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Conserved domains on  [gi|1720355205|ref|XP_030109810|]
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2-5A-dependent ribonuclease isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RNase_RNase-L cd10423
RNase domain (also known as the kinase extension nuclease domain) of RNase L; Ribonuclease L ...
588-707 1.62e-70

RNase domain (also known as the kinase extension nuclease domain) of RNase L; Ribonuclease L (RNase L), sometimes referred to as the 2-5A-dependent RNase, is a highly regulated, latent endoribonuclease (thus the 'L' in RNase L) and is widely expressed in most mammalian tissues. It is involved in the mediation of the antiviral and pro-apoptotic activities of the interferon-inducible 2-5A system, which blocks infections by certain types of viruses through cleavage of viral and cellular single-stranded RNA. RNase L is unique in that it is composed of three major domains; N-terminus regulatory ankyrin repeat domain (ARD), followed by a linker, a protein kinase (PK)-like domain and a C-terminal ribonuclease (RNase) domain. The RNase domain has homology with IRE1, also containing both a kinase and an endoribonuclease, that functions in the unfolded protein response (UPR). RNase L has been shown to have an impact on the pathogenesis of prostate cancer; the RNase L gene, RNASEL, has been identified as a strong candidate for the hereditary prostate cancer 1 (HPC1) allele. The broad range of biological functions of RNase offers a possibility for RNase L as a therapeutic target.


:

Pssm-ID: 199218  Cd Length: 119  Bit Score: 225.81  E-value: 1.62e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 588 ENRYRTLRNVGNESDIKVRKCKSDLLRLLQHQTLEPPRSFDQWTSKIDKNVMDEMNHFYEKRKkNPYQDTVGDLLKFIRN 667
Cdd:cd10423     1 ENRYRTLRNVGNESDIKTRDDKSDILRLLQAGKSECSRSFPNWTSKIDKEVMDIMNKFYEKKK-FFYQDTVGDLLKFIRN 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1720355205 668 IGEHINEEKKRGMKEILGDPSRYFQETFPDLVIYIYKKLK 707
Cdd:cd10423    80 LGEHIDEEKNKRMKEIIGDPSEYFQKTFPDLVIYVYKKLR 119
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-299 1.17e-48

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.22  E-value: 1.17e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  24 EDDSSLIKAVQKGDVVRVQQLLEKGADANACEDTWGWTPLHNAVQAGRVDIVNLLLSHGADPHRRKKNGATPFIIAGIQG 103
Cdd:COG0666    52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 104 DVKLLEILLSCGADVNECDENGFTAFMEAAERGNAEALRFLFAKGANVNLRRqttkdkrrlkQGGATALMSAAEKGHLEV 183
Cdd:COG0666   132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD----------NDGETPLHLAAENGHLEI 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 184 LRILLNdmkaevdardnmgrnalirtllnwdcenveeitsiliqHGADVNVRGERGKTPLIAAVERKHTGLVQMLLSReG 263
Cdd:COG0666   202 VKLLLE--------------------------------------AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA-G 242
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1720355205 264 INIDARDNEGKTALLIAVDKQLKEIVQLLLEKGADK 299
Cdd:COG0666   243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
361-585 1.09e-21

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 cd13982:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 269  Bit Score: 95.42  E-value: 1.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 361 KIFIHDDyKIAGTSEGA-VYLGIYDNREVAVK-VFRENSPRGCKEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVSLCEW 438
Cdd:cd13982     1 KLTFSPK-VLGYGSEGTiVFRGTFDGRPVAVKrLLPEFFDFADREVQLLRESDEHPNVIRYFCTEKDRQFLYIALELCAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 439 TLEEFLRLPREEPvengedKFAH------SILLSIFEGVQKLHLHGYSHQDLQPQNILID---SKKAVR--LADF----- 502
Cdd:cd13982    80 SLQDLVESPRESK------LFLRpglepvRLLRQIASGLAHLHSLNIVHRDLKPQNILIStpnAHGNVRamISDFglckk 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 503 ----DQSIR----------W----MGESQMVRR-----DLEDLGRLVLYVVMKGEIPF-ETLKTQ--------NDEVLLT 550
Cdd:cd13982   154 ldvgRSSFSrrsgvagtsgWiapeMLSGSTKRRqtravDIFSLGCVFYYVLSGGSHPFgDKLEREanilkgkySLDKLLS 233
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1720355205 551 MSP-DEETKDLIHCLFSPGENVKNCLVDLLGHPFFW 585
Cdd:cd13982   234 LGEhGPEAQDLIERMIDFDPEKRPSAEEVLNHPFFW 269
 
Name Accession Description Interval E-value
RNase_RNase-L cd10423
RNase domain (also known as the kinase extension nuclease domain) of RNase L; Ribonuclease L ...
588-707 1.62e-70

RNase domain (also known as the kinase extension nuclease domain) of RNase L; Ribonuclease L (RNase L), sometimes referred to as the 2-5A-dependent RNase, is a highly regulated, latent endoribonuclease (thus the 'L' in RNase L) and is widely expressed in most mammalian tissues. It is involved in the mediation of the antiviral and pro-apoptotic activities of the interferon-inducible 2-5A system, which blocks infections by certain types of viruses through cleavage of viral and cellular single-stranded RNA. RNase L is unique in that it is composed of three major domains; N-terminus regulatory ankyrin repeat domain (ARD), followed by a linker, a protein kinase (PK)-like domain and a C-terminal ribonuclease (RNase) domain. The RNase domain has homology with IRE1, also containing both a kinase and an endoribonuclease, that functions in the unfolded protein response (UPR). RNase L has been shown to have an impact on the pathogenesis of prostate cancer; the RNase L gene, RNASEL, has been identified as a strong candidate for the hereditary prostate cancer 1 (HPC1) allele. The broad range of biological functions of RNase offers a possibility for RNase L as a therapeutic target.


Pssm-ID: 199218  Cd Length: 119  Bit Score: 225.81  E-value: 1.62e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 588 ENRYRTLRNVGNESDIKVRKCKSDLLRLLQHQTLEPPRSFDQWTSKIDKNVMDEMNHFYEKRKkNPYQDTVGDLLKFIRN 667
Cdd:cd10423     1 ENRYRTLRNVGNESDIKTRDDKSDILRLLQAGKSECSRSFPNWTSKIDKEVMDIMNKFYEKKK-FFYQDTVGDLLKFIRN 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1720355205 668 IGEHINEEKKRGMKEILGDPSRYFQETFPDLVIYIYKKLK 707
Cdd:cd10423    80 LGEHIDEEKNKRMKEIIGDPSEYFQKTFPDLVIYVYKKLR 119
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-299 1.17e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.22  E-value: 1.17e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  24 EDDSSLIKAVQKGDVVRVQQLLEKGADANACEDTWGWTPLHNAVQAGRVDIVNLLLSHGADPHRRKKNGATPFIIAGIQG 103
Cdd:COG0666    52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 104 DVKLLEILLSCGADVNECDENGFTAFMEAAERGNAEALRFLFAKGANVNLRRqttkdkrrlkQGGATALMSAAEKGHLEV 183
Cdd:COG0666   132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD----------NDGETPLHLAAENGHLEI 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 184 LRILLNdmkaevdardnmgrnalirtllnwdcenveeitsiliqHGADVNVRGERGKTPLIAAVERKHTGLVQMLLSReG 263
Cdd:COG0666   202 VKLLLE--------------------------------------AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA-G 242
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1720355205 264 INIDARDNEGKTALLIAVDKQLKEIVQLLLEKGADK 299
Cdd:COG0666   243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
Ribonuc_2-5A pfam06479
Ribonuclease 2-5A; This domain is a endoribonuclease. Specifically it cleaves an intron from ...
590-717 6.01e-39

Ribonuclease 2-5A; This domain is a endoribonuclease. Specifically it cleaves an intron from Hac1 mRNA in humans, which causes it to be much more efficiently translated.


Pssm-ID: 461930  Cd Length: 127  Bit Score: 140.31  E-value: 6.01e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 590 RYRTLRNVGNESDIKVRKCKSDLLRLLQHQTLEPPRSfdQWTSKIDKNVMDEMNHFYekrkkNPYQDTVGDLLKFIRNIG 669
Cdd:pfam06479   1 RLAFLQDVSDRFEKEPRDPPSPLLQLLESGASEVVGG--DWTKKLDKEFVDNLGKYR-----KYDGDSVRDLLRAIRNKK 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720355205 670 EHINEEKKrGMKEILGD-PS---RYFQETFPDLVIYIYKKLKET-EYRKHFPQ 717
Cdd:pfam06479  74 HHYRELPE-EVKEILGPlPDgflSYFTSRFPNLLIHVYKVVKETlKDEDHFKK 125
PHA03100 PHA03100
ankyrin repeat protein; Provisional
61-298 3.66e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 102.82  E-value: 3.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  61 TPLHNAVQAGRVDIVNLLLSHGADPHRRKKNGATPFIIAG-----IQGDVKLLEILLSCGADVNECDENGFTAFMEAA-- 133
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAIsk 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 134 ERGNAEALRFLFAKGANVNLRRQTtkdkrrlkqgGATALMSAAEKGH--LEVLRILLnDMKAEVDARDnmgrnalirtll 211
Cdd:PHA03100  117 KSNSYSIVEYLLDNGANVNIKNSD----------GENLLHLYLESNKidLKILKLLI-DKGVDINAKN------------ 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 212 nwdceNVEeitsILIQHGADVNVRGERGKTPLIAAVERKHTGLVQMLLsREGINIDARDNEGKTALLIAVDKQLKEIVQL 291
Cdd:PHA03100  174 -----RVN----YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLL-DLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243

                  ....*..
gi 1720355205 292 LLEKGAD 298
Cdd:PHA03100  244 LLNNGPS 250
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
361-585 1.09e-21

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: 95.42  E-value: 1.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 361 KIFIHDDyKIAGTSEGA-VYLGIYDNREVAVK-VFRENSPRGCKEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVSLCEW 438
Cdd:cd13982     1 KLTFSPK-VLGYGSEGTiVFRGTFDGRPVAVKrLLPEFFDFADREVQLLRESDEHPNVIRYFCTEKDRQFLYIALELCAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 439 TLEEFLRLPREEPvengedKFAH------SILLSIFEGVQKLHLHGYSHQDLQPQNILID---SKKAVR--LADF----- 502
Cdd:cd13982    80 SLQDLVESPRESK------LFLRpglepvRLLRQIASGLAHLHSLNIVHRDLKPQNILIStpnAHGNVRamISDFglckk 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 503 ----DQSIR----------W----MGESQMVRR-----DLEDLGRLVLYVVMKGEIPF-ETLKTQ--------NDEVLLT 550
Cdd:cd13982   154 ldvgRSSFSrrsgvagtsgWiapeMLSGSTKRRqtravDIFSLGCVFYYVLSGGSHPFgDKLEREanilkgkySLDKLLS 233
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1720355205 551 MSP-DEETKDLIHCLFSPGENVKNCLVDLLGHPFFW 585
Cdd:cd13982   234 LGEhGPEAQDLIERMIDFDPEKRPSAEEVLNHPFFW 269
Ank_2 pfam12796
Ankyrin repeats (3 copies);
63-154 2.18e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.24  E-value: 2.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  63 LHNAVQAGRVDIVNLLLSHGADPHRRKKNGATPFIIAGIQGDVKLLEILLSCgADVNECDeNGFTAFMEAAERGNAEALR 142
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|..
gi 1720355205 143 FLFAKGANVNLR 154
Cdd:pfam12796  79 LLLEKGADINVK 90
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
376-584 9.39e-19

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 86.43  E-value: 9.39e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  376 GAVYLGIY--DNREVAVKVFR-----ENSPRGCKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEW-TLEEFLRlp 447
Cdd:smart00220  13 GKVYLARDkkTGKLVAIKVIKkkkikKDRERILREIKILKKL-KHPNIVRLYDVFEDEDKLYLVMEYCEGgDLFDLLK-- 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  448 reepvENG--EDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSIRWMGESQM----------- 514
Cdd:smart00220  90 -----KRGrlSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLttfvgtpeyma 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  515 ---VRRDLED-------LGrLVLYVVMKGEIPFETLKTQNDEVLLTMSPD-----------EETKDLIHCLFspgenVKN 573
Cdd:smart00220 165 pevLLGKGYGkavdiwsLG-VILYELLTGKPPFPGDDQLLELFKKIGKPKppfpppewdisPEAKDLIRKLL-----VKD 238
                          250
                   ....*....|....*.
gi 1720355205  574 -----CLVDLLGHPFF 584
Cdd:smart00220 239 pekrlTAEEALQHPFF 254
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
352-502 1.10e-13

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 74.28  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 352 MTRPMIGKLKIfihdDYKIAGTSEGAVYLG--IYDNREVAVKVFRENSPRGCKEVSCLRD----CG--DHSNLVAFYGRE 423
Cdd:COG0515     1 MSALLLGRYRI----LRLLGRGGMGVVYLArdLRLGRPVALKVLRPELAADPEARERFRRearaLArlNHPNIVRVYDVG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 424 DDKGCLYVC------VSLCEWtLEEFLRLPREEpvengedkfAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAV 497
Cdd:COG0515    77 EEDGRPYLVmeyvegESLADL-LRRRGPLPPAE---------ALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRV 146

                  ....*
gi 1720355205 498 RLADF 502
Cdd:COG0515   147 KLIDF 151
PUG smart00580
domain in protein kinases, N-glycanases and other nuclear proteins;
657-707 1.86e-11

domain in protein kinases, N-glycanases and other nuclear proteins;


Pssm-ID: 197798  Cd Length: 57  Bit Score: 59.62  E-value: 1.86e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720355205  657 TVGDLLKFIRNIGEHINEEK-----KRGMKEILGDPSRYFQETFPDLVIY-IYKKLK 707
Cdd:smart00580   1 SVRDLLRALRNILHHPREEKgnpaiKERLGPVPGGFELYFTVGFPRLLISeVYTLPK 57
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
376-502 9.32e-10

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: 59.82  E-value: 9.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIYD------NREVAVKVFRENSPRG-----CKEVSCLRDcGDHSNLVAFYG--REDDKgcLYVCVSLCEW-TLE 441
Cdd:pfam07714  13 GEVYKGTLKgegentKIKVAVKTLKEGADEEeredfLEEASIMKK-LDHPNIVKLLGvcTQGEP--LYIVTEYMPGgDLL 89
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720355205 442 EFLRLPREepvengedKFAHSILLS----IFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:pfam07714  90 DFLRKHKR--------KLTLKDLLSmalqIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDF 146
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
166-314 1.14e-08

