESKKFVHRDLAARNVLVSEDN---VAKVSDFGLAKEASSNQDGG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2923 QLlgnP-EFAAPEIILGNPVSLTADTWSVGVLTYVLLS-GVSPF----LDDSVE-----------ETClnicrldfsfPE 2985
Cdd:cd05039    160 KL---PiKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPYpripLKDVVPhvekgyrmeapEGC----------PP 226
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1907111721 2986 DYFQGVSQkakefvCFllQEDPAKRPSAALALQE 3019
Cdd:cd05039    227 EVYKVMKN------CW--ELDPAKRPTFKQLREK 252
PH_PLEKHG1_G2_G3 cd13243
Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) ...
1417-1560 1.80e-10

Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) domain; PLEKHG1 (also called ARHGEF41), PLEKHG2 (also called ARHGEF42 or CLG/common-site lymphoma/leukemia guanine nucleotide exchange factor2), and PLEKHG3 (also called ARHGEF43) have RhoGEF DH/double-homology domains in tandem with a PH domain which is involved in phospholipid binding. They function as a guanine nucleotide exchange factor (GEF) and are involved in the regulation of Rho protein signal transduction. Mutations in PLEKHG1 have been associated panic disorder (PD), an anxiety disorder characterized by panic attacks and anticipatory anxiety. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270063 [Multi-domain]  Cd Length: 147  Bit Score: 61.60  E-value: 1.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1417 EIKDGLEVMLSVPKRAND-------AMHL----SMLEGFDE-NIESQGELILQESFqvwdpkTLIRKGRERHLFLFEMSL 1484
Cdd:cd13243      3 VVEEALDTMTQVAWHINDmkrkhehAVRVqeiqSLLDGWEGpELTTYGDLVLEGTF------RMAGAKNERLLFLFDKML 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907111721 1485 VFSKEVKDSSgrskYLYKSKLFTSELGVTEHVEGDPCKFalWVGRTPTSDNKIVLKASSIENKQDWIKHIREVIQE 1560
Cdd:cd13243     77 LITKKREDGI----LQYKTHIMCSNLMLSESIPKEPLSF--QVLPFDNPKLQYTLQAKNQEQKRLWTQEIKRLILE 146
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
2762-2964 2.09e-10

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: 64.44  E-value: 2.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2762 DNFDA--FYSEVAELGRGRFAVVKKCDQKGTKRAVatkfvnKKLMK---------RDQVTHELGILQNLQHPLLVSLLDT 2830
Cdd:cd14158      9 NNFDErpISVGGNKLGEGGFGVVFKGYINDKNVAV------KKLAAmvdistedlTKQFEQEIQVMAKCQHENLVELLGY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2831 FETPTSYVLVLEMADQGRLLD---CV-----VRWG---SLTEGKVRahlgevleAVRYLHNCRIAHLDLKPENILVDQSL 2899
Cdd:cd14158     83 SCDGPQLCLVYTYMPNGSLLDrlaCLndtppLSWHmrcKIAQGTAN--------GINYLHENNHIHRDIKSANILLDETF 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907111721 2900 akpTIKLADFGDA---VQLNTTYYIHQLLGNPEFAAPEIILGNpVSLTADTWSVGVLTYVLLSGVSPF 2964
Cdd:cd14158    155 ---VPKISDFGLArasEKFSQTIMTERIVGTTAYMAPEALRGE-ITPKSDIFSFGVVLLEIITGLPPV 218
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
2774-2964 2.19e-10

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 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: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 64.82  E-value: 2.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKR--DQVTHELGILQNLQHPLLVSLLDTFETPTSY--VLVLEMADQGRL 2849
Cdd:cd13988      1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSFMRplDVQMREFEVLKKLNHKNIVKLFAIEEELTTRhkVLVMELCPCGSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2850 ---LDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENIL-VDQSLAKPTIKLADFGDAVQLNTTYYIHQLL 2925
Cdd:cd13988     81 ytvLEEPSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrVIGEDGQSVYKLTDFGAARELEDDEQFVSLY 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1907111721 2926 GNPEFAAPEI----IL----GNPVSLTADTWSVGVLTYVLLSGVSPF 2964
Cdd:cd13988    161 GTEEYLHPDMyeraVLrkdhQKKYGATVDLWSIGVTFYHAATGSLPF 207
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
2773-2964 2.30e-10

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk 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: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 64.11  E-value: 2.30e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRaVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDC 2852
Cdd:cd05114     11 ELGSGLFGVVRLGKWRAQYK-VAIKAIREGAMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENGCLLNY 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2853 V-VRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDA-VQLNTTYYIHQLLGNP-E 2929
Cdd:cd05114     90 LrQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVN---DTGVVKVSDFGMTrYVLDDQYTSSSGAKFPvK 166
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1907111721 2930 FAAPEIILGNPVSLTADTWSVGVLTY-VLLSGVSPF 2964
Cdd:cd05114    167 WSPPEVFNYSKFSSKSDVWSFGVLMWeVFTEGKMPF 202
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
2762-2971 2.30e-10

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK1 binds with high affinity the alternative splicing factor, SRSF1 (serine/arginine-rich splicing factor 1), and regiospecifically phosphorylates 10-12 serines in its RS domain. It plays a role in the regulation of pre-mRNA splicing, chromatin structure, and germ cell development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK 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: 271118 [Multi-domain]  Cd Length: 349  Bit Score: 65.05  E-value: 2.30e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2762 DNFDAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQHP--------LLVSLLDTFET 2833
Cdd:cd14216      6 DLFNGRYHVIRKLGWGHFSTVWLSWDIQGKRFVAMKVVKSAEHYTETALDEIKLLKSVRNSdpndpnreMVVQLLDDFKI 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2834 P----TSYVLVLEMADQgRLLDCVVR--WGSLTEGKVRAHLGEVLEAVRYLHN-CRIAHLDLKPENILVD---------- 2896
Cdd:cd14216     86 SgvngTHICMVFEVLGH-HLLKWIIKsnYQGLPLPCVKKIIRQVLQGLDYLHTkCRIIHTDIKPENILLSvneqyirrla 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2897 -----------------QSLAKPTIKLADFGDAVQLNTtyYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLS 2959
Cdd:cd14216    165 aeatewqrnflvnplepKNAEKLKVKIADLGNACWVHK--HFTEDIQTRQYRSLEVLIGSGYNTPADIWSTACMAFELAT 242
                          250
                   ....*....|..
gi 1907111721 2960 GVSPFLDDSVEE 2971
Cdd:cd14216    243 GDYLFEPHSGED 254
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
2662-2748 2.53e-10

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 59.44  E-value: 2.53e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2662 PLSEVTCETGETVVFRCRVCGRPKASITWKGPEHNTLNNDDHYsiSYSDIGEaTLKIIGVSTEDDGIYTCIAVNDM-GSA 2740
Cdd:cd20970      8 PSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNTRY--IVRENGT-TLTIRNIRRSDMGIYLCIASNGVpGSV 84

                   ....*...
gi 1907111721 2741 SSSASLRV 2748
Cdd:cd20970     85 EKRITLQV 92
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
2708-2967 2.89e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 64.90  E-value: 2.89e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2708 YSDIGEATLKIIGVST------EDDGiytCIAVNDMGSASSSASL-----RVLGPGSDGIVVtwkdnfdafyseVAELGR 2776
Cdd:PHA03209    25 YSDISDGDLEYSDDDSasesddDDDD---GLIPTKQKAREVVASLgytviKTLTPGSEGRVF------------VATKPG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2777 GRFAVVKKCDQKGTKravatkfvnkkLMkrdqvthELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDCVVRW 2856
Cdd:PHA03209    90 QPDPVVLKIGQKGTT-----------LI-------EAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYSSDLYTYLTKRS 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2857 GSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGdAVQLNTTY-YIHQLLGNPEFAAPEI 2935
Cdd:PHA03209   152 RPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFIN---DVDQVCIGDLG-AAQFPVVApAFLGLAGTVETNAPEV 227
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1907111721 2936 ILGNPVSLTADTWSVGVLTYVLLSGVSPFLDD 2967
Cdd:PHA03209   228 LARDKYNSKADIWSAGIVLFEMLAYPSTIFED 259
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
2774-2964 2.95e-10

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK 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: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 63.60  E-value: 2.95e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKK---CDQKGTKRAVATKF--VNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYvLVLEMADQGR 2848
Cdd:cd05056     14 IGEGQFGDVYQgvyMSPENEKIAVAVKTckNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVITENPVW-IVMELAPLGE 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCV-VRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdqsLAKPTIKLADFGDAVQLNTTYYIHQLLGN 2927
Cdd:cd05056     93 LRSYLqVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLV---SSPDCVKLGDFGLSRYMEDESYYKASKGK 169
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1907111721 2928 -P-EFAAPEIILGNPVSLTADTWSVGVLTYVLLS-GVSPF 2964
Cdd:cd05056    170 lPiKWMAPESINFRRFTSASDVWMFGVCMWEILMlGVKPF 209
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
2657-2748 3.05e-10

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 59.05  E-value: 3.05e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2657 PEFVIPLSEVTCETGETVVFRCRVCGRPKASITWKGPEHNTLNNDDHySISYSDIGEATLKIIGVSTEDDGIYTCIAVND 2736
Cdd:cd05744      1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAH-KMLVRENGRHSLIIEPVTKRDAGIYTCIARNR 79
                           90
                   ....*....|..
gi 1907111721 2737 MGSASSSASLRV 2748
Cdd:cd05744     80 AGENSFNAELVV 91
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
2819-2968 3.77e-10

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 65.59  E-value: 3.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2819 LQHPLLVSLLDTFETPTSYVLVLEMADqGRLLDCVVRwgslTEGKVRAH-----LGEVLEAVRYLHNCRIAHLDLKPENI 2893
Cdd:NF033483    64 LSHPNIVSVYDVGEDGGIPYIVMEYVD-GRTLKDYIR----EHGPLSPEeaveiMIQILSALEHAHRNGIVHRDIKPQNI 138
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907111721 2894 LVDQSlakPTIKLADFGDAVQLN--TTYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDS 2968
Cdd:NF033483   139 LITKD---GRVKVTDFGIARALSstTMTQTNSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDS 212
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
2768-2964 3.81e-10

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta 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: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 64.54  E-value: 3.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATK-----FVNKKLMKRdqVTHELGILQNLQHPLLVSLLDTFETPTSY----- 2837
Cdd:cd07879     17 YTSLKQVGSGAYGSVCSAIDKRTGEKVAIKklsrpFQSEIFAKR--AYRELTLLKHMQHENVIGLLDVFTSAVSGdefqd 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2838 ---VLVLEMADQGRlldcvVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQ 2914
Cdd:cd07879     95 fylVMPYMQTDLQK-----IMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDC---ELKILDFGLARH 166
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907111721 2915 LN---TTYYIHQLlgnpeFAAPEIILG-NPVSLTADTWSVGVLTYVLLSGVSPF 2964
Cdd:cd07879    167 ADaemTGYVVTRW-----YRAPEVILNwMHYNQTVDIWSVGCIMAEMLTGKTLF 215
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
2768-3013 3.81e-10

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: 63.22  E-value: 3.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKC-DQKGTKRAVATKFVNKKLMKRDQ--VTHELGILQNLQHPLLVSLLDTFETPTSYVLVL--- 2841
Cdd:cd08223      2 YQFLRVIGKGSYGEVWLVrHKRDRKQYVIKKLNLKNASKRERkaAEQEAKLLSKLKHPNIVSYKESFEGEDGFLYIVmgf 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2842 -EMAD--------QGRLLD--CVVRWgsltegkvrahLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFG 2910
Cdd:cd08223     82 cEGGDlytrlkeqKGVLLEerQVVEW-----------FVQIAMALQYMHERNILHRDLKTQNIFLTKS---NIIKVGDLG 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2911 DAVQLNTTYYI-HQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDF-SFPEDYf 2988
Cdd:cd08223    148 IARVLESSSDMaTTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLpPMPKQY- 226
                          250       260
                   ....*....|....*....|....*
gi 1907111721 2989 qgvSQKAKEFVCFLLQEDPAKRPSA 3013
Cdd:cd08223    227 ---SPELGELIKAMLHQDPEKRPSV 248
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
2771-2965 4.35e-10

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak 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: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 63.55  E-value: 4.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2771 VAELGRGRFAVVKKC----DQKGTKRAVATKFVN--KKLMKRDQVTHELGILQNLQHPLLVSLLDTFETP--TSYVLVLE 2842
Cdd:cd05038      9 IKQLGEGHFGSVELCrydpLGDNTGEQVAVKSLQpsGEEQHMSDFKREIEILRTLDHEYIVKYKGVCESPgrRSLRLIME 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2843 MADQGRLLDcvvrwgSLTEGKVRAHLGEVL-------EAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQL 2915
Cdd:cd05038     89 YLPSGSLRD------YLQRHRDQIDLKRLLlfasqicKGMEYLGSQRYIHRDLAARNILVES---EDLVKISDFGLAKVL 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907111721 2916 NTT---YYIHQLLGNPEF-AAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFL 2965
Cdd:cd05038    160 PEDkeyYYVKEPGESPIFwYAPECLRESRFSSASDVWSFGVTLYELFTYGDPSQ 213
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
52-179 4.60e-10

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 60.03  E-value: 4.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721   52 GGPILTFPARS-NHDRIRQEDLRRLISYLACIPSEEVCKRGFTVIVDMRGSKWDS------IKPLLKILQESFPCCIHIA 124
Cdd:pfam13716    1 GRPVLVFISKLlPSRPASLDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTGVTSENfpslsfLKKAYDLLPRAFKKNLKAV 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  125 LIIKPDNFWQKQ----RTNFGSSKFEFETNMVS-LEGLTKVVDPSQLTPEFDGCLEYNHE 179
Cdd:pfam13716   81 YVVHPSTFLRTFlktlGSLLGSKKLRKKVHYVSsLSELWEGIDREQLPTELPGVLSYDEE 140
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
2807-3019 5.80e-10

