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Conserved domains on  [gi|40806181|ref|NP_955749|]
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dual serine/threonine and tyrosine protein kinase isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
651-867 4.94e-163

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd13975:

Pssm-ID: 419665 [Multi-domain]  Cd Length: 262  Bit Score: 475.44  E-value: 4.94e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 651 KPKLGQELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLPKHERLVDLHGSVIDYNYGGGSSIAV 730
Cdd:cd13975   1 KPKLGRELGRGQYGVVYACDSWGGHFPCALKSVVPPDDKHWNDLALEFHYTRSLPKHERIVSLHGSVIDYSYGGGSSIAV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 731 LLIMERLHRDLYTGLKAGLTLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSIV 810
Cdd:cd13975  81 LLIMERLHRDLYTGIKAGLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKPEAMMSGSIV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 811 GTPIHMAPELFTG---------------------------------------------ARPERLPVFDEECWQLMEACWD 845
Cdd:cd13975 161 GTPIHMAPELFSGkydnsvdvyafgilfwylcaghvklpeafeqcaskdhlwnnvrkgVRPERLPVFDEECWNLMEACWS 240
                       250       260
                ....*....|....*....|..
gi 40806181 846 GDPLKRPLLGIVQPMLQGIMNR 867
Cdd:cd13975 241 GDPSQRPLLGIVQPKLQGIMDR 262
 
Name Accession Description Interval E-value
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
651-867 4.94e-163

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: 475.44  E-value: 4.94e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 651 KPKLGQELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLPKHERLVDLHGSVIDYNYGGGSSIAV 730
Cdd:cd13975   1 KPKLGRELGRGQYGVVYACDSWGGHFPCALKSVVPPDDKHWNDLALEFHYTRSLPKHERIVSLHGSVIDYSYGGGSSIAV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 731 LLIMERLHRDLYTGLKAGLTLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSIV 810
Cdd:cd13975  81 LLIMERLHRDLYTGIKAGLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKPEAMMSGSIV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 811 GTPIHMAPELFTG---------------------------------------------ARPERLPVFDEECWQLMEACWD 845
Cdd:cd13975 161 GTPIHMAPELFSGkydnsvdvyafgilfwylcaghvklpeafeqcaskdhlwnnvrkgVRPERLPVFDEECWNLMEACWS 240
                       250       260
                ....*....|....*....|..
gi 40806181 846 GDPLKRPLLGIVQPMLQGIMNR 867
Cdd:cd13975 241 GDPSQRPLLGIVQPKLQGIMDR 262
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
653-852 4.35e-32

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 125.33  E-value: 4.35e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181    653 KLGQELGRGQYGVVYLCDNWGGHFPCALKSV-VPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssiaVL 731
Cdd:smart00220   2 EILEKLGEGSFGKVYLARDKKTGKLVAIKVIkKKKIKKDRERILREIKILKKL-KHPNIVRLYDVFEDEDK-------LY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181    732 LIMERL-HRDLYTGLKA--GLTLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK--PEAMMS 806
Cdd:smart00220  74 LVMEYCeGGDLFDLLKKrgRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARqlDPGEKL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181    807 GSIVGTPIHMAPE----------------------LFTGARP----------------------ERLPVFDEECWQLMEA 842
Cdd:smart00220 154 TTFVGTPEYMAPEvllgkgygkavdiwslgvilyeLLTGKPPfpgddqllelfkkigkpkppfpPPEWDISPEAKDLIRK 233
                          250
                   ....*....|
gi 40806181    843 CWDGDPLKRP 852
Cdd:smart00220 234 LLVKDPEKRL 243
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
653-852 2.19e-25

Protein tyrosine kinase;


