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Conserved domains on  [gi|124804138|ref|XP_001347913|]
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calcium-dependent protein kinase 7 [Plasmodium falciparum 3D7]

Protein Classification

CAMK family serine/threonine-protein kinase( domain architecture ID 10351314)

CAMK family serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; contains a Pleckstrin homology (PH) domain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
1821-2076 8.92e-104

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: 333.29  E-value: 8.92e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd05117     2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMELC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCAPNELLKEP 1980
Cdd:cd05117    82 TGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIFEEGEKLKTV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEM--NIQKNYvLSFKDYIWKSISSSAKDLISKLL 2058
Cdd:cd05117   162 CGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELfeKILKGK-YSFDSPEWKNVSEEAKDLIKRLL 240
                         250
                  ....*....|....*...
gi 124804138 2059 ELNVEKRISANEALEHIW 2076
Cdd:cd05117   241 VVDPKKRLTAAEALNHPW 258
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
1716-1808 1.62e-13

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13288:

Pssm-ID: 473070 [Multi-domain]  Cd Length: 120  Bit Score: 69.19  E-value: 1.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1716 KEGILYKIGKHLHQFKARYYILFDNLLYYYDKKRNLKPRGFMFLEGCYVELIAKNDninKYGFSICHKGTkqvqKRNLYV 1795
Cdd:cd13288    10 KEGYLWKKGERNTSYQKRWFVLKGNLLFYFEKKGDREPLGVIVLEGCTVELAEDAE---PYAFAIRFDGP----GARSYV 82
                          90
                  ....*....|....*.
gi 124804138 1796 ---NTLEERDEWVQAL 1808
Cdd:cd13288    83 laaENQEDMESWMKAL 98
 
Name Accession Description Interval E-value
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
1821-2076 8.92e-104

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: 333.29  E-value: 8.92e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd05117     2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMELC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCAPNELLKEP 1980
Cdd:cd05117    82 TGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIFEEGEKLKTV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEM--NIQKNYvLSFKDYIWKSISSSAKDLISKLL 2058
Cdd:cd05117   162 CGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELfeKILKGK-YSFDSPEWKNVSEEAKDLIKRLL 240
                         250
                  ....*....|....*...
gi 124804138 2059 ELNVEKRISANEALEHIW 2076
Cdd:cd05117   241 VVDPKKRLTAAEALNHPW 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
1821-2077 5.28e-92

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 299.06  E-value: 5.28e-92
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138   1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERILR-EIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYC 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138   1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLSTLCAPNELLKEP 1980
Cdd:smart00220   80 EGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLD---EDGHVKLADFGLARQLDPGEKLTTF 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138   1981 CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTE--MNIQKNYVLSFKDYIWKsISSSAKDLISKLL 2058
Cdd:smart00220  157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLelFKKIGKPKPPFPPPEWD-ISPEAKDLIRKLL 235
                           250
                    ....*....|....*....
gi 124804138   2059 ELNVEKRISANEALEHIWV 2077
Cdd:smart00220  236 VKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
1821-2077 2.52e-61

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 209.79  E-value: 2.52e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138  1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138  1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVaylhrcgiihrdikpenilltdksrdaqikltdfglstlcAPNELLKEP 1980
Cdd:pfam00069   81 EGGSLFDLLSEKGAFSEREAKFIMKQILEGL----------------------------------------ESGSSLTTF 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138  1981 CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYVLSFKDYIWKSISSSAKDLISKLLEL 2060
Cdd:pfam00069  121 VGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPSNLSEEAKDLLKKLLKK 200
                          250
                   ....*....|....*..
gi 124804138  2061 NVEKRISANEALEHIWV 2077
Cdd:pfam00069  201 DPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
1821-2073 5.04e-50

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 186.37  E-value: 5.04e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYE-KELLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEaRERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLSTLCAPNELLKE 1979
Cdd:COG0515    89 VEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLT---PDGRVKLIDFGIARALGGATLTQT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 --PCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEM--NIQKNYVLSFKDyIWKSISSSAKDLIS 2055
Cdd:COG0515   166 gtVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELlrAHLREPPPPPSE-LRPDLPPALDAIVL 244
                         250
                  ....*....|....*....
gi 124804138 2056 KLLELNVEKRI-SANEALE 2073
Cdd:COG0515   245 RALAKDPEERYqSAAELAA 263
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
1821-2066 5.96e-34

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 134.56  E-value: 5.96e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSV-SIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:PTZ00263   20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREIlKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEF 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLCApnELLKE 1979
Cdd:PTZ00263  100 VVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNK---GHVKVTDFGFAKKVP--DRTFT 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 PCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpiNKNTEMNIQKNyVLSFKDYIWKSISSSAKDLISKLLE 2059
Cdd:PTZ00263  175 LCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPF--FDDTPFRIYEK-ILAGRLKFPNWFDGRARDLVKGLLQ 251

                  ....*..
gi 124804138 2060 LNVEKRI 2066
Cdd:PTZ00263  252 TDHTKRL 258
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
1821-2020 1.12e-26

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 117.59  E-value: 1.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdkRSvsiyekELLRSEISILRLLR---------HPNV--IYlkeiiNT 1889
Cdd:NF033483    9 YEIGERIGRGGMAEVYLAKDTRLDRDVAVKVL--RP------DLARDPEFVARFRReaqsaaslsHPNIvsVY-----DV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1890 KET---LYISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFG 1966
Cdd:NF033483   76 GEDggiPYIVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILIT---KDGRVKVTDFG 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124804138 1967 L------STLCAPNELLkepcGTLAYVAPEvitlQGYNHKVDA----WSIGIILYLLLSGKLPF 2020
Cdd:NF033483  153 IaralssTTMTQTNSVL----GTVHYLSPE----QARGGTVDArsdiYSLGIVLYEMLTGRPPF 208
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
1842-2017 4.21e-17

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: 88.36  E-value: 4.21e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138  1842 QTNSEFAIKVI-DKRSVSIYEKELLRSEISILRLLRHPNVIYLkeiINTKET----LYISMELVKGGELYDFLLAETRLS 1916
Cdd:TIGR03903    1 MTGHEVAIKLLrTDAPEEEHQRARFRRETALCARLYHPNIVAL---LDSGEAppglLFAVFEYVPGRTLREVLAADGALP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138  1917 EIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCAPNE--------LLKEPCGTLAYVA 1988
Cdd:TIGR03903   78 AGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPHAKVLDFGIGTLLPGVRdadvatltRTTEVLGTPTYCA 157
                          170       180
                   ....*....|....*....|....*....
gi 124804138  1989 PEVITLQGYNHKVDAWSIGIILYLLLSGK 2017
Cdd:TIGR03903  158 PEQLRGEPVTPNSDLYAWGLIFLECLTGQ 186
PH_Ses cd13288
Sesquipedalian family Pleckstrin homology (PH) domain; The sesquipedalian family has 2 ...
1716-1808 1.62e-13

Sesquipedalian family Pleckstrin homology (PH) domain; The sesquipedalian family has 2 mammalian members: Ses1 and Ses2, which are also callled 7 kDa inositol polyphosphate phosphatase-interacting protein 1 and 2. They play a role in endocytic trafficking and are required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane. Members of this family form homodimers and heterodimers. Sesquipedalian interacts with inositol polyphosphate 5-phosphatase OCRL-1 (INPP5F) also known as Lowe oculocerebrorenal syndrome protein, a phosphatase enzyme that is involved in actin polymerization and is found in the trans-Golgi network and INPP5B. Sesquipedalian contains a single 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: 270105 [Multi-domain]  Cd Length: 120  Bit Score: 69.19  E-value: 1.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1716 KEGILYKIGKHLHQFKARYYILFDNLLYYYDKKRNLKPRGFMFLEGCYVELIAKNDninKYGFSICHKGTkqvqKRNLYV 1795
Cdd:cd13288    10 KEGYLWKKGERNTSYQKRWFVLKGNLLFYFEKKGDREPLGVIVLEGCTVELAEDAE---PYAFAIRFDGP----GARSYV 82
                          90
                  ....*....|....*.
gi 124804138 1796 ---NTLEERDEWVQAL 1808
Cdd:cd13288    83 laaENQEDMESWMKAL 98
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
1715-1813 8.18e-12

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: 63.72  E-value: 8.18e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138   1715 LKEGILYKIGK-HLHQFKARYYILFDNLLYYYDKK---RNLKPRGFMFLEGCYVELIAKNDNIN-KYGFSICHKGTKQVq 1789
Cdd:smart00233    2 IKEGWLYKKSGgGKKSWKKRYFVLFNSTLLYYKSKkdkKSYKPKGSIDLSGCTVREAPDPDSSKkPHCFEIKTSDRKTL- 80
                            90       100
                    ....*....|....*....|....
gi 124804138   1790 krNLYVNTLEERDEWVQALYSSTK 1813
Cdd:smart00233   81 --LLQAESEEEREKWVEALRKAIA 102
PH pfam00169
PH domain; PH stands for pleckstrin homology.
1716-1813 1.53e-11

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 62.97  E-value: 1.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138  1716 KEGILYKIGKHLH-QFKARYYILFDNLLYYYDKK---RNLKPRGFMFLEGCYVELIAKNDNIN-KYGFSICHKGTKQVQK 1790
Cdd:pfam00169    3 KEGWLLKKGGGKKkSWKKRYFVLFDGSLLYYKDDksgKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTGKRT 82
                           90       100
                   ....*....|....*....|...
gi 124804138  1791 RNLYVNTLEERDEWVQALYSSTK 1813
Cdd:pfam00169   83 YLLQAESEEERKDWIKAIQSAIR 105
 
Name Accession Description Interval E-value
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
1821-2076 8.92e-104

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: 333.29  E-value: 8.92e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd05117     2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMELC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCAPNELLKEP 1980
Cdd:cd05117    82 TGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIFEEGEKLKTV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEM--NIQKNYvLSFKDYIWKSISSSAKDLISKLL 2058
Cdd:cd05117   162 CGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELfeKILKGK-YSFDSPEWKNVSEEAKDLIKRLL 240
                         250
                  ....*....|....*...
gi 124804138 2059 ELNVEKRISANEALEHIW 2076
Cdd:cd05117   241 VVDPKKRLTAAEALNHPW 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
1821-2077 5.28e-92

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 299.06  E-value: 5.28e-92
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138   1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERILR-EIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYC 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138   1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLSTLCAPNELLKEP 1980
Cdd:smart00220   80 EGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLD---EDGHVKLADFGLARQLDPGEKLTTF 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138   1981 CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTE--MNIQKNYVLSFKDYIWKsISSSAKDLISKLL 2058
Cdd:smart00220  157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLelFKKIGKPKPPFPPPEWD-ISPEAKDLIRKLL 235
                           250
                    ....*....|....*....
gi 124804138   2059 ELNVEKRISANEALEHIWV 2077
Cdd:smart00220  236 VKDPEKRLTAEEALQHPFF 254
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
1821-2076 2.38e-91

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: 297.12  E-value: 2.38e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd14003     2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtDKsrDAQIKLTDFGLSTLCAPNELLKEP 1980
Cdd:cd14003    82 SGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILL-DK--NGNLKIIDFGLSNEFRGGSLLKTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 CGTLAYVAPEVITLQGYN-HKVDAWSIGIILYLLLSGKLPFpinKNTEMNIQKNYVLSFKDYIWKSISSSAKDLISKLLE 2059
Cdd:cd14003   159 CGTPAYAAPEVLLGRKYDgPKADVWSLGVILYAMLTGYLPF---DDDNDSKLFRKILKGKYPIPSHLSPDARDLIRRMLV 235
                         250
                  ....*....|....*..
gi 124804138 2060 LNVEKRISANEALEHIW 2076
Cdd:cd14003   236 VDPSKRITIEEILNHPW 252
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
1821-2082 5.31e-73

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: 246.01  E-value: 5.31e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKrsvsiyEKELLRSEISIL-RLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd14091     2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDK------SKRDPSEEIEILlRYGQHPNIITLRDVYDDGNSVYLVTEL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQ-IKLTDFGLS-TLCAPNELL 1977
Cdd:cd14091    76 LRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDPEsLRICDFGFAkQLRAENGLL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKN-TEMNIQK---NYVLSFKDYIWKSISSSAKDL 2053
Cdd:cd14091   156 MTPCYTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFASGPNdTPEVILArigSGKIDLSGGNWDHVSDSAKDL 235
                         250       260
                  ....*....|....*....|....*....
gi 124804138 2054 ISKLLELNVEKRISANEALEHIWVKNPTA 2082
Cdd:cd14091   236 VRKMLHVDPSQRPTAAQVLQHPWIRNRDS 264
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
1821-2076 7.09e-72

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: 241.46  E-value: 7.09e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKeLLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd14095     2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEH-MIENEVAILRRVKHPNIVQLIEEYDTDTELYLVMELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENiLLTDKSRDAQI--KLTDFGLSTLCapNELLK 1978
Cdd:cd14095    81 KGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPEN-LLVVEHEDGSKslKLADFGLATEV--KEPLF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1979 EPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF--PINKNTEM--NIQKNYVlSFKDYIWKSISSSAKDLI 2054
Cdd:cd14095   158 TVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFrsPDRDQEELfdLILAGEF-EFLSPYWDNISDSAKDLI 236
                         250       260
                  ....*....|....*....|..
gi 124804138 2055 SKLLELNVEKRISANEALEHIW 2076
Cdd:cd14095   237 SRMLVVDPEKRYSAGQVLDHPW 258
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
1818-2076 1.13e-71

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: 241.49  E-value: 1.13e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1818 YNLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRS--VSIYEKELL----RSEISILRLL-RHPNVIYLKEIINTK 1890
Cdd:cd14093     2 YAKYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIDITGekSSENEAEELreatRREIEILRQVsGHPNIIELHDVFESP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1891 ETLYISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTL 1970
Cdd:cd14093    82 TFIFLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDD---NLNVKISDFGFATR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1971 CAPNELLKEPCGTLAYVAPEVI------TLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEM--NIQK-NYvlSFKDY 2041
Cdd:cd14093   159 LDEGEKLRELCGTPGYLAPEVLkcsmydNAPGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMlrNIMEgKY--EFGSP 236
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 124804138 2042 IWKSISSSAKDLISKLLELNVEKRISANEALEHIW 2076
Cdd:cd14093   237 EWDDISDTAKDLISKLLVVDPKKRLTAEEALEHPF 271
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
1821-2078 2.70e-70

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: 236.99  E-value: 2.70e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRS-VSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd14007     2 FEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQlQKSGLEHQLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSrdaQIKLTDFGLSTLcAPNELLKE 1979
Cdd:cd14007    82 APNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNG---ELKLADFGWSVH-APSNRRKT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 PCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpiNKNTEMNIQKNyVLSFKDYIWKSISSSAKDLISKLLE 2059
Cdd:cd14007   158 FCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPF--ESKSHQETYKR-IQNVDIKFPSSVSPEAKDLISKLLQ 234
                         250
                  ....*....|....*....
gi 124804138 2060 LNVEKRISANEALEHIWVK 2078
Cdd:cd14007   235 KDPSKRLSLEQVLNHPWIK 253
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1821-2078 4.69e-70

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: 238.35  E-value: 4.69e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YEL---HEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRsvsiyeKELLRsEISILRLLR-HPNVIYLKEIINTKETLYIS 1896
Cdd:cd14092     5 YELdlrEEALGDGSFSVCRKCVHKKTGQEFAVKIVSRR------LDTSR-EVQLLRLCQgHPNIVKLHEVFQDELHTYLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1897 MELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCAPNEL 1976
Cdd:cd14092    78 MELLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDAEIKIVDFGFARLKPENQP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1977 LKEPCGTLAYVAPEVI----TLQGYNHKVDAWSIGIILYLLLSGKLPF-PINKNTE----MNIQKNYVLSFKDYIWKSIS 2047
Cdd:cd14092   158 LKTPCFTLPYAAPEVLkqalSTQGYDESCDLWSLGVILYTMLSGQVPFqSPSRNESaaeiMKRIKSGDFSFDGEEWKNVS 237
                         250       260       270
                  ....*....|....*....|....*....|.
gi 124804138 2048 SSAKDLISKLLELNVEKRISANEALEHIWVK 2078
Cdd:cd14092   238 SEAKSLIQGLLTVDPSKRLTMSELRNHPWLQ 268
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1821-2076 8.31e-69

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: 233.03  E-value: 8.31e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEkELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd14083     5 YEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKE-DSLENEIAVLRKIKHPNIVQLLDIYESKSHLYLVMELV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCApNELLKEP 1980
Cdd:cd14083    84 TGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSPDEDSKIMISDFGLSKMED-SGVMSTA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEM--NIQKNYvLSFKDYIWKSISSSAKDLISKLL 2058
Cdd:cd14083   163 CGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLfaQILKAE-YEFDSPYWDDISDSAKDFIRHLM 241
                         250
                  ....*....|....*...
gi 124804138 2059 ELNVEKRISANEALEHIW 2076
Cdd:cd14083   242 EKDPNKRYTCEQALEHPW 259
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
1821-2077 2.72e-67

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: 228.57  E-value: 2.72e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSiyeKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd14087     3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKCRG---REVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMELA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLC--APNELLK 1978
Cdd:cd14087    80 TGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPDSKIMITDFGLASTRkkGPNCLMK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1979 EPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMN---IQKNYvlSFKDYIWKSISSSAKDLIS 2055
Cdd:cd14087   160 TTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYrqiLRAKY--SYSGEPWPSVSNLAKDFID 237
                         250       260
                  ....*....|....*....|..
gi 124804138 2056 KLLELNVEKRISANEALEHIWV 2077
Cdd:cd14087   238 RLLTVNPGERLSATQALKHPWI 259
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
1821-2076 6.01e-67

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: 227.29  E-value: 6.01e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDK-RSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd14663     2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKeQVAREGMVEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVMEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPNE---L 1976
Cdd:cd14663    82 VTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDE---DGNLKISDFGLSALSEQFRqdgL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1977 LKEPCGTLAYVAPEVITLQGYN-HKVDAWSIGIILYLLLSGKLPFPiNKNTEMNIQKNYVLSFKDYIWksISSSAKDLIS 2055
Cdd:cd14663   159 LHTTCGTPNYVAPEVLARRGYDgAKADIWSCGVILFVLLAGYLPFD-DENLMALYRKIMKGEFEYPRW--FSPGAKSLIK 235
                         250       260
                  ....*....|....*....|.
gi 124804138 2056 KLLELNVEKRISANEALEHIW 2076
Cdd:cd14663   236 RILDPNPSTRITVEQIMASPW 256
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
1827-2076 6.55e-66

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: 224.02  E-value: 6.55e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGELY 1906
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1907 DFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCAPNELLKEPCGTLAY 1986
Cdd:cd14009    81 QYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDDPVLKIADFGFARSLQPASMAETLCGSPLY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1987 VAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEM--NIQKNyVLSFKDYIWKSISSSAKDLISKLLELNVEK 2064
Cdd:cd14009   161 MAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLlrNIERS-DAVIPFPIAAQLSPDCKDLLRRLLRRDPAE 239
                         250
                  ....*....|..
gi 124804138 2065 RISANEALEHIW 2076
Cdd:cd14009   240 RISFEEFFAHPF 251
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
1821-2077 4.15e-64

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: 219.96  E-value: 4.15e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKEL------LRSEISILRLLRHPNVIYLKEIINTKETLY 1894
Cdd:cd14084     8 YIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKFTIGSRREinkprnIETEIEILKKLSHPCIIKIEDFFDAEDDYY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCAPN 1974
Cdd:cd14084    88 IVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEECLIKITDFGLSKILGET 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1975 ELLKEPCGTLAYVAPEVIT---LQGYNHKVDAWSIGIILYLLLSGKLPFpINKNTEMNIQKNYV---LSFKDYIWKSISS 2048
Cdd:cd14084   168 SLMKTLCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPF-SEEYTQMSLKEQILsgkYTFIPKAWKNVSE 246
                         250       260
                  ....*....|....*....|....*....
gi 124804138 2049 SAKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14084   247 EAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
1827-2071 8.84e-64

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: 218.16  E-value: 8.84e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKEL-LRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGEL 1905
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEhTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1906 YDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLST-LCAPNELLKEPCGTL 1984
Cdd:cd05123    81 FSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDS---DGHIKLTDFGLAKeLSSDGDRTYTFCGTP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1985 AYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEM--NIQKNyVLSFKDYiwksISSSAKDLISKLLELNV 2062
Cdd:cd05123   158 EYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIyeKILKS-PLKFPEY----VSPEAKSLISGLLQKDP 232

                  ....*....
gi 124804138 2063 EKRISANEA 2071
Cdd:cd05123   233 TKRLGSGGA 241
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
1827-2076 1.37e-63

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: 217.52  E-value: 1.37e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVsiyEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGELY 1906
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAAKFIPKRDK---KKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1907 DFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsRDAQIKLTDFGLSTLCAPNELLKEPCGTLAY 1986
Cdd:cd14006    78 DRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADR-PSPQIKIIDFGLARKLNPGEELKEIFGTPEF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1987 VAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF--PINKNTEMNIqKNYVLSFKDYIWKSISSSAKDLISKLLELNVEK 2064
Cdd:cd14006   157 VAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFlgEDDQETLANI-SACRVDFSEEYFSSVSQEAKDFIRKLLVKEPRK 235
                         250
                  ....*....|..
gi 124804138 2065 RISANEALEHIW 2076
Cdd:cd14006   236 RPTAQEALQHPW 247
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
1821-2076 2.43e-63

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: 217.34  E-value: 2.43e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEK--ELLRSEISILRLLRHPNVIYLKEIINTKETLYISME 1898
Cdd:cd14098     2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDKnlQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdKSRDAQIKLTDFGLSTLCAPNELLK 1978
Cdd:cd14098    82 YVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILIT-QDDPVIVKISDFGLAKVIHTGTFLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1979 EPCGTLAYVAPEVITLQ------GYNHKVDAWSIGIILYLLLSGKLPFpiNKNTEMNIQKnyVLSFKDYIWK-----SIS 2047
Cdd:cd14098   161 TFCGTMAYLAPEILMSKeqnlqgGYSNLVDMWSVGCLVYVMLTGALPF--DGSSQLPVEK--RIRKGRYTQPplvdfNIS 236
                         250       260
                  ....*....|....*....|....*....
gi 124804138 2048 SSAKDLISKLLELNVEKRISANEALEHIW 2076
Cdd:cd14098   237 EEAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1819-2079 2.54e-63

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: 218.45  E-value: 2.54e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISME 1898
Cdd:cd14086     1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTlcapnELLK 1978
Cdd:cd14086    81 LVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAAVKLADFGLAI-----EVQG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1979 EP------CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQ-KNYVLSFKDYIWKSISSSAK 2051
Cdd:cd14086   156 DQqawfgfAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQiKAGAYDYPSPEWDTVTPEAK 235
                         250       260
                  ....*....|....*....|....*...
gi 124804138 2052 DLISKLLELNVEKRISANEALEHIWVKN 2079
Cdd:cd14086   236 DLINQMLTVNPAKRITAAEALKHPWICQ 263
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
1821-2077 3.72e-63

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: 216.35  E-value: 3.72e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSvsIYEKELLRS---EISILRLLRHPNVIYLKEIINTKETLYISM 1897
Cdd:cd14081     3 YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEK--LSKESVLMKverEIAIMKLIEHPNVLKLYDVYENKKYLYLVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSrdaQIKLTDFGLSTLCAPNELL 1977
Cdd:cd14081    81 EYVSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKN---NIKIADFGMASLQPEGSLL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPCGTLAYVAPEVITLQGYN-HKVDAWSIGIILYLLLSGKLPFPiNKNTEMNIQKNYVLSFkdYIWKSISSSAKDLISK 2056
Cdd:cd14081   158 ETSCGSPHYACPEVIKGEKYDgRKADIWSCGVILYALLVGALPFD-DDNLRQLLEKVKRGVF--HIPHFISPDAQDLLRR 234
                         250       260
                  ....*....|....*....|.
gi 124804138 2057 LLELNVEKRISANEALEHIWV 2077
Cdd:cd14081   235 MLEVNPEKRITIEEIKKHPWF 255
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1819-2077 5.62e-63

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: 216.43  E-value: 5.62e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELlRSEISILRLLRHPNVIYLKEIINTKETLYISME 1898
Cdd:cd14167     3 DIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKETSI-ENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCAPNELLK 1978
Cdd:cd14167    82 LVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLDEDSKIMISDFGLSKIEGSGSVMS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1979 EPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNT---EMNIQKNYvlSFKDYIWKSISSSAKDLIS 2055
Cdd:cd14167   162 TACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAklfEQILKAEY--EFDSPYWDDISDSAKDFIQ 239
                         250       260
                  ....*....|....*....|..
gi 124804138 2056 KLLELNVEKRISANEALEHIWV 2077
Cdd:cd14167   240 HLMEKDPEKRFTCEQALQHPWI 261
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
1821-2076 1.71e-62

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: 214.90  E-value: 1.71e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEkELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd14184     3 YKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKE-HLIENEVSILRRVKHPNIIMLIEEMDTPAELYLVMELV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQ-IKLTDFGLSTLC-APnelLK 1978
Cdd:cd14184    82 KGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEYPDGTKsLKLGDFGLATVVeGP---LY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1979 EPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpinkNTEMNIQKNYV-------LSFKDYIWKSISSSAK 2051
Cdd:cd14184   159 TVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPF----RSENNLQEDLFdqillgkLEFPSPYWDNITDSAK 234
                         250       260
                  ....*....|....*....|....*
gi 124804138 2052 DLISKLLELNVEKRISANEALEHIW 2076
Cdd:cd14184   235 ELISHMLQVNVEARYTAEQILSHPW 259
Pkinase pfam00069
Protein kinase domain;
1821-2077 2.52e-61

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 209.79  E-value: 2.52e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138  1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138  1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVaylhrcgiihrdikpenilltdksrdaqikltdfglstlcAPNELLKEP 1980
Cdd:pfam00069   81 EGGSLFDLLSEKGAFSEREAKFIMKQILEGL----------------------------------------ESGSSLTTF 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138  1981 CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYVLSFKDYIWKSISSSAKDLISKLLEL 2060
Cdd:pfam00069  121 VGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPSNLSEEAKDLLKKLLKK 200
                          250
                   ....*....|....*..
gi 124804138  2061 NVEKRISANEALEHIWV 2077
Cdd:pfam00069  201 DPSKRLTATQALQHPWF 217
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
1821-2076 3.93e-61

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: 210.59  E-value: 3.93e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKR---SVSIYEKelLRSEISILRLLRHPNVIYLKEIINTKETLYISM 1897
Cdd:cd14079     4 YILGKTLGVGSFGKVKLAEHELTGHKVAVKILNRQkikSLDMEEK--IRREIQILKLFRHPHIIRLYEVIETPTDIFMVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLSTLCAPNELL 1977
Cdd:cd14079    82 EYVSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLD---SNMNVKIADFGLSNIMRDGEFL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPCGTLAYVAPEVITLQGY-NHKVDAWSIGIILYLLLSGKLPFPiNKNTEMNIQKnyVLSFKDYIWKSISSSAKDLISK 2056
Cdd:cd14079   159 KTSCGSPNYAAPEVISGKLYaGPEVDVWSCGVILYALLCGSLPFD-DEHIPNLFKK--IKSGIYTIPSHLSPGARDLIKR 235
                         250       260
                  ....*....|....*....|
gi 124804138 2057 LLELNVEKRISANEALEHIW 2076
Cdd:cd14079   236 MLVVDPLKRITIPEIRQHPW 255
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
1821-2077 1.18e-60

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: 209.35  E-value: 1.18e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSE--FAIKVIDKRSVS--IYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYIS 1896
Cdd:cd14080     2 YRLGKTIGEGSYSKVKLAEYTKSGLKekVACKIIDKKKAPkdFLEKFLPR-ELEILRKLRHPNIIQVYSIFERGSKVFIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1897 MELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRdaqIKLTDFGLSTLCAPNE- 1975
Cdd:cd14080    81 MEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNN---VKLSDFGFARLCPDDDg 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1976 --LLKEPCGTLAYVAPEVitLQG--YNHKV-DAWSIGIILYLLLSGKLPFP---INKNTEMNIQKNyvLSFKDYIWKsIS 2047
Cdd:cd14080   158 dvLSKTFCGSAAYAAPEI--LQGipYDPKKyDIWSLGVILYIMLCGSMPFDdsnIKKMLKDQQNRK--VRFPSSVKK-LS 232
                         250       260       270
                  ....*....|....*....|....*....|
gi 124804138 2048 SSAKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14080   233 PECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
1821-2079 5.45e-60

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: 208.71  E-value: 5.45e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKrsvsiyEKELLRSEISIL-RLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd14178     5 YEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDK------SKRDPSEEIEILlRYGQHPNIITLKDVYDDGKFVYLVMEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQ-IKLTDFGLS-TLCAPNELL 1977
Cdd:cd14178    79 MRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESGNPEsIRICDFGFAkQLRAENGLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF---PINKNTEMNIQ---KNYVLSFKDyiWKSISSSAK 2051
Cdd:cd14178   159 MTPCYTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFangPDDTPEEILARigsGKYALSGGN--WDSISDAAK 236
                         250       260
                  ....*....|....*....|....*...
gi 124804138 2052 DLISKLLELNVEKRISANEALEHIWVKN 2079
Cdd:cd14178   237 DIVSKMLHVDPHQRLTAPQVLRHPWIVN 264
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1817-2082 9.23e-60

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: 208.14  E-value: 9.23e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1817 LYNLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSvsiyEKELLRSEISILRLLRHPNVIYLKEIINTKETLYIS 1896
Cdd:cd14085     1 LEDFFEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKTV----DKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1897 MELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCAPNEL 1976
Cdd:cd14085    77 LELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAPLKIADFGLSKIVDQQVT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1977 LKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpINKNTEMNIQKNYVLSFKDYI---WKSISSSAKDL 2053
Cdd:cd14085   157 MKTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPF-YDERGDQYMFKRILNCDYDFVspwWDDVSLNAKDL 235
                         250       260
                  ....*....|....*....|....*....
gi 124804138 2054 ISKLLELNVEKRISANEALEHIWVKNPTA 2082
Cdd:cd14085   236 VKKLIVLDPKKRLTTQQALQHPWVTGKAA 264
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1821-2082 2.25e-59

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: 206.77  E-value: 2.25e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSiyEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd14166     5 FIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLS--RDSSLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQLV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLcAPNELLKEP 1980
Cdd:cd14166    83 SGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTPDENSKIMITDFGLSKM-EQNGIMSTA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEM--NIQKNYvLSFKDYIWKSISSSAKDLISKLL 2058
Cdd:cd14166   162 CGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLfeKIKEGY-YEFESPFWDDISESAKDFIRHLL 240
                         250       260
                  ....*....|....*....|....
gi 124804138 2059 ELNVEKRISANEALEHIWVKNPTA 2082
Cdd:cd14166   241 EKNPSKRYTCEKALSHPWIIGNTA 264
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
1827-2076 2.73e-59

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: 205.15  E-value: 2.73e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSiyEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGELY 1906
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAK--DREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGELF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1907 DFLLAET-RLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDaQIKLTDFGLSTLCAPNELLKEPCGTLA 1985
Cdd:cd14103    79 ERVVDDDfELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRTGN-QIKIIDFGLARKYDPDKKLKVLFGTPE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1986 YVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEM--NIQKnYVLSFKDYIWKSISSSAKDLISKLLELNVE 2063
Cdd:cd14103   158 FVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETlaNVTR-AKWDFDDEAFDDISDEAKDFISKLLVKDPR 236
                         250
                  ....*....|...
gi 124804138 2064 KRISANEALEHIW 2076
Cdd:cd14103   237 KRMSAAQCLQHPW 249
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
1821-2077 3.10e-59

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: 206.80  E-value: 3.10e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEkellrsEISIL-RLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd14175     3 YVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPSE------EIEILlRYGQHPNIITLKDVYDDGKHVYLVTEL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQ-IKLTDFGLS-TLCAPNELL 1977
Cdd:cd14175    77 MRGGELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESGNPEsLRICDFGFAkQLRAENGLL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF---PINKNTEMNIQ---KNYVLSFKDyiWKSISSSAK 2051
Cdd:cd14175   157 MTPCYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFangPSDTPEEILTRigsGKFTLSGGN--WNTVSDAAK 234
                         250       260
                  ....*....|....*....|....*.
gi 124804138 2052 DLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14175   235 DLVSKMLHVDPHQRLTAKQVLQHPWI 260
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1820-2083 3.85e-59

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: 205.89  E-value: 3.85e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1820 LYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKeLLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd14169     4 VYELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEA-MVENEIAVLRRINHENIVSLEDIYESPTHLYLAMEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCAPNeLLKE 1979
Cdd:cd14169    83 VTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATPFEDSKIMISDFGLSKIEAQG-MLST 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 PCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMN---IQKNYvlSFKDYIWKSISSSAKDLISK 2056
Cdd:cd14169   162 ACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFnqiLKAEY--EFDSPYWDDISESAKDFIRH 239
                         250       260
                  ....*....|....*....|....*..
gi 124804138 2057 LLELNVEKRISANEALEHIWVKNPTAV 2083
Cdd:cd14169   240 LLERDPEKRFTCEQALQHPWISGDTAL 266
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
1819-2077 6.04e-59

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: 204.89  E-value: 6.04e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYEL-HEQLGQGKFSTVYRGINKQTNSEFAIKVIDKR-SVSIYEKELLRsEISILRL-LRHPNVIYLKEIINTKETLYI 1895
Cdd:cd14106     7 EVYTVeSTPLGRGKFAVVRKCIHKETGKEYAAKFLRKRrRGQDCRNEILH-EIAVLELcKDCPRVVNLHEVYETRSELIL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1896 SMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCAPNE 1975
Cdd:cd14106    86 ILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPLGDIKLCDFGISRVIGEGE 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1976 LLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTE--MNIQKnYVLSFKDYIWKSISSSAKDL 2053
Cdd:cd14106   166 EIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQEtfLNISQ-CNLDFPEELFKDVSPLAIDF 244
                         250       260
                  ....*....|....*....|....
gi 124804138 2054 ISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14106   245 IKRLLVKDPEKRLTAKECLEHPWL 268
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
1819-2076 6.57e-59

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: 204.57  E-value: 6.57e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYEL--HEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYIS 1896
Cdd:cd14082     1 QLYQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1897 MELVKGGELYDFLLAET-RLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCAPNE 1975
Cdd:cd14082    81 MEKLHGDMLEMILSSEKgRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPFPQVKLCDFGFARIIGEKS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1976 LLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpiNKNTEMNIQ-KNYVLSFKDYIWKSISSSAKDLI 2054
Cdd:cd14082   161 FRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDINDQiQNAAFMYPPNPWKEISPDAIDLI 238
                         250       260
                  ....*....|....*....|..
gi 124804138 2055 SKLLELNVEKRISANEALEHIW 2076
Cdd:cd14082   239 NNLLQVKMRKRYSVDKSLSHPW 260
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
1821-2077 1.07e-58

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: 205.36  E-value: 1.07e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEF-AIKVIDKRSVS-----IYEKELLRSEISILRLLRHPNVIYLKEIINTKETLY 1894
Cdd:cd14096     3 YRLINKIGEGAFSNVYKAVPLRNTGKPvAIKVVRKADLSsdnlkGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYYY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLT-----------DKSRD------ 1957
Cdd:cd14096    83 IVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEpipfipsivklRKADDdetkvd 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1958 -------------AQIKLTDFGLSTLCAPNElLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF---P 2021
Cdd:cd14096   163 egefipgvggggiGIVKLADFGLSKQVWDSN-TKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPFydeS 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 124804138 2022 INKNTEMNIQKNYvlSFKDYIWKSISSSAKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14096   242 IETLTEKISRGDY--TFLSPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
1821-2075 2.20e-58

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: 202.82  E-value: 2.20e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYE-KELLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd14014     2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEfRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPNELL-- 1977
Cdd:cd14014    82 VEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTE---DGRVKLTDFGIARALGDSGLTqt 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNY--VLSFKDYIwKSISSSAKDLIS 2055
Cdd:cd14014   159 GSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQeaPPPPSPLN-PDVPPALDAIIL 237
                         250       260
                  ....*....|....*....|.
gi 124804138 2056 KLLELNVEKRI-SANEALEHI 2075
Cdd:cd14014   238 RALAKDPEERPqSAAELLAAL 258
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
1827-2075 2.61e-58

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: 200.96  E-value: 2.61e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGELY 1906
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLLEELLR-EIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1907 DFLLA-ETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPNELLKEPCGTL- 1984
Cdd:cd00180    80 DLLKEnKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDS---DGTVKLADFGLAKDLDSDDSLLKTTGGTt 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1985 --AYVAPEVITLQGYNHKVDAWSIGIILYlllsgklpfpinkntEMNiqknyvlsfkdyiwksissSAKDLISKLLELNV 2062
Cdd:cd00180   157 ppYYAPPELLGGRYYGPKVDIWSLGVILY---------------ELE-------------------ELKDLIRRMLQYDP 202
                         250
                  ....*....|...
gi 124804138 2063 EKRISANEALEHI 2075
Cdd:cd00180   203 KKRPSAKELLEHL 215
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
1821-2077 6.24e-58

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: 201.46  E-value: 6.24e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSiyeKELLR--SEISILRLLRHPNVIYLKEIINTKETLYISME 1898
Cdd:cd14078     5 YELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKALG---DDLPRvkTEIEALKNLSHQHICRLYHVIETDNKIFMVLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGlstLCAP----- 1973
Cdd:cd14078    82 YCPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDE---DQNLKLIDFG---LCAKpkggm 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1974 NELLKEPCGTLAYVAPEVITLQGY-NHKVDAWSIGIILYLLLSGKLPFPINkntemNIQKNY--VLSFKDYIWKSISSSA 2050
Cdd:cd14078   156 DHHLETCCGSPAYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDDD-----NVMALYrkIQSGKYEEPEWLSPSS 230
                         250       260
                  ....*....|....*....|....*..
gi 124804138 2051 KDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14078   231 KLLLDQMLQVDPKKRITVKELLNHPWV 257
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
1817-2074 6.60e-58

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: 202.07  E-value: 6.60e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1817 LYNLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVID---KRSVSIYEKELLRS----EISILRLLR-HPNVIYLKEIIN 1888
Cdd:cd14182     1 FYEKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDitgGGSFSPEEVQELREatlkEIDILRKVSgHPNIIQLKDTYE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1889 TKETLYISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLS 1968
Cdd:cd14182    81 TNTFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDD---DMNIKLTDFGFS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1969 TLCAPNELLKEPCGTLAYVAPEVITL------QGYNHKVDAWSIGIILYLLLSGKLPFPINKNT---EMNIQKNYvlSFK 2039
Cdd:cd14182   158 CQLDPGEKLREVCGTPGYLAPEIIECsmddnhPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMlmlRMIMSGNY--QFG 235
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 124804138 2040 DYIWKSISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd14182   236 SPEWDDRSDTVKDLISRFLVVQPQKRYTAEEALAH 270
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
1827-2077 9.24e-58

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: 201.24  E-value: 9.24e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVS---IYEK---------ELLRSEISILRLLRHPNVIYLKEIIN--TKET 1892
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRLRkrrEGKNdrgkiknalDDVRREIAIMKKLDHPNIVRLYEVIDdpESDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1893 LYISMELVKGGELYDFLLAETR--LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTL 1970
Cdd:cd14008    81 LYLVLEYCEGGPVMELDSGDRVppLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTA---DGTVKISDFGVSEM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1971 CA-PNELLKEPCGTLAYVAPEVI-----TLQGYnhKVDAWSIGIILYLLLSGKLPFpiNKNTEMNIQKNYVLSFKDYIW- 2043
Cdd:cd14008   158 FEdGNDTLQKTAGTPAFLAPELCdgdskTYSGK--AADIWALGVTLYCLVFGRLPF--NGDNILELYEAIQNQNDEFPIp 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 124804138 2044 KSISSSAKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14008   234 PELSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
1805-2079 1.02e-57

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: 204.10  E-value: 1.02e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1805 VQALYSSTKQNTlyNLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKrsvsiyEKELLRSEISIL-RLLRHPNVIYL 1883
Cdd:cd14176     7 VQQLHRNSIQFT--DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDK------SKRDPTEEIEILlRYGQHPNIITL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1884 KEIINTKETLYISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQ-IKL 1962
Cdd:cd14176    79 KDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPEsIRI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1963 TDFGLST-LCAPNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF---PINKNTEMNIQ-KNYVLS 2037
Cdd:cd14176   159 CDFGFAKqLRAENGLLMTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARiGSGKFS 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 124804138 2038 FKDYIWKSISSSAKDLISKLLELNVEKRISANEALEHIWVKN 2079
Cdd:cd14176   239 LSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVH 280
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
1821-2076 1.26e-57

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: 200.47  E-value: 1.26e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSI-YEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd14099     3 YRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKpKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCA-PNELLK 1978
Cdd:cd14099    83 CSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDE---NMNVKIGDFGLAARLEyDGERKK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1979 EPCGTLAYVAPEVIT-LQGYNHKVDAWSIGIILYLLLSGKLPF--PINKNTEMNIQKNyvlsfkDYIW---KSISSSAKD 2052
Cdd:cd14099   160 TLCGTPNYIAPEVLEkKKGHSFEVDIWSLGVILYTLLVGKPPFetSDVKETYKRIKKN------EYSFpshLSISDEAKD 233
                         250       260
                  ....*....|....*....|....
gi 124804138 2053 LISKLLELNVEKRISANEALEHIW 2076
Cdd:cd14099   234 LIRSMLQPDPTKRPSLDEILSHPF 257
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1817-2079 1.53e-57

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: 202.58  E-value: 1.53e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1817 LYNLYEL---HEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKEllrseISILRLLR-HPNVIYLKEIINTKET 1892
Cdd:cd14179     2 FYQHYELdlkDKPLGEGSFSICRKCLHKKTNQEYAVKIVSKRMEANTQRE-----IAALKLCEgHPNIVKLHEVYHDQLH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1893 LYISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCA 1972
Cdd:cd14179    77 TFLVMELLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDNSEIKIIDFGFARLKP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1973 P-NELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYVL--------SFKDYIW 2043
Cdd:cd14179   157 PdNQPLKTPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKSLTCTSAEEIMkkikqgdfSFEGEAW 236
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 124804138 2044 KSISSSAKDLISKLLELNVEKRISANEALEHIWVKN 2079
Cdd:cd14179   237 KNVSQEAKDLIQGLLTVDPNKRIKMSGLRYNEWLQD 272
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
1820-2077 2.43e-57

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: 200.08  E-value: 2.43e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1820 LYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd14097     2 IYTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENIL----LTDKSRDAQIKLTDFGLS--TLCAP 1973
Cdd:cd14097    82 CEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILvkssIIDNNDKLNIKVTDFGLSvqKYGLG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1974 NELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpINKNTE--MNIQKNYVLSFKDYIWKSISSSAK 2051
Cdd:cd14097   162 EDMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPF-VAKSEEklFEEIRKGDLTFTQSVWQSVSDAAK 240
                         250       260
                  ....*....|....*....|....*.
gi 124804138 2052 DLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14097   241 NVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
1817-2074 2.39e-56

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: 197.89  E-value: 2.39e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1817 LYNLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKEL------LRSEISILRLLR-HPNVIYLKEIINT 1889
Cdd:cd14181     8 FYQKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEVTAERLSPEQLeevrssTLKEIHILRQVSgHPSIITLIDSYES 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1890 KETLYISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLST 1969
Cdd:cd14181    88 STFIFLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDD---QLHIKLSDFGFSC 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1970 LCAPNELLKEPCGTLAYVAPEVI------TLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNT---EMNIQKNYvlSFKD 2040
Cdd:cd14181   165 HLEPGEKLRELCGTPGYLAPEILkcsmdeTHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMlmlRMIMEGRY--QFSS 242
                         250       260       270
                  ....*....|....*....|....*....|....
gi 124804138 2041 YIWKSISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd14181   243 PEWDDRSSTVKDLISRLLVVDPEIRLTAEQALQH 276
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1821-2082 2.66e-56

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: 198.94  E-value: 2.66e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQ---LGQGKFSTVYRGINKQTNSEFAIKVIDKRSvsiyeKELLRSEISILRLLR-HPNVIYLKEIINTKETLYIS 1896
Cdd:cd14180     5 YELDLEepaLGEGSFSVCRKCRHRQSGQEYAVKIISRRM-----EANTQREVAALRLCQsHPNIVALHEVLHDQYHTYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1897 MELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCAPN-E 1975
Cdd:cd14180    80 MELLRGGELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDGAVLKVIDFGFARLRPQGsR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1976 LLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTE--------MNIQKNYVLSFKDYIWKSIS 2047
Cdd:cd14180   160 PLQTPCFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGKMfhnhaadiMHKIKEGDFSLEGEAWKGVS 239
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 124804138 2048 SSAKDLISKLLELNVEKRISANEALEHIWVKNPTA 2082
Cdd:cd14180   240 EEAKDLVRGLLTVDPAKRLKLSELRESDWLQGGSA 274
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
1819-2077 9.99e-56

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: 196.77  E-value: 9.99e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKrsvsiyEKELLRSEISIL-RLLRHPNVIYLKEIINTKETLYISM 1897
Cdd:cd14177     4 DVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDK------SKRDPSEEIEILmRYGQHPNIITLKDVYDDGRYVYLVT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDA-QIKLTDFGLS-TLCAPNE 1975
Cdd:cd14177    78 ELMKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSANAdSIRICDFGFAkQLRGENG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1976 LLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF---PINKNTEMNIQ---KNYVLSFKDyiWKSISSS 2049
Cdd:cd14177   158 LLLTPCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFangPNDTPEEILLRigsGKFSLSGGN--WDTVSDA 235
                         250       260
                  ....*....|....*....|....*...
gi 124804138 2050 AKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14177   236 AKDLLSHMLHVDPHQRYTAEQVLKHSWI 263
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
1820-2077 1.25e-55

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: 194.94  E-value: 1.25e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1820 LYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd14074     4 LYDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDDVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLILEL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLA-ETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSrdAQIKLTDFGLSTLCAPNELLK 1978
Cdd:cd14074    84 GDGGDMYDYIMKhENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQ--GLVKLTDFGFSNKFQPGEKLE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1979 EPCGTLAYVAPEVITLQGYNH-KVDAWSIGIILYLLLSGKLPFPINKNTEMNIQknyVLSFKDYIWKSISSSAKDLISKL 2057
Cdd:cd14074   162 TSCGSLAYSAPEILLGDEYDApAVDIWSLGVILYMLVCGQPPFQEANDSETLTM---IMDCKYTVPAHVSPECKDLIRRM 238
                         250       260
                  ....*....|....*....|
gi 124804138 2058 LELNVEKRISANEALEHIWV 2077
Cdd:cd14074   239 LIRDPKKRASLEEIENHPWL 258
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
1819-2077 3.18e-55

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: 194.24  E-value: 3.18e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSI----YEKELLRSEISILRLLRHPNVIYLKEIINTKETLY 1894
Cdd:cd14105     5 DFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKAsrrgVSREDIEREVSILRQVLHPNIITLHDVFENKTDVV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRD-AQIKLTDFGLSTLCAP 1973
Cdd:cd14105    85 LILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVPiPRIKLIDFGLAHKIED 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1974 NELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF--PINKNTEMNIQK-NYvlSFKDYIWKSISSSA 2050
Cdd:cd14105   165 GNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlgDTKQETLANITAvNY--DFDDEYFSNTSELA 242
                         250       260
                  ....*....|....*....|....*..
gi 124804138 2051 KDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14105   243 KDFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
1819-2077 7.94e-55

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: 192.93  E-value: 7.94e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISME 1898
Cdd:cd14069     1 EDWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSrdaQIKLTDFGLSTLCAPN---E 1975
Cdd:cd14069    81 YASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDEND---NLKISDFGLATVFRYKgkeR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1976 LLKEPCGTLAYVAPEVITLQGYN-HKVDAWSIGIILYLLLSGKLPF--PINKNTE-MNIQKNYvlSFKDYIWKSISSSAK 2051
Cdd:cd14069   158 LLNKMCGTLPYVAPELLAKKKYRaEPVDVWSCGIVLFAMLAGELPWdqPSDSCQEySDWKENK--KTYLTPWKKIDTAAL 235
                         250       260
                  ....*....|....*....|....*.
gi 124804138 2052 DLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14069   236 SLLRKILTENPNKRITIEDIKKHPWY 261
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
1829-2079 2.08e-54

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: 192.05  E-value: 2.08e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1829 QGKFSTVYRGINKQTNSEFAIKVIDKRSVsIYE--KELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGELY 1906
Cdd:cd05579     3 RGAYGRVYLAKKKSTGDLYAIKVIKKRDM-IRKnqVDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDLY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1907 DFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLS----------------TL 1970
Cdd:cd05579    82 SLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILID---ANGHLKLTDFGLSkvglvrrqiklsiqkkSN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1971 CAPNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpiNKNTEMNIQKNyVLSfKDYIW---KSIS 2047
Cdd:cd05579   159 GAPEKEDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPF--HAETPEEIFQN-ILN-GKIEWpedPEVS 234
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 124804138 2048 SSAKDLISKLLELNVEKRISANEALE---HIWVKN 2079
Cdd:cd05579   235 DEAKDLISKLLTPDPEKRLGAKGIEEiknHPFFKG 269
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
1820-2077 3.12e-54

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: 190.88  E-value: 3.12e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1820 LYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSiyEKELLRSEISILRLLRHPNVI-YLKEIInTKETLYISME 1898
Cdd:cd05122     1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKE--KKESILNEIAILKKCKHPNIVkYYGSYL-KKDELWIVME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFLLA-ETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPNELL 1977
Cdd:cd05122    78 FCSGGSLKDLLKNtNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTS---DGEVKLIDFGLSAQLSDGKTR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPinkntEMNIQK-------NYVLSFKDYIWKSIssSA 2050
Cdd:cd05122   155 NTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYS-----ELPPMKalfliatNGPPGLRNPKKWSK--EF 227
                         250       260
                  ....*....|....*....|....*..
gi 124804138 2051 KDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd05122   228 KDFLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
1821-2076 3.86e-54

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: 190.54  E-value: 3.86e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEkELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd14185     2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKE-DMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILL---TDKSRdaQIKLTDFGLSTLCApnELL 1977
Cdd:cd14185    81 RGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhnPDKST--TLKLADFGLAKYVT--GPI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF--PINKNTEM-NIQKNYVLSFKDYIWKSISSSAKDLI 2054
Cdd:cd14185   157 FTVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFrsPERDQEELfQIIQLGHYEFLPPYWDNISEAAKDLI 236
                         250       260
                  ....*....|....*....|..
gi 124804138 2055 SKLLELNVEKRISANEALEHIW 2076
Cdd:cd14185   237 SRLLVVDPEKRYTAKQVLQHPW 258
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
1825-2077 8.97e-54

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: 189.65  E-value: 8.97e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVI-YL-KEIinTKETLYISMELVKG 1902
Cdd:cd06606     6 ELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVrYLgTER--TENTLNIFLEYVPG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1903 GELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPNEL---LKE 1979
Cdd:cd06606    84 GSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDS---DGVVKLADFGCAKRLAEIATgegTKS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 PCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPinkntemNIQKNYVLSFK-------DYIWKSISSSAKD 2052
Cdd:cd06606   161 LRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWS-------ELGNPVAALFKigssgepPPIPEHLSEEAKD 233
                         250       260
                  ....*....|....*....|....*
gi 124804138 2053 LISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd06606   234 FLRKCLQRDPKKRPTADELLQHPFL 258
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
1816-2079 1.09e-53

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: 189.82  E-value: 1.09e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1816 TLYNLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEkELLRSEISILRLLRHPNVIYLKEIINTKETLYI 1895
Cdd:cd14183     3 SISERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKE-HMIQNEVSILRRVKHPNIVLLIEEMDMPTELYL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1896 SMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQ-IKLTDFGLSTLCapN 1974
Cdd:cd14183    82 VMELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQDGSKsLKLGDFGLATVV--D 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1975 ELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYVLSFKDY---IWKSISSSAK 2051
Cdd:cd14183   160 GPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEVLFDQILMGQVDFpspYWDNVSDSAK 239
                         250       260
                  ....*....|....*....|....*...
gi 124804138 2052 DLISKLLELNVEKRISANEALEHIWVKN 2079
Cdd:cd14183   240 ELITMMLQVDVDQRYSALQVLEHPWVND 267
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
1820-2077 3.32e-53

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: 187.93  E-value: 3.32e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1820 LYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd14075     3 FYRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQKTQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRdaqIKLTDFGLSTLCAPNELLKE 1979
Cdd:cd14075    83 ASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNC---VKVGDFGFSTHAKRGETLNT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 PCGTLAYVAPEVITLQGY-NHKVDAWSIGIILYLLLSGKLPFPINKNTEMniqKNYVLSFKDYIWKSISSSAKDLISKLL 2058
Cdd:cd14075   160 FCGSPPYAAPELFKDEHYiGIYVDIWALGVLLYFMVTGVMPFRAETVAKL---KKCILEGTYTIPSYVSEPCQELIRGIL 236
                         250
                  ....*....|....*....
gi 124804138 2059 ELNVEKRISANEALEHIWV 2077
Cdd:cd14075   237 QPVPSDRYSIDEIKNSEWL 255
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
1821-2076 2.05e-52

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: 185.67  E-value: 2.05e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd14071     2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSrdaQIKLTDFGLSTLCAPNELLKEP 1980
Cdd:cd14071    82 SNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANM---NIKIADFGFSNFFKPGELLKTW 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 CGTLAYVAPEVITLQGYNH-KVDAWSIGIILYLLLSGKLPFpiNKNTeMNIQKNYVLSFKDYIWKSISSSAKDLISKLLE 2059
Cdd:cd14071   159 CGSPPYAAPEVFEGKEYEGpQLDIWSLGVVLYVLVCGALPF--DGST-LQTLRDRVLSGRFRIPFFMSTDCEHLIRRMLV 235
                         250
                  ....*....|....*..
gi 124804138 2060 LNVEKRISANEALEHIW 2076
Cdd:cd14071   236 LDPSKRLTIEQIKKHKW 252
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
1821-2077 2.47e-52

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: 185.61  E-value: 2.47e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELlRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd14088     3 YDLGQVIKTEEFCEIFRAKDKTTGKLYTCKKFLKRDGRKVRKAA-KNEINILKMVKHPNILQLVDVFETRKEYFIFLELA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLcaPNELLKEP 1980
Cdd:cd14088    82 TGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNRLKNSKIVISDFHLAKL--ENGLIKEP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF--PINKNTEMNIQKNYV-------LSFKDYIWKSISSSAK 2051
Cdd:cd14088   160 CGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFydEAEEDDYENHDKNLFrkilagdYEFDSPYWDDISQAAK 239
                         250       260
                  ....*....|....*....|....*.
gi 124804138 2052 DLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14088   240 DLVTRLMEVEQDQRITAEEAISHEWI 265
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
1821-2077 5.17e-52

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: 184.38  E-value: 5.17e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSiyEKEL--LRSEISILRLLRHPNVIYLKEIINTKETLYISME 1898
Cdd:cd14002     3 YHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKS--EKELrnLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKgGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLSTLCAPNEL-L 1977
Cdd:cd14002    81 YAQ-GELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIG---KGGVVKLCDFGFARAMSCNTLvL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINkntemNIQKNYVLSFKDYI-W-KSISSSAKDLIS 2055
Cdd:cd14002   157 TSIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTN-----SIYQLVQMIVKDPVkWpSNMSPEFKSFLQ 231
                         250       260
                  ....*....|....*....|..
gi 124804138 2056 KLLELNVEKRISANEALEHIWV 2077
Cdd:cd14002   232 GLLNKDPSKRLSWPDLLEHPFV 253
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
1819-2077 1.46e-51

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: 183.62  E-value: 1.46e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEI----SILRLLRHPNVIYLKEIINTKETLY 1894
Cdd:cd14196     5 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIerevSILRQVLHPNIITLHDVYENRTDVV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRD-AQIKLTDFGLSTLCAP 1973
Cdd:cd14196    85 LILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPiPHIKLIDFGLAHEIED 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1974 NELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF--PINKNTEMNIQK-NYvlSFKDYIWKSISSSA 2050
Cdd:cd14196   165 GVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlgDTKQETLANITAvSY--DFDEEFFSHTSELA 242
                         250       260
                  ....*....|....*....|....*..
gi 124804138 2051 KDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14196   243 KDFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
1821-2079 1.55e-51

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: 184.67  E-value: 1.55e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDK---RSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISM 1897
Cdd:cd14094     5 YELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVakfTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGG----ELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCAP 1973
Cdd:cd14094    85 EFMDGAdlcfEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1974 NELLKE-PCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNT--EMNIQKNYvlSFKDYIWKSISSSA 2050
Cdd:cd14094   165 SGLVAGgRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERlfEGIIKGKY--KMNPRQWSHISESA 242
                         250       260
                  ....*....|....*....|....*....
gi 124804138 2051 KDLISKLLELNVEKRISANEALEHIWVKN 2079
Cdd:cd14094   243 KDLVRRMLMLDPAERITVYEALNHPWIKE 271
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
1821-2077 4.49e-51

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: 181.82  E-value: 4.49e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIyEKEL--LRSEISILRLLRHPNVIYLKEIINTKETLYISME 1898
Cdd:cd14073     3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIED-EQDMvrIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRdaqIKLTDFGLSTLCAPNELLK 1978
Cdd:cd14073    82 YASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGN---AKIADFGLSNLYSKDKLLQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1979 EPCGTLAYVAPEVITLQGYNH-KVDAWSIGIILYLLLSGKLPFPINKNTEMNIQknyvLSFKDYIWKSISSSAKDLISKL 2057
Cdd:cd14073   159 TFCGSPLYASPEIVNGTPYQGpEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQ----ISSGDYREPTQPSDASGLIRWM 234
                         250       260
                  ....*....|....*....|
gi 124804138 2058 LELNVEKRISANEALEHIWV 2077
Cdd:cd14073   235 LTVNPKRRATIEDIANHWWV 254
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
1821-2076 6.63e-51

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: 180.89  E-value: 6.63e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdkRSVSIYEKELLRsEISILRLLR----HPNVIYLKEIINTKE--TLY 1894
Cdd:cd05118     1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKI--KNDFRHPKAALR-EIKLLKHLNdvegHPNIVKLLDVFEHRGgnHLC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVkGGELYDFL-LAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdKSRDAQIKLTDFGLSTLCAP 1973
Cdd:cd05118    78 LVFELM-GMNLYELIkDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILI--NLELGQLKLADFGLARSFTS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1974 NELLKEPCgTLAYVAPEVI-TLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNtemniqknyvlsfKDYIWKSI----SS 2048
Cdd:cd05118   155 PPYTPYVA-TRWYRAPEVLlGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSE-------------VDQLAKIVrllgTP 220
                         250       260
                  ....*....|....*....|....*...
gi 124804138 2049 SAKDLISKLLELNVEKRISANEALEHIW 2076
Cdd:cd05118   221 EALDLLSKMLKYDPAKRITASQALAHPY 248
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
1819-2077 1.25e-50