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (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. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 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: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 62.74  E-value: 5.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2807 DQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDcvvrwgSLTEGKVRAHL-----GEVLEAVRYLHN- 2880
Cdd:cd14147     47 ESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAGGPLSR------ALAGRRVPPHVlvnwaVQIARGMHYLHCe 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2881 --CRIAHLDLKPENIL-----VDQSLAKPTIKLADFGDAVQLNTTYYIhQLLGNPEFAAPEIILGNPVSLTADTWSVGVL 2953
Cdd:cd14147    121 alVPVIHRDLKSNNILllqpiENDDMEHKTLKITDFGLAREWHKTTQM-SAAGTYAWMAPEVIKASTFSKGSDVWSFGVL 199
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907111721 2954 TYVLLSGVSPF--LDDSVEETCLNICRLDFSFPEDYFQGVSQKAKEfvCFllQEDPAKRPSAALALQE 3019
Cdd:cd14147    200 LWELLTGEVPYrgIDCLAVAYGVAVNKLTLPIPSTCPEPFAQLMAD--CW--AQDPHRRPDFASILQQ 263
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
2762-2987 5.81e-10

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK3 is highly expressed in the heart and skeletal muscles, and is controlled by a muscle-specific enhancer that is regulated by MEF2. It may play an important role in muscle development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK 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: 271120 [Multi-domain]  Cd Length: 365  Bit Score: 63.88  E-value: 5.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2762 DNFDAFYSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQ--------NLQHPLLVSLLDTFET 2833
Cdd:cd14218      6 DLFNGRYHVVRKLGWGHFSTVWLCWDIQRKRFVALKVVKSAVHYTETAVDEIKLLKcvrdsdpsDPKRETIVQLIDDFKI 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2834 P----TSYVLVLEMADQgRLLDCVVR--WGSLTEGKVRAHLGEVLEAVRYLHN-CRIAHLDLKPENILV----------- 2895
Cdd:cd14218     86 SgvngVHVCMVLEVLGH-QLLKWIIKsnYQGLPLPCVKSILRQVLQGLDYLHTkCKIIHTDIKPENILMcvdegyvrrla 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2896 --------------------------------DQSLAKPTIKLADFGDAVQLNTtyYIHQLLGNPEFAAPEIILGNPVSL 2943
Cdd:cd14218    165 aeatiwqqagapppsgssvsfgasdflvnplePQNADKIRVKIADLGNACWVHK--HFTEDIQTRQYRALEVLIGAEYGT 242
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1907111721 2944 TADTWSVGVLTYVLLSGVSPFLDDSVEetclnicrlDFSFPEDY 2987
Cdd:cd14218    243 PADIWSTACMAFELATGDYLFEPHSGE---------DYTRDEDH 277
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
2774-2953 7.25e-10

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: 62.12  E-value: 7.25e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKfVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDCV 2853
Cdd:cd14065      1 LGKGFFGEVYKVTHRETGKVMVMK-ELKRFDEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLEELL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2854 VRWGSLTEGKVRAHLG-EVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAVQLNTTYYIH-------QLL 2925
Cdd:cd14065     80 KSMDEQLPWSQRVSLAkDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRNAVVADFGLAREMPDEKTKKpdrkkrlTVV 159
                          170       180
                   ....*....|....*....|....*...
gi 1907111721 2926 GNPEFAAPEIILGNPVSLTADTWSVGVL 2953
Cdd:cd14065    160 GSPYWMAPEMLRGESYDEKVDVFSFGIV 187
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
2768-2953 8.31e-10

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 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: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 63.52  E-value: 8.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATK-----FVNKKLMKRdqVTHELGILQNLQHPLLVSLLDTFeTPTSYV---- 2838
Cdd:cd07875     26 YQNLKPIGSGAQGIVCAAYDAILERNVAIKklsrpFQNQTHAKR--AYRELVLMKCVNHKNIIGLLNVF-TPQKSLeefq 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2839 ---LVLEMADQGRlldCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQL 2915
Cdd:cd07875    103 dvyIVMELMDANL---CQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDC---TLKILDFGLARTA 176
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1907111721 2916 NTTYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVL 2953
Cdd:cd07875    177 GTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCI 214
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
2771-3022 1.07e-09

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 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: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 62.33  E-value: 1.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2771 VAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQHPL-LVSLLDTF--ETPTSY----VLVLEM 2843
Cdd:cd06636     21 VEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKKYSHHRnIATYYGAFikKSPPGHddqlWLVMEF 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQGRLLDCV--VRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTY-Y 2920
Cdd:cd06636    101 CGAGSVTDLVknTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTEN---AEVKLVDFGVSAQLDRTVgR 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2921 IHQLLGNPEFAAPEIIL--GNPVS---LTADTWSVGVLTYVLLSGVSPFLDdsveetcLNICRLDFSFPEDYFQGVSQK- 2994
Cdd:cd06636    178 RNTFIGTPYWMAPEVIAcdENPDAtydYRSDIWSLGITAIEMAEGAPPLCD-------MHPMRALFLIPRNPPPKLKSKk 250
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1907111721 2995 -AKEFVCFL---LQEDPAKRPSAALALQEQWL 3022
Cdd:cd06636    251 wSKKFIDFIegcLVKNYLSRPSTEQLLKHPFI 282
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
2774-2955 1.31e-09

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 61.53  E-value: 1.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRaVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDcv 2853
Cdd:cd05034      3 LGAGQFGEVWMGVWNGTTK-VAVKTLKPGTMSPEAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKGSLLD-- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2854 vrwgSLTEGKVRA-HLGEVL-------EAVRYLHNCRIAHLDLKPENILVDQSLAkptIKLADFGDAVQLNTTYYI-HQL 2924
Cdd:cd05034     80 ----YLRTGEGRAlRLPQLIdmaaqiaSGMAYLESRNYIHRDLAARNILVGENNV---CKVADFGLARLIEDDEYTaREG 152
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1907111721 2925 LGNP-EFAAPEIILGNPVSLTADTWSVGVLTY 2955
Cdd:cd05034    153 AKFPiKWTAPEAALYGRFTIKSDVWSFGILLY 184
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
2768-2993 1.66e-09

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 61.90  E-value: 1.66e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVT--HELGILQNLQHPLLVSLLDTFETPTSYVLVLEMAD 2845
Cdd:cd07870      2 YLNLEKLGEGSYATVYKGISRINGQLVALKVISMKTEEGVPFTaiREASLLKGLKHANIVLLHDIIHTKETLTFVFEYMH 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2846 QGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVdQSLAKptIKLADFG--DAVQLNTTYYIHQ 2923
Cdd:cd07870     82 TDLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLI-SYLGE--LKLADFGlaRAKSIPSQTYSSE 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907111721 2924 LLgNPEFAAPEIILG-NPVSLTADTWSVGVLTYVLLSGVSPFLD-DSVEETCLNICRLDFSFPEDYFQGVSQ 2993
Cdd:cd07870    159 VV-TLWYRPPDVLLGaTDYSSALDIWGAGCIFIEMLQGQPAFPGvSDVFEQLEKIWTVLGVPTEDTWPGVSK 229
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
2665-2748 1.71e-09

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 56.74  E-value: 1.71e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2665 EVTCETGETVVFRCRVCGRPKASITWKGPEHNTLNNDDHYSIsysdIGEATLKIIGVSTEDDGIYTCIAVNDMGSASSSA 2744
Cdd:cd20952      8 NQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDERITT----LENGSLQIKGAEKSDTGEYTCVALNLSGEATWSA 83

                   ....
gi 1907111721 2745 SLRV 2748
Cdd:cd20952     84 VLDV 87
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
2810-2955 1.71e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 62.99  E-value: 1.71e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2810 THELGILQNLQHPLLVSLLDTFETPTSYVLVLE--MADQGRLLDCVVRwgSLTEGKVRAHLGEVLEAVRYLHNCRIAHLD 2887
Cdd:PHA03211   208 VHEARLLRRLSHPAVLALLDVRVVGGLTCLVLPkyRSDLYTYLGARLR--PLGLAQVTAVARQLLSAIDYIHGEGIIHRD 285
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907111721 2888 LKPENILVDqslAKPTIKLADFGDAVQLN---TTYYIHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTY 2955
Cdd:PHA03211   286 IKTENVLVN---GPEDICLGDFGAACFARgswSTPFHYGIAGTVDTNAPEVLAGDPYTPSVDIWSAGLVIF 353
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
2870-3017 1.93e-09

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK 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: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 61.65  E-value: 1.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2870 EVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIklADFGDAVQLNTTyyiHQLL----GNPEFAAPEIILGNPVSLTA 2945
Cdd:cd13974    140 DVVRVVEALHKKNIVHRDLKLGNMVLNKRTRKITI--TNFCLGKHLVSE---DDLLkdqrGSPAYISPDVLSGKPYLGKP 214
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907111721 2946 -DTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDyfQGVSQKAKEFVCFLLQEDPAKRPSAALAL 3017
Cdd:cd13974    215 sDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYTIPED--GRVSENTVCLIRKLLVLNPQKRLTASEVL 285
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
2765-2951 3.15e-09

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK 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: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 61.62  E-value: 3.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2765 DAFYSEVAELGRGRFAVVKKCDQKGTKRAVATK-----FVNKKLMKRdqVTHELGILQNLQHPLLVSLLDTFETP----- 2834
Cdd:cd07858      4 DTKYVPIKPIGRGAYGIVCSAKNSETNEKVAIKkianaFDNRIDAKR--TLREIKLLRHLDHENVIAIKDIMPPPhreaf 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2835 TSYVLVLEMADQGrlLDCVVRWG-SLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFG--- 2910
Cdd:cd07858     82 NDVYIVYELMDTD--LHQIIRSSqTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLN---ANCDLKICDFGlar 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907111721 2911 ---DAVQLNTTYYIHQLlgnpeFAAPEIILGNPVSLTA-DTWSVG 2951
Cdd:cd07858    157 ttsEKGDFMTEYVVTRW-----YRAPELLLNCSEYTTAiDVWSVG 196
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
2768-3023 4.11e-09

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: 61.33  E-value: 4.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRG-RFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDT---------------F 2831
Cdd:cd07854      7 YMDLRPLGCGsNGLVFSAVDSDCDKRVAVKKIVLTDPQSVKHALREIKIIRRLDHDNIVKVYEVlgpsgsdltedvgslT 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2832 ETPTSYVlVLEMADQGrlLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlaKPTIKLADFGD 2911
Cdd:cd07854     87 ELNSVYI-VQEYMETD--LANVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTE--DLVLKIGDFGL 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2912 AVQLNTTY----YIHQLLGNPEFAAPEIILG-NPVSLTADTWSVGVLTYVLLSGVS------------------PFLDDS 2968
Cdd:cd07854    162 ARIVDPHYshkgYLSEGLVTKWYRSPRLLLSpNNYTKAIDMWAAGCIFAEMLTGKPlfagaheleqmqlilesvPVVREE 241
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907111721 2969 VEETCLNI----CRLDFSFPE----DYFQGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQ 3023
Cdd:cd07854    242 DRNELLNVipsfVRNDGGEPRrplrDLLPGVNPEALDFLEQILTFNPMDRLTAEEALMHPYMS 304
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
2770-3023 4.40e-09

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK 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: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 60.50  E-value: 4.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2770 EVAEL-GRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQHPL-LVSLLDTF--ETP----TSYVLVL 2841
Cdd:cd06637      9 ELVELvGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEIKQEINMLKKYSHHRnIATYYGAFikKNPpgmdDQLWLVM 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2842 EMADQGRLLDCV--VRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakPTIKLADFGDAVQLNTTY 2919
Cdd:cd06637     89 EFCGAGSVTDLIknTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTEN---AEVKLVDFGVSAQLDRTV 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2920 -YIHQLLGNPEFAAPEIIL--GNP---VSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRldFSFPEDYFQGVSQ 2993
Cdd:cd06637    166 gRRNTFIGTPYWMAPEVIAcdENPdatYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRALFLIPR--NPAPRLKSKKWSK 243
                          250       260       270
                   ....*....|....*....|....*....|
gi 1907111721 2994 KAKEFVCFLLQEDPAKRPSAALALQEQWLQ 3023
Cdd:cd06637    244 KFQSFIESCLVKNHSQRPSTEQLMKHPFIR 273
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
2774-3019 5.61e-09

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK 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: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 60.22  E-value: 5.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTkravATKFVNKKLMKRDQ-----VTHELGILQNLQ-HPLLVSLLDTFETP--------TSYVL 2839
Cdd:cd14036      8 IAEGGFAFVYEAQDVGT----GKEYALKRLLSNEEeknkaIIQEINFMKKLSgHPNIVQFCSAASIGkeesdqgqAEYLL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2840 VLEMAdQGRLLDCVVRwgslTEGKVRAHLGEVLE-------AVRYLHNCR--IAHLDLKPENILVDqslAKPTIKLADFG 2910
Cdd:cd14036     84 LTELC-KGQLVDFVKK----VEAPGPFSPDTVLKifyqtcrAVQHMHKQSppIIHRDLKIENLLIG---NQGQIKLCDFG 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2911 ----------------------DAVQLNTTyyihqllgnPEFAAPEII---LGNPVSLTADTWSVGVLTYVLLSGVSPFL 2965
Cdd:cd14036    156 satteahypdyswsaqkrslveDEITRNTT---------PMYRTPEMIdlySNYPIGEKQDIWALGCILYLLCFRKHPFE 226
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2966 DDSVeetcLNICRLDFSFPEDyfqgvsqkAKEFVCF------LLQEDPAKRPSAALALQE 3019
Cdd:cd14036    227 DGAK----LRIINAKYTIPPN--------DTQYTVFhdlirsTLKVNPEERLSITEIVEQ 274
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
2771-2964 5.62e-09