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 58.55  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 166 QGGATALMSAAEKGHL-EVLRILLNDMKAEVDARDNMGRNALIRTLLnwdcENV-EEITSILIQHgadvNVRGERGKTPL 243
Cdd:TIGR00870  15 SDEEKAFLPAAERGDLaSVYRDLEEPKKLNINCPDRLGRSALFVAAI----ENEnLELTELLLNL----SCRGAVGDTLL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 244 IAAVERKHTGlVQMLLSREGINIDARDN-------------EGKTALLIAVDKQLKEIVQLLLEKGAD-----KCDDLVW 305
Cdd:TIGR00870  87 HAISLEYVDA-VEAILLHLLAAFRKSGPlelandqytseftPGITALHLAAHRQNYEIVKLLLERGASvparaCGDFFVK 165

                  ....*....
gi 1720355205 306 IARRNHDYH 314
Cdd:TIGR00870 166 SQGVDSFYH 174
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
307-502 3.71e-08

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 55.99  E-value: 3.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 307 ARRNHDyhlVKLLLPY----VANPDTDPPAGDWSPHSSrwGTALKSLHSMTRPMIGKLKIFihddYKIAGTSEGAVYLGI 382
Cdd:PLN00034   24 PRRRPD---LTLPLPQrdpsLAVPLPLPPPSSSSSSSS--SSSASGSAPSAAKSLSELERV----NRIGSGAGGTVYKVI 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 383 Y--DNREVAVKVF---RENSPRG--CKEVSCLRDCgDHSNLVAFYGREDDKGCLYVcvslcewtLEEFLRLPREEPVENG 455
Cdd:PLN00034   95 HrpTGRLYALKVIygnHEDTVRRqiCREIEILRDV-NHPNVVKCHDMFDHNGEIQV--------LLEFMDGGSLEGTHIA 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1720355205 456 EDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:PLN00034  166 DEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADF 212
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
156-298 1.50e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 51.68  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 156 QTTKDKRRLKQGGATALMSAAEKGHLEVLRIL--LNDMKAEVDARD---------NMGRNALIRTLLNWDcENVEEITSI 224
Cdd:cd22194    37 ELAKEEQRDKKKRLKKVSEAAVEELGELLKELkdLSRRRRKTDVPDflmhkltasDTGKTCLMKALLNIN-ENTKEIVRI 115
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355205 225 LIQHGadvnvrgergktpliaaverKHTGLVQMLLSREginIDARDNEGKTALLIAVDKQLKEIVQLLLEKGAD 298
Cdd:cd22194   116 LLAFA--------------------EENGILDRFINAE---YTEEAYEGQTALNIAIERRQGDIVKLLIAKGAD 166
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
59-86 9.84e-06

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.57  E-value: 9.84e-06
                           10        20
                   ....*....|....*....|....*...
gi 1720355205   59 GWTPLHNAVQAGRVDIVNLLLSHGADPH 86
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
378-502 9.99e-06

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 49.02  E-value: 9.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 378 VYLGiYD---NREVAVKVFRE---NSP-------RGCKEVSCLrdcgDHSNLVAFY--GREDD---------KGClyvcv 433
Cdd:NF033483   23 VYLA-KDtrlDRDVAVKVLRPdlaRDPefvarfrREAQSAASL----SHPNIVSVYdvGEDGGipyivmeyvDGR----- 92
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720355205 434 slcewTLEEFLR----LPREEPVEngedkfahsILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:NF033483   93 -----TLKDYIRehgpLSPEEAVE---------IMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDF 151
 
Name Accession Description Interval E-value
RNase_RNase-L cd10423
RNase domain (also known as the kinase extension nuclease domain) of RNase L; Ribonuclease L ...
588-707 1.62e-70

RNase domain (also known as the kinase extension nuclease domain) of RNase L; Ribonuclease L (RNase L), sometimes referred to as the 2-5A-dependent RNase, is a highly regulated, latent endoribonuclease (thus the 'L' in RNase L) and is widely expressed in most mammalian tissues. It is involved in the mediation of the antiviral and pro-apoptotic activities of the interferon-inducible 2-5A system, which blocks infections by certain types of viruses through cleavage of viral and cellular single-stranded RNA. RNase L is unique in that it is composed of three major domains; N-terminus regulatory ankyrin repeat domain (ARD), followed by a linker, a protein kinase (PK)-like domain and a C-terminal ribonuclease (RNase) domain. The RNase domain has homology with IRE1, also containing both a kinase and an endoribonuclease, that functions in the unfolded protein response (UPR). RNase L has been shown to have an impact on the pathogenesis of prostate cancer; the RNase L gene, RNASEL, has been identified as a strong candidate for the hereditary prostate cancer 1 (HPC1) allele. The broad range of biological functions of RNase offers a possibility for RNase L as a therapeutic target.


Pssm-ID: 199218  Cd Length: 119  Bit Score: 225.81  E-value: 1.62e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 588 ENRYRTLRNVGNESDIKVRKCKSDLLRLLQHQTLEPPRSFDQWTSKIDKNVMDEMNHFYEKRKkNPYQDTVGDLLKFIRN 667
Cdd:cd10423     1 ENRYRTLRNVGNESDIKTRDDKSDILRLLQAGKSECSRSFPNWTSKIDKEVMDIMNKFYEKKK-FFYQDTVGDLLKFIRN 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1720355205 668 IGEHINEEKKRGMKEILGDPSRYFQETFPDLVIYIYKKLK 707
Cdd:cd10423    80 LGEHIDEEKNKRMKEIIGDPSEYFQKTFPDLVIYVYKKLR 119
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-299 1.17e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.22  E-value: 1.17e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  24 EDDSSLIKAVQKGDVVRVQQLLEKGADANACEDTWGWTPLHNAVQAGRVDIVNLLLSHGADPHRRKKNGATPFIIAGIQG 103
Cdd:COG0666    52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 104 DVKLLEILLSCGADVNECDENGFTAFMEAAERGNAEALRFLFAKGANVNLRRqttkdkrrlkQGGATALMSAAEKGHLEV 183
Cdd:COG0666   132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD----------NDGETPLHLAAENGHLEI 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 184 LRILLNdmkaevdardnmgrnalirtllnwdcenveeitsiliqHGADVNVRGERGKTPLIAAVERKHTGLVQMLLSReG 263
Cdd:COG0666   202 VKLLLE--------------------------------------AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA-G 242
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1720355205 264 INIDARDNEGKTALLIAVDKQLKEIVQLLLEKGADK 299
Cdd:COG0666   243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
44-334 4.45e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 165.90  E-value: 4.45e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  44 LLEKGADANACEDTWGWTPLHNAVQAGRVDIVNLLLSHGADPHRRKKNGATPFIIAGIQGDVKLLEILLSCGADVNECDE 123
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 124 NGFTAFMEAAERGNAEALRFLFAKGANVNlrrqtTKDKRrlkqgGATALMSAAEKGHLEVLRILLnDMKAEVDARDNMGR 203
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVN-----ARDKD-----GETPLHLAAYNGNLEIVKLLL-EAGADVNAQDNDGN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 204 NALIRTLLNWDcenvEEITSILIQHGADVNVRGERGKTPLIAAVERKHTGLVQMLLSReGINIDARDNEGKTALLIAVDK 283
Cdd:COG0666   155 TPLHLAAANGN----LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAEN 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720355205 284 QLKEIVQLLLEKGADK------CDDLVWIARRNHDYHLVKLLLPYVANPDTDPPAGD 334
Cdd:COG0666   230 GNLEIVKLLLEAGADLnakdkdGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
Ribonuc_2-5A pfam06479
Ribonuclease 2-5A; This domain is a endoribonuclease. Specifically it cleaves an intron from ...
590-717 6.01e-39

Ribonuclease 2-5A; This domain is a endoribonuclease. Specifically it cleaves an intron from Hac1 mRNA in humans, which causes it to be much more efficiently translated.


Pssm-ID: 461930  Cd Length: 127  Bit Score: 140.31  E-value: 6.01e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 590 RYRTLRNVGNESDIKVRKCKSDLLRLLQHQTLEPPRSfdQWTSKIDKNVMDEMNHFYekrkkNPYQDTVGDLLKFIRNIG 669
Cdd:pfam06479   1 RLAFLQDVSDRFEKEPRDPPSPLLQLLESGASEVVGG--DWTKKLDKEFVDNLGKYR-----KYDGDSVRDLLRAIRNKK 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720355205 670 EHINEEKKrGMKEILGD-PS---RYFQETFPDLVIYIYKKLKET-EYRKHFPQ 717
Cdd:pfam06479  74 HHYRELPE-EVKEILGPlPDgflSYFTSRFPNLLIHVYKVVKETlKDEDHFKK 125
RNase_Ire1_like cd10321
RNase domain (also known as the kinase extension nuclease domain) of Ire1 and RNase L; This ...
588-707 1.22e-24

RNase domain (also known as the kinase extension nuclease domain) of Ire1 and RNase L; This RNase domain is found in the multi-functional protein Ire1; Ire1 also contains a type I transmembrane serine/threonine protein kinase (STK) domain, and a Luminal dimerization domain. Ire1 is essential for the endoplasmic reticulum (ER) unfolded protein response (UPR). The UPR is activated when protein misfolding is detected in the ER in order to reduce the synthesis of new proteins and increase the capacity of the ER to cope with the stress. IRE1 acts as an ER stress sensor; IRE1 dimerizes through its N-terminal luminal domain and forms oligomers, promoting trans-autophosphorylation by its cytosolic kinase domain which stimulates its endoribonuclease (RNase) activity and results in the cleavage of its mRNA substrate, Hac1 in yeast and Xbp1 in metazoans, thus promoting a splicing event that enables translation into a transcription factor which activates the UPR. This RNase domain is also found in Ribonuclease L (RNase L), sometimes referred to as the 2-5A-dependent RNase. RNase L is a highly regulated, latent endoribonuclease widely expressed in most mammalian tissues. It is involved in the mediation of the antiviral and pro-apoptotic activities of the interferon-inducible 2-5A system; the interferon (IFN)-inducible 2'-5'-oligoadenylate synthetase (OAS)/RNase L pathway blocks infections by certain types of viruses through cleavage of viral and cellular single-stranded RNA. RNase L has been shown to have an impact on the pathogenesis of prostate cancer; the RNase L gene, RNASEL, has been identified as a strong candidate for the hereditary prostate cancer 1 (HPC1) allele.


Pssm-ID: 199216  Cd Length: 127  Bit Score: 99.79  E-value: 1.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 588 ENRYRTLRNVGNESDIKVRKcKSDLLRLLQH--QTLEPPRSFDQWTSKIDKNVMDEMNHFYEKrkknPYQ-DTVGDLLKF 664
Cdd:cd10321     1 EKKIQFIDAVLNLLKDSNLP-PSTLNKLLNPgsDTVSSSFLSKPWNTLIDKNLMDDLSNFVRR----TYNyDQVKDLIRC 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720355205 665 IRNIGEHINE------EKKRGMKEIL---GDPSRYFQETFPDLVIYIYKKLK 707
Cdd:cd10321    76 IRNTIQHHKEiknqlpEKNKEILESLksqDSFFNYFESRFPNLLIFLYYKFK 127
PHA03100 PHA03100
ankyrin repeat protein; Provisional
61-298 3.66e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 102.82  E-value: 3.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  61 TPLHNAVQAGRVDIVNLLLSHGADPHRRKKNGATPFIIAG-----IQGDVKLLEILLSCGADVNECDENGFTAFMEAA-- 133
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAIsk 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 134 ERGNAEALRFLFAKGANVNLRRQTtkdkrrlkqgGATALMSAAEKGH--LEVLRILLnDMKAEVDARDnmgrnalirtll 211
Cdd:PHA03100  117 KSNSYSIVEYLLDNGANVNIKNSD----------GENLLHLYLESNKidLKILKLLI-DKGVDINAKN------------ 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 212 nwdceNVEeitsILIQHGADVNVRGERGKTPLIAAVERKHTGLVQMLLsREGINIDARDNEGKTALLIAVDKQLKEIVQL 291
Cdd:PHA03100  174 -----RVN----YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLL-DLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243

                  ....*..
gi 1720355205 292 LLEKGAD 298
Cdd:PHA03100  244 LLNNGPS 250
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
361-585 1.09e-21

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: 95.42  E-value: 1.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 361 KIFIHDDyKIAGTSEGA-VYLGIYDNREVAVK-VFRENSPRGCKEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVSLCEW 438
Cdd:cd13982     1 KLTFSPK-VLGYGSEGTiVFRGTFDGRPVAVKrLLPEFFDFADREVQLLRESDEHPNVIRYFCTEKDRQFLYIALELCAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 439 TLEEFLRLPREEPvengedKFAH------SILLSIFEGVQKLHLHGYSHQDLQPQNILID---SKKAVR--LADF----- 502
Cdd:cd13982    80 SLQDLVESPRESK------LFLRpglepvRLLRQIASGLAHLHSLNIVHRDLKPQNILIStpnAHGNVRamISDFglckk 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 503 ----DQSIR----------W----MGESQMVRR-----DLEDLGRLVLYVVMKGEIPF-ETLKTQ--------NDEVLLT 550
Cdd:cd13982   154 ldvgRSSFSrrsgvagtsgWiapeMLSGSTKRRqtravDIFSLGCVFYYVLSGGSHPFgDKLEREanilkgkySLDKLLS 233
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1720355205 551 MSP-DEETKDLIHCLFSPGENVKNCLVDLLGHPFFW 585
Cdd:cd13982   234 LGEhGPEAQDLIERMIDFDPEKRPSAEEVLNHPFFW 269
PHA03095 PHA03095
ankyrin-like protein; Provisional
37-329 2.15e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 98.17  E-value: 2.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  37 DVVRVQQLLEKGADANaCEDTWGWTPLHNAVQAG---RVDIVNLLLSHGADPHRRKKNGATPFIIAGIQGDV-KLLEILL 112
Cdd:PHA03095   26 TVEEVRRLLAAGADVN-FRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLI 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 113 SCGADVNECDENGFTAFME--AAERGNAEALRFLFAKGANVNlrrqttkdkrRLKQGGATALmSAAEKGH---LEVLRIL 187
Cdd:PHA03095  105 KAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVN----------ALDLYGMTPL-AVLLKSRnanVELLRLL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 188 LnDMKAEVDARDNMGrnaliRTLLNWDCENV---EEITSILIQHGADVNVRGERGKTPL--IAAVERKHTGLVQMLLsRE 262
Cdd:PHA03095  174 I-DAGADVYAVDDRF-----RSLLHHHLQSFkprARIVRELIRAGCDPAATDMLGNTPLhsMATGSSCKRSLVLPLL-IA 246
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355205 263 GINIDARDNEGKTALLIAVDKQLKEIVQLLLEKGAD---------KCDDLvwiARRNHDYHLVKLLLPyvANPDTD 329
Cdd:PHA03095  247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADinavssdgnTPLSL---MVRNNNGRAVRAALA--KNPSAE 317
Ank_2 pfam12796
Ankyrin repeats (3 copies);
63-154 2.18e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.24  E-value: 2.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  63 LHNAVQAGRVDIVNLLLSHGADPHRRKKNGATPFIIAGIQGDVKLLEILLSCgADVNECDeNGFTAFMEAAERGNAEALR 142
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|..
gi 1720355205 143 FLFAKGANVNLR 154
Cdd:pfam12796  79 LLLEKGADINVK 90
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
376-584 9.39e-19