Pssm-ID: 400179 [Multi-domain]  Cd Length: 258  Bit Score: 106.04  E-value: 2.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181   653 KLGQELGRGQYGVVYLC----DNWGGHFPCALKSVVPP-DEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggss 727
Cdd:pfam07714   2 TLGEKLGEGAFGEVYKGtlkgEGENTKIKVAVKTLKEGaDEEEREDFLEEASIMKKL-DHPNIVKLLGVCTQGEP----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181   728 iaVLLIMERL-HRDLYTGL---KAGLTLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEA 803
Cdd:pfam07714  76 --LYIVTEYMpGGDLLDFLrkhKRKLTLPDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181   804 MMSGSIVGT----PIH-MAP----------------------ELFT--------------------GARPERLPVFDEEC 836
Cdd:pfam07714 154 DDDYYRKRGggklPIKwMAPeslkdgkftsksdvwsfgvllwEIFTlgeqpypgmsneevleyledGYRLPQPENCPDEL 233
                         250
                  ....*....|....*.
gi 40806181   837 WQLMEACWDGDPLKRP 852
Cdd:pfam07714 234 YDLMKQCWAYDPEDRP 249
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
653-828 2.59e-21

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 97.12  E-value: 2.59e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 653 KLGQELGRGQYGVVYLCDNwggHFPCALKSVVPPDEKHWNDLAL---EFHYMRSLPKHERLVDLHGSvidYNYGGGSSIA 729
Cdd:COG0515   3 RILRKLGEGSFGEVYLARD---RKLVALKVLAKKLESKSKEVERflrEIQILASLNHPPNIVKLYDF---FQDEGSLYLV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 730 VLLIMERLHRDLY--TGLKAGLTLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQ-NRAKITDLGFCK------ 800
Cdd:COG0515  77 MEYVDGGSLEDLLkkIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDgRVVKLIDFGLAKllpdpg 156
                       170       180       190
                ....*....|....*....|....*....|.
gi 40806181 801 ---PEAMMSGSIVGTPIHMAPELFTGARPER 828
Cdd:COG0515 157 stsSIPALPSTSVGTPGYMAPEVLLGLSLAY 187
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
760-820 6.32e-10

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 61.76  E-value: 6.32e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40806181  760 DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSIVGTPIHMAPEL 820
Cdd:PTZ00263 126 ELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPDRTFTLCGTPEYLAPEV 186
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
732-819 8.66e-10

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 62.12  E-value: 8.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181  732 LIMERLH-RDLYTGLKAG--LTLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKpeAM---- 804
Cdd:NF033483  84 IVMEYVDgRTLKDYIREHgpLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIAR--ALsstt 161
                         90
                 ....*....|....*..
gi 40806181  805 --MSGSIVGTPIHMAPE 819
Cdd:NF033483 162 mtQTNSVLGTVHYLSPE 178
 
Name Accession Description Interval E-value
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
651-867 4.94e-163

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: 475.44  E-value: 4.94e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 651 KPKLGQELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLPKHERLVDLHGSVIDYNYGGGSSIAV 730
Cdd:cd13975   1 KPKLGRELGRGQYGVVYACDSWGGHFPCALKSVVPPDDKHWNDLALEFHYTRSLPKHERIVSLHGSVIDYSYGGGSSIAV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 731 LLIMERLHRDLYTGLKAGLTLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSIV 810
Cdd:cd13975  81 LLIMERLHRDLYTGIKAGLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKPEAMMSGSIV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 811 GTPIHMAPELFTG---------------------------------------------ARPERLPVFDEECWQLMEACWD 845
Cdd:cd13975 161 GTPIHMAPELFSGkydnsvdvyafgilfwylcaghvklpeafeqcaskdhlwnnvrkgVRPERLPVFDEECWNLMEACWS 240
                       250       260
                ....*....|....*....|..
gi 40806181 846 GDPLKRPLLGIVQPMLQGIMNR 867
Cdd:cd13975 241 GDPSQRPLLGIVQPKLQGIMDR 262
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
658-852 2.25e-37