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 60.05  E-value: 5.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2771 VAELGRGRFAVVKKCDQKGTKRaVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLL 2850
Cdd:cd05072     12 VKKLGAGQFGEVWMGYYNNSTK-VAVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEYMAKGSLL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2851 DCVV--RWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDA-VQLNTTYYIHQLLGN 2927
Cdd:cd05072     91 DFLKsdEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESL---MCKIADFGLArVIEDNEYTAREGAKF 167
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1907111721 2928 P-EFAAPEIILGNPVSLTADTWSVGVLTYVLLS-GVSPF 2964
Cdd:cd05072    168 PiKWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPY 206
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
2774-2964 6.89e-09

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 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: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 59.37  E-value: 6.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGtkRAVATKFVNKKLMKRDQVThELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDCV 2853
Cdd:cd14058      1 VGRGSFGVVCKARWRN--QIVAVKIIESESEKKAFEV-EVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLYNVL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2854 VRWGSLTEGKVRAHLGEVL---EAVRYLHNCR---IAHLDLKPENILVdqsLAKPT-IKLADFGDAVQLNTtyYIHQLLG 2926
Cdd:cd14058     78 HGKEPKPIYTAAHAMSWALqcaKGVAYLHSMKpkaLIHRDLKPPNLLL---TNGGTvLKICDFGTACDIST--HMTNNKG 152
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1907111721 2927 NPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPF 2964
Cdd:cd14058    153 SAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPF 190
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
2773-3012 7.03e-09

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 59.16  E-value: 7.03e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRaVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVlVLEMADQGRLLDc 2852
Cdd:cd14203      2 KLGQGCFGEVWMGTWNGTTK-VAIKTLKPGTMSPEAFLEEAQIMKKLRHDKLVQLYAVVSEEPIYI-VTEFMSKGSLLD- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2853 vvrwgSLTEGKVRA--------HLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAkptIKLADFGDAVQL-NTTYYIHQ 2923
Cdd:cd14203     79 -----FLKDGEGKYlklpqlvdMAAQIASGMAYIERMNYIHRDLRAANILVGDNLV---CKIADFGLARLIeDNEYTARQ 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2924 LLGNP-EFAAPEIILGNPVSLTADTWSVGVL-TYVLLSGVSPFLDDSVEETCLNICRlDFSFPEDyfQGVSQKAKEFVCF 3001
Cdd:cd14203    151 GAKFPiKWTAPEAALYGRFTIKSDVWSFGILlTELVTKGRVPYPGMNNREVLEQVER-GYRMPCP--PGCPESLHELMCQ 227
                          250
                   ....*....|.
gi 1907111721 3002 LLQEDPAKRPS 3012
Cdd:cd14203    228 CWRKDPEERPT 238
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
2674-2746 9.40e-09

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 54.51  E-value: 9.40e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907111721 2674 VVFRCRVCGRPKASITWkgpehnTLNND-----DHYSIsysdIGEATLKIIGVSTEDDGIYTCIAVNDMGSASSSASL 2746
Cdd:cd05723     15 IVFECEVTGKPTPTVKW------VKNGDvvipsDYFKI----VKEHNLQVLGLVKSDEGFYQCIAENDVGNAQASAQL 82
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
2771-2959 9.80e-09

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family 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: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 59.52  E-value: 9.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2771 VAELGRGRFAVVKKC--DQKG--TKRAVATKFVNKKLMKRDQ-VTHELGILQNLQHPLLVSLLDTFETP--TSYVLVLEM 2843
Cdd:cd05081      9 ISQLGKGNFGSVELCryDPLGdnTGALVAVKQLQHSGPDQQRdFQREIQILKALHSDFIVKYRGVSYGPgrRSLRLVMEY 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 ADQGRLLDCVVR-WGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDA--VQLNTTYY 2920
Cdd:cd05081     89 LPSGCLRDFLQRhRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVE---SEAHVKIADFGLAklLPLDKDYY 165
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1907111721 2921 IHQLLG-NPEF-AAPEIILGNPVSLTADTWSVGVLTYVLLS 2959
Cdd:cd05081    166 VVREPGqSPIFwYAPESLSDNIFSRQSDVWSFGVVLYELFT 206
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
2762-2951 1.01e-08

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK1/4 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: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 59.86  E-value: 1.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2762 DNFDAFYSEVAELGRGRFAVVKKC-DQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQHP------LLVSLLDTFETP 2834
Cdd:cd14213      8 DVLRARYEIVDTLGEGAFGKVVECiDHKMGGMHVAVKIVKNVDRYREAARSEIQVLEHLNTTdpnstfRCVQMLEWFDHH 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2835 TSYVLVLEMADQGRLlDCVVRWGSLT--EGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQS-------------- 2898
Cdd:cd14213     88 GHVCIVFELLGLSTY-DFIKENSFLPfpIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQSdyvvkynpkmkrde 166
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907111721 2899 --LAKPTIKLADFGDAvqlntTY---YIHQLLGNPEFAAPEIILGNPVSLTADTWSVG 2951
Cdd:cd14213    167 rtLKNPDIKVVDFGSA-----TYddeHHSTLVSTRHYRAPEVILALGWSQPCDVWSIG 219
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
2800-2912 1.05e-08

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 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: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 59.05  E-value: 1.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2800 NKKLMKrdqvthELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDCVVRWGSLTEGKVRAHLgEVLEAVRYLH 2879
Cdd:cd14027     35 NEALLE------EGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMHVLKKVSVPLSVKGRIIL-EIIEGMAYLH 107
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1907111721 2880 NCRIAHLDLKPENILVDQSLAkptIKLADFGDA 2912
Cdd:cd14027    108 GKGVIHKDLKPENILVDNDFH---IKIADLGLA 137
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
2657-2748 1.11e-08

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 54.72  E-value: 1.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2657 PEFVIPLSEVTCETGETVVFRCRVCGRPKASITWKGPEHNTLNNDDHYSISYSDIGEATLKIIGVSTEDDGIYTCIAVND 2736
Cdd:cd05893      1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDHYTIQRDLDGTCSLHTTASTLDDDGNYTIMAANP 80
                           90
                   ....*....|..
gi 1907111721 2737 MGSASSSASLRV 2748
Cdd:cd05893     81 QGRISCTGRLMV 92
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
2774-3013 1.13e-08

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK 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: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 59.12  E-value: 1.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATK--FVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTF-ETPTS---------YV-LV 2840
Cdd:cd14048     14 LGRGGFGVVFEAKNKVDDCNYAVKriRLPNNELAREKVLREVRALAKLDHPGIVRYFNAWlERPPEgwqekmdevYLyIQ 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2841 LEMADQGRLLDCVVRWGSLTEGKVRAHLG---EVLEAVRYLHNCRIAHLDLKPENIL--VDQslakpTIKLADFGDAV-- 2913
Cdd:cd14048     94 MQLCRKENLKDWMNRRCTMESRELFVCLNifkQIASAVEYLHSKGLIHRDLKPSNVFfsLDD-----VVKVGDFGLVTam 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2914 ----------QLNTTYYIH-QLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSveETCLNICRLDfs 2982
Cdd:cd14048    169 dqgepeqtvlTPMPAYAKHtGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELIYSFSTQMERI--RTLTDVRKLK-- 244
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1907111721 2983 FPEDYFQGVSQKAKeFVCFLLQEDPAKRPSA 3013
Cdd:cd14048    245 FPALFTNKYPEERD-MVQQMLSPSPSERPEA 274
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
2870-3022 1.16e-08

Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNT7 is a plant thylakoid-associated kinase that is essential in short- and long-term acclimation responses to cope with various light conditions in order to maintain photosynthetic redox poise for optimal photosynthetic performance. Short-term response involves state transitions over periods of minutes while the long-term response (LTR) occurs over hours to days and involves changing the relative amounts of photosystems I and II. SNT7 acts as a redox sensor and a signal transducer for both responses, which are triggered by the redox state of the plastoquinone (PQ) pool. It is positioned at the top of a phosphorylation cascade that induces state transitions by phosphorylating light-harvesting complex II (LHCII), and triggers the LTR through the phosphorylation of chloroplast proteins. The SNT7 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: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 59.37  E-value: 1.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2870 EVLEAVRYLHNCRIAHLDLKPENILVDQSlaKPTIKLADFGDAVQLNT--TYYIHQLLGNPEFAAPE-IILGN------- 2939
Cdd:cd14013    128 QILVALRKLHSTGIVHRDVKPQNIIVSEG--DGQFKIIDLGAAADLRIgiNYIPKEFLLDPRYAPPEqYIMSTqtpsapp 205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2940 -PVSLTA-------------DTWSVGVltyVLLSGVSPFL--DDSVEETCLNICRLDFSFP-----------EDYFQGVS 2992
Cdd:cd14013    206 aPVAAALspvlwqmnlpdrfDMYSAGV---ILLQMAFPNLrsDSNLIAFNRQLKQCDYDLNawrmlveprasADLREGFE 282
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1907111721 2993 ------QKAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14013    283 ildlddGAGWDLVTKLIRYKPRGRLSASAALAHPYF 318
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
2777-3021 1.18e-08

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). 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 CDC2L1 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: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 59.16  E-value: 1.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2777 GRFAVVKKCDQKGTKRAVATKFVnkKLMKRDQ---VT--HELGILQNLQHPLLVSL--------LDTFETPTSYVlvlEM 2843
Cdd:cd07843     16 GTYGVVYRARDKKTGEIVALKKL--KMEKEKEgfpITslREINILLKLQHPNIVTVkevvvgsnLDKIYMVMEYV---EH 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2844 aDQGRLLDcvVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDA--VQLNTTYYI 2921
Cdd:cd07843     91 -DLKSLME--TMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNN---RGILKICDFGLAreYGSPLKPYT 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2922 hQLLGNPEFAAPEIILGNPVSLTA-DTWSVGVLTYVLLSGvSPFLDDSVEETCLN-ICRL-----DFSFPE--------- 2985
Cdd:cd07843    165 -QLVVTLWYRAPELLLGAKEYSTAiDMWSVGCIFAELLTK-KPLFPGKSEIDQLNkIFKLlgtptEKIWPGfselpgakk 242
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2986 ------------DYFQ--GVSQKAKEFVCFLLQEDPAKRPSAALALQEQW 3021
Cdd:cd07843    243 ktftkypynqlrKKFPalSLSDNGFDLLNRLLTYDPAKRISAEDALKHPY 292
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
2671-2748 1.20e-08

Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; member of the I-set of IgSF domains; This group contains the immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins. The SALM (for synaptic adhesion-like molecules; also known as Lrfn for leucine-rich repeat and fibronectin type III domain containing) family of adhesion molecules consists of five known members: SALM1/Lrfn2, SALM2/Lrfn1, SALM3/Lrfn4, SALM4/Lrfn3, and SALM5/Lrfn5. SALMs share a similar domain structure, containing leucine-rich repeats (LRRs), an immunoglobulin (Ig) domain, and a fibronectin III (FNIII) domain, followed by a transmembrane domain and a C-terminal PDZ-binding motif. SALM5 is implicated in autism spectrum disorders (ASDs) and schizophrenia, induces presynaptic differentiation in contacting axons. SALM5 interacts with the Ig domains of LAR (Leukocyte common Antigen-Related) family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta, and PTPsigma). In addition, PTPdelta is implicated in ASDs, ADHD, bipolar disorder, and restless leg syndrome. Studies have shown that LAR-RPTPs are novel and splicing-dependent presynaptic ligands for SALM5, and that they mediate SALM5-dependent presynaptic differentiation. Furthermore, SALM5 maintains AMPA receptor (AMPAR)-mediated excitatory synaptic transmission through mechanisms involving the interaction of SALM5 with LAR-RPTPs. This group belongs to the I-set of immunoglobulin superfamily (IgSF) domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409421 [Multi-domain]  Cd Length: 88  Bit Score: 54.40  E-value: 1.20e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907111721 2671 GETVVFRCRVCGRPKASITWKGPEHNTLNNDDHySISYSDigeATLKIIGVSTEDDGIYTCIAVNDMGSASSSASLRV 2748
Cdd:cd05764     15 GQRATLRCKARGDPEPAIHWISPEGKLISNSSR-TLVYDN---GTLDILITTVKDTGAFTCIASNPAGEATARVELHI 88
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
2773-3012 1.36e-08

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 58.93  E-value: 1.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRaVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVlVLEMADQGRLLDC 2852
Cdd:cd05069     19 KLGQGCFGEVWMGTWNGTTK-VAIKTLKPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPIYI-VTEFMGKGSLLDF 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2853 vvrwgsLTEGKVRaHL---------GEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQL-NTTYYIH 2922
Cdd:cd05069     97 ------LKEGDGK-YLklpqlvdmaAQIADGMAYIERMNYIHRDLRAANILVGDNL---VCKIADFGLARLIeDNEYTAR 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2923 QLLGNP-EFAAPEIILGNPVSLTADTWSVGVL-TYVLLSGVSPFlDDSVEETCLNICRLDFSFPEDyfQGVSQKAKEFVC 3000
Cdd:cd05069    167 QGAKFPiKWTAPEAALYGRFTIKSDVWSFGILlTELVTKGRVPY-PGMVNREVLEQVERGYRMPCP--QGCPESLHELMK 243
                          250
                   ....*....|..
gi 1907111721 3001 FLLQEDPAKRPS 3012
Cdd:cd05069    244 LCWKKDPDERPT 255
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
2858-3018 1.46e-08