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 86.43  E-value: 9.39e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  376 GAVYLGIY--DNREVAVKVFR-----ENSPRGCKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEW-TLEEFLRlp 447
Cdd:smart00220  13 GKVYLARDkkTGKLVAIKVIKkkkikKDRERILREIKILKKL-KHPNIVRLYDVFEDEDKLYLVMEYCEGgDLFDLLK-- 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  448 reepvENG--EDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSIRWMGESQM----------- 514
Cdd:smart00220  90 -----KRGrlSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLttfvgtpeyma 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  515 ---VRRDLED-------LGrLVLYVVMKGEIPFETLKTQNDEVLLTMSPD-----------EETKDLIHCLFspgenVKN 573
Cdd:smart00220 165 pevLLGKGYGkavdiwsLG-VILYELLTGKPPFPGDDQLLELFKKIGKPKppfpppewdisPEAKDLIRKLL-----VKD 238
                          250
                   ....*....|....*.
gi 1720355205  574 -----CLVDLLGHPFF 584
Cdd:smart00220 239 pekrlTAEEALQHPFF 254
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
376-502 1.87e-18

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: 84.63  E-value: 1.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIY--DNREVAVKVFRENSPRG-----CKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCE-WTLEEFLRLP 447
Cdd:cd00180     7 GKVYKARDkeTGKKVAVKVIPKEKLKKlleelLREIEILKKL-NHPNIVKLYDVFETENFLYLVMEYCEgGSLKDLLKEN 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720355205 448 REEPVEngedKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd00180    86 KGPLSE----EEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADF 136
Ank_2 pfam12796
Ankyrin repeats (3 copies);
96-199 5.32e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.39  E-value: 5.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  96 FIIAGIQGDVKLLEILLSCGADVNECDENGFTAFMEAAERGNAEALRFLfAKGANVNLRRQttkdkrrlkqgGATALMSA 175
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDN-----------GRTALHYA 68
                          90       100
                  ....*....|....*....|....
gi 1720355205 176 AEKGHLEVLRILLnDMKAEVDARD 199
Cdd:pfam12796  69 ARSGHLEIVKLLL-EKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
29-119 8.00e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 8.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  29 LIKAVQKGDVVRVQQLLEKGADANaCEDTWGWTPLHNAVQAGRVDIVNLLLSHgADPhRRKKNGATPFIIAGIQGDVKLL 108
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN-LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADV-NLKDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|.
gi 1720355205 109 EILLSCGADVN 119
Cdd:pfam12796  78 KLLLEKGADIN 88
PHA02875 PHA02875
ankyrin repeat protein; Provisional
4-188 2.33e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 85.04  E-value: 2.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205   4 PDYNTPqggtpsagsqrtvvEDDSSLIKAVQKGDVVRVQQLLEKGADANACEDTWGWTPLHNAVQAGRVDIVNLLLSHGA 83
Cdd:PHA02875   61 PDVKYP--------------DIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGA 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  84 DPHRRKKNGATPFIIAGIQGDVKLLEILLSCGADVNECDENGFTAFMEAAERGNAEALRFLFAKGANVNLRRqttkdkrr 163
Cdd:PHA02875  127 DPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFG-------- 198
                         170       180
                  ....*....|....*....|....*
gi 1720355205 164 lKQGGATALMSAAEKGHLEVLRILL 188
Cdd:PHA02875  199 -KNGCVAALCYAIENNKIDIVRLFI 222
PHA03095 PHA03095
ankyrin-like protein; Provisional
118-301 7.32e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 80.84  E-value: 7.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 118 VNECDENGFTAFMEAAERGNAEALRFLFAKGANVNLRrqttkdkrrlKQGGATAL---MSAAEKGHLEVLRILLnDMKAE 194
Cdd:PHA03095    7 VDIIMEAALYDYLLNASNVTVEEVRRLLAAGADVNFR----------GEYGKTPLhlyLHYSSEKVKDIVRLLL-EAGAD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 195 VDARDNMGRNALIRTLLNwdcENVEEITSILIQHGADVNVRGERGKTPLIA--AVERKHTGLVQMLLsREGINIDARDNE 272
Cdd:PHA03095   76 VNAPERCGFTPLHLYLYN---ATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLL-RKGADVNALDLY 151
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1720355205 273 GKT---ALLIAVDKQLkEIVQLLLEKGADKCD 301
Cdd:PHA03095  152 GMTplaVLLKSRNANV-ELLRLLIDAGADVYA 182
Ank_2 pfam12796
Ankyrin repeats (3 copies);
220-299 9.53e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 9.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 220 EITSILIQHGADVNVRGERGKTPLIAAVERKHTGLVQMLLSREGINIdarDNEGKTALLIAVDKQLKEIVQLLLEKGADK 299
Cdd:pfam12796  11 ELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIVKLLLEKGADI 87
PHA02876 PHA02876
ankyrin repeat protein; Provisional
24-304 1.65e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 80.49  E-value: 1.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  24 EDDSSLIKAVQKGDVVRVQQLLEKGADANACEDtWGWTPLHNAVQAGRVD-IVNLLLSHGADPHRRKKNGATPFIIAGIQ 102
Cdd:PHA02876  239 KNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDD-CKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKN 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 103 G-DVKLLEILLSCGADVNECDENGFTAFMEAAERG-NAEALRFLFAKGANVNLRRQTTKdkrrlkqggaTALMSAAEKGH 180
Cdd:PHA02876  318 GyDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDK----------TPIHYAAVRNN 387
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 181 LEVLRILLnDMKAEVDARDNMgrnalIRTLLNWDCENVEEITSI--LIQHGADVNVRGERGKTPLIAAVERK-HTGLVQM 257
Cdd:PHA02876  388 VVIINTLL-DYGADIEALSQK-----IGTALHFALCGTNPYMSVktLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEM 461
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1720355205 258 LLSrEGINIDARDNEGKTALLIAVDKQlkEIVQLLLEKGADKCDDLV 304
Cdd:PHA02876  462 LLD-NGADVNAINIQNQYPLLIALEYH--GIVNILLHYGAELRDSRV 505
PHA03100 PHA03100
ankyrin repeat protein; Provisional
28-271 3.10e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.55  E-value: 3.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  28 SLIKAVQKGDVVRVQQLLEKGADANACeDTWGWTPLHNAVQA--GRVDIVNLLLSHGADPHRRKKNGATPFIIA--GIQG 103
Cdd:PHA03100   76 SNIKYNLTDVKEIVKLLLEYGANVNAP-DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKI 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 104 DVKLLEILLSCGADVNECDEngftafmeaaergnaeaLRFLFAKGANVNlrrqtTKDKRrlkqgGATALMSAAEKGHLEV 183
Cdd:PHA03100  155 DLKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPIN-----IKDVY-----GFTPLHYAVYNNNPEF 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 184 LRILLNdmkaevdardnmgrnalirtllnwdcenveeitsiliqHGADVNVRGERGKTPLIAAVERKHTGLVQMLLSReG 263
Cdd:PHA03100  208 VKYLLD--------------------------------------LGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNN-G 248

                  ....*...
gi 1720355205 264 INIDARDN 271
Cdd:PHA03100  249 PSIKTIIE 256
PHA02876 PHA02876
ankyrin repeat protein; Provisional
23-298 3.75e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 79.34  E-value: 3.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  23 VEDDSSLIKAVQKGDVVRVQQLLEKGADANAcEDTWGWTPLHNAVQAGRVDIVNLLLSHGADPHRRKKNGATPFIIAGIQ 102
Cdd:PHA02876  143 IEYMKLIKERIQQDELLIAEMLLEGGADVNA-KDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDS 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 103 GDVKLLEILLSCGADVNECDengfTAFMEAAERGNAEALRFLFAKGANVNlrrqTTKDKRRlkqggaTALMSAAEKGHLE 182
Cdd:PHA02876  222 KNIDTIKAIIDNRSNINKND----LSLLKAIRNEDLETSLLLYDAGFSVN----SIDDCKN------TPLHHASQAPSLS 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 183 VLRILLNDMKAEVDARDNMGRNALIRTLLN-WDCENVEeitsILIQHGADVNVRGERGKTPLIAAVERKHTGLVQMLLSR 261
Cdd:PHA02876  288 RLVPKLLERGADVNAKNIKGETPLYLMAKNgYDTENIR----TLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLE 363
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1720355205 262 EGINIDARDNEGKTALLIAVDKQLKEIVQLLLEKGAD 298
Cdd:PHA02876  364 LGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
376-502 1.16e-14

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: 74.11  E-value: 1.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIYDNREVAVKVFRENSPRG------CKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEW-TLEEFLRlpR 448
Cdd:cd13999     7 GEVYKGKWRGTDVAIKKLKVEDDNDellkefRREVSILSKL-RHPNIVQFIGACLSPPPLCIVTEYMPGgSLYDLLH--K 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720355205 449 EEPVENGEDKFahSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd13999    84 KKIPLSWSLRL--KIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADF 135
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
369-517 1.37e-14

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: 74.65  E-value: 1.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 369 KIAGTSEGAVYLGI-YDNREV-AVKV--FRENSPRGCKEV-------SCLrdcgDHSNLVAFYGREDDKGCLYVCVSLC- 436
Cdd:cd06626     7 KIGEGTFGKVYTAVnLDTGELmAMKEirFQDNDPKTIKEIademkvlEGL----DHPNLVRYYGVEVHREEVYIFMEYCq 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 437 EWTLEEFLRLPREEPvENGEDKFAHSILlsifEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSIRWMGESQMVR 516
Cdd:cd06626    83 EGTLEELLRHGRILD-EAVIRVYTLQLL----EGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNNTTTMA 157

                  .
gi 1720355205 517 R 517
Cdd:cd06626   158 P 158
PHA02874 PHA02874
ankyrin repeat protein; Provisional
21-298 2.02e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 76.16  E-value: 2.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  21 TVVEDDSSLIKAVQKGDVVRVQQLLEKGADANACeDTWGWTPLHNAVQAGRVDIVNLLLSHGADphrrkkngATPFIIAG 100
Cdd:PHA02874   31 SVDETTTPLIDAIRSGDAKIVELFIKHGADINHI-NTKIPHPLLTAIKIGAHDIIKLLIDNGVD--------TSILPIPC 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 101 IQGDvkLLEILLSCGADVNECDENGFTAFMEAAERGNAEALRFLFAKGANVNLRrqttkdkrrlKQGGATALMSAAEKGH 180
Cdd:PHA02874  102 IEKD--MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIE----------DDNGCYPIHIAIKHNF 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 181 LEVLRILLNDmKAEVDARDNMGRNALIRTLLNWDCENVEeitsILIQHGADVNVRGERGKTPLIAAVERKHTgLVQMLLS 260
Cdd:PHA02874  170 FDIIKLLLEK-GAYANVKDNNGESPLHNAAEYGDYACIK----LLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLIN 243
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1720355205 261 REGINIdaRDNEGKTALLIAVDKQL-KEIVQLLLEKGAD 298
Cdd:PHA02874  244 NASIND--QDIDGSTPLHHAINPPCdIDIIDILLYHKAD 280
PHA02875 PHA02875
ankyrin repeat protein; Provisional
63-329 3.67e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 75.03  E-value: 3.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  63 LHNAVQAGRVDIVNLLLSHGADPHRRKKNGATPFIIAGIQGDVKLLEILLSCGA--DVNECDENgfTAFMEAAERGNAEA 140
Cdd:PHA02875    6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIE--SELHDAVEEGDVKA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 141 LRFLFAKGANVNlrrqttkdkRRLKQGGATALMSAAEKGHLEVLRILLNdMKAEVDARDNMGRNALIRTLLNWDCENVEe 220
Cdd:PHA02875   84 VEELLDLGKFAD---------DVFYKDGMTPLHLATILKKLDIMKLLIA-RGADPDIPNTDKFSPLHLAVMMGDIKGIE- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 221 itsILIQHGADVNVRGERGKTPLIAAVERKHTGLVQMLLSrEGINIDARDNEGKTALL-IAVDKQLKEIVQLLLEKGADk 299
Cdd:PHA02875  153 ---LLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLD-SGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGAD- 227
                         250       260       270
                  ....*....|....*....|....*....|
gi 1720355205 300 CDDLVWIarRNHDYHLVKLLLPYVANPDTD 329
Cdd:PHA02875  228 CNIMFMI--EGEECTILDMICNMCTNLESE 255
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
352-502 1.10e-13

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 74.28  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 352 MTRPMIGKLKIfihdDYKIAGTSEGAVYLG--IYDNREVAVKVFRENSPRGCKEVSCLRD----CG--DHSNLVAFYGRE 423
Cdd:COG0515     1 MSALLLGRYRI----LRLLGRGGMGVVYLArdLRLGRPVALKVLRPELAADPEARERFRRearaLArlNHPNIVRVYDVG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 424 DDKGCLYVC------VSLCEWtLEEFLRLPREEpvengedkfAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAV 497
Cdd:COG0515    77 EEDGRPYLVmeyvegESLADL-LRRRGPLPPAE---------ALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRV 146

                  ....*
gi 1720355205 498 RLADF 502
Cdd:COG0515   147 KLIDF 151
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
374-507 1.82e-13

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: 71.01  E-value: 1.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 374 SEGAVYLGIYDN--REVAVKV--FRENSPRG----CKEVSCLRDCgDHSNLVAFYGREDDKGCLYVcvsLCEWT------ 439
Cdd:cd06606    12 SFGSVYLALNLDtgELMAVKEveLSGDSEEElealEREIRILSSL-KHPNIVRYLGTERTENTLNI---FLEYVpggsla 87
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 440 --LEEFLRLPreEPVENgedKFAHSILlsifEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSIR 507
Cdd:cd06606    88 slLKKFGKLP--EPVVR---KYTRQIL----EGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKR 148
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
3-125 1.94e-12

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 70.70  E-value: 1.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205   3 TPDYN-TPQGGTPSAGSQRTVVEddssLIKAVQKGDVVRVQQLLEKGADANaCEDTWGWTPLHNAVQAGRVDIVNLLLSH 81
Cdd:PTZ00322   63 TPDHNlTTEEVIDPVVAHMLTVE----LCQLAASGDAVGARILLTGGADPN-CRDYDGRTPLHIACANGHVQVVRVLLEF 137
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1720355205  82 GADPHRRKKNGATPFIIAGIQGDVKLLEILLSCGADVNECDENG 125
Cdd:PTZ00322  138 GADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANA 181
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
376-502 2.33e-12