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: 180.99  E-value: 1.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKR----SVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLY 1894
Cdd:cd14194     5 DYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRrtksSRRGVSREDIEREVSILKEIQHPNVITLHEVYENKTDVI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKS-RDAQIKLTDFGLSTLCAP 1973
Cdd:cd14194    85 LILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNvPKPRIKIIDFGLAHKIDF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1974 NELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF--PINKNTEMNIQK-NYvlSFKDYIWKSISSSA 2050
Cdd:cd14194   165 GNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlgDTKQETLANVSAvNY--EFEDEYFSNTSALA 242
                         250       260
                  ....*....|....*....|....*..
gi 124804138 2051 KDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14194   243 KDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1820-2083 1.63e-50

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: 181.78  E-value: 1.63e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1820 LYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELlRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd14168    11 IFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKESSI-ENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCAPNELLKE 1979
Cdd:cd14168    90 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQDEESKIMISDFGLSKMEGKGDVMST 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 PCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNT---EMNIQKNYvlSFKDYIWKSISSSAKDLISK 2056
Cdd:cd14168   170 ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSklfEQILKADY--EFDSPYWDDISDSAKDFIRN 247
                         250       260
                  ....*....|....*....|....*..
gi 124804138 2057 LLELNVEKRISANEALEHIWVKNPTAV 2083
Cdd:cd14168   248 LMEKDPNKRYTCEQALRHPWIAGDTAL 274
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
1827-2065 4.35e-50

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: 178.50  E-value: 4.35e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKqtNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGELY 1906
Cdd:cd13999     1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1907 DFLL-AETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCA-PNELLKEPCGTL 1984
Cdd:cd13999    79 DLLHkKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDE---NFTVKIADFGLSRIKNsTTEKMTGVVGTP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1985 AYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPiNKNTEMNIQKNYVLSFKDYIWKSISSSAKDLISKLLELNVEK 2064
Cdd:cd13999   156 RWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFK-ELSPIQIAAAVVQKGLRPPIPPDCPPELSKLIKRCWNEDPEK 234

                  .
gi 124804138 2065 R 2065
Cdd:cd13999   235 R 235
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
1821-2073 5.04e-50

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 186.37  E-value: 5.04e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYE-KELLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEaRERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLSTLCAPNELLKE 1979
Cdd:COG0515    89 VEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLT---PDGRVKLIDFGIARALGGATLTQT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 --PCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEM--NIQKNYVLSFKDyIWKSISSSAKDLIS 2055
Cdd:COG0515   166 gtVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELlrAHLREPPPPPSE-LRPDLPPALDAIVL 244
                         250
                  ....*....|....*....
gi 124804138 2056 KLLELNVEKRI-SANEALE 2073
Cdd:COG0515   245 RALAKDPEERYqSAAELAA 263
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
1821-2077 9.85e-50

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: 177.71  E-value: 9.85e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd14072     2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCAPNELLKEP 1980
Cdd:cd14072    82 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLL---DADMNIKIADFGFSNEFTPGNKLDTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 CGTLAYVAPEVITLQGYNH-KVDAWSIGIILYLLLSGKLPFPINKNTEMniqKNYVLSFKDYIWKSISSSAKDLISKLLE 2059
Cdd:cd14072   159 CGSPPYAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPFDGQNLKEL---RERVLRGKYRIPFYMSTDCENLLKKFLV 235
                         250
                  ....*....|....*...
gi 124804138 2060 LNVEKRISANEALEHIWV 2077
Cdd:cd14072   236 LNPSKRGTLEQIMKDRWM 253
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
1821-2077 1.57e-49

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: 177.64  E-value: 1.57e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRS-------------EISILRLLRHPNVIYLKEII 1887
Cdd:cd14077     3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPRASNAGLKKEREKRlekeisrdirtirEAALSSLLNHPHICRLRDFL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1888 NTKETLYISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSrdaQIKLTDFGL 1967
Cdd:cd14077    83 RTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSG---NIKIIDFGL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1968 STLCAPNELLKEPCGTLAYVAPEVITLQGY-NHKVDAWSIGIILYLLLSGKLPFPiNKNTEM---NIQKNYVlsfkDYIw 2043
Cdd:cd14077   160 SNLYDPRRLLRTFCGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKVPFD-DENMPAlhaKIKKGKV----EYP- 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 124804138 2044 KSISSSAKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14077   234 SYLSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
1821-2077 3.66e-49

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: 176.26  E-value: 3.66e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd06627     2 YQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPNELLKE- 1979
Cdd:cd06627    82 ENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTK---DGLVKLADFGVATKLNEVEKDENs 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 PCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLP----------FPINKNTEMNIQKNyvlsfkdyiwksISSS 2049
Cdd:cd06627   159 VVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPyydlqpmaalFRIVQDDHPPLPEN------------ISPE 226
                         250       260
                  ....*....|....*....|....*...
gi 124804138 2050 AKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd06627   227 LRDFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
1819-2077 1.58e-48

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: 175.68  E-value: 1.58e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELH-EQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKeLLRsEISILRLLR-HPNVIYLKEIINTKETLYIS 1896
Cdd:cd14090     1 DLYKLTgELLGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRSR-VFR-EVETLHQCQgHPNILQLIEYFEDDERFYLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1897 MELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGL-------ST 1969
Cdd:cd14090    79 FEKMRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVSPVKICDFDLgsgiklsST 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1970 LCAP---NELLKePCGTLAYVAPEVITL-----QGYNHKVDAWSIGIILYLLLSGKLPFPINKNT--------------E 2027
Cdd:cd14090   159 SMTPvttPELLT-PVGSAEYMAPEVVDAfvgeaLSYDKRCDLWSLGVILYIMLCGYPPFYGRCGEdcgwdrgeacqdcqE 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 124804138 2028 M---NIQKNYvLSFKDYIWKSISSSAKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14090   238 LlfhSIQEGE-YEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPWV 289
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
1821-2076 2.80e-48

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: 174.01  E-value: 2.80e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQ-LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLrseisiLRLLRHPNVIYLKEII-NT---KETLYI 1895
Cdd:cd14089     2 YTISKQvLGLGINGKVLECFHKKTGEKFALKVLRDNPKARREVELH------WRASGCPHIVRIIDVYeNTyqgRKCLLV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1896 SMELVKGGELYDFL--LAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCAP 1973
Cdd:cd14089    76 VMECMEGGELFSRIqeRADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAILKLTDFGFAKETTT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1974 NELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF------PINKNTEMNIqKNYVLSFKDYIWKSIS 2047
Cdd:cd14089   156 KKSLQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFysnhglAISPGMKKRI-RNGQYEFPNPEWSNVS 234
                         250       260
                  ....*....|....*....|....*....
gi 124804138 2048 SSAKDLISKLLELNVEKRISANEALEHIW 2076
Cdd:cd14089   235 EEAKDLIRGLLKTDPSERLTIEEVMNHPW 263
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
1827-2076 2.81e-48

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: 173.95  E-value: 2.81e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIY-EKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGEL 1905
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTrQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1906 YDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRdaqIKLTDFGLSTLCAPNELLKEPCGTLA 1985
Cdd:cd05572    81 WTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGY---VKLVDFGFAKKLGSGRKTWTFCGTPE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1986 YVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNI-----QKNYVLSFKDYiwksISSSAKDLISKLLEL 2060
Cdd:cd05572   158 YVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDPMKIyniilKGIDKIEFPKY----IDKNAKNLIKQLLRR 233
                         250       260
                  ....*....|....*....|.
gi 124804138 2061 NVEKRI-----SANEALEHIW 2076
Cdd:cd05572   234 NPEERLgylkgGIRDIKKHKW 254
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
1821-2078 3.82e-48

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: 174.04  E-value: 3.82e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEI----SILRLLRHPNVIYLKEIINTKETLYIS 1896
Cdd:cd14195     7 YEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSRRGVSREEIerevNILREIQHPNIITLHDIFENKTDVVLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1897 MELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSR-DAQIKLTDFGLSTLCAPNE 1975
Cdd:cd14195    87 LELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVpNPRIKLIDFGIAHKIEAGN 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1976 LLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF--PINKNTEMNIQK-NYvlSFKDYIWKSISSSAKD 2052
Cdd:cd14195   167 EFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlgETKQETLTNISAvNY--DFDEEYFSNTSELAKD 244
                         250       260
                  ....*....|....*....|....*.
gi 124804138 2053 LISKLLELNVEKRISANEALEHIWVK 2078
Cdd:cd14195   245 FIRRLLVKDPKKRMTIAQSLEHSWIK 270
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
1821-2077 5.19e-48

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: 173.08  E-value: 5.19e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSV--SIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISME 1898
Cdd:cd14070     4 YLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAkkDSYVTKNLRREGRIQQMIRHPNITQLLDILETENSYYLVME 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTlCAPNELLK 1978
Cdd:cd14070    84 LCPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDE---NDNIKLIDFGLSN-CAGILGYS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1979 EP----CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYVLSFKDYIWKSISSSAKDLI 2054
Cdd:cd14070   160 DPfstqCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEPFSLRALHQKMVDKEMNPLPTDLSPGAISFL 239
                         250       260
                  ....*....|....*....|...
gi 124804138 2055 SKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14070   240 RSLLEPDPLKRPNIKQALANRWL 262
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
1821-2077 6.41e-48

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: 172.87  E-value: 6.41e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVS-IYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd14162     2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPeDYLQKFLPREIEVIKGLKHPNLICFYEAIETTSRVYIIMEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtDKsrDAQIKLTDFG-----LSTLCAPN 1974
Cdd:cd14162    82 AENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLL-DK--NNNLKITDFGfargvMKTKDGKP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1975 ELLKEPCGTLAYVAPEVITLQGYN-HKVDAWSIGIILYLLLSGKLPFP-INKNTEMN-IQKNYVLSFKdyiwKSISSSAK 2051
Cdd:cd14162   159 KLSETYCGSYAYASPEILRGIPYDpFLSDIWSMGVVLYTMVYGRLPFDdSNLKVLLKqVQRRVVFPKN----PTVSEECK 234
                         250       260
                  ....*....|....*....|....*.
gi 124804138 2052 DLISKLLELnVEKRISANEALEHIWV 2077
Cdd:cd14162   235 DLILRMLSP-VKKRITIEEIKRDPWF 259
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
1818-2077 1.25e-47

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: 172.00  E-value: 1.25e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1818 YNLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSiyEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISM 1897
Cdd:cd14114     1 YDHYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHES--DKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLIL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGGELYDFLLAE-TRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsRDAQIKLTDFGLSTLCAPNEL 1976
Cdd:cd14114    79 EFLSGGELFERIAAEhYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTK-RSNEVKLIDFGLATHLDPKES 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1977 LKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTE-MNIQKNYVLSFKDYIWKSISSSAKDLIS 2055
Cdd:cd14114   158 VKVTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDEtLRNVKSCDWNFDDSAFSGISEEAKDFIR 237
                         250       260
                  ....*....|....*....|..
gi 124804138 2056 KLLELNVEKRISANEALEHIWV 2077
Cdd:cd14114   238 KLLLADPNKRMTIHQALEHPWL 259
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
1821-2077 3.46e-47

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: 171.13  E-value: 3.46e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNS-----EFAIKVIDKRSVSIYEKEL-LRSEISILRLLRHPNVIYLKEIINTKETLY 1894
Cdd:cd14076     3 YILGRTLGEGEFGKVKLGWPLPKANhrsgvQVAIKLIRRDTQQENCQTSkIMREINILKGLTHPNIVRLLDVLKTKKYIG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtDKSRDaqIKLTDFGLSTLCAPN 1974
Cdd:cd14076    83 IVLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLL-DKNRN--LVITDFGFANTFDHF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1975 --ELLKEPCGTLAYVAPEVITLQGYNH--KVDAWSIGIILYLLLSGKLPF---PINKNTEmNIQKNY------VLSFKDY 2041
Cdd:cd14076   160 ngDLMSTSCGSPCYAAPELVVSDSMYAgrKADIWSCGVILYAMLAGYLPFdddPHNPNGD-NVPRLYryicntPLIFPEY 238
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 124804138 2042 iwksISSSAKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14076   239 ----VTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
1821-2076 5.93e-47

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: 170.74  E-value: 5.93e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdkrsVSIYEKE-----LLRsEISILRLLRHPNVIYLKEIINTKETLYI 1895
Cdd:cd07829     1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKI----RLDNEEEgipstALR-EISLLKELKHPNIVKLLDVIHTENKLYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1896 SMELVkggE--LYDFL-LAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLSTLCA 1972
Cdd:cd07829    76 VFEYC---DqdLKKYLdKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLIN---RDGVLKLADFGLARAFG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1973 -PNELLKEPCGTLAYVAPEVitLQG---YNHKVDAWSIGIILYLLLSGKLPFP-----------------INKNTEMNIQ 2031
Cdd:cd07829   150 iPLRTYTHEVVTLWYRAPEI--LLGskhYSTAVDIWSVGCIFAELITGKPLFPgdseidqlfkifqilgtPTEESWPGVT 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 124804138 2032 K--NYVLSFKDY-------IWKSISSSAKDLISKLLELNVEKRISANEALEHIW 2076
Cdd:cd07829   228 KlpDYKPTFPKWpkndlekVLPRLDPEGIDLLSKMLQYNPAKRISAKEALKHPY 281
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
1821-2075 1.18e-46

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: 169.18  E-value: 1.18e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd08215     2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLA----ETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRdaqIKLTDFGLS-TLCAPNE 1975
Cdd:cd08215    82 DGGDLAQKIKKqkkkGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGV---VKLGDFGISkVLESTTD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1976 LLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFP-------INKNTEMNIQKnyvlsfkdyIWKSISS 2048
Cdd:cd08215   159 LAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEannlpalVYKIVKGQYPP---------IPSQYSS 229
                         250       260
                  ....*....|....*....|....*..
gi 124804138 2049 SAKDLISKLLELNVEKRISANEALEHI 2075
Cdd:cd08215   230 ELRDLVNSMLQKDPEKRPSANEILSSP 256
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
1827-2077 2.70e-46

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: 168.25  E-value: 2.70e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTV--YRGINKQTNSEFAIKVIDKRSVSIYEK---ELLRSEISILRLLRHPNVI-YLKEIINTKETLYISMELV 1900
Cdd:cd13994     1 IGKGATSVVriVTKKNPRSGVLYAVKEYRRRDDESKRKdyvKRLTSEYIISSKLHHPNIVkVLDLCQDLHGKWCLVMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLST-LCAPNELL-- 1977
Cdd:cd13994    81 PGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDE---DGVLKLTDFGTAEvFGMPAEKEsp 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 --KEPCGTLAYVAPEVITLQGYNHK-VDAWSIGIILYLLLSGKLPFPINKNTEmNIQKNYVLSFKDYIWK------SISS 2048
Cdd:cd13994   158 msAGLCGSEPYMAPEVFTSGSYDGRaVDVWSCGIVLFALFTGRFPWRSAKKSD-SAYKAYEKSGDFTNGPyepienLLPS 236
                         250       260
                  ....*....|....*....|....*....
gi 124804138 2049 SAKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd13994   237 ECRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
1821-2077 5.22e-46

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: 167.09  E-value: 5.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKR-SVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKE-TLYISME 1898
Cdd:cd14163     2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSgGPEEFIQRFLPRELQIVERLDHKNIIHVYEMLESADgKIYLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSrdaqIKLTDFGLSTLCAPN--EL 1976
Cdd:cd14163    82 LAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGFT----LKLTDFGFAKQLPKGgrEL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1977 LKEPCGTLAYVAPEVitLQGYNH---KVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYVLSFKDYIwkSISSSAKDL 2053
Cdd:cd14163   158 SQTFCGSTAYAAPEV--LQGVPHdsrKGDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQQQKGVSLPGHL--GVSRTCQDL 233
                         250       260
                  ....*....|....*....|....
gi 124804138 2054 ISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14163   234 LKRLLEPDMVLRPSIEEVSWHPWL 257
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
1821-2070 5.28e-46

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: 167.78  E-value: 5.28e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKR---------SVSIyEKEllrseisILRLLRHPNVIYLKEIINTKE 1891
Cdd:cd05581     3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRhiikekkvkYVTI-EKE-------VLSRLAHPGIVKLYYTFQDES 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1892 TLYISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRdaqIKLTDFGLSTLC 1971
Cdd:cd05581    75 KLYFVLEYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMH---IKITDFGTAKVL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1972 APNELLKEP------------------CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpiNKNTEMNIQKN 2033
Cdd:cd05581   152 GPDSSPESTkgdadsqiaynqaraasfVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPF--RGSNEYLTFQK 229
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 124804138 2034 YV-LSFKdyIWKSISSSAKDLISKLLELNVEKRISANE 2070
Cdd:cd05581   230 IVkLEYE--FPENFPPDAKDLIQKLLVLDPSKRLGVNE 265
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
1821-2077 2.71e-45

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: 165.10  E-value: 2.71e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYE----KELLRSEISILRL---LRHPNVIYLKEIINTKETL 1893
Cdd:cd14005     2 YEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTEWAmingPVPVPLEIALLLKaskPGVPGVIRLLDWYERPDGF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1894 YISMELVKGGE-LYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdkSRDAQIKLTDFGlstlCA 1972
Cdd:cd14005    82 LLIMERPEPCQdLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLIN--LRTGEVKLIDFG----CG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1973 pnELLK-----EPCGTLAYVAPEVITLQGYNHK-VDAWSIGIILYLLLSGKLPFpinkNTEMNIQKNYVlsfkdYIWKSI 2046
Cdd:cd14005   156 --ALLKdsvytDFDGTRVYSPPEWIRHGRYHGRpATVWSLGILLYDMLCGDIPF----ENDEQILRGNV-----LFRPRL 224
                         250       260       270
                  ....*....|....*....|....*....|.
gi 124804138 2047 SSSAKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14005   225 SKECCDLISRCLQFDPSKRPSLEQILSHPWF 255
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
1821-2077 3.35e-45

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: 165.09  E-value: 3.35e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELH--EQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSiyEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISME 1898
Cdd:cd14190     4 FSIHskEVLGGGKFGKVHTCTEKRTGLKLAAKVINKQNSK--DKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFLLAET-RLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSrDAQIKLTDFGLSTLCAPNELL 1977
Cdd:cd14190    82 YVEGGELFERIVDEDyHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRT-GHQVKIIDFGLARRYNPREKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEmniQKNYVLS----FKDYIWKSISSSAKDL 2053
Cdd:cd14190   161 KVNFGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTE---TLNNVLMgnwyFDEETFEHVSDEAKDF 237
                         250       260
                  ....*....|....*....|....
gi 124804138 2054 ISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14190   238 VSNLIIKERSARMSATQCLKHPWL 261
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
1819-2077 3.48e-45

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: 164.79  E-value: 3.48e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdkRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISME 1898
Cdd:cd14191     2 DFYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFF--KAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFLLAET-RLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSrDAQIKLTDFGLSTLCAPNELL 1977
Cdd:cd14191    80 MVSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKT-GTKIKLIDFGLARRLENAGSL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF-PINKNTEMNIQKNYVLSFKDYIWKSISSSAKDLISK 2056
Cdd:cd14191   159 KVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFmGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISN 238
                         250       260
                  ....*....|....*....|.
gi 124804138 2057 LLELNVEKRISANEALEHIWV 2077
Cdd:cd14191   239 LLKKDMKARLTCTQCLQHPWL 259
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
1825-2074 5.58e-45

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: 164.00  E-value: 5.58e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSEF-AIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGG 1903
Cdd:cd14121     1 EKLGSGTYATVYKAYRKSGAREVvAVKCVSKSSLNKASTENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 ELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdKSRDAQIKLTDFGLSTLCAPNELLKEPCGT 1983
Cdd:cd14121    81 DLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLS-SRYNPVLKLADFGFAQHLKPNDEAHSLRGS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1984 LAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPIN--KNTEMNIQKNYVLSFKDYIwkSISSSAKDLISKLLELN 2061
Cdd:cd14121   160 PLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRsfEELEEKIRSSKPIEIPTRP--ELSADCRDLLLRLLQRD 237
                         250
                  ....*....|...
gi 124804138 2062 VEKRISANEALEH 2074
Cdd:cd14121   238 PDRRISFEEFFAH 250
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
1821-2076 6.21e-45

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: 164.18  E-value: 6.21e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVS--IYEKELLRsEISILRLLRHPNVIYLKEIINTKE-TLYISM 1897
Cdd:cd14165     3 YILGINLGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPddFVEKFLPR-ELEILARLNHKSIIKTYEIFETSDgKVYIVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtDKsrDAQIKLTDFGLSTLCAPNE-- 1975
Cdd:cd14165    82 ELGVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLL-DK--DFNIKLTDFGFSKRCLRDEng 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1976 ---LLKEPCGTLAYVAPEVITLQGYNHKV-DAWSIGIILYLLLSGKLPFPINKNTEM-NIQKNYVLSFKDYiwKSISSSA 2050
Cdd:cd14165   159 rivLSKTFCGSAAYAAPEVLQGIPYDPRIyDIWSLGVILYIMVCGSMPYDDSNVKKMlKIQKEHRVRFPRS--KNLTSEC 236
                         250       260
                  ....*....|....*....|....*.
gi 124804138 2051 KDLISKLLELNVEKRISANEALEHIW 2076
Cdd:cd14165   237 KDLIYRLLQPDVSQRLCIDEVLSHPW 262
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
1820-2074 9.83e-45

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: 163.54  E-value: 9.83e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1820 LYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSiyeKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd06614     1 LYKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQN---KELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFL-LAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLST-LCAPNELL 1977
Cdd:cd06614    78 MDGGSLTDIItQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILL---SKDGSVKLADFGFAAqLTKEKSKR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpINKNTEMN---IQKNYVLSFKDYiwKSISSSAKDLI 2054
Cdd:cd06614   155 NSVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPY-LEEPPLRAlflITTKGIPPLKNP--EKWSPEFKDFL 231
                         250       260
                  ....*....|....*....|
gi 124804138 2055 SKLLELNVEKRISANEALEH 2074
Cdd:cd06614   232 NKCLVKDPEKRPSAEELLQH 251
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
1819-2079 1.05e-44

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: 163.95  E-value: 1.05e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSvSIYEKELLRSEISILRLLRHPNVI-----YLKeiiNTKetL 1893
Cdd:cd06609     1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEE-AEDEIEDIQQEIQFLSQCDSPYITkyygsFLK---GSK--L 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1894 YISMELVKGGELYDfLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLS----- 1968
Cdd:cd06609    75 WIIMEYCGGGSVLD-LLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSE---EGDVKLADFGVSgqlts 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1969 TLCAPNELLkepcGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLP----------FPINKNTEMNIQKNyvlsf 2038
Cdd:cd06609   151 TMSKRNTFV----GTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPlsdlhpmrvlFLIPKNNPPSLEGN----- 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 124804138 2039 kdyiwkSISSSAKDLISKLLELNVEKRISANEALEHIWVKN 2079
Cdd:cd06609   222 ------KFSKPFKDFVELCLNKDPKERPSAKELLKHKFIKK 256
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
1821-2077 1.10e-44

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: 163.59  E-value: 1.10e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKE-LLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd14116     7 FEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEhQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLStLCAPNELLKE 1979
Cdd:cd14116    87 APLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLL---GSAGELKIADFGWS-VHAPSSRRTT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 PCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYV-LSFKDYiwksISSSAKDLISKLL 2058
Cdd:cd14116   163 LCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVeFTFPDF----VTEGARDLISRLL 238
                         250
                  ....*....|....*....
gi 124804138 2059 ELNVEKRISANEALEHIWV 2077
Cdd:cd14116   239 KHNPSQRPMLREVLEHPWI 257
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
1826-2079 2.07e-44

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: 162.76  E-value: 2.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1826 QLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGEL 1905
Cdd:cd06623     8 VLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEEFRKQLLR-ELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDGGSL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1906 YDFLLAETRLSEIHANKIITQLIKTVAYLHRC-GIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCAPNellKEPC--- 1981
Cdd:cd06623    87 ADLLKKVGKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLI---NSKGEVKIADFGISKVLENT---LDQCntf 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1982 -GTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYVLSFKDYIWKS--ISSSAKDLISKLL 2058
Cdd:cd06623   161 vGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFELMQAICDGPPPSLPAeeFSPEFRDFISACL 240
                         250       260
                  ....*....|....*....|.
gi 124804138 2059 ELNVEKRISANEALEHIWVKN 2079
Cdd:cd06623   241 QKDPKKRPSAAELLQHPFIKK 261
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
1817-2077 2.43e-44

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: 162.78  E-value: 2.43e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1817 LYNLYEL-HEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLR-HPNVIYLKEIINTKETLY 1894
Cdd:cd14198     5 FNNFYILtSKELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEILHEIAVLELAKsNPRVVNLHEVYETTSEII 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVKGGELYDFLLAE--TRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCA 1972
Cdd:cd14198    85 LILEYAAGGEIFNLCVPDlaEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPLGDIKIVDFGMSRKIG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1973 PNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF--PINKNTEMNIQKNYVlSFKDYIWKSISSSA 2050
Cdd:cd14198   165 HACELREIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFvgEDNQETFLNISQVNV-DYSEETFSSVSQLA 243
                         250       260
                  ....*....|....*....|....*..
gi 124804138 2051 KDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14198   244 TDFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
1827-2074 2.69e-44

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: 162.15  E-value: 2.69e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQ-TNSEFAIKVIDKRSVSiYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGEL 1905
Cdd:cd14120     1 IGHGAFAVVFKGRHRKkPDLPVAIKCITKKNLS-KSQNLLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1906 YDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSR------DAQIKLTDFGLSTLCAPNELLKE 1979
Cdd:cd14120    80 ADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGrkpspnDIRLKIADFGFARFLQDGMMAAT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 PCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNI--QKNYVLsfKDYIWKSISSSAKDLISKL 2057
Cdd:cd14120   160 LCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELKAfyEKNANL--RPNIPSGTSPALKDLLLGL 237
                         250
                  ....*....|....*..
gi 124804138 2058 LELNVEKRISANEALEH 2074
Cdd:cd14120   238 LKRNPKDRIDFEDFFSH 254
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
1817-2077 3.05e-44

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: 162.05  E-value: 3.05e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1817 LYNLYELHEQLGQGKFSTVYRGINKQtNSEFAIKVIDKRSVSiYEKELL--RSEISILRLLRHPNVIYLKEIINTKETLY 1894
Cdd:cd14161     1 LKHRYEFLETLGKGTYGRVKKARDSS-GRLVAIKSIRKDRIK-DEQDLLhiRREIEIMSSLNHPHIISVYEVFENSSKIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCAPN 1974
Cdd:cd14161    79 IVMEYASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILL---DANGNIKIADFGLSNLYNQD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1975 ELLKEPCGTLAYVAPEVITLQGY-NHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQknyvLSFKDYIWKSISSSAKDL 2053
Cdd:cd14161   156 KFLQTYCGSPLYASPEIVNGRPYiGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQ----ISSGAYREPTKPSDACGL 231
                         250       260
                  ....*....|....*....|....
gi 124804138 2054 ISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14161   232 IRWLLMVNPERRATLEDVASHWWV 255
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
1828-2077 3.26e-44

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: 162.47  E-value: 3.26e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1828 GQGKFSTVYRGINKQTNSEFAIKVI---DKRSVSIyekELLRSEISILRLLRHPNVI--YLKEIinTKETLYISMELVKG 1902
Cdd:cd06626     9 GEGTFGKVYTAVNLDTGELMAMKEIrfqDNDPKTI---KEIADEMKVLEGLDHPNLVryYGVEV--HREEVYIFMEYCQE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1903 GELYDfLLAETR-LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSrdaQIKLTDFGLSTLCAPNELLKEP- 1980
Cdd:cd06626    84 GTLEE-LLRHGRiLDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNG---LIKLGDFGSAVKLKNNTTTMAPg 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 -----CGTLAYVAPEVITLQ---GYNHKVDAWSIGIILYLLLSGKLPFPinkntemNIQKNYVLSFK----------DYI 2042
Cdd:cd06626   160 evnslVGTPAYMAPEVITGNkgeGHGRAADIWSLGCVVLEMATGKRPWS-------ELDNEWAIMYHvgmghkppipDSL 232
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 124804138 2043 wkSISSSAKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd06626   233 --QLSPEGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
1824-2077 4.77e-44

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: 161.67  E-value: 4.77e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1824 HEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSiyEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGG 1903
Cdd:cd14192     9 HEVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAK--EREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 ELYDFLLAET-RLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDaQIKLTDFGLSTLCAPNELLKEPCG 1982
Cdd:cd14192    87 ELFDRITDESyQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNSTGN-QIKIIDFGLARRYKPREKLKVNFG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1983 TLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTE-MNIQKNYVLSFKDYIWKSISSSAKDLISKLLELN 2061
Cdd:cd14192   166 TPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAEtMNNIVNCKWDFDAEAFENLSEEAKDFISRLLVKE 245
                         250
                  ....*....|....*.
gi 124804138 2062 VEKRISANEALEHIWV 2077
Cdd:cd14192   246 KSCRMSATQCLKHEWL 261
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
1821-2104 8.49e-44

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: 163.47  E-value: 8.49e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVI-DKRSVSIYEKELLRsEISILRLLRHPNVIYLKEII-----NTKETLY 1894
Cdd:cd07834     2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKIsNVFDDLIDAKRILR-EIKILRHLKHENIIGLLDILrppspEEFNDVY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELvKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPN 1974
Cdd:cd07834    81 IVTEL-METDLHKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNS---NCDLKICDFGLARGVDPD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1975 EL---LKEPCGTLAYVAPEVI-TLQGYNHKVDAWSIGIILYLLLSGKLPFP-------INKNTEM-------NIQ----- 2031
Cdd:cd07834   157 EDkgfLTEYVVTRWYRAPELLlSSKKYTKAIDIWSVGCIFAELLTRKPLFPgrdyidqLNLIVEVlgtpseeDLKfisse 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 2032 --KNYVLSFKDY-------IWKSISSSAKDLISKLLELNVEKRISANEALEHIWVK-------NPTAVINENSFIYKNEE 2095
Cdd:cd07834   237 kaRNYLKSLPKKpkkplseVFPGASPEAIDLLEKMLVFNPKKRITADEALAHPYLAqlhdpedEPVAKPPFDFPFFDDEE 316

                  ....*....
gi 124804138 2096 INILNLQDV 2104
Cdd:cd07834   317 LTIEELKEL 325
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
1826-2077 1.28e-43

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: 160.87  E-value: 1.28e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1826 QLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLR-HPNVIYLKEIINTKETLYISMELVKGGE 1904
Cdd:cd14197    16 ELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRMEIIHEIAVLELAQaNPWVINLHEVYETASEMILVLEYAAGGE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAETR--LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCAPNELLKEPCG 1982
Cdd:cd14197    96 IFNQCVADREeaFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLGDIKIVDFGLSRILKNSEELREIMG 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1983 TLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTE--MNI-QKNYVLSFKDYiwKSISSSAKDLISKLLE 2059
Cdd:cd14197   176 TPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQEtfLNIsQMNVSYSEEEF--EHLSESAIDFIKTLLI 253
                         250
                  ....*....|....*...
gi 124804138 2060 LNVEKRISANEALEHIWV 2077
Cdd:cd14197   254 KKPENRATAEDCLKHPWL 271
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
1819-2078 2.72e-43

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: 160.58  E-value: 2.72e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYEL-HEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSvSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISM 1897
Cdd:cd14174     1 DLYRLtDELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNA-GHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFG------LSTLC 1971
Cdd:cd14174    80 EKLRGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVSPVKICDFDlgsgvkLNSAC 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1972 AP--NELLKEPCGTLAYVAPEVITL-----QGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYV--------- 2035
Cdd:cd14174   160 TPitTPELTTPCGSAEYMAPEVVEVftdeaTFYDKRCDLWSLGVILYIMLSGYPPFVGHCGTDCGWDRGEVcrvcqnklf 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 124804138 2036 -------LSFKDYIWKSISSSAKDLISKLLELNVEKRISANEALEHIWVK 2078
Cdd:cd14174   240 esiqegkYEFPDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
1815-2077 4.05e-43

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: 158.92  E-value: 4.05e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1815 NTLYNLYElHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSiyEKELLRSEISILRLLRHPNVIYLKEIINTKETLY 1894
Cdd:cd14193     1 NSYYNVNK-EEILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQK--EKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVKGGELYDFLLAET-RLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdkSRDA-QIKLTDFGLSTLCA 1972
Cdd:cd14193    78 LVMEYVDGGELFDRIIDENyNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCV--SREAnQVKIIDFGLARRYK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1973 PNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF-PINKNTEMNIQKNYVLSFKDYIWKSISSSAK 2051
Cdd:cd14193   156 PREKLRVNFGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFlGEDDNETLNNILACQWDFEDEEFADISEEAK 235
                         250       260
                  ....*....|....*....|....*.
gi 124804138 2052 DLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14193   236 DFISKLLIKEKSWRMSASEALKHPWL 261
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
1827-2074 4.16e-43

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: 159.41  E-value: 4.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQT-NSEFAIKVIDKRSVSiYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGEL 1905
Cdd:cd14202    10 IGHGAFAVVFKGRHKEKhDLEVAVKCINKKNLA-KSQTLLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNGGDL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1906 YDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKS------RDAQIKLTDFGLSTLCAPNELLKE 1979
Cdd:cd14202    89 ADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpNNIRIKIADFGFARYLQNNMMAAT 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 PCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNI--QKNYVLSfkDYIWKSISSSAKDLISKL 2057
Cdd:cd14202   169 LCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLRLfyEKNKSLS--PNIPRETSSHLRQLLLGL 246
                         250
                  ....*....|....*..
gi 124804138 2058 LELNVEKRISANEALEH 2074
Cdd:cd14202   247 LQRNQKDRMDFDEFFHH 263
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
1819-2077 6.59e-43

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: 159.42  E-value: 6.59e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELHEQ-LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEIsILRLLRHPNVIYLKEIINTKETLYISM 1897
Cdd:cd14173     1 DVYQLQEEvLGEGAYARVQTCINLITNKEYAVKIIEKRPGHSRSRVFREVEM-LYQCQGHRNVLELIEFFEEEDKFYLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFG------LSTLC 1971
Cdd:cd14173    80 EKMRGGSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVSPVKICDFDlgsgikLNSDC 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1972 AP---NELLKePCGTLAYVAPEVITLQG-----YNHKVDAWSIGIILYLLLSGKLPF----------------PINKNTE 2027
Cdd:cd14173   160 SPistPELLT-PCGSAEYMAPEVVEAFNeeasiYDKRCDLWSLGVILYIMLSGYPPFvgrcgsdcgwdrgeacPACQNML 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 124804138 2028 MNIQKNYVLSFKDYIWKSISSSAKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14173   239 FESIQEGKYEFPEKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
1821-2076 7.37e-43

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: 158.19  E-value: 7.37e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSvsIYEKELLRS---EISILRLLRHPNVIYLKEIINTKETLYISM 1897
Cdd:cd05578     2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQK--CIEKDSVRNvlnELEILQELEHPFLVNLWYSFQDEEDMYMVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLCAPNELL 1977
Cdd:cd05578    80 DLLLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQ---GHVHITDFNIATKLTDGTLA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYVLSFKDYIWKSISSSAKDLISKL 2057
Cdd:cd05578   157 TSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRTSIEEIRAKFETASVLYPAGWSEEAIDLINKL 236
                         250       260
                  ....*....|....*....|
gi 124804138 2058 LELNVEKRISANEAL-EHIW 2076
Cdd:cd05578   237 LERDPQKRLGDLSDLkNHPY 256
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
1821-2076 9.03e-43

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: 158.01  E-value: 9.03e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDkRSVSIYEKelLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd14662     2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIE-RGLKIDEN--VQREIINHRSLRHPNIIRFKEVVLTPTHLAIVMEYA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtDKSRDAQIKLTDFGLSTLCAPNELLKEP 1980
Cdd:cd14662    79 AGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLL-DGSPAPRLKICDFGYSKSSVLHSQPKST 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 CGTLAYVAPEVITLQGYNHKV-DAWSIGIILYLLLSGKLPF-----PinKNTEMNIQKNYVLSFK--DYIwkSISSSAKD 2052
Cdd:cd14662   158 VGTPAYIAPEVLSRKEYDGKVaDVWSCGVTLYVMLVGAYPFedpddP--KNFRKTIQRIMSVQYKipDYV--RVSQDCRH 233
                         250       260
                  ....*....|....*....|....
gi 124804138 2053 LISKLLELNVEKRISANEALEHIW 2076
Cdd:cd14662   234 LLSRIFVANPAKRITIPEIKNHPW 257
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
1821-2065 1.47e-42

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: 158.51  E-value: 1.47e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVsIYEKEL--LRSEISILRLLRHPNVIYLKEIINTKETLYISME 1898
Cdd:cd05580     3 FEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKI-IKLKQVehVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLS--------TL 1970
Cdd:cd05580    82 YVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLL---DSDGHIKITDFGFAkrvkdrtyTL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1971 capnellkepCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpiNKNTEMNIQKNyVLSFKDYIWKSISSSA 2050
Cdd:cd05580   159 ----------CGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPF--FDENPMKIYEK-ILEGKIRFPSFFDPDA 225
                         250
                  ....*....|....*
gi 124804138 2051 KDLISKLLELNVEKR 2065
Cdd:cd05580   226 KDLIKRLLVVDLTKR 240
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
1821-2078 1.70e-42

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: 157.72  E-value: 1.70e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVsiyEKE----LLRSEISILRLLRHPNVIYLKEIINTKETLYIS 1896
Cdd:cd14117     8 FDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQI---EKEgvehQLRREIEIQSHLRHPNILRLYNYFHDRKRIYLI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1897 MELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLStLCAPNEL 1976
Cdd:cd14117    85 LEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYK---GELKIADFGWS-VHAPSLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1977 LKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYV-LSFKdyiwKSISSSAKDLIS 2055
Cdd:cd14117   161 RRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVdLKFP----PFLSDGSRDLIS 236
                         250       260
                  ....*....|....*....|...
gi 124804138 2056 KLLELNVEKRISANEALEHIWVK 2078
Cdd:cd14117   237 KLLRYHPSERLPLKGVMEHPWVK 259
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1827-2079 5.64e-42

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: 156.01  E-value: 5.64e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVY--RGI-NKQTNSEFAIKVIDKRSVSIYEK--ELLRSEISILRLLRH-PNVIYLKEIINTKETLYISMELV 1900
Cdd:cd05583     2 LGTGAYGKVFlvRKVgGHDAGKLYAMKVLKKATIVQKAKtaEHTMTERQVLEAVRQsPFLVTLHYAFQTDAKLHLILDYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCAPNELLK-- 1978
Cdd:cd05583    82 NGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILL---DSEGHVVLTDFGLSKEFLPGENDRay 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1979 EPCGTLAYVAPEVIT--LQGYNHKVDAWSIGIILYLLLSGKLPFPIN--KNTEMNIQKNyVLSFKDYIWKSISSSAKDLI 2054
Cdd:cd05583   159 SFCGTIEYMAPEVVRggSDGHDKAVDWWSLGVLTYELLTGASPFTVDgeRNSQSEISKR-ILKSHPPIPKTFSAEAKDFI 237
                         250       260       270
                  ....*....|....*....|....*....|
gi 124804138 2055 SKLLELNVEKRISAN-----EALEHIWVKN 2079
Cdd:cd05583   238 LKLLEKDPKKRLGAGprgahEIKEHPFFKG 267
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
1821-2076 5.76e-42

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: 156.54  E-value: 5.76e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd07830     1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKKKFYSWEECMNLREVKSLRKLNEHPNIVKLKEVFRENDELYFVFEYM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KgGELYDFLLAETR--LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRdaqIKLTDFGLStlcapNELLK 1978
Cdd:cd07830    81 E-GNLYQLMKDRKGkpFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEV---VKIADFGLA-----REIRS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1979 EPCGTlAYV------APEVITLQG-YNHKVDAWSIGIILYLLLSGKLPFP-------INKNTE----------------- 2027
Cdd:cd07830   152 RPPYT-DYVstrwyrAPEILLRSTsYSSPVDIWALGCIMAELYTLRPLFPgsseidqLYKICSvlgtptkqdwpegykla 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 124804138 2028 --MNIQ--KNYVLSFKDYIwKSISSSAKDLISKLLELNVEKRISANEALEHIW 2076
Cdd:cd07830   231 skLGFRfpQFAPTSLHQLI-PNASPEAIDLIKDMLRWDPKKRPTASQALQHPY 282
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
1825-2079 6.59e-42

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: 157.40  E-value: 6.59e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVsIYEKELLR--SEISILRLLRHPNVIYLKEIINTKETLYISMELVKG 1902
Cdd:cd05574     7 KLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEM-IKRNKVKRvlTEREILATLDHPFLPTLYASFQTSTHLCFVMDYCPG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1903 GELYDFL--LAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLSTLCA-------- 1972
Cdd:cd05574    86 GELFRLLqkQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLH---ESGHIMLTDFDLSKQSSvtpppvrk 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1973 --------------PNELLKEP--------CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF--PINKNTEM 2028
Cdd:cd05574   163 slrkgsrrssvksiEKETFVAEpsarsnsfVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFkgSNRDETFS 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 124804138 2029 NIQKNYVlSFKDYIwkSISSSAKDLISKLLELNVEKRI----SANEALEHIWVKN 2079
Cdd:cd05574   243 NILKKEL-TFPESP--PVSSEAKDLIRKLLVKDPSKRLgskrGASEIKRHPFFRG 294
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
1821-2076 1.07e-41

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: 154.76  E-value: 1.07e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDkRSVSIYEKelLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd14665     2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIE-RGEKIDEN--VQREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtDKSRDAQIKLTDFGLSTLCAPNELLKEP 1980
Cdd:cd14665    79 AGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLL-DGSPAPRLKICDFGYSKSSVLHSQPKST 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 CGTLAYVAPEVITLQGYNHKV-DAWSIGIILYLLLSGKLPF--PIN-KNTEMNIQK--NYVLSFKDYIwkSISSSAKDLI 2054
Cdd:cd14665   158 VGTPAYIAPEVLLKKEYDGKIaDVWSCGVTLYVMLVGAYPFedPEEpRNFRKTIQRilSVQYSIPDYV--HISPECRHLI 235
                         250       260
                  ....*....|....*....|..
gi 124804138 2055 SKLLELNVEKRISANEALEHIW 2076
Cdd:cd14665   236 SRIFVADPATRITIPEIRNHEW 257
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
1827-2077 1.22e-41

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: 154.72  E-value: 1.22e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVS--IYEKELLRSEISILRLLRHPNVIYLKEIINT--KETLYISMELVKG 1902
Cdd:cd14119     1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLRriPNGEANVKREIQILRRLNHRNVIKLVDVLYNeeKQKLYMVMEYCVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1903 GeLYDFLL--AETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLS---TLCAPNELL 1977
Cdd:cd14119    81 G-LQEMLDsaPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTT---DGTLKISDFGVAealDLFAEDDTC 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPCGTLAYVAPEVITLQGYNH--KVDAWSIGIILYLLLSGKLPFpinknTEMNIQKNY-VLSFKDYIW-KSISSSAKDL 2053
Cdd:cd14119   157 TTSQGSPAFQPPEIANGQDSFSgfKVDIWSAGVTLYNMTTGKYPF-----EGDNIYKLFeNIGKGEYTIpDDVDPDLQDL 231
                         250       260
                  ....*....|....*....|....
gi 124804138 2054 ISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14119   232 LRGMLEKDPEKRFTIEQIRQHPWF 255
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
1821-2074 2.24e-41

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: 155.03  E-value: 2.24e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSvsiyEKE-----LLRsEISILRLLRHPNVIYLKEII------NT 1889
Cdd:cd07840     1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMEN----EKEgfpitAIR-EIKLLQKLDHPNVVRLKEIVtskgsaKY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1890 KETLYISMELVKggelYDF--LLA--ETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDF 1965
Cdd:cd07840    76 KGSIYMVFEYMD----HDLtgLLDnpEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINN---DGVLKLADF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1966 GLSTLCAPNEllKEPCG----TLAYVAPEVitLQG---YNHKVDAWSIGIILYLLLSGKLPFPinKNTEMN--------- 2029
Cdd:cd07840   149 GLARPYTKEN--NADYTnrviTLWYRPPEL--LLGatrYGPEVDMWSVGCILAELFTGKPIFQ--GKTELEqlekifelc 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124804138 2030 ---------------------IQKNYVLSFKDYIWKSISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd07840   223 gspteenwpgvsdlpwfenlkPKKPYKRRLREVFKNVIDPSALDLLDKLLTLDPKKRISADQALQH 288
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
1821-2077 4.37e-41

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: 153.09  E-value: 4.37e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKR--SVSIYEKELLRsEISILRLLRHPNVIYLKEIIN-TKETLYISM 1897
Cdd:cd14164     2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRraSPDFVQKFLPR-ELSILRRVNHPNIVQMFECIEvANGRLYIVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ElVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRdaQIKLTDFGLST-LCAPNEL 1976
Cdd:cd14164    81 E-AAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDR--KIKIADFGFARfVEDYPEL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1977 LKEPCGTLAYVAPEVITlqGYNH---KVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYVLSFKDYiwkSISSSAKDL 2053
Cdd:cd14164   158 STTFCGSRAYTPPEVIL--GTPYdpkKYDVWSLGVVLYVMVTGTMPFDETNVRRLRLQQRGVLYPSGV---ALEEPCRAL 232
                         250       260
                  ....*....|....*....|....
gi 124804138 2054 ISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14164   233 IRTLLQFNPSTRPSIQQVAGNSWL 256
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
1821-2074 1.00e-40

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: 152.47  E-value: 1.00e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQ-TNSEFAIKVIDKRSVSiYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd14201     8 YSRKDLVGHGAFAVVFKGRHRKkTDWEVAIKSINKKNLS-KSQILLGKEIKILKELQHENIVALYDVQEMPNSVFLVMEY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDA------QIKLTDFGLSTLCAP 1973
Cdd:cd14201    87 CNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRKKssvsgiRIKIADFGFARYLQS 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1974 NELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYVLSFKDYIWKSISSSAKDL 2053
Cdd:cd14201   167 NMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYEKNKNLQPSIPRETSPYLADL 246
                         250       260
                  ....*....|....*....|.
gi 124804138 2054 ISKLLELNVEKRISANEALEH 2074
Cdd:cd14201   247 LLGLLQRNQKDRMDFEAFFSH 267
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
1821-2074 2.04e-40

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: 151.36  E-value: 2.04e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVID--KRSVSIYEkelLRSEISILRLLRHPNVIYLKEIINTKETLYISME 1898
Cdd:cd06610     3 YELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDleKCQTSMDE---LRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYD---FLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPN- 1974
Cdd:cd06610    80 LLSGGSLLDimkSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGE---DGSVKIADFGVSASLATGg 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1975 ----ELLKEPCGTLAYVAPEVIT-LQGYNHKVDAWSIGIILYLLLSGKLPF---PINKNTEMNIQKNYVLSFKDYIWKSI 2046
Cdd:cd06610   157 drtrKVRKTFVGTPCWMAPEVMEqVRGYDFKADIWSFGITAIELATGAAPYskyPPMKVLMLTLQNDPPSLETGADYKKY 236
                         250       260
                  ....*....|....*....|....*...
gi 124804138 2047 SSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd06610   237 SKSFRKMISLCLQKDPSKRPTAEELLKH 264
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
1819-2076 2.26e-40

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: 150.82  E-value: 2.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSvsiYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISME 1898
Cdd:cd14108     2 DYYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRA---KKKTSARRELALLAELDHKSIVRFHDAFEKRRVVIIVTE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDfLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDaQIKLTDFGLSTLCAPNELLK 1978
Cdd:cd14108    79 LCHEELLER-ITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTD-QVRICDFGNAQELTPNEPQY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1979 EPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF--PINKNTEMNIqKNYVLSFKDYIWKSISSSAKDLISK 2056
Cdd:cd14108   157 CKYGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFvgENDRTTLMNI-RNYNVAFEESMFKDLCREAKGFIIK 235
                         250       260
                  ....*....|....*....|
gi 124804138 2057 LLeLNVEKRISANEALEHIW 2076
Cdd:cd14108   236 VL-VSDRLRPDAEETLEHPW 254
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
1821-2074 6.20e-40

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: 149.63  E-value: 6.20e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSV-SIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd14186     3 FKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMqKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLEM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETR-LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLST-LCAPNELL 1977
Cdd:cd14186    83 CHNGEMSRYLKNRKKpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLT---RNMNIKIADFGLATqLKMPHEKH 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpiNKNTEMNIQKNYVLSfkDYIWKS-ISSSAKDLISK 2056
Cdd:cd14186   160 FTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPF--DTDTVKNTLNKVVLA--DYEMPAfLSREAQDLIHQ 235
                         250
                  ....*....|....*...
gi 124804138 2057 LLELNVEKRISANEALEH 2074
Cdd:cd14186   236 LLRKNPADRLSLSSVLDH 253
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
1827-2105 1.02e-39

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: 151.40  E-value: 1.02e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRgINKQTNSE----FAIKVIDKRSVSIYEKELL--RSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd05584     4 LGKGGYGKVFQ-VRKTTGSDkgkiFAMKVLKKASIVRNQKDTAhtKAERNILEAVKHPFIVDLHYAFQTGGKLYLILEYL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGlstLCAP----NEL 1976
Cdd:cd05584    83 SGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILL---DAQGHVKLTDFG---LCKEsihdGTV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1977 LKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpINKNTEMNIQKnyVLSFKDYIWKSISSSAKDLISK 2056
Cdd:cd05584   157 THTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPF-TAENRKKTIDK--ILKGKLNLPPYLTNEARDLLKK 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 124804138 2057 LLELNVEKRI-----SANEALEHIWVKNptavINENSFIYKNEE----INILNLQDVS 2105
Cdd:cd05584   234 LLKRNVSSRLgsgpgDAEEIKAHPFFRH----INWDDLLAKKVEppfkPLLQSEEDVS 287
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
1821-2078 1.46e-39

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: 148.92  E-value: 1.46e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSiyEKELLRSEISILRLLRHPNVI-YLKEIINTKEtLYISMEL 1899
Cdd:cd06647     9 YTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQP--KKELIINEILVMRENKNPNIVnYLDSYLVGDE-LWVVMEY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDfLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCAPNELLKE 1979
Cdd:cd06647    86 LAGGSLTD-VVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILL---GMDGSVKLTDFGFCAQITPEQSKRS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 P-CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpINKNTEMN---IQKNYVLSFKDYiwKSISSSAKDLIS 2055
Cdd:cd06647   162 TmVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY-LNENPLRAlylIATNGTPELQNP--EKLSAIFRDFLN 238
                         250       260
                  ....*....|....*....|...
gi 124804138 2056 KLLELNVEKRISANEALEHIWVK 2078
Cdd:cd06647   239 RCLEMDVEKRGSAKELLQHPFLK 261
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
1822-2036 2.78e-39

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: 147.70  E-value: 2.78e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138   1822 ELHEQLGQGKFSTVYRGINKQTNSEF----AIKVIdKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISM 1897
Cdd:smart00221    2 TLGKKLGEGAFGEVYKGTLKGKGDGKevevAVKTL-KEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVM 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138   1898 ELVKGGELYDFL--LAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPNE 1975
Cdd:smart00221   81 EYMPGGDLLDYLrkNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGE---NLVVKISDFGLSRDLYDDD 157
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124804138   1976 LLKEPCGTL--AYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFPINKNTEM--NIQKNYVL 2036
Cdd:smart00221  158 YYKVKGGKLpiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEPYPGMSNAEVleYLKKGYRL 223
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
1821-2078 3.76e-39

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: 148.74  E-value: 3.76e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSV-SIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd05612     3 FERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEViRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLStlcapNELLKE 1979
Cdd:cd05612    83 VPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILL---DKEGHIKLTDFGFA-----KKLRDR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 P---CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpINKNTEMNIQKnyVLSFKDYIWKSISSSAKDLISK 2056
Cdd:cd05612   155 TwtlCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPF-FDDNPFGIYEK--ILAGKLEFPRHLDLYAKDLIKK 231
                         250       260
                  ....*....|....*....|....*..
gi 124804138 2057 LLELNVEKRI-----SANEALEHIWVK 2078
Cdd:cd05612   232 LLVVDRTRRLgnmknGADDVKNHRWFK 258
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
1825-2077 6.12e-39

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: 147.99  E-value: 6.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSiyekellRSEISILRLLR-HPNVIYLKEII----------NTKETL 1893
Cdd:cd14171    12 QKLGTGISGPVRVCVKKSTGERFALKILLDRPKA-------RTEVRLHMMCSgHPNIVQIYDVYansvqfpgesSPRARL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1894 YISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLcaP 1973
Cdd:cd14171    85 LIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEDAPIKLCDFGFAKV--D 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1974 NELLKEPCGTLAYVAPEVITLQ-----------------GYNHKVDAWSIGIILYLLLSGKLPF-------PINKNTEMN 2029
Cdd:cd14171   163 QGDLMTPQFTPYYVAPQVLEAQrrhrkersgiptsptpyTYDKSCDMWSLGVIIYIMLCGYPPFysehpsrTITKDMKRK 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 124804138 2030 IQkNYVLSFKDYIWKSISSSAKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14171   243 IM-TGSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
1819-2074 1.15e-38

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: 145.87  E-value: 1.15e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELHEQLGQGKFSTVYRGINKQTNSEFAIKV--IDKRSVSIyEKEllrseISILRLLRHPNVIYLKEIINTKETLYIS 1896
Cdd:cd06612     3 EVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVvpVEEDLQEI-IKE-----ISILKQCDSPYIVKYYGSYFKNTDLWIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1897 MELVKGGELYDFL-LAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLST-LCAPN 1974
Cdd:cd06612    77 MEYCGAGSVSDIMkITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNE---EGQAKLADFGVSGqLTDTM 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1975 ELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLP-FPINKNTEM-NIQKNYVLSFKDYiwKSISSSAKD 2052
Cdd:cd06612   154 AKRNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPySDIHPMRAIfMIPNKPPPTLSDP--EKWSPEFND 231
                         250       260
                  ....*....|....*....|..
gi 124804138 2053 LISKLLELNVEKRISANEALEH 2074
Cdd:cd06612   232 FVKKCLVKDPEERPSAIQLLQH 253
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
1827-2076 1.45e-38

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: 147.89  E-value: 1.45e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIdKRSVSIYEKELLRS--EISILRLLRHPNVIYLKEIINTKETLYISMELVKGGE 1904
Cdd:cd05571     3 LGKGTFGKVILCREKATGELYAIKIL-KKEVIIAKDEVAHTltENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGlstLCAPN----ELLKEP 1980
Cdd:cd05571    82 LFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLL---DKDGHIKITDFG---LCKEEisygATTKTF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpinKNTEMNIQKNYVLSFKDYIWKSISSSAKDLISKLLEL 2060
Cdd:cd05571   156 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF---YNRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKK 232
                         250       260
                  ....*....|....*....|.
gi 124804138 2061 NVEKRI-----SANEALEHIW 2076
Cdd:cd05571   233 DPKKRLgggprDAKEIMEHPF 253
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
1821-2081 1.49e-38

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: 146.95  E-value: 1.49e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdkRSVSIYEKE------LLRsEISILRLLRHPNVIYLKEIINTKETLY 1894
Cdd:cd07841     2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKI--KLGERKEAKdginftALR-EIKLLQELKHPNIIGLLDVFGHKSNIN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELvkggelydfllAETRLSEIHANKIIT-----------QLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLT 1963
Cdd:cd07841    79 LVFEF-----------METDLEKVIKDKSIVltpadiksymlMTLRGLEYLHSNWILHRDLKPNNLLIAS---DGVLKLA 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1964 DFGLSTLCA-PNELLKEPCGTLAYVAPEVitLQG---YNHKVDAWSIGIILYLLLSGKLPFP-------INK-------N 2025
Cdd:cd07841   145 DFGLARSFGsPNRKMTHQVVTRWYRAPEL--LFGarhYGVGVDMWSVGCIFAELLLRVPFLPgdsdidqLGKifealgtP 222
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124804138 2026 TEMNIQ-----KNYV-------LSFKDYIwKSISSSAKDLISKLLELNVEKRISANEALEHIWVKN---PT 2081
Cdd:cd07841   223 TEENWPgvtslPDYVefkpfppTPLKQIF-PAASDDALDLLQRLLTLNPNKRITARQALEHPYFSNdpaPT 292
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
1818-2076 2.32e-38

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: 145.03  E-value: 2.32e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1818 YNLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSiyeKELLRSEISILRLLRHPNVIYLKEIINTKETLYISM 1897
Cdd:cd14107     1 HSVYEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSST---RARAFQERDILARLSHRRLTCLLDQFETRKTLILIL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDaQIKLTDFGLSTLCAPNELL 1977
Cdd:cd14107    78 ELCSSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTRE-DIKICDFGFAQEITPSEHQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF--PINKNTEMNIQKNyVLSFKDYIWKSISSSAKDLIS 2055
Cdd:cd14107   157 FSKYGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFagENDRATLLNVAEG-VVSWDTPEITHLSEDAKDFIK 235
                         250       260
                  ....*....|....*....|.
gi 124804138 2056 KLLELNVEKRISANEALEHIW 2076
Cdd:cd14107   236 RVLQPDPEKRPSASECLSHEW 256
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
1826-2077 3.98e-38

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: 145.19  E-value: 3.98e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1826 QLGQGKFSTVYRGINKQTNSEFAIKVIDKR---------------------SVSIYEKELLRSEISILRLLRHPNVIYLK 1884
Cdd:cd14118     1 EIGKGSYGIVKLAYNEEDNTLYAMKILSKKkllkqagffrrppprrkpgalGKPLDPLDRVYREIAILKKLDHPNVVKLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1885 EIIN--TKETLYISMELVKGGELYDfLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKL 1962
Cdd:cd14118    81 EVLDdpNEDNLYMVFELVDKGAVME-VPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGD---DGHVKI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1963 TDFGLSTLCAPNE-LLKEPCGTLAYVAPEviTLQGYNHK-----VDAWSIGIILYLLLSGKLPFPINKNTEMNIQ-KNYV 2035
Cdd:cd14118   157 ADFGVSNEFEGDDaLLSSTAGTPAFMAPE--ALSESRKKfsgkaLDIWAMGVTLYCFVFGRCPFEDDHILGLHEKiKTDP 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 124804138 2036 LSFKDYIwkSISSSAKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14118   235 VVFPDDP--VVSEQLKDLILRMLDKNPSERITLPEIKEHPWV 274
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
1821-2077 5.83e-38

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: 144.33  E-value: 5.83e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdKRSVSIYEKELlrSEISILRLLR------HPNVIYLKEIINTKETLY 1894
Cdd:cd14133     1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKII-KNNKDYLDQSL--DEIRLLELLNkkdkadKYHIVRLKDVFYFKNHLC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVkGGELYDFLlAETR---LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRdAQIKLTDFGLStlC 1971
Cdd:cd14133    78 IVFELL-SQNLYEFL-KQNKfqyLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSR-CQIKIIDFGSS--C 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1972 APNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYVLSFKDY--IWKSISSS 2049
Cdd:cd14133   153 FLTQRLYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPAhmLDQGKADD 232
                         250       260       270
                  ....*....|....*....|....*....|
gi 124804138 2050 AK--DLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14133   233 ELfvDFLKKLLEIDPKERPTASQALSHPWL 262
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
1822-2036 7.30e-38