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 58.39  E-value: 1.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2858 SLTEgkVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTikLADFGDAvqlNTTYYIHQLLGN----PEFAAP 2933
Cdd:cd14019     99 SLTD--IRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRETGKGV--LVDFGLA---QREEDRPEQRAPragtRGFRAP 171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2934 EIILGNPVSLTA-DTWSVGVLTYVLLSGVSPFLDDSVEETCL-NICRLdFSFPEDYfqgvsqkakEFVCFLLQEDPAKRP 3011
Cdd:cd14019    172 EVLFKCPHQTTAiDIWSAGVILLSILSGRFPFFFSSDDIDALaEIATI-FGSDEAY---------DLLDKLLELDPSKRI 241

                   ....*..
gi 1907111721 3012 SAALALQ 3018
Cdd:cd14019    242 TAEEALK 248
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
2657-2748 1.47e-08

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 54.39  E-value: 1.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2657 PEFVIPLSEVTCETGETVVFRCRVCGRPKASITWKGPEHNTLNNDDHYSISYSDIGEATLKIIGVSTEDDGIYTCIAVND 2736
Cdd:cd05892      1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQDNCGRICLLIQNANKKDAGWYTVSAVNE 80
                           90
                   ....*....|..
gi 1907111721 2737 MGSASSSASLRV 2748
Cdd:cd05892     81 AGVVSCNARLDV 92
PH_unc89 cd13325
unc89 pleckstrin homology (PH) domain; unc89 is a myofibrillar protein. unc89-B the largest ...
1447-1560 1.53e-08

unc89 pleckstrin homology (PH) domain; unc89 is a myofibrillar protein. unc89-B the largest isoform is composed of 53 immunoglobulin (Ig) domains, 2 Fn3 domains, a triplet of SH3, DH and PH domains at its N-terminus, and 2 protein kinase domains (PK1 and PK2) at its C-terminus. unc-89 mutants display disorganization of muscle A-bands, and usually lack M-lines. The COOH-terminal region of obscurin, the human homolog of unc89, interacts via two specific Ig-like domains with the NH(2)-terminal Z-disk region of titin, a protein that connects the Z line to the M line in the sarcomere and contributes to the contraction of striated muscle. obscurin is also thought to be involved in Ca2+/calmodulin via its IQ domains, as well as G protein-coupled signal transduction in the sarcomere via its RhoGEF/DH domain. The DH-PH region of OBSCN and unc89, the C. elegans homolog, has exchange activity for RhoA and Rho-1 respectively, but not for the small GTPases homologous to Cdc42 or Rac. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270134  Cd Length: 114  Bit Score: 55.05  E-value: 1.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1447 NIESQGELILQESFQVWDPKTlirKGRERHLFLFEMSLVFSKEVKDSSGRSKYLYKSKLFTSELGVTEHvEGDPCKFALW 1526
Cdd:cd13325      2 NIHKLGRLLRHDWFTVTDGEG---KAKERYLFLFKSRILITKVRRISEDRSVFILKDIIRLPEVNVKQH-PDDERTFELQ 77
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1907111721 1527 VGRTPTSDNKIVLKASSIENKQDWIKHIREVIQE 1560
Cdd:cd13325     78 PKLPAFGILPIDFKAHKDEIKDYWLNEIEEYAND 111
CRAL_TRIO pfam00650
CRAL/TRIO domain;
47-172 1.68e-08

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 56.11  E-value: 1.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721   47 GRDKRGGPILTF-PARSNHDRIRQEDLRRLISYLACI---PSEEVCKRGFTVIVDMRGSK--------WDSIKPLLKILQ 114
Cdd:pfam00650    8 GRDKEGRPVLYLrLGRHDPKKSSEEELVRFLVLVLERallLMPEGQVEGLTVIIDLKGLSlsnmdwwsISLLKKIIKILQ 87
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907111721  115 ESFPCCIHIALIIKPD---NFWQKQRTNFGS----SKFEFeTNMVSLEGLTKVVDPSQLTPEFDG 172
Cdd:pfam00650   88 DNYPERLGKILIVNAPwifNTIWKLIKPFLDpktrEKIVF-LKNSNEEELEKYIPPEQLPKEYGG 151
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
2768-3013 2.04e-08

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 58.50  E-value: 2.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQ---------KGTKRAVATKfVNKKLMKRDQVTHE-LGilqnlQHPLLVSLLDTFETPTSY 2837
Cdd:cd14138      7 FHELEKIGSGEFGSVFKCVKrldgciyaiKRSKKPLAGS-VDEQNALREVYAHAvLG-----QHSHVVRYYSAWAEDDHM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2838 VLVLEMADQGRLLDCVV----RWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAV 2913
Cdd:cd14138     81 LIQNEYCNGGSLADAISenyrIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRTSIPNAASEEGDEDEW 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2914 QLNTTYYIHQLLG------NPE-------FAAPEIILGNPVSL-TADTWSVGvLTYVLLSGVSPFLDDSVEETCLNICRL 2979
Cdd:cd14138    161 ASNKVIFKIGDLGhvtrvsSPQveegdsrFLANEVLQENYTHLpKADIFALA-LTVVCAAGAEPLPTNGDQWHEIRQGKL 239
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1907111721 2980 DfSFPedyfQGVSQKAKEFVCFLLQEDPAKRPSA 3013
Cdd:cd14138    240 P-RIP----QVLSQEFLDLLKVMIHPDPERRPSA 268
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
2656-2748 2.12e-08

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 53.73  E-value: 2.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2656 PPeFVIPLSEVTCETGETVVFRCRVCGRPKASITW-KG----PehntlnnDDHYSISYSDigeATLKIIGVST-EDDGIY 2729
Cdd:cd20958      1 PP-FIRPMGNLTAVAGQTLRLHCPVAGYPISSITWeKDgrrlP-------LNHRQRVFPN---GTLVIENVQRsSDEGEY 69
                           90       100
                   ....*....|....*....|
gi 1907111721 2730 TCIAVNDMG-SASSSASLRV 2748
Cdd:cd20958     70 TCTARNQQGqSASRSVFVKV 89
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
2661-2746 2.23e-08

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 53.74  E-value: 2.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2661 IPLSEVTCETGETVVFRCRV-CGRPKASITWKGpEHNTLNNDDHYSISYSDIGEATLKIIGVSTEDDGIYTCIAVNDMGS 2739
Cdd:pfam00047    1 SAPPTVTVLEGDSATLTCSAsTGSPGPDVTWSK-EGGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGS 79

                   ....*..
gi 1907111721 2740 ASSSASL 2746
Cdd:pfam00047   80 ATLSTSL 86
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
2656-2748 2.50e-08

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 53.74  E-value: 2.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2656 PPEFVIPLSEVTCETGETVVFRCRVCGRPKASITW--KGPE-HNTLNnddhysISYSDIGEATLKIIGVSTEDD-GIYTC 2731
Cdd:cd20972      1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWfcEGKElQNSPD------IQIHQEGDLHSLIIAEAFEEDtGRYSC 74
                           90
                   ....*....|....*..
gi 1907111721 2732 IAVNDMGSASSSASLRV 2748
Cdd:cd20972     75 LATNSVGSDTTSAEIFV 91
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
2768-2964 2.58e-08

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 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: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 58.48  E-value: 2.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKC-DQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQHP------LLVSLLDTFETPTSYVLV 2840
Cdd:cd14214     15 YEIVGDLGEGTFGKVVEClDHARGKSQVALKIIRNVGKYREAARLEINVLKKIKEKdkenkfLCVLMSDWFNFHGHMCIA 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2841 LEMADQGR---LLDCVVRWGSLTEgkVRAHLGEVLEAVRYLHNCRIAHLDLKPENILV----------------DQSLAK 2901
Cdd:cd14214     95 FELLGKNTfefLKENNFQPYPLPH--IRHMAYQLCHALKFLHENQLTHTDLKPENILFvnsefdtlynesksceEKSVKN 172
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907111721 2902 PTIKLADFGDAV---QLNTTyyihqLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPF 2964
Cdd:cd14214    173 TSIRVADFGSATfdhEHHTT-----IVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLF 233
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
2770-3014 3.27e-08

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1b subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 57.63  E-value: 3.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2770 EVAELGRGRFAVVKKCDQ---------KGTKRAVAtKFVNKKLMKRDQVTHE-LGilqnlQHPLLVSLLDTFETPTSYVL 2839
Cdd:cd14139      4 ELEKIGVGEFGSVYKCIKrldgcvyaiKRSMRPFA-GSSNEQLALHEVYAHAvLG-----HHPHVVRYYSAWAEDDHMII 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2840 VLEMADQGRLLDCVVRWGSL----TEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILV------------------DQ 2897
Cdd:cd14139     78 QNEYCNGGSLQDAISENTKSgnhfEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFIchkmqsssgvgeevsneeDE 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2898 SLAKPTI-KLADFGDAVQLNTTYYIHqllGNPEFAAPEIILGNPVSL-TADTWSVGvLTYVLLSGVSPFLDDSVEETCLN 2975
Cdd:cd14139    158 FLSANVVyKIGDLGHVTSINKPQVEE---GDSRFLANEILQEDYRHLpKADIFALG-LTVALAAGAEPLPTNGAAWHHIR 233
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1907111721 2976 icrlDFSFPeDYFQGVSQKAKEFVCFLLQEDPAKRPSAA 3014
Cdd:cd14139    234 ----KGNFP-DVPQELPESFSSLLKNMIQPDPEQRPSAT 267
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
2791-3015 3.48e-08

Pseudokinase domain 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: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 57.40  E-value: 3.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2791 KRAVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLD-CVVRWGSLTEGKVRAHLG 2869
Cdd:cd13992     25 GRTVAIKHITFSRTEKRTILQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDvLLNREIKMDWMFKSSFIK 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2870 EVLEAVRYLHNCRI-AHLDLKPENILVDQSLakpTIKLADFG-------DAVQLNTTYYIH-QLLgnpeFAAPEIILGNP 2940
Cdd:cd13992    105 DIVKGMNYLHSSSIgYHGRLKSSNCLVDSRW---VVKLTDFGlrnlleeQTNHQLDEDAQHkKLL----WTAPELLRGSL 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2941 V----SLTADTWSVGVLTYVLLSGVSPFLDDSVE---------ETCLNICRLDFS---FPEDYFQGVSQkakefvCFLlq 3004
Cdd:cd13992    178 LevrgTQKGDVYSFAIILYEILFRSDPFALEREVaivekvisgGNKPFRPELAVLldeFPPRLVLLVKQ------CWA-- 249
                          250
                   ....*....|.
gi 1907111721 3005 EDPAKRPSAAL 3015
Cdd:cd13992    250 ENPEKRPSFKQ 260
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
2667-2748 3.82e-08

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 52.92  E-value: 3.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2667 TCETGETVVFRCRVCGRPKASITW-KGPEHntLNNDDHYSIsysdIGEATLKIIGVSTEDDGIYTCIAVNDMGSASSSAS 2745
Cdd:cd20957     12 TVDFGRTAVFNCSVTGNPIHTVLWmKDGKP--LGHSSRVQI----LSEDVLVIPSVKREDKGMYQCFVRNDGDSAQATAE 85

                   ...
gi 1907111721 2746 LRV 2748
Cdd:cd20957     86 LKL 88
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
2771-3012 4.08e-08

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 57.39  E-value: 4.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2771 VAELGRGRFAVVKKCDQKGTKRaVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVlVLEMADQGRLL 2850
Cdd:cd05070     14 IKRLGNGQFGEVWMGTWNGNTK-VAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYI-VTEYMSKGSLL 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2851 DCvvrwgsLTEGKVRA--------HLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQL-NTTYYI 2921
Cdd:cd05070     92 DF------LKDGEGRAlklpnlvdMAAQVAAGMAYIERMNYIHRDLRSANILVGNGL---ICKIADFGLARLIeDNEYTA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2922 HQLLGNP-EFAAPEIILGNPVSLTADTWSVGV-LTYVLLSGVSPFLDDSVEETCLNICR-LDFSFPEDyfqgVSQKAKEF 2998
Cdd:cd05070    163 RQGAKFPiKWTAPEAALYGRFTIKSDVWSFGIlLTELVTKGRVPYPGMNNREVLEQVERgYRMPCPQD----CPISLHEL 238
                          250
                   ....*....|....
gi 1907111721 2999 VCFLLQEDPAKRPS 3012
Cdd:cd05070    239 MIHCWKKDPEERPT 252
PH_Collybistin_ASEF cd01224
Collybistin/APC-stimulated guanine nucleotide exchange factor pleckstrin homology (PH) domain; ...
1437-1561 4.37e-08