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: 67.94  E-value: 2.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIY--DNREVAVKVFRE--NSPRGC---KEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVSLCEWTLEEFLRLPR 448
Cdd:cd07830    13 GSVYLARNkeTGELVAIKKMKKkfYSWEECmnlREVKSLRKLNEHPNIVKLKEVFRENDELYFVFEYMEGNLYQLMKDRK 92
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720355205 449 EEPVENGEDKfahSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd07830    93 GKPFSESVIR---SIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADF 143
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
376-502 2.70e-12

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: 67.61  E-value: 2.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIY--DNREVAVKVFRENSPRG----CKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEW-TLEEFLRLpR 448
Cdd:cd05122    14 GVVYKARHkkTGQIVAIKKINLESKEKkesiLNEIAILKKC-KHPNIVKYYGSYLKKDELWIVMEFCSGgSLKDLLKN-T 91
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720355205 449 EEPVEngEDKFAhSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd05122    92 NKTLT--EQQIA-YVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDF 142
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
17-197 3.61e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 69.90  E-value: 3.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  17 GSQRTVVEDDSSLIKAVQKGDVVRVQQLLEKGADANAcEDTWGWTPLHNAVQAGRVDIVNLLLSHGADPHRRKKNGATPF 96
Cdd:PLN03192  517 GGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDI-GDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL 595
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  97 IIAGIQGDVKLLEILLSCGADVNEcdENGFTAFMEAAERGNAEALRFLFAKGANVNlrrqtTKDKRrlkqgGATALMSAA 176
Cdd:PLN03192  596 WNAISAKHHKIFRILYHFASISDP--HAAGDLLCTAAKRNDLTAMKELLKQGLNVD-----SEDHQ-----GATALQVAM 663
                         170       180
                  ....*....|....*....|.
gi 1720355205 177 EKGHLEVLRILLNDmKAEVDA 197
Cdd:PLN03192  664 AEDHVDMVRLLIMN-GADVDK 683
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
376-502 5.19e-12

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: 66.80  E-value: 5.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  376 GAVYLGIYDNR------EVAVKVFRENSPRG-----CKEVSCLRDCgDHSNLVAFYG--REDDKgcLYVCVSLCEW-TLE 441
Cdd:smart00221  13 GEVYKGTLKGKgdgkevEVAVKTLKEDASEQqieefLREARIMRKL-DHPNIVKLLGvcTEEEP--LMIVMEYMPGgDLL 89
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720355205  442 EFLRLPREEPVENGEdkfAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:smart00221  90 DYLRKNRPKELSLSD---LLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDF 147
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
376-502 7.95e-12

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 66.02  E-value: 7.95e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  376 GAVYLGIYDNR------EVAVKVFRENSPRG-----CKEVSCLRDCgDHSNLVAFYG--REDDKgcLYVCVSLCEW-TLE 441
Cdd:smart00219  13 GEVYKGKLKGKggkkkvEVAVKTLKEDASEQqieefLREARIMRKL-DHPNVVKLLGvcTEEEP--LYIVMEYMEGgDLL 89
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720355205  442 EFLRLPReepvengeDKFAHSILLS----IFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:smart00219  90 SYLRKNR--------PKLSLSDLLSfalqIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDF 146
PHA02878 PHA02878
ankyrin repeat protein; Provisional
62-327 1.08e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.60  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  62 PLHNAVQAGRVDIVNLLLSHGADPHRRKKNGATPFIIAGIQGDVKLLEILLScgaDVNECD-ENGFTAFMEAAERGNAEA 140
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR---SINKCSvFYTLVAIKDAFNNRNVEI 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 141 LRFLFAKganvNLRRQTTKDKRRLKQGGATALMSAaekghlEVLRILLnDMKAEVDARDnmgRNALiRTLLNWDCENVE- 219
Cdd:PHA02878  117 FKIILTN----RYKNIQTIDLVYIDKKSKDDIIEA------EITKLLL-SYGADINMKD---RHKG-NTALHYATENKDq 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 220 EITSILIQHGADVNVRGERGKTPLIAAVERKHTGLVQMLLsREGINIDARDNEGKTALLIAVDKQLK-EIVQLLLEKGAD 298
Cdd:PHA02878  182 RLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILL-ENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVD 260
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1720355205 299 -----KCDDLVWIARRNHDYHLVKLLLPYVANPD 327
Cdd:PHA02878  261 vnaksYILGLTALHSSIKSERKLKLLLEYGADIN 294
PHA02874 PHA02874
ankyrin repeat protein; Provisional
41-248 1.15e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 67.30  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  41 VQQLLEKGADANAcEDTWGWTPLHNAVQAGRVDIVNLLLSHGADPHRRKKNGATPFIIAGIQGDVKLLEILLSCGADVNE 120
Cdd:PHA02874  107 IKTILDCGIDVNI-KDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 121 CDENGFTAFMEAAERGNAEALRFLFAKGANVnlrrqTTKDKRrlkqgGATALMSAAEKGHlEVLRILLNDmkAEVDARDN 200
Cdd:PHA02874  186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHI-----MNKCKN-----GFTPLHNAIIHNR-SAIELLINN--ASINDQDI 252
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1720355205 201 MGRNALiRTLLNWDCEnvEEITSILIQHGADVNVRGERGKTPLIAAVE 248
Cdd:PHA02874  253 DGSTPL-HHAINPPCD--IDIIDILLYHKADISIKDNKGENPIDTAFK 297
PUG smart00580
domain in protein kinases, N-glycanases and other nuclear proteins;
657-707 1.86e-11

domain in protein kinases, N-glycanases and other nuclear proteins;


Pssm-ID: 197798  Cd Length: 57  Bit Score: 59.62  E-value: 1.86e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720355205  657 TVGDLLKFIRNIGEHINEEK-----KRGMKEILGDPSRYFQETFPDLVIY-IYKKLK 707
Cdd:smart00580   1 SVRDLLRALRNILHHPREEKgnpaiKERLGPVPGGFELYFTVGFPRLLISeVYTLPK 57
PHA02878 PHA02878
ankyrin repeat protein; Provisional
73-302 3.03e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.44  E-value: 3.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  73 DIVNLLLSHGADPHRRKKN-GATPFIIAGIQGDVKLLEILLSCGADVNECDENGFTAFMEAAERGNAEALRFLFAKGANV 151
Cdd:PHA02878  148 EITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 152 NLRRQTtkdkrrlkqgGATAL-MSAAEKGHLEVLRILLnDMKAEVDARDN-MGRNALIRTLLNwdcenvEEITSILIQHG 229
Cdd:PHA02878  228 DARDKC----------GNTPLhISVGYCKDYDILKLLL-EHGVDVNAKSYiLGLTALHSSIKS------ERKLKLLLEYG 290
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 230 ADVNVRGERGKTPLIAAVeRKHTG------LVQMLLSREGINIDARDNEG--KTALLIAVDKQLKEIvqlllekgADKCD 301
Cdd:PHA02878  291 ADINSLNSYKLTPLSSAV-KQYLCinigriLISNICLLKRIKPDIKNSEGfiDNMDCITSNKRLNQI--------KDKCE 361

                  .
gi 1720355205 302 D 302
Cdd:PHA02878  362 D 362
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
369-502 6.76e-11

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: 63.38  E-value: 6.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 369 KIAGTSEGAVYLGIY--DNREVAVKVFRENSPRG---CKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEW-TLEE 442
Cdd:cd06614     7 KIGEGASGEVYKATDraTGKEVAIKKMRLRKQNKeliINEILIMKEC-KHPNIVDYYDSYLVGDELWVVMEYMDGgSLTD 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 443 FLRlprEEPVENGEDKFAhSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd06614    86 IIT---QNPVRMNESQIA-YVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADF 141
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
372-502 7.22e-11

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: 63.66  E-value: 7.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 372 GTSeGAVYLG--IYDNREVAVKVFR-ENSPRG-----CKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEWTLEEF 443
Cdd:cd07829    10 GTY-GVVYKAkdKKTGEIVALKKIRlDNEEEGipstaLREISLLKEL-KHPNIVKLLDVIHTENKLYLVFEYCDQDLKKY 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720355205 444 LRLpREEPVENGEDKfahSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd07829    88 LDK-RPGPLPPNLIK---SIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADF 142
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
374-538 1.18e-10

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: 62.13  E-value: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 374 SEGAVYLGIYDNREVAVKVFRENSPRGCKEVSCLrdcgDHSNLVAFYGREDDKGCLYVCVSLCEW-TLEEFLRLPREEPv 452
Cdd:cd14059     5 AQGAVFLGKFRGEEVAVKKVRDEKETDIKHLRKL----NHPNIIKFKGVCTQAPCYCILMEYCPYgQLYEVLRAGREIT- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 453 engedkfaHSILLS----IFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQS---------------IRWMGeSQ 513
Cdd:cd14059    80 --------PSLLVDwskqIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSkelsekstkmsfagtVAWMA-PE 150
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1720355205 514 MVRR-------DLEDLGrLVLYVVMKGEIPFE 538
Cdd:cd14059   151 VIRNepcsekvDIWSFG-VVLWELLTGEIPYK 181
Ank_2 pfam12796
Ankyrin repeats (3 copies);
29-88 1.37e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.20  E-value: 1.37e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  29 LIKAVQKGDVVRVQQLLEKgADANACEDtwGWTPLHNAVQAGRVDIVNLLLSHGADPHRR 88
Cdd:pfam12796  34 LHLAAKNGHLEIVKLLLEH-ADVNLKDN--GRTALHYAARSGHLEIVKLLLEKGADINVK 90
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
376-548 1.45e-10

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: 62.56  E-value: 1.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIYDN-----REVAVKVFRENSPRG-----CKEVSCLRDCGdHSNLVAFYGREDDKGCLYVCVSLCEWT-LEEFL 444
Cdd:cd00192     9 GEVYKGKLKGgdgktVDVAVKTLKEDASESerkdfLKEARVMKKLG-HPNVVRLLGVCTEEEPLYLVMEYMEGGdLLDFL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 445 RLPREEPVENGEDKFAHSILLS----IFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF--------DQS------- 505
Cdd:cd00192    88 RKSRPVFPSPEPSTLSLKDLLSfaiqIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFglsrdiydDDYyrkktgg 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720355205 506 ---IRWMG-ESqmvrrdLED-----------LGrLVLY-VVMKGEIPFETLKtqNDEVL 548
Cdd:cd00192   168 klpIRWMApES------LKDgiftsksdvwsFG-VLLWeIFTLGATPYPGLS--NEEVL 217
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
376-514 1.65e-10

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: 62.22  E-value: 1.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGI--YDNREVAVKVFRE---NSPRGCK----EVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEW-TLEEFLR 445
Cdd:cd14014    14 GEVYRARdtLLGRPVAIKVLRPelaEDEEFRErflrEARALARL-SHPNIVRVYDVGEDDGRPYIVMEYVEGgSLADLLR 92
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720355205 446 lpREEPVENGEdkfAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSiRWMGESQM 514
Cdd:cd14014    93 --ERGPLPPRE---ALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIA-RALGDSGL 155
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
369-502 1.76e-10

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: 61.87  E-value: 1.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 369 KIAGTSEGAVYLGiYD---NREVAVKVFRENSP---RGCKEVS---CLRDCGDHSNLVAFYGREDDKGCLYVCV--SLCE 437
Cdd:cd05118     6 KIGEGAFGTVWLA-RDkvtGEKVAIKKIKNDFRhpkAALREIKllkHLNDVEGHPNIVKLLDVFEHRGGNHLCLvfELMG 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355205 438 WTLEEFLRLpREEPVENgedKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKK-AVRLADF 502
Cdd:cd05118    85 MNLYELIKD-YPRGLPL---DLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELgQLKLADF 146
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
367-537 1.94e-10

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: 61.96  E-value: 1.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 367 DYKIAGT-SEGA---VYLGIYDNRE--VAVKVF-----RENSPRGCKEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVSL 435
Cdd:cd14069     2 DWDLVQTlGEGAfgeVFLAVNRNTEeaVAVKFVdmkraPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 436 CEWTlEEFLRLpreEPvENG-EDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFdqsirwmGESQM 514
Cdd:cd14069    82 ASGG-ELFDKI---EP-DVGmPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDF-------GLATV 149
                         170       180
                  ....*....|....*....|...
gi 1720355205 515 VRRDledlGRLVLYVVMKGEIPF 537
Cdd:cd14069   150 FRYK----GKERLLNKMCGTLPY 168
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
376-564 3.74e-10

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: 61.42  E-value: 3.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLG--IYDNREVAVKVF----------RENSPRGCK--------EVSCLRDCgDHSNLVAFYGREDD--KGCLYVCV 433
Cdd:cd14008     7 GKVKLAldTETGQLYAIKIFnksrlrkrreGKNDRGKIKnalddvrrEIAIMKKL-DHPNIVRLYEVIDDpeSDKLYLVL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 434 SLCEwtLEEFLRLPREEPVENGEDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFdqsirwmGESQ 513
Cdd:cd14008    86 EYCE--GGPVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDF-------GVSE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 514 MVRRDLEDL-----------------------GRLV--------LYVVMKGEIPF---------ETLKTQNDEVLLTMSP 553
Cdd:cd14008   157 MFEDGNDTLqktagtpaflapelcdgdsktysGKAAdiwalgvtLYCLVFGRLPFngdnilelyEAIQNQNDEFPIPPEL 236
                         250
                  ....*....|..
gi 1720355205 554 DEETKDLI-HCL 564
Cdd:cd14008   237 SPELKDLLrRML 248
PHA03100 PHA03100
ankyrin repeat protein; Provisional
40-124 5.23e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 62.38  E-value: 5.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  40 RVQQLLEKGADANAcEDTWGWTPLHNAVQAGRVDIVNLLLSHGADPHRRKKNGATPFIIAGIQGDVKLLEILLSCGADVN 119
Cdd:PHA03100  174 RVNYLLSYGVPINI-KDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252

                  ....*
gi 1720355205 120 ECDEN 124
Cdd:PHA03100  253 TIIET 257
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
412-584 7.38e-10