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: 139.33  E-value: 2.25e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 658 LGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKH-WNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssiaVLLIMER 736
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKlLEELLREIEILKKL-NHPNIVKLYDVFETENF-------LYLVMEY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 737 L-HRDLYTGLK---AGLTLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSIVG- 811
Cdd:cd00180  73 CeGGSLKDLLKenkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTt 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 40806181 812 ----TPIHMAPELFTGarPERLPVFD-----------EECWQLMEACWDGDPLKRP 852
Cdd:cd00180 153 ggttPPYYAPPELLGG--RYYGPKVDiwslgvilyelEELKDLIRRMLQYDPKKRP 206
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
653-852 4.35e-32

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 125.33  E-value: 4.35e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181    653 KLGQELGRGQYGVVYLCDNWGGHFPCALKSV-VPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssiaVL 731
Cdd:smart00220   2 EILEKLGEGSFGKVYLARDKKTGKLVAIKVIkKKKIKKDRERILREIKILKKL-KHPNIVRLYDVFEDEDK-------LY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181    732 LIMERL-HRDLYTGLKA--GLTLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK--PEAMMS 806
Cdd:smart00220  74 LVMEYCeGGDLFDLLKKrgRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARqlDPGEKL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181    807 GSIVGTPIHMAPE----------------------LFTGARP----------------------ERLPVFDEECWQLMEA 842
Cdd:smart00220 154 TTFVGTPEYMAPEvllgkgygkavdiwslgvilyeLLTGKPPfpgddqllelfkkigkpkppfpPPEWDISPEAKDLIRK 233
                          250
                   ....*....|
gi 40806181    843 CWDGDPLKRP 852
Cdd:smart00220 234 LLVKDPEKRL 243
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
658-852 3.21e-30

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: 119.95  E-value: 3.21e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 658 LGRGQYGVVYLcDNWGGHfPCALKS--VVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssiaVLLIME 735
Cdd:cd13999   1 IGSGSFGEVYK-GKWRGT-DVAIKKlkVEDDNDELLKEFRREVSILSKL-RHPNIVQFIGACLSPPP-------LCIVTE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 736 RLHR-DLYTGLKAG---LTLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEA---MMSGS 808
Cdd:cd13999  71 YMPGgSLYDLLHKKkipLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNsttEKMTG 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 809 IVGTPIHMAPELFTG---------------------------------------ARPERLPVfDEECWQ----LMEACWD 845
Cdd:cd13999 151 VVGTPRWMAPEVLRGepytekadvysfgivlwelltgevpfkelspiqiaaavvQKGLRPPI-PPDCPPelskLIKRCWN 229

                ....*..
gi 40806181 846 GDPLKRP 852
Cdd:cd13999 230 EDPEKRP 236
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
653-826 2.86e-27

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: 111.52  E-value: 2.86e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 653 KLGQELGRGQYGVVYLCDNWGGHFPCALKsVVPP----DEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssi 728
Cdd:cd14014   3 RLVRLLGRGGMGEVYRARDTLLGRPVAIK-VLRPelaeDEEFRERFLREARALARL-SHPNIVRVYDVGEDDGR------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 729 aVLLIMERLH-RDLYTGLKAG--LTLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEA-- 803
Cdd:cd14014  75 -PYIVMEYVEgGSLADLLRERgpLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGds 153
                       170       180
                ....*....|....*....|....*
gi 40806181 804 --MMSGSIVGTPIHMAPELFTGARP 826
Cdd:cd14014 154 glTQTGSVLGTPAYMAPEQARGGPV 178
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
653-852 3.00e-27