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 143.83  E-value: 7.30e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138   1822 ELHEQLGQGKFSTVYRGINKQTNS----EFAIKVIdKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISM 1897
Cdd:smart00219    2 TLGKKLGEGAFGEVYKGKLKGKGGkkkvEVAVKTL-KEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVM 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138   1898 ELVKGGELYDFLLA-ETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPNEL 1976
Cdd:smart00219   81 EYMEGGDLLSYLRKnRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGE---NLVVKISDFGLSRDLYDDDY 157
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124804138   1977 LKEPCGTL--AYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFPINKNTEM--NIQKNYVL 2036
Cdd:smart00219  158 YRKRGGKLpiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVleYLKNGYRL 222
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
1826-2077 1.12e-37

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: 143.26  E-value: 1.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1826 QLGQGKFSTVYRGINKQTNSEFAIKVID-KRSVSIYEKEL--LRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKG 1902
Cdd:cd06625     7 LLGQGAFGQVYLCYDADTGRELAVKQVEiDPINTEASKEVkaLECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1903 GELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILltdksRDA--QIKLTDFG----LSTLCAPNEl 1976
Cdd:cd06625    87 GSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANIL-----RDSngNVKLGDFGaskrLQTICSSTG- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1977 LKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLP----------FPINKNTemniqKNYVLSfkdyiwKSI 2046
Cdd:cd06625   161 MKSVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPwaefepmaaiFKIATQP-----TNPQLP------PHV 229
                         250       260       270
                  ....*....|....*....|....*....|.
gi 124804138 2047 SSSAKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd06625   230 SEDARDFLSLIFVRNKKQRPSAEELLSHSFV 260
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
1821-2078 1.24e-37

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: 144.08  E-value: 1.24e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRS-VSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd14209     3 FDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKvVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGL--------STLc 1971
Cdd:cd14209    83 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQ---GYIKVTDFGFakrvkgrtWTL- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1972 apnellkepCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMniqKNYVLSFKDYIWKSISSSAK 2051
Cdd:cd14209   159 ---------CGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQI---YEKIVSGKVRFPSHFSSDLK 226
                         250       260       270
                  ....*....|....*....|....*....|..
gi 124804138 2052 DLISKLLELNVEKRI-----SANEALEHIWVK 2078
Cdd:cd14209   227 DLLRNLLQVDLTKRFgnlknGVNDIKNHKWFA 258
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
1821-2075 1.39e-37

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: 143.26  E-value: 1.39e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVI-----DKRSVSIYEKELLRSEISILRLL-RHPNVIYLKEIINTKETLY 1894
Cdd:cd13993     2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLyksgpNSKDGNDFQKLPQLREIDLHRRVsRHPNIITLHDVFETEVAIY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVKGGELYDFLLAETR--LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrDAQIKLTDFGLSTLCA 1972
Cdd:cd13993    82 IVLEYCPNGDLFEAITENRIyvGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQD--EGTVKLCDFGLATTEK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1973 PNelLKEPCGTLAYVAPEVIT-----LQGYN-HKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYVLS---FKDYIw 2043
Cdd:cd13993   160 IS--MDFGVGSEFYMAPECFDevgrsLKGYPcAAGDIWSLGIILLNLTFGRNPWKIASESDPIFYDYYLNSpnlFDVIL- 236
                         250       260       270
                  ....*....|....*....|....*....|..
gi 124804138 2044 kSISSSAKDLISKLLELNVEKRISANEALEHI 2075
Cdd:cd13993   237 -PMSDDFYNLLRQIFTVNPNNRILLPELQLLV 267
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
1827-2075 1.75e-37

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: 144.47  E-value: 1.75e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVY---RGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGG 1903
Cdd:cd05582     3 LGQGSFGKVFlvrKITGPDAGTLYAMKVLKKATLKVRDRVRTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFLRGG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 ELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLStlcapnellKEP--- 1980
Cdd:cd05582    83 DLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDE---DGHIKLTDFGLS---------KESidh 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 -------CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFP-INKNTEMNIqknyVLSFKDYIWKSISSSAKD 2052
Cdd:cd05582   151 ekkaysfCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQgKDRKETMTM----ILKAKLGMPQFLSPEAQS 226
                         250       260
                  ....*....|....*....|....
gi 124804138 2053 LISKLLELNVEKRISAN-EALEHI 2075
Cdd:cd05582   227 LLRALFKRNPANRLGAGpDGVEEI 250
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
1822-2075 2.39e-37

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: 142.25  E-value: 2.39e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138  1822 ELHEQLGQGKFSTVYRGI----NKQTNSEFAIKVIdKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISM 1897
Cdd:pfam07714    2 TLGEKLGEGAFGEVYKGTlkgeGENTKIKVAVKTL-KEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138  1898 ELVKGGELYDFLLAETR-LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLS-TLCAPNE 1975
Cdd:pfam07714   81 EYMPGGDLLDFLRKHKRkLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSE---NLVVKISDFGLSrDIYDDDY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138  1976 LLKEPCGTL--AYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFPINKNTEM--NIQKNYVLSFKDYIWKSIsssa 2050
Cdd:pfam07714  158 YRKRGGGKLpiKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVleFLEDGYRLPQPENCPDEL---- 233
                          250       260
                   ....*....|....*....|....*
gi 124804138  2051 KDLISKLLELNVEKRISANEALEHI 2075
Cdd:pfam07714  234 YDLMKQCWAYDPEDRPTFSELVEDL 258
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1821-2074 3.23e-37

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: 142.29  E-value: 3.23e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVI-YLKEIIN-TKETLYISME 1898
Cdd:cd08217     2 YEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMSEKEKQQLVSEVNILRELKHPNIVrYYDRIVDrANTTLYIVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFL----LAETRLSEIHANKIITQLIKTVAYLHRCG-----IIHRDIKPENILLtdkSRDAQIKLTDFGLS- 1968
Cdd:cd08217    82 YCEGGDLAQLIkkckKENQYIPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFL---DSDNNVKLGDFGLAr 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1969 TLCAPNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTE--MNIQKNYVLSFKDYiwksI 2046
Cdd:cd08217   159 VLSHDSSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLElaKKIKEGKFPRIPSR----Y 234
                         250       260
                  ....*....|....*....|....*...
gi 124804138 2047 SSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd08217   235 SSELNEVIKSMLNVDPDKRPSVEELLQL 262
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
1820-2077 7.41e-37

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: 141.27  E-value: 7.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1820 LYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRsvsIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd14113     8 FYSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNKK---LMKRDQVTHELGVLQSLQHPQLVGLLDTFETPTSYILVLEM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFG----LSTLCAPNE 1975
Cdd:cd14113    85 ADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSKPTIKLADFGdavqLNTTYYIHQ 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1976 LLKEPcgtlAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpINKNTE---MNIQKnYVLSFKDYIWKSISSSAKD 2052
Cdd:cd14113   165 LLGSP----EFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPF-LDESVEetcLNICR-LDFSFPDDYFKGVSQKAKD 238
                         250       260
                  ....*....|....*....|....*
gi 124804138 2053 LISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14113   239 FVCFLLQMDPAKRPSAALCLQEQWL 263
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
1821-2074 1.18e-36

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: 141.26  E-value: 1.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdkrSVSIYEKEL----LRsEISILRLLR---HPNVIYLKEIINTKET- 1892
Cdd:cd07838     1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKV---RVPLSEEGIplstIR-EIALLKQLEsfeHPNVVRLLDVCHGPRTd 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1893 ----LYISMELVKGgELYDFL--LAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFG 1966
Cdd:cd07838    77 relkLTLVFEHVDQ-DLATYLdkCPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVT---SDGQVKLADFG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1967 LSTLCAPNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPinKNTEMN-IQK------------- 2032
Cdd:cd07838   153 LARIYSFEMALTSVVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFR--GSSEADqLGKifdviglpseeew 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 124804138 2033 -------------NYVLSFKDYIwKSISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd07838   231 prnsalprssfpsYTPRPFKSFV-PEIDEEGLDLLKKMLTFNPHKRISAFEALQH 284
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
1821-2077 1.32e-36

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: 140.51  E-value: 1.32e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQ-LGQGKFSTVYRGINKQTNSEFAIKVIdkrsvsiYEKELLRSEISI-LRLLRHPNVIYL----KEIINTKETLY 1894
Cdd:cd14172     5 YKLSKQvLGLGVNGKVLECFHRRTGQKCALKLL-------YDSPKARREVEHhWRASGGPHIVHIldvyENMHHGKRCLL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVKGGELYDFLLA--ETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCA 1972
Cdd:cd14172    78 IIMECMEGGELFSRIQErgDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDAVLKLTDFGFAKETT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1973 PNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMN--IQKNYVL---SFKDYIWKSIS 2047
Cdd:cd14172   158 VQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISpgMKRRIRMgqyGFPNPEWAEVS 237
                         250       260       270
                  ....*....|....*....|....*....|
gi 124804138 2048 SSAKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14172   238 EEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
1825-2077 1.49e-36

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: 139.85  E-value: 1.49e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSEFAIK---VIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVK 1901
Cdd:cd06632     6 QLLGSGSFGSVYEGFNGDTGDFFAVKevsLVDDDKKSRESVKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1902 GGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtDKsrDAQIKLTDFGLSTLCAPNELLKEPC 1981
Cdd:cd06632    86 GGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILV-DT--NGVVKLADFGMAKHVEAFSFAKSFK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1982 GTLAYVAPEVITLQ--GYNHKVDAWSIGIILYLLLSGKLP----------FPINKNTEMNIqknyvlsfkdyIWKSISSS 2049
Cdd:cd06632   163 GSPYWMAPEVIMQKnsGYGLAVDIWSLGCTVLEMATGKPPwsqyegvaaiFKIGNSGELPP-----------IPDHLSPD 231
                         250       260
                  ....*....|....*....|....*...
gi 124804138 2050 AKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd06632   232 AKDFIRLCLQRDPEDRPTASQLLEHPFV 259
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
1829-2079 1.59e-36

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: 139.92  E-value: 1.59e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1829 QGKFSTVYRGINKQTNSEFAIKVIDKRS-VSIYEKELLRSEISILRLLRH-PNVIYLKEIINTKETLYISMELVKGGELY 1906
Cdd:cd05611     6 KGAFGSVYLAKKRSTGDYFAIKVLKKSDmIAKNQVTNVKAERAIMMIQGEsPYVAKLYYSFQSKDYLYLVMEYLNGGDCA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1907 DFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCAPNELLKEPCGTLAY 1986
Cdd:cd05611    86 SLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLI---DQTGHLKLTDFGLSRNGLEKRHNKKFVGTPDY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1987 VAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpiNKNTEMNIQKNYV---LSFKDYIWKSISSSAKDLISKLLELNVE 2063
Cdd:cd05611   163 LAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPF--HAETPDAVFDNILsrrINWPEEVKEFCSPEAVDLINRLLCMDPA 240
                         250
                  ....*....|....*....
gi 124804138 2064 KRISANEALE---HIWVKN 2079
Cdd:cd05611   241 KRLGANGYQEiksHPFFKS 259
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
1821-2078 2.39e-36

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: 140.00  E-value: 2.39e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdkrSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd14104     2 YMIAEELGRGQFGIVHRCVETSSKKTYMAKFV---KVKGADQVLVKKEISILNIARHRNILRLHESFESHEELVMIFEFI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFL-LAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsRDAQIKLTDFGLSTLCAPNELLKE 1979
Cdd:cd14104    79 SGVDIFERItTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTR-RGSYIKIIEFGQSRQLKPGDKFRL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 PCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF--PINKNTEMNIqKNYVLSFKDYIWKSISSSAKDLISKL 2057
Cdd:cd14104   158 QYTSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFeaETNQQTIENI-RNAEYAFDDEAFKNISIEALDFVDRL 236
                         250       260
                  ....*....|....*....|.
gi 124804138 2058 LELNVEKRISANEALEHIWVK 2078
Cdd:cd14104   237 LVKERKSRMTAQEALNHPWLK 257
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
1819-2077 3.09e-36

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: 140.10  E-value: 3.09e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSV---------------------SIYEK---ELLRSEISILRL 1874
Cdd:cd14199     2 NQYKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLmrqagfprrppprgaraapegCTQPRgpiERVYQEIAILKK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1875 LRHPNVIYLKEIIN--TKETLYISMELVKGGELYDfLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLT 1952
Cdd:cd14199    82 LDHPNVVKLVEVLDdpSEDHLYMVFELVKQGPVME-VPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1953 DksrDAQIKLTDFGLS-TLCAPNELLKEPCGTLAYVAPEVI--TLQGYNHK-VDAWSIGIILYLLLSGKLPFPINKNTEM 2028
Cdd:cd14199   161 E---DGHIKIADFGVSnEFEGSDALLTNTVGTPAFMAPETLseTRKIFSGKaLDVWAMGVTLYCFVFGQCPFMDERILSL 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 124804138 2029 NIQ-KNYVLSFKDYiwKSISSSAKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14199   238 HSKiKTQPLEFPDQ--PDISDDLKDLLFRMLDKNPESRISVPEIKLHPWV 285
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
1821-2074 3.93e-36

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: 141.28  E-value: 3.93e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVS-IYEKELLRsEISILRLLRHPNVIYLKEIINTKETL------ 1893
Cdd:cd07851    17 YQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRPFQSaIHAKRTYR-ELRLLKHMKHENVIGLLDVFTPASSLedfqdv 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1894 YISMELVkGGELYDfLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCap 1973
Cdd:cd07851    96 YLVTHLM-GADLNN-IVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNE---DCELKILDFGLARHT-- 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1974 NELLKEPCGTLAYVAPEVITLQG-YNHKVDAWSIGIILYLLLSGKLPFP----INKNTE-MNI----------------Q 2031
Cdd:cd07851   169 DDEMTGYVATRWYRAPEIMLNWMhYNQTVDIWSVGCIMAELLTGKTLFPgsdhIDQLKRiMNLvgtpdeellkkissesA 248
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 124804138 2032 KNYVLS--------FKDyIWKSISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd07851   249 RNYIQSlpqmpkkdFKE-VFSGANPLAIDLLEKMLVLDPDKRITAAEALAH 298
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
1820-2086 5.38e-36

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: 139.15  E-value: 5.38e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1820 LYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSiYEKELLRSEISILRLLRH---PNVI-----YLKEiintkE 1891
Cdd:cd06917     2 LYRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLDTDD-DDVSDIQKEVALLSQLKLgqpKNIIkyygsYLKG-----P 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1892 TLYISMELVKGGELYDFLLAEtRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLSTLC 1971
Cdd:cd06917    76 SLWIIMDYCEGGSIRTLMRAG-PIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVT---NTGNVKLCDFGVAASL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1972 APNELLKEP-CGTLAYVAPEVITL-QGYNHKVDAWSIGIILYLLLSGKLPFPINKNTE--MNIQKNYVLSFKDYIWksiS 2047
Cdd:cd06917   152 NQNSSKRSTfVGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPYSDVDALRavMLIPKSKPPRLEGNGY---S 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 124804138 2048 SSAKDLISKLLELNVEKRISANEALEHIWVK----NPTAVINE 2086
Cdd:cd06917   229 PLLKEFVAACLDEEPKDRLSADELLKSKWIKqhskTPTSVLKE 271
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
1821-2073 1.09e-35

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: 138.31  E-value: 1.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVsiyekeLLRSEIS-------ILRLLRHPNVIYLKEIINTKETL 1893
Cdd:cd05609     2 FETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNL------ILRNQIQqvfverdILTFAENPFVVSMYCSFETKRHL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1894 YISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLC-- 1971
Cdd:cd05609    76 CMVMEYVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSM---GHIKLTDFGLSKIGlm 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1972 --------------APNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQknyVLS 2037
Cdd:cd05609   153 slttnlyeghiekdTREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQ---VIS 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 124804138 2038 fKDYIW----KSISSSAKDLISKLLELNVEKRISANEALE 2073
Cdd:cd05609   230 -DEIEWpegdDALPDDAQDLITRLLQQNPLERLGTGGAEE 268
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
1826-2075 2.58e-35

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: 138.60  E-value: 2.58e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1826 QLGQGKFSTVYRGINKQTNSEFAIKVIDKRSV-SIYEKELLRSEISIL-RLLRHPNVIYLKEIINTKETLYISMELVKGG 1903
Cdd:cd05575     2 VIGKGSFGKVLLARHKAEGKLYAVKVLQKKAIlKRNEVKHIMAERNVLlKNVKHPFLVGLHYSFQTKDKLYFVLDYVNGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 ELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLstlC----APNELLKE 1979
Cdd:cd05575    82 ELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILL---DSQGHVVLTDFGL---CkegiEPSDTTST 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 PCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEM--NIQkNYVLSFKDYiwksISSSAKDLISKL 2057
Cdd:cd05575   156 FCGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMydNIL-HKPLRLRTN----VSPSARDLLEGL 230
                         250
                  ....*....|....*...
gi 124804138 2058 LELNVEKRISANEALEHI 2075
Cdd:cd05575   231 LQKDRTKRLGSGNDFLEI 248
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
1821-2077 3.23e-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: 135.98  E-value: 3.23e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVS----IYEKEL--LRSEISILRLLR---HPNVIYLKEIINTKE 1891
Cdd:cd14004     2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILvdtwVRDRKLgtVPLEIHILDTLNkrsHPNIVKLLDFFEDDE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1892 TLYISMELVKGG-ELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRdaqIKLTDFGLSTL 1970
Cdd:cd14004    82 FYYLVMEKHGSGmDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGT---IKLIDFGSAAY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1971 CAPNElLKEPCGTLAYVAPEVITLQGYNHK-VDAWSIGIILYLLLSGKLPF-PINKNTEMNIQKNYVLSfKDYIwksiss 2048
Cdd:cd14004   159 IKSGP-FDTFVGTIDYAAPEVLRGNPYGGKeQDIWALGVLLYTLVFKENPFyNIEEILEADLRIPYAVS-EDLI------ 230
                         250       260
                  ....*....|....*....|....*....
gi 124804138 2049 sakDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14004   231 ---DLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
1821-2076 3.27e-35

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: 137.08  E-value: 3.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIK-VIDKRSVSIYEKELLRsEISILRLLR-HPNVIYLKEIINTKETLYISME 1898
Cdd:cd07832     2 YKILGRIGEGAHGIVFKAKDRETGETVALKkVALRKLEGGIPNQALR-EIKALQACQgHPYVVKLRDVFPHGTGFVLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVkGGELYDFLLAETR-LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPNE-- 1975
Cdd:cd07832    81 YM-LSSLSEVLRDEERpLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISS---TGVLKIADFGLARLFSEEDpr 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1976 LLKEPCGTLAYVAPEVI-TLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEmniQKNYVL---------------SFK 2039
Cdd:cd07832   157 LYSHQVATRWYRAPELLyGSRKYDEGVDLWAVGCIFAELLNGSPLFPGENDIE---QLAIVLrtlgtpnektwpeltSLP 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 124804138 2040 DY-----------IWKSI----SSSAKDLISKLLELNVEKRISANEALEHIW 2076
Cdd:cd07832   234 DYnkitfpeskgiRLEEIfpdcSPEAIDLLKGLLVYNPKKRLSAEEALRHPY 285
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
1827-2072 3.65e-35

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: 136.22  E-value: 3.65e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSV-SIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGEL 1905
Cdd:cd14187    15 LGKGGFAKCYEITDADTKEVFAGKIVPKSLLlKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRRSL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1906 YDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPN-ELLKEPCGTL 1984
Cdd:cd14187    95 LELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLND---DMEVKIGDFGLATKVEYDgERKKTLCGTP 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1985 AYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPIN--KNTEMNIQKNyvlsfkDY-IWKSISSSAKDLISKLLELN 2061
Cdd:cd14187   172 NYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSclKETYLRIKKN------EYsIPKHINPVAASLIQKMLQTD 245
                         250
                  ....*....|.
gi 124804138 2062 VEKRISANEAL 2072
Cdd:cd14187   246 PTARPTINELL 256
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
1827-2076 4.03e-35

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: 135.47  E-value: 4.03e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRsvsIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGELY 1906
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKDVAVKFVSKK---MKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1907 DFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCAPNELLKEPCGTLAY 1986
Cdd:cd14115    78 DYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHRHVHHLLGNPEF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1987 VAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYV-LSFKDYIWKSISSSAKDLISKLLELNVEKR 2065
Cdd:cd14115   158 AAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVdFSFPDEYFGDVSQAARDFINVILQEDPRRR 237
                         250
                  ....*....|.
gi 124804138 2066 ISANEALEHIW 2076
Cdd:cd14115   238 PTAATCLQHPW 248
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
1821-2074 4.18e-35

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: 136.63  E-value: 4.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRsEISILRLLR-HPNVIYLKEIINTKET--LYISM 1897
Cdd:cd07831     1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKHFKSLEQVNNLR-EIQALRRLSpHPNILRLIEVLFDRKTgrLALVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGgELYDFLLAETR-LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdksRDAQIKLTDFGLSTLCAPNEL 1976
Cdd:cd07831    80 ELMDM-NLYELIKGRKRpLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILI----KDDILKLADFGSCRGIYSKPP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1977 LKEPCGTLAYVAPEVITLQG-YNHKVDAWSIGIILYLLLSGKLPFP---------------------INKNTEMNIQKNY 2034
Cdd:cd07831   155 YTEYISTRWYRAPECLLTDGyYGPKMDIWAVGCVFFEILSLFPLFPgtneldqiakihdvlgtpdaeVLKKFRKSRHMNY 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 124804138 2035 VLSFKDYIW-----KSISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd07831   235 NFPSKKGTGlrkllPNASAEGLDLLKKLLAYDPDERITAKQALRH 279
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
1821-2074 6.24e-35

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: 135.21  E-value: 6.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd08530     2 FKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQKEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFL----LAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLcAPNEL 1976
Cdd:cd08530    82 PFGDLSKLIskrkKKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILL---SAGDLVKIGDLGISKV-LKKNL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1977 LKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNiqkNYVLSFK-DYIWKSISSSAKDLIS 2055
Cdd:cd08530   158 AKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELR---YKVCRGKfPPIPPVYSQDLQQIIR 234
                         250
                  ....*....|....*....
gi 124804138 2056 KLLELNVEKRISANEALEH 2074
Cdd:cd08530   235 SLLQVNPKKRPSCDKLLQS 253
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
1827-2074 9.96e-35

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: 134.67  E-value: 9.96e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSI-YEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGEL 1905
Cdd:cd14189     9 LGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKpHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRKSL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1906 YDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLST-LCAPNELLKEPCGTL 1984
Cdd:cd14189    89 AHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINE---NMELKVGDFGLAArLEPPEQRKKTICGTP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1985 AYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpinKNTEMNIQKNYVLSFKDYIWKSISSSAKDLISKLLELNVEK 2064
Cdd:cd14189   166 NYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPF---ETLDLKETYRCIKQVKYTLPASLSLPARHLLAGILKRNPGD 242
                         250
                  ....*....|
gi 124804138 2065 RISANEALEH 2074
Cdd:cd14189   243 RLTLDQILEH 252
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
1821-2079 1.03e-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: 137.42  E-value: 1.03e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELL-RSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd05573     3 FEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAHvRAERDILADADSPWIVRLHYAFQDEDHLYLVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLST---------- 1969
Cdd:cd05573    83 MPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLD---ADGHIKLADFGLCTkmnksgdres 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1970 --------LCAPNELLKE------------PCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTE-- 2027
Cdd:cd05573   160 ylndsvntLFQDNVLARRrphkqrrvraysAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVEty 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 124804138 2028 ---MNIQKNyvLSFKDYiwKSISSSAKDLISKLLeLNVEKRI-SANEALEHIWVKN 2079
Cdd:cd05573   240 skiMNWKES--LVFPDD--PDVSPEAIDLIRRLL-CDPEDRLgSAEEIKAHPFFKG 290
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
1820-2077 2.67e-34

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: 133.58  E-value: 2.67e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1820 LYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdkrsvSIYEKE---LLRSEISILRLLRHPNVI-----YLKEiintkE 1891
Cdd:cd06613     1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVI-----KLEPGDdfeIIQQEISMLKECRHPNIVayfgsYLRR-----D 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1892 TLYISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLS--- 1968
Cdd:cd06613    71 KLWIVMEYCGGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTE---DGDVKLADFGVSaql 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1969 --TLCAPNELLkepcGTLAYVAPEVITLQ---GYNHKVDAWSIGIILYLLLSGKLPfpinkNTEMNIQKN-YVLSFKDY- 2041
Cdd:cd06613   148 taTIAKRKSFI----GTPYWMAPEVAAVErkgGYDGKCDIWALGITAIELAELQPP-----MFDLHPMRAlFLIPKSNFd 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 124804138 2042 --------IWksiSSSAKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd06613   219 ppklkdkeKW---SPDFHDFIKKCLTKNPKKRPTATKLLQHPFV 259
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
1827-2065 3.49e-34

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: 135.03  E-value: 3.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEK-ELLRSEISILRL-LRHPNVIYLKEIINTKETLYISMELVKGGE 1904
Cdd:cd05570     3 LGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDvECTMTEKRVLALaNRHPFLTGLHACFQTEDRLYFVMEYVNGGD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLstlC----APNELLKEP 1980
Cdd:cd05570    83 LMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLD---AEGHIKIADFGM---CkegiWGGNTTSTF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTE--MNIQKNYVLsfkdyIWKSISSSAKDLISKLL 2058
Cdd:cd05570   157 CGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDElfEAILNDEVL-----YPRWLSREAVSILKGLL 231

                  ....*..
gi 124804138 2059 ELNVEKR 2065
Cdd:cd05570   232 TKDPARR 238
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
1827-2074 3.79e-34

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: 133.43  E-value: 3.79e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEK-------ELLRSEISILRLLRHPNVI-YLKEIINTkETLYISME 1898
Cdd:cd06628     8 IGSGSFGSVYLGMNASSGELMAVKQVELPSVSAENKdrkksmlDALQREIALLRELQHENIVqYLGSSSDA-NHLNIFLE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLCAPNELL- 1977
Cdd:cd06628    87 YVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNK---GGIKISDFGISKKLEANSLSt 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 ----KEPC--GTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPinKNTEMN----IQKNYVLSFKDyiwkSIS 2047
Cdd:cd06628   164 knngARPSlqGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFP--DCTQMQaifkIGENASPTIPS----NIS 237
                         250       260
                  ....*....|....*....|....*..
gi 124804138 2048 SSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd06628   238 SEARDFLEKTFEIDHNKRPTADELLKH 264
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
1826-2074 4.26e-34

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: 132.95  E-value: 4.26e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1826 QLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSiyEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGEL 1905
Cdd:cd06648    14 KIGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQ--RRELLFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGGAL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1906 YDfLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGlstLCA------PNEllKE 1979
Cdd:cd06648    92 TD-IVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLT---SDGRVKLSDFG---FCAqvskevPRR--KS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 PCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF----PINKNTemNIQKNYVLSFKDYiwKSISSSAKDLIS 2055
Cdd:cd06648   163 LVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYfnepPLQAMK--RIRDNEPPKLKNL--HKVSPRLRSFLD 238
                         250
                  ....*....|....*....
gi 124804138 2056 KLLELNVEKRISANEALEH 2074
Cdd:cd06648   239 RMLVRDPAQRATAAELLNH 257
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
1827-2075 4.34e-34

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: 132.83  E-value: 4.34e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIyeKELLRsEISI-LRLLRHPNVIYLKEIINTKETLYI-SMELVKGGE 1904
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKL--KDFLR-EYNIsLELSVHPHIIKTYDVAFETEDYYVfAQEYAPYGD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRdAQIKLTDFGLSTlcAPNELLKEPCGTL 1984
Cdd:cd13987    78 LFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDC-RRVKLCDFGLTR--RVGSTVKRVSGTI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1985 AYVAPEVITL---QGY--NHKVDAWSIGIILYLLLSGKLPFPI----NKNTEMNIQ----KNYVLSFKdyiWKSISSSAK 2051
Cdd:cd13987   155 PYTAPEVCEAkknEGFvvDPSIDVWAFGVLLFCCLTGNFPWEKadsdDQFYEEFVRwqkrKNTAVPSQ---WRRFTPKAL 231
                         250       260
                  ....*....|....*....|....
gi 124804138 2052 DLISKLLELNVEKRISANEALEHI 2075
Cdd:cd13987   232 RMFKKLLAPEPERRCSIKEVFKYL 255
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
1821-2066 5.96e-34

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 134.56  E-value: 5.96e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSV-SIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:PTZ00263   20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREIlKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEF 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLCApnELLKE 1979
Cdd:PTZ00263  100 VVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNK---GHVKVTDFGFAKKVP--DRTFT 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 PCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpiNKNTEMNIQKNyVLSFKDYIWKSISSSAKDLISKLLE 2059
Cdd:PTZ00263  175 LCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPF--FDDTPFRIYEK-ILAGRLKFPNWFDGRARDLVKGLLQ 251

                  ....*..
gi 124804138 2060 LNVEKRI 2066
Cdd:PTZ00263  252 TDHTKRL 258
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1821-2079 9.20e-34

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: 132.82  E-value: 9.20e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVY--RGIN-KQTNSEFAIKVIDKRSVSIYEK--ELLRSEISILRLLRH-PNVIYLKEIINTKETLY 1894
Cdd:cd05613     2 FELLKVLGTGAYGKVFlvRKVSgHDAGKLYAMKVLKKATIVQKAKtaEHTRTERQVLEHIRQsPFLVTLHYAFQTDTKLH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLST--LCA 1972
Cdd:cd05613    82 LILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILL---DSSGHVVLTDFGLSKefLLD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1973 PNELLKEPCGTLAYVAPEVIT--LQGYNHKVDAWSIGIILYLLLSGKLPFPIN--KNTEMNIQKNYVLSFKDYIwKSISS 2048
Cdd:cd05613   159 ENERAYSFCGTIEYMAPEIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDgeKNSQAEISRRILKSEPPYP-QEMSA 237
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 124804138 2049 SAKDLISKLLELNVEKRI-----SANEALEHIWVKN 2079
Cdd:cd05613   238 LAKDIIQRLLMKDPKKRLgcgpnGADEIKKHPFFQK 273
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
1821-2074 1.02e-33

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: 132.15  E-value: 1.02e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQ-----LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSiyEKELLRSEISILRLLRHPNVI-YLKEIINtKETLY 1894
Cdd:cd06624     5 YEYDESgervvLGKGTFGVVYAARDLSTQVRIAIKEIPERDSR--EVQPLHEEIALHSRLSHKNIVqYLGSVSE-DGFFK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVKGGELYDFLLAETRLSEIHANKII---TQLIKTVAYLHRCGIIHRDIKPENILLTDKSrdAQIKLTDFGLST-L 1970
Cdd:cd06624    82 IFMEQVPGGSLSALLRSKWGPLKDNENTIGyytKQILEGLKYLHDNKIVHRDIKGDNVLVNTYS--GVVKISDFGTSKrL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1971 CAPNELLKEPCGTLAYVAPEVIT--LQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKnyVLSFKDY--IWKSI 2046
Cdd:cd06624   160 AGINPCTETFTGTLQYMAPEVIDkgQRGYGPPADIWSLGCTIIEMATGKPPFIELGEPQAAMFK--VGMFKIHpeIPESL 237
                         250       260
                  ....*....|....*....|....*...
gi 124804138 2047 SSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd06624   238 SEEAKSFILRCFEPDPDKRATASDLLQD 265
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
1825-2076 1.19e-33

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: 132.60  E-value: 1.19e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELVKGgE 1904
Cdd:cd07836     6 EKLGEGTYATVYKGRNRTTGEIVALKEIHLDAEEGTPSTAIR-EISLMKELKHENIVRLHDVIHTENKLMLVFEYMDK-D 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAETRLSEIHANKI---ITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLS-TLCAPNELLKEP 1980
Cdd:cd07836    84 LKKYMDTHGVRGALDPNTVksfTYQLLKGIAFCHENRVLHRDLKPQNLLI---NKRGELKLADFGLArAFGIPVNTFSNE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 CGTLAYVAPEVitLQG---YNHKVDAWSIGIILYLLLSGKLPFP-INKNTEMNIQKNYVLSFKDYIWKSISSSAK----- 2051
Cdd:cd07836   161 VVTLWYRAPDV--LLGsrtYSTSIDIWSVGCIMAEMITGRPLFPgTNNEDQLLKIFRIMGTPTESTWPGISQLPEykptf 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 124804138 2052 --------------------DLISKLLELNVEKRISANEALEHIW 2076
Cdd:cd07836   239 pryppqdlqqlfphadplgiDLLHRLLQLNPELRISAHDALQHPW 283
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
1825-2075 1.22e-33

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 131.51  E-value: 1.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGI---NKQTNSEFAIKVIdKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVK 1901
Cdd:cd00192     1 KKLGEGAFGEVYKGKlkgGDGKTVDVAVKTL-KEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1902 GGELYDFLLAETRLSEIHANKIITQLIKT---------VAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCA 1972
Cdd:cd00192    80 GGDLLDFLRKSRPVFPSPEPSTLSLKDLLsfaiqiakgMEYLASKKFVHRDLAARNCLVGE---DLVVKISDFGLSRDIY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1973 PNELLKEPCGTLAYV---APEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFPINKNTEM--NIQKNYVLSFKDYIWKSI 2046
Cdd:cd00192   157 DDDYYRKKTGGKLPIrwmAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPGLSNEEVleYLRKGYRLPKPENCPDEL 236
                         250       260
                  ....*....|....*....|....*....
gi 124804138 2047 sssaKDLISKLLELNVEKRISANEALEHI 2075
Cdd:cd00192   237 ----YELMLSCWQLDPEDRPTFSELVERL 261
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
1827-2078 1.67e-33

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: 131.31  E-value: 1.67e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGELY 1906
Cdd:cd06605     9 LGEGNGGVVSKVRHRPSGQIMAVKVIRLEIDEALQKQILR-ELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMDGGSLD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1907 DFLLAETRLSEIHANKIITQLIKTVAYLH-RCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLCApNELLKEPCGTLA 1985
Cdd:cd06605    88 KILKEVGRIPERILGKIAVAVVKGLIYLHeKHKIIHRDVKPSNILVNSR---GQVKLCDFGVSGQLV-DSLAKTFVGTRS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1986 YVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFP-INKNTEMNIqknyvLSFKDYIWK---------SISSSAKDLIS 2055
Cdd:cd06605   164 YMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPpPNAKPSMMI-----FELLSYIVDepppllpsgKFSPDFQDFVS 238
                         250       260
                  ....*....|....*....|...
gi 124804138 2056 KLLELNVEKRISANEALEHIWVK 2078
Cdd:cd06605   239 QCLQKDPTERPSYKELMEHPFIK 261
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1821-2068 2.36e-33

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: 133.12  E-value: 2.36e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVY--RGIN-KQTNSEFAIKVIDKRSVSIYEK--ELLRSEISILRLLRH-PNVIYLKEIINTKETLY 1894
Cdd:cd05614     2 FELLKVLGTGAYGKVFlvRKVSgHDANKLYAMKVLRKAALVQKAKtvEHTRTERNVLEHVRQsPFLVTLHYAFQTDAKLH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLStlcapN 1974
Cdd:cd05614    82 LILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILL---DSEGHVVLTDFGLS-----K 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1975 ELLKEP-------CGTLAYVAPEVITLQ-GYNHKVDAWSIGIILYLLLSGKLPFPI--NKNTEMNIQKNyVLSFKDYIWK 2044
Cdd:cd05614   154 EFLTEEkertysfCGTIEYMAPEIIRGKsGHGKAVDWWSLGILMFELLTGASPFTLegEKNTQSEVSRR-ILKCDPPFPS 232
                         250       260
                  ....*....|....*....|....
gi 124804138 2045 SISSSAKDLISKLLELNVEKRISA 2068
Cdd:cd05614   233 FIGPVARDLLQKLLCKDPKKRLGA 256
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
1821-2072 2.72e-33

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: 130.61  E-value: 2.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd08529     2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAET--RLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLSTLCAPNELL- 1977
Cdd:cd08529    82 ENGDLHSLIKSQRgrPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLD---KGDNVKIGDLGVAKILSDTTNFa 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpinkntEMNIQKNYVLSFKDYIWKSISSSAK----DL 2053
Cdd:cd08529   159 QTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPF------EAQNQGALILKIVRGKYPPISASYSqdlsQL 232
                         250
                  ....*....|....*....
gi 124804138 2054 ISKLLELNVEKRISANEAL 2072
Cdd:cd08529   233 IDSCLTKDYRQRPDTTELL 251
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
1826-2075 3.08e-33

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: 130.92  E-value: 3.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1826 QLGQGKFSTVYRGINKQTNSEFAIKvidkRSVSIYEKEL--LRSEISIL-RLLRHPNVI--YLKEII---NTKETLyISM 1897
Cdd:cd13985     7 QLGEGGFSYVYLAHDVNTGRRYALK----RMYFNDEEQLrvAIKEIEIMkRLCGHPNIVqyYDSAILsseGRKEVL-LLM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVkGGELYDFL--LAETRLSEIHANKIITQLIKTVAYLHRCG--IIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAP 1973
Cdd:cd13985    82 EYC-PGSLVDILekSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSN---TGRFKLCDFGSATTEHY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1974 NELLKEPCG----------TLAYVAPEVITLQGY---NHKVDAWSIGIILYLLLSGKLPFpiNKNTEMNIQ-KNYVLSFK 2039
Cdd:cd13985   158 PLERAEEVNiieeeiqkntTPMYRAPEMIDLYSKkpiGEKADIWALGCLLYKLCFFKLPF--DESSKLAIVaGKYSIPEQ 235
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 124804138 2040 DYIWKSIsssaKDLISKLLELNVEKRISANEALEHI 2075
Cdd:cd13985   236 PRYSPEL----HDLIRHMLTPDPAERPDIFQVINII 267
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
1821-2083 3.33e-33

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: 131.70  E-value: 3.33e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQ-LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLrseisilrlLRHPNVIYLKEIINTKETLY----- 1894
Cdd:cd14170     3 YKVTSQvLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELH---------WRASQCPHIVRIVDVYENLYagrkc 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 --ISMELVKGGELYDFLL--AETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTL 1970
Cdd:cd14170    74 llIVMECLDGGELFSRIQdrGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1971 CAPNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMN--IQKNYVL---SFKDYIWKS 2045
Cdd:cd14170   154 TTSHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISpgMKTRIRMgqyEFPNPEWSE 233
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 124804138 2046 ISSSAKDLISKLLELNVEKRISANEALEHIWVKNPTAV 2083
Cdd:cd14170   234 VSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQSTKV 271
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
1821-2078 4.06e-33

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: 131.38  E-value: 4.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSiyEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd06655    21 YTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQP--KKELIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDfLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCAPNELLKEP 1980
Cdd:cd06655    99 AGGSLTD-VVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLL---GMDGSVKLTDFGFCAQITPEQSKRST 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 -CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpINKNTEMN---IQKNYVLSFKDYiwKSISSSAKDLISK 2056
Cdd:cd06655   175 mVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY-LNENPLRAlylIATNGTPELQNP--EKLSPIFRDFLNR 251
                         250       260
                  ....*....|....*....|..
gi 124804138 2057 LLELNVEKRISANEALEHIWVK 2078
Cdd:cd06655   252 CLEMDVEKRGSAKELLQHPFLK 273
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
1819-2074 4.12e-33

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: 130.90  E-value: 4.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELHEQLGQGKFSTVYRGINKQTNSEFAIK-VIDKRSVSIYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISM 1897
Cdd:cd07833     1 NKYEVLGVVGEGAYGVVLKCRNKATGEIVAIKkFKESEDDEDVKKTALR-EVKVLRQLRHENIVNLKEAFRRKGRLYLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTL--CAPNE 1975
Cdd:cd07833    80 EYVERTLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILV---SESGVLKLCDFGFARAltARPAS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1976 LLKEPCGTLAYVAPEVitLQG---YNHKVDAWSIGIILYLLLSGKLPFP----------INK------------------ 2024
Cdd:cd07833   157 PLTDYVATRWYRAPEL--LVGdtnYGKPVDVWAIGCIMAELLDGEPLFPgdsdidqlylIQKclgplppshqelfssnpr 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 124804138 2025 -NTEMNIQKNYVLSFKDYIWKSISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd07833   235 fAGVAFPEPSQPESLERRYPGKVSSPALDFLKACLRMDPKERLTCDELLQH 285
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
1821-2074 4.58e-33

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: 130.96  E-value: 4.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdkrsvSIYEKE-----LLRsEISILRLLRHPNVIYLKEIINTKETLYI 1895
Cdd:cd07844     2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEI-----RLEHEEgapftAIR-EASLLKDLKHANIVTLHDIIHTKKTLTL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1896 SMELVKGgELYDFLLAETRLSEIHANKIIT-QLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLS------ 1968
Cdd:cd07844    76 VFEYLDT-DLKQYMDDCGGGLSMHNVRLFLfQLLRGLAYCHQRRVLHRDLKPQNLLISER---GELKLADFGLAraksvp 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1969 TLCAPNELLkepcgTLAYVAPEVitLQG---YNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQK------------- 2032
Cdd:cd07844   152 SKTYSNEVV-----TLWYRPPDV--LLGsteYSTSLDMWGVGCIFYEMATGRPLFPGSTDVEDQLHKifrvlgtpteetw 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 124804138 2033 -------NYV-LSFKDY-------IWKSIS--SSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd07844   225 pgvssnpEFKpYSFPFYpprplinHAPRLDriPHGEELALKFLQYEPKKRISAAEAMKH 283
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
1827-2073 5.15e-33

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: 130.11  E-value: 5.15e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVI-----YLKEIintkeTLYISMELVK 1901
Cdd:cd13996    14 LGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSASEKVLR-EVKALAKLNHPNIVryytaWVEEP-----PLYIQMELCE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1902 GGELYDFLLAETRLSEIHAN---KIITQLIKTVAYLHRCGIIHRDIKPENILLTdkSRDAQIKLTDFGLSTLCAPNELLK 1978
Cdd:cd13996    88 GGTLRDWIDRRNSSSKNDRKlalELFKQILKGVSYIHSKGIVHRDLKPSNIFLD--NDDLQVKIGDFGLATSIGNQKREL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1979 EP---------------CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSgklPFpinkNTEM---NIQKNyvlsFKD 2040
Cdd:cd13996   166 NNlnnnnngntsnnsvgIGTPLYASPEQLDGENYNEKADIYSLGIILFEMLH---PF----KTAMersTILTD----LRN 234
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 124804138 2041 YIWKSISSSA----KDLISKLLELNVEKRISANEALE 2073
Cdd:cd13996   235 GILPESFKAKhpkeADLIQSLLSKNPEERPSAEQLLR 271
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
1821-2074 5.61e-33

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: 130.52  E-value: 5.61e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKV--------IDKRSVsiYEKELLRsEISILRLLRHPNVIYLKEIINT-KE 1891
Cdd:cd13990     2 YLLLNLLGKGGFSEVYKAFDLVEQRYVACKIhqlnkdwsEEKKQN--YIKHALR-EYEIHKSLDHPRIVKLYDVFEIdTD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1892 TLYISMELVKGGELyDFLLAETR-LSEIHANKIITQLIKTVAYL--HRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLS 1968
Cdd:cd13990    79 SFCTVLEYCDGNDL-DFYLKQHKsIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSGNVSGEIKITDFGLS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1969 TLCAPN-------ELLKEPCGTLAYVAPEVITLQG----YNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYVLS 2037
Cdd:cd13990   158 KIMDDEsynsdgmELTSQGAGTYWYLPPECFVVGKtppkISSKVDVWSVGVIFYQMLYGRKPFGHNQSQEAILEENTILK 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 124804138 2038 FKDYIWKS---ISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd13990   238 ATEVEFPSkpvVSSEAKDFIRRCLTYRKEDRPDVLQLAND 277
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
1821-2081 5.68e-33

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: 130.25  E-value: 5.68e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSvsiyEKEL--LRSEISILRLLRHPNVIYLKEIINTKETLYISME 1898
Cdd:cd06611     7 WEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIES----EEELedFMVEIDILSECKHPNIVGLYEAYFYENKLWILIE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFLLA-ETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLSTLCApNELL 1977
Cdd:cd06611    83 FCDGGALDSIMLElERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLT---LDGDVKLADFGVSAKNK-STLQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPC--GTLAYVAPEVITL-----QGYNHKVDAWSIGIILYLLLSGKLPfpinkNTEMNIQKnyVLsFKdyIWKS----- 2045
Cdd:cd06611   159 KRDTfiGTPYWMAPEVVACetfkdNPYDYKADIWSLGITLIELAQMEPP-----HHELNPMR--VL-LK--ILKSepptl 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 124804138 2046 -----ISSSAKDLISKLLELNVEKRISANEALEHIWVKNPT 2081
Cdd:cd06611   229 dqpskWSSSFNDFLKSCLVKDPDDRPTAAELLKHPFVSDQS 269
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
1821-2078 5.70e-33

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: 131.00  E-value: 5.70e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSiyEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd06656    21 YTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQP--KKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDfLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCAPNELLKEP 1980
Cdd:cd06656    99 AGGSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL---GMDGSVKLTDFGFCAQITPEQSKRST 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 -CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpINKNTEMN---IQKNYVLSFKDYiwKSISSSAKDLISK 2056
Cdd:cd06656   175 mVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY-LNENPLRAlylIATNGTPELQNP--ERLSAVFRDFLNR 251
                         250       260
                  ....*....|....*....|..
gi 124804138 2057 LLELNVEKRISANEALEHIWVK 2078
Cdd:cd06656   252 CLEMDVDRRGSAKELLQHPFLK 273
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
1821-2086 7.04e-33

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: 131.72  E-value: 7.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRS-VSIYEKELLRsEISILRLLRHPNVIYLKEIINTKETL------ 1893
Cdd:cd07855     7 YEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFdVVTTAKRTLR-ELKILRHFKHDNIIAIRDILRPKVPYadfkdv 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1894 YISMELVKGgELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAP 1973
Cdd:cd07855    86 YVVLDLMES-DLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNE---NCELKIGDFGMARGLCT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1974 NEL-----LKEPCGTLAYVAPEVI-TLQGYNHKVDAWSIGIILYLLLSGKLPFPiNKNTEMNIQ---------------- 2031
Cdd:cd07855   162 SPEehkyfMTEYVATRWYRAPELMlSLPEYTQAIDMWSVGCIFAEMLGRRQLFP-GKNYVHQLQliltvlgtpsqavina 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124804138 2032 ------KNYVLSFKDY-------IWKSISSSAKDLISKLLELNVEKRISANEALEHIWVKNPTAVINE 2086
Cdd:cd07855   241 igadrvRRYIQNLPNKqpvpwetLYPKADQQALDLLSQMLRFDPSERITVAEALQHPFLAKYHDPDDE 308
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
1821-2078 7.76e-33

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: 130.61  E-value: 7.76e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSiyEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd06654    22 YTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQP--KKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDfLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCAPNELLKEP 1980
Cdd:cd06654   100 AGGSLTD-VVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILL---GMDGSVKLTDFGFCAQITPEQSKRST 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 -CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpINKNTEMN---IQKNYVLSFKDYiwKSISSSAKDLISK 2056
Cdd:cd06654   176 mVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY-LNENPLRAlylIATNGTPELQNP--EKLSAIFRDFLNR 252
                         250       260
                  ....*....|....*....|..
gi 124804138 2057 LLELNVEKRISANEALEHIWVK 2078
Cdd:cd06654   253 CLEMDVEKRGSAKELLQHQFLK 274
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
1821-2074 1.04e-32

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: 129.34  E-value: 1.04e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRsvsiyEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd14010     2 YVLYDEIGRGKHSVVYKGRRKGTIEFVAIKCVDKS-----KRPEVLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtDKSrdAQIKLTDFGLStlCAPNELLKEP 1980
Cdd:cd14010    77 TGGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILL-DGN--GTLKLSDFGLA--RREGEILKEL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 CGTLA-------------------YVAPEVitLQGYNHKV--DAWSIGIILYLLLSGKLPFPINKNTEM--NIQKNYVLS 2037
Cdd:cd14010   152 FGQFSdegnvnkvskkqakrgtpyYMAPEL--FQGGVHSFasDLWALGCVLYEMFTGKPPFVAESFTELveKILNEDPPP 229
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 124804138 2038 FKDYIWKSISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd14010   230 PPPKVSSKPSPDFKSLLKGLLEKDPAKRLSWDELVKH 266
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
1821-2074 1.19e-32

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: 131.27  E-value: 1.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVIYLKEII--NTKETL---YI 1895
Cdd:cd07849     7 YQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISPFEHQTYCLRTLR-EIKILLRFKHENIIGILDIQrpPTFESFkdvYI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1896 SMELVKGgELYDfLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCAPNE 1975
Cdd:cd07849    86 VQELMET-DLYK-LIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLL---NTNCDLKICDFGLARIADPEH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1976 ----LLKEPCGTLAYVAPEV-ITLQGYNHKVDAWSIGIILYLLLSGKLPFP--------------INKNTEMNIQ----- 2031
Cdd:cd07849   161 dhtgFLTEYVATRWYRAPEImLNSKGYTKAIDIWSVGCILAEMLSNRPLFPgkdylhqlnlilgiLGTPSQEDLNciisl 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 124804138 2032 --KNYVLS--FKDYI-WKSI----SSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd07849   241 kaRNYIKSlpFKPKVpWNKLfpnaDPKALDLLDKMLTFNPHKRITVEEALAH 292
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
1821-2077 1.37e-32

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: 129.30  E-value: 1.37e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSV------------------------SIYEKELLRSEISILRLLR 1876
Cdd:cd14200     2 YKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKLlkqygfprrppprgskaaqgeqakPLAPLERVYQEIAILKKLD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1877 HPNVIYLKEIIN--TKETLYISMELVKGGELYDfLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDk 1954
Cdd:cd14200    82 HVNIVKLIEVLDdpAEDNLYMVFDLLRKGPVME-VPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGD- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1955 srDAQIKLTDFGLSTLCAPNE-LLKEPCGTLAYVAPEVI--TLQGYNHK-VDAWSIGIILYLLLSGKLPFpINKN--TEM 2028
Cdd:cd14200   160 --DGHVKIADFGVSNQFEGNDaLLSSTAGTPAFMAPETLsdSGQSFSGKaLDVWAMGVTLYCFVYGKCPF-IDEFilALH 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 124804138 2029 NIQKNYVLSFKDYiwKSISSSAKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14200   237 NKIKNKPVEFPEE--PEISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
1821-2078 1.81e-32

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: 130.76  E-value: 1.81e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVI-DKRSVSIYEKELLRsEISILRLLR-HPNVIYLKEII---NTKEtLYI 1895
Cdd:cd07852     9 YEILKKLGKGAYGIVWKAIDKKTGEVVALKKIfDAFRNATDAQRTFR-EIMFLQELNdHPNIIKLLNVIraeNDKD-IYL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1896 SMELVkggelydfllaETRLS---------EIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFG 1966
Cdd:cd07852    87 VFEYM-----------ETDLHaviranileDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILL---NSDCRVKLADFG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1967 LS------TLCAPNELLKEPCGTLAYVAPEVitLQG---YNHKVDAWSIGIILYLLLSGKLPFP--------------IN 2023
Cdd:cd07852   153 LArslsqlEEDDENPVLTDYVATRWYRAPEI--LLGstrYTKGVDMWSVGCILGEMLLGKPLFPgtstlnqlekiievIG 230
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124804138 2024 KNTEMNIQ-------------------KNYVLSFKDYiwksiSSSAKDLISKLLELNVEKRISANEALEHIWVK 2078
Cdd:cd07852   231 RPSAEDIEsiqspfaatmleslppsrpKSLDELFPKA-----SPDALDLLKKLLVFNPNKRLTAEEALRHPYVA 299
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
1827-2068 2.45e-32

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: 129.70  E-value: 2.45e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVsIYEKE---LLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGG 1903
Cdd:cd05603     3 IGKGSFGKVLLAKRKCDGKFYAVKVLQKKTI-LKKKEqnhIMAERNVLLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 ELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdksrDAQ--IKLTDFGlstLCA----PNELL 1977
Cdd:cd05603    82 ELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILL-----DCQghVVLTDFG---LCKegmePEETT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMniqKNYVLSFKDYIWKSISSSAKDLISKL 2057
Cdd:cd05603   154 STFCGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQM---YDNILHKPLHLPGGKTVAACDLLQGL 230
                         250
                  ....*....|.
gi 124804138 2058 LELNVEKRISA 2068
Cdd:cd05603   231 LHKDQRRRLGA 241
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
1821-2074 3.09e-32

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: 128.77  E-value: 3.09e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIK--VIDKRsvsiyekelLRS-EISILRLLRHPNVIYLKEIINTKET----- 1892
Cdd:cd14137     6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIKkvLQDKR---------YKNrELQIMRRLKHPNIVKLKYFFYSSGEkkdev 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1893 -LYISMELVkGGELYDFL----LAETRLSEIHAnKIIT-QLIKTVAYLHRCGIIHRDIKPENILLTDKSrdAQIKLTDFG 1966
Cdd:cd14137    77 yLNLVMEYM-PETLYRVIrhysKNKQTIPIIYV-KLYSyQLFRGLAYLHSLGICHRDIKPQNLLVDPET--GVLKLCDFG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1967 LSTLCAPNELLKEPCGTLAYVAPEVItL--QGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEM---------------- 2028
Cdd:cd14137   153 SAKRLVPGEPNVSYICSRYYRAPELI-FgaTDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQlveiikvlgtptreqi 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 124804138 2029 -NIQKNYVlSFKDYIWKSISSS----------AKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd14137   232 kAMNPNYT-EFKFPQIKPHPWEkvfpkrtppdAIDLLSKILVYNPSKRLTALEALAH 287
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
1827-2074 3.59e-32

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: 129.36  E-value: 3.59e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIdKRSVSIYEKELLRS--EISILRLLRHPNVIYLKEIINTKETLYISMELVKGGE 1904
Cdd:cd05595     3 LGKGTFGKVILVREKATGRYYAMKIL-RKEVIIAKDEVAHTvtESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCAPNE-LLKEPCGT 1983
Cdd:cd05595    82 LFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLML---DKDGHIKITDFGLCKEGITDGaTMKTFCGT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1984 LAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpINKNTEMNIQKnyVLSFKDYIWKSISSSAKDLISKLLELNVE 2063
Cdd:cd05595   159 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF-YNQDHERLFEL--ILMEEIRFPRTLSPEAKSLLAGLLKKDPK 235
                         250
                  ....*....|....*.
gi 124804138 2064 KRI-----SANEALEH 2074
Cdd:cd05595   236 QRLgggpsDAKEVMEH 251
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
1819-2074 6.47e-32

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: 126.18  E-value: 6.47e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELHEQLGQGKFSTVYRGINKQT-------NSEFAIKVIDKRSVS--IYekellrSEISILRLLR-HPNVIYLKEIIN 1888
Cdd:cd14019     1 NKYRIIEKIGEGTFSSVYKAEDKLHdlydrnkGRLVALKHIYPTSSPsrIL------NELECLERLGgSNNVSGLITAFR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1889 TKETLYISMELVKGGELYDFL----LAETRlseihanKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRdaQIKLTD 1964
Cdd:cd14019    75 NEDQVVAVLPYIEHDDFRDFYrkmsLTDIR-------IYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRETG--KGVLVD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1965 FGLSTLCAPNELLKEPC-GTLAYVAPEVitLQGYNH---KVDAWSIGIILYLLLSGKLPFpINKNTEMNIQKNYVLSFKd 2040
Cdd:cd14019   146 FGLAQREEDRPEQRAPRaGTRGFRAPEV--LFKCPHqttAIDIWSAGVILLSILSGRFPF-FFSSDDIDALAEIATIFG- 221
                         250       260       270
                  ....*....|....*....|....*....|....
gi 124804138 2041 yiwksiSSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd14019   222 ------SDEAYDLLDKLLELDPSKRITAEEALKH 249
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
1819-2077 9.92e-32

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: 126.65  E-value: 9.92e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDkrsVSIYEKELLRSEISILRLL-RHPNVI-----YLKEIINTKE- 1891
Cdd:cd06608     6 GIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMD---IIEDEEEEIKLEINILRKFsNHPNIAtfygaFIKKDPPGGDd 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1892 TLYISMELVKGGELYD----FLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGL 1967
Cdd:cd06608    83 QLWLVMEYCGGGSVTDlvkgLRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLT---EEAEVKLVDFGV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1968 STLCAPNELLKEPC-GTLAYVAPEVITL-----QGYNHKVDAWSIGIILYLLLSGKLPF------------PINKNTEMN 2029
Cdd:cd06608   160 SAQLDSTLGRRNTFiGTPYWMAPEVIACdqqpdASYDARCDVWSLGITAIELADGKPPLcdmhpmralfkiPRNPPPTLK 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 124804138 2030 IQKNYVLSFKDYiwksisssakdlISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd06608   240 SPEKWSKEFNDF------------ISECLIKNYEQRPFTEELLEHPFI 275
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
1825-2078 1.11e-31

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: 126.77  E-value: 1.11e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVI-YLKEIINTKET-LYISMELVKG 1902
Cdd:cd06621     7 SSLGEGAGGSVTKCRLRNTKTIFALKTITTDPNPDVQKQILR-ELEINKSCASPYIVkYYGAFLDEQDSsIGIAMEYCEG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1903 GEL---YDFLLAET-RLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLSTLcAPNELLK 1978
Cdd:cd06621    86 GSLdsiYKKVKKKGgRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLT---RKGQVKLCDFGVSGE-LVNSLAG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1979 EPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMN-------IQKNYVLSFKDYIWKSI--SSS 2049
Cdd:cd06621   162 TFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPPLGpiellsyIVNMPNPELKDEPENGIkwSES 241
                         250       260
                  ....*....|....*....|....*....
gi 124804138 2050 AKDLISKLLELNVEKRISANEALEHIWVK 2078
Cdd:cd06621   242 FKDFIEKCLEKDGTRRPGPWQMLAHPWIK 270
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
1821-2074 1.26e-31

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: 127.81  E-value: 1.26e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDK------RSVSIYEKELlrseiSILRLLRHPNVIYLKEIINTKETLY 1894
Cdd:cd05601     3 FEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKsetlaqEEVSFFEEER-----DIMAKANSPWITKLQYAFQDSENLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVKGGELYDfLLA--ETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCA 1972
Cdd:cd05601    78 LVMEYHPGGDLLS-LLSryDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILI---DRTGHIKLADFGSAAKLS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1973 PNELL--KEPCGTLAYVAPEVITL------QGYNHKVDAWSIGIILYLLLSGKLPFpinknTEMNIQKNY--VLSFKDYI 2042
Cdd:cd05601   154 SDKTVtsKMPVGTPDYIAPEVLTSmnggskGTYGVECDWWSLGIVAYEMLYGKTPF-----TEDTVIKTYsnIMNFKKFL 228
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 124804138 2043 W----KSISSSAKDLISKLLElNVEKRISANEALEH 2074
Cdd:cd05601   229 KfpedPKVSESAVDLIKGLLT-DAKERLGYEGLCCH 263
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
1820-2077 1.30e-31