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: 60.26  E-value: 7.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 412 DHSNLVAFYGREDDKGCLYVCVSLCE-WTLEEFLRlpREEPVENGEDKFahsILLSIFEGVQKLHLHGYSHQDLQPQNIL 490
Cdd:cd14099    59 KHPNIVKFHDCFEDEENVYILLELCSnGSLMELLK--RRKALTEPEVRY---FMRQILSGVKYLHSNRIIHRDLKLGNLF 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 491 IDSKKAVRLADFDQSIRWM-------------------------GESQMVrrDLEDLGrLVLYVVMKGEIPFET--LKT- 542
Cdd:cd14099   134 LDENMNVKIGDFGLAARLEydgerkktlcgtpnyiapevlekkkGHSFEV--DIWSLG-VILYTLLVGKPPFETsdVKEt 210
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1720355205 543 -----QND-EVLLTMSPDEETKDLIHCLFSPGENVKNCLVDLLGHPFF 584
Cdd:cd14099   211 ykrikKNEySFPSHLSISDEAKDLIRSMLQPDPTKRPSLDEILSHPFF 258
PHA02875 PHA02875
ankyrin repeat protein; Provisional
29-153 8.47e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.55  E-value: 8.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  29 LIKAVQKGDVVRVqqLLEKGADANAcEDTWGWTPLHNAVQAGRVDIVNLLLSHGADPHRRKKNGATPFIIAGIQGDVKLL 108
Cdd:PHA02875  108 LATILKKLDIMKL--LIARGADPDI-PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAIC 184
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720355205 109 EILLSCGADVNECDENGFTAFM-EAAERGNAEALRFLFAKGANVNL 153
Cdd:PHA02875  185 KMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGADCNI 230
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
376-502 9.32e-10

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: 59.82  E-value: 9.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIYD------NREVAVKVFRENSPRG-----CKEVSCLRDcGDHSNLVAFYG--REDDKgcLYVCVSLCEW-TLE 441
Cdd:pfam07714  13 GEVYKGTLKgegentKIKVAVKTLKEGADEEeredfLEEASIMKK-LDHPNIVKLLGvcTQGEP--LYIVTEYMPGgDLL 89
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720355205 442 EFLRLPREepvengedKFAHSILLS----IFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:pfam07714  90 DFLRKHKR--------KLTLKDLLSmalqIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDF 146
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
367-505 1.02e-09

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: 60.42  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 367 DYKIAG-TSEGA-----VYLGIYDNREVAVKVFRENSPRGC------KEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVS 434
Cdd:cd07832     1 RYKILGrIGEGAhgivfKAKDRETGETVALKKVALRKLEGGipnqalREIKALQACQGHPYVVKLRDVFPHGTGFVLVFE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720355205 435 LCEWTLEEFLRlPREEPVENGEDKfahSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQS 505
Cdd:cd07832    81 YMLSSLSEVLR-DEERPLTEAQVK---RYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLA 147
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
471-589 1.16e-09

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: 60.85  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 471 VQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSIRwMGESQMVRRD-------------LEDLGR------------- 524
Cdd:cd05596   138 LDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCMK-MDKDGLVRSDtavgtpdyispevLKSQGGdgvygrecdwwsv 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 525 -LVLYVVMKGEIPF--ETL-----KTQNDEVLLTMSPD----EETKDLIhCLFSPGENV---KNCLVDLLGHPFF----W 585
Cdd:cd05596   217 gVFLYEMLVGDTPFyaDSLvgtygKIMNHKNSLQFPDDveisKDAKSLI-CAFLTDREVrlgRNGIEEIKAHPFFkndqW 295

                  ....
gi 1720355205 586 TWEN 589
Cdd:cd05596   296 TWDN 299
Ank_4 pfam13637
Ankyrin repeats (many copies);
59-112 2.27e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 2.27e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720355205  59 GWTPLHNAVQAGRVDIVNLLLSHGADPHRRKKNGATPFIIAGIQGDVKLLEILL 112
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
384-502 2.41e-09

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: 59.04  E-value: 2.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 384 DNREVAVKVFRENSPRGCKEVSCLRDCgDHSNLVAFYGREDD----------------KGCLYVCVSLCE-WTLEEFLRL 446
Cdd:cd14047    30 DGKTYAIKRVKLNNEKAEREVKALAKL-DHPNIVRYNGCWDGfdydpetsssnssrskTKCLFIQMEFCEkGTLESWIEK 108
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355205 447 PREEPVENGEdkfAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd14047   109 RNGEKLDKVL---ALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDF 161
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
376-502 2.45e-09

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: 58.90  E-value: 2.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLG--IYDNREVAVKVFRENSPRGC-----------KEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVSLCEWT-LE 441
Cdd:cd13993    14 GVVYLAvdLRTGRKYAIKCLYKSGPNSKdgndfqklpqlREIDLHRRVSRHPNIITLHDVFETEVAIYIVLEYCPNGdLF 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720355205 442 EFLRLPReepVENGEDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILID-SKKAVRLADF 502
Cdd:cd13993    94 EAITENR---IYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSqDEGTVKLCDF 152
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
384-502 2.95e-09

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: 58.47  E-value: 2.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 384 DNREVAVKVFRE------NSPRGCKEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVSLCEWTLEEFL----RLPREEpve 453
Cdd:cd14050    25 DGKLYAVKRSRSrfrgekDRKRKLEEVERHEKLGEHPNCVRFIKAWEEKGILYIQTELCDTSLQQYCeethSLPESE--- 101
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1720355205 454 ngedkfAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd14050   102 ------VWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDF 144
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
376-584 3.36e-09

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: 58.14  E-value: 3.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLgIYD---NREVAVKVFR--ENSPRGCKEVSCLrDCG-------DHSNLVAFYGREDDKGCLYVCVSLCEW-TLEE 442
Cdd:cd06625    14 GQVYL-CYDadtGRELAVKQVEidPINTEASKEVKAL-ECEiqllknlQHERIVQYYGCLQDEKSLSIFMEYMPGgSVKD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 443 FLRL--PREEPVENgedKFAHSILlsifEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFD-----QSIR-------- 507
Cdd:cd06625    92 EIKAygALTENVTR---KYTRQIL----EGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGaskrlQTICsstgmksv 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 508 -----WM------GESQMVRRDLEDLGRLVlyVVMKGEIP----FETLK------TQNDEVLLTMSPDEETKDLIHCLFS 566
Cdd:cd06625   165 tgtpyWMspevinGEGYGRKADIWSVGCTV--VEMLTTKPpwaeFEPMAaifkiaTQPTNPQLPPHVSEDARDFLSLIFV 242
                         250
                  ....*....|....*...
gi 1720355205 567 PGENVKNCLVDLLGHPFF 584
Cdd:cd06625   243 RNKKQRPSAEELLSHSFV 260
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
474-589 3.67e-09

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: 58.90  E-value: 3.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 474 LHLHGYSHQDLQPQNILIDSKKAVRLADFDQSIRwMGESQMVR----------------RDLED-------------LGr 524
Cdd:cd05597   118 IHQLGYVHRDIKPDNVLLDRNGHIRLADFGSCLK-LREDGTVQssvavgtpdyispeilQAMEDgkgrygpecdwwsLG- 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 525 LVLYVVMKGEIPF--ETL-----KTQNDEVLLTMSPD-----EETKDLIHCLFSPGENV--KNCLVDLLGHPFFW--TWE 588
Cdd:cd05597   196 VCMYEMLYGETPFyaESLvetygKIMNHKEHFSFPDDeddvsEEAKDLIRRLICSRERRlgQNGIDDFKKHPFFEgiDWD 275

                  .
gi 1720355205 589 N 589
Cdd:cd05597   276 N 276
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
367-502 4.60e-09

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: 57.66  E-value: 4.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 367 DYKIAGTSEGAVYLGIY--DNREVAVKVFR--ENSPRGCKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEW-TLE 441
Cdd:cd06612     8 LEKLGEGSYGSVYKAIHkeTGQVVAIKVVPveEDLQEIIKEISILKQC-DSPYIVKYYGSYFKNTDLWIVMEYCGAgSVS 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720355205 442 EFLRLpREEPVEngEDKFAhSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd06612    87 DIMKI-TNKTLT--EEEIA-AILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADF 143
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
366-502 4.80e-09

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: 57.75  E-value: 4.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 366 DDYK----IAGTSEGAVYLGIY--DNREVAVKVF-----RENSPRGCKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVS 434
Cdd:cd06610     1 DDYElievIGSGATAVVYAAYClpKKEKVAIKRIdlekcQTSMDELRKEIQAMSQC-NHPNVVSYYTSFVVGDELWLVMP 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720355205 435 LCEW-TLEEFLRlpREEPVENGEDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd06610    80 LLSGgSLLDIMK--SSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADF 146
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
367-562 5.39e-09

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: 57.53  E-value: 5.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 367 DYKIAGT----SEGAVYLGIY--DNREVAVKV-----FRENSPRGCK-EVSCLRDCgDHSNLVAFYGREDDKGCLYVCVS 434
Cdd:cd14003     1 NYELGKTlgegSFGKVKLARHklTGEKVAIKIidkskLKEEIEEKIKrEIEIMKLL-NHPNIIKLYEVIETENKIYLVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 435 LCEWT-----LEEFLRLPREEpvengedkfAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSIRWM 509
Cdd:cd14003    80 YASGGelfdyIVNNGRLSEDE---------ARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 510 GESQ--------------MVRRDLED--------LGrLVLYVVMKGEIPFEtlkTQNDEVLL------------TMSPDe 555
Cdd:cd14003   151 GGSLlktfcgtpayaapeVLLGRKYDgpkadvwsLG-VILYAMLTGYLPFD---DDNDSKLFrkilkgkypipsHLSPD- 225

                  ....*..
gi 1720355205 556 eTKDLIH 562
Cdd:cd14003   226 -ARDLIR 231
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
376-536 5.40e-09

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: 57.78  E-value: 5.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIYDNREVAVKVFR--------ENSPRGCKEVSCLRdcgdHSNLVAFYGRE--DDKGCL-YVCVSLC-EWTLEEF 443
Cdd:cd13979    17 GSVYKATYKGETVAVKIVRrrrknrasRQSFWAELNAARLR----HENIVRVLAAEtgTDFASLgLIIMEYCgNGTLQQL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 444 L-----RLPREEPVEngedkfahsILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSIRwMGESQMVRRD 518
Cdd:cd13979    93 IyegsePLPLAHRIL---------ISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVK-LGEGNEVGTP 162
                         170       180
                  ....*....|....*....|.
gi 1720355205 519 LEDLGRLVLYV---VMKGEIP 536
Cdd:cd13979   163 RSHIGGTYTYRapeLLKGERV 183
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
384-508 6.14e-09

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: 57.39  E-value: 6.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 384 DNREVAVK----VFRENSPRG--CKEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVSLCEW-TLEEFL-RLPREEPVENG 455
Cdd:cd13997    24 DGCLYAVKkskkPFRGPKERAraLREVEAHAALGQHPNIVRYYSSWEEGGHLYIQMELCENgSLQDALeELSPISKLSEA 103
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720355205 456 EDKfahSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSIRW 508
Cdd:cd13997   104 EVW---DLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRL 153
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
370-541 6.94e-09

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: 57.15  E-value: 6.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 370 IAGTSEGAVYLGIYDNREVAVKVFRENS-------PRGCKEVSCLrDCGDHSNLVAFYGREDDKGCLYVCVSLCEWTLEE 442
Cdd:cd14064     1 IGSGSFGKVYKGRCRNKIVAIKRYRANTycsksdvDMFCREVSIL-CRLNHPCVIQFVGACLDDPSQFAIVTQYVSGGSL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 443 FLRLPREEPVENGEDKFahSILLSIFEGVQKLH--LHGYSHQDLQPQNILIDSKKAVRLADFDQS--------------- 505
Cdd:cd14064    80 FSLLHEQKRVIDLQSKL--IIAVDVAKGMEYLHnlTQPIIHRDLNSHNILLYEDGHAVVADFGESrflqsldednmtkqp 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1720355205 506 --IRWMGE---SQMVRRDLE-DLGR--LVLYVVMKGEIPFETLK 541
Cdd:cd14064   158 gnLRWMAPevfTQCTRYSIKaDVFSyaLCLWELLTGEIPFAHLK 201
PHA02876 PHA02876
ankyrin repeat protein; Provisional
51-298 7.05e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.31  E-value: 7.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  51 ANACED-TWGWTPLHNAVQAGRVDIVNLLLSHGAD-----PHRRKKNGATPFIIAGI----------------------- 101
Cdd:PHA02876   32 ANQCENeSIPFTAIHQALQLRQIDIVEEIIQQNPEliyitDHKCHSTLHTICIIPNVmdivisltldcdiildikyasii 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 102 -------------------------------------------QGDVKLLEILLSCGADVNECDENGFTAFMEAAERGNA 138
Cdd:PHA02876  112 lnkhkldeacihilkeaisgndihydkinesieymklikeriqQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNA 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 139 EALRFLFAKGANVNLrrqttkdkrrLKQGGATALMSAAEKGHLEVLrillndmKAEVDARDNMGRN--ALIRTLLNWDCE 216
Cdd:PHA02876  192 KMVNLLLSYGADVNI----------IALDDLSVLECAVDSKNIDTI-------KAIIDNRSNINKNdlSLLKAIRNEDLE 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 217 nveeiTSILI-QHGADVNVRGERGKTPLIAAVERKH-TGLVQMLLSReGINIDARDNEGKTAL-LIAVDKQLKEIVQLLL 293
Cdd:PHA02876  255 -----TSLLLyDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLER-GADVNAKNIKGETPLyLMAKNGYDTENIRTLI 328

                  ....*
gi 1720355205 294 EKGAD 298
Cdd:PHA02876  329 MLGAD 333
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
376-502 1.07e-08

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: 56.92  E-value: 1.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYL--GIYDNREVAVKVFR-----ENSPRGCKEVSCLRdCGDHSNLVAFYGREDDKGCLYVCVSLCE-WTLEEFLRLP 447
Cdd:cd13996    20 GSVYKvrNKVDGVTYAIKKIRlteksSASEKVLREVKALA-KLNHPNIVRYYTAWVEEPPLYIQMELCEgGTLRDWIDRR 98
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355205 448 REEpvENGEDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSK-KAVRLADF 502
Cdd:cd13996    99 NSS--SKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDdLQVKIGDF 152
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
166-314 1.14e-08

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 58.55  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 166 QGGATALMSAAEKGHL-EVLRILLNDMKAEVDARDNMGRNALIRTLLnwdcENV-EEITSILIQHgadvNVRGERGKTPL 243
Cdd:TIGR00870  15 SDEEKAFLPAAERGDLaSVYRDLEEPKKLNINCPDRLGRSALFVAAI----ENEnLELTELLLNL----SCRGAVGDTLL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 244 IAAVERKHTGlVQMLLSREGINIDARDN-------------EGKTALLIAVDKQLKEIVQLLLEKGAD-----KCDDLVW 305
Cdd:TIGR00870  87 HAISLEYVDA-VEAILLHLLAAFRKSGPlelandqytseftPGITALHLAAHRQNYEIVKLLLERGASvparaCGDFFVK 165