Collybistin/APC-stimulated guanine nucleotide exchange factor pleckstrin homology (PH) domain; Collybistin (also called PEM2) is homologous to the Dbl proteins ASEF (also called ARHGEF4/RhoGEF4) and SPATA13 (Spermatogenesis-associated protein 13; also called ASEF2). It activates CDC42 specifically and not any other Rho-family GTPases. Collybistin consists of an SH3 domain, followed by a RhoGEF/DH and PH domain. In Dbl proteins, the DH and PH domains catalyze the exchange of GDP for GTP in Rho GTPases, allowing them to signal to downstream effectors. It induces submembrane clustering of the receptor-associated peripheral membrane protein gephyrin, which is thought to form a scaffold underneath the postsynaptic membrane linking receptors to the cytoskeleton. It also acts as a tumor suppressor that links adenomatous polyposis coli (APC) protein, a negative regulator of the Wnt signaling pathway and promotes the phosphorylation and degradation of beta-catenin, to Cdc42. Autoinhibition of collybistin is accomplished by the binding of its SH3 domain with both the RhoGEF and PH domains to block access of Cdc42 to the GTPase-binding site. Inactivation promotes cancer progression. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269931  Cd Length: 138  Bit Score: 54.57  E-value: 4.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1437 HLSMLEGFDENIES-QGELILQESFQVWDPKTL--IRKGR--ERHLFLFEMSLVFSKevKDSSGRSKYLYKSKLFTSELG 1511
Cdd:cd01224      3 NLEKLAAWQSTVEGwEGEDLSDRSSELIHSGELtkISAGRaqERTFFLFDHQLVYCK--KDLLRRKNYIYKGRIDTDNME 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907111721 1512 V------TEHVEGDPCKFALWVGRtpTSDNK-IVLKASSIENKQDWIKHIREviqER 1561
Cdd:cd01224     81 IedlpdgKDDESGVTVKNAWKIYN--ASKNKwYVLCAKSAEEKQRWLEAFAE---ER 132
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
2774-2964 4.44e-08

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl 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: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 57.05  E-value: 4.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLD--TFETPtsYVLVLEMADQGRLLD 2851
Cdd:cd05052     14 LGGGQYGEVYEGVWKKYNLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGvcTREPP--FYIITEFMPYGNLLD 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2852 CVVRWG-SLTEGKVRAHLG-EVLEAVRYLHNCRIAHLDLKPENILV-DQSLakptIKLADFGDA-VQLNTTYYIHQLLGN 2927
Cdd:cd05052     92 YLRECNrEELNAVVLLYMAtQIASAMEYLEKKNFIHRDLAARNCLVgENHL----VKVADFGLSrLMTGDTYTAHAGAKF 167
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1907111721 2928 P-EFAAPEIILGNPVSLTADTWSVGVLTYVLLS-GVSPF 2964
Cdd:cd05052    168 PiKWTAPESLAYNKFSIKSDVWAFGVLLWEIATyGMSPY 206
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
2656-2748 4.48e-08

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 52.95  E-value: 4.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2656 PPEFVIPLSEVTCETGETVVFRCRVCGRPKASITWKgPEHNTLNNDDHYSIS-Y-SDIGEAT--LKIIGVSTEDDGIYTC 2731
Cdd:cd20956      1 APVLLETFSEQTLQPGPSVSLKCVASGNPLPQITWT-LDGFPIPESPRFRVGdYvTSDGDVVsyVNISSVRVEDGGEYTC 79
                           90
                   ....*....|....*..
gi 1907111721 2732 IAVNDMGSASSSASLRV 2748
Cdd:cd20956     80 TATNDVGSVSHSARINV 96
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
876-967 7.42e-08

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 52.71  E-value: 7.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  876 QLRHLQAEVKQVLGWIRNGESMLNAGLItASSLQEAEQLQREHEQFQHAIEkTHQSALQ-VQQKAEAMLQANHYDMDMIR 954
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEALLSSEDY-GKDLESVQALLKKHKALEAELA-AHQDRVEaLNELAEKLIDEGHYASEEIQ 79
                           90
                   ....*....|...
gi 1907111721  955 DCAEKVASHWQQL 967
Cdd:pfam00435   80 ERLEELNERWEQL 92
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
2767-3021 7.45e-08

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. 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 CDK8-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: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 56.91  E-value: 7.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2767 FYSEVAELGRGRFAVVKKCDQKGTKRavaTKFVNKKLMKRDQVTH---------ELGILQNLQHPLLVSLLDTFETPT-- 2835
Cdd:cd07842      1 KYEIEGCIGRGTYGRVYKAKRKNGKD---GKEYAIKKFKGDKEQYtgisqsacrEIALLRELKHENVVSLVEVFLEHAdk 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2836 SYVLVLEMADQGrlLDCVVRW------GSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILV-DQSLAKPTIKLAD 2908
Cdd:cd07842     78 SVYLLFDYAEHD--LWQIIKFhrqakrVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVmGEGPERGVVKIGD 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2909 FGDAVQLNTTyyIHQLL-GNPE-----FAAPEIILGNPVSLTA-DTWSVGVLTYVLLSGV-------------SPFLDDS 2968
Cdd:cd07842    156 LGLARLFNAP--LKPLAdLDPVvvtiwYRAPELLLGARHYTKAiDIWAIGCIFAELLTLEpifkgreakikksNPFQRDQ 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2969 VEEtclnICRL------------------------------DFSFPEDYFQGVS-QKAKEFVCF--LLQEDPAKRPSAAL 3015
Cdd:cd07842    234 LER----IFEVlgtptekdwpdikkmpeydtlksdtkastyPNSLLAKWMHKHKkPDSQGFDLLrkLLEYDPTKRITAEE 309

                   ....*.
gi 1907111721 3016 ALQEQW 3021
Cdd:cd07842    310 ALEHPY 315
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
2657-2748 8.33e-08

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 52.55  E-value: 8.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2657 PEFVIPLSEVTCETGETVVFRCRVCGRPKASITWKGPEH---NTLNNDDHY--SISYSDIGEatLKIIGVSTEDDGIYTC 2731
Cdd:cd05765      1 PALVNSPTHQTVKVGETASFHCDVTGRPQPEITWEKQVPgkeNLIMRPNHVrgNVVVTNIGQ--LVIYNAQPQDAGLYTC 78
                           90
                   ....*....|....*..
gi 1907111721 2732 IAVNDMGSASSSASLRV 2748
Cdd:cd05765     79 TARNSGGLLRANFPLSV 95
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
2926-3022 8.50e-08

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 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: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 55.82  E-value: 8.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2926 GNPEFAAPEII--LGNPVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPEDyfqgVSQKAKEFVCFLL 3003
Cdd:cd14023    148 GCPAYVSPEILntTGTYSGKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPDH----VSPKARCLIRSLL 223
                           90
                   ....*....|....*....
gi 1907111721 3004 QEDPAKRPSAALALQEQWL 3022
Cdd:cd14023    224 RREPSERLTAPEILLHPWF 242
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
2877-2964 8.75e-08

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: 56.25  E-value: 8.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2877 YLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAV---QLNTTYYIHQLLGNPEFAAPEIIL---GNPVSLTADTWSV 2950
Cdd:cd14062    104 YLHAKNIIHRDLKSNNIFLHEDL---TVKIGDFGLATvktRWSGSQQFEQPTGSILWMAPEVIRmqdENPYSFQSDVYAF 180
                           90
                   ....*....|....
gi 1907111721 2951 GVLTYVLLSGVSPF 2964
Cdd:cd14062    181 GIVLYELLTGQLPY 194
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
2849-3013 8.98e-08

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: 56.56  E-value: 8.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2849 LLDCVVRWGsltegkvrahLGEVLEAVRYLHN-CRIAHLDLKPENILVDQSLAkptIKLADFGDAVQL----NTTYYIHQ 2923
Cdd:cd14011    111 LYDVEIKYG----------LLQISEALSFLHNdVKLVHGNICPESVVINSNGE---WKLAGFDFCISSeqatDQFPYFRE 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2924 --------LLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFLD--DSVEETCLNICRLDFsFPEDYFQGVSQ 2993
Cdd:cd14011    178 ydpnlpplAQPNLNYLAPEYILSKTCDPASDMFSLGVLIYAIYNKGKPLFDcvNNLLSYKKNSNQLRQ-LSLSLLEKVPE 256
                          170       180
                   ....*....|....*....|
gi 1907111721 2994 KAKEFVCFLLQEDPAKRPSA 3013
Cdd:cd14011    257 ELRDHVKTLLNVTPEVRPDA 276
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
2768-3022 9.02e-08

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. 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 CDK12 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: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 56.73  E-value: 9.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATKFV---NKKLMKRDQVTHELGILQNLQHPLLVSL----------LDTFETP 2834
Cdd:cd07864      9 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVrldNEKEGFPITAIREIKILRQLNHRSVVNLkeivtdkqdaLDFKKDK 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2835 TSYVLVLEMADQ---GRLLDCVVrwgSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGD 2911
Cdd:cd07864     89 GAFYLVFEYMDHdlmGLLESGLV---HFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNN---KGQIKLADFGL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2912 AVQLNT------TYYIHQLLGNPefaaPEIILGNPVSLTA-DTWSVGVLTYVLLSGvSPFLDDSVE----ETCLNIC--- 2977
Cdd:cd07864    163 ARLYNSeesrpyTNKVITLWYRP----PELLLGEERYGPAiDVWSCGCILGELFTK-KPIFQANQElaqlELISRLCgsp 237
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907111721 2978 ---------------------------RLDFSFpedyfqgVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd07864    238 cpavwpdviklpyfntmkpkkqyrrrlREEFSF-------IPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
2870-3022 9.22e-08

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


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 55.81  E-value: 9.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2870 EVLEAVRYLHNCRIAHLDLKPENiLVDQSLAKPTIKLADFGDAVQLN-TTYYIHQLLGNPEFAAPEII--LGNPVSLTAD 2946
Cdd:cd14022     92 QIASAVAHCHDGGLVLRDLKLRK-FVFKDEERTRVKLESLEDAYILRgHDDSLSDKHGCPAYVSPEILntSGSYSGKAAD 170
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907111721 2947 TWSVGVLTYVLLSGVSPFLDdsVEETCL--NICRLDFSFPEdyfqGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd14022    171 VWSLGVMLYTMLVGRYPFHD--IEPSSLfsKIRRGQFNIPE----TLSPKAKCLIRSILRREPSERLTSQEILDHPWF 242
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
2656-2748 1.06e-07

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 51.87  E-value: 1.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2656 PPEFVIPLSEVTCETGETVVFRCRVCGRPKASITWKGPEHNTLNNDDHYSIsysDIGEATLKIIGVSTEDDGIYTCIAVN 2735
Cdd:cd20976      1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRSTC---EAGVGELHIQDVLPEDHGTYTCLAKN 77
                           90
                   ....*....|...
gi 1907111721 2736 DMGSASSSASLRV 2748
Cdd:cd20976     78 AAGQVSCSAWVTV 90
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
2773-2959 1.06e-07

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family 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: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 56.18  E-value: 1.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCD----QKGTKRAVATKFVNKKLMK--RDqVTHELGILQNLQHPLLVSLLDTFETP--TSYVLVLEMA 2844
Cdd:cd14205     11 QLGKGNFGSVEMCRydplQDNTGEVVAVKKLQHSTEEhlRD-FEREIEILKSLQHDNIVKYKGVCYSAgrRNLRLIMEYL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2845 DQGRLLDCVVRWGS-LTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFG--DAVQLNTTYYI 2921
Cdd:cd14205     90 PYGSLRDYLQKHKErIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENEN---RVKIGDFGltKVLPQDKEYYK 166
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1907111721 2922 HQLLG-NPEF-AAPEIILGNPVSLTADTWSVGVLTYVLLS 2959
Cdd:cd14205    167 VKEPGeSPIFwYAPESLTESKFSVASDVWSFGVVLYELFT 206
PH pfam00169
PH domain; PH stands for pleckstrin homology.
1473-1558 1.07e-07

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 52.56  E-value: 1.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1473 RERHLFLFEMSLVFSKevkDSSGRSKYLYKSKLFTSELGVTEHVEGD----PCKFALWVGrTPTSDNKIVLKASSIENKQ 1548
Cdd:pfam00169   19 KKRYFVLFDGSLLYYK---DDKSGKSKEPKGSISLSGCEVVEVVASDspkrKFCFELRTG-ERTGKRTYLLQAESEEERK 94
                           90
                   ....*....|
gi 1907111721 1549 DWIKHIREVI 1558
Cdd:pfam00169   95 DWIKAIQSAI 104
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
2774-2964 1.12e-07

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: 56.22  E-value: 1.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTkraVATKFVNKKLMKRDQVT---HELGILQNLQHpLLVSLLDTFETPTSYVLVLEMADQGRLl 2850
Cdd:cd14151     16 IGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQafkNEVGVLRKTRH-VNILLFMGYSTKPQLAIVTQWCEGSSL- 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2851 dcvvrWGSLTEGKVRAHLGEVLEAVR-------YLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAV---QLNTTYY 2920
Cdd:cd14151     91 -----YHHLHIIETKFEMIKLIDIARqtaqgmdYLHAKSIIHRDLKSNNIFLHEDL---TVKIGDFGLATvksRWSGSHQ 162
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1907111721 2921 IHQLLGNPEFAAPEIIL---GNPVSLTADTWSVGVLTYVLLSGVSPF 2964
Cdd:cd14151    163 FEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPY 209
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
2774-2953 1.20e-07

Catalytic domain of an unknown subfamily of 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. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). 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: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 55.60  E-value: 1.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKfVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLDCV 2853
Cdd:cd14156      1 IGSGFFSKVYKVTHGATGKVMVVK-IYKNDVDQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEELL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2854 VRWGSLTEGKVRAHLG-EVLEAVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFGDAVQL-----NTTYYIHQLLGN 2927
Cdd:cd14156     80 AREELPLSWREKVELAcDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGREAVVTDFGLAREVgempaNDPERKLSLVGS 159
                          170       180
                   ....*....|....*....|....*.
gi 1907111721 2928 PEFAAPEIILGNPVSLTADTWSVGVL 2953
Cdd:cd14156    160 AFWMAPEMLRGEPYDRKVDVFSFGIV 185
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
2773-2953 1.29e-07