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: 125.70  E-value: 1.30e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1820 LYELHEQ-LGQGKFSTVYRGINKQTNSEFAIKVIdkrsvsiYEKELLRSEISILRLLRHPNVIYLKEIINT-KETLYISM 1897
Cdd:cd14109     4 LYEIGEEdEKRAAQGAPFHVTERSTGRNFLAQLR-------YGDPFLMREVDIHNSLDHPNIVQMHDAYDDeKLAVTVID 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGGELYDFLLAETR--LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdaQIKLTDFGLSTLCAPNE 1975
Cdd:cd14109    77 NLASTIELVRDNLLPGKdyYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDD----KLKLADFGQSRRLLRGK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1976 LLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF-PINKNTEMNIQKNYVLSFKDYIWKSISSSAKDLI 2054
Cdd:cd14109   153 LTTLIYGSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFlGDNDRETLTNVRSGKWSFDSSPLGNISDDARDFI 232
                         250       260
                  ....*....|....*....|...
gi 124804138 2055 SKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14109   233 KKLLVYIPESRLTVDEALNHPWF 255
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
1828-2078 1.35e-31

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: 127.73  E-value: 1.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1828 GQGKFSTVYRGINKQTNSEFAIKVIDKRSvsIYEKELL---RSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGE 1904
Cdd:cd05599    10 GRGAFGEVRLVRKKDTGHVYAMKKLRKSE--MLEKEQVahvRAERDILAEADNPWVVKLYYSFQDEENLYLIMEFLPGGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLSTLCAPNELLKEPCGTL 1984
Cdd:cd05599    88 MMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLD---ARGHIKLSDFGLCTGLKKSHLAYSTVGTP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1985 AYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTE-----MNIQKNyvLSFKDYIwkSISSSAKDLISKLLe 2059
Cdd:cd05599   165 DYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQEtcrkiMNWRET--LVFPPEV--PISPEAKDLIERLL- 239
                         250       260
                  ....*....|....*....|..
gi 124804138 2060 LNVEKRI---SANEALEHIWVK 2078
Cdd:cd05599   240 CDAEHRLganGVEEIKSHPFFK 261
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
1827-2074 1.59e-31

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: 125.85  E-value: 1.59e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGInKQTNSEFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGELY 1906
Cdd:cd14066     1 IGSGGFGTVYKGV-LENGTVVAVKRLNEMNCAASKKEFLT-ELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1907 DFLLA---------ETRLseihanKIITQLIKTVAYLH---RCGIIHRDIKPENILLtDKSRDAqiKLTDFGLSTLCAPN 1974
Cdd:cd14066    79 DRLHChkgspplpwPQRL------KIAKGIARGLEYLHeecPPPIIHGDIKSSNILL-DEDFEP--KLTDFGLARLIPPS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1975 ELLKE---PCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNiqknyvlsfkdyiwKSISSSAK 2051
Cdd:cd14066   150 ESVSKtsaVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRENASR--------------KDLVEWVE 215
                         250       260
                  ....*....|....*....|...
gi 124804138 2052 DLISKLLELNVEKRISANEALEH 2074
Cdd:cd14066   216 SKGKEELEDILDKRLVDDDGVEE 238
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
1821-2076 2.81e-31

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: 126.91  E-value: 2.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdkRSVSIYeKELLRSEISILRLLRH------PNVIYLKEIINTKETLY 1894
Cdd:cd14134    14 YKILRLLGEGTFGKVLECWDRKRKRYVAVKII--RNVEKY-REAAKIEIDVLETLAEkdpngkSHCVQLRDWFDYRGHMC 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVkGGELYDFLLAET----RLSEIHAnkIITQLIKTVAYLHRCGIIHRDIKPENILLTDKS--------------- 1955
Cdd:cd14134    91 IVFELL-GPSLYDFLKKNNygpfPLEHVQH--IAKQLLEAVAFLHDLKLTHTDLKPENILLVDSDyvkvynpkkkrqirv 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1956 -RDAQIKLTDFGLSTLcaPNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTE----M-- 2028
Cdd:cd14134   168 pKSTDIKLIDFGSATF--DDEYHSSIVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLFQTHDNLEhlamMer 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 2029 -------NIQKNYVLSFKDYI-------WKSISSSAK------------------------DLISKLLELNVEKRISANE 2070
Cdd:cd14134   246 ilgplpkRMIRRAKKGAKYFYfyhgrldWPEGSSSGRsikrvckplkrlmllvdpehrllfDLIRKMLEYDPSKRITAKE 325

                  ....*.
gi 124804138 2071 ALEHIW 2076
Cdd:cd14134   326 ALKHPF 331
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
1827-2073 3.73e-31

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: 124.46  E-value: 3.73e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKF--STVYRGInkQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVI-YLKEIINtKETLYISMELVKGG 1903
Cdd:cd08221     8 LGRGAFgeAVLYRKT--EDNSLVVWKEVNLSRLSEKERRDALNEIDILSLLNHDNIItYYNHFLD-GESLFIEMEYCNGG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 ELYDFLLAETR--LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLSTLCAPNELLKEPC 1981
Cdd:cd08221    85 NLHDKIAQQKNqlFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLT---KADLVKLGDFGISKVLDSESSMAESI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1982 -GTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF----PINKNTEMnIQKNYVLSFKDYiwksiSSSAKDLISK 2056
Cdd:cd08221   162 vGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFdatnPLRLAVKI-VQGEYEDIDEQY-----SEEIIQLVHD 235
                         250
                  ....*....|....*..
gi 124804138 2057 LLELNVEKRISANEALE 2073
Cdd:cd08221   236 CLHQDPEDRPTAEELLE 252
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
1821-2073 4.99e-31

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: 124.31  E-value: 4.99e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDkrsvsIYE--KELLRS----EISILRLLRHPNVI-YLKEIINTKEtL 1893
Cdd:cd08224     2 YEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQ-----IFEmmDAKARQdclkEIDLLQQLNHPNIIkYLASFIENNE-L 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1894 YISMELVKGGEL----YDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLS- 1968
Cdd:cd08224    76 NIVLELADAGDLsrliKHFKKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFIT---ANGVVKLGDLGLGr 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1969 -----TLCApNELLkepcGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpinKNTEMNIqknYVLSFK---- 2039
Cdd:cd08224   153 ffsskTTAA-HSLV----GTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPF---YGEKMNL---YSLCKKiekc 221
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 124804138 2040 DY--IWKSI-SSSAKDLISKLLELNVEKRISANEALE 2073
Cdd:cd08224   222 EYppLPADLySQELRDLVAACIQPDPEKRPDISYVLD 258
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
1820-2074 8.21e-31

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: 124.71  E-value: 8.21e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1820 LYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSiyEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd06659    22 LLENYVKIGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQ--RRELLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEY 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDfLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGlstLCA------P 1973
Cdd:cd06659   100 LQGGALTD-IVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLT---LDGRVKLSDFG---FCAqiskdvP 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1974 NEllKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF----PINKNTEMNIQ-----KNYvlsfkdyiwK 2044
Cdd:cd06659   173 KR--KSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYfsdsPVQAMKRLRDSpppklKNS---------H 241
                         250       260       270
                  ....*....|....*....|....*....|
gi 124804138 2045 SISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd06659   242 KASPVLRDFLERMLVRDPQERATAQELLDH 271
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
1819-2087 1.35e-30

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: 123.60  E-value: 1.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLrsEISILRLLRHPNVIYLKEIINTKETLYISME 1898
Cdd:cd06643     5 DFWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELEDYMV--EIDILASCDHPNIVKLLDAFYYENNLWILIE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFLLA-ETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLS-----TLCA 1972
Cdd:cd06643    83 FCAGGAVDAVMLElERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFT---LDGDIKLADFGVSakntrTLQR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1973 PNELLkepcGTLAYVAPEVITLQG-----YNHKVDAWSIGIILYLLLSGKLPfpinkNTEMN-------IQKNYVLSF-K 2039
Cdd:cd06643   160 RDSFI----GTPYWMAPEVVMCETskdrpYDYKADVWSLGVTLIEMAQIEPP-----HHELNpmrvllkIAKSEPPTLaQ 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 124804138 2040 DYIWksiSSSAKDLISKLLELNVEKRISANEALEHIWVknptAVINEN 2087
Cdd:cd06643   231 PSRW---SPEFKDFLRKCLEKNVDARWTTSQLLQHPFV----SVLVSN 271
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
1827-2075 1.98e-30

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: 124.30  E-value: 1.98e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSV--SIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGE 1904
Cdd:cd05604     4 IGKGSFGKVLLAKRKRDGKYYAVKVLQKKVIlnRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVNGGE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTL-CAPNELLKEPCGT 1983
Cdd:cd05604    84 LFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQ---GHIVLTDFGLCKEgISNSDTTTTFCGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1984 LAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEM--NI-QKNYVLSfkdyiwKSISSSAKDLISKLLEL 2060
Cdd:cd05604   161 PEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMyeNIlHKPLVLR------PGISLTAWSILEELLEK 234
                         250
                  ....*....|....*
gi 124804138 2061 NVEKRISANEALEHI 2075
Cdd:cd05604   235 DRQLRLGAKEDFLEI 249
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
1826-2073 2.97e-30

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: 123.97  E-value: 2.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1826 QLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVsiyekeLLRSEIS-------ILRLLRHPNVIYLKEIINTKETLYISME 1898
Cdd:cd05598     8 TIGVGAFGEVSLVRKKDTNALYAMKTLRKKDV------LKRNQVAhvkaerdILAEADNEWVVKLYYSFQDKENLYFVMD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLST--------- 1969
Cdd:cd05598    82 YIPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILI---DRDGHIKLTDFGLCTgfrwthdsk 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1970 -LCApNELLkepcGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQ-KNYVLSFKDYIWKSIS 2047
Cdd:cd05598   159 yYLA-HSLV----GTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKvINWRTTLKIPHEANLS 233
                         250       260
                  ....*....|....*....|....*.
gi 124804138 2048 SSAKDLISKLLeLNVEKRISANEALE 2073
Cdd:cd05598   234 PEAKDLILRLC-CDAEDRLGRNGADE 258
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
1827-2066 3.18e-30

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: 123.65  E-value: 3.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEK-ELLRSEISILRL-LRHPNVIYLKEIINTKETLYISMELVKGGE 1904
Cdd:cd05592     3 LGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDDDvECTMIERRVLALaSQHPFLTHLFCTFQTESHLFFVMEYLNGGD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLstlCAPNELLKEP---- 1980
Cdd:cd05592    83 LMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLL---DREGHIKIADFGM---CKENIYGENKastf 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEM--NIQKNYVlsfkdYIWKSISSSAKDLISKLL 2058
Cdd:cd05592   157 CGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELfwSICNDTP-----HYPRWLTKEAASCLSLLL 231

                  ....*...
gi 124804138 2059 ELNVEKRI 2066
Cdd:cd05592   232 ERNPEKRL 239
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
1827-2079 3.57e-30

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 123.72  E-value: 3.57e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKE-------------LLRsEISILRLLRHPNVIYLKEIINTKETL 1893
Cdd:PTZ00024   17 LGEGTYGKVEKAYDTLTGKIVAIKKVKIIEISNDVTKdrqlvgmcgihftTLR-ELKIMNEIKHENIMGLVDVYVEGDFI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1894 YISMELVKGgELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLC-- 1971
Cdd:PTZ00024   96 NLVMDIMAS-DLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSK---GICKIADFGLARRYgy 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1972 -------------APNELLKEPCGTLAYVAPEVitLQG---YNHKVDAWSIGIILYLLLSGKLPFPiNKNTEMNIQKNYV 2035
Cdd:PTZ00024  172 ppysdtlskdetmQRREEMTSKVVTLWYRAPEL--LMGaekYHFAVDMWSVGCIFAELLTGKPLFP-GENEIDQLGRIFE 248
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124804138 2036 L---------------------------SFKDYIwKSISSSAKDLISKLLELNVEKRISANEALEHIWVKN 2079
Cdd:PTZ00024  249 LlgtpnednwpqakklplyteftprkpkDLKTIF-PNASDDAIDLLQSLLKLNPLERISAKEALKHEYFKS 318
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
1821-2074 5.15e-30

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: 123.28  E-value: 5.15e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVidKRSVSIYEKELL--RS--EISILRLLR-HPNV--IYLKEIINTK--E 1891
Cdd:cd07857     2 YELIKELGQGAYGIVCSARNAETSEEETVAI--KKITNVFSKKILakRAlrELKLLRHFRgHKNItcLYDMDIVFPGnfN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1892 TLYISMELVKGgELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLSTLC 1971
Cdd:cd07857    80 ELYLYEELMEA-DLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVN---ADCELKICDFGLARGF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1972 APN-----ELLKEPCGTLAYVAPEV-ITLQGYNHKVDAWSIGIILYLLLSGKlPFPINKN---------------TEMNI 2030
Cdd:cd07857   156 SENpgenaGFMTEYVATRWYRAPEImLSFQSYTKAIDVWSVGCILAELLGRK-PVFKGKDyvdqlnqilqvlgtpDEETL 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 124804138 2031 QK-------NYVLSFKDYIWKSISSS-------AKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd07857   235 SRigspkaqNYIRSLPNIPKKPFESIfpnanplALDLLEKLLAFDPTKRISVEEALEH 292
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
1827-2073 5.20e-30

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: 122.68  E-value: 5.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRS-VSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGEL 1905
Cdd:cd05585     2 IGKGSFGKVMQVRKKDTSRIYALKTIRKAHiVSRSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1906 YDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTL-CAPNELLKEPCGTL 1984
Cdd:cd05585    82 FHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILL---DYTGHIALCDFGLCKLnMKDDDKTNTFCGTP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1985 AYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpINKNTEMNIQK--NYVLSFKDyiwkSISSSAKDLISKLLELNV 2062
Cdd:cd05585   159 EYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPF-YDENTNEMYRKilQEPLRFPD----GFDRDAKDLLIGLLNRDP 233
                         250
                  ....*....|.
gi 124804138 2063 EKRISANEALE 2073
Cdd:cd05585   234 TKRLGYNGAQE 244
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
1827-2075 6.53e-30

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: 123.20  E-value: 6.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSV--SIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGE 1904
Cdd:cd05602    15 IGKGSFGKVLLARHKSDEKFYAVKVLQKKAIlkKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDKLYFVLDYINGGE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTL-CAPNELLKEPCGT 1983
Cdd:cd05602    95 LFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQ---GHIVLTDFGLCKEnIEPNGTTSTFCGT 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1984 LAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEM--NIQkNYVLSFKdyiwKSISSSAKDLISKLLELN 2061
Cdd:cd05602   172 PEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMydNIL-NKPLQLK----PNITNSARHLLEGLLQKD 246
                         250
                  ....*....|....
gi 124804138 2062 VEKRISANEALEHI 2075
Cdd:cd05602   247 RTKRLGAKDDFTEI 260
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
1821-2076 6.93e-30

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: 121.95  E-value: 6.93e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdkrsvsIYEKEL-------LRsEISILRLLRHPNVIYLKEII--NTKE 1891
Cdd:cd07843     7 YEKLNRIEEGTYGVVYRARDKKTGEIVALKKL------KMEKEKegfpitsLR-EINILLKLQHPNIVTVKEVVvgSNLD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1892 TLYISMELVKGgELYDFLlaET-----RLSEIHAnkIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFG 1966
Cdd:cd07843    80 KIYMVMEYVEH-DLKSLM--ETmkqpfLQSEVKC--LMLQLLSGVAHLHDNWILHRDLKTSNLLLNNR---GILKICDFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1967 LSTLCA-PNELLKEPCGTLAYVAPEVitLQG---YNHKVDAWSIGIILYLLLSGKLPFP-------INK-------NTEM 2028
Cdd:cd07843   152 LAREYGsPLKPYTQLVVTLWYRAPEL--LLGakeYSTAIDMWSVGCIFAELLTKKPLFPgkseidqLNKifkllgtPTEK 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124804138 2029 N---------------IQKNYVLSFKDYIWKSISSSAKDLISKLLELNVEKRISANEALEHIW 2076
Cdd:cd07843   230 IwpgfselpgakkktfTKYPYNQLRKKFPALSLSDNGFDLLNRLLTYDPAKRISAEDALKHPY 292
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
1827-2074 1.70e-29

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: 119.35  E-value: 1.70e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSI-YEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGEL 1905
Cdd:cd14188     9 LGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKpHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1906 YDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPNELLKEP-CGTL 1984
Cdd:cd14188    89 AHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINE---NMELKVGDFGLAARLEPLEHRRRTiCGTP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1985 AYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINkntemNIQKNY--VLSFKDYIWKSISSSAKDLISKLLELNV 2062
Cdd:cd14188   166 NYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETT-----NLKETYrcIREARYSLPSSLLAPAKHLIASMLSKNP 240
                         250
                  ....*....|..
gi 124804138 2063 EKRISANEALEH 2074
Cdd:cd14188   241 EDRPSLDEIIRH 252
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
1825-2076 2.18e-29

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: 120.49  E-value: 2.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELVKGgE 1904
Cdd:cd07873     8 DKLGEGTYATVYKGRSKLTDNLVALKEIRLEHEEGAPCTAIR-EVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLDK-D 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAETRLSEIHANKI-ITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLCA-PNELLKEPCG 1982
Cdd:cd07873    86 LKQYLDDCGNSINMHNVKLfLFQLLRGLAYCHRRKVLHRDLKPQNLLINER---GELKLADFGLARAKSiPTKTYSNEVV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1983 TLAYVAPEVIT-LQGYNHKVDAWSIGIILYLLLSGKLPFP-------------------------INKNTEMnIQKNYVL 2036
Cdd:cd07873   163 TLWYRPPDILLgSTDYSTQIDMWGVGCIFYEMSTGRPLFPgstveeqlhfifrilgtpteetwpgILSNEEF-KSYNYPK 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 124804138 2037 SFKDYIWK---SISSSAKDLISKLLELNVEKRISANEALEHIW 2076
Cdd:cd07873   242 YRADALHNhapRLDSDGADLLSKLLQFEGRKRISAEEAMKHPY 284
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
1821-2077 3.66e-29

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: 119.35  E-value: 3.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDkrsvSIYE-KELLRSEISILRLLR-HPNV-----IYLKEIINTKETL 1893
Cdd:cd06638    20 WEIIETIGKGTYGKVFKVLNKKNGSKAAVKILD----PIHDiDEEIEAEYNILKALSdHPNVvkfygMYYKKDVKNGDQL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1894 YISMELVKGGELYD----FLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLST 1969
Cdd:cd06638    96 WLVLELCNGGSVTDlvkgFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTT---EGGVKLVDFGVSA 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1970 LCAPNELLKE-PCGTLAYVAPEVITLQ-----GYNHKVDAWSIGIILYLLLSGKLP----------FPINKNTEMNIQkn 2033
Cdd:cd06638   173 QLTSTRLRRNtSVGTPFWMAPEVIACEqqldsTYDARCDVWSLGITAIELGDGDPPladlhpmralFKIPRNPPPTLH-- 250
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 124804138 2034 yvlsfKDYIWksiSSSAKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd06638   251 -----QPELW---SNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
1827-2020 4.04e-29

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: 118.31  E-value: 4.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKqtNSEFAIKVIDKRSvsiyEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGELY 1906
Cdd:cd14058     1 VGRGSFGVVCKARWR--NQIVAVKIIESES----EKKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1907 DFLLAETRLSEI---HANKIITQLIKTVAYLHRCG---IIHRDIKPENILLTDKSRDaqIKLTDFGlsTLCAPNELLKEP 1980
Cdd:cd14058    75 NVLHGKEPKPIYtaaHAMSWALQCAKGVAYLHSMKpkaLIHRDLKPPNLLLTNGGTV--LKICDFG--TACDISTHMTNN 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 124804138 1981 CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd14058   151 KGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPF 190
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
1825-2077 4.53e-29

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: 118.64  E-value: 4.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSEFAIKVI----------DKRSVSIYEKelLRSEISILRLLRHPNVI-YLK-EiiNTKET 1892
Cdd:cd06629     7 ELIGKGTYGRVYLAMNATTGEMLAVKQVelpktssdraDSRQKTVVDA--LKSEIDTLKDLDHPNIVqYLGfE--ETEDY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1893 LYISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCA 1972
Cdd:cd06629    83 FSIFLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILV---DLEGICKISDFGISKKSD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1973 ------PNELLKepcGTLAYVAPEVITL--QGYNHKVDAWSIGIILYLLLSGKLPFPinkNTEMnIQKNYVLSFKdyiwK 2044
Cdd:cd06629   160 diygnnGATSMQ---GSVFWMAPEVIHSqgQGYSAKVDIWSLGCVVLEMLAGRRPWS---DDEA-IAAMFKLGNK----R 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 124804138 2045 S---------ISSSAKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd06629   229 SappvpedvnLSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
1827-2020 7.05e-29

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: 118.70  E-value: 7.05e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKR-SVSIYEKELLRSEISILRLLRHPNVIYLK------EIINTKETLYISMEL 1899
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTGEYVAIKKCRQElSPSDKNRERWCLEVQIMKKLNHPNVVSARdvppelEKLSPNDLPLLAMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFL-LAETR--LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCAPNEL 1976
Cdd:cd13989    81 CSGGDLRKVLnQPENCcgLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRVIYKLIDLGYAKELDQGSL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 124804138 1977 LKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd13989   161 CTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPF 204
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
1820-2076 7.37e-29

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: 119.31  E-value: 7.37e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1820 LYELHEQLGQGKFSTVY--RGINKQTNSEFAIKVIdKRSVSIYE---KELLRsEISILRLLRHPNVIYLKEIINTKETLY 1894
Cdd:cd07842     1 KYEIEGCIGRGTYGRVYkaKRKNGKDGKEYAIKKF-KGDKEQYTgisQSACR-EIALLRELKHENVVSLVEVFLEHADKS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMelvkggeLYDF----LLA------ETRLSEIHAN---KIITQLIKTVAYLHRCGIIHRDIKPENILLT-DKSRDAQI 1960
Cdd:cd07842    79 VYL-------LFDYaehdLWQiikfhrQAKRVSIPPSmvkSLLWQILNGIHYLHSNWVLHRDLKPANILVMgEGPERGVV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1961 KLTDFGLSTLCapNELLKEPCG------TLAYVAPEVitLQG---YNHKVDAWSIGIILYLLLSGKLPFPiNKNTEMNIQ 2031
Cdd:cd07842   152 KIGDLGLARLF--NAPLKPLADldpvvvTIWYRAPEL--LLGarhYTKAIDIWAIGCIFAELLTLEPIFK-GREAKIKKS 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 2032 KNY----------VLSF---------KDY-------------------------IWKSISSSAKDLISKLLELNVEKRIS 2067
Cdd:cd07842   227 NPFqrdqlerifeVLGTptekdwpdiKKMpeydtlksdtkastypnsllakwmhKHKKPDSQGFDLLRKLLEYDPTKRIT 306

                  ....*....
gi 124804138 2068 ANEALEHIW 2076
Cdd:cd07842   307 AEEALEHPY 315
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
1821-2076 7.98e-29

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: 119.34  E-value: 7.98e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSvsiyEKEL-----LRsEISILRLLRHPNVIYLKEII-----NTK 1890
Cdd:cd07866    10 YEILGKLGEGTFGEVYKARQIKTGRVVALKKILMHN----EKDGfpitaLR-EIKILKKLKHPNVVPLIDMAverpdKSK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1891 ETL--------YISMELVkgGELYDfllAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKL 1962
Cdd:cd07866    85 RKRgsvymvtpYMDHDLS--GLLEN---PSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQ---GILKI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1963 TDFGLS---TLCAPNELLKEPCGTLAYV---------APE-VITLQGYNHKVDAWSIGIILYLLLSGK------------ 2017
Cdd:cd07866   157 ADFGLArpyDGPPPNPKGGGGGGTRKYTnlvvtrwyrPPElLLGERRYTTAVDIWGIGCVFAEMFTRRpilqgksdidql 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124804138 2018 -----LPFPINKNTEMNIQK----NYVLSFKDYI------WKSISSSAKDLISKLLELNVEKRISANEALEHIW 2076
Cdd:cd07866   237 hlifkLCGTPTEETWPGWRSlpgcEGVHSFTNYPrtleerFGKLGPEGLDLLSKLLSLDPYKRLTASDALEHPY 310
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
1821-2080 8.48e-29

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: 119.01  E-value: 8.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVI----DKRSVSIYEkelLRsEISILRLLRHPNVIYLKEII--NTKETLY 1894
Cdd:cd07845     9 FEKLNRIGEGTYGIVYRARDTTSGEIVALKKVrmdnERDGIPISS---LR-EITLLLNLRHPNIVELKEVVvgKHLDSIF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVKG--GELYDFLlaETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLCA 1972
Cdd:cd07845    85 LVMEYCEQdlASLLDNM--PTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDK---GCLKIADFGLARTYG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1973 PNELLKEPC-GTLAYVAPEVitLQG---YNHKVDAWSIGIILYLLLSGKLPFPINKNTE---MNIQ-------------- 2031
Cdd:cd07845   160 LPAKPMTPKvVTLWYRAPEL--LLGcttYTTAIDMWAVGCILAELLAHKPLLPGKSEIEqldLIIQllgtpnesiwpgfs 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124804138 2032 -----KNYVLSFKDY-------IWksISSSAKDLISKLLELNVEKRISANEALEHIWVKNP 2080
Cdd:cd07845   238 dlplvGKFTLPKQPYnnlkhkfPW--LSEAGLRLLNFLLMYDPKKRATAEEALESSYFKEK 296
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
1827-2026 8.66e-29

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: 117.55  E-value: 8.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGELY 1906
Cdd:cd13978     1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1907 DFLLAET-------RLseihanKIITQLIKTVAYLH--RCGIIHRDIKPENILLTDksrDAQIKLTDFGLS-----TLCA 1972
Cdd:cd13978    81 SLLEREIqdvpwslRF------RIIHEIALGMNFLHnmDPPLLHHDLKPENILLDN---HFHVKISDFGLSklgmkSISA 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 124804138 1973 PNELLKEP-CGTLAYVAPEVI--TLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNT 2026
Cdd:cd13978   152 NRRRGTENlGGTPIYMAPEAFddFNKKPTSKSDVYSFAIVIWAVLTRKEPFENAINP 208
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
1819-2083 1.07e-28

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: 118.21  E-value: 1.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLrsEISILRLLRHPNVIYLKEIINTKETLYISME 1898
Cdd:cd06644    12 EVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYMV--EIEILATCNHPYIVKLLGAFYWDGKLWIMIE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFLLAETR-LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLS-----TLCA 1972
Cdd:cd06644    90 FCPGGAVDAIMLELDRgLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLT---LDGDIKLADFGVSaknvkTLQR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1973 PNELLkepcGTLAYVAPEVITLQG-----YNHKVDAWSIGIILYLLLSGKLPfpinkNTEMNIQKnYVLSFKDYIWKSIS 2047
Cdd:cd06644   167 RDSFI----GTPYWMAPEVVMCETmkdtpYDYKADIWSLGITLIEMAQIEPP-----HHELNPMR-VLLKIAKSEPPTLS 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 124804138 2048 SSAK------DLISKLLELNVEKRISANEALEHIWVKNPTAV 2083
Cdd:cd06644   237 QPSKwsmefrDFLKTALDKHPETRPSAAQLLEHPFVSSVTSN 278
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
1825-2074 1.11e-28

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: 117.37  E-value: 1.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFST-VYRGInkqtnsefaikvIDKRSVSIyeKELLRSEISI----LRLLR----HPNVI--YLKEiiNTKETL 1893
Cdd:cd13982     7 KVLGYGSEGTiVFRGT------------FDGRPVAV--KRLLPEFFDFadreVQLLResdeHPNVIryFCTE--KDRQFL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1894 YISMEL--------VKGGELYdfllAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIK--LT 1963
Cdd:cd13982    71 YIALELcaaslqdlVESPRES----KLFLRPGLEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILISTPNAHGNVRamIS 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1964 DFGLSTLCAPNE----LLKEPCGTLAYVAPEVI---TLQGYNHKVDAWSIGIILYLLLS-GKLPFPINKNTEMNIQKNYV 2035
Cdd:cd13982   147 DFGLCKKLDVGRssfsRRSGVAGTSGWIAPEMLsgsTKRRQTRAVDIFSLGCVFYYVLSgGSHPFGDKLEREANILKGKY 226
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 124804138 2036 LSFKDYIWKSISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd13982   227 SLDKLLSLGEHGPEAQDLIERMIDFDPEKRPSAEEVLNH 265
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
1821-2076 1.27e-28

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: 117.78  E-value: 1.27e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSvsiyEKELLRS----EISILRLLRHPNVIYLKEIINTKETLYIS 1896
Cdd:cd07835     1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIRLET----EDEGVPStairEISLLKELNHPNIVRLLDVVHSENKLYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1897 MELVKGgELYDFL--LAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLS-TLCAP 1973
Cdd:cd07835    77 FEFLDL-DLKKYMdsSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLI---DTEGALKLADFGLArAFGVP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1974 NELLKEPCGTLAYVAPEVitLQG---YNHKVDAWSIGIILYLLLSGKLPFP----INK--------NTEMNIQKNYVLSF 2038
Cdd:cd07835   153 VRTYTHEVVTLWYRAPEI--LLGskhYSTPVDIWSVGCIFAEMVTRRPLFPgdseIDQlfrifrtlGTPDEDVWPGVTSL 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 124804138 2039 KDYI-----WK---------SISSSAKDLISKLLELNVEKRISANEALEHIW 2076
Cdd:cd07835   231 PDYKptfpkWArqdlskvvpSLDEDGLDLLSQMLVYDPAKRISAKAALQHPY 282
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
1830-2079 1.52e-28

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 116.88  E-value: 1.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1830 GKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEkellrseISILRLLR-HPNVIYLKEIINTKETLYISMELVKGGELYDF 1908
Cdd:PHA03390   27 GKFGKVSVLKHKPTQKLFVQKIIKAKNFNAIE-------PMVHQLMKdNPNFIKLYYSVTTLKGHVLIMDYIKDGDLFDL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1909 LLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRdaQIKLTDFGLStlcapnELLKEPC---GTLA 1985
Cdd:PHA03390  100 LKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAKD--RIYLCDYGLC------KIIGTPScydGTLD 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1986 YVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQK-NYVLSFKDYIWKSISSSAKDLISKLLELNVEK 2064
Cdd:PHA03390  172 YFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDEELDLESlLKRQQKKLPFIKNVSKNANDFVQSMLKYNINY 251
                         250
                  ....*....|....*.
gi 124804138 2065 R-ISANEALEHIWVKN 2079
Cdd:PHA03390  252 RlTNYNEIIKHPFLKI 267
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
1825-2074 1.80e-28

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: 117.37  E-value: 1.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELVKGgE 1904
Cdd:cd07870     6 EKLGEGSYATVYKGISRINGQLVALKVISMKTEEGVPFTAIR-EASLLKGLKHANIVLLHDIIHTKETLTFVFEYMHT-D 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAETrlSEIHANKI---ITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLS-TLCAPNELLKEP 1980
Cdd:cd07870    84 LAQYMIQHP--GGLHPYNVrlfMFQLLRGLAYIHGQHILHRDLKPQNLLI---SYLGELKLADFGLArAKSIPSQTYSSE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 CGTLAYVAPEVIT-LQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYVL----------------------- 2036
Cdd:cd07870   159 VVTLWYRPPDVLLgATDYSSALDIWGAGCIFIEMLQGQPAFPGVSDVFEQLEKIWTVlgvptedtwpgvsklpnykpewf 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 124804138 2037 ------SFKDyIWKSISS--SAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd07870   239 lpckpqQLRV-VWKRLSRppKAEDLASQMLMMFPKDRISAQDALLH 283
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
1821-2074 2.29e-28

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: 116.54  E-value: 2.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQtNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRH-PNVIYLK--EIINTKETLYISM 1897
Cdd:cd14131     3 YEILKQLGKGGSSKVYKVLNPK-KKIYALKRVDLEGADEQTLQSYKNEIELLKKLKGsDRIIQLYdyEVTDEDDYLYMVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELvkgGElYDF--LLAETRLSEIHANKII---TQLIKTVAYLHRCGIIHRDIKPENILLTDKSrdaqIKLTDFGLSTLCA 1972
Cdd:cd14131    82 EC---GE-IDLatILKKKRPKPIDPNFIRyywKQMLEAVHTIHEEGIVHSDLKPANFLLVKGR----LKLIDFGIAKAIQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1973 PNE--LLKEP-CGTLAYVAPEVIT-LQGYNH---------KVDAWSIGIILYLLLSGKLPFPINKNtemNIQKNYVLSFK 2039
Cdd:cd14131   154 NDTtsIVRDSqVGTLNYMSPEAIKdTSASGEgkpkskigrPSDVWSLGCILYQMVYGKTPFQHITN---PIAKLQAIIDP 230
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 124804138 2040 DYI--WKSISS-SAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd14131   231 NHEieFPDIPNpDLIDVMKRCLQRDPKKRPSIPELLNH 268
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
1827-2020 3.26e-28

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: 115.28  E-value: 3.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGinKQTNSEFAIKVIDKrsvsiyEKEllrSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGELY 1906
Cdd:cd14059     1 LGSGAQGAVFLG--KFRGEEVAVKKVRD------EKE---TDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLY 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1907 DFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPNELLKEPCGTLAY 1986
Cdd:cd14059    70 EVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTY---NDVLKISDFGTSKELSEKSTKMSFAGTVAW 146
                         170       180       190
                  ....*....|....*....|....*....|....
gi 124804138 1987 VAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd14059   147 MAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPY 180
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
1821-2076 3.36e-28

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: 117.47  E-value: 3.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVI----DKRSVSIYEkelLRsEISILRLLRHPNVIYLKEIINTKET---- 1892
Cdd:cd07865    14 YEKLAKIGQGTFGEVFKARHRKTGQIVALKKVlmenEKEGFPITA---LR-EIKILQLLKHENVVNLIEICRTKATpynr 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1893 ----LYISMELVKggelYDF--LL--AETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTD 1964
Cdd:cd07865    90 ykgsIYLVFEFCE----HDLagLLsnKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILIT---KDGVLKLAD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1965 FGLSTLCAPNELLKEPC-----GTLAYVAPEVitLQG---YNHKVDAWSIGIIL-----------------YLLLSGKLP 2019
Cdd:cd07865   163 FGLARAFSLAKNSQPNRytnrvVTLWYRPPEL--LLGerdYGPPIDMWGAGCIMaemwtrspimqgnteqhQLTLISQLC 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124804138 2020 FPINKN-----------TEMNIQKNYVLSFKDYIWKSISS-SAKDLISKLLELNVEKRISANEALEHIW 2076
Cdd:cd07865   241 GSITPEvwpgvdklelfKKMELPQGQKRKVKERLKPYVKDpYALDLIDKLLVLDPAKRIDADTALNHDF 309
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
1826-2084 3.74e-28

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: 116.68  E-value: 3.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1826 QLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSiyEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGEL 1905
Cdd:cd06658    29 KIGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQ--RRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGAL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1906 YDfLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGlstLCA--PNELLKEP--C 1981
Cdd:cd06658   107 TD-IVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTS---DGRIKLSDFG---FCAqvSKEVPKRKslV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1982 GTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF----PInkNTEMNIQKNYVLSFKDYiwKSISSSAKDLISKL 2057
Cdd:cd06658   180 GTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYfnepPL--QAMRRIRDNLPPRVKDS--HKVSSVLRGFLDLM 255
                         250       260
                  ....*....|....*....|....*....
gi 124804138 2058 LELNVEKRISANEALEHIWVK--NPTAVI 2084
Cdd:cd06658   256 LVREPSQRATAQELLQHPFLKlaGPPSCI 284
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
1821-2010 4.18e-28

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: 115.98  E-value: 4.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQ-TNSEFAIKVIDKRSVSIYEKELLRSEISILRLLR---HPNVIYLKEIINTKETLYIS 1896
Cdd:cd14052     2 FANVELIGSGEFSQVYKVSERVpTGKVYAVKKLKPNYAGAKDRLRRLEEVSILRELTldgHDNIVQLIDSWEYHGHLYIQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1897 MELVKGGELyDFLLAE----TRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLSTLCa 1972
Cdd:cd14052    82 TELCENGSL-DVFLSElgllGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLIT---FEGTLKIGDFGMATVW- 156
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 124804138 1973 PNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIIL 2010
Cdd:cd14052   157 PLIRGIEREGDREYIAPEILSEHMYDKPADIFSLGLIL 194
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
1819-2074 4.28e-28

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: 116.37  E-value: 4.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISME 1898
Cdd:cd07846     1 EKYENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVKKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLS-TLCAPNELL 1977
Cdd:cd07846    81 FVDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILV---SQSGVVKLCDFGFArTLAAPGEVY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPCGTLAYVAPE-VITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTE-----MNIQKNYVLSFKDYIWKS------ 2045
Cdd:cd07846   158 TDYVATRWYRAPElLVGDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDqlyhiIKCLGNLIPRHQELFQKNplfagv 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 124804138 2046 -----------------ISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd07846   238 rlpevkeveplerrypkLSGVVIDLAKKCLHIDPDKRPSCSELLHH 283
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
1821-2077 4.88e-28

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: 115.31  E-value: 4.88e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDkrsvsiYEKELLRS---EISILRLLRHPNVIYLKEIINTKETLYISM 1897
Cdd:cd14111     5 YTFLDEKARGRFGVIRRCRENATGKNFPAKIVP------YQAEEKQGvlqEYEILKSLHHERIMALHEAYITPRYLVLIA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPNEL- 1976
Cdd:cd14111    79 EFCSGKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTN---LNAIKIVDFGSAQSFNPLSLr 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1977 -LKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF--PINKNTEMNIQKNYVLSFKDYiwKSISSSAKDL 2053
Cdd:cd14111   156 qLGRRTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFedQDPQETEAKILVAKFDAFKLY--PNVSQSASLF 233
                         250       260
                  ....*....|....*....|....
gi 124804138 2054 ISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14111   234 LKKVLSSYPWSRPTTKDCFAHAWL 257
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
1821-2077 5.74e-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: 115.32  E-value: 5.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEfAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd14112     5 FSFGSEIFRGRFSVIVKAVDSTTETD-AHCAVKIFEVSDEASEAVR-EFESLRTLQHENVQRLIAAFKPSNFAYLVMEKL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGgELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsRDAQIKLTDFGLSTLCAPnELLKEP 1980
Cdd:cd14112    83 QE-DVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSV-RSWQVKLVDFGRAQKVSK-LGKVPV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 CGTLAYVAPEVI-TLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKN--YVLSFKDYIWKSISSSAKDLISKL 2057
Cdd:cd14112   160 DGDTDWASPEFHnPETPITVQSDIWGLGVLTFCLLSGFHPFTSEYDDEEETKENviFVKCRPNLIFVEATQEALRFATWA 239
                         250       260
                  ....*....|....*....|
gi 124804138 2058 LELNVEKRISANEALEHIWV 2077
Cdd:cd14112   240 LKKSPTRRMRTDEALEHRWL 259
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
1813-2074 7.55e-28

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: 117.49  E-value: 7.55e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1813 KQNTLyNLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdKRSVSIYEKELLRS--EISILRLLRHPNVIYLKEIINTK 1890
Cdd:cd05593    10 KRKTM-NDFDYLKLLGKGTFGKVILVREKASGKYYAMKIL-KKEVIIAKDEVAHTltESRVLKNTRHPFLTSLKYSFQTK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1891 ETLYISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTL 1970
Cdd:cd05593    88 DRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML---DKDGHIKITDFGLCKE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1971 CAPN-ELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpINKNTEMNIQKNYVLSFKdyIWKSISSS 2049
Cdd:cd05593   165 GITDaATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF-YNQDHEKLFELILMEDIK--FPRTLSAD 241
                         250       260       270
                  ....*....|....*....|....*....|
gi 124804138 2050 AKDLISKLLELNVEKRI-----SANEALEH 2074
Cdd:cd05593   242 AKSLLSGLLIKDPNKRLgggpdDAKEIMRH 271
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1821-2020 1.10e-27

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: 114.52  E-value: 1.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRgINKQTNSE--FAIKVIDKRSVSIYEKELLR--------SEISILR-LLRHPNVIYLKEIINT 1889
Cdd:cd08528     2 YAVLELLGSGAFGCVYK-VRKKSNGQtlLALKEINMTNPAFGRTEQERdksvgdiiSEVNIIKeQLRHPNIVRYYKTFLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1890 KETLYISMELVKGGELYDFLLAetrLSEIHAN-------KIITQLIKTVAYLHR-CGIIHRDIKPENILLTDKSRdaqIK 1961
Cdd:cd08528    81 NDRLYIVMELIEGAPLGEHFSS---LKEKNEHftedriwNIFVQMVLALRYLHKeKQIVHRDLKPNNIMLGEDDK---VT 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1962 LTDFGLSTLCAPNEL-LKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd08528   155 ITDFGLAKQKGPESSkMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPF 214
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
1825-2074 1.12e-27

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: 114.45  E-value: 1.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSEFAIKVID--KRSVSIYEK--ELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd06630     6 PLLGTGAFSSCYQARDVKTGTLMAVKQVSfcRNSSSEQEEvvEAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDaqIKLTDFGL-----STLCAPNE 1975
Cdd:cd06630    86 AGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQR--LRIADFGAaarlaSKGTGAGE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1976 LLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINkntemNIQKNYVLSFK-------DYIWKSISS 2048
Cdd:cd06630   164 FQGQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAE-----KISNHLALIFKiasattpPPIPEHLSP 238
                         250       260
                  ....*....|....*....|....*.
gi 124804138 2049 SAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd06630   239 GLRDVTLRCLELQPEDRPPARELLKH 264
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
1827-2074 1.25e-27

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: 116.13  E-value: 1.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKR-SVSIYEKELLRsEISILRLLRHPNVIYLKEI-INTKETLYISMELVkGGE 1904
Cdd:cd07856    18 VGMGAFGLVCSARDQLTGQNVAVKKIMKPfSTPVLAKRTYR-ELKLLKHLRHENIISLSDIfISPLEDIYFVTELL-GTD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDfLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPNelLKEPCGTL 1984
Cdd:cd07856    96 LHR-LLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNE---NCDLKICDFGLARIQDPQ--MTGYVSTR 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1985 AYVAPEV-ITLQGYNHKVDAWSIGIILYLLLSGKLPFP----INKN---TEM----------NIQKNYVLSFKDYI---- 2042
Cdd:cd07856   170 YYRAPEImLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPgkdhVNQFsiiTELlgtppddvinTICSENTLRFVQSLpkre 249
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 124804138 2043 -------WKSISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd07856   250 rvpfsekFKNADPDAIDLLEKMLVFDPKKRISAAEALAH 288
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
1825-2074 1.29e-27

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: 114.91  E-value: 1.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSEFAIKVI--DKRSVSIYEKELlrSEISILRLLRHPNVIYLKEIINTKETLYISMELVKg 1902
Cdd:cd07860     6 EKIGEGTYGVVYKARNKLTGEVVALKKIrlDTETEGVPSTAI--REISLLKELNHPNIVKLLDVIHTENKLYLVFEFLH- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1903 GELYDFLLAeTRLSEIHANKI---ITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLS-TLCAPNELLK 1978
Cdd:cd07860    83 QDLKKFMDA-SALTGIPLPLIksyLFQLLQGLAFCHSHRVLHRDLKPQNLLI---NTEGAIKLADFGLArAFGVPVRTYT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1979 EPCGTLAYVAPEVIT-LQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQ-------------------KNYVLSF 2038
Cdd:cd07860   159 HEVVTLWYRAPEILLgCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRifrtlgtpdevvwpgvtsmPDYKPSF 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 124804138 2039 KDYIWKSISS-------SAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd07860   239 PKWARQDFSKvvppldeDGRDLLSQMLHYDPNKRISAKAALAH 281
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
1821-2074 1.38e-27

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: 114.06  E-value: 1.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd08220     2 YEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFL--LAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtDKSRDAqIKLTDFGLSTLCAPNELLK 1978
Cdd:cd08220    82 PGGTLFEYIqqRKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILL-NKKRTV-VKIGDFGISKILSSKSKAY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1979 EPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINK--NTEMNIQKNYVlsfkDYIWKSISSSAKDLISK 2056
Cdd:cd08220   160 TVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANlpALVLKIMRGTF----APISDRYSEELRHLILS 235
                         250
                  ....*....|....*...
gi 124804138 2057 LLELNVEKRISANEALEH 2074
Cdd:cd08220   236 MLHLDPNKRPTLSEIMAQ 253
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
1825-2074 1.52e-27

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: 114.72  E-value: 1.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELVKGgE 1904
Cdd:cd07871    11 DKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAIR-EVSLLKNLKHANIVTLHDIIHTERCLTLVFEYLDS-D 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAETRLSEIHANKIIT-QLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLS-TLCAPNELLKEPCG 1982
Cdd:cd07871    89 LKQYLDNCGNLMSMHNVKIFMfQLLRGLSYCHKRKILHRDLKPQNLLINEK---GELKLADFGLArAKSVPTKTYSNEVV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1983 TLAYVAPEVitLQG---YNHKVDAWSIGIILYLLLSGKLPFPINK-NTEMNIQKNYVLSFKDYIWKSISSSAK------- 2051
Cdd:cd07871   166 TLWYRPPDV--LLGsteYSTPIDMWGVGCILYEMATGRPMFPGSTvKEELHLIFRLLGTPTEETWPGVTSNEEfrsylfp 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 124804138 2052 -------------------DLISKLLELNVEKRISANEALEH 2074
Cdd:cd07871   244 qyraqplinhaprldtdgiDLLSSLLLYETKSRISAEAALRH 285
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
1823-2068 2.01e-27

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: 115.79  E-value: 2.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1823 LHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEK-ELLRSEISILRLL-RHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd05619     9 LHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDvECTMVEKRVLSLAwEHPFLTHLFCTFQTKENLFFVMEYL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLstlCAPNELLKEP 1980
Cdd:cd05619    89 NGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILL---DKDGHIKIADFGM---CKENMLGDAK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 ----CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEM--NIQKNyvlsfKDYIWKSISSSAKDLI 2054
Cdd:cd05619   163 tstfCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELfqSIRMD-----NPFYPRWLEKEAKDIL 237
                         250
                  ....*....|....
gi 124804138 2055 SKLLELNVEKRISA 2068
Cdd:cd05619   238 VKLFVREPERRLGV 251
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
1821-2073 2.11e-27

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: 113.37  E-value: 2.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd08218     2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAE--TRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLS-TLCAPNELL 1977
Cdd:cd08218    82 DGGDLYKRINAQrgVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLT---KDGIIKLGDFGIArVLNSTVELA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpinkntEMNIQKNYVLSFKDYIWKSI----SSSAKDL 2053
Cdd:cd08218   159 RTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAF------EAGNMKNLVLKIIRGSYPPVpsrySYDLRSL 232
                         250       260
                  ....*....|....*....|
gi 124804138 2054 ISKLLELNVEKRISANEALE 2073
Cdd:cd08218   233 VSQLFKRNPRDRPSINSILE 252
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
1808-2074 2.42e-27

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: 115.91  E-value: 2.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1808 LYSSTKQNTLYNLYELHEQL---GQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLK 1884
Cdd:cd07877     3 FYRQELNKTIWEVPERYQNLspvGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1885 EIINTKETL------YISMELVkGGELYDFLLAEtRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDA 1958
Cdd:cd07877    83 DVFTPARSLeefndvYLVTHLM-GADLNNIVKCQ-KLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNE---DC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1959 QIKLTDFGLSTLCApnellKEPCGTLA---YVAPEV-ITLQGYNHKVDAWSIGIILYLLLSGKLPFP----IN------- 2023
Cdd:cd07877   158 ELKILDFGLARHTD-----DEMTGYVAtrwYRAPEImLNWMHYNQTVDIWSVGCIMAELLTGRTLFPgtdhIDqlklilr 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124804138 2024 ----------KNTEMNIQKNYVLS--------FKDyIWKSISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd07877   233 lvgtpgaellKKISSESARNYIQSltqmpkmnFAN-VFIGANPLAVDLLEKMLVLDSDKRITAAQALAH 300
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
1825-2074 2.57e-27

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: 113.25  E-value: 2.57e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSEFAIKvidKRSVSIY---EKELLRSEISILRLL-RHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd13997     6 EQIGSGSFSEVFKVRSKVDGCLYAVK---KSKKPFRgpkERARALREVEAHAALgQHPNIVRYYSSWEEGGHLYIQMELC 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFL---LAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCAPNELL 1977
Cdd:cd13997    83 ENGSLQDALeelSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFI---SNKGTCKIGDFGLATRLETSGDV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEpcGTLAYVAPEVitLQG---YNHKVDAWSIGIILYLLLSGkLPFPINKNTEMNIQKNYVLSFKDYIwksISSSAKDLI 2054
Cdd:cd13997   160 EE--GDSRYLAPEL--LNEnytHLPKADIFSLGVTVYEAATG-EPLPRNGQQWQQLRQGKLPLPPGLV---LSQELTRLL 231
                         250       260
                  ....*....|....*....|
gi 124804138 2055 SKLLELNVEKRISANEALEH 2074
Cdd:cd13997   232 KVMLDPDPTRRPTADQLLAH 251
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
1826-2074 2.73e-27

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: 114.35  E-value: 2.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1826 QLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSiyEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGEL 1905
Cdd:cd06657    27 KIGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQ--RRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1906 YDfLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLSTLCAPN-ELLKEPCGTL 1984
Cdd:cd06657   105 TD-IVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLT---HDGRVKLSDFGFCAQVSKEvPRRKSLVGTP 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1985 AYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF---PINKNTEMnIQKNYVLSFKDYiwKSISSSAKDLISKLLELN 2061
Cdd:cd06657   181 YWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYfnePPLKAMKM-IRDNLPPKLKNL--HKVSPSLKGFLDRLLVRD 257
                         250
                  ....*....|...
gi 124804138 2062 VEKRISANEALEH 2074
Cdd:cd06657   258 PAQRATAAELLKH 270
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
1821-2077 3.16e-27

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: 113.22  E-value: 3.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVI--DKRSVSIY-EKELLRSEISILRLLRHPNVI-YLKEIINTKE-TLYI 1895
Cdd:cd06652     4 WRLGKLLGQGAFGRVYLCYDADTGRELAVKQVqfDPESPETSkEVNALECEIQLLKNLLHERIVqYYGCLRDPQErTLSI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1896 SMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILltdksRDA--QIKLTDFG----LST 1969
Cdd:cd06652    84 FMEYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANIL-----RDSvgNVKLGDFGaskrLQT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1970 LCAPNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPiNKNTEMNIQKNYVLSFKDYIWKSISSS 2049
Cdd:cd06652   159 ICLSGTGMKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWA-EFEAMAAIFKIATQPTNPQLPAHVSDH 237
                         250       260
                  ....*....|....*....|....*...
gi 124804138 2050 AKDLISKLLeLNVEKRISANEALEHIWV 2077
Cdd:cd06652   238 CRDFLKRIF-VEAKLRPSADELLRHTFV 264
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
1822-2086 3.36e-27

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: 114.36  E-value: 3.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1822 ELHEqLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEK-ELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd06633    25 DLHE-IGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKwQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEYC 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGElYDFLLAETR-LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLCAP-NELLk 1978
Cdd:cd06633   104 LGSA-SDLLEVHKKpLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEP---GQVKLADFGSASIASPaNSFV- 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1979 epcGTLAYVAPEVITLQG---YNHKVDAWSIGIILYLLLSGKLP-FPINKNTEM-NIQKNYVLSFKDYIWksiSSSAKDL 2053
Cdd:cd06633   179 ---GTPYWMAPEVILAMDegqYDGKVDIWSLGITCIELAERKPPlFNMNAMSALyHIAQNDSPTLQSNEW---TDSFRGF 252
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 124804138 2054 ISKLLELNVEKRISANEALEH--IWVKNPTAVINE 2086
Cdd:cd06633   253 VDYCLQKIPQERPSSAELLRHdfVRRERPPRVLID 287
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
1825-2074 3.82e-27

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: 112.91  E-value: 3.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQtNSEFAIK--VIDKRSVSIYEKEL--LRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd06631     7 NVLGKGAYGTVYCGLTST-GQLIAVKqvELDTSDKEKAEKEYekLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEFV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSrdaQIKLTDFG-------LSTLCAP 1973
Cdd:cd06631    86 PGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNG---VIKLIDFGcakrlciNLSSGSQ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1974 NELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF----PINKNTEMNIQKNYVLSFKDyiwkSISSS 2049
Cdd:cd06631   163 SQLLKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWadmnPMAAIFAIGSGRKPVPRLPD----KFSPE 238
                         250       260
                  ....*....|....*....|....*
gi 124804138 2050 AKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd06631   239 ARDFVHACLTRDQDERPSAEQLLKH 263
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1821-2073 4.93e-27

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: 112.36  E-value: 4.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd08225     2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAE--TRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAqiKLTDFGLS-TLCAPNELL 1977
Cdd:cd08225    82 DGGDLMKRINRQrgVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVA--KLGDFGIArQLNDSMELA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPIN--KNTEMNIQKNYVLSfkdyIWKSISSSAKDLIS 2055
Cdd:cd08225   160 YTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNnlHQLVLKICQGYFAP----ISPNFSRDLRSLIS 235
                         250
                  ....*....|....*...
gi 124804138 2056 KLLELNVEKRISANEALE 2073
Cdd:cd08225   236 QLFKVSPRDRPSITSILK 253
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
1815-2074 6.54e-27

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: 114.23  E-value: 6.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1815 NTLYNL---YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVS-IYEKELLRsEISILRLLRHPNVIYLKEIINTK 1890
Cdd:cd07879     8 KTVWELperYTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSRPFQSeIFAKRAYR-ELTLLKHMQHENVIGLLDVFTSA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1891 etlyismelVKGGELYDFLLA----ETRLSEIHANK--------IITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDA 1958
Cdd:cd07879    87 ---------VSGDEFQDFYLVmpymQTDLQKIMGHPlsedkvqyLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNE---DC 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1959 QIKLTDFGLSTlCAPNELLKEPCgTLAYVAPEVI-TLQGYNHKVDAWSIGIILYLLLSGKLPFP----------INKNT- 2026
Cdd:cd07879   155 ELKILDFGLAR-HADAEMTGYVV-TRWYRAPEVIlNWMHYNQTVDIWSVGCIMAEMLTGKTLFKgkdyldqltqILKVTg 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124804138 2027 ----------EMNIQKNYVLSF-----KDY--IWKSISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd07879   233 vpgpefvqklEDKAAKSYIKSLpkyprKDFstLFPKASPQAVDLLEKMLELDVDKRLTATEALEH 297
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
1827-2074 7.00e-27

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: 114.00  E-value: 7.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVI----DKRsvsIYEKELLRsEISILRLLRHPNVIYLKEII-----NTKETLYISM 1897
Cdd:cd07858    13 IGRGAYGIVCSAKNSETNEKVAIKKIanafDNR---IDAKRTLR-EIKLLRHLDHENVIAIKDIMppphrEAFNDVYIVY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGgELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLS-TLCAPNEL 1976
Cdd:cd07858    89 ELMDT-DLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLL---NANCDLKICDFGLArTTSEKGDF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1977 LKEPCGTLAYVAPEVI-TLQGYNHKVDAWSIGIILYLLLSGKLPFP--------------INKNTEMNIQ-------KNY 2034
Cdd:cd07858   165 MTEYVVTRWYRAPELLlNCSEYTTAIDVWSVGCIFAELLGRKPLFPgkdyvhqlklitelLGSPSEEDLGfirnekaRRY 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 124804138 2035 VLSFKDY-------IWKSISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd07858   245 IRSLPYTprqsfarLFPHANPLAIDLLEKMLVFDPSKRITVEEALAH 291
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
1821-2074 7.75e-27

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: 113.25  E-value: 7.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd07869     7 YEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAIR-EASLLKGLKHANIVLLHDIIHTKETLTLVFEYV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGgELYDFLlaETRLSEIHANKI---ITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLS-TLCAPNEL 1976
Cdd:cd07869    86 HT-DLCQYM--DKHPGGLHPENVklfLFQLLRGLSYIHQRYILHRDLKPQNLLISDT---GELKLADFGLArAKSVPSHT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1977 LKEPCGTLAYVAPEVIT-LQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYVL------------------- 2036
Cdd:cd07869   160 YSNEVVTLWYRPPDVLLgSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDIQDQLERIFLVlgtpnedtwpgvhslphfk 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 124804138 2037 --SFKDY-------IWKSIS--SSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd07869   240 peRFTLYspknlrqAWNKLSyvNHAEDLASKLLQCFPKNRLSAQAALSH 288
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
1826-2020 1.05e-26

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: 112.36  E-value: 1.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1826 QLGQGKFSTVYRGINKQTNSEFAIKVIdKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETL------YISMEL 1899
Cdd:cd14038     1 RLGTGGFGNVLRWINQETGEQVAIKQC-RQELSPKNRERWCLEIQIMKRLNHPNVVAARDVPEGLQKLapndlpLLAMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFL-LAET--RLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCAPNEL 1976
Cdd:cd14038    80 CQGGDLRKYLnQFENccGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRLIHKIIDLGYAKELDQGSL 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 124804138 1977 LKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd14038   160 CTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPF 203
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
1821-2020 1.12e-26

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 117.59  E-value: 1.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdkRSvsiyekELLRSEISILRLLR---------HPNV--IYlkeiiNT 1889
Cdd:NF033483    9 YEIGERIGRGGMAEVYLAKDTRLDRDVAVKVL--RP------DLARDPEFVARFRReaqsaaslsHPNIvsVY-----DV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1890 KET---LYISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFG 1966
Cdd:NF033483   76 GEDggiPYIVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILIT---KDGRVKVTDFG 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124804138 1967 L------STLCAPNELLkepcGTLAYVAPEvitlQGYNHKVDA----WSIGIILYLLLSGKLPF 2020
Cdd:NF033483  153 IaralssTTMTQTNSVL----GTVHYLSPE----QARGGTVDArsdiYSLGIVLYEMLTGRPPF 208
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
1808-2074 1.20e-26

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: 113.61  E-value: 1.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1808 LYSSTKQNTLYNLYELHEQL---GQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLK 1884
Cdd:cd07878     1 FYRQELNKTVWEVPERYQNLtpvGSGAYGSVCSAYDTRLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHMKHENVIGLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1885 EIINTKETL------YISMELVkGGELYDFLLAEtRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDA 1958
Cdd:cd07878    81 DVFTPATSIenfnevYLVTNLM-GADLNNIVKCQ-KLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNE---DC 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1959 QIKLTDFGLSTlcAPNELLKEPCGTLAYVAPEV-ITLQGYNHKVDAWSIGIILYLLLSGKLPFPIN-------------- 2023
Cdd:cd07878   156 ELRILDFGLAR--QADDEMTGYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNdyidqlkrimevvg 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124804138 2024 -------KNTEMNIQKNYVLSF-----KDY--IWKSISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd07878   234 tpspevlKKISSEHARKYIQSLphmpqQDLkkIFRGANPLAIDLLEKMLVLDSDKRISASEALAH 298
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
1820-2078 1.38e-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: 1.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1820 LYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEK----ELLRSEISILRLL----RHPNVIYLKEIINTKE 1891
Cdd:cd14101     1 QYTMGNLLGKGGFGTVYAGHRISDGLQVAIKQISRNRVQQWSKlpgvNPVPNEVALLQSVgggpGHRGVIRLLDWFEIPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1892 TLYISMEL-VKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdKSRDAQIKLTDFGlSTL 1970
Cdd:cd14101    81 GFLLVLERpQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILV--DLRTGDIKLIDFG-SGA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1971 CAPNELLKEPCGTLAYVAPEVITLQGYnHKVDA--WSIGIILYLLLSGKLPFpiNKNTEmniqknyVLSFKDYIWKSISS 2048
Cdd:cd14101   158 TLKDSMYTDFDGTRVYSPPEWILYHQY-HALPAtvWSLGILLYDMVCGDIPF--ERDTD-------ILKAKPSFNKRVSN 227
                         250       260       270
                  ....*....|....*....|....*....|
gi 124804138 2049 SAKDLISKLLELNVEKRISANEALEHIWVK 2078
Cdd:cd14101   228 DCRSLIRSCLAYNPSDRPSLEQILLHPWMM 257
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
1818-2077 1.46e-26