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: 111.49  E-value: 3.00e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181    653 KLGQELGRGQYGVVYLC----DNWGGHFPCALKSVVPP-DEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDynygGGSS 727
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGtlkgKGDGKEVEVAVKTLKEDaSEQQIEEFLREARIMRKL-DHPNIVKLLGVCTE----EEPL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181    728 IAVLLIMErlHRDLYTGLK----AGLTLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEA 803
Cdd:smart00221  77 MIVMEYMP--GGDLLDYLRknrpKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLY 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181    804 -----MMSGSIVgtPIH-MAP----------------------ELFT--------------------GARPERLPVFDEE 835
Cdd:smart00221 155 dddyyKVKGGKL--PIRwMAPeslkegkftsksdvwsfgvllwEIFTlgeepypgmsnaevleylkkGYRLPKPPNCPPE 232
                          250
                   ....*....|....*..
gi 40806181    836 CWQLMEACWDGDPLKRP 852
Cdd:smart00221 233 LYKLMLQCWAEDPEDRP 249
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
653-852 1.27e-26

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 109.93  E-value: 1.27e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181    653 KLGQELGRGQYGVVYLCD----NWGGHFPCALKSV-VPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDynygGGSS 727
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKlkgkGGKKKVEVAVKTLkEDASEQQIEEFLREARIMRKL-DHPNVVKLLGVCTE----EEPL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181    728 IAVLLIMErlHRDLYTGLKA---GLTLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPE-- 802
Cdd:smart00219  77 YIVMEYME--GGDLLSYLRKnrpKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLyd 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181    803 ----AMMSGSIvgtPIH-MAP----------------------ELFT--------------------GARPERLPVFDEE 835
Cdd:smart00219 155 ddyyRKRGGKL---PIRwMAPeslkegkftsksdvwsfgvllwEIFTlgeqpypgmsneevleylknGYRLPQPPNCPPE 231
                          250
                   ....*....|....*..
gi 40806181    836 CWQLMEACWDGDPLKRP 852
Cdd:smart00219 232 LYDLMLQCWAEDPEDRP 248
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
653-852 2.19e-25

Protein tyrosine kinase;


Pssm-ID: 400179 [Multi-domain]  Cd Length: 258  Bit Score: 106.04  E-value: 2.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181   653 KLGQELGRGQYGVVYLC----DNWGGHFPCALKSVVPP-DEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggss 727
Cdd:pfam07714   2 TLGEKLGEGAFGEVYKGtlkgEGENTKIKVAVKTLKEGaDEEEREDFLEEASIMKKL-DHPNIVKLLGVCTQGEP----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181   728 iaVLLIMERL-HRDLYTGL---KAGLTLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEA 803
Cdd:pfam07714  76 --LYIVTEYMpGGDLLDFLrkhKRKLTLPDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181   804 MMSGSIVGT----PIH-MAP----------------------ELFT--------------------GARPERLPVFDEEC 836
Cdd:pfam07714 154 DDDYYRKRGggklPIKwMAPeslkdgkftsksdvwsfgvllwEIFTlgeqpypgmsneevleyledGYRLPQPENCPDEL 233
                         250
                  ....*....|....*.
gi 40806181   837 WQLMEACWDGDPLKRP 852
Cdd:pfam07714 234 YDLMKQCWAYDPEDRP 249
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
653-823 2.56e-23

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: 100.29  E-value: 2.56e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 653 KLGQELGRGQYGVVYLC--DNWGGHFpcALKSV--VPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVID---YN---- 721
Cdd:cd06606   3 KKGELLGKGSFGSVYLAlnLDTGELM--AVKEVelSGDSEEELEALEREIRILSSL-KHPNIVRYLGTERTentLNifle 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 722 YGGGSSIAVLLimERlhrdlYTGLKagltlETRLQI-ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK 800
Cdd:cd06606  80 YVPGGSLASLL--KK-----FGKLP-----EPVVRKyTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAK 147
                       170       180
                ....*....|....*....|....*...
gi 40806181 801 -----PEAMMSGSIVGTPIHMAPELFTG 823
Cdd:cd06606 148 rlaeiATGEGTKSLRGTPYWMAPEVIRG 175
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
653-823 2.68e-23