                  ....*....
gi 1720355205 306 IARRNHDYH 314
Cdd:TIGR00870 166 SQGVDSFYH 174
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
376-502 1.30e-08

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: 56.57  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIYDN--REVAVKV---FRENSPRGC-KEVSCLRDCGDHSNLVAFYG-----REDDKGCLYVcVSLCEWTLEEFL 444
Cdd:cd13985    14 SYVYLAHDVNtgRRYALKRmyfNDEEQLRVAiKEIEIMKRLCGHPNIVQYYDsailsSEGRKEVLLL-MEYCPGSLVDIL 92
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355205 445 RlpreepvENGEDKFAHSILLSIF----EGVQklHLHGYS----HQDLQPQNILIDSKKAVRLADF 502
Cdd:cd13985    93 E-------KSPPSPLSEEEVLRIFyqicQAVG--HLHSQSppiiHRDIKIENILFSNTGRFKLCDF 149
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
187-327 2.20e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.12  E-value: 2.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 187 LLNDMKAEVDARDNMGRNALIRTLLNWDCENVEEITSILIQHGADVNVRGERGKTPLIAAVERKHTGLVQMLLSREGINI 266
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720355205 267 DARDNEGKTALLIAVDKQLKEIVQLLLEKGAD------KCDDLVWIARRNHDYHLVKLLLPYVANPD 327
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADvnardkDGETPLHLAAYNGNLEIVKLLLEAGADVN 147
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
376-502 3.11e-08

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: 55.74  E-value: 3.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLG--IYDNREVAVKVFR-ENSPRGC-----KEVSCLR--DCGDHSNLV----AFYGREDDKGC-LYVCVSLCEWTL 440
Cdd:cd07838    13 GTVYKArdLQDGRFVALKKVRvPLSEEGIplstiREIALLKqlESFEHPNVVrlldVCHGPRTDRELkLTLVFEHVDQDL 92
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720355205 441 EEFL-RLPreEPVEnGEDKFAHsILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd07838    93 ATYLdKCP--KPGL-PPETIKD-LMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADF 151
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
307-502 3.71e-08

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 55.99  E-value: 3.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 307 ARRNHDyhlVKLLLPY----VANPDTDPPAGDWSPHSSrwGTALKSLHSMTRPMIGKLKIFihddYKIAGTSEGAVYLGI 382
Cdd:PLN00034   24 PRRRPD---LTLPLPQrdpsLAVPLPLPPPSSSSSSSS--SSSASGSAPSAAKSLSELERV----NRIGSGAGGTVYKVI 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 383 Y--DNREVAVKVF---RENSPRG--CKEVSCLRDCgDHSNLVAFYGREDDKGCLYVcvslcewtLEEFLRLPREEPVENG 455
Cdd:PLN00034   95 HrpTGRLYALKVIygnHEDTVRRqiCREIEILRDV-NHPNVVKCHDMFDHNGEIQV--------LLEFMDGGSLEGTHIA 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1720355205 456 EDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:PLN00034  166 DEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADF 212
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
374-502 4.03e-08

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: 54.91  E-value: 4.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 374 SEGAVYLGIY--DNREVAVKVFRENSPRG-----CKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEW-TLEEFLR 445
Cdd:cd06623    13 SSGVVYKVRHkpTGKIYALKKIHVDGDEEfrkqlLRELKTLRSC-ESPYVVKCYGAFYKEGEISIVLEYMDGgSLADLLK 91
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355205 446 lpREEPVenGEDKFAhSILLSIFEGVQKLHL-HGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd06623    92 --KVGKI--PEPVLA-YIARQILKGLDYLHTkRHIIHRDIKPSNLLINSKGEVKIADF 144
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
385-550 4.82e-08

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: 55.03  E-value: 4.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 385 NREVAVKVFRENSPRGCKEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVSLCEWTlEEFLRLPREEPVENGEdkfAHSIL 464
Cdd:cd14175    26 NMEYAVKVIDKSKRDPSEEIEILLRYGQHPNIITLKDVYDDGKHVYLVTELMRGG-ELLDKILRQKFFSERE---ASSVL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 465 LSIFEGVQKLHLHGYSHQDLQPQNIL-IDSK---KAVRLADFDQSIRWMGES---------------QMVRR-------D 518
Cdd:cd14175   102 HTICKTVEYLHSQGVVHRDLKPSNILyVDESgnpESLRICDFGFAKQLRAENgllmtpcytanfvapEVLKRqgydegcD 181
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1720355205 519 LEDLGrLVLYVVMKGEIPFETLKTQNDEVLLT 550
Cdd:cd14175   182 IWSLG-ILLYTMLAGYTPFANGPSDTPEEILT 212
Ank_4 pfam13637
Ankyrin repeats (many copies);
94-144 4.86e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 4.86e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720355205  94 TPFIIAGIQGDVKLLEILLSCGADVNECDENGFTAFMEAAERGNAEALRFL 144
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
91-298 5.49e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.41  E-value: 5.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  91 NGATPFIIAGIQGDVKLLEILLSCGADVNECDENGFTAFMEAAERGNAEALRFLFAKGANVNLRrqttkdkrrlKQGGAT 170
Cdd:PLN03192  524 NMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIR----------DANGNT 593
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 171 ALMSAAEKGHLEVLRILLndmkaevdardnmgrnalirtllnwdcenveEITSILIQH-GADVnvrgergktpLIAAVER 249
Cdd:PLN03192  594 ALWNAISAKHHKIFRILY-------------------------------HFASISDPHaAGDL----------LCTAAKR 632
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1720355205 250 KHTGLVQMLLsREGINIDARDNEGKTALLIAVDKQLKEIVQLLLEKGAD 298
Cdd:PLN03192  633 NDLTAMKELL-KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
378-502 6.66e-08

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: 54.15  E-value: 6.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 378 VYLGIYD--NREVAVKVF---------RENSPRgckEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEW-TLEEFLR 445
Cdd:cd14009     9 VWKGRHKqtGEVVAIKEIsrkklnkklQENLES---EIAILKSI-KHPNIVRLYDVQKTEDFIYLVLEYCAGgDLSQYIR 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 446 lpREEPVEngeDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILI--DSKKAV-RLADF 502
Cdd:cd14009    85 --KRGRLP---EAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLstSGDDPVlKIADF 139
Ank_5 pfam13857
Ankyrin repeats (many copies);
44-99 1.12e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 1.12e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355205  44 LLEKGADANACEDTWGWTPLHNAVQAGRVDIVNLLLSHGADPHRRKKNGATPFIIA 99
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
368-502 1.55e-07

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


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 53.55  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 368 YKIAGTSEGA--VYLGIYDNREVAVKVF---RENSPRGCKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCE-WTLE 441
Cdd:cd13992     6 GASSHTGEPKyvKKVGVYGGRTVAIKHItfsRTEKRTILQELNQLKEL-VHDNLNKFIGICINPPNIAVVTEYCTrGSLQ 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720355205 442 EFLrLPREEPVEngeDKFAHSILLSIFEGVQKLHLH-GYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd13992    85 DVL-LNREIKMD---WMFKSSFIKDIVKGMNYLHSSsIGYHGRLKSSNCLVDSRWVVKLTDF 142
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
376-502 1.59e-07

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: 53.73  E-value: 1.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIY--DNREVAVKVFRENSPRGCK---------EVSCLRDCgDHSN---LVAFYGReddKGCLYVCVSLCEWTLE 441
Cdd:cd07841    14 AVVYKARDkeTGRIVAIKKIKLGERKEAKdginftalrEIKLLQEL-KHPNiigLLDVFGH---KSNINLVFEFMETDLE 89
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355205 442 EFLRlpreepvengeDKF-----AH--SILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd07841    90 KVIK-----------DKSivltpADikSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADF 146
Ank_4 pfam13637
Ankyrin repeats (many copies);
27-79 2.05e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 2.05e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720355205  27 SSLIKAVQKGDVVRVQQLLEKGADANACeDTWGWTPLHNAVQAGRVDIVNLLL 79
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAV-DGNGETALHFAASNGNVEVLKLLL 54
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
376-502 2.10e-07

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: 52.85  E-value: 2.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYL--GIYDNREVAVKVFR-ENSPRGCK-----EVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCE-WTLEEFLRL 446
Cdd:cd08215    14 GSAYLvrRKSDGKLYVLKEIDlSNMSEKEReealnEVKLLSKL-KHPNIVKYYESFEENGKLCIVMEYADgGDLAQKIKK 92
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 447 PREEpvengEDKFAHSILLSIF----EGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd08215    93 QKKK-----GQPFPEEQILDWFvqicLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDF 147
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
370-502 2.25e-07

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: 53.05  E-value: 2.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 370 IAGTSEGAVYLGIY-DNREVAVKVFRENSPRGCK-----EVSCLRDCgDHSNLVAFYG--REDDKGCLyVCVSLCEWTLE 441
Cdd:cd14066     1 IGSGGFGTVYKGVLeNGTVVAVKRLNEMNCAASKkefltELEMLGRL-RHPNLVRLLGycLESDEKLL-VYEYMPNGSLE 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355205 442 EFLRLPREEPVENGEDKFahSILLSIFEGVQklHLHGYS-----HQDLQPQNILIDSKKAVRLADF 502
Cdd:cd14066    79 DRLHCHKGSPPLPWPQRL--KIAKGIARGLE--YLHEECpppiiHGDIKSSNILLDEDFEPKLTDF 140
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
376-502 2.35e-07

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: 53.15  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIYDN------REVAVKVFR----ENSPRGCK-EVSCLRDCgDHSNLVAFYGREDDKGCLYVCVsLCEW----TL 440
Cdd:cd05038    18 GSVELCRYDPlgdntgEQVAVKSLQpsgeEQHMSDFKrEIEILRTL-DHEYIVKYKGVCESPGRRSLRL-IMEYlpsgSL 95
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355205 441 EEFLRLPReepvengeDKFAHSILLS----IFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd05038    96 RDYLQRHR--------DQIDLKRLLLfasqICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDF 153
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
369-584 2.43e-07

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: 52.57  E-value: 2.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 369 KIAGTSEGAVYLGIYDN----REVAVKV---------FRENS-PRgckEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVS 434
Cdd:cd14080     7 TIGEGSYSKVKLAEYTKsglkEKVACKIidkkkapkdFLEKFlPR---ELEILRKL-RHPNIIQVYSIFERGSKVFIFME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 435 LCEWT-LEEFLRLpreepveNG---EDKfAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSiRWMG 510
Cdd:cd14080    83 YAEHGdLLEYIQK-------RGalsESQ-ARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFA-RLCP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 511 ESQmvRRDLED----------------------------LGrLVLYVVMKGEIPF------ETLKTQNDEVLLTMS---- 552
Cdd:cd14080   154 DDD--GDVLSKtfcgsaayaapeilqgipydpkkydiwsLG-VILYIMLCGSMPFddsnikKMLKDQQNRKVRFPSsvkk 230
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1720355205 553 PDEETKDLIHCLFSPGENVKNCLVDLLGHPFF 584
Cdd:cd14080   231 LSPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
457-507 3.66e-07

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: 52.36  E-value: 3.66e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720355205 457 DKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSIR 507
Cdd:cd14093   108 EKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATR 158
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
376-502 4.80e-07

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: 52.12  E-value: 4.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIYDNRE--VAVK-VFreNSPRGC-KEVSCLRDCgDHSNLV----AFYGREDDKGCLYVCVSLcEW---TLEEFL 444
Cdd:cd14137    18 GVVYQAKLLETGevVAIKkVL--QDKRYKnRELQIMRRL-KHPNIVklkyFFYSSGEKKDEVYLNLVM-EYmpeTLYRVI 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720355205 445 R--LPREEPVENGEDKfahsiLLS--IFEGVQKLHLHGYSHQDLQPQNILIDSKKAV-RLADF 502
Cdd:cd14137    94 RhySKNKQTIPIIYVK-----LYSyqLFRGLAYLHSLGICHRDIKPQNLLVDPETGVlKLCDF 151
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
399-508 4.93e-07

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: 52.04  E-value: 4.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 399 RGCKEVSCLRD--CGDHSNLVAFYGREDDKGCLYVCVSLCE-WTLEEFLrlprEEPVENG--EDKFAHSILLSIFEGVQK 473
Cdd:cd14052    46 RRLEEVSILREltLDGHDNIVQLIDSWEYHGHLYIQTELCEnGSLDVFL----SELGLLGrlDEFRVWKILVELSLGLRF 121
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1720355205 474 LHLHGYSHQDLQPQNILIDSKKAVRLADFDQSIRW 508
Cdd:cd14052   122 IHDHHFVHLDLKPANVLITFEGTLKIGDFGMATVW 156
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
423-501 5.54e-07

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: 51.76  E-value: 5.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 423 EDDKGCLYVCVSLCEWTLEEFLRLPREEPVENGEDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAV-RLAD 501
Cdd:cd07837    74 ENGKPLLYLVFEYLDTDLKKFIDSYGRGPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGLlKIAD 153
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
369-502 6.35e-07

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: 51.52  E-value: 6.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 369 KIAGTSEGAVY--LGIYDNREVAVKVFR-ENSPRGC-----KEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEWTL 440
Cdd:cd07835     6 KIGEGTYGVVYkaRDKLTGEIVALKKIRlETEDEGVpstaiREISLLKEL-NHPNIVRLLDVVHSENKLYLVFEFLDLDL 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720355205 441 EEFLRLPREEPVEngeDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd07835    85 KKYMDSSPLTGLD---PPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADF 143
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
403-593 7.20e-07

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: 51.19  E-value: 7.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 403 EVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEWT-LEEFLRlpREEPVenGEDKFAhSILLSIFEGVQKLH-LHGYS 480
Cdd:cd06605    49 ELDVLHKC-NSPYIVGFYGAFYSEGDISICMEYMDGGsLDKILK--EVGRI--PERILG-KIAVAVVKGLIYLHeKHKII 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 481 HQDLQPQNILIDSKKAVRLADFDQSIR--------------WM------GESQMVRRDLEDLGrLVLYVVMKGEIPF--E 538
Cdd:cd06605   123 HRDVKPSNILVNSRGQVKLCDFGVSGQlvdslaktfvgtrsYMaperisGGKYTVKSDIWSLG-LSLVELATGRFPYppP 201
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355205 539 TLKTQNDEV-LLTMSPDEETKDLIHCLFSPG--ENVKNCLV----------DLLGHPFFwtweNRYRT 593
Cdd:cd06605   202 NAKPSMMIFeLLSYIVDEPPPLLPSGKFSPDfqDFVSQCLQkdpterpsykELMEHPFI----KRYEY 265
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
471-626 7.99e-07