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: 111.16  E-value: 1.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1818 YNLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSvsiYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISM 1897
Cdd:cd14110     2 EKTYAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYKP---EDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSrdaQIKLTDFGLSTLCAPNE-L 1976
Cdd:cd14110    79 ELCSGPELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKN---LLKIVDLGNAQPFNQGKvL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1977 LKEPCG-TLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEM--NIQKNYVLSFKDYiwKSISSSAKDL 2053
Cdd:cd14110   156 MTDKKGdYVETMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERdrNIRKGKVQLSRCY--AGLSGGAVNF 233
                         250       260
                  ....*....|....*....|....
gi 124804138 2054 ISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14110   234 LKSTLCAKPWGRPTASECLQNPWL 257
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
1827-2068 2.92e-26

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: 112.28  E-value: 2.92e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVsIYEKELLRS--EISILR---LLRHPNVIYLKEIINTKETLYISMELVK 1901
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVI-VAKKEVAHTigERNILVrtaLDESPFIVGLKFSFQTPTDLYLVTDYMS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1902 GGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTL-CAPNELLKEP 1980
Cdd:cd05586    80 GGELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILL---DANGHIALCDFGLSKAdLTDNKTTNTF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 CGTLAYVAPEVITLQ-GYNHKVDAWSIGIILYLLLSGKLPFPINKNTEM--NIQKNYVLSFKDyiwkSISSSAKDLISKL 2057
Cdd:cd05586   157 CGTTEYLAPEVLLDEkGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMyrNIAFGKVRFPKD----VLSDEGRSFVKGL 232
                         250
                  ....*....|.
gi 124804138 2058 LELNVEKRISA 2068
Cdd:cd05586   233 LNRNPKHRLGA 243
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
1821-2036 3.68e-26

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: 109.83  E-value: 3.68e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKqTNSEFAIKVIdkRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd05148     8 FTLERKLGSGYFGEVWEGLWK-NRVRVAIKIL--KSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITELM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLL-AETR-LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLStlcapnELLK 1978
Cdd:cd05148    85 EKGSLLAFLRsPEGQvLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGE---DLVCKVADFGLA------RLIK 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124804138 1979 EPCGT-------LAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFP--INKNTEMNIQKNYVL 2036
Cdd:cd05148   156 EDVYLssdkkipYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPgmNNHEVYDQITAGYRM 223
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
1817-2074 3.72e-26

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: 110.54  E-value: 3.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1817 LYNLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVI-YLKEIINTKEtLYI 1895
Cdd:cd14046     4 YLTDFEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRSESKNNSRILR-EVMLLSRLNHQHVVrYYQAWIERAN-LYI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1896 SMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtDKSRDaqIKLTDFGLST-----L 1970
Cdd:cd14046    82 QMEYCEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFL-DSNGN--VKIGDFGLATsnklnV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1971 CAPNELLKEP--------------CGTLAYVAPEVI--TLQGYNHKVDAWSIGIILYlllsgKLPFPINKNTE----MNI 2030
Cdd:cd14046   159 ELATQDINKStsaalgssgdltgnVGTALYVAPEVQsgTKSTYNEKVDMYSLGIIFF-----EMCYPFSTGMErvqiLTA 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 124804138 2031 QKNYVLSFKDYIWKSISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd14046   234 LRSVSIEFPPDFDDNKHSKQAKLIRWLLNHDPAKRPSAQELLKS 277
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
1810-2086 4.63e-26

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 112.22  E-value: 4.63e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1810 SSTKQNTLYNLYELHE--QLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVIYLKEII 1887
Cdd:PLN00034   63 SGSAPSAAKSLSELERvnRIGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTVRRQICR-EIEILRDVNHPNVVKCHDMF 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1888 NTKETLYISMELVKGGELYDFLLA-ETRLSEIHankiiTQLIKTVAYLHRCGIIHRDIKPENILLTDKSRdaqIKLTDFG 1966
Cdd:PLN00034  142 DHNGEIQVLLEFMDGGSLEGTHIAdEQFLADVA-----RQILSGIAYLHRRHIVHRDIKPSNLLINSAKN---VKIADFG 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1967 LSTLCAPNellKEPC----GTLAYVAPEVITLQgYNHKV------DAWSIGI-ILYLLLsGKLPFPINKNTEmniqknyv 2035
Cdd:PLN00034  214 VSRILAQT---MDPCnssvGTIAYMSPERINTD-LNHGAydgyagDIWSLGVsILEFYL-GRFPFGVGRQGD-------- 280
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124804138 2036 lsfkdyiWKSI----------------SSSAKDLISKLLELNVEKRISANEALEHIWVKNPTAVINE 2086
Cdd:PLN00034  281 -------WASLmcaicmsqppeapataSREFRHFISCCLQREPAKRWSAMQLLQHPFILRAQPGQGQ 340
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
1821-2077 5.63e-26

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: 109.46  E-value: 5.63e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEqLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEK--ELLRsEISILRLLRHPNVI-----YLKEiintkETL 1893
Cdd:cd06607     4 EDLRE-IGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTEKwqDIIK-EVKFLRQLRHPNTIeykgcYLRE-----HTA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1894 YISMELVKGG-----ELYDFLLAETrlsEIHAnkIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLS 1968
Cdd:cd06607    77 WLVMEYCLGSasdivEVHKKPLQEV---EIAA--ICHGALQGLAYLHSHNRIHRDVKAGNILLTE---PGTVKLADFGSA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1969 TLCAP-NELLkepcGTLAYVAPEVITL--QG-YNHKVDAWSIGIILYLLLSGKLP-FPINKNTEM-NIQKNYVLSFKDYI 2042
Cdd:cd06607   149 SLVCPaNSFV----GTPYWMAPEVILAmdEGqYDGKVDVWSLGITCIELAERKPPlFNMNAMSALyHIAQNDSPTLSSGE 224
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 124804138 2043 WksiSSSAKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd06607   225 W---SDDFRNFVDSCLQKIPQDRPSAEDLLKHPFV 256
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
1821-2020 6.51e-26

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: 109.34  E-value: 6.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVI----DKRSVSiYEKELLRSEISILRLLRHPNVIYLKEIIN--TKETLY 1894
Cdd:cd06653     4 WRLGKLLGRGAFGEVYLCYDADTGRELAVKQVpfdpDSQETS-KEVNALECEIQLLKNLRHDRIVQYYGCLRdpEEKKLS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILltdksRDA--QIKLTDFGLS---- 1968
Cdd:cd06653    83 IFVEYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANIL-----RDSagNVKLGDFGASkriq 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 124804138 1969 TLCAPNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd06653   158 TICMSGTGIKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPW 209
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
1825-2074 7.23e-26

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: 108.85  E-value: 7.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLK---EIINTKETLYISmELVK 1901
Cdd:cd13983     7 EVLGRGSFKTVYRAFDTEEGIEVAWNEIKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYdswESKSKKEVIFIT-ELMT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1902 GGELYDFLLAETRLSEihanKIIT----QLIKTVAYLHRCG--IIHRDIKPENILLTdkSRDAQIKLTDFGLSTLCAPNE 1975
Cdd:cd13983    86 SGTLKQYLKRFKRLKL----KVIKswcrQILEGLNYLHTRDppIIHRDLKCDNIFIN--GNTGEVKIGDLGLATLLRQSF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1976 lLKEPCGTLAYVAPEVItLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKnyVLS--FKDYIWKSISSSAKDL 2053
Cdd:cd13983   160 -AKSVIGTPEFMAPEMY-EEHYDEKVDIYAFGMCLLEMATGEYPYSECTNAAQIYKK--VTSgiKPESLSKVKDPELKDF 235
                         250       260
                  ....*....|....*....|.
gi 124804138 2054 ISKLLElNVEKRISANEALEH 2074
Cdd:cd13983   236 IEKCLK-PPDERPSARELLEH 255
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
1868-2078 7.39e-26

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: 111.35  E-value: 7.39e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1868 EISILRLLRHPNVIYLKEIINTKETL------YISMELVKGG--ELYDFLLAETRLSeihanKIITQLIKTVAYLHRCGI 1939
Cdd:cd07850    49 ELVLMKLVNHKNIIGLLNVFTPQKSLeefqdvYLVMELMDANlcQVIQMDLDHERMS-----YLLYQMLCGIKHLHSAGI 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1940 IHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLP 2019
Cdd:cd07850   124 IHRDLKPSNIVVKS---DCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVL 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 2020 FP-------INKNTE----------MNIQ---KNYVLS------------FKDYIWKSISSS--------AKDLISKLLE 2059
Cdd:cd07850   201 FPgtdhidqWNKIIEqlgtpsdefmSRLQptvRNYVENrpkyagysfeelFPDVLFPPDSEEhnklkasqARDLLSKMLV 280
                         250
                  ....*....|....*....
gi 124804138 2060 LNVEKRISANEALEHIWVK 2078
Cdd:cd07850   281 IDPEKRISVDDALQHPYIN 299
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
1827-2020 7.79e-26

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: 110.86  E-value: 7.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIdKRSVSIYEK--ELLRSEISILRLL-RHPNVIYLKEIINTKETLYISMELVKGG 1903
Cdd:cd05616     8 LGKGSFGKVMLAERKGTDELYAVKIL-KKDVVIQDDdvECTMVEKRVLALSgKPPFLTQLHSCFQTMDRLYFVMEYVNGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 ELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLstlCAPNEL----LKE 1979
Cdd:cd05616    87 DLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVML---DSEGHIKIADFGM---CKENIWdgvtTKT 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 124804138 1980 PCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd05616   161 FCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPF 201
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
1821-2074 1.06e-25

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: 110.81  E-value: 1.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVS-IYEKELLRsEISILRLLRHPNVIYLKEIINTKETL------ 1893
Cdd:cd07880    17 YRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRPFQSeLFAKRAYR-ELRLLKHMKHENVIGLLDVFTPDLSLdrfhdf 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1894 YISMELVkGGELYDFLLAEtRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLStlcap 1973
Cdd:cd07880    96 YLVMPFM-GTDLGKLMKHE-KLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNE---DCELKILDFGLA----- 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1974 NELLKEPCG---TLAYVAPEVI-TLQGYNHKVDAWSIGIILYLLLSGKLPFP----INKNTE-MNIQ------------- 2031
Cdd:cd07880   166 RQTDSEMTGyvvTRWYRAPEVIlNWMHYTQTVDIWSVGCIMAEMLTGKPLFKghdhLDQLMEiMKVTgtpskefvqklqs 245
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 124804138 2032 ---KNYVLSF-----KDY--IWKSISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd07880   246 edaKNYVKKLprfrkKDFrsLLPNANPLAVNVLEKMLVLDAESRITAAEALAH 298
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
1825-2065 1.11e-25

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: 108.57  E-value: 1.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGinkQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIInTKETLYISMELVKGGE 1904
Cdd:cd14150     6 KRIGTGSFGTVFRG---KWHGDVAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGFM-TRPNFAIITQWCEGSS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFL-LAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTL---CAPNELLKEP 1980
Cdd:cd14150    82 LYRHLhVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHE---GLTVKIGDFGLATVktrWSGSQQVEQP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 CGTLAYVAPEVITLQG---YNHKVDAWSIGIILYLLLSGKLPFP-INKNTEM--NIQKNYVLSFKDYIWKSISSSAKDLI 2054
Cdd:cd14150   159 SGSILWMAPEVIRMQDtnpYSFQSDVYAYGVVLYELMSGTLPYSnINNRDQIifMVGRGYLSPDLSKLSSNCPKAMKRLL 238
                         250
                  ....*....|.
gi 124804138 2055 SKLLELNVEKR 2065
Cdd:cd14150   239 IDCLKFKREER 249
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
1813-2074 1.11e-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: 111.27  E-value: 1.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1813 KQNTLYNLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdKRSVSIYEKELLRS--EISILRLLRHPNVIYLKEIINTK 1890
Cdd:cd05594    19 KHKVTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKIL-KKEVIVAKDEVAHTltENRVLQNSRHPFLTALKYSFQTH 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1891 ETLYISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLH-RCGIIHRDIKPENILLtdkSRDAQIKLTDFGLST 1969
Cdd:cd05594    98 DRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLML---DKDGHIKITDFGLCK 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1970 LCAPN-ELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpINKNTEmniqKNYVLSFKDYIW--KSI 2046
Cdd:cd05594   175 EGIKDgATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF-YNQDHE----KLFELILMEEIRfpRTL 249
                         250       260       270
                  ....*....|....*....|....*....|...
gi 124804138 2047 SSSAKDLISKLLELNVEKRI-----SANEALEH 2074
Cdd:cd05594   250 SPEAKSLLSGLLKKDPKQRLgggpdDAKEIMQH 282
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
1827-2020 1.17e-25

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: 108.86  E-value: 1.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRG-----------INKQTNSEFAIKVID------KRSVSIYEKELLRSEISILRLLRHPNVIYLKEIinT 1889
Cdd:cd14000     2 LGDGGFGSVYRAsykgepvavkiFNKHTSSNFANVPADtmlrhlRATDAMKNFRLLRQELTVLSHLHHPSIVYLLGI--G 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1890 KETLYISMELVKGGELyDFLLAETRLSEIH-----ANKIITQLIKTVAYLHRCGIIHRDIKPENILL--TDKSRDAQIKL 1962
Cdd:cd14000    80 IHPLMLVLELAPLGSL-DHLLQQDSRSFASlgrtlQQRIALQVADGLRYLHSAMIIYRDLKSHNVLVwtLYPNSAIIIKI 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 124804138 1963 TDFGLSTLCAPnELLKEPCGTLAYVAPEVITLQG-YNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd14000   159 ADYGISRQCCR-MGAKGSEGTPGFRAPEIARGNViYNEKVDVFSFGMLLYEILSGGAPM 216
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
1821-2077 1.28e-25

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: 109.94  E-value: 1.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdKRSVSIYEKELLrsEISILRLLRH------PNVIYLKEIINTKETLY 1894
Cdd:cd14210    15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKII-RNKKRFHQQALV--EVKILKHLNDndpddkHNIVRYKDSFIFRGHLC 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVkGGELYDFLLAET--RLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRdAQIKLTDFGLStlCA 1972
Cdd:cd14210    92 IVFELL-SINLYELLKSNNfqGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSK-SSIKVIDFGSS--CF 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1973 PNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFP----------------------INKNT---- 2026
Cdd:cd14210   168 EGEKVYTYIQSRFYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPgeneeeqlacimevlgvppkslIDKASrrkk 247
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124804138 2027 ---EMNIQKNYVLSFKDYIWKSISSSAK----------DLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14210   248 ffdSNGKPRPTTNSKGKKRRPGSKSLAQvlkcddpsflDFLKKCLRWDPSERMTPEEALQHPWI 311
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
1827-2020 1.30e-25

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: 108.25  E-value: 1.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGinkQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIInTKETLYISMELVKGGELY 1906
Cdd:cd14062     1 IGSGSFGTVYKG---RWHGDVAVKKLNVTDPTPSQLQAFKNEVAVLRKTRHVNILLFMGYM-TKPQLAIVTQWCEGSSLY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1907 DFL-LAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTL---CAPNELLKEPCG 1982
Cdd:cd14062    77 KHLhVLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHE---DLTVKIGDFGLATVktrWSGSQQFEQPTG 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 124804138 1983 TLAYVAPEVITLQG---YNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd14062   154 SILWMAPEVIRMQDenpYSFQSDVYAFGIVLYELLTGQLPY 194
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
1822-2034 1.78e-25

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: 108.26  E-value: 1.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1822 ELHEQLGQGKFSTVYRGI-NKQTnsEFAIKVIDKRSVSiyEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd05068    11 KLLRKLGSGQFGEVWEGLwNNTT--PVAVKTLKPGTMD--PEDFLR-EAQIMKKLRHPKLIQLYAVCTLEEPIYIITELM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRlsEIHANKII---TQLIKTVAYLHRCGIIHRDIKPENILLTDKSrdaQIKLTDFGLSTLCAPNELL 1977
Cdd:cd05068    86 KHGSLLEYLQGKGR--SLQLPQLIdmaAQVASGMAYLESQNYIHRDLAARNVLVGENN---ICKVADFGLARVIKVEDEY 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124804138 1978 KEPCGT---LAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFPINKNTEM--NIQKNY 2034
Cdd:cd05068   161 EAREGAkfpIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTyGRIPYPGMTNAEVlqQVERGY 223
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
1826-2058 2.59e-25

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: 110.51  E-value: 2.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1826 QLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIY-EKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGE 1904
Cdd:cd05600    18 QVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLnEVNHVLTERDILTTTNSPWLVKLLYAFQDPENVYLAMEYVPGGD 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtDKSrdAQIKLTDFGLSTLCAPNEL-------L 1977
Cdd:cd05600    98 FRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLI-DSS--GHIKLTDFGLASGTLSPKKiesmkirL 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEP-------------------------------CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPIN--K 2024
Cdd:cd05600   175 EEVkntafleltakerrniyramrkedqnyansvVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFSGStpN 254
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 124804138 2025 NTEMNIqKNYVLSFKDYIWK------SISSSAKDLISKLL 2058
Cdd:cd05600   255 ETWANL-YHWKKTLQRPVYTdpdlefNLSDEAWDLITKLI 293
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
1827-2074 3.02e-25

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: 108.00  E-value: 3.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLR-SEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGEL 1905
Cdd:cd05577     1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMAlNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1906 YDFL--LAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPNELLKEPCGT 1983
Cdd:cd05577    81 KYHIynVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDD---HGHVRISDLGLAVEFKGGKKIKGRVGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1984 LAYVAPEVITLQ-GYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQ-KNYVLSFKDYIWKSISSSAKDLISKLLELN 2061
Cdd:cd05577   158 HGYMAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEElKRRTLEMAVEYPDSFSPEARSLCEGLLQKD 237
                         250
                  ....*....|....*...
gi 124804138 2062 VEKRI-----SANEALEH 2074
Cdd:cd05577   238 PERRLgcrggSADEVKEH 255
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
1821-2074 3.49e-25

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: 108.40  E-value: 3.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdkrsVSIYEKELLRsEISILRLLR-HPNVIYLKEIINTKETLYIS--M 1897
Cdd:cd14132    20 YEIIRKIGRGKYSEVFEGINIGNNEKVVIKVL----KPVKKKKIKR-EIKILQNLRgGPNIVKLLDVVKDPQSKTPSliF 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGgelYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENIlLTDKSRDaQIKLTDFGLSTLCAPNELL 1977
Cdd:cd14132    95 EYVNN---TDFKTLYPTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNI-MIDHEKR-KLRLIDWGLAEFYHPGQEY 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPCGTLAYVAPEV-ITLQGYNHKVDAWSIGIILYLLLSGKLP-FPINKNTEM--------------------NIQ---- 2031
Cdd:cd14132   170 NVRVASRYYKGPELlVDYQYYDYSLDMWSLGCMLASMIFRKEPfFHGHDNYDQlvkiakvlgtddlyayldkyGIElppr 249
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 124804138 2032 -KNYVLSFKDYIWKS---------ISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd14132   250 lNDILGRHSKKPWERfvnsenqhlVTPEALDLLDKLLRYDHQERITAKEAMQH 302
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
1821-2072 3.57e-25

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: 106.98  E-value: 3.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd08219     2 YNVLRVVGEGSFGRALLVQHVNSDQKYAMKEI-RLPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFL-LAETRL-SEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLSTLCA-PNELL 1977
Cdd:cd08219    81 DGGDLMQKIkLQRGKLfPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLT---QNGKVKLGDFGSARLLTsPGAYA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpinkntEMNIQKNYVLSFKDYIWKSI----SSSAKDL 2053
Cdd:cd08219   158 CTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPF------QANSWKNLILKVCQGSYKPLpshySYELRSL 231
                         250
                  ....*....|....*....
gi 124804138 2054 ISKLLELNVEKRISANEAL 2072
Cdd:cd08219   232 IKQMFKRNPRSRPSATTIL 250
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
1825-2065 3.63e-25

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: 107.37  E-value: 3.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSEFAIK---VIDKRSVsiyekELLRSEISILRLLR-HPNVI-YLKEIIN-TKETLY---I 1895
Cdd:cd14037     9 KYLAEGGFAHVYLVKTSNGGNRAALKrvyVNDEHDL-----NVCKREIEIMKRLSgHKNIVgYIDSSANrSGNGVYevlL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1896 SMELVKGGELYDFLLA--ETRLSEIHANKIITQLIKTVAYLHRCG--IIHRDIKPENILLTDKSrdaQIKLTDFGLSTLC 1971
Cdd:cd14037    84 LMEYCKGGGVIDLMNQrlQTGLTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSG---NYKLCDFGSATTK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1972 APN------------ELLKEPcgTLAYVAPEVITL---QGYNHKVDAWSIGIILYLLLSGKLPFpiNKNTEMNIQK-NYv 2035
Cdd:cd14037   161 ILPpqtkqgvtyveeDIKKYT--TLQYRAPEMIDLyrgKPITEKSDIWALGCLLYKLCFYTTPF--EESGQLAILNgNF- 235
                         250       260       270
                  ....*....|....*....|....*....|
gi 124804138 2036 lSFKDYiwKSISSSAKDLISKLLELNVEKR 2065
Cdd:cd14037   236 -TFPDN--SRYSKRLHKLIRYMLEEDPEKR 262
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
1821-2074 4.75e-25

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: 107.46  E-value: 4.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIK-VIDKRSVSIYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd07847     3 YEKLSKIGEGSYGVVFKCRNRETGQIVAIKkFVESEDDPVIKKIALR-EIRMLKQLKHPNLVNLIEVFRRKRKLHLVFEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLS-TLCAPNELLK 1978
Cdd:cd07847    82 CDHTVLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILIT---KQGQIKLCDFGFArILTGPGDDYT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1979 EPCGTLAYVAPEVIT--LQgYNHKVDAWSIGIILYLLLSGKLPFP----------INKNT-EMNIQKNYVLSFKDYI--- 2042
Cdd:cd07847   159 DYVATRWYRAPELLVgdTQ-YGPPVDVWAIGCVFAELLTGQPLWPgksdvdqlylIRKTLgDLIPRHQQIFSTNQFFkgl 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 124804138 2043 --------------WKSISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd07847   238 sipepetrepleskFPNISSPALSFLKGCLQMDPTERLSCEELLEH 283
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
1821-2079 4.93e-25

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 107.60  E-value: 4.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSvsiyEKELLRS----EISILRLLRHPNVIYLKEIINTKETLYIS 1896
Cdd:PLN00009    4 YEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQ----EDEGVPStairEISLLKEMQHGNIVRLQDVVHSEKRLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1897 MELVKGgELYDFLLAETRLSEIH--ANKIITQLIKTVAYLHRCGIIHRDIKPENiLLTDKSRDAqIKLTDFGLS-TLCAP 1973
Cdd:PLN00009   80 FEYLDL-DLKKHMDSSPDFAKNPrlIKTYLYQILRGIAYCHSHRVLHRDLKPQN-LLIDRRTNA-LKLADFGLArAFGIP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1974 NELLKEPCGTLAYVAPEVIT-LQGYNHKVDAWSIGIILYLLLSGKLPFPinKNTEMN-IQKNY-------------VLSF 2038
Cdd:PLN00009  157 VRTFTHEVVTLWYRAPEILLgSRHYSTPVDIWSVGCIFAEMVNQKPLFP--GDSEIDeLFKIFrilgtpneetwpgVTSL 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 124804138 2039 KDYI-----WKS---------ISSSAKDLISKLLELNVEKRISANEALEHIWVKN 2079
Cdd:PLN00009  235 PDYKsafpkWPPkdlatvvptLEPAGVDLLSKMLRLDPSKRITARAALEHEYFKD 289
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
1827-2020 5.25e-25

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: 108.46  E-value: 5.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIdKRSVSIYEK--ELLRSEISILRLLR-HPNVIYLKEIINTKETLYISMELVKGG 1903
Cdd:cd05590     3 LGKGSFGKVMLARLKESGRLYAVKVL-KKDVILQDDdvECTMTEKRILSLARnHPFLTQLYCCFQTPDRLFFVMEFVNGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 ELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCAPNELLKEP-CG 1982
Cdd:cd05590    82 DLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLL---DHEGHCKLADFGMCKEGIFNGKTTSTfCG 158
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 124804138 1983 TLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd05590   159 TPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPF 196
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
1821-2074 5.55e-25

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: 107.12  E-value: 5.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSvsiyEKELLRS----EISILRLLRHPNVIYLKEIINTKETLYI- 1895
Cdd:cd07861     2 YTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLES----EEEGVPStairEISLLKELQHPNIVCLEDVLMQENRLYLv 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1896 ----SMELVK------GGELYDFLLAETRLSeihankiitQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDF 1965
Cdd:cd07861    78 feflSMDLKKyldslpKGKYMDAELVKSYLY---------QILQGILFCHSRRVLHRDLKPQNLLIDNK---GVIKLADF 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1966 GLS-TLCAPNELLKEPCGTLAYVAPEVIT-LQGYNHKVDAWSIGIILYLLLSGKLPF----PINK--------NTEMNIQ 2031
Cdd:cd07861   146 GLArAFGIPVRVYTHEVVTLWYRAPEVLLgSPRYSTPVDIWSIGTIFAEMATKKPLFhgdsEIDQlfrifrilGTPTEDI 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 124804138 2032 KNYVLSFKDY-----IW---------KSISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd07861   226 WPGVTSLPDYkntfpKWkkgslrtavKNLDEDGLDLLEKMLIYDPAKRISAKKALVH 282
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
1821-2077 5.83e-25

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: 106.65  E-value: 5.83e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEkeLLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd06646    11 YELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPGDDFS--LIQQEIFMVKECKHCNIVAYFGSYLSREKLWICMEYC 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLST-LCAPNELLKE 1979
Cdd:cd06646    89 GGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTD---NGDVKLADFGVAAkITATIAKRKS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 PCGTLAYVAPEVITLQ---GYNHKVDAWSIGIILYLLLSGKLPF----PINKNTEMNIQKNYVLSFKDYI-WksiSSSAK 2051
Cdd:cd06646   166 FIGTPYWMAPEVAAVEkngGYNQLCDIWAVGITAIELAELQPPMfdlhPMRALFLMSKSNFQPPKLKDKTkW---SSTFH 242
                         250       260
                  ....*....|....*....|....*.
gi 124804138 2052 DLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd06646   243 NFVKISLTKNPKKRPTAERLLTHLFV 268
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
1825-2020 5.97e-25

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: 106.70  E-value: 5.97e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKqtNSEFAIKVIDKRSVSIYEKELLRSEISILRLlRHPNVIYLKEII--NTKETL-YISMELVK 1901
Cdd:cd13979     9 EPLGSGGFGSVYKATYK--GETVAVKIVRRRRKNRASRQSFWAELNAARL-RHENIVRVLAAEtgTDFASLgLIIMEYCG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1902 GGELYDFLL-AETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLStlcapnELLKEP 1980
Cdd:cd13979    86 NGTLQQLIYeGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISE---QGVCKLCDFGCS------VKLGEG 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 C----------GTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd13979   157 NevgtprshigGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPY 206
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
1827-2066 6.97e-25

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: 107.86  E-value: 6.97e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIdKRSVSIYEK--ELLRSEISILRLLRHPN-VIYLKEIINTKETLYISMELVKGG 1903
Cdd:cd05587     4 LGKGSFGKVMLAERKGTDELYAIKIL-KKDVIIQDDdvECTMVEKRVLALSGKPPfLTQLHSCFQTMDRLYFVMEYVNGG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 ELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLstlCAPN----ELLKE 1979
Cdd:cd05587    83 DLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML---DAEGHIKIADFGM---CKEGifggKTTRT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 PCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEM--NIQKNYVlSFKdyiwKSISSSAKDLISKL 2057
Cdd:cd05587   157 FCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELfqSIMEHNV-SYP----KSLSKEAVSICKGL 231

                  ....*....
gi 124804138 2058 LELNVEKRI 2066
Cdd:cd05587   232 LTKHPAKRL 240
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
1825-2079 7.06e-25

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: 107.77  E-value: 7.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELVKGgE 1904
Cdd:cd07872    12 EKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAIR-EVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLDK-D 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAETRLSEIHANKI-ITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLS-TLCAPNELLKEPCG 1982
Cdd:cd07872    90 LKQYMDDCGNIMSMHNVKIfLYQILRGLAYCHRRKVLHRDLKPQNLLINER---GELKLADFGLArAKSVPTKTYSNEVV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1983 TLAYVAPEVITLQG-YNHKVDAWSIGIILYLLLSGKLPFPINK-NTEMNIQKNYVLSFKDYIWKSISSSAK--------- 2051
Cdd:cd07872   167 TLWYRPPDVLLGSSeYSTQIDMWGVGCIFFEMASGRPLFPGSTvEDELHLIFRLLGTPTEETWPGISSNDEfknynfpky 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 124804138 2052 -----------------DLISKLLELNVEKRISANEALEHIWVKN 2079
Cdd:cd07872   247 kpqplinhaprldtegiELLTKFLQYESKKRISAEEAMKHAYFRS 291
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
1820-2042 7.55e-25

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: 106.68  E-value: 7.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1820 LYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSiYEKELLRSEISILRLLRHPNVI-----YLKeiintKETLY 1894
Cdd:cd06642     5 LFTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAE-DEIEDIQQEITVLSQCDSPYITryygsYLK-----GTKLW 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVKGGELYDfLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLCAPN 1974
Cdd:cd06642    79 IIMEYLGGGSALD-LLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQ---GDVKLADFGVAGQLTDT 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124804138 1975 ELLKEP-CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLP----------FPINKNTEMNIQKNYVLSFKDYI 2042
Cdd:cd06642   155 QIKRNTfVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPnsdlhpmrvlFLIPKNSPPTLEGQHSKPFKEFV 233
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
1821-2075 1.10e-24

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: 106.23  E-value: 1.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVI---DKRSVsiyeKELLRsEISILRLLRHPNVIYL-----KEIINTKET 1892
Cdd:cd13986     2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKIlchSKEDV----KEAMR-EIENYRLFNHPNILRLldsqiVKEAGGKKE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1893 LYISMELVKGGELYDFL----LAETRLSEIHANKIITQLIKTVAYLH---RCGIIHRDIKPENILLTDksrDAQIKLTDF 1965
Cdd:cd13986    77 VYLLLPYYKRGSLQDEIerrlVKGTFFPEDRILHIFLGICRGLKAMHepeLVPYAHRDIKPGNVLLSE---DDEPILMDL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1966 G---LSTLCAPN--------ELLKEPCgTLAYVAPEVITLQGY---NHKVDAWSIGIILYLLLSGKLPFpinkntEMNIQ 2031
Cdd:cd13986   154 GsmnPARIEIEGrrealalqDWAAEHC-TMPYRAPELFDVKSHctiDEKTDIWSLGCTLYALMYGESPF------ERIFQ 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 124804138 2032 KNYVLSF----KDYIWK---SISSSAKDLISKLLELNVEKRISANEALEHI 2075
Cdd:cd13986   227 KGDSLALavlsGNYSFPdnsRYSEELHQLVKSMLVVNPAERPSIDDLLSRV 277
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
1827-2073 1.27e-24

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: 105.42  E-value: 1.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQtnSEFAIKVIDKRSVSiyekELLRSEISILRLLRHPNVIYLkeIINTKETLYISMELVKGGELy 1906
Cdd:cd14068     2 LGDGGFGSVYRAVYRG--EDVAVKIFNKHTSF----RLLRQELVVLSHLHHPSLVAL--LAAGTAPRMLVMELAPKGSL- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1907 DFLLAETR--LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQI--KLTDFGLSTLCApNELLKEPCG 1982
Cdd:cd14068    73 DALLQQDNasLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNCAIiaKIADYGIAQYCC-RMGIKTSEG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1983 TLAYVAPEVItlQG---YNHKVDAWSIGIILYLLLSG------KLPFPiNKNTEMNIQKNYVLSFKDY---IWKSISSsa 2050
Cdd:cd14068   152 TPGFRAPEVA--RGnviYNQQADVYSFGLLLYDILTCgeriveGLKFP-NEFDELAIQGKLPDPVKEYgcaPWPGVEA-- 226
                         250       260
                  ....*....|....*....|...
gi 124804138 2051 kdLISKLLELNVEKRISANEALE 2073
Cdd:cd14068   227 --LIKDCLKENPQCRPTSAQVFD 247
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
1821-2074 1.55e-24

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: 105.20  E-value: 1.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSV-SIYEKELLRS--EISILRLLRHPNVIYLKEIINTKETLYISM 1897
Cdd:cd08222     2 YRVVRKLGSGNFGTVYLVSDLKATADEELKVLKEISVgELQPDETVDAnrEAKLLSKLDHPAIVKFHDSFVEKESFCIVT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGGELyDFLLAETRLS--EIHANKIIT---QLIKTVAYLHRCGIIHRDIKPENILLtdksRDAQIKLTDFGLS-TLC 1971
Cdd:cd08222    82 EYCEGGDL-DDKISEYKKSgtTIDENQILDwfiQLLLAVQYMHERRILHRDLKAKNIFL----KNNVIKVGDFGISrILM 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1972 APNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpINKNTeMNIQKNYVLSFKDYIWKSISSSAK 2051
Cdd:cd08222   157 GTSDLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAF-DGQNL-LSVMYKIVEGETPSLPDKYSKELN 234
                         250       260
                  ....*....|....*....|...
gi 124804138 2052 DLISKLLELNVEKRISANEALEH 2074
Cdd:cd08222   235 AIYSRMLNKDPALRPSAAEILKI 257
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
1821-2088 1.84e-24

Catalytic domain of the Serine/Threonine Kinases, Plant TDY 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 TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. 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 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY 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: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 107.17  E-value: 1.84e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEII-----NTKETLYI 1895
Cdd:cd07859     2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSDATRILREIKLLRLLRHPDIVEIKHIMlppsrREFKDIYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1896 SMELVkGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILltdKSRDAQIKLTDFGL---STLCA 1972
Cdd:cd07859    82 VFELM-ESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNIL---ANADCKLKICDFGLarvAFNDT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1973 PNELL-KEPCGTLAYVAPEVIT--LQGYNHKVDAWSIGIILYLLLSGKLPFPiNKN------------------------ 2025
Cdd:cd07859   158 PTAIFwTDYVATRWYRAPELCGsfFSKYTPAIDIWSIGCIFAEVLTGKPLFP-GKNvvhqldlitdllgtpspetisrvr 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124804138 2026 --------TEMNIQKNYVLSFKdyiWKSISSSAKDLISKLLELNVEKRISANEALEHIWVKNPTAVINENS 2088
Cdd:cd07859   237 nekarrylSSMRKKQPVPFSQK---FPNADPLALRLLERLLAFDPKDRPTAEEALADPYFKGLAKVEREPS 304
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
1827-2066 2.05e-24

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: 106.57  E-value: 2.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEK-ELLRSEISILRLL-RHPNVIYLKEIINTKETLYISMELVKGGE 1904
Cdd:cd05620     3 LGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDDvECTMVEKRVLALAwENPFLTHLYCTFQTKEHLFFVMEFLNGGD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLstlCAPNELLKEP---- 1980
Cdd:cd05620    83 LMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVML---DRDGHIKIADFGM---CKENVFGDNRastf 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEM--NIQKNyvlsfKDYIWKSISSSAKDLISKLL 2058
Cdd:cd05620   157 CGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELfeSIRVD-----TPHYPRWITKESKDILEKLF 231

                  ....*...
gi 124804138 2059 ELNVEKRI 2066
Cdd:cd05620   232 ERDPTRRL 239
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
1827-2074 2.45e-24

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: 105.16  E-value: 2.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVI--DKRSVSIY-EKELLRSEISILRLLRHPNVIYLKEII--NTKETLYISMELVK 1901
Cdd:cd06651    15 LGQGAFGRVYLCYDVDTGRELAAKQVqfDPESPETSkEVSALECEIQLLKNLQHERIVQYYGCLrdRAEKTLTIFMEYMP 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1902 GGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILltdKSRDAQIKLTDFG----LSTLCAPNELL 1977
Cdd:cd06651    95 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL---RDSAGNVKLGDFGaskrLQTICMSGTGI 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPiNKNTEMNIQKNYVLSFKDYIWKSISSSAKDLISKL 2057
Cdd:cd06651   172 RSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA-EYEAMAAIFKIATQPTNPQLPSHISEHARDFLGCI 250
                         250
                  ....*....|....*..
gi 124804138 2058 LeLNVEKRISANEALEH 2074
Cdd:cd06651   251 F-VEARHRPSAEELLRH 266
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
1820-2067 3.01e-24

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: 104.77  E-value: 3.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1820 LYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSiYEKELLRSEISILRLLRHPNVI--YLKEIINTKetLYISM 1897
Cdd:cd06641     5 LFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAE-DEIEDIQQEITVLSQCDSPYVTkyYGSYLKDTK--LWIIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGGELYDfLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCAPNELL 1977
Cdd:cd06641    82 EYLGGGSALD-LLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLL---SEHGEVKLADFGVAGQLTDTQIK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEP-CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLP----------FPINKNTEMNIQKNYVLSFKDYIWK-- 2044
Cdd:cd06641   158 RN*fVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPhselhpmkvlFLIPKNNPPTLEGNYSKPLKEFVEAcl 237
                         250       260
                  ....*....|....*....|....*..
gi 124804138 2045 ----SISSSAKDLISKLLELNVEKRIS 2067
Cdd:cd06641   238 nkepSFRPTAKELLKHKFILRNAKKTS 264
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
1827-2020 3.02e-24

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: 104.40  E-value: 3.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKqtNSEFAIKVI-----DKRSVSIyekELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVK 1901
Cdd:cd14061     2 IGVGGFGKVYRGIWR--GEEVAVKAArqdpdEDISVTL---ENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYAR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1902 GGELYDFLLAETRLSEIHANKIItQLIKTVAYLHRCG---IIHRDIKPENILLTDKSRDAQI-----KLTDFGLStlcap 1973
Cdd:cd14061    77 GGALNRVLAGRKIPPHVLVDWAI-QIARGMNYLHNEApvpIIHRDLKSSNILILEAIENEDLenktlKITDFGLA----- 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 124804138 1974 NELLK----EPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd14061   151 REWHKttrmSAAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPY 201
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
1823-2074 3.80e-24

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: 104.73  E-value: 3.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1823 LHEQLGQGKFSTVYRGinkQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIInTKETLYISMELVKG 1902
Cdd:cd14149    16 LSTRIGSGSFGTVYKG---KWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYM-TKDNLAIVTQWCEG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1903 GELYDFL-LAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAP---NELLK 1978
Cdd:cd14149    92 SSLYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHE---GLTVKIGDFGLATVKSRwsgSQQVE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1979 EPCGTLAYVAPEVITLQG---YNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNI---QKNYVLSFKDYIWKSISSSAKD 2052
Cdd:cd14149   169 QPTGSILWMAPEVIRMQDnnpFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIfmvGRGYASPDLSKLYKNCPKAMKR 248
                         250       260
                  ....*....|....*....|....*...
gi 124804138 2053 LISKLLELNVEKR------ISANEALEH 2074
Cdd:cd14149   249 LVADCIKKVKEERplfpqiLSSIELLQH 276
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
1821-2078 5.04e-24

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: 104.69  E-value: 5.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDkrSVSIYEKELlRSEISILRLL-RHPNVI-----YLKEIINTKETLY 1894
Cdd:cd06639    24 WDIIETIGKGTYGKVYKVTNKKDGSLAAVKILD--PISDVDEEI-EAEYNILRSLpNHPNVVkfygmFYKADQYVGGQLW 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVKGGELYDF----LLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLSTL 1970
Cdd:cd06639   101 LVLELCNGGSVTELvkglLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLT---TEGGVKLVDFGVSAQ 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1971 CAPNELLKE-PCGTLAYVAPEVITLQ-----GYNHKVDAWSIGIILYLLLSGKLP----------FPINKN---TEMNIQ 2031
Cdd:cd06639   178 LTSARLRRNtSVGTPFWMAPEVIACEqqydySYDARCDVWSLGITAIELADGDPPlfdmhpvkalFKIPRNpppTLLNPE 257
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 124804138 2032 KnYVLSFKDYiwksisssakdlISKLLELNVEKRISANEALEHIWVK 2078
Cdd:cd06639   258 K-WCRGFSHF------------ISQCLIKDFEKRPSVTHLLEHPFIK 291
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
1820-2077 5.19e-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: 103.51  E-value: 5.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1820 LYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYeKEL---LRSEISILRLLR----HPNVIYLKEIINTKET 1892
Cdd:cd14100     1 QYQVGPLLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSEW-GELpngTRVPMEIVLLKKvgsgFRGVIRLLDWFERPDS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1893 LYISME---LVKggELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtDKSRdAQIKLTDFGLST 1969
Cdd:cd14100    80 FVLVLErpePVQ--DLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILI-DLNT-GELKLIDFGSGA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1970 LCApNELLKEPCGTLAYVAPEVITLQGYNHKVDA-WSIGIILYLLLSGKLPFPinkntemniQKNYVLSFKDYIWKSISS 2048
Cdd:cd14100   156 LLK-DTVYTDFDGTRVYSPPEWIRFHRYHGRSAAvWSLGILLYDMVCGDIPFE---------HDEEIIRGQVFFRQRVSS 225
                         250       260
                  ....*....|....*....|....*....
gi 124804138 2049 SAKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14100   226 ECQHLIKWCLALRPSDRPSFEDIQNHPWM 254
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
1822-2076 5.21e-24

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: 106.37  E-value: 5.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1822 ELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDK---RSVSIyeKELLRsEISILRLLRHPNVIYLKEIINTK-----ETL 1893
Cdd:cd07853     3 EPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNvfqNLVSC--KRVFR-ELKMLCFFKHDNVLSALDILQPPhidpfEEI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1894 YISMELVKGgELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAP 1973
Cdd:cd07853    80 YVVTELMQS-DLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNS---NCVLKICDFGLARVEEP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1974 NE--LLKEPCGTLAYVAPEVIT-LQGYNHKVDAWSIGIILYLLLSGKLPF----PINK------------NTEMNIQ--- 2031
Cdd:cd07853   156 DEskHMTQEVVTQYYRAPEILMgSRHYTSAVDIWSVGCIFAELLGRRILFqaqsPIQQldlitdllgtpsLEAMRSAceg 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 124804138 2032 -KNYVLSFKD---------YIWKSISSSAKDLISKLLELNVEKRISANEALEHIW 2076
Cdd:cd07853   236 aRAHILRGPHkppslpvlyTLSSQATHEAVHLLCRMLVFDPDKRISAADALAHPY 290
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
1821-2077 6.84e-24

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: 103.59  E-value: 6.84e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEkeLLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd06645    13 FELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFA--VVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEFC 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLST-LCAPNELLKE 1979
Cdd:cd06645    91 GGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTD---NGHVKLADFGVSAqITATIAKRKS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 PCGTLAYVAPEVITLQ---GYNHKVDAWSIGIILYLLLSGKLPF----PINKNTEMNIQKNYVLSFKDYI-WksiSSSAK 2051
Cdd:cd06645   168 FIGTPYWMAPEVAAVErkgGYNQLCDIWAVGITAIELAELQPPMfdlhPMRALFLMTKSNFQPPKLKDKMkW---SNSFH 244
                         250       260
                  ....*....|....*....|....*.
gi 124804138 2052 DLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd06645   245 HFVKMALTKNPKKRPTAEKLLQHPFV 270
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
1822-2020 7.25e-24

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: 103.58  E-value: 7.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1822 ELHEQLGQGKFSTVYRGinkQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVK 1901
Cdd:cd14063     3 EIKEVIGKGRFGRVHRG---RWHGDVAIKLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTSLCK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1902 GGELYDFLlaETRLSEIHANKII---TQLIKTVAYLHRCGIIHRDIKPENILLtDKSRdaqIKLTDFGLSTLCA------ 1972
Cdd:cd14063    80 GRTLYSLI--HERKEKFDFNKTVqiaQQICQGMGYLHAKGIIHKDLKSKNIFL-ENGR---VVITDFGLFSLSGllqpgr 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 124804138 1973 PNELLKEPCGTLAYVAPEVIT----------LQGYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd14063   154 REDTLVIPNGWLCYLAPEIIRalspdldfeeSLPFTKASDVYAFGTVWYELLAGRWPF 211
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
1826-2020 9.58e-24

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: 103.67  E-value: 9.58e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1826 QLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVI-YLKEIINTKETLYISMELVKGGE 1904
Cdd:cd06620    12 DLGAGNGGSVSKVLHIPTGTIMAKKVIHIDAKSSVRKQILR-ELQILHECHSPYIVsFYGAFLNENNNIIICMEYMDCGS 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAETRLSEIHANKIITQLIKTVAYL---HRcgIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLCApNELLKEPC 1981
Cdd:cd06620    91 LDKILKKKGPFPEEVLGKIAVAVLEGLTYLynvHR--IIHRDIKPSNILVNSK---GQIKLCDFGVSGELI-NSIADTFV 164
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 124804138 1982 GTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd06620   165 GTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPF 203
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
1823-2020 1.03e-23

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: 103.22  E-value: 1.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1823 LHEQLGQGKFSTVYRGinkQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIiNTKETLYISMELVKG 1902
Cdd:cd14151    12 VGQRIGSGSFGTVYKG---KWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGY-STKPQLAIVTQWCEG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1903 GELYDFL-LAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTL---CAPNELLK 1978
Cdd:cd14151    88 SSLYHHLhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHE---DLTVKIGDFGLATVksrWSGSHQFE 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 124804138 1979 EPCGTLAYVAPEVITLQG---YNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd14151   165 QLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPY 209
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
1827-2020 1.18e-23

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: 102.76  E-value: 1.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKqtNSEFAIKVI--DKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGE 1904
Cdd:cd14148     2 IGVGGFGKVYKGLWR--GEEVAVKAArqDPDEDIAVTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAETRLSEIHANKIItQLIKTVAYLHR---CGIIHRDIKPENILLTDKSR-----DAQIKLTDFGLStlcapNEL 1976
Cdd:cd14148    80 LNRALAGKKVPPHVLVNWAV-QIARGMNYLHNeaiVPIIHRDLKSSNILILEPIEnddlsGKTLKITDFGLA-----REW 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 124804138 1977 LK----EPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd14148   154 HKttkmSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPY 201
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
1821-2074 1.26e-23

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: 103.03  E-value: 1.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVI-YLKEIINT-------KET 1892
Cdd:cd14048     8 FEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPNNELAREKVLR-EVRALAKLDHPGIVrYFNAWLERppegwqeKMD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1893 ---LYISMELVKGGELYDFLLAETRLS--EIHANK-IITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFG 1966
Cdd:cd14048    87 evyLYIQMQLCRKENLKDWMNRRCTMEsrELFVCLnIFKQIASAVEYLHSKGLIHRDLKPSNVFF---SLDDVVKVGDFG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1967 LSTLC---APNELLKEP----------CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLsgkLPFpinkntemNIQKN 2033
Cdd:cd14048   164 LVTAMdqgEPEQTVLTPmpayakhtgqVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELI---YSF--------STQME 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 124804138 2034 YVLSFKDY-------IWKSISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd14048   233 RIRTLTDVrklkfpaLFTNKYPEERDMVQQMLSPSPSERPEAHEVIEH 280
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
1822-2034 1.32e-23

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: 102.66  E-value: 1.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1822 ELHEQLGQGKFSTVYRGINKqTNSEFAIKVIDKRSVSIyekELLRSEISILRLLRHPNVIYLKEIInTKETLYISMELVK 1901
Cdd:cd05067    10 KLVERLGAGQFGEVWMGYYN-GHTKVAIKSLKQGSMSP---DAFLAEANLMKQLQHQRLVRLYAVV-TQEPIYIITEYME 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1902 GGELYDFLLAETRLsEIHANKII---TQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCAPNELL- 1977
Cdd:cd05067    85 NGSLVDFLKTPSGI-KLTINKLLdmaAQIAEGMAFIEERNYIHRDLRAANILV---SDTLSCKIADFGLARLIEDNEYTa 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124804138 1978 ----KEPcgtLAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFPINKNTEM--NIQKNY 2034
Cdd:cd05067   161 regaKFP---IKWTAPEAINYGTFTIKSDVWSFGILLTEIVThGRIPYPGMTNPEViqNLERGY 221
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
1821-2070 1.37e-23

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: 104.18  E-value: 1.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdkRSVSIYEKELLRSEISILRLL--RHPNVIYLKEII----------- 1887
Cdd:cd13977     2 YSLIREVGRGSYGVVYEAVVRRTGARVAVKKI--RCNAPENVELALREFWALSSIqrQHPNVIQLEECVlqrdglaqrms 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1888 --NTKETLYIS-----------------------MELVKGGELYDFLLAEtRLSEIHANKIITQLIKTVAYLHRCGIIHR 1942
Cdd:cd13977    80 hgSSKSDLYLLlvetslkgercfdprsacylwfvMEFCDGGDMNEYLLSR-RPDRQTNTSFMLQLSSALAFLHRNQIVHR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1943 DIKPENILLTDKSRDAQIKLTDFGLSTLCAPNEL------------LKEPCGTLAYVAPEVitLQG-YNHKVDAWSIGII 2009
Cdd:cd13977   159 DLKPDNILISHKRGEPILKVADFGLSKVCSGSGLnpeepanvnkhfLSSACGSDFYMAPEV--WEGhYTAKADIFALGII 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 2010 LYLLLSgKLPFpINKNTEMNIQKNYVLSFKDYI--------------------WKSISSSAKDLISKLLELNVEKRISAN 2069
Cdd:cd13977   237 IWAMVE-RITF-RDGETKKELLGTYIQQGKEIVplgeallenpklelqiplkkKKSMNDDMKQLLRDMLAANPQERPDAF 314

                  .
gi 124804138 2070 E 2070
Cdd:cd13977   315 Q 315
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1821-2074 1.80e-23

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: 102.13  E-value: 1.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKE-TLYISMEL 1899
Cdd:cd08223     2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEDgFLYIVMGF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAE--TRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLS-TLCAPNEL 1976
Cdd:cd08223    82 CEGGDLYTRLKEQkgVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLT---KSNIIKVGDLGIArVLESSSDM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1977 LKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpinKNTEMNIQKNYVLSFK-DYIWKSISSSAKDLIS 2055
Cdd:cd08223   159 ATTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAF---NAKDMNSLVYKILEGKlPPMPKQYSPELGELIK 235
                         250
                  ....*....|....*....
gi 124804138 2056 KLLELNVEKRISANEALEH 2074
Cdd:cd08223   236 AMLHQDPEKRPSVKRILRQ 254
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
1820-2027 2.65e-23

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: 102.12  E-value: 2.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1820 LYELHEQLGQGKFSTVYRGINKQTNSE---FAIKVIdKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIInTKETLYIS 1896
Cdd:cd05056     7 DITLGRCIGEGQFGDVYQGVYMSPENEkiaVAVKTC-KNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVI-TENPVWIV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1897 MELVKGGELYDFLLAE-TRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSrdaQIKLTDFGLSTLCAPNE 1975
Cdd:cd05056    85 MELAPLGELRSYLQVNkYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPD---CVKLGDFGLSRYMEDES 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 124804138 1976 LLKEPCGTL--AYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFPINKNTE 2027
Cdd:cd05056   162 YYKASKGKLpiKWMAPESINFRRFTSASDVWMFGVCMWEILMlGVKPFQGVKNND 216
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
1827-2074 2.73e-23

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: 103.71  E-value: 2.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVI---DKRSVsiyeKELLRsEISILRLLRHPNVIYLKEIINTK------------- 1890
Cdd:cd07854    13 LGCGSNGLVFSAVDSDCDKRVAVKKIvltDPQSV----KHALR-EIKIIRRLDHDNIVKVYEVLGPSgsdltedvgslte 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1891 -ETLYISMELVKGgelyDF--LLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdkSRDAQIKLTDFGL 1967
Cdd:cd07854    88 lNSVYIVQEYMET----DLanVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFIN--TEDLVLKIGDFGL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1968 STLCAPNE----LLKEPCGTLAYVAPE-VITLQGYNHKVDAWSIGIILYLLLSGKLPFP-----------------INKN 2025
Cdd:cd07854   162 ARIVDPHYshkgYLSEGLVTKWYRSPRlLLSPNNYTKAIDMWAAGCIFAEMLTGKPLFAgaheleqmqlilesvpvVREE 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 124804138 2026 TEMNIQKNYVLSFKDYIWK----------SISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd07854   242 DRNELLNVIPSFVRNDGGEprrplrdllpGVNPEALDFLEQILTFNPMDRLTAEEALMH 300
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
1822-2034 3.04e-23

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: 101.66  E-value: 3.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1822 ELHEQLGQGKFSTVYRGINKQTnSEFAIKVIDKRSVSIyekELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVK 1901
Cdd:cd05072    10 KLVKKLGAGQFGEVWMGYYNNS-TKVAVKTLKPGTMSV---QAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEYMA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1902 GGELYDFLLAETRlSEIHANKII---TQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLCAPNELLK 1978
Cdd:cd05072    86 KGSLLDFLKSDEG-GKVLLPKLIdfsAQIAEGMAYIERKNYIHRDLRAANVLVSES---LMCKIADFGLARVIEDNEYTA 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124804138 1979 EPCGT--LAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFPINKNTEM--NIQKNY 2034
Cdd:cd05072   162 REGAKfpIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPYPGMSNSDVmsALQRGY 222
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
1827-2074 3.40e-23

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: 103.42  E-value: 3.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRS-VSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGEL 1905
Cdd:cd05610    12 ISRGAFGKVYLGRKKNNSKLYAVKVVKKADmINKNMVHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1906 YDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLC-------------- 1971
Cdd:cd05610    92 KSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLI---SNEGHIKLTDFGLSKVTlnrelnmmdilttp 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1972 -----------APNELL--------------KEP---------------CGTLAYVAPEVITLQGYNHKVDAWSIGIILY 2011
Cdd:cd05610   169 smakpkndysrTPGQVLslisslgfntptpyRTPksvrrgaarvegeriLGTPDYLAPELLLGKPHGPAVDWWALGVCLF 248
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124804138 2012 LLLSGKLPFpiNKNTEMNIQKNyVLSfKDYIW----KSISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd05610   249 EFLTGIPPF--NDETPQQVFQN-ILN-RDIPWpegeEELSVNAQNAIEILLTMDPTKRAGLKELKQH 311
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
1821-2077 3.67e-23

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: 102.19  E-value: 3.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSvsiyEKE-----LLRsEISILRLLRHPNVIYLKEII-------- 1887
Cdd:cd07864     9 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDN----EKEgfpitAIR-EIKILRQLNHRSVVNLKEIVtdkqdald 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1888 --NTKETLYISMELVKggelYDFL-LAETRL---SEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIK 1961
Cdd:cd07864    84 fkKDKGAFYLVFEYMD----HDLMgLLESGLvhfSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNK---GQIK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1962 LTDFGLSTLCAPNE--LLKEPCGTLAYVAPEVIT-LQGYNHKVDAWSIGIILYLLLSGKLPFPINK-------------- 2024
Cdd:cd07864   157 LADFGLARLYNSEEsrPYTNKVITLWYRPPELLLgEERYGPAIDVWSCGCILGELFTKKPIFQANQelaqlelisrlcgs 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124804138 2025 ---------------NTeMNIQKNYVLSFKDYiWKSISSSAKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd07864   237 pcpavwpdviklpyfNT-MKPKKQYRRRLREE-FSFIPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
1827-2020 3.84e-23

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: 102.96  E-value: 3.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIdKRSVSIYEK--ELLRSEISILRLL-RHPNVIYLKEIINTKETLYISMELVKGG 1903
Cdd:cd05591     3 LGKGSFGKVMLAERKGTDEVYAIKVL-KKDVILQDDdvDCTMTEKRILALAaKHPFLTALHSCFQTKDRLFFVMEYVNGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 ELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLstlC----APNELLKE 1979
Cdd:cd05591    82 DLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILL---DAEGHCKLADFGM---CkegiLNGKTTTT 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 124804138 1980 PCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd05591   156 FCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPF 196
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
1827-2046 3.87e-23

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: 102.88  E-value: 3.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEK-ELLRSEISILRLL-RHPNVIYLKEIINTKETLYISMELVKGGE 1904
Cdd:cd05588     3 IGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDDEDiDWVQTEKHVFETAsNHPFLVGLHSCFQTESRLFFVIEFVNGGD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLstlCA----PNELLKEP 1980
Cdd:cd05588    83 LMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLL---DSEGHIKLTDYGM---CKeglrPGDTTSTF 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124804138 1981 CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEmNIQKNYvlsfKDYIWKSI 2046
Cdd:cd05588   157 CGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFDIVGSSD-NPDQNT----EDYLFQVI 217
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
1821-2070 4.10e-23

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: 102.76  E-value: 4.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRS-VSIYEKELLRSEISILRLL---RHPNVIYLKEIINTKETLYIS 1896
Cdd:cd05589     1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDiIARDEVESLMCEKRIFETVnsaRHPFLVNLFACFQTPEHVCFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1897 MELVKGGEL----YDFLLAETRlSEIHANKIITQLiktvAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLstlCa 1972
Cdd:cd05589    81 MEYAAGGDLmmhiHEDVFSEPR-AVFYAACVVLGL----QFLHEHKIVYRDLKLDNLLL---DTEGYVKIADFGL---C- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1973 pnellKEP----------CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEmniqknyvlsfkdyI 2042
Cdd:cd05589   149 -----KEGmgfgdrtstfCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEE--------------V 209
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 124804138 2043 WKSI-----------SSSAKDLISKLLELNVEKRISANE 2070
Cdd:cd05589   210 FDSIvndevryprflSTEAISIMRRLLRKNPERRLGASE 248
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
1827-2020 4.51e-23

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: 102.57  E-value: 4.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVsIYEKELLRSEISILRLLRHPNVIYL---KEIINTKETLyISMELVKGG 1903
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSF-MRPLDVQMREFEVLKKLNHKNIVKLfaiEEELTTRHKV-LVMELCPCG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 ELYDFLLAETR---LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENIL-LTDKSRDAQIKLTDFGLSTLCAPNELLKE 1979
Cdd:cd13988    79 SLYTVLEEPSNaygLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrVIGEDGQSVYKLTDFGAARELEDDEQFVS 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 124804138 1980 PCGTLAYVAPEVI--------TLQGYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd13988   159 LYGTEEYLHPDMYeravlrkdHQKKYGATVDLWSIGVTFYHAATGSLPF 207
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
1825-2034 5.42e-23

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: 100.43  E-value: 5.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGI-NKQTnsEFAIKVIDKRSVSIyeKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELVKGG 1903
Cdd:cd05034     1 KKLGAGQFGEVWMGVwNGTT--KVAVKTLKPGTMSP--EAFLQ-EAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 ELYDFLLAETRlSEIHANKII---TQLIKTVAYLHRCGIIHRDIKPENILLTDKSrdaQIKLTDFGLSTLCA-----PNE 1975
Cdd:cd05034    76 SLLDYLRTGEG-RALRLPQLIdmaAQIASGMAYLESRNYIHRDLAARNILVGENN---VCKVADFGLARLIEddeytARE 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124804138 1976 LLKEPcgtLAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFPINKNTEM--NIQKNY 2034
Cdd:cd05034   152 GAKFP---IKWTAPEAALYGRFTIKSDVWSFGILLYEIVTyGRVPYPGMTNREVleQVERGY 210
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
1816-2070 5.90e-23