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: 99.90  E-value: 2.68e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 653 KLGQELGRGQYGVVYLcdnwGGHFP----CALKsVVP---PDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYggg 725
Cdd:cd14003   3 ELGKTLGEGSFGKVKL----ARHKLtgekVAIK-IIDkskLKEEIEEKIKREIEIMKLL-NHPNIIKLYEVIETENK--- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 726 ssiaVLLIMERLHR-DLYTGLKAGLTL---ETRL---QIaldvVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGF 798
Cdd:cd14003  74 ----IYLVMEYASGgELFDYIVNNGRLsedEARRffqQL----ISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGL 145
                       170       180
                ....*....|....*....|....*...
gi 40806181 799 CK---PEAMMSgSIVGTPIHMAPELFTG 823
Cdd:cd14003 146 SNefrGGSLLK-TFCGTPAYAAPEVLLG 172
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
653-826 7.68e-23

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: 99.00  E-value: 7.68e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 653 KLGQELGRGQYGVVYLCDNWGGHfpCALKSVvppdEKHWNDLAL------EFHYMRSlpKHERLVDLHG--SVIDYNYGG 724
Cdd:cd13979   6 RLQEPLGSGGFGSVYKATYKGET--VAVKIV----RRRRKNRASrqsfwaELNAARL--RHENIVRVLAaeTGTDFASLG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 725 gssiavLLIMER-----LHRDLYTGLKAgLTLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG-- 797
Cdd:cd13979  78 ------LIIMEYcgngtLQQLIYEGSEP-LPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGcs 150
                       170       180       190
                ....*....|....*....|....*....|....
gi 40806181 798 -----FCKPEAMMSGsIVGTPIHMAPELFTGARP 826
Cdd:cd13979 151 vklgeGNEVGTPRSH-IGGTYTYRAPELLKGERV 183
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
657-852 2.03e-22

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: 97.61  E-value: 2.03e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 657 ELGRGQYGVVYLC---DNWGGHFPCALKSVVP-PDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssiaVLL 732
Cdd:cd00192   2 KLGEGAFGEVYKGklkGGDGKTVDVAVKTLKEdASESERKDFLKEARVMKKL-GHPNVVRLLGVCTEEEP-------LYL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 733 IME-----------RLHRD-LYTGLKAGLTLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK 800
Cdd:cd00192  74 VMEymeggdlldflRKSRPvFPSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 801 PEAMMSGSIVGT----PIH-MAP----------------------ELFT--------------------GARPERLPVFD 833
Cdd:cd00192 154 DIYDDDYYRKKTggklPIRwMAPeslkdgiftsksdvwsfgvllwEIFTlgatpypglsneevleylrkGYRLPKPENCP 233
                       250
                ....*....|....*....
gi 40806181 834 EECWQLMEACWDGDPLKRP 852
Cdd:cd00192 234 DELYELMLSCWQLDPEDRP 252
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
658-823 1.93e-21

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: 94.93  E-value: 1.93e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 658 LGRGQYGVVYLC-DNWGGHFpCALKSV-------------VPPDEKHW-NDLALEFHYMRSLpKHERLVDLHGsVIDYNY 722
Cdd:cd14008   1 LGRGSFGKVKLAlDTETGQL-YAIKIFnksrlrkrregknDRGKIKNAlDDVRREIAIMKKL-DHPNIVRLYE-VIDDPE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 723 GGgssiAVLLIME------RLHRDLYTGLKAgLTLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDL 796
Cdd:cd14008  78 SD----KLYLVLEyceggpVMELDSGDRVPP-LPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDF 152
                       170       180       190
                ....*....|....*....|....*....|.
gi 40806181 797 G----FCKPEAMMSGSiVGTPIHMAPELFTG 823
Cdd:cd14008 153 GvsemFEDGNDTLQKT-AGTPAFLAPELCDG 182
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
658-839 1.96e-21