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: 51.93  E-value: 7.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 471 VQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSIRWMGE---------------SQMVRRDLED-LGR---------- 524
Cdd:cd05624   186 IHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSCLKMNDDgtvqssvavgtpdyiSPEILQAMEDgMGKygpecdwwsl 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 525 -LVLYVVMKGEIPF--ETL-----KTQNDEVLLTMSP-----DEETKDLIHCLFSPGENV--KNCLVDLLGHPFF--WTW 587
Cdd:cd05624   266 gVCMYEMLYGETPFyaESLvetygKIMNHEERFQFPShvtdvSEEAKDLIQRLICSRERRlgQNGIEDFKKHAFFegLNW 345
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1720355205 588 ENrYRTLR-----NVGNESDIKVRKCKSDLLRllqHQTLEPPRS 626
Cdd:cd05624   346 EN-IRNLEapyipDVSSPSDTSNFDVDDDVLR---NPEILPPSS 385
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
366-503 9.11e-07

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: 51.06  E-value: 9.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 366 DDYKIAGT----SEGAVYLG--IYDNREVAVK---------------VFREnsprgcKEVscLRDCgDHSNLVAFYGRED 424
Cdd:cd05581     1 NDFKFGKPlgegSYSTVVLAkeKETGKEYAIKvldkrhiikekkvkyVTIE------KEV--LSRL-AHPGIVKLYYTFQ 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 425 DKGCLYVCVSLCEW-TLEEFLRLpreepVENGEDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFD 503
Cdd:cd05581    72 DESKLYFVLEYAPNgDLLEYIRK-----YGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFG 146
PHA02798 PHA02798
ankyrin-like protein; Provisional
181-298 1.05e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 51.76  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 181 LEVLRILLNdMKAEVDARDNMGRNALIRTLLNW-DCENVEEITSILIQHGADVNVRGERGKTPLIAAVERKHTGLVQMLL 259
Cdd:PHA02798   51 TDIVKLFIN-LGANVNGLDNEYSTPLCTILSNIkDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILL 129
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1720355205 260 S--REGINIDARDNEGKTALLIAVDKQLK---EIVQLLLEKGAD 298
Cdd:PHA02798  130 FmiENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVD 173
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
376-502 1.11e-06

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: 50.81  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIYDNREVAVKVFRENSPRG---CKEVSC---LRdcgdHSNLVAFYGREDDKGCLYVCVSLCE-WTLEEFLRlPR 448
Cdd:cd05039    20 GDVMLGDYRGQKVAVKCLKDDSTAAqafLAEASVmttLR----HPNLVQLLGVVLEGNGLYIVTEYMAkGSLVDYLR-SR 94
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355205 449 EEPVENGED--KFAhsilLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd05039    95 GRAVITRKDqlGFA----LDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDF 146
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
369-502 1.12e-06

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: 50.77  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 369 KIAGTSEGAVYLG--IYDNREVAVKVFR----ENSPRGCKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCE-WTLE 441
Cdd:cd06613     7 RIGSGTYGDVYKArnIATGELAAVKVIKlepgDDFEIIQQEISMLKEC-RHPNIVAYFGSYLRRDKLWIVMEYCGgGSLQ 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720355205 442 EFLRLPReePVEngEDKFAHsILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd06613    86 DIYQVTG--PLS--ELQIAY-VCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADF 141
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
376-502 1.13e-06

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 50.81  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIYDNrEVAVKVFRENSPRGCK------EVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCE-WTLEEFLRLPR 448
Cdd:cd14063    14 GRVHRGRWHG-DVAIKLLNIDYLNEEQleafkeEVAAYKNT-RHDNLVLFMGACMDPPHLAIVTSLCKgRTLYSLIHERK 91
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355205 449 EepvengedKFAHS----ILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVrLADF 502
Cdd:cd14063    92 E--------KFDFNktvqIAQQICQGMGYLHAKGIIHKDLKSKNIFLENGRVV-ITDF 140
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
156-298 1.50e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 51.68  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 156 QTTKDKRRLKQGGATALMSAAEKGHLEVLRIL--LNDMKAEVDARD---------NMGRNALIRTLLNWDcENVEEITSI 224
Cdd:cd22194    37 ELAKEEQRDKKKRLKKVSEAAVEELGELLKELkdLSRRRRKTDVPDflmhkltasDTGKTCLMKALLNIN-ENTKEIVRI 115
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355205 225 LIQHGadvnvrgergktpliaaverKHTGLVQMLLSREginIDARDNEGKTALLIAVDKQLKEIVQLLLEKGAD 298
Cdd:cd22194   116 LLAFA--------------------EENGILDRFINAE---YTEEAYEGQTALNIAIERRQGDIVKLLIAKGAD 166
Ank_5 pfam13857
Ankyrin repeats (many copies);
225-280 1.50e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 1.50e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720355205 225 LIQHG-ADVNVRGERGKTPLIAAVERKHTGLVQMLLSReGINIDARDNEGKTALLIA 280
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALDLA 56
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
370-502 1.75e-06

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: 50.42  E-value: 1.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 370 IAGTSEGAvYLGIYDNRE-------VAVKVFR-ENSPRG-----CKEVSCLR--DCGDHSNLVAFY-----GREDDKGCL 429
Cdd:cd07862     6 VAEIGEGA-YGKVFKARDlknggrfVALKRVRvQTGEEGmplstIREVAVLRhlETFEHPNVVRLFdvctvSRTDRETKL 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720355205 430 YVCVSLCEWTLEEFLRLPREE--PVENGEDkfahsILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd07862    85 TLVFEHVDQDLTTYLDKVPEPgvPTETIKD-----MMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADF 154
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
376-517 1.91e-06

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: 50.44  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIYDNREVAVKVFRENSpRGC----KEVSCLRDCgDHSNLVAFYGRED-----------------DKGCLyvCVS 434
Cdd:cd14054     9 GTVWKGSLDERPVAVKVFPARH-RQNfqneKDIYELPLM-EHSNILRFIGADErptadgrmeyllvleyaPKGSL--CSY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 435 LCEWTL--EEFLRLpreepvengedkfahsiLLSIFEGVQKLH--LH-------GYSHQDLQPQNILIDSKKAVRLADFD 503
Cdd:cd14054    85 LRENTLdwMSSCRM-----------------ALSLTRGLAYLHtdLRrgdqykpAIAHRDLNSRNVLVKADGSCVICDFG 147
                         170
                  ....*....|....
gi 1720355205 504 QSIRWMGESQMVRR 517
Cdd:cd14054   148 LAMVLRGSSLVRGR 161
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
59-90 2.86e-06

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.20  E-value: 2.86e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1720355205  59 GWTPLHNAV-QAGRVDIVNLLLSHGADPHRRKK 90
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
381-502 3.03e-06

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


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 49.47  E-value: 3.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 381 GIYDNREVAVKVFREN----SPRGCKEVSCLRDCgDHSNLVAFYGreddkGCLYV-----CVSLC-EWTLEEFLrLPREE 450
Cdd:cd14045    26 GIYDGRTVAIKKIAKKsftlSKRIRKEVKQVREL-DHPNLCKFIG-----GCIEVpnvaiITEYCpKGSLNDVL-LNEDI 98
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720355205 451 PVENGedkFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd14045    99 PLNWG---FRFSFATDIARGMAYLHQHKIYHGRLKSSNCVIDDRWVCKIADY 147
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
403-518 3.04e-06

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: 49.36  E-value: 3.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 403 EVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEWTLEEFLRLPREEPVENGEDKFahsILLSIFEGVQKLHLHGYSHQ 482
Cdd:cd06611    52 EIDILSEC-KHPNIVGLYEAYFYENKLWILIEFCDGGALDSIMLELERGLTEPQIRY---VCRQMLEALNFLHSHKVIHR 127
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1720355205 483 DLQPQNILIDSKKAVRLADFDQSIRwmGESQMVRRD 518
Cdd:cd06611   128 DLKAGNILLTLDGDVKLADFGVSAK--NKSTLQKRD 161
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
75-144 3.04e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 3.04e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  75 VNLLLSHGADPHRRKKNGATPFIIAGIQGDVKLLEILLSCGADVNECDENGFTAFMEAAERGNAEALRFL 144
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
369-502 3.40e-06

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: 49.43  E-value: 3.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 369 KIAGTSEGAVYLGiyDNRE----VAVKVFR-----ENSPR-GCKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEW 438
Cdd:cd07860     7 KIGEGTYGVVYKA--RNKLtgevVALKKIRldtetEGVPStAIREISLLKEL-NHPNIVKLLDVIHTENKLYLVFEFLHQ 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355205 439 TLEEFLRLpreEPVENGEDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd07860    84 DLKKFMDA---SALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADF 144
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
385-502 4.15e-06

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: 49.17  E-value: 4.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 385 NREVAVKVFrENSPRGC-KEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVSLCEW--TLEEFLRLPreepveNGEDKFAH 461
Cdd:cd14091    25 GKEYAVKII-DKSKRDPsEEIEILLRYGQHPNIITLRDVYDDGNSVYLVTELLRGgeLLDRILRQK------FFSEREAS 97
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1720355205 462 SILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKA----VRLADF 502
Cdd:cd14091    98 AVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGdpesLRICDF 142
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
385-502 4.91e-06

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: 48.85  E-value: 4.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 385 NREVAVKVFREN---------SPRgckEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEWTLEEFLrlpreEPVENG 455
Cdd:cd07833    26 GEIVAIKKFKESeddedvkktALR---EVKVLRQL-RHENIVNLKEAFRRKGRLYLVFEYVERTLLELL-----EASPGG 96
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720355205 456 EDkfAHSILLSIFE---GVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd07833    97 LP--PDAVRSYIWQllqAIAYCHSHNIIHRDIKPENILVSESGVLKLCDF 144
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
385-591 5.38e-06

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: 48.86  E-value: 5.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 385 NREVAVKVFRENSPRGCKEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVSLCEWTlEEFLRLPREEPVENGEdkfAHSIL 464
Cdd:cd14177    29 NMEFAVKIIDKSKRDPSEEIEILMRYGQHPNIITLKDVYDDGRYVYLVTELMKGG-ELLDRILRQKFFSERE---ASAVL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 465 LSIFEGVQKLHLHGYSHQDLQPQNILI--DSKKA--VRLADFDQSIRWMGESQMVRR----------------------D 518
Cdd:cd14177   105 YTITKTVDYLHCQGVVHRDLKPSNILYmdDSANAdsIRICDFGFAKQLRGENGLLLTpcytanfvapevlmrqgydaacD 184
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355205 519 LEDLGRLvLYVVMKGEIPFETLKTQN-DEVLLTMSPDEETkdlihclFSPG--ENVKNCLVDLLGHPFFWTWENRY 591
Cdd:cd14177   185 IWSLGVL-LYTMLAGYTPFANGPNDTpEEILLRIGSGKFS-------LSGGnwDTVSDAAKDLLSHMLHVDPHQRY 252
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
385-584 5.59e-06

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: 48.47  E-value: 5.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 385 NREVAVK-VFRENSPRG----CKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEW-TLEEFLRLPREEpvenGEDK 458
Cdd:cd14202    28 DLEVAVKcINKKNLAKSqtllGKEIKILKEL-KHENIVALYDFQEIANSVYLVMEYCNGgDLADYLHTMRTL----SEDT 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 459 FahSILLSIFEGVQK-LHLHGYSHQDLQPQNILID---SKKA------VRLADFDQSiRWMGESQMV------------- 515
Cdd:cd14202   103 I--RLFLQQIAGAMKmLHSKGIIHRDLKPQNILLSysgGRKSnpnnirIKIADFGFA-RYLQNNMMAatlcgspmymape 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 516 ---------RRDLEDLGRLVlYVVMKGEIPFETLKTQN-------DEVLLTMSPDEETKDLIHCLFSPGE-NVKNCLV-- 576
Cdd:cd14202   180 vimsqhydaKADLWSIGTII-YQCLTGKAPFQASSPQDlrlfyekNKSLSPNIPRETSSHLRQLLLGLLQrNQKDRMDfd 258

                  ....*...
gi 1720355205 577 DLLGHPFF 584
Cdd:cd14202   259 EFFHHPFL 266
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
376-552 5.89e-06

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: 48.41  E-value: 5.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIYDN-REVAVKVFREN--SPRGCKEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVSLCE-WTLEEFLRLPReep 451
Cdd:cd05112    18 GLVHLGYWLNkDKVAIKTIREGamSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEhGCLSDYLRTQR--- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 452 vengeDKFAHSILLS----IFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF--------DQ---------SIRWMG 510
Cdd:cd05112    95 -----GLFSAETLLGmcldVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFgmtrfvldDQytsstgtkfPVKWSS 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1720355205 511 ESQM------VRRDLEDLGRLVLYVVMKGEIPFETlkTQNDEVLLTMS 552
Cdd:cd05112   170 PEVFsfsrysSKSDVWSFGVLMWEVFSEGKIPYEN--RSNSEVVEDIN 215
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
474-592 5.89e-06

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: 49.21  E-value: 5.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 474 LHLHGYSHQDLQPQNILIDSKKAVRLADF---------------------------DQSIRWMGESQMVRR--------- 517
Cdd:cd05573   117 LHKLGFIHRDIKPDNILLDADGHIKLADFglctkmnksgdresylndsvntlfqdnVLARRRPHKQRRVRAysavgtpdy 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 518 ---------------DLEDLGrLVLYVVMKGEIPF------ET-LKTQNDEVLLTMSPD----EETKDLI-HCLFSPGEN 570
Cdd:cd05573   197 iapevlrgtgygpecDWWSLG-VILYEMLYGFPPFysdslvETySKIMNWKESLVFPDDpdvsPEAIDLIrRLLCDPEDR 275
                         170       180
                  ....*....|....*....|....*.
gi 1720355205 571 VKNcLVDLLGHPFF----WTWENRYR 592
Cdd:cd05573   276 LGS-AEEIKAHPFFkgidWENLRESP 300
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
372-502 6.12e-06

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: 48.71  E-value: 6.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 372 GTSeGAVYLG--IYDNREVAVKVFR-ENSPRG-----CKEVSCLRDCgDHSNLVAFY------GREDDKGCLYVCVSLCE 437
Cdd:cd07840    10 GTY-GQVYKArnKKTGELVALKKIRmENEKEGfpitaIREIKLLQKL-DHPNVVRLKeivtskGSAKYKGSIYMVFEYMD 87
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720355205 438 WTLEEFLRlpreepveNGEDKFAHS----ILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd07840    88 HDLTGLLD--------NPEVKFTESqikcYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADF 148
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
224-293 6.19e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 6.19e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 224 ILIQHGADVNVRGERGKTPLIAAVERKHTGLVQMLLSReGINIDARDNEGKTALLIAVDKQLKEIVQLLL 293
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEF-GADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
402-544 6.21e-06