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: 102.06  E-value: 5.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1816 TLYNLYELHEQLGQGKFSTVYRGINKQTNSEFAIKV-------IDKRSVSiYEKELLRsEISILRLLRHPNVIYLKEIIN 1888
Cdd:cd14041     3 TLNDRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIhqlnknwRDEKKEN-YHKHACR-EYRIHKELDHPRIVKLYDYFS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1889 TKETLYIS-MELVKGGELyDFLLAETRL-SEIHANKIITQLIKTVAYLH--RCGIIHRDIKPENILLTDKSRDAQIKLTD 1964
Cdd:cd14041    81 LDTDSFCTvLEYCEGNDL-DFYLKQHKLmSEKEARSIIMQIVNALKYLNeiKPPIIHYDLKPGNILLVNGTACGEIKITD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1965 FGLSTLCAPN--------ELLKEPCGTLAYVAPEVITL----QGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQK 2032
Cdd:cd14041   160 FGLSKIMDDDsynsvdgmELTSQGAGTYWYLPPECFVVgkepPKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQE 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 124804138 2033 NYVLSFKDYIWKS---ISSSAKDLISKLLELNVEKRISANE 2070
Cdd:cd14041   240 NTILKATEVQFPPkpvVTPEAKAFIRRCLAYRKEDRIDVQQ 280
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
1825-2037 6.77e-23

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: 100.21  E-value: 6.77e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGE 1904
Cdd:cd05041     1 EKIGRGNFGDVYRGVLKPDNTEVAVKTCRETLPPDLKRKFLQ-EARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLlaETRLSEIHANKIITQLIKTVA---YLHRCGIIHRDIKPENILLTDKSrdaQIKLTDFGLSTLCAPNEL----- 1976
Cdd:cd05041    80 LLTFL--RKKGARLTVKQLLQMCLDAAAgmeYLESKNCIHRDLAARNCLVGENN---VLKISDFGMSREEEDGEYtvsdg 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124804138 1977 LKE-PcgtLAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFP--INKNTEMNIQKNYVLS 2037
Cdd:cd05041   155 LKQiP---IKWTAPEALNYGRYTSESDVWSFGILLWEIFSlGATPYPgmSNQQTREQIESGYRMP 216
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
1820-2042 8.19e-23

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: 100.90  E-value: 8.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1820 LYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSiYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd06640     5 LFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAE-DEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETrLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLCAPNELLKE 1979
Cdd:cd06640    84 LGGGSALDLLRAGP-FDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQ---GDVKLADFGVAGQLTDTQIKRN 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124804138 1980 P-CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLP----------FPINKNTEMNIQKNYVLSFKDYI 2042
Cdd:cd06640   160 TfVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPnsdmhpmrvlFLIPKNNPPTLVGDFSKPFKEFI 233
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
1821-2074 8.85e-23

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: 100.59  E-value: 8.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVI----DKRSVSiyeKELLRsEISILRLLRHPNVIYLKEIINTKETLYIS 1896
Cdd:cd07839     2 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVrlddDDEGVP---SSALR-EICLLKELKHKNIVRLYDVLHSDKKLTLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1897 ME-----LVKggeLYDFLLAETRLSEIHAnkIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGLS--- 1968
Cdd:cd07839    78 FEycdqdLKK---YFDSCNGDIDPEIVKS--FMFQLLKGLAFCHSHNVLHRDLKPQNLLIN---KNGELKLADFGLAraf 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1969 ---TLCAPNELLkepcgTLAYVAPEVIT-LQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYVL-------- 2036
Cdd:cd07839   150 gipVRCYSAEVV-----TLWYRPPDVLFgAKLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDDQLKRIFRLlgtptees 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 124804138 2037 --------SFKDY-------IWKSI----SSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd07839   225 wpgvsklpDYKPYpmypattSLVNVvpklNSTGRDLLQNLLVCNPVQRISAEEALQH 281
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
1868-2077 9.48e-23

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: 102.41  E-value: 9.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1868 EISILRLLRHPNVIYLKEIINTKETL------YISMELVKGG--ELYDFLLAETRLSeihanKIITQLIKTVAYLHRCGI 1939
Cdd:cd07876    70 ELVLLKCVNHKNIISLLNVFTPQKSLeefqdvYLVMELMDANlcQVIHMELDHERMS-----YLLYQMLCGIKHLHSAGI 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1940 IHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLP 2019
Cdd:cd07876   145 IHRDLKPSNIVVKS---DCTLKILDFGLARTACTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVI 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 2020 F-------PINKNTE-------------MNIQKNYVLS------------FKDYIWKSIS-------SSAKDLISKLLEL 2060
Cdd:cd07876   222 FqgtdhidQWNKVIEqlgtpsaefmnrlQPTVRNYVENrpqypgisfeelFPDWIFPSESerdklktSQARDLLSKMLVI 301
                         250
                  ....*....|....*..
gi 124804138 2061 NVEKRISANEALEHIWV 2077
Cdd:cd07876   302 DPDKRISVDEALRHPYI 318
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
1827-2079 1.00e-22

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: 100.48  E-value: 1.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLR-SEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGEL 1905
Cdd:cd05630     8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMAlNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGGDL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1906 --YDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPNELLKEPCGT 1983
Cdd:cd05630    88 kfHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDD---HGHIRISDLGLAVHVPEGQTIKGRVGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1984 LAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNtemNIQKNYVLSF-----KDYIWKsISSSAKDLISKLL 2058
Cdd:cd05630   165 VGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKK---KIKREEVERLvkevpEEYSEK-FSPQARSLCSMLL 240
                         250       260
                  ....*....|....*....|....*.
gi 124804138 2059 ELNVEKRI-----SANEALEHIWVKN 2079
Cdd:cd05630   241 CKDPAERLgcrggGAREVKEHPLFKK 266
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
1825-2034 1.21e-22

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: 100.34  E-value: 1.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLrSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGE 1904
Cdd:cd06619     7 EILGHGNGGTVYKAYHLLTRRILAVKVIPLDITVELQKQIM-SELEILYKCDSPYIIGFYGAFFVENRISICTEFMDGGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFllaeTRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLCApNELLKEPCGTL 1984
Cdd:cd06619    86 LDVY----RKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTR---GQVKLCDFGVSTQLV-NSIAKTYVGTN 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 124804138 1985 AYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPinkntemNIQKNY 2034
Cdd:cd06619   158 AYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYP-------QIQKNQ 200
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
1827-2020 1.35e-22

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: 99.73  E-value: 1.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKqtNSEFAIKVI--DKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGE 1904
Cdd:cd14146     2 IGVGGFGKVYRATWK--GQEVAVKAArqDPDEDIKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAETRLSEIHANKII---------TQLIKTVAYLHR---CGIIHRDIKPENILLTDKSRDAQI-----KLTDFGL 1967
Cdd:cd14146    80 LNRALAAANAAPGPRRARRIpphilvnwaVQIARGMLYLHEeavVPILHRDLKSSNILLLEKIEHDDIcnktlKITDFGL 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 124804138 1968 STLCAPNELLkEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd14146   160 AREWHRTTKM-SAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPY 211
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1821-2030 1.40e-22

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: 99.72  E-value: 1.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKvidkrSVSIYE------KELLRSEISILRLLRHPNVI-YLKEIINTKEtL 1893
Cdd:cd08228     4 FQIEKKIGRGQFSEVYRATCLLDRKPVALK-----KVQIFEmmdakaRQDCVKEIDLLKQLNHPNVIkYLDSFIEDNE-L 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1894 YISMELVKGGELYDFLL---AETRL-SEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksRDAQIKLTDFGL-- 1967
Cdd:cd08228    78 NIVLELADAGDLSQMIKyfkKQKRLiPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFIT---ATGVVKLGDLGLgr 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124804138 1968 ---STLCAPNELLkepcGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKnteMNI 2030
Cdd:cd08228   155 ffsSKTTAAHSLV----GTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDK---MNL 213
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
1821-2066 2.15e-22

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: 101.65  E-value: 2.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEK-ELLRSEISIL-RLLRHPNVIYLKEIINTKETLYISME 1898
Cdd:cd05618    22 FDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDiDWVQTEKHVFeQASNHPFLVGLHSCFQTESRLFFVIE 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTL-CAPNELL 1977
Cdd:cd05618   102 YVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLL---DSEGHIKLTDYGMCKEgLRPGDTT 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPI---NKNTEMNIQK---NYVLSFKDYIWKSISSSAK 2051
Cdd:cd05618   179 STFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIvgsSDNPDQNTEDylfQVILEKQIRIPRSLSVKAA 258
                         250
                  ....*....|....*
gi 124804138 2052 DLISKLLELNVEKRI 2066
Cdd:cd05618   259 SVLKSFLNKDPKERL 273
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
1827-2056 2.21e-22

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: 100.84  E-value: 2.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIdKRSVSIYEK--ELLRSEISILRLL-RHPNVIYLKEIINTKETLYISMELVKGG 1903
Cdd:cd05615    18 LGKGSFGKVMLAERKGSDELYAIKIL-KKDVVIQDDdvECTMVEKRVLALQdKPPFLTQLHSCFQTVDRLYFVMEYVNGG 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 ELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLstlCAPNEL----LKE 1979
Cdd:cd05615    97 DLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVML---DSEGHIKIADFGM---CKEHMVegvtTRT 170
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124804138 1980 PCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEM--NIQKNYVlSFKDYIWKSISSSAKDLISK 2056
Cdd:cd05615   171 FCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELfqSIMEHNV-SYPKSLSKEAVSICKGLMTK 248
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
1816-2070 2.22e-22

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: 100.13  E-value: 2.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1816 TLYNLYELHEQLGQGKFSTVYRGINKQTNSEFAIKV-------IDKRSVSiYEKELLRsEISILRLLRHPNVIYLKEIIN 1888
Cdd:cd14040     3 TLNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIhqlnkswRDEKKEN-YHKHACR-EYRIHKELDHPRIVKLYDYFS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1889 -TKETLYISMELVKGGELyDFLLAETRL-SEIHANKIITQLIKTVAYLH--RCGIIHRDIKPENILLTDKSRDAQIKLTD 1964
Cdd:cd14040    81 lDTDTFCTVLEYCEGNDL-DFYLKQHKLmSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGTACGEIKITD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1965 FGLSTLCAPN-------ELLKEPCGTLAYVAPEVITL----QGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKN 2033
Cdd:cd14040   160 FGLSKIMDDDsygvdgmDLTSQGAGTYWYLPPECFVVgkepPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQEN 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 124804138 2034 YVLSFKDY---IWKSISSSAKDLISKLLELNVEKRISANE 2070
Cdd:cd14040   240 TILKATEVqfpVKPVVSNEAKAFIRRCLAYRKEDRFDVHQ 279
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
1821-2066 2.49e-22

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: 101.25  E-value: 2.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEK-ELLRSEISIL-RLLRHPNVIYLKEIINTKETLYISME 1898
Cdd:cd05617    17 FDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDiDWVQTEKHVFeQASSNPFLVGLHSCFQTTSRLFLVIE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTL-CAPNELL 1977
Cdd:cd05617    97 YVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLL---DADGHIKLTDYGMCKEgLGPGDTT 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFP-INKNTEMNIQK---NYVLSFKDYIWKSISSSAKDL 2053
Cdd:cd05617   174 STFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDiITDNPDMNTEDylfQVILEKPIRIPRFLSVKASHV 253
                         250
                  ....*....|...
gi 124804138 2054 ISKLLELNVEKRI 2066
Cdd:cd05617   254 LKGFLNKDPKERL 266
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
1823-2020 3.53e-22

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: 98.58  E-value: 3.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1823 LHEQLGQGKFSTVYRGINKQtnSEFAIKVI--DKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd14145    10 LEEIIGIGGFGKVYRAIWIG--DEVAVKAArhDPDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIItQLIKTVAYLHRCGI---IHRDIKPENILLTDKSRDAQI-----KLTDFGLSTLCA 1972
Cdd:cd14145    88 RGGPLNRVLSGKRIPPDILVNWAV-QIARGMNYLHCEAIvpvIHRDLKSSNILILEKVENGDLsnkilKITDFGLAREWH 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 124804138 1973 PNELLkEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd14145   167 RTTKM-SAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPF 213
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
1826-2074 3.90e-22

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: 98.15  E-value: 3.90e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1826 QLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYL----KEIINTKETLYISMELVK 1901
Cdd:cd14033     8 EIGRGSFKTVYRGLDTETTVEVAWCELQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFydswKSTVRGHKCIILVTELMT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1902 GGELYDFLlaeTRLSEIHA---NKIITQLIKTVAYLH-RC-GIIHRDIKPENILLTDKSrdAQIKLTDFGLSTLCAPNeL 1976
Cdd:cd14033    88 SGTLKTYL---KRFREMKLkllQRWSRQILKGLHFLHsRCpPILHRDLKCDNIFITGPT--GSVKIGDLGLATLKRAS-F 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1977 LKEPCGTLAYVAPEVITlQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYVLSFKDYIWKSISSSAKDLISK 2056
Cdd:cd14033   162 AKSVIGTPEFMAPEMYE-EKYDEAVDVYAFGMCILEMATSEYPYSECQNAAQIYRKVTSGIKPDSFYKVKVPELKEIIEG 240
                         250
                  ....*....|....*...
gi 124804138 2057 LLELNVEKRISANEALEH 2074
Cdd:cd14033   241 CIRTDKDERFTIQDLLEH 258
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
1820-2077 4.05e-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: 98.10  E-value: 4.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1820 LYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIY----------EKELLRSEISILRllrhpNVIYLKEIINT 1889
Cdd:cd14102     1 VYQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWgtlngvmvplEIVLLKKVGSGFR-----GVIKLLDWYER 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1890 KETLYISME---LVKggELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdKSRDAQIKLTDFG 1966
Cdd:cd14102    76 PDGFLIVMErpePVK--DLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLV--DLRTGELKLIDFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1967 LSTLCApNELLKEPCGTLAYVAPEVITLQGYNHK-VDAWSIGIILYLLLSGKLPFPinkntemniQKNYVLSFKDYIWKS 2045
Cdd:cd14102   152 SGALLK-DTVYTDFDGTRVYSPPEWIRYHRYHGRsATVWSLGVLLYDMVCGDIPFE---------QDEEILRGRLYFRRR 221
                         250       260       270
                  ....*....|....*....|....*....|..
gi 124804138 2046 ISSSAKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14102   222 VSPECQQLIKWCLSLRPSDRPTLEQIFDHPWM 253
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
1819-2079 4.43e-22

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 104.82  E-value: 4.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVI-YLKEIIN-TKETLYIS 1896
Cdd:PTZ00266   13 NEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKEREKSQLVIEVNVMRELKHKNIVrYIDRFLNkANQKLYIL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1897 MELVKGGELYDFLLAETRL---SEIHANKIIT-QLIKTVAYLHRCG-------IIHRDIKPENILLTDKSR-----DAQ- 1959
Cdd:PTZ00266   93 MEFCDAGDLSRNIQKCYKMfgkIEEHAIVDITrQLLHALAYCHNLKdgpngerVLHRDLKPQNIFLSTGIRhigkiTAQa 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1960 --------IKLTDFGLSTLCAPNELLKEPCGTLAYVAPEVI--TLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMN 2029
Cdd:PTZ00266  173 nnlngrpiAKIGDFGLSKNIGIESMAHSCVGTPYYWSPELLlhETKSYDDKSDMWALGCIIYELCSGKTPFHKANNFSQL 252
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 124804138 2030 IQKnyVLSFKDYIWKSISSSAKDLISKLLELNVEKRISANEALEHIWVKN 2079
Cdd:PTZ00266  253 ISE--LKRGPDLPIKGKSKELNILIKNLLNLSAKERPSALQCLGYQIIKN 300
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
1827-2071 5.01e-22

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: 100.86  E-value: 5.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSV-SIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGEL 1905
Cdd:cd05626     9 LGIGAFGEVCLACKVDTHALYAMKTLRKKDVlNRNQVAHVKAERDILAEADNEWVVKLYYSFQDKDNLYFVMDYIPGGDM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1906 YDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLST---------------- 1969
Cdd:cd05626    89 MSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILI---DLDGHIKLTDFGLCTgfrwthnskyyqkgsh 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1970 ----------------LCAPNELLK----------EPC------GTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGK 2017
Cdd:cd05626   166 irqdsmepsdlwddvsNCRCGDRLKtleqratkqhQRClahslvGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEMLVGQ 245
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 124804138 2018 LPFPINKNTEMNIQK-NYVLSFKDYIWKSISSSAKDLISKLLeLNVEKRISANEA 2071
Cdd:cd05626   246 PPFLAPTPTETQLKViNWENTLHIPPQVKLSPEAVDLITKLC-CSAEERLGRNGA 299
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
1905-2075 5.36e-22

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: 98.63  E-value: 5.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRdaQIKLTDFGLST-LCAPNELLKEPCGT 1983
Cdd:cd13974   119 LQHYVIREKRLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRTR--KITITNFCLGKhLVSEDDLLKDQRGS 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1984 LAYVAPEVITLQGYNHK-VDAWSIGIILYLLLSGKLPFPINKNTEM--NI-QKNYVLSFKDyiwkSISSSAKDLISKLLE 2059
Cdd:cd13974   197 PAYISPDVLSGKPYLGKpSDMWALGVVLFTMLYGQFPFYDSIPQELfrKIkAAEYTIPEDG----RVSENTVCLIRKLLV 272
                         170
                  ....*....|....*.
gi 124804138 2060 LNVEKRISANEALEHI 2075
Cdd:cd13974   273 LNPQKRLTASEVLDSL 288
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
1827-2076 7.23e-22

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: 97.11  E-value: 7.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDkrsvsiyEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELvKGGELY 1906
Cdd:cd13976     1 LEPAEGSSLYRCVDIHTGEELVCKVVP-------VPECHAVLRAYFRLPSHPNISGVHEVIAGETKAYVFFER-DHGDLH 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1907 DFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRdAQIKLTDF-GLSTLCAPNELLKEPCGTLA 1985
Cdd:cd13976    73 SYVRSRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEER-TKLRLESLeDAVILEGEDDSLSDKHGCPA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1986 YVAPEVITLQG-YNHK-VDAWSIGIILYLLLSGKLPFPINKNTEM--NIQKNYVLsfkdyIWKSISSSAKDLISKLLELN 2061
Cdd:cd13976   152 YVSPEILNSGAtYSGKaADVWSLGVILYTMLVGRYPFHDSEPASLfaKIRRGQFA-----IPETLSPRARCLIRSLLRRE 226
                         250
                  ....*....|....*
gi 124804138 2062 VEKRISANEALEHIW 2076
Cdd:cd13976   227 PSERLTAEDILLHPW 241
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
1827-2074 9.04e-22

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: 99.92  E-value: 9.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKrsVSIYEKELL---RSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGG 1903
Cdd:cd05629     9 IGKGAFGEVRLVQKKDTGKIYAMKTLLK--SEMFKKDQLahvKAERDVLAESDSPWVVSLYYSFQDAQYLYLIMEFLPGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 ELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLST-------------- 1969
Cdd:cd05629    87 DLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILI---DRGGHIKLSDFGLSTgfhkqhdsayyqkl 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1970 ----------------------LCAPNE------------LLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLS 2015
Cdd:cd05629   164 lqgksnknridnrnsvavdsinLTMSSKdqiatwkknrrlMAYSTVGTPDYIAPEIFLQQGYGQECDWWSLGAIMFECLI 243
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124804138 2016 GKLPFPINKNTE-----MNIQKNyvLSFKDYIwkSISSSAKDLISKLLElNVEKRI---SANEALEH 2074
Cdd:cd05629   244 GWPPFCSENSHEtyrkiINWRET--LYFPDDI--HLSVEAEDLIRRLIT-NAENRLgrgGAHEIKSH 305
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
1825-2036 9.12e-22

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: 96.92  E-value: 9.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSEFAIKVIdKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGE 1904
Cdd:cd05084     2 ERIGRGNFGEVFSGRLRADNTPVAVKSC-RETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAE-TRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSrdaQIKLTDFGLS------TLCAPNELL 1977
Cdd:cd05084    81 FLTFLRTEgPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKN---VLKISDFGMSreeedgVYAATGGMK 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124804138 1978 KEPcgtLAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFPI--NKNTEMNIQKNYVL 2036
Cdd:cd05084   158 QIP---VKWTAPEALNYGRYSSESDVWSFGILLWETFSlGAVPYANlsNQQTREAVEQGVRL 216
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
1827-2070 1.57e-21

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: 97.28  E-value: 1.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKE---LLRSEIsiLRLLRHPNVIYLKEIINTKETLYISMELVKGG 1903
Cdd:cd05607    10 LGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEkmaLLEKEI--LEKVNSPFIVSLAYAFETKTHLCLVMSLMNGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 ELyDFLLAETRLSEIHANKII---TQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPNELLKEP 1980
Cdd:cd05607    88 DL-KYHIYNVGERGIEMERVIfysAQITCGILHLHSLKIVYRDMKPENVLLDD---NGNCRLSDLGLAVEVKEGKPITQR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpinKNTEMNIQKNYVL--SFKDYI---WKSISSSAKDLIS 2055
Cdd:cd05607   164 AGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPF---RDHKEKVSKEELKrrTLEDEVkfeHQNFTEEAKDICR 240
                         250
                  ....*....|....*
gi 124804138 2056 KLLELNVEKRISANE 2070
Cdd:cd05607   241 LFLAKKPENRLGSRT 255
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
1825-2020 1.62e-21

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: 96.26  E-value: 1.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNS---EFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVIYLKEIINTkETLYISMELVK 1901
Cdd:cd05060     1 KELGHGNFGSVRKGVYLMKSGkevEVAVKTLKQEHEKAGKKEFLR-EASVMAQLDHPCIVRLIGVCKG-EPLMLVMELAP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1902 GGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSrdaQIKLTDFGLS-TLCAPNELLKEP 1980
Cdd:cd05060    79 LGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRH---QAKISDFGMSrALGAGSDYYRAT 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 124804138 1981 CG---TLAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPF 2020
Cdd:cd05060   156 TAgrwPLKWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPY 199
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
1822-2021 1.63e-21

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: 96.27  E-value: 1.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1822 ELHEQLGQGKFSTVYRGINKqtNSEFAIKVIdKRSVSIYEKELLrsEISILRLLRHPNVIYLKEIINTKETLYISMELVK 1901
Cdd:cd05039     9 KLGELIGKGEFGDVMLGDYR--GQKVAVKCL-KDDSTAAQAFLA--EASVMTTLRHPNLVQLLGVVLEGNGLYIVTEYMA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1902 GGELYDFLLAETRLSEIHANKII--TQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLStlcapnellKE 1979
Cdd:cd05039    84 KGSLVDYLRSRGRAVITRKDQLGfaLDVCEGMEYLESKKFVHRDLAARNVLVSE---DNVAKVSDFGLA---------KE 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 PCGTLA-------YVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFP 2021
Cdd:cd05039   152 ASSNQDggklpikWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPYP 201
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
1826-2084 1.75e-21

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: 97.81  E-value: 1.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1826 QLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEK-ELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGE 1904
Cdd:cd06635    32 EIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKwQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEYCLGSA 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLCAPNELLkepCGTL 1984
Cdd:cd06635   112 SDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEP---GQVKLADFGSASIASPANSF---VGTP 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1985 AYVAPEVITLQG---YNHKVDAWSIGIILYLLLSGKLP-FPINKNTEM-NIQKNYVLSFKDYIWksiSSSAKDLISKLLE 2059
Cdd:cd06635   186 YWMAPEVILAMDegqYDGKVDVWSLGITCIELAERKPPlFNMNAMSALyHIAQNESPTLQSNEW---SDYFRNFVDSCLQ 262
                         250       260
                  ....*....|....*....|....*..
gi 124804138 2060 LNVEKRISANEALEHIWV--KNPTAVI 2084
Cdd:cd06635   263 KIPQDRPTSEELLKHMFVlrERPETVL 289
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
1825-2075 3.06e-21

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: 95.64  E-value: 3.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSEFAIKVIDkrsvsiYEKELLRSEISILRLLRHPNVI----------------YLKEIIN 1888
Cdd:cd14047    12 ELIGSGGFGQVFKAKHRIDGKTYAIKRVK------LNNEKAEREVKALAKLDHPNIVryngcwdgfdydpetsSSNSSRS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1889 TKETLYISMELVKGGELYDFLLAETRLSEIH--ANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFG 1966
Cdd:cd14047    86 KTKCLFIQMEFCEKGTLESWIEKRNGEKLDKvlALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVD---TGKVKIGDFG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1967 LST-LCAPNELLKEPcGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSgKLPFPINKNTEMNIQKNYVLSFkdyIWKS 2045
Cdd:cd14047   163 LVTsLKNDGKRTKSK-GTLSYMSPEQISSQDYGKEVDIYALGLILFELLH-VCDSAFEKSKFWTDLRNGILPD---IFDK 237
                         250       260       270
                  ....*....|....*....|....*....|
gi 124804138 2046 ISSSAKDLISKLLELNVEKRISANEALEHI 2075
Cdd:cd14047   238 RYKIEKTIIKKMLSKKPEDRPNASEILRTL 267
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
1791-2096 3.90e-21

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 97.36  E-value: 3.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1791 RNLYVNTLEERDEWVQalySSTKQNTLYNLYELHEQLGQGKFSTVYRGINKQTN-SEFAIKVIDKRSVsIYEKEL--LRS 1867
Cdd:PTZ00426    5 KNLQLHKKKDSDSTKE---PKRKNKMKYEDFNFIRTLGTGSFGRVILATYKNEDfPPVAIKRFEKSKI-IKQKQVdhVFS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1868 EISILRLLRHPNVIYLKEIINTKETLYISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPE 1947
Cdd:PTZ00426   81 ERKILNYINHPFCVNLYGSFKDESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1948 NILLtdkSRDAQIKLTDFGLSTLCAPNELLKepCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINkntE 2027
Cdd:PTZ00426  161 NLLL---DKDGFIKMTDFGFAKVVDTRTYTL--CGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYAN---E 232
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124804138 2028 MNIQKNYVLSFKDYIWKSISSSAKDLISKLLELNVEKRI-----SANEALEHIWVKNptavINENSFIYKNEEI 2096
Cdd:PTZ00426  233 PLLIYQKILEGIIYFPKFLDNNCKHLMKKLLSHDLTKRYgnlkkGAQNVKEHPWFGN----IDWVSLLHKNVEV 302
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
1819-2021 4.86e-21

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: 97.00  E-value: 4.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdKRSVSIYEKELLrsEISILRLL-RHP-----NVIYLKEIINTKET 1892
Cdd:cd14226    13 DRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKII-KNKKAFLNQAQI--EVRLLELMnKHDtenkyYIVRLKRHFMFRNH 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1893 LYISMELVKgGELYDfLLAETRLSEIHAN---KIITQLIKTVAYLHR--CGIIHRDIKPENILLTDKSRDAqIKLTDFGL 1967
Cdd:cd14226    90 LCLVFELLS-YNLYD-LLRNTNFRGVSLNltrKFAQQLCTALLFLSTpeLSIIHCDLKPENILLCNPKRSA-IKIIDFGS 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 124804138 1968 StlCAPNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFP 2021
Cdd:cd14226   167 S--CQLGQRIYQYIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLFS 218
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
1821-2074 5.28e-21

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: 95.80  E-value: 5.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdkrSVSIYEKELLRS---EISILRLLR---HPNVIYLKEIINTKET-L 1893
Cdd:cd07863     2 YEPVAEIGVGAYGTVYKARDPHSGHFVALKSV---RVQTNEDGLPLStvrEVALLKRLEafdHPNIVRLMDVCATSRTdR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1894 YISMELVKggELYDFLLaETRLSEIHA--------NKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDF 1965
Cdd:cd07863    79 ETKVTLVF--EHVDQDL-RTYLDKVPPpglpaetiKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSG---GQVKLADF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1966 GLSTLCAPNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLS--------------GKLPFPINKNTEMNIQ 2031
Cdd:cd07863   153 GLARIYSCQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRrkplfcgnseadqlGKIFDLIGLPPEDDWP 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 124804138 2032 KNYVLSFKDYIWKS----------ISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd07863   233 RDVTLPRGAFSPRGprpvqsvvpeIEESGAQLLLEMLTFNPHKRISAFRALQH 285
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
1821-2074 5.77e-21

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: 95.67  E-value: 5.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKvidKRSVSIYEKEL----LRsEISILRLLRHPnvIYLKEII-------NT 1889
Cdd:cd07837     3 YEKLEKIGEGTYGKVYKARDKNTGKLVALK---KTRLEMEEEGVpstaLR-EVSLLQMLSQS--IYIVRLLdvehveeNG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1890 KETLYISMELVKGgELYDFLLAETR-----LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtDKSRDAqIKLTD 1964
Cdd:cd07837    77 KPLLYLVFEYLDT-DLKKFIDSYGRgphnpLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLV-DKQKGL-LKIAD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1965 FGLS-TLCAPNELLKEPCGTLAYVAPEVitLQG---YNHKVDAWSIGIILYLLLSGKLPFPINKNTE--MNIQKNY---- 2034
Cdd:cd07837   154 LGLGrAFTIPIKSYTHEIVTLWYRAPEV--LLGsthYSTPVDMWSVGCIFAEMSRKQPLFPGDSELQqlLHIFRLLgtpn 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 124804138 2035 ------VLSFKDY----IWK---------SISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd07837   232 eevwpgVSKLRDWheypQWKpqdlsravpDLEPEGVDLLTKMLAYDPAKRISAKAALQH 290
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
1821-2116 5.93e-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: 97.06  E-value: 5.93e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDK-----RSVSIYEKEllrsEISILRLLRHPNVIYLKEIINTKETLYI 1895
Cdd:cd05596    28 FDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKfemikRSDSAFFWE----ERDIMAHANSEWIVQLHYAFQDDKYLYM 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1896 SMELVKGGELYDfLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtDKSrdAQIKLTDFGLSTLCAPNE 1975
Cdd:cd05596   104 VMDYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLL-DAS--GHLKLADFGTCMKMDKDG 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1976 LLK--EPCGTLAYVAPEVITLQG----YNHKVDAWSIGIILYLLLSGKLPFPINK--NTEMNI--QKNYvLSFKDYIwkS 2045
Cdd:cd05596   180 LVRsdTAVGTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPFYADSlvGTYGKImnHKNS-LQFPDDV--E 256
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124804138 2046 ISSSAKDLISKLLELNvEKRISANEALEhiwvknptavINENSFiYKNEEINILNLQDvsvstfNIPRYTP 2116
Cdd:cd05596   257 ISKDAKSLICAFLTDR-EVRLGRNGIEE----------IKAHPF-FKNDQWTWDNIRE------TVPPVVP 309
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
1827-2020 6.27e-21

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: 95.37  E-value: 6.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIdKRSVSIYEKELLRSEISILRLLRHPNVIYLKEI-----INTKETLYISMELVK 1901
Cdd:cd14039     1 LGTGGFGNVCLYQNQETGEKIAIKSC-RLELSVKNKDRWCHEIQIMKKLNHPNVVKACDVpeemnFLVNDVPLLAMEYCS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1902 GGELYDFLLAETR---LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCAPNELLK 1978
Cdd:cd14039    80 GGDLRKLLNKPENccgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKIVHKIIDLGYAKDLDQGSLCT 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 124804138 1979 EPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd14039   160 SFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPF 201
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
1790-2069 8.95e-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: 97.39  E-value: 8.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1790 KRNLYVNtleERDEWVQALYSSTKQNTLY-NLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVsiyekeLLRSE 1868
Cdd:cd05624    45 RRDKYVS---EFLEWAKPFTQLVKEMQLHrDDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEM------LKRAE 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1869 ISILRLLRhpNVIY---------LKEIINTKETLYISMELVKGGELYDFLLA-ETRLSEIHANKIITQLIKTVAYLHRCG 1938
Cdd:cd05624   116 TACFREER--NVLVngdcqwittLHYAFQDENYLYLVMDYYVGGDLLTLLSKfEDKLPEDMARFYIGEMVLAIHSIHQLH 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1939 IIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCAPNELLKE--PCGTLAYVAPEVIT-----LQGYNHKVDAWSIGIILY 2011
Cdd:cd05624   194 YVHRDIKPDNVLL---DMNGHIRLADFGSCLKMNDDGTVQSsvAVGTPDYISPEILQamedgMGKYGPECDWWSLGVCMY 270
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124804138 2012 LLLSGKLPFPINKNTE-----MNIQKNYvlSFKDYIwKSISSSAKDLISKLLeLNVEKRISAN 2069
Cdd:cd05624   271 EMLYGETPFYAESLVEtygkiMNHEERF--QFPSHV-TDVSEEAKDLIQRLI-CSRERRLGQN 329
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
1821-2076 1.02e-20

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: 95.72  E-value: 1.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdkRSVSIYeKELLRSEISILRLLRH--PNVIYLKEII----NTKET-- 1892
Cdd:cd14136    12 YHVVRKLGWGHFSTVWLCWDLQNKRFVALKVV--KSAQHY-TEAALDEIKLLKCVREadPKDPGREHVVqlldDFKHTgp 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1893 --LYISMELVKGGelyDFLLAETRLSEIHA------NKIITQLIKTVAYLHR-CGIIHRDIKPENILLTdkSRDAQIKLT 1963
Cdd:cd14136    89 ngTHVCMVFEVLG---PNLLKLIKRYNYRGiplplvKKIARQVLQGLDYLHTkCGIIHTDIKPENVLLC--ISKIEVKIA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1964 DFGLStlCAPNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF-PINKNT------------EM-- 2028
Cdd:cd14136   164 DLGNA--CWTDKHFTEDIQTRQYRSPEVILGAGYGTPADIWSTACMAFELATGDYLFdPHSGEDysrdedhlaliiELlg 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 2029 NIQKNYVLSFKDyiWKSISSSAKDL--ISKL------------------------------LELNVEKRISANEALEHIW 2076
Cdd:cd14136   242 RIPRSIILSGKY--SREFFNRKGELrhISKLkpwpledvlvekykwskeeakefasfllpmLEYDPEKRATAAQCLQHPW 319
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
1827-2010 1.46e-20

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: 93.32  E-value: 1.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKvIDKRSVSiyEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGELY 1906
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGKVMVMK-ELKRFDE--QRSFLK-EVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1907 DFLL-AETRLS---EIHANKIITqliKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLcAPNELLKEP-- 1980
Cdd:cd14065    77 ELLKsMDEQLPwsqRVSLAKDIA---SGMAYLHSKNIIHRDLNSKNCLVREANRGRNAVVADFGLARE-MPDEKTKKPdr 152
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 124804138 1981 ------CGTLAYVAPEVITLQGYNHKVDAWSIGIIL 2010
Cdd:cd14065   153 kkrltvVGSPYWMAPEMLRGESYDEKVDVFSFGIVL 188
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
1821-2074 1.69e-20

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: 93.14  E-value: 1.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYE-KELLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd14050     3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDrKRKLEEVERHEKLGEHPNCVRFIKAWEEKGILYIQTEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VkGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCAPNELLKE 1979
Cdd:cd14050    83 C-DTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFL---SKDGVCKLGDFGLVVELDKEDIHDA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 PCGTLAYVAPEVitLQG-YNHKVDAWSIGIILyLLLSGKLPFPINKNTEMNIQKNYVlsfKDYIWKSISSSAKDLISKLL 2058
Cdd:cd14050   159 QEGDPRYMAPEL--LQGsFTKAADIFSLGITI-LELACNLELPSGGDGWHQLRQGYL---PEEFTAGLSPELRSIIKLMM 232
                         250
                  ....*....|....*.
gi 124804138 2059 ELNVEKRISANEALEH 2074
Cdd:cd14050   233 DPDPERRPTAEDLLAL 248
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
1823-2020 1.83e-20

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: 93.56  E-value: 1.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1823 LHEQLGQGKFSTVYRGINKqtNSEFAIKVIDK---RSVSIyEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd14147     7 LEEVIGIGGFGKVYRGSWR--GELVAVKAARQdpdEDISV-TAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETRLSEIHANKIItQLIKTVAYLHRCGI---IHRDIKPENILLT-----DKSRDAQIKLTDFGLSTLC 1971
Cdd:cd14147    84 AAGGPLSRALAGRRVPPHVLVNWAV-QIARGMHYLHCEALvpvIHRDLKSNNILLLqpienDDMEHKTLKITDFGLAREW 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 124804138 1972 APNELLKEpCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd14147   163 HKTTQMSA-AGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPY 210
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
1827-2073 1.87e-20

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: 95.88  E-value: 1.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEK-ELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGEL 1905
Cdd:cd05625     9 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQvAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1906 YDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLST---------------- 1969
Cdd:cd05625    89 MSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILI---DRDGHIKLTDFGLCTgfrwthdskyyqsgdh 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1970 ----------------LCAPNELLK----------EPC------GTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGK 2017
Cdd:cd05625   166 lrqdsmdfsnewgdpeNCRCGDRLKplerraarqhQRClahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQ 245
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 124804138 2018 LPFPINKNTEMNIQK-NYVLSFKDYIWKSISSSAKDLISKLLElNVEKRISANEALE 2073
Cdd:cd05625   246 PPFLAQTPLETQMKViNWQTSLHIPPQAKLSPEASDLIIKLCR-GPEDRLGKNGADE 301
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
1827-2100 2.14e-20

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: 93.90  E-value: 2.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLR-SEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGEL 1905
Cdd:cd05631     8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMAlNEKRILEKVNSRFVVSLAYAYETKDALCLVLTIMNGGDL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1906 --YDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLCAPNELLKEPCGT 1983
Cdd:cd05631    88 kfHIYNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDR---GHIRISDLGLAVQIPEGETVRGRVGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1984 LAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKN--TEMNIQKNYVLSFKDYIWKsISSSAKDLISKLLELN 2061
Cdd:cd05631   165 VGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKErvKREEVDRRVKEDQEEYSEK-FSEDAKSICRMLLTKN 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 124804138 2062 VEKRI-----SANEALEHIWVKNptavINensfiYKNEEINILN 2100
Cdd:cd05631   244 PKERLgcrgnGAAGVKQHPIFKN----IN-----FKRLEANMLE 278
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
1819-2021 3.11e-20

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: 93.52  E-value: 3.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISME 1898
Cdd:cd07848     1 NKFEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYdflLAETRLSEIHANKI---ITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCAP-- 1973
Cdd:cd07848    81 YVEKNMLE---LLEEMPNGVPPEKVrsyIYQLIKAIHWCHKNDIVHRDIKPENLLI---SHNDVLKLCDFGFARNLSEgs 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 124804138 1974 NELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFP 2021
Cdd:cd07848   155 NANYTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFP 202
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
1827-2020 3.48e-20

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting 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. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K 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: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 92.21  E-value: 3.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGinKQTNSEFAIKviDKRSVSIYEK---ELLRSEISILRLLRHPNVI-YLKEIINTKETLYISMELVKG 1902
Cdd:cd14064     1 IGSGSFGKVYKG--RCRNKIVAIK--RYRANTYCSKsdvDMFCREVSILCRLNHPCVIqFVGACLDDPSQFAIVTQYVSG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1903 GELYDFLLAETRLSEIHANKIIT-QLIKTVAYLHRCG--IIHRDIKPENILLTDksrDAQIKLTDFGLST-LCAPNE--L 1976
Cdd:cd14064    77 GSLFSLLHEQKRVIDLQSKLIIAvDVAKGMEYLHNLTqpIIHRDLNSHNILLYE---DGHAVVADFGESRfLQSLDEdnM 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 124804138 1977 LKEPcGTLAYVAPEVITLQG-YNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd14064   154 TKQP-GNLRWMAPEVFTQCTrYSIKADVFSYALCLWELLTGEIPF 197
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
1822-2028 3.98e-20

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: 92.40  E-value: 3.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1822 ELHEQLGQGKFSTVYRGI-NKQTnsEFAIKVIDKRSVSIyekELLRSEISILRLLRHPNVIYLKEIInTKETLYISMELV 1900
Cdd:cd05073    14 KLEKKLGAGQFGEVWMATyNKHT--KVAVKTMKPGSMSV---EAFLAEANVMKTLQHDKLVKLHAVV-TKEPIYIITEFM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRlSEIHANKII---TQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCAPNELL 1977
Cdd:cd05073    88 AKGSLLDFLKSDEG-SKQPLPKLIdfsAQIAEGMAFIEQRNYIHRDLRAANILV---SASLVCKIADFGLARVIEDNEYT 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 124804138 1978 KEPCGT--LAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFPINKNTEM 2028
Cdd:cd05073   164 AREGAKfpIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIPYPGMSNPEV 217
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
1829-2074 4.40e-20

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: 91.99  E-value: 4.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1829 QGKFSTVYRGINKQTNSEFAIKVIDKrsvsiyeKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGELYDF 1908
Cdd:cd13995    14 RGAFGKVYLAQDTKTKKRMACKLIPV-------EQFKPSDVEIQACFRHENIAELYGALLWEETVHLFMEAGEGGSVLEK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1909 LLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksrDAQIKLTDFGLST-----LCAPNELLkepcGT 1983
Cdd:cd13995    87 LESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFM----STKAVLVDFGLSVqmtedVYVPKDLR----GT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1984 LAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFpINK------NTEMNIQKNYVLSFKDyIWKSISSSAKDLISKL 2057
Cdd:cd13995   159 EIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPW-VRRyprsayPSYLYIIHKQAPPLED-IAQDCSPAMRELLEAA 236
                         250
                  ....*....|....*..
gi 124804138 2058 LELNVEKRISANEALEH 2074
Cdd:cd13995   237 LERNPNHRSSAAELLKH 253
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
1836-2077 5.32e-20

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 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 TRB3 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: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 91.48  E-value: 5.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1836 YRGINKQTNSEFAIKVIDKRSvsiYEKELLRSEisilRLLRHPNVIYLKEIINTKETLYISMElVKGGELYDFLLAETRL 1915
Cdd:cd14024    10 YRAEHYQTEKEYTCKVLSLRS---YQECLAPYD----RLGPHEGVCSVLEVVIGQDRAYAFFS-RHYGDMHSHVRRRRRL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1916 SEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDaqiKLTDFGLSTLC---APNELLKEPCGTLAYVAPEVI 1992
Cdd:cd14024    82 SEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRT---KLVLVNLEDSCplnGDDDSLTDKHGCPAYVGPEIL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1993 -TLQGYNHK-VDAWSIGIILYLLLSGKLPFpinKNTEMNIQKNYVLSFKDYIWKSISSSAKDLISKLLELNVEKRISANE 2070
Cdd:cd14024   159 sSRRSYSGKaADVWSLGVCLYTMLLGRYPF---QDTEPAALFAKIRRGAFSLPAWLSPGARCLVSCMLRRSPAERLKASE 235

                  ....*..
gi 124804138 2071 ALEHIWV 2077
Cdd:cd14024   236 ILLHPWL 242
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
1826-2028 5.81e-20

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: 92.57  E-value: 5.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1826 QLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKE--IINTKETLYISMELVKGg 1903
Cdd:cd14049    13 RLGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIVGYHTawMEHVQLMLYIQMQLCEL- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 ELYDFLLAETRLSEI--------------HANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdkSRDAQIKLTDFGLSt 1969
Cdd:cd14049    92 SLWDWIVERNKRPCEeefksapytpvdvdVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLH--GSDIHVRIGDFGLA- 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124804138 1970 lC------APNELLKEPC---------GTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSgklPFpinkNTEM 2028
Cdd:cd14049   169 -CpdilqdGNDSTTMSRLnglthtsgvGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELFQ---PF----GTEM 234
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
1816-2077 6.54e-20

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: 94.00  E-value: 6.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1816 TLYNLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETL-- 1893
Cdd:cd07874    14 TVLKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKSLee 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1894 ----YISMELVKGG--ELYDFLLAETRLSeihanKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGL 1967
Cdd:cd07874    94 fqdvYLVMELMDANlcQVIQMELDHERMS-----YLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKS---DCTLKILDFGL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1968 STLCAPNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFP-------INKNTEM----------NI 2030
Cdd:cd07874   166 ARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPgrdyidqWNKVIEQlgtpcpefmkKL 245
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124804138 2031 Q---KNYV--------LSFKDYIWKSI-----------SSSAKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd07874   246 QptvRNYVenrpkyagLTFPKLFPDSLfpadsehnklkASQARDLLSKMLVIDPAKRISVDEALQHPYI 314
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
1835-2076 7.18e-20

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: 91.25  E-value: 7.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1835 VYRGINKQTNSEFAIKVIDkrsVSIYEKELlrseISILRLLRHPNVIYLKEIINTKETLYISMELvKGGELYDFLLAETR 1914
Cdd:cd14022     9 VFRAVHLHSGEELVCKVFD---IGCYQESL----APCFCLPAHSNINQITEIILGETKAYVFFER-SYGDMHSFVRTCKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1915 LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRdAQIKLTDF-GLSTLCAPNELLKEPCGTLAYVAPEVIT 1993
Cdd:cd14022    81 LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEER-TRVKLESLeDAYILRGHDDSLSDKHGCPAYVSPEILN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1994 LQG-YNHK-VDAWSIGIILYLLLSGKLPFpinKNTEMNIQKNYVLSFKDYIWKSISSSAKDLISKLLELNVEKRISANEA 2071
Cdd:cd14022   160 TSGsYSGKaADVWSLGVMLYTMLVGRYPF---HDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEI 236

                  ....*
gi 124804138 2072 LEHIW 2076
Cdd:cd14022   237 LDHPW 241
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
1826-2082 8.33e-20

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: 91.71  E-value: 8.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1826 QLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYL----KEIINTKETLYISMELVK 1901
Cdd:cd14031    17 ELGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFydswESVLKGKKCIVLVTELMT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1902 GGELYDFLLAETRLSEIHANKIITQLIKTVAYLH--RCGIIHRDIKPENILLTDKSrdAQIKLTDFGLSTLCApNELLKE 1979
Cdd:cd14031    97 SGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHtrTPPIIHRDLKCDNIFITGPT--GSVKIGDLGLATLMR-TSFAKS 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 PCGTLAYVAPEVITlQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEmNIQKNYVLSFKDYIWKSISS-SAKDLISKLL 2058
Cdd:cd14031   174 VIGTPEFMAPEMYE-EHYDESVDVYAFGMCMLEMATSEYPYSECQNAA-QIYRKVTSGIKPASFNKVTDpEVKEIIEGCI 251
                         250       260
                  ....*....|....*....|....
gi 124804138 2059 ELNVEKRISANEALEHIWVKNPTA 2082
Cdd:cd14031   252 RQNKSERLSIKDLLNHAFFAEDTG 275
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
1819-2078 9.11e-20

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: 93.20  E-value: 9.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELL----RSEISILRLLRHPNVIYLKEIINTKETLY 1894
Cdd:cd05633     5 NDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLalneRIMLSLVSTGDCPFIVCMTYAFHTPDKLC 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLStlCAPN 1974
Cdd:cd05633    85 FILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEH---GHVRISDLGLA--CDFS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1975 EllKEP---CGTLAYVAPEVITL-QGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYVLSFKDYIWKSISSSA 2050
Cdd:cd05633   160 K--KKPhasVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDSFSPEL 237
                         250       260       270
                  ....*....|....*....|....*....|...
gi 124804138 2051 KDLISKLLELNVEKRI-----SANEALEHIWVK 2078
Cdd:cd05633   238 KSLLEGLLQRDVSKRLgchgrGAQEVKEHSFFK 270
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
1827-2020 9.40e-20

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


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 91.40  E-value: 9.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQtNSEFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGELy 1906
Cdd:cd14664     1 IGRGGAGTVYKGVMPN-GTLVAVKRLKGEGTQGGDHGFQA-EIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSL- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1907 DFLLAETRLSEIH-----ANKIITQLIKTVAYLHR-CG--IIHRDIKPENILLtDKSRDAQIklTDFGLSTLCAPN--EL 1976
Cdd:cd14664    78 GELLHSRPESQPPldwetRQRIALGSARGLAYLHHdCSplIIHRDVKSNNILL-DEEFEAHV--ADFGLAKLMDDKdsHV 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 124804138 1977 LKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd14664   155 MSSVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPF 198
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
1823-2034 1.01e-19

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: 91.67  E-value: 1.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1823 LHEQLGQGKFSTVYRGINKQTnSEFAIKVIDKRSVSiyeKELLRSEISILRLLRHPNVIYLKEIInTKETLYISMELVKG 1902
Cdd:cd05071    13 LEVKLGQGCFGEVWMGTWNGT-TRVAIKTLKPGTMS---PEAFLQEAQVMKKLRHEKLVQLYAVV-SEEPIYIVTEYMSK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1903 GELYDFLLAET----RLSEIhaNKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPNELLK 1978
Cdd:cd05071    88 GSLLDFLKGEMgkylRLPQL--VDMAAQIASGMAYVERMNYVHRDLRAANILVGE---NLVCKVADFGLARLIEDNEYTA 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124804138 1979 EPCGT--LAYVAPEVITLQGYNHKVDAWSIGIILY-LLLSGKLPFP--INKNTEMNIQKNY 2034
Cdd:cd05071   163 RQGAKfpIKWTAPEAALYGRFTIKSDVWSFGILLTeLTTKGRVPYPgmVNREVLDQVERGY 223
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
1821-2074 1.06e-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: 92.29  E-value: 1.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGIN-KQTNSEFAIKVIdkRSVSIYEKELLRsEISILRLL--------RHpnVIYLKEIINTKE 1891
Cdd:cd14135     2 YRVYGYLGKGVFSNVVRARDlARGNQEVAIKII--RNNELMHKAGLK-ELEILKKLndadpddkKH--CIRLLRHFEHKN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1892 TLYISMELVKGgELYDFLLAETRLSEIHANKI---ITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRdaQIKLTDFGLS 1968
Cdd:cd14135    77 HLCLVFESLSM-NLREVLKKYGKNVGLNIKAVrsyAQQLFLALKHLKKCNILHADIKPDNILVNEKKN--TLKLCDFGSA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1969 TLCAPNELLKepcgTLA---YVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEM----------------- 2028
Cdd:cd14135   154 SDIGENEITP----YLVsrfYRAPEIILGLPYDYPIDMWSVGCTLYELYTGKILFPGKTNNHMlklmmdlkgkfpkkmlr 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 2029 ------------------------NIQKNYVLSFKDyIWKSISSSA-----------------KDLISKLLELNVEKRIS 2067
Cdd:cd14135   230 kgqfkdqhfdenlnfiyrevdkvtKKEVRRVMSDIK-PTKDLKTLLigkqrlpdedrkkllqlKDLLDKCLMLDPEKRIT 308

                  ....*..
gi 124804138 2068 ANEALEH 2074
Cdd:cd14135   309 PNEALQH 315
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
1819-2021 1.16e-19

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. 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. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 91.66  E-value: 1.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELHEqLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISME 1898
Cdd:cd06616     7 DLKDLGE-IGRGAFGTVNKMLHKPSGTIMAVKRIRSTVDEKEQKRLLMDLDVVMRSSDCPYIVKFYGALFREGDCWICME 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGG--ELYDF--LLAETRLSEIHANKIITQLIKTVAYLHR-CGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCAP 1973
Cdd:cd06616    86 LMDISldKFYKYvyEVLDSVIPEEILGKIAVATVKALNYLKEeLKIIHRDVKPSNILL---DRNGNIKLCDFGISGQLVD 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 124804138 1974 NELLKEPCGTLAYVAPEVIT----LQGYNHKVDAWSIGIILYLLLSGKLPFP 2021
Cdd:cd06616   163 SIAKTRDAGCRPYMAPERIDpsasRDGYDVRSDVWSLGITLYEVATGKFPYP 214
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
1821-2066 1.25e-19

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: 92.42  E-value: 1.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELL----RSEISILRLLRHPNVIYLKEIINTKETLYIS 1896
Cdd:cd14223     2 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLalneRIMLSLVSTGDCPFIVCMSYAFHTPDKLSFI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1897 MELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLStlCAPNEl 1976
Cdd:cd14223    82 LDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEF---GHVRISDLGLA--CDFSK- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1977 lKEP---CGTLAYVAPEVITLQ-GYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYVLSFKDYIWKSISSSAKD 2052
Cdd:cd14223   156 -KKPhasVGTHGYMAPEVLQKGvAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTMAVELPDSFSPELRS 234
                         250
                  ....*....|....
gi 124804138 2053 LISKLLELNVEKRI 2066
Cdd:cd14223   235 LLEGLLQRDVNRRL 248
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
1827-2075 1.60e-19

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: 91.03  E-value: 1.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKvidkRSVSIYE---KELLRsEISILRLLR-HPNVIYL-------KEIINTKETLY- 1894
Cdd:cd14036     8 IAEGGFAFVYEAQDVGTGKEYALK----RLLSNEEeknKAIIQ-EINFMKKLSgHPNIVQFcsaasigKEESDQGQAEYl 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVKGGeLYDFLL---AETRLSEIHANKIITQLIKTVAYLHRCG--IIHRDIKPENILLTDksrDAQIKLTDFGLST 1969
Cdd:cd14036    83 LLTELCKGQ-LVDFVKkveAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGN---QGQIKLCDFGSAT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1970 LCA---------------PNELLKEPcgTLAYVAPEVITLQG---YNHKVDAWSIGIILYLLLSGKLPFPINKNTEMnIQ 2031
Cdd:cd14036   159 TEAhypdyswsaqkrslvEDEITRNT--TPMYRTPEMIDLYSnypIGEKQDIWALGCILYLLCFRKHPFEDGAKLRI-IN 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 124804138 2032 KNYVLSFKDYIWKSISssakDLISKLLELNVEKRISANEALEHI 2075
Cdd:cd14036   236 AKYTIPPNDTQYTVFH----DLIRSTLKVNPEERLSITEIVEQL 275
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
1820-2020 1.63e-19

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: 91.22  E-value: 1.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1820 LYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDkrsVSIYEKELLRSEISILRLLRHPNVI--YLKEIINTK-----ET 1892
Cdd:cd06636    17 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD---VTEDEEEEIKLEINMLKKYSHHRNIatYYGAFIKKSppghdDQ 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1893 LYISMELVKGGELYDfLLAETR---LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLS- 1968
Cdd:cd06636    94 LWLVMEFCGAGSVTD-LVKNTKgnaLKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTE---NAEVKLVDFGVSa 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124804138 1969 ----TLCAPNELLkepcGTLAYVAPEVITLQ-----GYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd06636   170 qldrTVGRRNTFI----GTPYWMAPEVIACDenpdaTYDYRSDIWSLGITAIEMAEGAPPL 226
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
1819-2079 1.70e-19

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: 91.96  E-value: 1.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKE-LLRSEISILRLLRHPNVIYLKEIINTKETLYISM 1897
Cdd:cd05632     2 NTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGEsMALNEKQILEKVNSQFVVNLAYAYETKDALCLVL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGGEL--YDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPNE 1975
Cdd:cd05632    82 TIMNGGDLkfHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDD---YGHIRISDLGLAVKIPEGE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1976 LLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKN-TEMNIQKNYVLSFKDYIWKSISSSAKDLI 2054
Cdd:cd05632   159 SIRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEkVKREEVDRRVLETEEVYSAKFSEEAKSIC 238
                         250       260       270
                  ....*....|....*....|....*....|
gi 124804138 2055 SKLLELNVEKRI-----SANEALEHIWVKN 2079
Cdd:cd05632   239 KMLLTKDPKQRLgcqeeGAGEVKRHPFFRN 268
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
1816-2077 1.73e-19

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: 92.80  E-value: 1.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1816 TLYNLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETL-- 1893
Cdd:cd07875    21 TVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLee 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1894 ----YISMELVKGG--ELYDFLLAETRLSeihanKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGL 1967
Cdd:cd07875   101 fqdvYIVMELMDANlcQVIQMELDHERMS-----YLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKS---DCTLKILDFGL 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1968 STLCAPNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFP-------INKNTEM----------NI 2030
Cdd:cd07875   173 ARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPgtdhidqWNKVIEQlgtpcpefmkKL 252
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124804138 2031 Q---KNYVLS------------FKDYIWKSIS-------SSAKDLISKLLELNVEKRISANEALEHIWV 2077
Cdd:cd07875   253 QptvRTYVENrpkyagysfeklFPDVLFPADSehnklkaSQARDLLSKMLVIDASKRISVDEALQHPYI 321
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
1826-2086 1.73e-19

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: 91.62  E-value: 1.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1826 QLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEK-ELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGE 1904
Cdd:cd06634    22 EIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKwQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEYCLGSA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLCAPNELLkepCGTL 1984
Cdd:cd06634   102 SDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEP---GLVKLGDFGSASIMAPANSF---VGTP 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1985 AYVAPEVITLQG---YNHKVDAWSIGIILYLLLSGKLP-FPINKNTEM-NIQKNYVLSFKDYIWksiSSSAKDLISKLLE 2059
Cdd:cd06634   176 YWMAPEVILAMDegqYDGKVDVWSLGITCIELAERKPPlFNMNAMSALyHIAQNESPALQSGHW---SEYFRNFVDSCLQ 252
                         250       260
                  ....*....|....*....|....*....
gi 124804138 2060 LNVEKRISANEALEHIWV--KNPTAVINE 2086
Cdd:cd06634   253 KIPQDRPTSDVLLKHRFLlrERPPTVIMD 281
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
1822-2078 1.94e-19

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: 91.06  E-value: 1.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1822 ELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdkrSVSIYEKEL--LRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd06622     4 EVLDELGKGNYGSVYKVLHRPTGVTMAMKEI---RLELDESKFnqIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGG---ELYDFLLAETRLSEIHANKIITQLIKTVAYL-HRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLS-TLCApn 1974
Cdd:cd06622    81 MDAGsldKLYAGGVATEGIPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGN---GQVKLCDFGVSgNLVA-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1975 ELLKEPCGTLAYVAPEVITLQG------YNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYVL-----SFKDyiw 2043
Cdd:cd06622   156 SLAKTNIGCQSYMAPERIKSGGpnqnptYTVQSDVWSLGLSILEMALGRYPYPPETYANIFAQLSAIVdgdppTLPS--- 232
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 124804138 2044 kSISSSAKDLISKLLELNVEKRISANEALEHIWVK 2078
Cdd:cd06622   233 -GYSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLV 266
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
1821-2021 2.59e-19

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: 91.69  E-value: 2.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdkRSVSIYEKELLrSEISILRLLRHP------NVIYLKEIINTKETLY 1894
Cdd:cd14225    45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKII--RNKKRFHHQAL-VEVKILDALRRKdrdnshNVIHMKEYFYFRNHLC 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVkGGELYD---------FLLAETRlseihanKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRdAQIKLTDF 1965
Cdd:cd14225   122 ITFELL-GMNLYElikknnfqgFSLSLIR-------RFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQ-SSIKVIDF 192
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 124804138 1966 GLStlCAPNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFP 2021
Cdd:cd14225   193 GSS--CYEHQRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFP 246
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
1821-2075 2.90e-19