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: 94.68  E-value: 1.96e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 658 LGRGQYGVVYLCD--NWGGHFPCALKSVVPPDEKHWND-----LALEFHYMRSLpKHERLVDlhgsVIDYNYGGGSSIav 730
Cdd:cd13994   1 IGKGATSVVRIVTkkNPRSGVLYAVKEYRRRDDESKRKdyvkrLTSEYIISSKL-HHPNIVK----VLDLCQDLHGKW-- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 731 LLIMERL-HRDLYTGLKAG--LTLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG----FCKP-- 801
Cdd:cd13994  74 CLVMEYCpGGDLFTLIEKAdsLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGtaevFGMPae 153
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 40806181 802 -EAMMSGSIVGTPIHMAPELFTGARPERLPVfdeECWQL 839
Cdd:cd13994 154 kESPMSAGLCGSEPYMAPEVFTSGSYDGRAV---DVWSC 189
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
653-828 2.59e-21

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 97.12  E-value: 2.59e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 653 KLGQELGRGQYGVVYLCDNwggHFPCALKSVVPPDEKHWNDLAL---EFHYMRSLPKHERLVDLHGSvidYNYGGGSSIA 729
Cdd:COG0515   3 RILRKLGEGSFGEVYLARD---RKLVALKVLAKKLESKSKEVERflrEIQILASLNHPPNIVKLYDF---FQDEGSLYLV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 730 VLLIMERLHRDLY--TGLKAGLTLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQ-NRAKITDLGFCK------ 800
Cdd:COG0515  77 MEYVDGGSLEDLLkkIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDgRVVKLIDFGLAKllpdpg 156
                       170       180       190
                ....*....|....*....|....*....|.
gi 40806181 801 ---PEAMMSGSIVGTPIHMAPELFTGARPER 828
Cdd:COG0515 157 stsSIPALPSTSVGTPGYMAPEVLLGLSLAY 187
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
653-823 1.02e-20

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: 92.65  E-value: 1.02e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 653 KLGQELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssiaVLL 732
Cdd:cd05122   3 EILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESILNEIAILKKC-KHPNIVKYYGSYLKKDE-------LWI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 733 IMERLH----RDLYTGLKAGLTLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK--PEAMMS 806
Cdd:cd05122  75 VMEFCSggslKDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAqlSDGKTR 154
                       170
                ....*....|....*..
gi 40806181 807 GSIVGTPIHMAPELFTG 823
Cdd:cd05122 155 NTFVGTPYWMAPEVIQG 171
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
653-836 4.03e-20

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: 91.00  E-value: 4.03e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 653 KLGQELGRGQYGVVYLCDNWGGHFPCALKSV--VPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssiaV 730
Cdd:cd05117   3 ELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIdkKKLKSEDEEMLRREIEILKRL-DHPNIVKLYEVFEDDKN-------L 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 731 LLIMERLH-RDLYTGLKAGLTL---ETRlQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRA---KITDLGFCK--- 800
Cdd:cd05117  75 YLVMELCTgGELFDRIVKKGSFserEAA-KIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDspiKIIDFGLAKife 153
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 40806181 801 PEAMMSGsIVGTPIHMAPELFTGARperlpvFDEEC 836
Cdd:cd05117 154 EGEKLKT-VCGTPYYVAPEVLKGKG------YGKKC 182
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
656-823 3.39e-19

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: 88.04  E-value: 3.39e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 656 QELGRGQYGVVYLCDNWGGHFPCALKsVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssiaVLLIME 735
Cdd:cd06614   6 EKIGEGASGEVYKATDRATGKEVAIK-KMRLRKQNKELIINEILIMKEC-KHPNIVDYYDSYLVGDE-------LWVVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 736 RLHR----DLYTGLKAGLTlETrlQIA---LDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC---KPEAMM 805
Cdd:cd06614  77 YMDGgsltDIITQNPVRMN-ES--QIAyvcREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAaqlTKEKSK 153
                       170
                ....*....|....*...
gi 40806181 806 SGSIVGTPIHMAPELFTG 823
Cdd:cd06614 154 RNSVVGTPYWMAPEVIKR 171
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
653-864 4.35e-18