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 55.85  E-value: 1.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRaVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLLDTFETPTSYVlVLEMADQGRLLDc 2852
Cdd:cd05071     16 KLGQGCFGEVWMGTWNGTTR-VAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYI-VTEYMSKGSLLD- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2853 vvrwgsLTEGKVRAHL---------GEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQL-NTTYYIH 2922
Cdd:cd05071     93 ------FLKGEMGKYLrlpqlvdmaAQIASGMAYVERMNYVHRDLRAANILVGENL---VCKVADFGLARLIeDNEYTAR 163
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1907111721 2923 QLLGNP-EFAAPEIILGNPVSLTADTWSVGVL 2953
Cdd:cd05071    164 QGAKFPiKWTAPEAALYGRFTIKSDVWSFGIL 195
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
2820-3022 1.32e-07

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


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 55.51  E-value: 1.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2820 QHPLLVSLLDTFeTPTSYVLVLEMADQGRLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPEN-ILVDQs 2898
Cdd:cd13976     43 SHPNISGVHEVI-AGETKAYVFFERDHGDLHSYVRSRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKfVFADE- 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2899 lAKPTIKLADFGDAVQLN-TTYYIHQLLGNPEFAAPEIIL------GNPvsltADTWSVGVLTYVLLSGVSPFLDDSVEE 2971
Cdd:cd13976    121 -ERTKLRLESLEDAVILEgEDDSLSDKHGCPAYVSPEILNsgatysGKA----ADVWSLGVILYTMLVGRYPFHDSEPAS 195
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907111721 2972 TCLNICRLDFSFPEdyfqGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWL 3022
Cdd:cd13976    196 LFAKIRRGQFAIPE----TLSPRARCLIRSLLRREPSERLTAEDILLHPWL 242
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
2767-2959 1.36e-07

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 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: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 56.09  E-value: 1.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2767 FYSEVAELGRGRFAVVKKC------DQKGTKRAVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSL--LDTFETPTSYV 2838
Cdd:cd05079      5 FLKRIRDLGEGHFGKVELCrydpegDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYkgICTEDGGNGIK 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2839 LVLEMADQGRLLDCVVRWGSLTEGKVRAHLG-EVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFG--DAVQL 2915
Cdd:cd05079     85 LIMEFLPSGSLKEYLPRNKNKINLKQQLKYAvQICKGMDYLGSRQYVHRDLAARNVLVE---SEHQVKIGDFGltKAIET 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1907111721 2916 NTTYY-IHQLLGNPEF-AAPEIILGNPVSLTADTWSVGVLTYVLLS 2959
Cdd:cd05079    162 DKEYYtVKDDLDSPVFwYAPECLIQSKFYIASDVWSFGVTLYELLT 207
SPEC smart00150
Spectrin repeats;
189-305 1.46e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.95  E-value: 1.46e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721   189 EEYISNAAHMLSRLEELQDVLAKKELPQDLEGARNMIDEHSQLKKKV--IKAPIEDLDLEGQKLLQriqssdsfpkknSG 266
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELeaHEERVEALNELGEQLIE------------EG 68
                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 1907111721   267 SGNAdlqnllPKVSTMLDRLHSTRQHLHQMWHVRKLKLD 305
Cdd:smart00150   69 HPDA------EEIEERLEELNERWEELKELAEERRQKLE 101
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
2774-2959 1.51e-07

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 55.49  E-value: 1.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKrAVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSL--LDTFETPTsYVlVLEMADQGRLLD 2851
Cdd:cd05068     16 LGSGQFGEVWEGLWNNTT-PVAVKTLKPGTMDPEDFLREAQIMKKLRHPKLIQLyaVCTLEEPI-YI-ITELMKHGSLLE 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2852 CVvrwgsltEGKVRA-HL-------GEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDA--VQLNTTYYI 2921
Cdd:cd05068     93 YL-------QGKGRSlQLpqlidmaAQVASGMAYLESQNYIHRDLAARNVLVGENN---ICKVADFGLArvIKVEDEYEA 162
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1907111721 2922 HQLLGNP-EFAAPEIILGNPVSLTADTWSVGVLTYVLLS 2959
Cdd:cd05068    163 REGAKFPiKWTAPEAANYNRFSIKSDVWSFGILLTEIVT 201
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
1451-1559 1.58e-07

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 51.78  E-value: 1.58e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  1451 QGELILQEsfqvwdpKTLIRKGRERHLFLFEMSLVFSKevkDSSGRSKYLYKSKLFTSELGVTEHVEGD----PCKFALW 1526
Cdd:smart00233    4 EGWLYKKS-------GGGKKSWKKRYFVLFNSTLLYYK---SKKDKKSYKPKGSIDLSGCTVREAPDPDsskkPHCFEIK 73
                            90       100       110
                    ....*....|....*....|....*....|...
gi 1907111721  1527 VGRTPTsdnkIVLKASSIENKQDWIKHIREVIQ 1559
Cdd:smart00233   74 TSDRKT----LLLQAESEEEREKWVEALRKAIA 102
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
2665-2748 1.65e-07

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 51.62  E-value: 1.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2665 EVTCETGETVVFRCRVCGRPKASITWKGPEHNTLN---NDDHYSISysdigEATLKIIGVSTEDDGIYTCIAVNDMGSAS 2741
Cdd:cd20969     11 QVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSaksNGRLTVFP-----DGTLEVRYAQVQDNGTYLCIAANAGGNDS 85

                   ....*..
gi 1907111721 2742 SSASLRV 2748
Cdd:cd20969     86 MPAHLHV 92
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
1630-1680 1.79e-07

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.


Pssm-ID: 212690 [Multi-domain]  Cd Length: 51  Bit Score: 49.77  E-value: 1.79e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907111721 1630 VVIHDFTACNSNELTIRRGQTVEVLERPHDkpDWCLVRTTDRSpaaEGLVP 1680
Cdd:cd00174      3 RALYDYEAQDDDELSFKKGDIITVLEKDDD--GWWEGELNGGR---EGLFP 48
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
2873-2964 2.14e-07

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: 55.02  E-value: 2.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2873 EAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAV---QLNTTYYIHQLLGNPEFAAPEIIL---GNPVSLTAD 2946
Cdd:cd14150    107 QGMDYLHAKNIIHRDLKSNNIFLHEGL---TVKIGDFGLATvktRWSGSQQVEQPSGSILWMAPEVIRmqdTNPYSFQSD 183
                           90
                   ....*....|....*...
gi 1907111721 2947 TWSVGVLTYVLLSGVSPF 2964
Cdd:cd14150    184 VYAYGVVLYELMSGTLPY 201
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
1937-2103 2.18e-07

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 57.21  E-value: 2.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1937 RRHYVLQELVETERDYVRDLGCVVEGYMALMKE-DGVPDDMKGK-DKIVFGNIHQIYDWHRDFfLGELEK--CLED-PEK 2011
Cdd:COG5422    484 KRQEAIYEVIYTERDFVKDLEYLRDTWIKPLEEsNIIPENARRNfIKHVFANINEIYAVNSKL-LKALTNrqCLSPiVNG 562
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2012 LGSLFVKHERRLHMYIVYCQNKP------KSEHIVSEYIDTFFED-LKQRLGHRLQLTDLLIKPVQRIMKYQLLLKDFLK 2084
Cdd:COG5422    563 IADIFLDYVPKFEPFIKYGASQPyakyefEREKSVNPNFARFDHEvERLDESRKLELDGYLTKPTTRLARYPLLLEEVLK 642
                          170
                   ....*....|....*....
gi 1907111721 2085 YSKKASLDTSELEKAVEVM 2103
Cdd:COG5422    643 FTDPDNPDTEDIPKVIDML 661
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
2662-2748 2.30e-07

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 50.87  E-value: 2.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2662 PLSEVTCETGETVVFRCRVCGRPKASITWKgPEHNTLNNDdhySISYSDIGEaTLKIIGVSTEDDGIYTCIAVNDMGSAS 2741
Cdd:cd05731      1 SESSTMVLRGGVLLLECIAEGLPTPDIRWI-KLGGELPKG---RTKFENFNK-TLKIENVSEADSGEYQCTASNTMGSAR 75

                   ....*..
gi 1907111721 2742 SSASLRV 2748
Cdd:cd05731     76 HTISVTV 82
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
1630-1681 2.56e-07

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 49.46  E-value: 2.56e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1907111721  1630 VVIHDFTACNSNELTIRRGQTVEVLERPHDkpDWCLVRTTDRspaAEGLVPC 1681
Cdd:smart00326    6 RALYDYTAQDPDELSFKKGDIITVLEKSDD--GWWKGRLGRG---KEGLFPS 52
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
2811-2965 2.80e-07

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 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: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 54.97  E-value: 2.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2811 HELGILQNLQHPLLVSLLDTFETPTSYVLvlEMADQGRLldcvvrwGSLTEGKVRAH----LGEVL---------EAVRY 2877
Cdd:cd14067     59 QEASMLHSLQHPCIVYLIGISIHPLCFAL--ELAPLGSL-------NTVLEENHKGSsfmpLGHMLtfkiayqiaAGLAY 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2878 LHNCRIAHLDLKPENILVdQSLAKP---TIKLADFGDAVQlnttyYIHQ----LLGNPEFAAPEIILGNPVSLTADTWSV 2950
Cdd:cd14067    130 LHKKNIIFCDLKSDNILV-WSLDVQehiNIKLSDYGISRQ-----SFHEgalgVEGTPGYQAPEIRPRIVYDEKVDMFSY 203
                          170
                   ....*....|....*
gi 1907111721 2951 GVLTYVLLSGVSPFL 2965
Cdd:cd14067    204 GMVLYELLSGQRPSL 218
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
2656-2748 2.84e-07

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 50.70  E-value: 2.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2656 PPEFVIPLSEV--TCETGETVVFRCRVCGRPKASITWKGPEHNTLNNDDHYSISYsDIGEATlkIIGVSTEDDGIYTCIA 2733
Cdd:cd05730      1 PPTIRARQSEVnaTANLGQSVTLACDADGFPEPTMTWTKDGEPIESGEEKYSFNE-DGSEMT--ILDVDKLDEAEYTCIA 77
                           90
                   ....*....|....*
gi 1907111721 2734 VNDMGSASSSASLRV 2748
Cdd:cd05730     78 ENKAGEQEAEIHLKV 92
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
1469-1554 2.91e-07

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 50.62  E-value: 2.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1469 IRKGRERHLFLFEMSLVFSKEVKDSSGRSKYLYKsklFTSELGVTEHVEGD-PCKFALWVgrtpTSDNKIVLKASSIENK 1547
Cdd:cd00821     13 LKSWKKRWFVLFEGVLLYYKSKKDSSYKPKGSIP---LSGILEVEEVSPKErPHCFELVT----PDGRTYYLQADSEEER 85

                   ....*..
gi 1907111721 1548 QDWIKHI 1554
Cdd:cd00821     86 QEWLKAL 92
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
2773-2964 3.18e-07

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 54.65  E-value: 3.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCD-QKGTKraVATKFVNKKLMKRDQVTHELGILQNLQHPLLVSLlDTFETPTSYVLVLEMADQGRLLD 2851
Cdd:cd05073     18 KLGAGQFGEVWMATyNKHTK--VAVKTMKPGSMSVEAFLAEANVMKTLQHDKLVKL-HAVVTKEPIYIITEFMAKGSLLD 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2852 CVvrwgSLTEG------KVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAVQLNTTYYIHQLL 2925
Cdd:cd05073     95 FL----KSDEGskqplpKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASL---VCKIADFGLARVIEDNEYTAREG 167
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907111721 2926 GN-P-EFAAPEIILGNPVSLTADTWSVGV-LTYVLLSGVSPF 2964
Cdd:cd05073    168 AKfPiKWTAPEAINFGSFTIKSDVWSFGIlLMEIVTYGRIPY 209
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
2773-3012 3.82e-07

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror 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: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 54.69  E-value: 3.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCD-----QKGTKRAVATKFVNKK-LMK-RDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMAD 2845
Cdd:cd05048     12 ELGEGAFGKVYKGEllgpsSEESAISVAIKTLKENaSPKtQQDFRREAELMSDLQHPNIVCLLGVCTKEQPQCMLFEYMA 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2846 QGRLLDCVVRWGSLTEGKVRAHLGEVLEAVR----------------YLHNCRIAHLDLKPENILVDQSLakpTIKLADF 2909
Cdd:cd05048     92 HGDLHEFLVRHSPHSDVGVSSDDDGTASSLDqsdflhiaiqiaagmeYLSSHHYVHRDLAARNCLVGDGL---TVKISDF 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2910 GDAVQL-NTTYY--IHQLLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLS-GVSPFLDDSVEETCLNI-CRLDFSFP 2984
Cdd:cd05048    169 GLSRDIySSDYYrvQSKSLLPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSyGLQPYYGYSNQEVIEMIrSRQLLPCP 248
                          250       260
                   ....*....|....*....|....*...
gi 1907111721 2985 EDYFQGVSQKAKEfvCFllQEDPAKRPS 3012
Cdd:cd05048    249 EDCPARVYSLMVE--CW--HEIPSRRPR 272
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
2657-2749 3.90e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 50.43  E-value: 3.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2657 PEFVIPLSEVTCETGETVVFRCRVCGRPKASITW-KGPEHNTLNNDDHYSISYSDiGEATLKIIGVSTEDDGIYTCIAVN 2735
Cdd:cd20974      1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWfRDGQVISTSTLPGVQISFSD-GRAKLSIPAVTKANSGRYSLTATN 79
                           90
                   ....*....|....
gi 1907111721 2736 DMGSASSSASLRVL 2749
Cdd:cd20974     80 GSGQATSTAELLVL 93
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
2774-2964 4.35e-07