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: 92.04  E-value: 2.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdkRSVSIYEKEL---LRSEISILRLLRHPNVIYLKEIINTKETLYISM 1897
Cdd:cd05627     4 FESLKVIGRGAFGEVRLVQKKDTGHIYAMKIL--RKADMLEKEQvahIRAERDILVEADGAWVVKMFYSFQDKRNLYLIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLCAP---- 1973
Cdd:cd05627    82 EFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAK---GHVKLSDFGLCTGLKKahrt 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1974 --------------------------------NELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFP 2021
Cdd:cd05627   159 efyrnlthnppsdfsfqnmnskrkaetwkknrRQLAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFC 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 124804138 2022 INKNTE-----MNIQKnyVLSFKDYIwkSISSSAKDLISKLLeLNVEKRIsANEALEHI 2075
Cdd:cd05627   239 SETPQEtyrkvMNWKE--TLVFPPEV--PISEKAKDLILRFC-TDAENRI-GSNGVEEI 291
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
1827-2020 3.47e-19

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR 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: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 90.17  E-value: 3.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGI----NKQTNSEFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISmELVKG 1902
Cdd:cd05057    15 LGSGAFGTVYKGVwipeGEKVKIPVAIKVLREETGPKANEEILD-EAYVMASVDHPHLVRLLGICLSSQVQLIT-QLMPL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1903 GELYDFLLA-ETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdKSRDaQIKLTDFGLSTLCAPNE---LLK 1978
Cdd:cd05057    93 GCLLDYVRNhRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLV--KTPN-HVKITDFGLAKLLDVDEkeyHAE 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 124804138 1979 EPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPF 2020
Cdd:cd05057   170 GGKVPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTfGAKPY 212
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
1834-2076 3.58e-19

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: 90.07  E-value: 3.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1834 TVYRGINKQTNSEFAIKVIDKRSVSIYEK-------ELLRSEISILRLLRHPNVIYLKEIINTK--------ETLYISME 1898
Cdd:cd14011    11 KIYNGSKKSTKQEVSVFVFEKKQLEEYSKrdreqilELLKRGVKQLTRLRHPRILTVQHPLEESreslafatEPVFASLA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKG----GELYDFLLAETRLSEIHANKIITQLIKTVAYLH-RCGIIHRDIKPENILLtDKSRDAqiKLTDFGLS----- 1968
Cdd:cd14011    91 NVLGerdnMPSPPPELQDYKLYDVEIKYGLLQISEALSFLHnDVKLVHGNICPESVVI-NSNGEW--KLAGFDFCisseq 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1969 ------TLCAPNELLKEPCG-TLAYVAPEVITLQGYNHKVDAWSIGIILY-LLLSGKLPFPINKN---TEMNIQKNYVLS 2037
Cdd:cd14011   168 atdqfpYFREYDPNLPPLAQpNLNYLAPEYILSKTCDPASDMFSLGVLIYaIYNKGKPLFDCVNNllsYKKNSNQLRQLS 247
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 124804138 2038 FKdyIWKSISSSAKDLISKLLELNVEKRISANEALEHIW 2076
Cdd:cd14011   248 LS--LLEKVPEELRDHVKTLLNVTPEVRPDAEQLSKIPF 284
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
1821-1969 3.76e-19

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 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: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 89.44  E-value: 3.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSvsiyEKELLRSEISILRLLRH----PNVIYLKEIINTKetlYIS 1896
Cdd:cd14016     2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDS----KHPQLEYEAKVYKLLQGgpgiPRLYWFGQEGDYN---VMV 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124804138 1897 MELVkGGELYD-FLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLST 1969
Cdd:cd14016    75 MDLL-GPSLEDlFNKCGRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNKVYLIDFGLAK 147
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
1868-2015 3.84e-19

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 91.48  E-value: 3.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1868 EISILRLLRHPNVIYLKEIINTKETLYISMELVKGgELYDFLLAE-TRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKP 1946
Cdd:PHA03209  107 EAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYSS-DLYTYLTKRsRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKT 185
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124804138 1947 ENILLTDKSrdaQIKLTDFGLS--TLCAPNELlkEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLS 2015
Cdd:PHA03209  186 ENIFINDVD---QVCIGDLGAAqfPVVAPAFL--GLAGTVETNAPEVLARDKYNSKADIWSAGIVLFEMLA 251
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
1825-2037 4.72e-19

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. 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. Fer kinase is a member of the Fes subfamily of proteins which 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. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 88.91  E-value: 4.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSeFAIKVIDKRSVSIYEKELLrSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGE 1904
Cdd:cd05085     2 ELLGKGNFGEVYKGTLKDKTP-VAVKTCKEDLPQELKIKFL-SEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLlaETRLSEIHANKIITQLIKT---VAYLHRCGIIHRDIKPENILLTDKSrdaQIKLTDFGLST-----LCAPNEL 1976
Cdd:cd05085    80 FLSFL--RKKKDELKTKQLVKFSLDAaagMAYLESKNCIHRDLAARNCLVGENN---ALKISDFGMSRqeddgVYSSSGL 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124804138 1977 LKEPcgtLAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFP--INKNTEMNIQKNYVLS 2037
Cdd:cd05085   155 KQIP---IKWTAPEALNYGRYSSESDVWSFGILLWETFSlGVCPYPgmTNQQAREQVEKGYRMS 215
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
1827-2066 5.19e-19

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: 89.94  E-value: 5.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSI---YEKELLrsEISILRLLRHPNVIYLKEIINTKETLYISMELVKGG 1903
Cdd:cd05608     9 LGKGGFGEVSACQMRATGKLYACKKLNKKRLKKrkgYEGAMV--EKRILAKVHSRFIVSLAYAFQTKTDLCLVMTIMNGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 EL----YDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLST-LCAPNELLK 1978
Cdd:cd05608    87 DLryhiYNVDEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDD---DGNVRISDLGLAVeLKDGQTKTK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1979 EPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPI-NKNTEMNIQKNYVLSFKDYIWKSISSSAKDLISKL 2057
Cdd:cd05608   164 GYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRArGEKVENKELKQRILNDSVTYSEKFSPASKSICEAL 243

                  ....*....
gi 124804138 2058 LELNVEKRI 2066
Cdd:cd05608   244 LAKDPEKRL 252
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
1827-2079 5.35e-19

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: 89.72  E-value: 5.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLR-SEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGEL 1905
Cdd:cd05605     8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMAlNEKQILEKVNSRFVVSLAYAYETKDALCLVLTIMNGGDL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1906 --YDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLCAPNELLKEPCGT 1983
Cdd:cd05605    88 kfHIYNMGNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDH---GHVRISDLGLAVEIPEGETIRGRVGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1984 LAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKN----TEM-----NIQKNYVLSFkdyiwksiSSSAKDLI 2054
Cdd:cd05605   165 VGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEkvkrEEVdrrvkEDQEEYSEKF--------SEEAKSIC 236
                         250       260       270
                  ....*....|....*....|....*....|
gi 124804138 2055 SKLLELNVEKRI-----SANEALEHIWVKN 2079
Cdd:cd05605   237 SQLLQKDPKTRLgcrgeGAEDVKSHPFFKS 266
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
1826-2028 5.81e-19

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: 88.82  E-value: 5.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1826 QLGQGKFSTVYRGINKQTnSEFAIKVIDKRSVSiyeKELLRSEISILRLLRHPNVIYLKEIInTKETLYISMELVKGGEL 1905
Cdd:cd14203     2 KLGQGCFGEVWMGTWNGT-TKVAIKTLKPGTMS---PEAFLEEAQIMKKLRHDKLVQLYAVV-SEEPIYIVTEFMSKGSL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1906 YDFL-------LAETRLSEIHAnkiitQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPNELL- 1977
Cdd:cd14203    77 LDFLkdgegkyLKLPQLVDMAA-----QIASGMAYIERMNYIHRDLRAANILVGD---NLVCKIADFGLARLIEDNEYTa 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 124804138 1978 ----KEPcgtLAYVAPEVITLQGYNHKVDAWSIGIILY-LLLSGKLPFPINKNTEM 2028
Cdd:cd14203   149 rqgaKFP---IKWTAPEAALYGRFTIKSDVWSFGILLTeLVTKGRVPYPGMNNREV 201
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
1823-2020 9.65e-19

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: 88.34  E-value: 9.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1823 LHEQLGQGKFSTVYRGINKQTNSEFAIKvidKRSVSIYEKEllrsEISILRLLRHPNVIYLKEIINTKETLYISMELVKG 1902
Cdd:cd13991    10 HQLRIGRGSFGEVHRMEDKQTGFQCAVK---KVRLEVFRAE----ELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKEG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1903 GELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAqiKLTDFGLSTLCAPNELLKE--- 1979
Cdd:cd13991    83 GSLGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSDA--FLCDFGHAECLDPDGLGKSlft 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 124804138 1980 ---PCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd13991   161 gdyIPGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPW 204
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
1822-2034 9.71e-19

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: 88.59  E-value: 9.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1822 ELHEQLGQGKFSTVYRGiNKQTNSEFAIKVIDKRSVSiyeKELLRSEISILRLLRHPNVIYLKEIInTKETLYISMELVK 1901
Cdd:cd05070    12 QLIKRLGNGQFGEVWMG-TWNGNTKVAIKTLKPGTMS---PESFLEEAQIMKKLKHDKLVQLYAVV-SEEPIYIVTEYMS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1902 GGELYDFLL-AETRLSEI-HANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPNELLKE 1979
Cdd:cd05070    87 KGSLLDFLKdGEGRALKLpNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGN---GLICKIADFGLARLIEDNEYTAR 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 PCGT--LAYVAPEVITLQGYNHKVDAWSIGIILY-LLLSGKLPFPINKNTEM--NIQKNY 2034
Cdd:cd05070   164 QGAKfpIKWTAPEAALYGRFTIKSDVWSFGILLTeLVTKGRVPYPGMNNREVleQVERGY 223
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
1825-2036 1.03e-18

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: 88.27  E-value: 1.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGinKQTNS-EFAIKVIDKRSVSiyEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELVKGG 1903
Cdd:cd05059    10 KELGSGQFGVVHLG--KWRGKiDVAIKMIKEGSMS--EDDFIE-EAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMANG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 ELYDFLlaeTRLSEIHANKII----TQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPNELL-- 1977
Cdd:cd05059    85 CLLNYL---RERRGKFQTEQLlemcKDVCEAMEYLESNGFIHRDLAARNCLVGE---QNVVKVSDFGLARYVLDDEYTss 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124804138 1978 ---KEPcgtLAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFPINKNTEM--NIQKNYVL 2036
Cdd:cd05059   159 vgtKFP---VKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSeGKMPYERFSNSEVveHISQGYRL 220
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
1821-2079 1.26e-18

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: 90.83  E-value: 1.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDK-RSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd05622    75 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDfLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtDKSrdAQIKLTDFGLSTLCAPNELLK- 1978
Cdd:cd05622   155 MPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL-DKS--GHLKLADFGTCMKMNKEGMVRc 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1979 -EPCGTLAYVAPEVITLQG----YNHKVDAWSIGIILYLLLSGKLPF----PINKNTEMNIQKNyVLSFKDYiwKSISSS 2049
Cdd:cd05622   231 dTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFyadsLVGTYSKIMNHKN-SLTFPDD--NDISKE 307
                         250       260       270
                  ....*....|....*....|....*....|...
gi 124804138 2050 AKDLISKLLElNVEKRISAN---EALEHIWVKN 2079
Cdd:cd05622   308 AKNLICAFLT-DREVRLGRNgveEIKRHLFFKN 339
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
1827-1966 1.66e-18

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: 84.03  E-value: 1.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDkrSVSIYEKELLRSEISILRLLR--HPNVIYLKEIINTKETLYISMELVKGGE 1904
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVAVKIGD--DVNNEEGEDLESEMDILRRLKglELNIPKVLVTEDVDGPNILLMELVKGGT 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124804138 1905 LYDFLLaETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFG 1966
Cdd:cd13968    79 LIAYTQ-EEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSE---DGNVKLIDFG 136
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
1821-2054 1.71e-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: 90.10  E-value: 1.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdkRSVSIYEKEL---LRSEISILRLLRHPNVIYLKEIINTKETLYISM 1897
Cdd:cd05628     3 FESLKVIGRGAFGEVRLVQKKDTGHVYAMKIL--RKADMLEKEQvghIRAERDILVEADSLWVVKMFYSFQDKLNLYLIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLCAP---- 1973
Cdd:cd05628    81 EFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSK---GHVKLSDFGLCTGLKKahrt 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1974 --------------------------------NELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFP 2021
Cdd:cd05628   158 efyrnlnhslpsdftfqnmnskrkaetwkrnrRQLAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFC 237
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 124804138 2022 INKNTE-----MNIQKnyVLSFKDYIwkSISSSAKDLI 2054
Cdd:cd05628   238 SETPQEtykkvMNWKE--TLIFPPEV--PISEKAKDLI 271
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
1811-2078 1.89e-18

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: 88.20  E-value: 1.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1811 STKQNTLYNLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTK 1890
Cdd:cd06618     7 GKKYKADLNDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRSGNKEENKRILMDLDVVLKSHDCPYIVKCYGYFITD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1891 ETLYISMELVkgGELYDFLLAETR--LSEIHANKIITQLIKTVAYL-HRCGIIHRDIKPENILLTDksrDAQIKLTDFGL 1967
Cdd:cd06618    87 SDVFICMELM--STCLDKLLKRIQgpIPEDILGKMTVSIVKALHYLkEKHGVIHRDVKPSNILLDE---SGNVKLCDFGI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1968 STLCAPNELLKEPCGTLAYVAPEVITLQG---YNHKVDAWSIGIILYLLLSGKLPFPiNKNTEMNIQKNY------VLSF 2038
Cdd:cd06618   162 SGRLVDSKAKTRSAGCAAYMAPERIDPPDnpkYDIRADVWSLGISLVELATGQFPYR-NCKTEFEVLTKIlneeppSLPP 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 124804138 2039 KdyiwKSISSSAKDLISKLLELNVEKRISANEALEHIWVK 2078
Cdd:cd06618   241 N----EGFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIR 276
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
1826-2015 2.03e-18

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: 87.82  E-value: 2.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1826 QLGQGKFSTVYRG----INKQTNSEFAIKVIdKRSVSIYEKELLRSEISILRLLRHPNVIYLKEII--NTKETLYISMEL 1899
Cdd:cd05038    11 QLGEGHFGSVELCrydpLGDNTGEQVAVKSL-QPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCesPGRRSLRLIMEY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLlaetrlsEIHANKIIT--------QLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLC 1971
Cdd:cd05038    90 LPSGSLRDYL-------QRHRDQIDLkrlllfasQICKGMEYLGSQRYIHRDLAARNILV---ESEDLVKISDFGLAKVL 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 124804138 1972 APNE---LLKEPCGT-LAYVAPEVITLQGYNHKVDAWSIGIILYLLLS 2015
Cdd:cd05038   160 PEDKeyyYVKEPGESpIFWYAPECLRESRFSSASDVWSFGVTLYELFT 207
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
1821-2074 2.07e-18

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: 88.17  E-value: 2.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAikVIDKRSVSIYEKELLRS---EISILRLLR---HPNVIYLKEIINTKET-- 1892
Cdd:cd07862     3 YECVAEIGEGAYGKVFKARDLKNGGRFV--ALKRVRVQTGEEGMPLStirEVAVLRHLEtfeHPNVVRLFDVCTVSRTdr 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1893 ---LYISMELVKGgELYDFL--LAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGL 1967
Cdd:cd07862    81 etkLTLVFEHVDQ-DLTTYLdkVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTS---SGQIKLADFGL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1968 STLCAPNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGK--------------------LPFPINKNTE 2027
Cdd:cd07862   157 ARIYSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKplfrgssdvdqlgkildvigLPGEEDWPRD 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 124804138 2028 MNIQKNYVLSFK----DYIWKSISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd07862   237 VALPRQAFHSKSaqpiEKFVTDIDELGKDLLLKCLTFNPAKRISAYSALSH 287
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
1827-2019 3.50e-18

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: 86.42  E-value: 3.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRsvsIYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGELY 1906
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGKVMVVKIYKND---VDQHKIVR-EISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1907 DFLL-AETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTL--CAPnelLKEP--- 1980
Cdd:cd14156    77 ELLArEELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGREAVVTDFGLAREvgEMP---ANDPerk 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 124804138 1981 ---CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLsGKLP 2019
Cdd:cd14156   154 lslVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEIL-ARIP 194
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
1821-2069 3.78e-18

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: 88.17  E-value: 3.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKrsvsiYEKeLLRSEISILRLLRHPNVIYLKEIINT-------KETL 1893
Cdd:cd05597     3 FEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNK-----WEM-LKRAETACFREERDVLVNGDRRWITKlhyafqdENYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1894 YISMELVKGGELYDFLLA-ETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCA 1972
Cdd:cd05597    77 YLVMDYYCGGDLLTLLSKfEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLL---DRNGHIRLADFGSCLKLR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1973 PNELLKE--PCGTLAYVAPEVitLQG-------YNHKVDAWSIGIILYLLLSGKLPFPINKNTE-----MNIQKNyvLSF 2038
Cdd:cd05597   154 EDGTVQSsvAVGTPDYISPEI--LQAmedgkgrYGPECDWWSLGVCMYEMLYGETPFYAESLVEtygkiMNHKEH--FSF 229
                         250       260       270
                  ....*....|....*....|....*....|.
gi 124804138 2039 KDYIwKSISSSAKDLISKLLeLNVEKRISAN 2069
Cdd:cd05597   230 PDDE-DDVSEEAKDLIRRLI-CSRERRLGQN 258
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
1821-2072 4.26e-18

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 90.31  E-value: 4.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEI---------SILRLlrHPNVIYlKEIINTKE 1891
Cdd:PTZ00283   34 YWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMSEADKNRAQAEVccllncdffSIVKC--HEDFAK-KDPRNPEN 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1892 TLYISMEL--VKGGELYDFLLAETRLS----EIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDF 1965
Cdd:PTZ00283  111 VLMIALVLdyANAGDLRQEIKSRAKTNrtfrEHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCS---NGLVKLGDF 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1966 GLSTLCA---PNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPiNKNTEMNIQKNYVLSFkDYI 2042
Cdd:PTZ00283  188 GFSKMYAatvSDDVGRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFD-GENMEEVMHKTLAGRY-DPL 265
                         250       260       270
                  ....*....|....*....|....*....|
gi 124804138 2043 WKSISSSAKDLISKLLELNVEKRISANEAL 2072
Cdd:PTZ00283  266 PPSISPEMQEIVTALLSSDPKRRPSSSKLL 295
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
1820-2079 5.12e-18

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: 87.08  E-value: 5.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1820 LYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDkrsVSIYEKELLRSEISILRLLRHPNVI--YLKEIINTK-----ET 1892
Cdd:cd06637     7 IFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMD---VTGDEEEEIKQEINMLKKYSHHRNIatYYGAFIKKNppgmdDQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1893 LYISMELVKGGELYDfLLAETR---LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLS- 1968
Cdd:cd06637    84 LWLVMEFCGAGSVTD-LIKNTKgntLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTE---NAEVKLVDFGVSa 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1969 ----TLCAPNELLkepcGTLAYVAPEVITLQ-----GYNHKVDAWSIGIILYLLLSGKLPF----PInkNTEMNIQKNYV 2035
Cdd:cd06637   160 qldrTVGRRNTFI----GTPYWMAPEVIACDenpdaTYDFKSDLWSLGITAIEMAEGAPPLcdmhPM--RALFLIPRNPA 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 124804138 2036 LSFKDYIWksiSSSAKDLISKLLELNVEKRISANEALEHIWVKN 2079
Cdd:cd06637   234 PRLKSKKW---SKKFQSFIESCLVKNHSQRPSTEQLMKHPFIRD 274
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
1823-2034 5.30e-18

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: 86.66  E-value: 5.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1823 LHEQLGQGKFSTVYRGINKQTnSEFAIKVIDKRSVSiyeKELLRSEISILRLLRHPNVIYLKEIInTKETLYISMELVKG 1902
Cdd:cd05069    16 LDVKLGQGCFGEVWMGTWNGT-TKVAIKTLKPGTMM---PEAFLQEAQIMKKLRHDKLVPLYAVV-SEEPIYIVTEFMGK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1903 GELYDFLlAETRLSEIHANKII---TQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPNELLKE 1979
Cdd:cd05069    91 GSLLDFL-KEGDGKYLKLPQLVdmaAQIADGMAYIERMNYIHRDLRAANILVGD---NLVCKIADFGLARLIEDNEYTAR 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 PCGT--LAYVAPEVITLQGYNHKVDAWSIGIILY-LLLSGKLPFP--INKNTEMNIQKNY 2034
Cdd:cd05069   167 QGAKfpIKWTAPEAALYGRFTIKSDVWSFGILLTeLVTKGRVPYPgmVNREVLEQVERGY 226
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
1827-2078 5.67e-18

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: 86.34  E-value: 5.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLR-SEISILRLLRH----PNVIYLKEIINTKETLYISMELVK 1901
Cdd:cd05606     2 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLAlNERIMLSLVSTggdcPFIVCMTYAFQTPDKLCFILDLMN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1902 GGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLStlCAPNEllKEP- 1980
Cdd:cd05606    82 GGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDE---HGHVRISDLGLA--CDFSK--KKPh 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1981 --CGTLAYVAPEVITL-QGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYVLSFKDYIWKSISSSAKDLISKL 2057
Cdd:cd05606   155 asVGTHGYMAPEVLQKgVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKDKHEIDRMTLTMNVELPDSFSPELKSLLEGL 234
                         250       260
                  ....*....|....*....|....*.
gi 124804138 2058 LELNVEKRI-----SANEALEHIWVK 2078
Cdd:cd05606   235 LQRDVSKRLgclgrGATEVKEHPFFK 260
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
1825-2028 6.35e-18

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: 85.77  E-value: 6.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGiNKQTNSEFAIKVIDKRSVSiyeKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGE 1904
Cdd:cd05112    10 QEIGSGQFGLVHLG-YWLNKDKVAIKTIREGAMS---EEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAET-RLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSrdaQIKLTDFGLSTLCAPNELLKEPcGT 1983
Cdd:cd05112    86 LSDYLRTQRgLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQ---VVKVSDFGMTRFVLDDQYTSST-GT 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 124804138 1984 ---LAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFPINKNTEM 2028
Cdd:cd05112   162 kfpVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYENRSNSEV 210
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
1835-2076 6.48e-18

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: 85.48  E-value: 6.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1835 VYRGINKQTNSEFAIKVidkRSVSIYEKELlRSEIsilRLLRHPNVIYLKEIINTKETLYISMElVKGGELYDFLLAETR 1914
Cdd:cd14023     9 VYRALQLHSGAELQCKV---FPLKHYQDKI-RPYI---QLPSHRNITGIVEVILGDTKAYVFFE-KDFGDMHSYVRSCKR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1915 LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRdAQIKLTDFGLSTLCAPNE-LLKEPCGTLAYVAPEVIT 1993
Cdd:cd14023    81 LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDEER-TQLRLESLEDTHIMKGEDdALSDKHGCPAYVSPEILN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1994 LQG-YNHK-VDAWSIGIILYLLLSGKLPFpinKNTEMNIQKNYVLSFKDYIWKSISSSAKDLISKLLELNVEKRISANEA 2071
Cdd:cd14023   160 TTGtYSGKsADVWSLGVMLYTLLVGRYPF---HDSDPSALFSKIRRGQFCIPDHVSPKARCLIRSLLRREPSERLTAPEI 236

                  ....*
gi 124804138 2072 LEHIW 2076
Cdd:cd14023   237 LLHPW 241
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
1821-2079 1.04e-17

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: 87.75  E-value: 1.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDK-----RSVSIYEKEllrsEISILRLLRHPNVIYLKEIINTKETLYI 1895
Cdd:cd05621    54 YDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKfemikRSDSAFFWE----ERDIMAFANSPWVVQLFCAFQDDKYLYM 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1896 SMELVKGGELYDfLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCAPNE 1975
Cdd:cd05621   130 VMEYMPGGDLVN-LMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLL---DKYGHLKLADFGTCMKMDETG 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1976 LLK--EPCGTLAYVAPEVITLQG----YNHKVDAWSIGIILYLLLSGKLPF----PINKNTEMNIQKNyVLSFKDYIwkS 2045
Cdd:cd05621   206 MVHcdTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFyadsLVGTYSKIMDHKN-SLNFPDDV--E 282
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 124804138 2046 ISSSAKDLISKLLElNVEKRISAN---EALEHIWVKN 2079
Cdd:cd05621   283 ISKHAKNLICAFLT-DREVRLGRNgveEIKQHPFFRN 318
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
1821-2021 1.72e-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: 86.15  E-value: 1.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdKRSVSIYEKELLrsEISILRLLR-------HPNVIYLKEIINTKETL 1893
Cdd:cd14212     1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVL-KNKPAYFRQAML--EIAILTLLNtkydpedKHHIVRLLDHFMHHGHL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1894 YISMELVkGGELYDfLLAETRLSEIHAN---KIITQLIKTVAYLHRCGIIHRDIKPENILLTDkSRDAQIKLTDFGLStl 1970
Cdd:cd14212    78 CIVFELL-GVNLYE-LLKQNQFRGLSLQlirKFLQQLLDALSVLKDARIIHCDLKPENILLVN-LDSPEIKLIDFGSA-- 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 124804138 1971 CAPNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGkLP-FP 2021
Cdd:cd14212   153 CFENYTLYTYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAAELFLG-LPlFP 203
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
1803-2069 2.09e-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: 86.99  E-value: 2.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1803 EWVQALYSSTKQNTLYNL-YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDK-RSVSIYEKELLRSEISILRLLRHPNV 1880
Cdd:cd05623    55 EWAKPFTSKVKQMRLHKEdFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKwEMLKRAETACFREERDVLVNGDSQWI 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1881 IYLKEIINTKETLYISMELVKGGELYDFLLA-ETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQ 1959
Cdd:cd05623   135 TTLHYAFQDDNNLYLVMDYYVGGDLLTLLSKfEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILM---DMNGH 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1960 IKLTDFGLSTLCAPNELLKE--PCGTLAYVAPEVI-TLQG----YNHKVDAWSIGIILYLLLSGKLPFPINKNTE----- 2027
Cdd:cd05623   212 IRLADFGSCLKLMEDGTVQSsvAVGTPDYISPEILqAMEDgkgkYGPECDWWSLGVCMYEMLYGETPFYAESLVEtygki 291
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 124804138 2028 MNIQKNYVLSFKdyiWKSISSSAKDLISKLLeLNVEKRISAN 2069
Cdd:cd05623   292 MNHKERFQFPTQ---VTDVSENAKDLIRRLI-CSREHRLGQN 329
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
1826-2082 2.29e-17

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: 84.36  E-value: 2.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1826 QLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINT----KETLYISMELVK 1901
Cdd:cd14032     8 ELGRGSFKTVYKGLDTETWVEVAWCELQDRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFWEScakgKRCIVLVTELMT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1902 GGELYDFLLAETRLSEIHANKIITQLIKTVAYLH--RCGIIHRDIKPENILLTDKSrdAQIKLTDFGLSTLcAPNELLKE 1979
Cdd:cd14032    88 SGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHtrTPPIIHRDLKCDNIFITGPT--GSVKIGDLGLATL-KRASFAKS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 PCGTLAYVAPEVITlQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEmNIQKNYVLSFKDYIWKSI-SSSAKDLISKLL 2058
Cdd:cd14032   165 VIGTPEFMAPEMYE-EHYDESVDVYAFGMCMLEMATSEYPYSECQNAA-QIYRKVTCGIKPASFEKVtDPEIKEIIGECI 242
                         250       260
                  ....*....|....*....|....
gi 124804138 2059 ELNVEKRISANEALEHIWVKNPTA 2082
Cdd:cd14032   243 CKNKEERYEIKDLLSHAFFAEDTG 266
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
1842-2017 4.21e-17

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: 88.36  E-value: 4.21e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138  1842 QTNSEFAIKVI-DKRSVSIYEKELLRSEISILRLLRHPNVIYLkeiINTKET----LYISMELVKGGELYDFLLAETRLS 1916
Cdd:TIGR03903    1 MTGHEVAIKLLrTDAPEEEHQRARFRRETALCARLYHPNIVAL---LDSGEAppglLFAVFEYVPGRTLREVLAADGALP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138  1917 EIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCAPNE--------LLKEPCGTLAYVA 1988
Cdd:TIGR03903   78 AGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPHAKVLDFGIGTLLPGVRdadvatltRTTEVLGTPTYCA 157
                          170       180
                   ....*....|....*....|....*....
gi 124804138  1989 PEVITLQGYNHKVDAWSIGIILYLLLSGK 2017
Cdd:TIGR03903  158 PEQLRGEPVTPNSDLYAWGLIFLECLTGQ 186
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
1828-2057 4.67e-17

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: 83.08  E-value: 4.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1828 GQGKFSTVYRGINKQTNSEFAIKVIDKrsvsiyekelLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGELYD 1907
Cdd:cd14060     2 GGGSFGSVYRAIWVSQDKEVAVKKLLK----------IEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1908 FLlAETRLSEIHANKIIT---QLIKTVAYLHR---CGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPNELLKePC 1981
Cdd:cd14060    72 YL-NSNESEEMDMDQIMTwatDIAKGMHYLHMeapVKVIHRDLKSRNVVIAA---DGVLKICDFGASRFHSHTTHMS-LV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1982 GTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFP-----------INKNTEMNIQKNYVLSFKDYI---WKSIS 2047
Cdd:cd14060   147 GTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKgleglqvawlvVEKNERPTIPSSCPRSFAELMrrcWEADV 226
                         250
                  ....*....|...
gi 124804138 2048 S---SAKDLISKL 2057
Cdd:cd14060   227 KerpSFKQIIGIL 239
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1806-2020 7.01e-17

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: 83.54  E-value: 7.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1806 QALYSSTKQNTLYNlYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSV-SIYEKELLRSEISILRLLRHPNVI-YL 1883
Cdd:cd08229    12 KALRPDMGYNTLAN-FRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLmDAKARADCIKEIDLLKQLNHPNVIkYY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1884 KEIINTKEtLYISMELVKGGELYD----FLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQ 1959
Cdd:cd08229    91 ASFIEDNE-LNIVLELADAGDLSRmikhFKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITAT---GV 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124804138 1960 IKLTDFGL-----STLCAPNELLkepcGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd08229   167 VKLGDLGLgrffsSKTTAAHSLV----GTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPF 228
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
1865-2019 7.63e-17

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: 83.09  E-value: 7.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1865 LRSEISILRLLRHPNVIYLKEIinTKETLYISMELVKGGELYDFLLAETR------LSEIHANKIITQLIKTVAYLHRCG 1938
Cdd:cd14067    57 FRQEASMLHSLQHPCIVYLIGI--SIHPLCFALELAPLGSLNTVLEENHKgssfmpLGHMLTFKIAYQIAAGLAYLHKKN 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1939 IIHRDIKPENILL--TDKSRDAQIKLTDFGLSTLCAPNELLKEPcGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSG 2016
Cdd:cd14067   135 IIFCDLKSDNILVwsLDVQEHINIKLSDYGISRQSFHEGALGVE-GTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELLSG 213

                  ...
gi 124804138 2017 KLP 2019
Cdd:cd14067   214 QRP 216
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
1823-2020 8.00e-17

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR 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: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 82.81  E-value: 8.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1823 LHEQLGQGKFSTVYRG---INKQTNSEFAIKVIdKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd05033     8 IEKVIGGGEFGEVCSGslkLPGKKEIDVAIKTL-KSGYSDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKSRPVMIVTEY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLA-ETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCAPNELLK 1978
Cdd:cd05033    87 MENGSLDKFLREnDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILV---NSDLVCKVSDFGLSRRLEDSEATY 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 124804138 1979 EPCG---TLAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPF 2020
Cdd:cd05033   164 TTKGgkiPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSyGERPY 209
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
1863-2074 8.33e-17

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: 82.41  E-value: 8.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1863 ELLRSEISILRLLRHPNVIYL-----KEIINTKE-TLYISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHR 1936
Cdd:cd14012    43 QLLEKELESLKKLRHPNLVSYlafsiERRGRSDGwKVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHR 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1937 CGIIHRDIKPENILLTDKSRDAQIKLTDFGLST----LCA-PNELLKEPCGtlaYVAPEVITLQG-YNHKVDAWSIGIIL 2010
Cdd:cd14012   123 NGVVHKSLHAGNVLLDRDAGTGIVKLTDYSLGKtlldMCSrGSLDEFKQTY---WLPPELAQGSKsPTRKTDVWDLGLLF 199
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124804138 2011 YLLLSGKLPFpiNKNTEMNIQKNYVlsfkdyiwkSISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd14012   200 LQMLFGLDVL--EKYTSPNPVLVSL---------DLSASLQDFLSKCLSLDPKKRPTALELLPH 252
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
1822-2020 8.50e-17

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function 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. The KSR2 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: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 82.75  E-value: 8.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1822 ELHEQLGQGKFSTVYRGinkQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVK 1901
Cdd:cd14153     3 EIGELIGKGRFGQVYHG---RWHGEVAIRLIDIERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1902 GGELYDFLL-AETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTdksrDAQIKLTDFGLSTLCA------PN 1974
Cdd:cd14153    80 GRTLYSVVRdAKVVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD----NGKVVITDFGLFTISGvlqagrRE 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 124804138 1975 ELLKEPCGTLAYVAPEVITLQG---------YNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd14153   156 DKLRIQSGWLCHLAPEIIRQLSpeteedklpFSKHSDVFAFGTIWYELHAREWPF 210
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
1827-2010 8.75e-17

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 82.94  E-value: 8.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKrsvsiYEKELLRS---EISILRLLRHPNVIYLKEIINTKETLYISMELVKGG 1903
Cdd:cd14154     1 LGKGFFGQAIKVTHRETGEVMVMKELIR-----FDEEAQRNflkEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 ELYDFLLAETR-LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLC------APNEL 1976
Cdd:cd14154    76 TLKDVLKDMARpLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVRE---DKTVVVADFGLARLIveerlpSGNMS 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 124804138 1977 -------LKEP--------CGTLAYVAPEVITLQGYNHKVDAWSIGIIL 2010
Cdd:cd14154   153 psetlrhLKSPdrkkrytvVGNPYWMAPEMLNGRSYDEKVDIFSFGIVL 201
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
1825-2020 1.23e-16

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 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: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 82.47  E-value: 1.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSEFAIKVIdKRSVSIYEKELLRSEISI-LRLLRHPNVIYLKEIINTKETLYISMELVKGg 1903
Cdd:cd06617     7 EELGRGAYGVVDKMRHVPTGTIMAVKRI-RATVNSQEQKRLLMDLDIsMRSVDCPYTVTFYGALFREGDVWICMEVMDT- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 ELYDF----LLAETRLSEIHANKIITQLIKTVAYLH-RCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCApNELLK 1978
Cdd:cd06617    85 SLDKFykkvYDKGLTIPEDILGKIAVSIVKALEYLHsKLSVIHRDVKPSNVLI---NRNGQVKLCDFGISGYLV-DSVAK 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 124804138 1979 E-PCGTLAYVAPEVI----TLQGYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd06617   161 TiDAGCKPYMAPERInpelNQKGYDVKSDVWSLGITMIELATGRFPY 207
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
1822-2021 1.84e-16

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: 81.57  E-value: 1.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1822 ELHEQLGQGKFSTV----YRGinkqtnSEFAIKVIDKRSVSiyekELLRSEISILRLLRHPNVI-YLKEIINTKETLYIS 1896
Cdd:cd05082     9 KLLQTIGKGEFGDVmlgdYRG------NKVAVKCIKNDATA----QAFLAEASVMTQLRHSNLVqLLGVIVEEKGGLYIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1897 MELVKGGELYDFLLAETRlSEIHANKIIT---QLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLST-LCA 1972
Cdd:cd05082    79 TEYMAKGSLVDYLRSRGR-SVLGGDCLLKfslDVCEAMEYLEGNNFVHRDLAARNVLV---SEDNVAKVSDFGLTKeASS 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 124804138 1973 PNELLKEPcgtLAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFP 2021
Cdd:cd05082   155 TQDTGKLP---VKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPYP 201
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
1822-2030 2.37e-16

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 81.55  E-value: 2.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1822 ELHEQLGQGKFSTVYRGinkQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVK 1901
Cdd:cd14152     3 ELGELIGQGRWGKVHRG---RWHGEVAIRLLEIDGNNQDHLKLFKKEVMNYRQTRHENVVLFMGACMHPPHLAIITSFCK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1902 GGELYDFLLAETRLSEIHANKIITQ-LIKTVAYLHRCGIIHRDIKPENILLTdksrDAQIKLTDFGLSTLCA-------P 1973
Cdd:cd14152    80 GRTLYSFVRDPKTSLDINKTRQIAQeIIKGMGYLHAKGIVHKDLKSKNVFYD----NGKVVITDFGLFGISGvvqegrrE 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124804138 1974 NElLKEPCGTLAYVAPEVITLQG---------YNHKVDAWSIGIILYLLLSGKLPFpINKNTEMNI 2030
Cdd:cd14152   156 NE-LKLPHDWLCYLAPEIVREMTpgkdedclpFSKAADVYAFGTIWYELQARDWPL-KNQPAEALI 219
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
1825-2011 3.84e-16

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: 80.46  E-value: 3.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSE---FAIKVIDKRSVSIYE--KELLRsEISILRLLRHPNVIYLKEIINTKETLYISmEL 1899
Cdd:cd05040     1 EKLGDGSFGVVRRGEWTTPSGKviqVAVKCLKSDVLSQPNamDDFLK-EVNAMHSLDHPNLIRLYGVVLSSPLMMVT-EL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDfllaetRLSEIHANKIIT-------QLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCA 1972
Cdd:cd05040    79 APLGSLLD------RLRKDQGHFLIStlcdyavQIANGMAYLESKRFIHRDLAARNILL---ASKDKVKIGDFGLMRALP 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 124804138 1973 PN-------ELLKEPcgtLAYVAPEVITLQGYNHKVDAWSIGIILY 2011
Cdd:cd05040   150 QNedhyvmqEHRKVP---FAWCAPESLKTRKFSHASDVWMFGVTLW 192
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
1822-2032 4.52e-16

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. The STRAD-beta 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: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 81.84  E-value: 4.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1822 ELHEQLGQG--KFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd08226     1 ELQVELGKGfcNLTSVYLARHTPTGTLVTVKITNLDNCSEEHLKALQNEVVLSHFFRHPNIMTHWTVFTEGSWLWVISPF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLA--ETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTdfGLSTLCApneLL 1977
Cdd:cd08226    81 MAYGSARGLLKTyfPEGMNEALIGNILYGAIKALNYLHQNGCIHRSVKASHILI---SGDGLVSLS--GLSHLYS---MV 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1978 KE-------------PCGTLAYVAPEVIT--LQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQK 2032
Cdd:cd08226   153 TNgqrskvvydfpqfSTSVLPWLSPELLRqdLHGYNVKSDIYSVGITACELARGQVPFQDMRRTQMLLQK 222
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
1827-2027 6.32e-16

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK 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: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 80.51  E-value: 6.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRG----INKQTNS-EFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELVK 1901
Cdd:cd05036    14 LGQGAFGEVYEGtvsgMPGDPSPlQVAVKTLPELCSEQDEMDFLM-EALIMSKFNHPNIVRCIGVCFQRLPRFILLELMA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1902 GGELYDFLlAETRLSEIHANKI----ITQLIKTVA----YLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLS-TLCA 1972
Cdd:cd05036    93 GGDLKSFL-RENRPRPEQPSSLtmldLLQLAQDVAkgcrYLEENHFIHRDIAARNCLLTCKGPGRVAKIGDFGMArDIYR 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 124804138 1973 PNELLKEPCGTL--AYVAPEVItLQG-YNHKVDAWSIGIILYLLLS-GKLPFPINKNTE 2027
Cdd:cd05036   172 ADYYRKGGKAMLpvKWMPPEAF-LDGiFTSKTDVWSFGVLLWEIFSlGYMPYPGKSNQE 229
K-ycf53 COG5752
Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 ...
1817-2117 8.48e-16

Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 porphyrin-binding domain [Signal transduction mechanisms];


Pssm-ID: 444462 [Multi-domain]  Cd Length: 466  Bit Score: 82.74  E-value: 8.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1817 LYNLYELHEQLGQGKFSTVYRGINKQTNSE--FAIK--VIDKRSVSIYEK--ELLRSE-ISILRLLRHPNVIYLKEIINT 1889
Cdd:COG5752    30 LKERYRAIKPLGQGGFGRTFLAVDEDIPSHphCVIKqfYFPEQGPSSFQKavELFRQEaVRLDELGKHPQIPELLAYFEQ 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1890 KETLYISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdKSRDAQIKLTDFGLST 1969
Cdd:COG5752   110 DQRLYLVQEFIEGQTLAQELEKKGVFSESQIWQLLKDLLPVLQFIHSRNVIHRDIKPANIIR--RRSDGKLVLIDFGVAK 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1970 LCAPNELLKEPC--GTLAYVAPEviTLQGynhKV----DAWSIGIILYLLLSGKLPFpinkntEMniqknYVLSFKDYIW 2043
Cdd:COG5752   188 LLTITALLQTGTiiGTPEYMAPE--QLRG---KVfpasDLYSLGVTCIYLLTGVSPF------DL-----FDVSEDRWVW 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 2044 -------KSISSSAKDLISKLLELNVEKRI-SANEALEHIWVkNPTAVINENSFIYKNEEINILNLQDVSVSTFNIPrYT 2115
Cdd:COG5752   252 rdflppgTKVSDRLGQILDKLLQNALKQRYqSATEVLQALKR-QPPVSYSPIPVAPTKLPIQAQPPDITLKSAKGVD-YT 329

                  ..
gi 124804138 2116 PL 2117
Cdd:COG5752   330 QL 331
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
1821-2021 8.86e-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: 80.87  E-value: 8.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd06650     7 FEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIR-ELQVLHECNSPYIVGFYGAFYSDGEISICMEHM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYL-HRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLCApNELLKE 1979
Cdd:cd06650    86 DGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLrEKHKIMHRDVKPSNILVNSR---GEIKLCDFGVSGQLI-DSMANS 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 124804138 1980 PCGTLAYVAPEviTLQGYNHKV--DAWSIGIILYLLLSGKLPFP 2021
Cdd:cd06650   162 FVGTRSYMSPE--RLQGTHYSVqsDIWSMGLSLVEMAVGRYPIP 203
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
1865-2026 9.67e-16

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 82.82  E-value: 9.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1865 LRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGgELYDF------------LLAETRlseihanKIITQLIKTVA 1932
Cdd:PHA03210  210 LENEILALGRLNHENILKIEEILRSEANTYMITQKYDF-DLYSFmydeafdwkdrpLLKQTR-------AIMKQLLCAVE 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1933 YLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTlcaPNELLKEP-----CGTLAYVAPEVITLQGYNHKVDAWSIG 2007
Cdd:PHA03210  282 YIHDKKLIHRDIKLENIFL---NCDGKIVLGDFGTAM---PFEKEREAfdygwVGTVATNSPEILAGDGYCEITDIWSCG 355
                         170
                  ....*....|....*....
gi 124804138 2008 IILYLLLSGKLpFPINKNT 2026
Cdd:PHA03210  356 LILLDMLSHDF-CPIGDGG 373
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
1820-2043 9.99e-16

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 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: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 80.09  E-value: 9.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1820 LYELHEQLGQGKFSTVYRGI---NKQTNSEFAIKVidKRSVSIYEKELLRSEISILRLLRHPNVIYLKEII-NTKETLYI 1895
Cdd:cd13981     1 TYVISKELGEGGYASVYLAKdddEQSDGSLVALKV--EKPPSIWEFYICDQLHSRLKNSRLRESISGAHSAhLFQDESIL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1896 SMELVKGGELYDfLLAETRLS------EIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDK------------SRD 1957
Cdd:cd13981    79 VMDYSSQGTLLD-VVNKMKNKtgggmdEPLAMFFTIELLKVVEALHEVGIIHGDIKPDNFLLRLEicadwpgegengWLS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1958 AQIKLTDFGLS---TLCAPNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNY 2034
Cdd:cd13981   158 KGLKLIDFGRSidmSLFPKNQSFKADWHTDSFDCIEMREGRPWTYQIDYFGIAATIHVMLFGKYMELTQESGRWKINQNL 237

                  ....*....
gi 124804138 2035 VLSFKDYIW 2043
Cdd:cd13981   238 KRYWQRDIW 246
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
1823-2021 2.04e-15

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: 78.62  E-value: 2.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1823 LHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIyeKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELVKG 1902
Cdd:cd05052    10 MKHKLGGGQYGEVYEGVWKKYNLTVAVKTLKEDTMEV--EEFLK-EAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1903 GELYDFL--LAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCApNELLKEP 1980
Cdd:cd05052    87 GNLLDYLreCNREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGE---NHLVKVADFGLSRLMT-GDTYTAH 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 124804138 1981 CGT---LAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFP 2021
Cdd:cd05052   163 AGAkfpIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATyGMSPYP 207
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
1825-2015 2.06e-15

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: 78.90  E-value: 2.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTV----YRGINKQTNSEFAIKVIdKRSVSIYEKELLRsEISILRLLRHPNVIYLKEIINT--KETLYISME 1898
Cdd:cd14205    10 QQLGKGNFGSVemcrYDPLQDNTGEVVAVKKL-QHSTEEHLRDFER-EIEILKSLQHDNIVKYKGVCYSagRRNLRLIME 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFLLA-ETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRdaqIKLTDFGLSTLCAPNE-- 1975
Cdd:cd14205    88 YLPYGSLRDYLQKhKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENR---VKIGDFGLTKVLPQDKey 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 124804138 1976 -LLKEPCGT-LAYVAPEVITLQGYNHKVDAWSIGIILYLLLS 2015
Cdd:cd14205   165 yKVKEPGESpIFWYAPESLTESKFSVASDVWSFGVVLYELFT 206
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
1878-2071 2.19e-15

Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-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: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 78.74  E-value: 2.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1878 PNVIYLKEIINTKETLYISMELVKGGELYDFLLAETRLSEIH-------------ANKIITQ-LIK------TVAY--LH 1935
Cdd:cd05576    51 PNMVCLRKYIISEESVFLVLQHAEGGKLWSYLSKFLNDKEIHqlfadlderlaaaSRFYIPEeCIQrwaaemVVALdaLH 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1936 RCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLCAPNellkepCGTLA----YVAPEVITLQGYNHKVDAWSIGIILY 2011
Cdd:cd05576   131 REGIVCRDLNPNNILLNDR---GHIQLTYFSRWSEVEDS------CDSDAienmYCAPEVGGISEETEACDWWSLGALLF 201
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 2012 LLLSGKlpfPINKNTEMNIQKNYVLSFKDYiwksISSSAKDLISKLLELNVEKRISANEA 2071
Cdd:cd05576   202 ELLTGK---ALVECHPAGINTHTTLNIPEW----VSEEARSLLQQLLQFNPTERLGAGVA 254
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
1823-2021 2.59e-15

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk 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: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 77.99  E-value: 2.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1823 LHEQLGQGKFSTVYRGinKQTNSEFAIKVIdKRSVSiyeKELLRSEISILRLLRHPNVIYLKEIInTKETLYISMELVKG 1902
Cdd:cd05083    10 LGEIIGEGEFGAVLQG--EYMGQKVAVKNI-KCDVT---AQAFLEETAVMTKLQHKNLVRLLGVI-LHNGLYIVMELMSK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1903 GELYDFLLAETR--LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTL---CAPNELL 1977
Cdd:cd05083    83 GNLVNFLRSRGRalVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILV---SEDGVAKISDFGLAKVgsmGVDNSRL 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 124804138 1978 KepcgtLAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFP 2021
Cdd:cd05083   160 P-----VKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSyGRAPYP 199
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
1821-2021 2.89e-15

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: 80.18  E-value: 2.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKrsvsiyEKELLRS---EISILRLLRHP------NVIYLKE------ 1885
Cdd:cd14224    67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRN------EKRFHRQaaeEIRILEHLKKQdkdntmNVIHMLEsftfrn 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1886 -IINTKETLYISM-ELVKGGELYDFLLAETRlseihanKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAqIKLT 1963
Cdd:cd14224   141 hICMTFELLSMNLyELIKKNKFQGFSLQLVR-------KFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRSG-IKVI 212
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 124804138 1964 DFGLStlCAPNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFP 2021
Cdd:cd14224   213 DFGSS--CYEHQRIYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGYPLFP 268
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
1821-2074 3.02e-15

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: 79.28  E-value: 3.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGIN-KQTNSEFAIKVIdkRSVSIYeKELLRSEISILRLLRHPN------VIYLKEIINTKETL 1893
Cdd:cd14214    15 YEIVGDLGEGTFGKVVECLDhARGKSQVALKII--RNVGKY-REAARLEINVLKKIKEKDkenkflCVLMSDWFNFHGHM 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1894 YISMELVkGGELYDFLLAETRLSE--IHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKS---------------- 1955
Cdd:cd14214    92 CIAFELL-GKNTFEFLKENNFQPYplPHIRHMAYQLCHALKFLHENQLTHTDLKPENILFVNSEfdtlynesksceeksv 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1956 RDAQIKLTDFGLSTLcaPNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYV 2035
Cdd:cd14214   171 KNTSIRVADFGSATF--DHEHHTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQTHENREHLVMMEKI 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 2036 LS----------------FK-DYIWKSISSSAK------------------------DLISKLLELNVEKRISANEALEH 2074
Cdd:cd14214   249 LGpipshmihrtrkqkyfYKgSLVWDENSSDGRyvsenckplmsymlgdslehtqlfDLLRRMLEFDPALRITLKEALLH 328
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
1826-2081 4.24e-15

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: 78.17  E-value: 4.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1826 QLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYL----KEIINTKETLYISMELVK 1901
Cdd:cd14030    32 EIGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKSERQRFKEEAGMLKGLQHPNIVRFydswESTVKGKKCIVLVTELMT 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1902 GGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCG--IIHRDIKPENILLTDKSrdAQIKLTDFGLSTLcAPNELLKE 1979
Cdd:cd14030   112 SGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPT--GSVKIGDLGLATL-KRASFAKS 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1980 PCGTLAYVAPEVITlQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEmNIQKNYVLSFKDYIWKSIS-SSAKDLISKLL 2058
Cdd:cd14030   189 VIGTPEFMAPEMYE-EKYDESVDVYAFGMCMLEMATSEYPYSECQNAA-QIYRRVTSGVKPASFDKVAiPEVKEIIEGCI 266
                         250       260
                  ....*....|....*....|...
gi 124804138 2059 ELNVEKRISANEALEHIWVKNPT 2081
Cdd:cd14030   267 RQNKDERYAIKDLLNHAFFQEET 289
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
1867-2072 6.81e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 79.12  E-value: 6.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1867 SEISILRLLRHPNVIYLKEIINTKETLYISMELVKggelYDFLLAETRLSEIHANKIIT---QLIKTVAYLHRCGIIHRD 1943
Cdd:PHA03207  135 REIDILKTISHRAIINLIHAYRWKSTVCMVMPKYK----CDLFTYVDRSGPLPLEQAITiqrRLLEALAYLHGRGIIHRD 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1944 IKPENILLtDKSRDAQikLTDFGLStlCAPNELLKEP-----CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKL 2018
Cdd:PHA03207  211 VKTENIFL-DEPENAV--LGDFGAA--CKLDAHPDTPqcygwSGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKNV 285
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 2019 P--------------------------FPINKNTEM-------NIQKNYVLSFKDYIWKSI-SSSAKDLISKLLELNVEK 2064
Cdd:PHA03207  286 TlfgkqvkssssqlrsiircmqvhpleFPQNGSTNLckhfkqyAIVLRPPYTIPPVIRKYGmHMDVEYLIAKMLTFDQEF 365

                  ....*...
gi 124804138 2065 RISANEAL 2072
Cdd:PHA03207  366 RPSAQDIL 373
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
1821-1968 7.87e-15

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK 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: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 76.91  E-value: 7.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSvsiyEKELLRSEISILRLLR-HPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd14017     2 WKVVKKIGGGGFGEIYKVRDVVDGEEVAMKVESKSQ----PKQVLKMEVAVLKKLQgKPHFCRLIGCGRTERYNYIVMTL 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124804138 1900 VkGGELYDFL--LAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILL-TDKSRDAQIKLTDFGLS 1968
Cdd:cd14017    78 L-GPNLAELRrsQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIgRGPSDERTVYILDFGLA 148
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
1822-2020 8.34e-15

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB 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: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 76.83  E-value: 8.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1822 ELHEQLGQGKFSTVYRGINKQTNSE---FAIKVIDKRSVSIYEKELLrSEISILRLLRHPNVIYLKEIINTKETLYISME 1898
Cdd:cd05065     7 KIEEVIGAGEFGEVCRGRLKLPGKReifVAIKTLKSGYTEKQRRDFL-SEASIMGQFDHPNIIHLEGVVTKSRPVMIITE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFL-LAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCAPNEll 1977
Cdd:cd05065    86 FMENGALDSFLrQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILV---NSNLVCKVSDFGLSRFLEDDT-- 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 124804138 1978 KEPCGTLA--------YVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPF 2020
Cdd:cd05065   161 SDPTYTSSlggkipirWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPY 212
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
1822-2074 8.67e-15

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear 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. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The 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: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 77.06  E-value: 8.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1822 ELHE--QLGQGKFSTVYRGINKQTNSEFAIKViDKRSV--SIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISM 1897
Cdd:cd14051     1 EFHEveKIGSGEFGSVYKCINRLDGCVYAIKK-SKKPVagSVDEQNALNEVYAHAVLGKHPHVVRYYSAWAEDDHMIIQN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGGELYDFL----LAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLT-------------------DK 1954
Cdd:cd14051    80 EYCNGGSLADAIseneKAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISrtpnpvsseeeeedfegeeDN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1955 SRDAQI--KLTDFGLSTlCAPNELLKEpcGTLAYVAPEVITlQGYNH--KVDAWSIGIILYLLLSGKlPFPINKNTEMNI 2030
Cdd:cd14051   160 PESNEVtyKIGDLGHVT-SISNPQVEE--GDCRFLANEILQ-ENYSHlpKADIFALALTVYEAAGGG-PLPKNGDEWHEI 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 124804138 2031 QKNYV--LSfkdyiwkSISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd14051   235 RQGNLppLP-------QCSPEFNELLRSMIHPDPEKRPSAAALLQH 273
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
1826-2028 1.08e-14

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: 76.54  E-value: 1.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1826 QLGQGKFSTVYRGINKQTNSE--FAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTkETLYISMELVKGG 1903
Cdd:cd05116     2 ELGSGNFGTVKKGYYQMKKVVktVAVKILKNEANDPALKDELLREANVMQQLDNPYIVRMIGICEA-ESWMLVMEMAELG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 ELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSrdaQIKLTDFGLSTLCAPNELLKEPCGT 1983
Cdd:cd05116    81 PLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQH---YAKISDFGLSKALRADENYYKAQTH 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 124804138 1984 ----LAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFPINKNTEM 2028
Cdd:cd05116   158 gkwpVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPYKGMKGNEV 207
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
1827-2035 1.25e-14

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


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 76.79  E-value: 1.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKqtNSEFAIKVIDKRSVSIYE--KELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGE 1904
Cdd:cd14159     1 IGEGGFGCVYQAVMR--NTEYAVKRLKEDSELDWSvvKNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVYLPNGS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAETR---LSEIHANKIITQLIKTVAYLHRC--GIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLC-------- 1971
Cdd:cd14159    79 LEDRLHCQVScpcLSWSQRLHVLLGTARAIQYLHSDspSLIHGDVKSSNILLDAA---LNPKLGDFGLARFSrrpkqpgm 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124804138 1972 ----APNELLKepcGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYV 2035
Cdd:cd14159   156 sstlARTQTVR---GTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAMEVDSCSPTKYLKDLV 220
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
1822-2021 1.28e-14

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR 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: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 76.69  E-value: 1.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1822 ELHEQLGQGKFSTV----YRGINKQTNSEFAIKViDKRSVSIYEKEL--LRSEISILRLL-RHPNVIYLKEIINTKETLY 1894
Cdd:cd05053    15 TLGKPLGEGAFGQVvkaeAVGLDNKPNEVVTVAV-KMLKDDATEKDLsdLVSEMEMMKMIgKHKNIINLLGACTQDGPLY 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVKGGELYDFLLAEtRLSEIHANKIIT-----------------QLIKTVAYLHRCGIIHRDIKPENILLTDksrD 1957
Cdd:cd05053    94 VVVEYASKGNLREFLRAR-RPPGEEASPDDPrvpeeqltqkdlvsfayQVARGMEYLASKKCIHRDLAARNVLVTE---D 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124804138 1958 AQIKLTDFGLSTLCAPNELLKEPC-GTLAY--VAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFP 2021
Cdd:cd05053   170 NVMKIADFGLARDIHHIDYYRKTTnGRLPVkwMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYP 237
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
1821-2074 1.54e-14

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: 77.20  E-value: 1.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGIN-KQTNSEFAIKVIdkRSVSIYeKELLRSEISILRLL--RHPNVIY----LKEIINTKETL 1893
Cdd:cd14213    14 YEIVDTLGEGAFGKVVECIDhKMGGMHVAVKIV--KNVDRY-REAARSEIQVLEHLntTDPNSTFrcvqMLEWFDHHGHV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1894 YISMELVkGGELYDFLLAETRL--SEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTD----------KSRDAQ-- 1959
Cdd:cd14213    91 CIVFELL-GLSTYDFIKENSFLpfPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQsdyvvkynpkMKRDERtl 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1960 ----IKLTDFGLSTLcaPNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIIL-----------------YLLLSGKL 2018
Cdd:cd14213   170 knpdIKVVDFGSATY--DDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILieyylgftvfqthdskeHLAMMERI 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 2019 PFPINKNTEMNIQKNYVLSFKDYIWKSISSSAK------------------------DLISKLLELNVEKRISANEALEH 2074
Cdd:cd14213   248 LGPLPKHMIQKTRKRKYFHHDQLDWDEHSSAGRyvrrrckplkefmlsqdvdheqlfDLIQKMLEYDPAKRITLDEALKH 327
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
1821-2021 1.57e-14

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: 77.40  E-value: 1.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd06649     7 FERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAIRNQIIR-ELQVLHECNSPYIVGFYGAFYSDGEISICMEHM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETRLSEIHANKIITQLIKTVAYL-HRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLCApNELLKE 1979
Cdd:cd06649    86 DGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLrEKHQIMHRDVKPSNILVNSR---GEIKLCDFGVSGQLI-DSMANS 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 124804138 1980 PCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFP 2021
Cdd:cd06649   162 FVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIP 203
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
1824-2020 2.33e-14

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: 75.61  E-value: 2.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1824 HEQLGQGKFSTVYRGINKqtnsefaikvidkrsvSIYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELVKGG 1903
Cdd:cd14027    14 HRTQGLVVLKTVYTGPNC----------------IEHNEALLE-EGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 ELYDFLLAETRLSEIHAnKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCAPNELLKEP--- 1980
Cdd:cd14027    77 NLMHVLKKVSVPLSVKG-RIILEIIEGMAYLHGKGVIHKDLKPENILV---DNDFHIKIADLGLASFKMWSKLTKEEhne 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 124804138 1981 -----------CGTLAYVAPEviTLQGYN----HKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd14027   153 qrevdgtakknAGTLYYMAPE--HLNDVNakptEKSDVYSFAIVLWAIFANKEPY 205
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
1816-2021 2.79e-14