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: 84.71  E-value: 4.35e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 653 KLGQELGRGQYGVVYLCDnWGGHFpCALKsVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDynyggGSSIavLL 732
Cdd:cd05039   9 KLGELIGKGEFGDVMLGD-YRGQK-VAVK-CLKDDSTAAQAFLAEASVMTTL-RHPNLVQLLGVVLE-----GNGL--YI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 733 IMERLHRD-----LYTGLKAGLTLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAmmSG 807
Cdd:cd05039  78 VTEYMAKGslvdyLRSRGRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEAS--SN 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 808 SIVGT-PIH-MAPE-----LFT------------------GARP-ERLPVFD--------------EEC----WQLMEAC 843
Cdd:cd05039 156 QDGGKlPIKwTAPEalrekKFStksdvwsfgillweiysfGRVPyPRIPLKDvvphvekgyrmeapEGCppevYKVMKNC 235
                       250       260
                ....*....|....*....|.
gi 40806181 844 WDGDPLKRPLLGIVQPMLQGI 864
Cdd:cd05039 236 WELDPAKRPTFKQLREKLEHI 256
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
658-852 1.50e-17

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: 83.27  E-value: 1.50e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 658 LGRGQYGVVYLC--DNWGGHFpcALKSV--VPPDEKHWNDLALEFHYMRSLpKHERLVDL---------HGSVIDYNYGG 724
Cdd:cd13978   1 LGSGGFGTVSKArhVSWFGMV--AIKCLhsSPNCIEERKALLKEAEKMERA-RHSYVLPLlgvcverrsLGLVMEYMENG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 725 gsSIAVLLIMErlhrdlYTGLKAGLtletRLQIALDVVEGIRFLH--SQGLVHRDIKLKNVLLDKQNRAKITDLGFCK-- 800
Cdd:cd13978  78 --SLKSLLERE------IQDVPWSL----RFRIIHEIALGMNFLHnmDPPLLHHDLKPENILLDNHFHVKISDFGLSKlg 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 801 ------PEAMMSGSIVGTPIHMAPELF--------------------------------------------TGARPErLP 830
Cdd:cd13978 146 mksisaNRRRGTENLGGTPIYMAPEAFddfnkkptsksdvysfaiviwavltrkepfenainpllimqivsKGDRPS-LD 224
                       250       260       270
                ....*....|....*....|....*....|
gi 40806181 831 VFDEECW--------QLMEACWDGDPLKRP 852
Cdd:cd13978 225 DIGRLKQienvqeliSLMIRCWDGNPDARP 254
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
650-852 2.23e-17

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: 83.20  E-value: 2.23e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 650 RKPKLGQELGRGQYGVVYLC------DNWGGHfpCALKSVVPP-DEKHWNDLALEFHYMRSLpKHERLVDLHGsvIDYNY 722
Cdd:cd05038   4 RHLKFIKQLGEGHFGSVELCrydplgDNTGEQ--VAVKSLQPSgEEQHMSDFKREIEILRTL-DHEYIVKYKG--VCESP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 723 GGGSsiaVLLIMERLH----RDLYTGLKAGLTLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGF 798
Cdd:cd05038  79 GRRS---LRLIMEYLPsgslRDYLQRHRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40806181 799 CK-----------------------PEAMM-----SGSIV---GTPIHmapELFTGARP--------------------- 826
Cdd:cd05038 156 AKvlpedkeyyyvkepgespifwyaPECLResrfsSASDVwsfGVTLY---ELFTYGDPsqsppalflrmigiaqgqmiv 232
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 40806181 827 ----------ERLPVFD---EECWQLMEACWDGDPLKRP 852
Cdd:cd05038 233