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 53.99  E-value: 4.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTKRAVATKFVNKKLMK--RDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLLD 2851
Cdd:cd05041      3 IGRGNFGDVYRGVLKPDNTEVAVKTCRETLPPdlKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGSLLT 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2852 CVVRWGSltEGKVRAHLGEVLEA---VRYLH--NCriAHLDLKPENILVDQslaKPTIKLADFGDAVQLNTTYYIHQ--L 2924
Cdd:cd05041     83 FLRKKGA--RLTVKQLLQMCLDAaagMEYLEskNC--IHRDLAARNCLVGE---NNVLKISDFGMSREEEDGEYTVSdgL 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907111721 2925 LGNP-EFAAPEIILGNPVSLTADTWSVGVLTYVLLS-GVSPF 2964
Cdd:cd05041    156 KQIPiKWTAPEALNYGRYTSESDVWSFGILLWEIFSlGATPY 197
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
2874-3013 4.77e-07

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L 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: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 54.48  E-value: 4.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2874 AVRYLHNCRIAHLDLKPENILVDQSLAKPTIKLADFG-------------DAVQLNtTYYIHQLLGNPEFAAPEIILGNp 2940
Cdd:cd13977    146 ALAFLHRNQIVHRDLKPDNILISHKRGEPILKVADFGlskvcsgsglnpeEPANVN-KHFLSSACGSDFYMAPEVWEGH- 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2941 VSLTADTWSVGVLTYVLLSGVSpFLDDSVEETCLN--ICR----------------LDFSFPEDYFQGVSQKAKEFVCFL 3002
Cdd:cd13977    224 YTAKADIFALGIIIWAMVERIT-FRDGETKKELLGtyIQQgkeivplgeallenpkLELQIPLKKKKSMNDDMKQLLRDM 302
                          170
                   ....*....|.
gi 1907111721 3003 LQEDPAKRPSA 3013
Cdd:cd13977    303 LAANPQERPDA 313
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
2768-2964 4.78e-07

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 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: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 54.64  E-value: 4.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKC-DQKGTKRAVATKFVNKKLMKRDQVTHELGILQ--NLQHP----LLVSLLDTFETPTSYVLV 2840
Cdd:cd14215     14 YEIVSTLGEGTFGRVVQCiDHRRGGARVALKIIKNVEKYKEAARLEINVLEkiNEKDPenknLCVQMFDWFDYHGHMCIS 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2841 LEMADqgrlldcVVRWGSLTEG--------KVRAHLGEVLEAVRYLHNCRIAHLDLKPENILV---------------DQ 2897
Cdd:cd14215     94 FELLG-------LSTFDFLKENnylpypihQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFvnsdyeltynlekkrDE 166
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2898 SLAKPT-IKLADFGDAvqlnTTYYIHQ--LLGNPEFAAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPF 2964
Cdd:cd14215    167 RSVKSTaIRVVDFGSA----TFDHEHHstIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLF 232
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
2773-3019 5.01e-07

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes 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: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 53.78  E-value: 5.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMK--RDQVTHELGILQNLQHPLLVSLLDTFETPTSYVLVLEMADQGRLL 2850
Cdd:cd05084      3 RIGRGNFGEVFSGRLRADNTPVAVKSCRETLPPdlKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDFL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2851 DCVVRWGSLTEGKVRAHLGE-VLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFGDAVQLNTTYY-----IHQL 2924
Cdd:cd05084     83 TFLRTEGPRLKVKELIRMVEnAAAGMEYLESKHCIHRDLAARNCLVTE---KNVLKISDFGMSREEEDGVYaatggMKQI 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2925 lgnP-EFAAPEIILGNPVSLTADTWSVGVLTYVLLS-GVSPFLDDSVEET-----------CLNICrldfsfPEDYFQGV 2991
Cdd:cd05084    160 ---PvKWTAPEALNYGRYSSESDVWSFGILLWETFSlGAVPYANLSNQQTreaveqgvrlpCPENC------PDEVYRLM 230
                          250       260
                   ....*....|....*....|....*...
gi 1907111721 2992 SQkakefvCFllQEDPAKRPSAALALQE 3019
Cdd:cd05084    231 EQ------CW--EYDPRKRPSFSTVHQD 250
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
2773-2960 5.21e-07

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: 54.03  E-value: 5.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2773 ELGRGRFAVVKKCDQKGTKRAVATKFVNKKLMKR-DQVTHELGILQNL-QHPLLVSL----LD-TFETPTSYVLVLEMAD 2845
Cdd:cd13975      7 ELGRGQYGVVYACDSWGGHFPCALKSVVPPDDKHwNDLALEFHYTRSLpKHERIVSLhgsvIDySYGGGSSIAVLLIMER 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2846 QGRLLDCVVRWG-SLTEgkvRAHLG-EVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFG----DAVQLNTty 2919
Cdd:cd13975     87 LHRDLYTGIKAGlSLEE---RLQIAlDVVEGIRFLHSQGLVHRDIKLKNVLLDK---KNRAKITDLGfckpEAMMSGS-- 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1907111721 2920 yihqLLGNPEFAAPEIILGNPVSlTADTWSVGVLTYVLLSG 2960
Cdd:cd13975    159 ----IVGTPIHMAPELFSGKYDN-SVDVYAFGILFWYLCAG 194
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
2671-2748 5.21e-07

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 49.55  E-value: 5.21e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907111721 2671 GETVVFRCRVCGRPKASITW-KGpeHNTLNNDDHYSIsysdIGEATLKIIGVSTEDDGIYTCIAVNDMGSASSSASLRV 2748
Cdd:cd05745      2 GQTVDFLCEAQGYPQPVIAWtKG--GSQLSVDRRHLV----LSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
2767-2965 6.29e-07

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 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: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 53.75  E-value: 6.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2767 FYSEVAELGRGRFA-VVKKC---DQKGTKRAVATKFVNKK--LMKRDQVTHELGILQNLQHPLLVSLLDTFETP--TSYV 2838
Cdd:cd05080      5 YLKKIRDLGEGHFGkVSLYCydpTNDGTGEMVAVKALKADcgPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQggKSLQ 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2839 LVLEMADQGRLLDCVVRwGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQslaKPTIKLADFG--DAVQLN 2916
Cdd:cd05080     85 LIMEYVPLGSLRDYLPK-HSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDN---DRLVKIGDFGlaKAVPEG 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907111721 2917 TTYY-IHQLLGNPEF-AAPEIILGNPVSLTADTWSVGVLTYVLLSGVSPFL 2965
Cdd:cd05080    161 HEYYrVREDGDSPVFwYAPECLKEYKFYYASDVWSFGVTLYELLTHCDSSQ 211
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1111-1211 6.37e-07

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 50.01  E-value: 6.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1111 FERSAKQALEWIHDNGEFYLSThtSTGSSIQHTQELLKEHEEFQITAKQTKERVKLLIQLADGFCEKGHAHAAEIKKCVT 1190
Cdd:pfam00435    6 FFRDADDLESWIEEKEALLSSE--DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83
                           90       100
                   ....*....|....*....|.
gi 1907111721 1191 AVDKRYRDFSLRMEKYRTSLE 1211
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLE 104
SPEC smart00150
Spectrin repeats;
644-751 7.08e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 50.02  E-value: 7.08e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721   644 FHTHVKELWTWLEELQKELLDDVYAESVEAVQDLIKR---FGQQQQTTLQVTVNVIKEGEDLIQQlrdsaissnktpHNS 720
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKheaFEAELEAHEERVEALNELGEQLIEE------------GHP 70
                            90       100       110
                    ....*....|....*....|....*....|.
gi 1907111721   721 SINHIETVLQQLDEAQSQMEELFQERKIKLE 751
Cdd:smart00150   71 DAEEIEERLEELNERWEELKELAEERRQKLE 101
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
2870-2964 7.66e-07

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: 53.50  E-value: 7.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2870 EVLEAVRYLHNCRIAHLDLKPENILVDQSLakpTIKLADFGDAV---QLNTTYYIHQLLGNPEFAAPEIIL---GNPVSL 2943
Cdd:cd14149    116 QTAQGMDYLHAKNIIHRDMKSNNIFLHEGL---TVKIGDFGLATvksRWSGSQQVEQPTGSILWMAPEVIRmqdNNPFSF 192
                           90       100
                   ....*....|....*....|.
gi 1907111721 2944 TADTWSVGVLTYVLLSGVSPF 2964
Cdd:cd14149    193 QSDVYSYGIVLYELMTGELPY 213
SH3_Eps8 cd11764
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar ...
1628-1681 7.76e-07

Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar proteins; This group is composed of Eps8 and Eps8-like proteins including Eps8-like 1-3, among others. These proteins contain N-terminal Phosphotyrosine-binding (PTB), central SH3, and C-terminal effector domains. Eps8 binds either Abi1 (also called E3b1) or Rab5 GTPase activating protein RN-tre through its SH3 domain. With Abi1 and Sos1, it becomes part of a trimeric complex that is required to activate Rac. Together with RN-tre, it inhibits the internalization of EGFR. The SH3 domains of Eps8 and similar proteins recognize peptides containing a PxxDY motif, instead of the classical PxxP motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212698 [Multi-domain]  Cd Length: 54  Bit Score: 48.41  E-value: 7.76e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907111721 1628 LTVVIHDFTACNSNELTIRRGQTVEVLErphDKPDWCLVRTtdrSPAAEGLVPC 1681
Cdd:cd11764      1 YVRVLYDFTARNSKELSVLKGEYLEVLD---DSRQWWKVRN---SRGQVGYVPH 48
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
2768-2960 7.79e-07

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 53.85  E-value: 7.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2768 YSEVAELGRGRFAVVKKCDQKGTKRAVATK----FVNKKLMKRdqVTHELGILQNLQHPLLVSLLD-----TFETPTSYV 2838
Cdd:cd07849      7 YQNLSYIGEGAYGMVCSAVHKPTGQKVAIKkispFEHQTYCLR--TLREIKILLRFKHENIIGILDiqrppTFESFKDVY 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2839 LVLEMADQGrlLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDqslAKPTIKLADFGDA-VQLNT 2917
Cdd:cd07849     85 IVQELMETD--LYKLIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLN---TNCDLKICDFGLArIADPE 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2918 TYYIHQLLgnpEFA------APEIILGNPVSLTA-DTWSVGVLTYVLLSG 2960
Cdd:cd07849    160 HDHTGFLT---EYVatrwyrAPEIMLNSKGYTKAiDIWSVGCILAEMLSN 206
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
1248-1425 1.03e-06

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 54.90  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1248 HELNEEKRKSARRKEFIMAELIQTEKAYVRDLRECMDTY---LWEMTsgveeIPPGIVNKELI--IFGNMQEIYEFhNNI 1322
Cdd:COG5422    472 KEVWESLPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWikpLEESN-----IIPENARRNFIkhVFANINEIYAV-NSK 545
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 1323 FLKELEK---YEQLPEDVGHCFVTWADKFQMYVTYCKNKPDSTQLIlEHAGS-------YFDEIQ-----QRHGlansIS 1387
Cdd:COG5422    546 LLKALTNrqcLSPIVNGIADIFLDYVPKFEPFIKYGASQPYAKYEF-EREKSvnpnfarFDHEVErldesRKLE----LD 620
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1907111721 1388 SYLIKPVQRITKYQLLLKELLTCCEEGKGEIKDGLEVM 1425
Cdd:COG5422    621 GYLTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVI 658
SH3_p47phox_like cd11856
Src homology 3 domains of the p47phox subunit of NADPH oxidase and similar domains; This ...
1630-1681 1.10e-06

Src homology 3 domains of the p47phox subunit of NADPH oxidase and similar domains; This family is composed of the tandem SH3 domains of p47phox subunit of NADPH oxidase and Nox Organizing protein 1 (NoxO1), the four SH3 domains of Tks4 (Tyr kinase substrate with four SH3 domains), the five SH3 domains of Tks5, the SH3 domain of obscurin, Myosin-I, and similar domains. Most members of this group also contain Phox homology (PX) domains, except for obscurin and Myosin-I. p47phox and NoxO1 are regulators of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) and nonphagocytic NADPH oxidase Nox1, respectively. They play roles in the activation of their respective NADPH oxidase, which catalyzes the transfer of electrons from NADPH to molecular oxygen to form superoxide. Tks proteins are Src substrates and scaffolding proteins that play important roles in the formation of podosomes and invadopodia, the dynamic actin-rich structures that are related to cell migration and cancer cell invasion. Obscurin is a giant muscle protein that plays important roles in the organization and assembly of the myofibril and the sarcoplasmic reticulum. Type I myosins (Myosin-I) are actin-dependent motors in endocytic actin structures and actin patches. They play roles in membrane traffic in endocytic and secretory pathways, cell motility, and mechanosensing. Myosin-I contains an N-terminal actin-activated ATPase, a phospholipid-binding TH1 (tail homology 1) domain, and a C-terminal extension which includes an F-actin-binding TH2 domain, an SH3 domain, and an acidic peptide that participates in activating the Arp2/3complex. The SH3 domain of myosin-I is required for myosin-I-induced actin polymerization. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212790 [Multi-domain]  Cd Length: 53  Bit Score: 47.63  E-value: 1.10e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907111721 1630 VVIHDFTACNSNELTIRRGQTVEVLERphDKPDWCLVRTTDRspaaEGLVPC 1681
Cdd:cd11856      3 VAIADYEAQGDDEISLQEGEVVEVLEK--NDSGWWYVRKGDK----EGWVPA 48
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
2765-2959 1.22e-06