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: 76.67  E-value: 2.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1816 TLYNLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELlrsEISILRLLRHP-----NVIYLKEIINTK 1890
Cdd:cd14227    12 SMTNTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQI---EVSILARLSTEsaddyNFVRAYECFQHK 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1891 ETLYISMELVKGgELYDFLlAETRLSEI---HANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDA-QIKLTDFG 1966
Cdd:cd14227    89 NHTCLVFEMLEQ-NLYDFL-KQNKFSPLplkYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPSRQPyRVKVIDFG 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 124804138 1967 lstlcAPNELLKEPCGTLA----YVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFP 2021
Cdd:cd14227   167 -----SASHVSKAVCSTYLqsryYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYP 220
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
1827-2027 2.92e-14

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros 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: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 75.15  E-value: 2.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINK------QTNSEFAIKVIdKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELV 1900
Cdd:cd05044     3 LGSGAFGEVFEGTAKdilgdgSGETKVAVKTL-RKGATDQEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILELM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAE-------TRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKS-RDAQIKLTDFGLSTLCA 1972
Cdd:cd05044    82 EGGDLLSYLRAArptaftpPLLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSKDyRERVVKIGDFGLARDIY 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1973 PNELL-KEPCGTLA--YVAPEVItLQGY-NHKVDAWSIGIILYLLLS-GKLPFPINKNTE 2027
Cdd:cd05044   162 KNDYYrKEGEGLLPvrWMAPESL-VDGVfTTQSDVWAFGVLMWEILTlGQQPYPARNNLE 220
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
1819-2028 3.09e-14

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 75.19  E-value: 3.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELhEQLGQGKFSTVYRGINKQTNSE-----FAIKVIDKRSVSIYEKELlRSEISILRLLRHPNVIYLKEIINTKETL 1893
Cdd:cd05046     6 NLQEI-TTLGRGEFGEVFLAKAKGIEEEggetlVLVKALQKTKDENLQSEF-RRELDMFRKLSHKNVVRLLGLCREAEPH 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1894 YISMELVKGGELYDFLLAETR---------LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTD 1964
Cdd:cd05046    84 YMILEYTDLGDLKQFLRATKSkdeklkpppLSTKQKVALCTQIALGMDHLSNARFVHRDLAARNCLV---SSQREVKVSL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124804138 1965 FGLSTLCAPNE--LLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFPINKNTEM 2028
Cdd:cd05046   161 LSLSKDVYNSEyyKLRNALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTqGELPFYGLSDEEV 227
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
1826-2028 3.30e-14

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: 74.98  E-value: 3.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1826 QLGQGKFSTVYRGINKQTNSEF--AIKVIDKRSVSIYEKELLRsEISILRLLRHPNVIYLKEIINTkETLYISMELVKGG 1903
Cdd:cd05115    11 ELGSGNFGCVKKGVYKMRKKQIdvAIKVLKQGNEKAVRDEMMR-EAQIMHQLDNPYIVRMIGVCEA-EALMLVMEMASGG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 ELYDFLLAETrlSEIHANKIIT---QLIKTVAYLHRCGIIHRDIKPENILLTDKSrdaQIKLTDFGLS-TLCAPNELLKE 1979
Cdd:cd05115    89 PLNKFLSGKK--DEITVSNVVElmhQVSMGMKYLEEKNFVHRDLAARNVLLVNQH---YAKISDFGLSkALGADDSYYKA 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 124804138 1980 PCG---TLAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFPINKNTEM 2028
Cdd:cd05115   164 RSAgkwPLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSyGQKPYKKMKGPEV 216
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
1895-2021 3.86e-14

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: 75.55  E-value: 3.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYL---HRcgIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLC 1971
Cdd:cd06615    76 ICMEHMDGGSLDQVLKKAGRIPENILGKISIAVLRGLTYLrekHK--IMHRDVKPSNILV---NSRGEIKLCDFGVSGQL 150
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 124804138 1972 ApNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFP 2021
Cdd:cd06615   151 I-DSMANSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPIP 199
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
1820-2032 6.30e-14

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD 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: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 75.02  E-value: 6.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1820 LYELHEQLGQGKFSTVYRgiNKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVI-YLKEIINtKETLYISME 1898
Cdd:cd08216     3 LYEIGKCFKGGGVVHLAK--HKPTNTLVAVKKINLESDSKEDLKFLQQEILTSRQLQHPNILpYVTSFVV-DNDLYVVTP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFLLA--ETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTdfGLSTLC----- 1971
Cdd:cd08216    80 LMAYGSCRDLLKThfPEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILI---SGDGKVVLS--GLRYAYsmvkh 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124804138 1972 -----APNELLKEPCGTLAYVAPEVI--TLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQK 2032
Cdd:cd08216   155 gkrqrVVHDFPKSSEKNLPWLSPEVLqqNLLGYNEKSDIYSVGITACELANGVVPFSDMPATQMLLEK 222
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
1866-2099 7.62e-14

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 76.59  E-value: 7.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1866 RSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGELYDFLLAETR----LSEIHANKIITQLIKTVAYLHRCGIIH 1941
Cdd:PTZ00267  113 RSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQIKQRLKehlpFQEYEVGLLFYQIVLALDEVHSRKMMH 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1942 RDIKPENILLTDKsrdAQIKLTDFGLSTLCAPN---ELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKL 2018
Cdd:PTZ00267  193 RDLKSANIFLMPT---GIIKLGDFGFSKQYSDSvslDVASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHR 269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 2019 PFpiNKNTEMNIQKNYVLSFKDYIWKSISSSAKDLISKLLELNVEKRISANEALEHIWVKNPTAVINE----NSFIYKNE 2094
Cdd:PTZ00267  270 PF--KGPSQREIMQQVLYGKYDPFPCPVSSGMKALLDPLLSKNPALRPTTQQLLHTEFLKYVANLFQDivrhSETISPHD 347

                  ....*
gi 124804138 2095 EINIL 2099
Cdd:PTZ00267  348 REEIL 352
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
1827-2010 7.81e-14

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 73.66  E-value: 7.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKRSvsiYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGELY 1906
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQVMALKMNTLSS---NRANMLR-EVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNLE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1907 DFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCAPNELLKEP---CGT 1983
Cdd:cd14155    77 QLLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDENGYTAVVGDFGLAEKIPDYSDGKEKlavVGS 156
                         170       180
                  ....*....|....*....|....*..
gi 124804138 1984 LAYVAPEVITLQGYNHKVDAWSIGIIL 2010
Cdd:cd14155   157 PYWMAPEVLRGEPYNEKADVFSYGIIL 183
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
1825-2020 8.37e-14

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: 74.28  E-value: 8.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRG------INKQTNSeFAIKVI-DKRSVSIyeKELLRSEISILRLLRHPNVIYLKEIINTKETLYISM 1897
Cdd:cd05091    12 EELGEDRFGKVYKGhlfgtaPGEQTQA-VAIKTLkDKAEGPL--REEFRHEAMLRSRLQHPNIVCLLGVVTKEQPMSMIF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGGELYDFLLAETRLSEIHANK----------------IITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIK 1961
Cdd:cd05091    89 SYCSHGDLHEFLVMRSPHSDVGSTDddktvkstlepadflhIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDK---LNVK 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124804138 1962 LTDFGL-STLCAPN--ELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPF 2020
Cdd:cd05091   166 ISDLGLfREVYAADyyKLMGNSLLPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSyGLQPY 228
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
1827-2028 1.03e-13

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily 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).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 73.85  E-value: 1.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINK---QTNSEFAIKVIdKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGG 1903
Cdd:cd05063    13 IGAGEFGEVFRGILKmpgRKEVAVAIKTL-KPGYTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYMENG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 ELYDFLL-AETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLcapneLLKEPCG 1982
Cdd:cd05063    92 ALDKYLRdHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNS---NLECKVSDFGLSRV-----LEDDPEG 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 124804138 1983 T---------LAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFPINKNTEM 2028
Cdd:cd05063   164 TyttsggkipIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSfGERPYWDMSNHEV 219
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
1821-2016 1.08e-13

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: 74.79  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdKRSVSiYEKELlRSEISILRLLRHP-----NVIYLKEIINTKETLYI 1895
Cdd:cd14211     1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKIL-KNHPS-YARQG-QIEVSILSRLSQEnadefNFVRAYECFQHKNHTCL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1896 SMELVKGgELYDFLlAETRLSEI---HANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDA-QIKLTDFGLSTLC 1971
Cdd:cd14211    78 VFEMLEQ-NLYDFL-KQNKFSPLplkYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVRQPyRVKVIDFGSASHV 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 124804138 1972 ApnellKEPCGTLA----YVAPEVITLQGYNHKVDAWSIGIILYLLLSG 2016
Cdd:cd14211   156 S-----KAVCSTYLqsryYRAPEIILGLPFCEAIDMWSLGCVIAELFLG 199
PH_Ses cd13288
Sesquipedalian family Pleckstrin homology (PH) domain; The sesquipedalian family has 2 ...
1716-1808 1.62e-13

Sesquipedalian family Pleckstrin homology (PH) domain; The sesquipedalian family has 2 mammalian members: Ses1 and Ses2, which are also callled 7 kDa inositol polyphosphate phosphatase-interacting protein 1 and 2. They play a role in endocytic trafficking and are required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane. Members of this family form homodimers and heterodimers. Sesquipedalian interacts with inositol polyphosphate 5-phosphatase OCRL-1 (INPP5F) also known as Lowe oculocerebrorenal syndrome protein, a phosphatase enzyme that is involved in actin polymerization and is found in the trans-Golgi network and INPP5B. Sesquipedalian contains a single 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: 270105 [Multi-domain]  Cd Length: 120  Bit Score: 69.19  E-value: 1.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1716 KEGILYKIGKHLHQFKARYYILFDNLLYYYDKKRNLKPRGFMFLEGCYVELIAKNDninKYGFSICHKGTkqvqKRNLYV 1795
Cdd:cd13288    10 KEGYLWKKGERNTSYQKRWFVLKGNLLFYFEKKGDREPLGVIVLEGCTVELAEDAE---PYAFAIRFDGP----GARSYV 82
                          90
                  ....*....|....*.
gi 124804138 1796 ---NTLEERDEWVQAL 1808
Cdd:cd13288    83 laaENQEDMESWMKAL 98
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
1823-2021 1.67e-13

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET 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: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 73.46  E-value: 1.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1823 LHEQLGQGKFSTVYRGINKQTN-----SEFAIKVIDKRSVSIYEKELLrSEISILRLLRHPNVIYLKEIINTKETLYISM 1897
Cdd:cd05045     4 LGKTLGEGEFGKVVKATAFRLKgragyTTVAVKMLKENASSSELRDLL-SEFNLLKQVNHPHVIKLYGACSQDGPLLLIV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGGELYDFLlAETRLSE----------------------IHANKIIT---QLIKTVAYLHRCGIIHRDIKPENILLT 1952
Cdd:cd05045    83 EYAKYGSLRSFL-RESRKVGpsylgsdgnrnssyldnpderaLTMGDLISfawQISRGMQYLAEMKLVHRDLAARNVLVA 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124804138 1953 DKSRdaqIKLTDFGLS-TLCAPNELLKEPCGTL--AYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFP 2021
Cdd:cd05045   162 EGRK---MKISDFGLSrDVYEEDSYVKRSKGRIpvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYP 231
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
1825-2015 1.67e-13

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: 73.18  E-value: 1.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSE-----FAIKVIdKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMEL 1899
Cdd:cd05048    11 EELGEGAFGKVYKGELLGPSSEesaisVAIKTL-KENASPKTQQDFRREAELMSDLQHPNIVCLLGVCTKEQPQCMLFEY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLAETRLSEIHANK----------------IITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLT 1963
Cdd:cd05048    90 MAHGDLHEFLVRHSPHSDVGVSSdddgtassldqsdflhIAIQIAAGMEYLSSHHYVHRDLAARNCLVGDG---LTVKIS 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 124804138 1964 DFGLSTLCAPNELLKEPCGTLAYV---APEVITLQGYNHKVDAWSIGIILYLLLS 2015
Cdd:cd05048   167 DFGLSRDIYSSDYYRVQSKSLLPVrwmPPEAILYGKFTTESDVWSFGVVLWEIFS 221
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
1867-2017 1.69e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 75.03  E-value: 1.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1867 SEISILRLLRHPNVIYLKEIINTKETLYISMELVKGgELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKP 1946
Cdd:PHA03212  132 TEAHILRAINHPSIIQLKGTFTYNKFTCLILPRYKT-DLYCYLAAKRNIAICDILAIERSVLRAIQYLHENRIIHRDIKA 210
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124804138 1947 ENILLtdkSRDAQIKLTDFGLStlCAPNELLKEP----CGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGK 2017
Cdd:PHA03212  211 ENIFI---NHPGDVCLGDFGAA--CFPVDINANKyygwAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATCH 280
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
1821-2021 1.75e-13

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: 73.91  E-value: 1.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELlrsEISILRLLRHPNV-----IYLKEIINTKETLYI 1895
Cdd:cd14229     2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQGQI---EVGILARLSNENAdefnfVRAYECFQHRNHTCL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1896 SMELVKGgELYDFLlAETRLSEIHAnKIITQLIKTVAY----LHRCGIIHRDIKPENILLTDKSRDA-QIKLTDFGlstl 1970
Cdd:cd14229    79 VFEMLEQ-NLYDFL-KQNKFSPLPL-KVIRPILQQVATalkkLKSLGLIHADLKPENIMLVDPVRQPyRVKVIDFG---- 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 124804138 1971 cAPNELLKEPCGTLA----YVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFP 2021
Cdd:cd14229   152 -SASHVSKTVCSTYLqsryYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYP 205
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
1822-2021 1.96e-13

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 73.15  E-value: 1.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1822 ELHEQLGQGKFSTVYRGINK-----QTNSEFAIKVIDKRSVSIYEKELLrSEISILRLLRHPNVIYLKEIINTKETLYIS 1896
Cdd:cd05032     9 TLIRELGQGSFGMVYEGLAKgvvkgEPETRVAIKTVNENASMRERIEFL-NEASVMKEFNCHHVVRLLGVVSTGQPTLVV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1897 MELVKGGELYDFlLAETRLSEIHANK--IIT---------QLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDF 1965
Cdd:cd05032    88 MELMAKGDLKSY-LRSRRPEAENNPGlgPPTlqkfiqmaaEIADGMAYLAAKKFVHRDLAARNCMV---AEDLTVKIGDF 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1966 GLSTLCAPNELLKEPCGTLAYV---APEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFP 2021
Cdd:cd05032   164 GMTRDIYETDYYRKGGKGLLPVrwmAPESLKDGVFTTKSDVWSFGVVLWEMATlAEQPYQ 223
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
1823-2021 2.01e-13

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 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: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 73.46  E-value: 2.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1823 LHEQLGQGKFSTVYR----GINKQTNSEFAIKVIDKRSVSIYEKEL--LRSEISILRLL-RHPNVIYLKEIINTKETLYI 1895
Cdd:cd05099    16 LGKPLGEGCFGQVVRaeayGIDKSRPDQTVTVAVKMLKDNATDKDLadLISEMELMKLIgKHKNIINLLGVCTQEGPLYV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1896 SMELVKGGELYDFLLAE-----------TRLSE--IHANKIIT---QLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQ 1959
Cdd:cd05099    96 IVEYAAKGNLREFLRARrppgpdytfdiTKVPEeqLSFKDLVScayQVARGMEYLESRRCIHRDLAARNVLVTE---DNV 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124804138 1960 IKLTDFGLSTLCAPNELLKEPCG---TLAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFP 2021
Cdd:cd05099   173 MKIADFGLARGVHDIDYYKKTSNgrlPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTlGGSPYP 238
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
1848-2010 2.29e-13

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 72.67  E-value: 2.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1848 AIKVIDKRSVSIY-EKELLR----------SEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGELYDFLLAETRLS 1916
Cdd:cd14222     9 AIKVTHKATGKVMvMKELIRcdeetqktflTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKDFLRADDPFP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1917 EIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCAPNELLKEP---------------- 1980
Cdd:cd14222    89 WQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLI---KLDKTVVVADFGLSRLIVEEKKKPPPdkpttkkrtlrkndrk 165
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 124804138 1981 -----CGTLAYVAPEVITLQGYNHKVDAWSIGIIL 2010
Cdd:cd14222   166 krytvVGNPYWMAPEMLNGKSYDEKVDIFSFGIVL 200
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
1825-2011 2.53e-13

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 72.69  E-value: 2.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGinKQTNSEFAIKVIDKRSVSIYEKEllrSEISILRLLRHPNVI-YLKEIINTKET---LYISMELV 1900
Cdd:cd14056     1 KTIGKGRYGEVWLG--KYRGEKVAVKIFSSRDEDSWFRE---TEIYQTVMLRHENILgFIAADIKSTGSwtqLWLITEYH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1901 KGGELYDFLLAETrLSEIHANKIITQLIKTVAYLH--------RCGIIHRDIKPENILLtdkSRDAQIKLTDFGLStLCA 1972
Cdd:cd14056    76 EHGSLYDYLQRNT-LDTEEALRLAYSAASGLAHLHteivgtqgKPAIAHRDLKSKNILV---KRDGTCCIADLGLA-VRY 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 124804138 1973 PN--ELLKEP----CGTLAYVAPEVI--TLQGYN----HKVDAWSIGIILY 2011
Cdd:cd14056   151 DSdtNTIDIPpnprVGTKRYMAPEVLddSINPKSfesfKMADIYSFGLVLW 201
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
1825-2027 3.66e-13

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: 71.83  E-value: 3.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGiNKQTNSEFAIKVIDKRSVSiyEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGE 1904
Cdd:cd05113    10 KELGTGQFGVVKYG-KWRGQYDVAIKMIKEGSMS--EDEFIE-EAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLA-ETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLCAPNELLKEpCGT 1983
Cdd:cd05113    86 LLNYLREmRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVND---QGVVKVSDFGLSRYVLDDEYTSS-VGS 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 124804138 1984 ---LAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFPINKNTE 2027
Cdd:cd05113   162 kfpVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPYERFTNSE 209
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
1825-2077 4.36e-13

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: 72.47  E-value: 4.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTN-SEFAIKVIDKRSVSIYEKELLRSEisilRLLR--------------HPNV-------IY 1882
Cdd:cd14013     1 KKLGEGGFGTVYKGSLLQKDpGGEKRRVVLKKAKEYGEVEIWMNE----RVRRacpsscaefvgaflDTTSkkftkpsLW 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1883 LKEIINTKETLYISM----------ELVKGGELYDFLLAETRLSEIhaNKIITQLIKTVAYLHRCGIIHRDIKPENILLT 1952
Cdd:cd14013    77 LVWKYEGDATLADLMqgkefpynlePIIFGRVLIPPRGPKRENVII--KSIMRQILVALRKLHSTGIVHRDVKPQNIIVS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1953 DKSRdaQIKLTDFGLST-LCA-----PNELLKEPcgtlAYVAPE----------------------VITLQGYNHKVDAW 2004
Cdd:cd14013   155 EGDG--QFKIIDLGAAAdLRIginyiPKEFLLDP----RYAPPEqyimstqtpsappapvaaalspVLWQMNLPDRFDMY 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 2005 SIGIILYlllsgKLPFPINKNTEMNIQKNYVLSFKDY---IWKS-----ISSSAK--------------DLISKLLELNV 2062
Cdd:cd14013   229 SAGVILL-----QMAFPNLRSDSNLIAFNRQLKQCDYdlnAWRMlveprASADLRegfeildlddgagwDLVTKLIRYKP 303
                         330
                  ....*....|....*
gi 124804138 2063 EKRISANEALEHIWV 2077
Cdd:cd14013   304 RGRLSASAALAHPYF 318
pknD PRK13184
serine/threonine-protein kinase PknD;
1821-2020 4.48e-13

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 75.19  E-value: 4.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKrsvSIYEKELLRS----EISILRLLRHPNVIYLKEIINTKETLYIS 1896
Cdd:PRK13184    4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIRE---DLSENPLLKKrflrEAKIAADLIHPGIVPVYSICSDGDPVYYT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1897 MELVKGGELYDfLLAETR----LSEIHANK--------IITQLIKTVAYLHRCGIIHRDIKPENILL------------- 1951
Cdd:PRK13184   81 MPYIEGYTLKS-LLKSVWqkesLSKELAEKtsvgaflsIFHKICATIEYVHSKGVLHRDLKPDNILLglfgevvildwga 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124804138 1952 -------TDKSRDAQIKLTDFGLSTLCAPNELLkepcGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:PRK13184  160 aifkkleEEDLLDIDVDERNICYSSMTIPGKIV----GTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPY 231
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
1825-2015 4.50e-13

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 71.98  E-value: 4.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGinKQTNSEFAIKVI---DKRSvsiYEKELlrsEISILRLLRHPNVIY----LKEIINTKETLYISM 1897
Cdd:cd14053     1 EIKARGRFGAVWKA--QYLNRLVAVKIFplqEKQS---WLTER---EIYSLPGMKHENILQfigaEKHGESLEAEYWLIT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGGELYDFLLAETrLSEIHANKIITQLIKTVAYLH------RCG----IIHRDIKPENILLTDksrDAQIKLTDFGL 1967
Cdd:cd14053    73 EFHERGSLCDYLKGNV-ISWNELCKIAESMARGLAYLHedipatNGGhkpsIAHRDFKSKNVLLKS---DLTACIADFGL 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 124804138 1968 STLCAPNELLKEP---CGTLAYVAPEVitLQG-YNHKVDA------WSIGIILYLLLS 2015
Cdd:cd14053   149 ALKFEPGKSCGDThgqVGTRRYMAPEV--LEGaINFTRDAflridmYAMGLVLWELLS 204
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
1827-2060 5.23e-13

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: 71.76  E-value: 5.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNseFAIKVIDKRSVSIYE--KELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGE 1904
Cdd:cd14158    23 LGEGGFGVVFKGYINDKN--VAVKKLAAMVDISTEdlTKQFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMPNGS 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFL--LAET-RLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLCAPNEL---LK 1978
Cdd:cd14158   101 LLDRLacLNDTpPLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLDET---FVPKISDFGLARASEKFSQtimTE 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1979 EPCGTLAYVAPEviTLQG-YNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQ-----KNYVLSFKDYIWKSISSSAKD 2052
Cdd:cd14158   178 RIVGTTAYMAPE--ALRGeITPKSDIFSFGVVLLEIITGLPPVDENRDPQLLLDikeeiEDEEKTIEDYVDKKMGDWDST 255

                  ....*...
gi 124804138 2053 LISKLLEL 2060
Cdd:cd14158   256 SIEAMYSV 263
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
1827-2020 5.67e-13

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR 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: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 72.36  E-value: 5.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGI----NKQTNSEFAIKVIDKRSVSIYEKELLrSEISILRLLRHPNVIYLKEIINTkETLYISMELVKG 1902
Cdd:cd05108    15 LGSGAFGTVYKGLwipeGEKVKIPVAIKELREATSPKANKEIL-DEAYVMASVDNPHVCRLLGICLT-STVQLITQLMPF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1903 GELYDFLLA-ETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSrdaQIKLTDFGLSTLCAPNELLKEPC 1981
Cdd:cd05108    93 GCLLDYVREhKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQ---HVKITDFGLAKLLGAEEKEYHAE 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 124804138 1982 G---TLAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPF 2020
Cdd:cd05108   170 GgkvPIKWMALESILHRIYTHQSDVWSYGVTVWELMTfGSKPY 212
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
1825-2015 8.37e-13

Catalytic domain of Transforming Growth Factor beta Receptor-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 receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-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: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 71.32  E-value: 8.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGinKQTNSEFAIKVIDKRsvsiyEKELLRSEISILR--LLRHPNVIYL----KEIINTKETLYISME 1898
Cdd:cd13998     1 EVIGKGRFGEVWKA--SLKNEPVAVKIFSSR-----DKQSWFREKEIYRtpMLKHENILQFiaadERDTALRTELWLVTA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFLLAETrLSEIHANKIITQLIKTVAYLH----RCG-----IIHRDIKPENILLtdkSRDAQIKLTDFGLST 1969
Cdd:cd13998    74 FHPNGSL*DYLSLHT-IDWVSLCRLALSVARGLAHLHseipGCTqgkpaIAHRDLKSKNILV---KNDGTCCIADFGLAV 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 124804138 1970 LCAPN--ELLKEP---CGTLAYVAPEV----ITLQGYNH--KVDAWSIGIILYLLLS 2015
Cdd:cd13998   150 RLSPStgEEDNANngqVGTKRYMAPEVlegaINLRDFESfkRVDIYAMGLVLWEMAS 206
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
1816-2021 8.90e-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: 72.04  E-value: 8.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1816 TLYNLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELlrsEISILRLLRHPNV-----IYLKEIINTK 1890
Cdd:cd14228    12 SMTNSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQI---EVSILSRLSSENAdeynfVRSYECFQHK 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1891 ETLYISMELVKGgELYDFLlAETRLSEI---HANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDA-QIKLTDFG 1966
Cdd:cd14228    89 NHTCLVFEMLEQ-NLYDFL-KQNKFSPLplkYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPVRQPyRVKVIDFG 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 124804138 1967 lstlcAPNELLKEPCGTLA----YVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFP 2021
Cdd:cd14228   167 -----SASHVSKAVCSTYLqsryYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYP 220
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
1825-2028 1.00e-12

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: 70.66  E-value: 1.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGiNKQTNSEFAIKVIdkRSVSIYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGE 1904
Cdd:cd05114    10 KELGSGLFGVVRLG-KWRAQYKVAIKAI--REGAMSEEDFIE-EAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENGC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAET-RLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLCAPNELLKEpCGT 1983
Cdd:cd05114    86 LLNYLRQRRgKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDT---GVVKVSDFGMTRYVLDDQYTSS-SGA 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 124804138 1984 ---LAYVAPEVITLQGYNHKVDAWSIGIILY-LLLSGKLPFPINKNTEM 2028
Cdd:cd05114   162 kfpVKWSPPEVFNYSKFSSKSDVWSFGVLMWeVFTEGKMPFESKSNYEV 210
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
1826-2015 2.34e-12

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: 69.92  E-value: 2.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1826 QLGQGKFSTV----YRGINKQTNSEFAIKVIDKRSVSiyEKELLRSEISILRLLRHPNVIYLKEIINT--KETLYISMEL 1899
Cdd:cd05081    11 QLGKGNFGSVelcrYDPLGDNTGALVAVKQLQHSGPD--QQRDFQREIQILKALHSDFIVKYRGVSYGpgRRSLRLVMEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1900 VKGGELYDFLLA-ETRLSEIHANKIITQLIKTVAYL--HRCgiIHRDIKPENILLTDKsrdAQIKLTDFGLSTLCAPNE- 1975
Cdd:cd05081    89 LPSGCLRDFLQRhRARLDASRLLLYSSQICKGMEYLgsRRC--VHRDLAARNILVESE---AHVKIADFGLAKLLPLDKd 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 124804138 1976 --LLKEPCGT-LAYVAPEVITLQGYNHKVDAWSIGIILYLLLS 2015
Cdd:cd05081   164 yyVVREPGQSpIFWYAPESLSDNIFSRQSDVWSFGVVLYELFT 206
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
1821-2028 2.36e-12

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They 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. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. 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 serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 69.43  E-value: 2.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFA------IKVIDKRSVSIYEkELLRSeISILRLLRHPNVIYLKEIINTKETLy 1894
Cdd:cd05037     1 ITFHEHLGQGTFTNIYDGILREVGDGRVqevevlLKVLDSDHRDISE-SFFET-ASLMSQISHKHLVKLYGVCVADENI- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1895 ISMELVKGGELYDFLLAETRLSEIHAN-KIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQ---IKLTDFGLSTL 1970
Cdd:cd05037    78 MVQEYVRYGPLDKYLRRMGNNVPLSWKlQVAKQLASALHYLEDKKLIHGNVRGRNILLAREGLDGYppfIKLSDPGVPIT 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124804138 1971 CAPNELLKEPcgtLAYVAPEVI--TLQGYNHKVDAWSIGIILYLLLS-GKLPFPINKNTEM 2028
Cdd:cd05037   158 VLSREERVDR---IPWIAPECLrnLQANLTIAADKWSFGTTLWEICSgGEEPLSALSSQEK 215
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
1822-2074 2.50e-12

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: 69.67  E-value: 2.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1822 ELHE--QLGQGKFSTVYRGINKQTNSEFAIKVIDKR-SVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISME 1898
Cdd:cd14138     6 EFHEleKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPlAGSVDEQNALREVYAHAVLGQHSHVVRYYSAWAEDDHMLIQNE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFLLAETR----LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDK----------------SRDA 1958
Cdd:cd14138    86 YCNGGSLADAISENYRimsyFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRTsipnaaseegdedewaSNKV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1959 QIKLTDFG-LSTLCAPNelLKEpcGTLAYVAPEVITlQGYNH--KVDAWSIGIILyLLLSGKLPFPINKNTEMNIQKNYV 2035
Cdd:cd14138   166 IFKIGDLGhVTRVSSPQ--VEE--GDSRFLANEVLQ-ENYTHlpKADIFALALTV-VCAAGAEPLPTNGDQWHEIRQGKL 239
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 124804138 2036 lsfkDYIWKSISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd14138   240 ----PRIPQVLSQEFLDLLKVMIHPDPERRPSAVALVKH 274
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
1826-2020 3.29e-12

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. 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 CDC2L6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 70.10  E-value: 3.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1826 QLGQGKFSTVYRGINK--QTNSEFAIKVIDKRSVSIYEKEllrsEISILRLLRHPNVIYLKEIintketlYISMELVKGG 1903
Cdd:cd07867     9 KVGRGTYGHVYKAKRKdgKDEKEYALKQIEGTGISMSACR----EIALLRELKHPNVIALQKV-------FLSHSDRKVW 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 ELYDFllAETRLSEI-------HANK------------IITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRD-AQIKLT 1963
Cdd:cd07867    78 LLFDY--AEHDLWHIikfhrasKANKkpmqlprsmvksLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPErGRVKIA 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124804138 1964 DFGLSTL----CAPNELLKEPCGTLAYVAPEVIT-LQGYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd07867   156 DMGFARLfnspLKPLADLDPVVVTFWYRAPELLLgARHYTKAIDIWAIGCIFAELLTSEPIF 217
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
1821-2027 3.85e-12

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: 70.05  E-value: 3.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGIN-KQTNSEFAIKVIdkRSVSIYeKELLRSEISILRLLRHPN------VIYLKEIINTKETL 1893
Cdd:cd14215    14 YEIVSTLGEGTFGRVVQCIDhRRGGARVALKII--KNVEKY-KEAARLEINVLEKINEKDpenknlCVQMFDWFDYHGHM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1894 YISMELVkGGELYDFLLAETRLS-EIH-ANKIITQLIKTVAYLHRCGIIHRDIKPENILLT----------DKSRDAQ-- 1959
Cdd:cd14215    91 CISFELL-GLSTFDFLKENNYLPyPIHqVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVnsdyeltynlEKKRDERsv 169
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124804138 1960 ----IKLTDFGLSTLcaPNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTE 2027
Cdd:cd14215   170 kstaIRVVDFGSATF--DHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNRE 239
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
1827-2010 3.95e-12

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 68.83  E-value: 3.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGINKQTNSEFAIKVIDKrsvsiYEKELLRS---EISILRLLRHPNVIYLKEIINTKETLYISMELVKGG 1903
Cdd:cd14221     1 LGKGCFGQAIKVTHRETGEVMVMKELIR-----FDEETQRTflkEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 ELYDFLLA-ETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTL-----CAPNEL- 1976
Cdd:cd14221    76 TLRGIIKSmDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRE---NKSVVVADFGLARLmvdekTQPEGLr 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 124804138 1977 -LKEP--------CGTLAYVAPEVITLQGYNHKVDAWSIGIIL 2010
Cdd:cd14221   153 sLKKPdrkkrytvVGNPYWMAPEMINGRSYDEKVDVFSFGIVL 195
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
1841-2032 4.01e-12

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha, stabilized through ATP and MO25, may be needed to activate LKB1. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. The STRAD alpha 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: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 69.97  E-value: 4.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1841 KQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGELYDFLLAETR--LSEI 1918
Cdd:cd08227    22 KPTGEYVTVRRINLEACTNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMdgMSEL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1919 HANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTdfGLSTLCA----------PNELLKEPCGTLAYVA 1988
Cdd:cd08227   102 AIAYILQGVLKALDYIHHMGYVHRSVKASHILI---SVDGKVYLS--GLRSNLSminhgqrlrvVHDFPKYSVKVLPWLS 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 124804138 1989 PEVI--TLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQK 2032
Cdd:cd08227   177 PEVLqqNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEK 222
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
1821-2077 4.03e-12

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: 70.06  E-value: 4.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdkRSVSIYEKELLrSEISILRLLRH-----PN---VIYLKE--IINTK 1890
Cdd:cd14216    12 YHVIRKLGWGHFSTVWLSWDIQGKRFVAMKVV--KSAEHYTETAL-DEIKLLKSVRNsdpndPNremVVQLLDdfKISGV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1891 ETLYISMEL-VKGGELYDFLLAETR--LSEIHANKIITQLIKTVAYLH-RCGIIHRDIKPENILLT-------------- 1952
Cdd:cd14216    89 NGTHICMVFeVLGHHLLKWIIKSNYqgLPLPCVKKIIRQVLQGLDYLHtKCRIIHTDIKPENILLSvneqyirrlaaeat 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1953 -------------DKSRDAQIKLTDFGlsTLCAPNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLP 2019
Cdd:cd14216   169 ewqrnflvnplepKNAEKLKVKIADLG--NACWVHKHFTEDIQTRQYRSLEVLIGSGYNTPADIWSTACMAFELATGDYL 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 2020 FPINKNTEMN---------------IQKNYVLSFK-----------------------------DYIW-KSISSSAKDLI 2054
Cdd:cd14216   247 FEPHSGEDYSrdedhialiiellgkVPRKLIVAGKyskefftkkgdlkhitklkpwglfevlveKYEWsQEEAAGFTDFL 326
                         330       340
                  ....*....|....*....|...
gi 124804138 2055 SKLLELNVEKRISANEALEHIWV 2077
Cdd:cd14216   327 LPMLELIPEKRATAAECLRHPWL 349
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
1825-2019 5.29e-12

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: 68.97  E-value: 5.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYR----GINKQTNSEFAIKVIDKR----SVSIYEKELlRSEISILRLLRHPNVIYLKEIINTKE-TLYI 1895
Cdd:cd14001     5 KKLGYGTGVNVYLmkrsPRGGSSRSPWAVKKINSKcdkgQRSLYQERL-KEEAKILKSLNHPNIVGFRAFTKSEDgSLCL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1896 SMElvKGGE-LYDFLLA--ETRLSEIHANKIIT---QLIKTVAYLHR-CGIIHRDIKPENILLtdKSRDAQIKLTDFGLS 1968
Cdd:cd14001    84 AME--YGGKsLNDLIEEryEAGLGPFPAATILKvalSIARALEYLHNeKKILHGDIKSGNVLI--KGDFESVKLCDFGVS 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 124804138 1969 -TLCAPNELLKEP----CGTLAYVAPEVITLQG-YNHKVDAWSIGIILYLLLSGKLP 2019
Cdd:cd14001   160 lPLTENLEVDSDPkaqyVGTEPWKAKEALEEGGvITDKADIFAYGLVLWEMMTLSVP 216
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
1827-2020 6.19e-12

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 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: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 68.51  E-value: 6.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGI----NKQTNSEFAIKVIDKRSVSIYEKELLrSEISILRLLRHPNVIYLKEIINTkETLYISMELVKG 1902
Cdd:cd05109    15 LGSGAFGTVYKGIwipdGENVKIPVAIKVLRENTSPKANKEIL-DEAYVMAGVGSPYVCRLLGICLT-STVQLVTQLMPY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1903 GELYDFLLA-ETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSrdaQIKLTDFGLSTLCAPNELLKEPC 1981
Cdd:cd05109    93 GCLLDYVREnKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPN---HVKITDFGLARLLDIDETEYHAD 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 124804138 1982 G---TLAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPF 2020
Cdd:cd05109   170 GgkvPIKWMALESILHRRFTHQSDVWSYGVTVWELMTfGAKPY 212
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
1819-2028 8.00e-12

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer 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: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 68.42  E-value: 8.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1819 NLYELHEQLGQGKFSTVYRGINKQ---TNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYI 1895
Cdd:cd14204     7 NLLSLGKVLGEGEFGSVMEGELQQpdgTNHKVAVKTMKLDNFSQREIEEFLSEAACMKDFNHPNVIRLLGVCLEVGSQRI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1896 SMELV-----KGGELYDFLLaETRLSEIHANKIITQLIK-------TVAYLHRCGIIHRDIKPENILLTDksrDAQIKLT 1963
Cdd:cd14204    87 PKPMVilpfmKYGDLHSFLL-RSRLGSGPQHVPLQTLLKfmidialGMEYLSSRNFLHRDLAARNCMLRD---DMTVCVA 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124804138 1964 DFGLSTLCAPNELLKEpcGTLA-----YVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFPINKNTEM 2028
Cdd:cd14204   163 DFGLSKKIYSGDYYRQ--GRIAkmpvkWIAVESLADRVYTVKSDVWAFGVTMWEIATrGMTPYPGVQNHEI 231
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
1715-1813 8.18e-12

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: 63.72  E-value: 8.18e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138   1715 LKEGILYKIGK-HLHQFKARYYILFDNLLYYYDKK---RNLKPRGFMFLEGCYVELIAKNDNIN-KYGFSICHKGTKQVq 1789
Cdd:smart00233    2 IKEGWLYKKSGgGKKSWKKRYFVLFNSTLLYYKSKkdkKSYKPKGSIDLSGCTVREAPDPDSSKkPHCFEIKTSDRKTL- 80
                            90       100
                    ....*....|....*....|....
gi 124804138   1790 krNLYVNTLEERDEWVQALYSSTK 1813
Cdd:smart00233   81 --LLQAESEEEREKWVEALRKAIA 102
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
1923-2051 9.02e-12

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: 67.90  E-value: 9.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1923 IITQLIKTVAYLHRCGIIHRDIKPENILLtDKSRDAqiKLTDFGlstLCAPNELLK-EPCGTLAYVAPEVITLQgYNHKV 2001
Cdd:cd13975   107 IALDVVEGIRFLHSQGLVHRDIKLKNVLL-DKKNRA--KITDLG---FCKPEAMMSgSIVGTPIHMAPELFSGK-YDNSV 179
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 124804138 2002 DAWSIGIILYLLLSG--KLPFPINKntemniqknyvLSFKDYIWKSISSSAK 2051
Cdd:cd13975   180 DVYAFGILFWYLCAGhvKLPEAFEQ-----------CASKDHLWNNVRKGVR 220
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
1808-2020 9.64e-12

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 67.86  E-value: 9.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1808 LYSSTKQNTLYNLyeLHEqlgqGKFSTVYRGINKQTNS---EFAIKVIdKRSVSIYEKELLRSEISILRLLRHPNVIYLK 1884
Cdd:cd05043     1 IAVSRERVTLSDL--LQE----GTFGRIFHGILRDEKGkeeEVLVKTV-KDHASEIQVTMLLQESSLLYGLSHQNLLPIL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1885 EI-INTKETLYISMELVKGGELYDFLlAETRLSEIHANKIIT---------QLIKTVAYLHRCGIIHRDIKPENILLTDK 1954
Cdd:cd05043    74 HVcIEDGEKPMVLYPYMNWGNLKLFL-QQCRLSEANNPQALStqqlvhmalQIACGMSYLHRRGVIHKDIAARNCVIDDE 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1955 SrdaQIKLTDFGLSTLCAPNE---LLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPF 2020
Cdd:cd05043   153 L---QVKITDNALSRDLFPMDyhcLGDNENRPIKWMSLESLVNKEYSSASDVWSFGVLLWELMTlGQTPY 219
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
1820-2037 1.20e-11

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 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: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 67.64  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1820 LYELHEQLGQGKFSTVYRGINKQTNSEF---AIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEII---NTKETL 1893
Cdd:cd05074    10 QFTLGRMLGKGEFGSVREAQLKSEDGSFqkvAVKMLKADIFSSSDIEEFLREAACMKEFDHPNVIKLIGVSlrsRAKGRL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1894 YISM---ELVKGGELYDFLLAeTRLSEIHANKIITQLIK-------TVAYLHRCGIIHRDIKPENILLTDksrDAQIKLT 1963
Cdd:cd05074    90 PIPMvilPFMKHGDLHTFLLM-SRIGEEPFTLPLQTLVRfmidiasGMEYLSSKNFIHRDLAARNCMLNE---NMTVCVA 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124804138 1964 DFGLSTLCAPNELLKEPCGT---LAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFPINKNTEMniqKNYVLS 2037
Cdd:cd05074   166 DFGLSKKIYSGDYYRQGCASklpVKWLALESLADNVYTTHSDVWAFGVTMWEIMTrGQTPYAGVENSEI---YNYLIK 240
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
1823-2028 1.39e-11

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl 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: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 67.34  E-value: 1.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1823 LHEQLGQGKFSTVYRGINKQTNS--EFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEII--NTKETLYIS-- 1896
Cdd:cd05075     4 LGKTLGEGEFGSVMEGQLNQDDSvlKVAVKTMKIAICTRSEMEDFLSEAVCMKEFDHPNVMRLIGVClqNTESEGYPSpv 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1897 --MELVKGGELYDFLLAeTRLSEIHAN-------KIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLTDFGL 1967
Cdd:cd05075    84 viLPFMKHGDLHSFLLY-SRLGDCPVYlptqmlvKFMTDIASGMEYLSSKNFIHRDLAARNCMLNE---NMNVCVADFGL 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124804138 1968 STLCAPNELLKEpcGTLA-----YVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFPINKNTEM 2028
Cdd:cd05075   160 SKKIYNGDYYRQ--GRISkmpvkWIAIESLADRVYTTKSDVWSFGVTMWEIATrGQTPYPGVENSEI 224
PH pfam00169
PH domain; PH stands for pleckstrin homology.
1716-1813 1.53e-11

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 62.97  E-value: 1.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138  1716 KEGILYKIGKHLH-QFKARYYILFDNLLYYYDKK---RNLKPRGFMFLEGCYVELIAKNDNIN-KYGFSICHKGTKQVQK 1790
Cdd:pfam00169    3 KEGWLLKKGGGKKkSWKKRYFVLFDGSLLYYKDDksgKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTGKRT 82
                           90       100
                   ....*....|....*....|...
gi 124804138  1791 RNLYVNTLEERDEWVQALYSSTK 1813
Cdd:pfam00169   83 YLLQAESEEERKDWIKAIQSAIR 105
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
1825-2015 2.05e-11

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: 67.23  E-value: 2.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTV----YRGINKQTNSEFAIKVIdKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTK--ETLYISME 1898
Cdd:cd05080    10 RDLGEGHFGKVslycYDPTNDGTGEMVAVKAL-KADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQggKSLQLIME 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1899 LVKGGELYDFLlAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCAPNELL- 1977
Cdd:cd05080    89 YVPLGSLRDYL-PKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLL---DNDRLVKIGDFGLAKAVPEGHEYy 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 124804138 1978 ---KEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLS 2015
Cdd:cd05080   165 rvrEDGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLT 205
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
1823-2028 2.57e-11

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM 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: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 66.79  E-value: 2.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1823 LHEQLGQGKFSTVYRGINKQTNSEF---AIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETL------ 1893
Cdd:cd05035     3 LGKILGEGEFGSVMEAQLKQDDGSQlkvAVKTMKVDIHTYSEIEEFLSEAACMKDFDHPNVMRLIGVCFTASDLnkppsp 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1894 YISMELVKGGELYDFLLAeTRLSEIHANKIITQLIKTVA-------YLHRCGIIHRDIKPENILLTDksrDAQIKLTDFG 1966
Cdd:cd05035    83 MVILPFMKHGDLHSYLLY-SRLGGLPEKLPLQTLLKFMVdiakgmeYLSNRNFIHRDLAARNCMLDE---NMTVCVADFG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124804138 1967 LSTLCAPNELLKEPCGT---LAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFPINKNTEM 2028
Cdd:cd05035   159 LSRKIYSGDYYRQGRISkmpVKWIALESLADNVYTSKSDVWSFGVTMWEIATrGQTPYPGVENHEI 224
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
1827-2016 2.64e-11

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. 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 (a pseudokinase in the case of IRAK3), 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. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 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: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 66.45  E-value: 2.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGinKQTNSEFAIKVIDKRSVSIYEK--ELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGE 1904
Cdd:cd14160     1 IGEGEIFEVYRV--RIGNRSYAVKLFKQEKKMQWKKhwKRFLSELEVLLLFQHPNILELAAYFTETEKFCLVYPYMQNGT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFL---LAETRLSEIHANKIITQLIKTVAYLHR---CGIIHRDIKPENILLTDKsrdAQIKLTDFGLSTLcAPNeLLK 1978
Cdd:cd14160    79 LFDRLqchGVTKPLSWHERINILIGIAKAIHYLHNsqpCTVICGNISSANILLDDQ---MQPKLTDFALAHF-RPH-LED 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 124804138 1979 EPC---------GTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSG 2016
Cdd:cd14160   154 QSCtinmttalhKHLWYMPEEYIRQGKLSVKTDVYSFGIVIMEVLTG 200
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
1868-2011 2.66e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 68.38  E-value: 2.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1868 EISILRLLRHPNVIYLkeiintketlyISMELVKG----------GELYDFLLAETR-LSEIHANKIITQLIKTVAYLHR 1936
Cdd:PHA03211  210 EARLLRRLSHPAVLAL-----------LDVRVVGGltclvlpkyrSDLYTYLGARLRpLGLAQVTAVARQLLSAIDYIHG 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1937 CGIIHRDIKPENILLTDKSrdaQIKLTDFGLStlCAPNELLKEP-----CGTLAYVAPEVITLQGYNHKVDAWSIGIILY 2011
Cdd:PHA03211  279 EGIIHRDIKTENVLVNGPE---DICLGDFGAA--CFARGSWSTPfhygiAGTVDTNAPEVLAGDPYTPSVDIWSAGLVIF 353
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
1874-2071 3.75e-11

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: 66.75  E-value: 3.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1874 LLRHPNVIYLK---EIINTKETLYISMELvkggelYDF----LLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKP 1946
Cdd:cd14018    93 IEDYPDVLPARlnpSGLGHNRTLFLVMKN------YPCtlrqYLWVNTPSYRLARVMILQLLEGVDHLVRHGIAHRDLKS 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1947 ENILLT-DKSRDAQIKLTDFGLSTLCAPNElLKEPC--------GTLAYVAPEVIT-LQGYN-----HKVDAWSIGIILY 2011
Cdd:cd14018   167 DNILLElDFDGCPWLVIADFGCCLADDSIG-LQLPFsswyvdrgGNACLMAPEVSTaVPGPGvvinySKADAWAVGAIAY 245
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 2012 LLLSGKLPFPINKNTeMNIQKNYVLSFKDYIWKSISSSAKDLISKLLELNVEKRISANEA 2071
Cdd:cd14018   246 EIFGLSNPFYGLGDT-MLESRSYQESQLPALPSAVPPDVRQVVKDLLQRDPNKRVSARVA 304
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
1822-2016 4.21e-11

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. Jaks 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 Jak3 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: 271110 [Multi-domain]  Cd Length: 260  Bit Score: 65.70  E-value: 4.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1822 ELHEQLGQGKFSTVYRGINKQT------NSEFAIKVIDKRSVSIYEKELlrSEISILRLLRHPNVIYLKEIINTKETLYI 1895
Cdd:cd14208     2 TFMESLGKGSFTKIYRGLRTDEeddercETEVLLKVMDPTHGNCQESFL--EAASIMSQISHKHLVLLHGVCVGKDSIMV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1896 SmELVKGGELYDFLLAETRLSEIHAN---KIITQLIKTVAYLHRCGIIHRDIKPENILLT---DKSRDAQIKLTDFGLST 1969
Cdd:cd14208    80 Q-EFVCHGALDLYLKKQQQKGPVAISwklQVVKQLAYALNYLEDKQLVHGNVSAKKVLLSregDKGSPPFIKLSDPGVSI 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 124804138 1970 LCAPNELLKEpcgTLAYVAPEVIT-LQGYNHKVDAWSIGIILYLLLSG 2016
Cdd:cd14208   159 KVLDEELLAE---RIPWVAPECLSdPQNLALEADKWGFGATLWEIFSG 203
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
1811-2020 4.45e-11

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: 66.62  E-value: 4.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1811 STKQNTLYNLYELHE-QLGQGKFSTVYRGINK--QTNSEFAIKVIDKRSVSIYEKEllrsEISILRLLRHPNVIYLKEIi 1887
Cdd:cd07868     8 TGERERVEDLFEYEGcKVGRGTYGHVYKAKRKdgKDDKDYALKQIEGTGISMSACR----EIALLRELKHPNVISLQKV- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1888 ntketlYISMELVKGGELYDFllAETRLSEI-------HANK------------IITQLIKTVAYLHRCGIIHRDIKPEN 1948
Cdd:cd07868    83 ------FLSHADRKVWLLFDY--AEHDLWHIikfhrasKANKkpvqlprgmvksLLYQILDGIHYLHANWVLHRDLKPAN 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124804138 1949 ILLTDKSRD-AQIKLTDFGLSTL----CAPNELLKEPCGTLAYVAPEVIT-LQGYNHKVDAWSIGIILYLLLSGKLPF 2020
Cdd:cd07868   155 ILVMGEGPErGRVKIADMGFARLfnspLKPLADLDPVVVTFWYRAPELLLgARHYTKAIDIWAIGCIFAELLTSEPIF 232
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
1823-2027 4.50e-11

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk 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: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 65.95  E-value: 4.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1823 LHEQLGQGKFSTVYRG-----INKQTNSEFAIKVIDKRSVSIYEKELLRsEISILRLLRHPNVIYLKEIINTKETLYISM 1897
Cdd:cd05049     9 LKRELGEGAFGKVFLGecynlEPEQDKMLVAVKTLKDASSPDARKDFER-EAELLTNLQHENIVKFYGVCTEGDPLLMVF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1898 ELVKGGELYDFL--------------LAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDksrDAQIKLT 1963
Cdd:cd05049    88 EYMEHGDLNKFLrshgpdaaflasedSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGT---NLVVKIG 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124804138 1964 DFGLSTLCAPNELLKEPCGTL---AYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFPINKNTE 2027
Cdd:cd05049   165 DFGMSRDIYSTDYYRVGGHTMlpiRWMPPESILYRKFTTESDVWSFGVVLWEIFTyGKQPWFQLSNTE 232
Kinase-like pfam14531
Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. ...
1903-2065 4.59e-11

Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. These proteins have a typical bilobed protein kinase fold, but lack catalytic actvity.


Pssm-ID: 405254 [Multi-domain]  Cd Length: 288  Bit Score: 65.98  E-value: 4.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138  1903 GELYDFLLAETRLSEIHANKIIT-QLIKTVAYLHRCGIIHRDIKPENILLTDKSRdaqIKLTDFG----------LSTLC 1971
Cdd:pfam14531  128 GEVLLSHSSTHKSLVHHARLQLTlQLIRLAANLQHYGLVHGQFTVDNFFLDQRGG---VFLGGFEhlvrdgtkvvASEVP 204
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138  1972 ---APNELlkepCGTLAYVAPEVITLqgYNHKVDAWSIGIILYLLLSGKLPFPInkntemnIQKNYVLSFKDYIWKSISS 2048
Cdd:pfam14531  205 rgfAPPEL----LGSRGGYTMKNTTL--MTHAFDAWQLGLVIYWIWCLDLPNTL-------DAEEGGIEWKFRLCKNIPE 271
                          170
                   ....*....|....*..
gi 124804138  2049 SAKDLISKLLELNVEKR 2065
Cdd:pfam14531  272 PVRALLKGFLNYSQEDR 288
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
1827-2020 4.67e-11

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA 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: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 65.66  E-value: 4.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGinkqtnsefAIKVIDKRSVSIYEKEL-----------LRSEISILRLLRHPNVIYLKEIINTKETLYI 1895
Cdd:cd05066    12 IGAGEFGEVCSG---------RLKLPGKREIPVAIKTLkagytekqrrdFLSEASIMGQFDHPNIIHLEGVVTRSKPVMI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1896 SMELVKGGELYDFLLA-ETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdkSRDAQIKLTDFGLSTLCA-- 1972
Cdd:cd05066    83 VTEYMENGSLDAFLRKhDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILV---NSNLVCKVSDFGLSRVLEdd 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 124804138 1973 PNELLKEPCGTLA--YVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPF 2020
Cdd:cd05066   160 PEAAYTTRGGKIPirWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPY 210
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
1825-2074 4.99e-11

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: 65.72  E-value: 4.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLL-RHPNVIYLKEIINTKETLYISMELVKGG 1903
Cdd:cd14139     6 EKIGVGEFGSVYKCIKRLDGCVYAIKRSMRPFAGSSNEQLALHEVYAHAVLgHHPHVVRYYSAWAEDDHMIIQNEYCNGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1904 ELYDFLLAETRL----SEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDK-------------------SRDAQI 1960
Cdd:cd14139    86 SLQDAISENTKSgnhfEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFICHKmqsssgvgeevsneedeflSANVVY 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1961 KLTDFGLSTlCAPNELLKEpcGTLAYVAPEVITLQgYNH--KVDAWSIGIILyLLLSGKLPFPINKNTEMNIQKNYVLSf 2038
Cdd:cd14139   166 KIGDLGHVT-SINKPQVEE--GDSRFLANEILQED-YRHlpKADIFALGLTV-ALAAGAEPLPTNGAAWHHIRKGNFPD- 239
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 124804138 2039 kdyIWKSISSSAKDLISKLLELNVEKRISANEALEH 2074
Cdd:cd14139   240 ---VPQELPESFSSLLKNMIQPDPEQRPSATALARH 272
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
1823-2021 5.29e-11

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 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: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 66.19  E-value: 5.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1823 LHEQLGQGKFSTVYR----GINKQTNSEFAIKVIDKRSVSIYEKEL--LRSEISILRLL-RHPNVIYLKEIINTKETLYI 1895
Cdd:cd05101    28 LGKPLGEGCFGQVVMaeavGIDKDKPKEAVTVAVKMLKDDATEKDLsdLVSEMEMMKMIgKHKNIINLLGACTQDGPLYV 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1896 SMELVKGGELYDFLLAE-----------TRLSE--IHANKIIT---QLIKTVAYLHRCGIIHRDIKPENILLTDKSrdaQ 1959
Cdd:cd05101   108 IVEYASKGNLREYLRARrppgmeysydiNRVPEeqMTFKDLVSctyQLARGMEYLASQKCIHRDLAARNVLVTENN---V 184
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124804138 1960 IKLTDFGLSTLCAPNELLKEPCG---TLAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPFP 2021
Cdd:cd05101   185 MKIADFGLARDINNIDYYKKTTNgrlPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTlGGSPYP 250
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
1825-2011 5.56e-11

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 65.85  E-value: 5.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGinKQTNSEFAIKVIDKRSVSIYEKELlrsEISILRLLRHPNVIYLkeiINTKETLY--------IS 1896
Cdd:cd14054     1 QLIGQGRYGTVWKG--SLDERPVAVKVFPARHRQNFQNEK---DIYELPLMEHSNILRF---IGADERPTadgrmeylLV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1897 MELVKGGELYDFLLAETrLSEIHANKIITQLIKTVAYLH---------RCGIIHRDIKPENILLTDksrDAQIKLTDFGL 1967
Cdd:cd14054    73 LEYAPKGSLCSYLRENT-LDWMSSCRMALSLTRGLAYLHtdlrrgdqyKPAIAHRDLNSRNVLVKA---DGSCVICDFGL 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124804138 1968 STLCAPNELLKEP-----------CGTLAYVAPEVI-------TLQGYNHKVDAWSIGIILY 2011
Cdd:cd14054   149 AMVLRGSSLVRGRpgaaenasiseVGTLRYMAPEVLegavnlrDCESALKQVDVYALGLVLW 210
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
1825-2025 6.50e-11

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-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: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 65.21  E-value: 6.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1825 EQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIinTKETLYISMELVKGGE 1904
Cdd:cd14025     2 EKVGSGGFGQVYKVRHKHWKTWLAIKCPPSLHVDDSERMELLEEAKKMEMAKFRHILPVYGI--CSEPVGLVMEYMETGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1905 LYDFLLAETRLSEIHAnKIITQLIKTVAYLH--RCGIIHRDIKPENILLTDksrDAQIKLTDFGLSTLcapNELLKEP-- 1980
Cdd:cd14025    80 LEKLLASEPLPWELRF-RIIHETAVGMNFLHcmKPPLLHLDLKPANILLDA---HYHVKISDFGLAKW---NGLSHSHdl 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 124804138 1981 -----CGTLAYVAPEVITLQG--YNHKVDAWSIGIILYLLLSGKLPFPINKN 2025
Cdd:cd14025   153 srdglRGTIAYLPPERFKEKNrcPDTKHDVYSFAIVIWGILTQKKPFAGENN 204
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
1827-2020 7.00e-11

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 65.36  E-value: 7.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1827 LGQGKFSTVYRGI----NKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLlRHPNVIYLKEIInTKETLYISMELVKG 1902
Cdd:cd05111    15 LGSGVFGTVHKGIwipeGDSIKIPVAIKVIQDRSGRQSFQAVTDHMLAIGSL-DHAYIVRLLGIC-PGASLQLVTQLLPL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1903 GELYDFLlaETRLSEIHANKIIT---QLIKTVAYLHRCGIIHRDIKPENILLtdKSrDAQIKLTDFGLSTLCAPNE---L 1976
Cdd:cd05111    93 GSLLDHV--RQHRGSLGPQLLLNwcvQIAKGMYYLEEHRMVHRNLAARNVLL--KS-PSQVQVADFGVADLLYPDDkkyF 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 124804138 1977 LKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLS-GKLPF 2020
Cdd:cd05111   168 YSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMTfGAEPY 212
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
1821-2072 1.63e-10

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 65.83  E-value: 1.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1821 YELHEQLGQGKFSTVYRGINKQTNSEFAIKVIdkrsvsIYEKELLRSEISILRLLRHPNVIYLKEIINTKET-------- 1892
Cdd:PTZ00036   68 YKLGNIIGNGSFGVVYEAICIDTSEKVAIKKV------LQDPQYKNRELLIMKNLNHINIIFLKDYYYTECFkkneknif 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1893 LYISMELVKGgELYDFLLAETR----LSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLtdKSRDAQIKLTDFGLS 1968
Cdd:PTZ00036  142 LNVVMEFIPQ-TVHKYMKHYARnnhaLPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLI--DPNTHTLKLCDFGSA 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124804138 1969 -TLCAPNELLKEPCGTLaYVAPEV-ITLQGYNHKVDAWSIGIIL------YLLLSGK------------LPFPINKN-TE 2027
Cdd:PTZ00036  219 kNLLAGQRSVSYICSRF-YRAPELmLGATNYTTHIDLWSLGCIIaemilgYPIFSGQssvdqlvriiqvLGTPTEDQlKE 297
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 124804138 2028 MNiqKNYV-LSFKDYIWKSIS--------SSAKDLISKLLELNVEKRISANEAL 2072
Cdd:PTZ00036  298 MN--PNYAdIKFPDVKPKDLKkvfpkgtpDDAINFISQFLKYEPLKRLNPIEAL 349
 
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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