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. 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 CDK8 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: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 53.52  E-value: 1.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2765 DAFYSEVAELGRGRFAVVKKCDQKGTK--RAVATKFVNKKLMKRdQVTHELGILQNLQHPLLVSLLDTF--ETPTSYVLV 2840
Cdd:cd07868     16 DLFEYEGCKVGRGTYGHVYKAKRKDGKddKDYALKQIEGTGISM-SACREIALLRELKHPNVISLQKVFlsHADRKVWLL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2841 LEMADQG--------RLLDCVVRWGSLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILV-DQSLAKPTIKLADFGD 2911
Cdd:cd07868     95 FDYAEHDlwhiikfhRASKANKKPVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmGEGPERGRVKIADMGF 174
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907111721 2912 AVQLNTTYY----IHQLLGNPEFAAPEIILG-NPVSLTADTWSVGVLTYVLLS 2959
Cdd:cd07868    175 ARLFNSPLKpladLDPVVVTFWYRAPELLLGaRHYTKAIDIWAIGCIFAELLT 227
pknD PRK13184
serine/threonine-protein kinase PknD;
2875-2964 1.30e-06

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 54.39  E-value: 1.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2875 VRYLHNCRIAHLDLKPENIL---------VDQSLAKPTIKLADFGDAVQLNTTYYIH-------QLLGNPEFAAPEIILG 2938
Cdd:PRK13184   126 IEYVHSKGVLHRDLKPDNILlglfgevviLDWGAAIFKKLEEEDLLDIDVDERNICYssmtipgKIVGTPDYMAPERLLG 205
                           90       100
                   ....*....|....*....|....*.
gi 1907111721 2939 NPVSLTADTWSVGVLTYVLLSGVSPF 2964
Cdd:PRK13184   206 VPASESTDIYALGVILYQMLTLSFPY 231
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
2774-3018 1.36e-06

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 52.74  E-value: 1.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2774 LGRGRFAVVKKCDQKGTkraVATKFVNKKLMKRDQV---THELGILQNLQHPLLVSLLDTFETPTSYVLVLEMAdQGRLL 2850
Cdd:cd14063      8 IGKGRFGRVHRGRWHGD---VAIKLLNIDYLNEEQLeafKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTSLC-KGRTL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2851 DCVVRWG--SLTEGKVRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDQSlakpTIKLADFG--DAVQLNTTYYIHQLLG 2926
Cdd:cd14063     84 YSLIHERkeKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENG----RVVITDFGlfSLSGLLQPGRREDTLV 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2927 NPE----FAAPEIIlGN-----------PVSLTADTWSVGVLTYVLLSGVSPFLDDSVEETCLNI-CRLDFSFPEdyfQG 2990
Cdd:cd14063    160 IPNgwlcYLAPEII-RAlspdldfeeslPFTKASDVYAFGTVWYELLAGRWPFKEQPAESIIWQVgCGKKQSLSQ---LD 235
                          250       260
                   ....*....|....*....|....*...
gi 1907111721 2991 VSQKAKEFVCFLLQEDPAKRPSAALALQ 3018
Cdd:cd14063    236 IGREVKDILMQCWAYDPEKRPTFSDLLR 263
IgI_1_NCAM-1 cd05865
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the ...
2671-2743 1.43e-06

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1). NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-nonNCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409451  Cd Length: 97  Bit Score: 48.88  E-value: 1.43e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907111721 2671 GETVVFRCRVCGRPKAS-ITWKGPEHNTLN-NDDHYSISYSDIGEATLKIIGVSTEDDGIYTCIAVNDMGSASSS 2743
Cdd:cd05865     15 GESKFFLCQVAGEAKDKdISWFSPNGEKLTpNQQRISVVRNDDYSSTLTIYNANIDDAGIYKCVVSNEDEGESEA 89
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
2666-2738 1.60e-06

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 48.75  E-value: 1.60e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907111721 2666 VTCETGETVVFRCRVCGRPKASITWKGPEHNtLNNDDHYSISYSDIGEATLKIIGVSTEDDGIYTCIAVNDMG 2738
Cdd:cd05891     11 VTIMEGKTLNLTCTVFGNPDPEVIWFKNDQD-IELSEHYSVKLEQGKYASLTIKGVTSEDSGKYSINVKNKYG 82
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
309-412 3.05e-06

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 48.08  E-value: 3.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  309 QLRLFEQDAEKMFDWIThNKGLFLNSyTEIGTSHPHAMELQTQHNHFAMNcMNVY-VNINRIMSVANRLVESGHYASQQI 387
Cdd:pfam00435    2 LLQQFFRDADDLESWIE-EKEALLSS-EDYGKDLESVQALLKKHKALEAE-LAAHqDRVEALNELAEKLIDEGHYASEEI 78
                           90       100
                   ....*....|....*....|....*
gi 1907111721  388 KQIANQLEQEWKAFAAALDERSTLL 412
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKL 103
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
2143-2238 9.08e-06

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 46.77  E-value: 9.08e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  2143 QDAGLLPRCKERRVFLFEQIVIFSEPLDKKKGFSMPGFLFKNSIKVSClCLEENVESDPCKFALTSRTGdavETFVLHSS 2222
Cdd:smart00233   10 KSGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKGSIDLSGCTVRE-APDPDSSKKPHCFEIKTSDR---KTLLLQAE 85
                            90
                    ....*....|....*.
gi 1907111721  2223 SPSVRQTWIHEINQIL 2238
Cdd:smart00233   86 SEEEREKWVEALRKAI 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
539-638 1.03e-05

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 46.54  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  539 FQQDVQQVLDWIENHgEAFLSKhTGVGKSLHRARALQKRHEDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYQAAH 618
Cdd:pfam00435    6 FFRDADDLESWIEEK-EALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83
                           90       100
                   ....*....|....*....|
gi 1907111721  619 QLEDRIQDFVRRVEQRKILL 638
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKL 103
PH pfam00169
PH domain; PH stands for pleckstrin homology.
2143-2239 1.36e-05

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 46.40  E-value: 1.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2143 QDAGLLPRCKERRVFLFEQIVIFSepldkKKGFSMPGFLFKNSIKVSCLCLEENVESD----PCKFALTSRTGDAVETFV 2218
Cdd:pfam00169   10 KGGGKKKSWKKRYFVLFDGSLLYY-----KDDKSGKSKEPKGSISLSGCEVVEVVASDspkrKFCFELRTGERTGKRTYL 84
                           90       100
                   ....*....|....*....|.
gi 1907111721 2219 LHSSSPSVRQTWIHEINQILE 2239
Cdd:pfam00169   85 LQAESEEERKDWIKAIQSAIR 105
PH_Obscurin cd13239
Obscurin pleckstrin homology (PH) domain; Obscurin (also called Obscurin-RhoGEF; ...
2119-2243 4.30e-05

Obscurin pleckstrin homology (PH) domain; Obscurin (also called Obscurin-RhoGEF; Obscurin-myosin light chain kinase/Obscurin-MLCK) is a giant muscle protein that is concentrated at the peripheries of Z-disks and M-lines. It binds small ankyrin I, a component of the sarcoplasmic reticulum (SR) membrane. It is associated with the contractile apparatus through binding with titin and sarcomeric myosin. It plays important roles in the organization and assembly of the myofibril and the SR. Obscurin has been observed as alternatively-spliced isoforms. The major isoform in sleletal muscle, approximately 800 kDa in size, is composed of many adhesion modules and signaling domains. It harbors 49 Ig and 2 FNIII repeats at the N-terminues, a complex middle region with additional Ig domains, an IQ motif, and a conserved SH3 domain near RhoGEF and PH domains, and a non-modular C-terminus with phosphorylation motifs. The obscurin gene also encodes two kinase domains, which are not part of the 800 kDa form of the protein, but is part of smaller spliced products that present in heart muscle. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270059  Cd Length: 125  Bit Score: 45.61  E-value: 4.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2119 LQGFDGKIVAQGKLLLQDTFLVTDQDAGLLP--RCKERRVFLFEQIVIFSEPlDKKKGFSMPGFLFKNSIKVSCLCLEEN 2196
Cdd:cd13239      2 IENYPAPLQALGEPIRQGHFTVWEEAPEVKTssRGHHRHVFLFKNCVVICKP-KRDSRTDTVTYVFKNKMKLSDIDVKDT 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1907111721 2197 VESDPCKFALTSRTGDAVETFVLHSSSPSVRQTWIHEINQIleNQRN 2243
Cdd:cd13239     81 VEGDDRSFGLWHEHRGSVRKYTLQARSAIIKSSWLKDLRDL--QQRL 125
PH_unc89 cd13325
unc89 pleckstrin homology (PH) domain; unc89 is a myofibrillar protein. unc89-B the largest ...
2124-2240 1.14e-04

unc89 pleckstrin homology (PH) domain; unc89 is a myofibrillar protein. unc89-B the largest isoform is composed of 53 immunoglobulin (Ig) domains, 2 Fn3 domains, a triplet of SH3, DH and PH domains at its N-terminus, and 2 protein kinase domains (PK1 and PK2) at its C-terminus. unc-89 mutants display disorganization of muscle A-bands, and usually lack M-lines. The COOH-terminal region of obscurin, the human homolog of unc89, interacts via two specific Ig-like domains with the NH(2)-terminal Z-disk region of titin, a protein that connects the Z line to the M line in the sarcomere and contributes to the contraction of striated muscle. obscurin is also thought to be involved in Ca2+/calmodulin via its IQ domains, as well as G protein-coupled signal transduction in the sarcomere via its RhoGEF/DH domain. The DH-PH region of OBSCN and unc89, the C. elegans homolog, has exchange activity for RhoA and Rho-1 respectively, but not for the small GTPases homologous to Cdc42 or Rac. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270134  Cd Length: 114  Bit Score: 43.88  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2124 GKIVAQGKLLLQDTFLVTDQDAgllpRCKERRVFLFEQIVIFSepldKKKGFSMPG--FLFKNSIKVScLCLEENVESDP 2201
Cdd:cd13325      1 GNIHKLGRLLRHDWFTVTDGEG----KAKERYLFLFKSRILIT----KVRRISEDRsvFILKDIIRLP-EVNVKQHPDDE 71
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1907111721 2202 CKFAL---TSRTGDAVETFVLHSssPSVRQTWIHEINQILEN 2240
Cdd:cd13325     72 RTFELqpkLPAFGILPIDFKAHK--DEIKDYWLNEIEEYAND 111
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
188-306 5.83e-04

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 41.54  E-value: 5.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  188 FEEYISNAAHMLSRLEELQDVLAKKELPQDLEGARNMIDEHSQLKK--KVIKAPIEDLDLEGQKLLQRiQSSDSfpkkns 265
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAelAAHQDRVEALNELAEKLIDE-GHYAS------ 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1907111721  266 gsgnadlqnllPKVSTMLDRLHSTRQHLHQMWHVRKLKLDQ 306
Cdd:pfam00435   76 -----------EEIQERLEELNERWEQLLELAAERKQKLEE 105
SH3_Kalirin_2 cd11853
Second Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
1630-1680 1.17e-03

Second Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or TRAD, is a large neuronal dual Rho guanine nucleotide exchange factor (RhoGEF) that activates Rac1, RhoA, and RhoG using two RhoGEF domains. Kalirin exists in many isoforms generated by alternative splicing and the use of multiple promoters; the major isoforms are kalirin-7, -9, and -12, which differ at their C-terminal ends. Kalirin-12, the longest isoform, contains an N-terminal Sec14p domain, spectrin-like repeats, two RhoGEF domains, two SH3 domains, as well as Ig, FNIII, and kinase domains at the C-terminal end. Kalirin-7 contains only a single RhoGEF domain and does not contain an SH3 domain. Kalirin, through its many isoforms, interacts with many different proteins and is able to localize to different locations within the cell. It influences neurite initiation, axon growth, dendritic morphogenesis, vesicle trafficking, neuronal maintenance, and neurodegeneration. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212787  Cd Length: 59  Bit Score: 39.35  E-value: 1.17e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907111721 1630 VVIHDFTACNSNELTIRRGQTVEVLERphDKPDWCLVR--TTDRSPAAEGLVP 1680
Cdd:cd11853      3 PVIQDYYALKEDEICVSQGEVVQILAA--NQQNMFLVYrpATDQSPAAEGWIP 53
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
644-751 1.45e-03

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 40.38  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  644 FHTHVKELWTWLEELQKELLDDVYAESVEAVQDLIKRFGQQQQTTLQVTVNViKEGEDLIQQLRDSAISSNKtphnssin 723
Cdd:pfam00435    6 FFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRV-EALNELAEKLIDEGHYASE-------- 76
                           90       100
                   ....*....|....*....|....*...
gi 1907111721  724 HIETVLQQLDEAQSQMEELFQERKIKLE 751
Cdd:pfam00435   77 EIQERLEELNERWEQLLELAAERKQKLE 104
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
2152-2234 4.05e-03

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 39.06  E-value: 4.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721 2152 KERRVFLFEQIVIFSEplDKKKGFSMPgflfKNSIKVS--CLCLEENVESDPCKFALTSRTGdavETFVLHSSSPSVRQT 2229
Cdd:cd00821     17 KKRWFVLFEGVLLYYK--SKKDSSYKP----KGSIPLSgiLEVEEVSPKERPHCFELVTPDG---RTYYLQADSEEERQE 87

                   ....*
gi 1907111721 2230 WIHEI 2234
Cdd:cd00821     88 WLKAL 92
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
177-307 4.16e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 41.28  E-value: 4.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111721  177 NHEEWIEIRVAFEEYISNAAHMLSRLEELQDVLAKKELPQDLEGARNMIDEHSQLKKKV--IKAPIEDLDLEGQKLLQRI 254
Cdd:cd00176     97 ERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELeaHEPRLKSLNELAEELLEEG 176
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907111721  255 QSSDsfpkknsgsgnadlqnlLPKVSTMLDRLHSTRQHLHQMWHVRKLKLDQC 307
Cdd:cd00176    177 HPDA-----------------DEEIEEKLEELNERWEELLELAEERQKKLEEA 212
 
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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