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: 48.57  E-value: 6.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 402 KEVSCLRDCGdHSNLVAFYGR--EDDKGCLYVCVSLCE-WTLEEFLRLPREEPVENGED---KFAHSILlsifEGVQKLH 475
Cdd:cd06621    48 RELEINKSCA-SPYIVKYYGAflDEQDSSIGIAMEYCEgGSLDSIYKKVKKKGGRIGEKvlgKIAESVL----KGLSYLH 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 476 LHGYSHQDLQPQNILIDSKKAVRLADFDQS--------------------IRWMGESQMVRRDLEDLGrLVLYVVMKGEI 535
Cdd:cd06621   123 SRKIIHRDIKPSNILLTRKGQVKLCDFGVSgelvnslagtftgtsyymapERIQGGPYSITSDVWSLG-LTLLEVAQNRF 201

                  ....*....
gi 1720355205 536 PFETLKTQN 544
Cdd:cd06621   202 PFPPEGEPP 210
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
402-502 6.32e-06

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: 48.66  E-value: 6.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 402 KEVSCLRDCGDHSNLVAFYG------REDDKGC--LYVCVSLCEWTLEEFLRlpreepVENGEDKFAHSILLSIF----E 469
Cdd:cd14036    46 QEINFMKKLSGHPNIVQFCSaasigkEESDQGQaeYLLLTELCKGQLVDFVK------KVEAPGPFSPDTVLKIFyqtcR 119
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1720355205 470 GVQklHLHGYS----HQDLQPQNILIDSKKAVRLADF 502
Cdd:cd14036   120 AVQ--HMHKQSppiiHRDLKIENLLIGNQGQIKLCDF 154
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
413-583 6.62e-06

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 48.32  E-value: 6.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 413 HSNLVAFYGREDDKGCLYVCVSLCE-WTLEEFLRlPREEPVENGEdkfAHSILLSIFEGVQKLHLHGYSHQDLQPQNILI 491
Cdd:cd14186    60 HPSILELYNYFEDSNYVYLVLEMCHnGEMSRYLK-NRKKPFTEDE---ARHFMHQIVTGMLYLHSHGILHRDLTLSNLLL 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 492 DSKKAVRLADFD--QSIRWMGESQM--------------------VRRDLEDLGrLVLYVVMKGEIPFETLKTQND---- 545
Cdd:cd14186   136 TRNMNIKIADFGlaTQLKMPHEKHFtmcgtpnyispeiatrsahgLESDVWSLG-CMFYTLLVGRPPFDTDTVKNTlnkv 214
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1720355205 546 ---EVLLTMSPDEETKDLIHCLFSPGENVKNCLVDLLGHPF 583
Cdd:cd14186   215 vlaDYEMPAFLSREAQDLIHQLLRKNPADRLSLSSVLDHPF 255
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
384-502 6.68e-06

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: 48.52  E-value: 6.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 384 DNREVAVK--VFRENSP---RGCKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCE-WTLEEFlrlpreepVENG-- 455
Cdd:cd14046    30 DGRYYAIKkiKLRSESKnnsRILREVMLLSRL-NHQHVVRYYQAWIERANLYIQMEYCEkSTLRDL--------IDSGlf 100
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1720355205 456 -EDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd14046   101 qDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDF 148
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
385-502 6.73e-06

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: 48.86  E-value: 6.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 385 NREVAVKVFRENSPRGCKEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVSLCEWTlEEFLRLPREEPVENGEdkfAHSIL 464
Cdd:cd14176    44 NMEFAVKIIDKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGG-ELLDKILRQKFFSERE---ASAVL 119
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1720355205 465 LSIFEGVQKLHLHGYSHQDLQPQNIL-IDSK---KAVRLADF 502
Cdd:cd14176   120 FTITKTVEYLHAQGVVHRDLKPSNILyVDESgnpESIRICDF 161
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
376-507 7.21e-06

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: 48.12  E-value: 7.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLgIYD---NREVAVKV--FRENSPRGCKEVSCLrDCGD-------HSNLVAFYGreddkgCLYvcvSLCEWTLEEF 443
Cdd:cd06652    16 GRVYL-CYDadtGRELAVKQvqFDPESPETSKEVNAL-ECEIqllknllHERIVQYYG------CLR---DPQERTLSIF 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720355205 444 LRLPREEPV-----------ENGEDKFAHSILlsifEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSIR 507
Cdd:cd06652    85 MEYMPGGSIkdqlksygaltENVTRKYTRQIL----EGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKR 155
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
369-502 7.36e-06

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: 48.57  E-value: 7.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 369 KIAGTSEGAVYLGIY--DNREVAVKVFR-ENSPRGC-----KEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEWTL 440
Cdd:cd07861     7 KIGEGTYGVVYKGRNkkTGQIVAMKKIRlESEEEGVpstaiREISLLKEL-QHPNIVCLEDVLMQENRLYLVFEFLSMDL 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720355205 441 EEFL-RLPREEPVENgedKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd07861    86 KKYLdSLPKGKYMDA---ELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADF 145
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
358-502 7.98e-06

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: 48.47  E-value: 7.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 358 GKLKIFIhddyKIAGTSEGAvYLGIYDNRE------VAVKVFR----ENSP-RGCKEVSCLRDCgDHSNLVAFYGREDDK 426
Cdd:cd07871     2 GKLETYV----KLDKLGEGT-YATVFKGRSkltenlVALKEIRleheEGAPcTAIREVSLLKNL-KHANIVTLHDIIHTE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 427 GCLYVCVSLCEWTLEEFLrlpreepvEN-GEDKFAHSILLSIFE---GVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd07871    76 RCLTLVFEYLDSDLKQYL--------DNcGNLMSMHNVKIFMFQllrGLSYCHKRKILHRDLKPQNLLINEKGELKLADF 147
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
369-502 8.46e-06

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 48.28  E-value: 8.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 369 KIAGTSEGAVYLGI--YDNREVAVKVFR-----ENSPR-GCKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEWTL 440
Cdd:PLN00009    9 KIGEGTYGVVYKARdrVTNETIALKKIRleqedEGVPStAIREISLLKEM-QHGNIVRLQDVVHSEKRLYLVFEYLDLDL 87
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720355205 441 EEFLRlprEEPVENGEDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILID-SKKAVRLADF 502
Cdd:PLN00009   88 KKHMD---SSPDFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDrRTNALKLADF 147
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
59-86 9.84e-06

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.57  E-value: 9.84e-06
                           10        20
                   ....*....|....*....|....*...
gi 1720355205   59 GWTPLHNAVQAGRVDIVNLLLSHGADPH 86
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
378-502 9.99e-06

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 49.02  E-value: 9.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 378 VYLGiYD---NREVAVKVFRE---NSP-------RGCKEVSCLrdcgDHSNLVAFY--GREDD---------KGClyvcv 433
Cdd:NF033483   23 VYLA-KDtrlDRDVAVKVLRPdlaRDPefvarfrREAQSAASL----SHPNIVSVYdvGEDGGipyivmeyvDGR----- 92
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720355205 434 slcewTLEEFLR----LPREEPVEngedkfahsILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:NF033483   93 -----TLKDYIRehgpLSPEEAVE---------IMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDF 151
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
368-502 1.17e-05

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: 48.05  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 368 YKIAG-TSEGA---VYLGI----YDNREVAVKVFREN-------SPRGCKEVSCLRDCgDHSNLVAFYG--REDDKGCLY 430
Cdd:cd07842     2 YEIEGcIGRGTygrVYKAKrkngKDGKEYAIKKFKGDkeqytgiSQSACREIALLREL-KHENVVSLVEvfLEHADKSVY 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355205 431 VCVSLCEWTLEEFLRLPREEPVENGEDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILI----DSKKAVRLADF 502
Cdd:cd07842    81 LLFDYAEHDLWQIIKFHRQAKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVmgegPERGVVKIGDL 156
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
385-502 1.18e-05

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: 47.70  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 385 NREVAVKVFRENSPRGCKEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVSLCEWTlEEFLRLPREEPVENGEdkfAHSIL 464
Cdd:cd14178    28 STEYAVKIIDKSKRDPSEEIEILLRYGQHPNIITLKDVYDDGKFVYLVMELMRGG-ELLDRILRQKCFSERE---ASAVL 103
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1720355205 465 LSIFEGVQKLHLHGYSHQDLQPQNIL-ID---SKKAVRLADF 502
Cdd:cd14178   104 CTITKTVEYLHSQGVVHRDLKPSNILyMDesgNPESIRICDF 145
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
386-502 1.39e-05

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: 47.50  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 386 REVAVKVFREnsprgCKEVSCLRdcgdHSNLVAFYGR--EDDKGCLYVCVSLCEWTLEEFLRLPREEPVENGEDKFAH-- 461
Cdd:cd14049    46 KRDCMKVLRE-----VKVLAGLQ----HPNIVGYHTAwmEHVQLMLYIQMQLCELSLWDWIVERNKRPCEEEFKSAPYtp 116
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1720355205 462 -------SILLSIFEGVQKLHLHGYSHQDLQPQNILID-SKKAVRLADF 502
Cdd:cd14049   117 vdvdvttKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIHVRIGDF 165
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
376-505 1.40e-05

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: 47.30  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIY--DNREVAVKVF---RENSPRGCKEVSCLRDCGDHSNLVAFYG---REDDKGC---LYVCVSLCE-WTLEEF 443
Cdd:cd06608    20 GKVYKARHkkTGQLAAIKIMdiiEDEEEEIKLEINILRKFSNHPNIATFYGafiKKDPPGGddqLWLVMEYCGgGSVTDL 99
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720355205 444 LRLPREEPVENGEDKFAHsILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQS 505
Cdd:cd06608   100 VKGLRKKGKRLKEEWIAY-ILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVS 160
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
384-551 1.52e-05

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: 47.68  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 384 DNREVAVKVF--RENSPRgckEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVslcewtleEFLR----LPREEPVENGED 457
Cdd:cd14092    30 TGQEFAVKIVsrRLDTSR---EVQLLRLCQGHPNIVKLHEVFQDELHTYLVM--------ELLRggelLERIRKKKRFTE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 458 KFAHSILLSIFEGVQKLHLHGYSHQDLQPQNIL---IDSKKAVRLADF---------------------------DQSIR 507
Cdd:cd14092    99 SEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLftdEDDDAEIKIVDFgfarlkpenqplktpcftlpyaapevlKQALS 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1720355205 508 WMGESQMVrrDLEDLGrLVLYVVMKGEIPFETlKTQNDEVLLTM 551
Cdd:cd14092   179 TQGYDESC--DLWSLG-VILYTMLSGQVPFQS-PSRNESAAEIM 218
Ank_4 pfam13637
Ankyrin repeats (many copies);
127-188 1.59e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 1.59e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720355205 127 TAFMEAAERGNAEALRFLFAKGANVNLRrqttkDKrrlkqGGATALMSAAEKGHLEVLRILL 188
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAV-----DG-----NGETALHFAASNGNVEVLKLLL 54
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
457-589 1.63e-05

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: 48.08  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 457 DKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSIRwMGESQMVRRDL----------EDL---- 522
Cdd:cd05622   171 EKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMK-MNKEGMVRCDTavgtpdyispEVLksqg 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 523 -----GR--------LVLYVVMKGEIPF--ETL-----KTQNDEVLLTMSPD----EETKDLIhCLFSPGENV---KNCL 575
Cdd:cd05622   250 gdgyyGRecdwwsvgVFLYEMLVGDTPFyaDSLvgtysKIMNHKNSLTFPDDndisKEAKNLI-CAFLTDREVrlgRNGV 328
                         170
                  ....*....|....*...
gi 1720355205 576 VDLLGHPFF----WTWEN 589
Cdd:cd05622   329 EEIKRHLFFkndqWAWET 346
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
457-502 1.68e-05

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: 47.27  E-value: 1.68e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1720355205 457 DKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd14181   115 EKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDF 160
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
388-505 1.77e-05

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: 46.98  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 388 VAVKVFRENSPRGCK-----EVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEWTlEEFLRLpreepVENGE--DKFA 460
Cdd:cd14083    31 VAIKCIDKKALKGKEdslenEIAVLRKI-KHPNIVQLLDIYESKSHLYLVMELVTGG-ELFDRI-----VEKGSytEKDA 103
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720355205 461 HSILLSIFEGVQKLHLHGYSHQDLQPQNILI-----DSKkaVRLADFDQS 505
Cdd:cd14083   104 SHLIRQVLEAVDYLHSLGIVHRDLKPENLLYyspdeDSK--IMISDFGLS 151
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
423-502 1.97e-05

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: 47.18  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 423 EDDKGCLYVCVSLC-EWTLEEFLRlpREEPVENGEDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLAD 501
Cdd:cd14048    84 KMDEVYLYIQMQLCrKENLKDWMN--RRCTMESRELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGD 161

                  .
gi 1720355205 502 F 502
Cdd:cd14048   162 F 162
PHA02798 PHA02798
ankyrin-like protein; Provisional
41-299 2.41e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.52  E-value: 2.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  41 VQQLLEKGADANACEDTWGwTPLHNAVQ-----AGRVDIVNLLLSHGADPHRRKKNGATPFIIAGIQGDVKLLEILL--- 112
Cdd:PHA02798   54 VKLFINLGANVNGLDNEYS-TPLCTILSnikdyKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmi 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 113 SCGADVNECDENGFTAFMEAAERGNA---EALRFLFAKGANVNLRRQttkdkrrlkQGGATALMSAAEKghlEVLRILLN 189
Cdd:PHA02798  133 ENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHNN---------KEKYDTLHCYFKY---NIDRIDAD 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 190 DMKAEVD------ARDNMGRNALIRTL--LNWDCENVEEITSILIQHGADVNVRGERGKTPLIAAVERKHTGLVQMLLSR 261
Cdd:PHA02798  201 ILKLFVDngfiinKENKSHKKKFMEYLnsLLYDNKRFKKNILDFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQL 280
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1720355205 262 EGiNIDARDNEGKTALLIAVDKQLKEIVQLLLEKGADK 299
Cdd:PHA02798  281 GG-DINIITELGNTCLFTAFENESKFIFNSILNKKPNK 317
PHA02946 PHA02946
ankyin-like protein; Provisional
41-125 2.85e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 47.36  E-value: 2.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  41 VQQLLEKGADANACEDTwGWTPLHNAVQAGRVDIVNLLLSHGADPHRRKKNGATP-FIIAGIQGDV-KLLEILLSCGADV 118
Cdd:PHA02946   55 VEELLHRGYSPNETDDD-GNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPlYYLSGTDDEViERINLLVQYGAKI 133

                  ....*...
gi 1720355205 119 -NECDENG 125
Cdd:PHA02946  134 nNSVDEEG 141
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
375-503 3.00e-05

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: 46.56  E-value: 3.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 375 EGAVYLgiYDNREVAVKVFRENS----PRGCKEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVslcewtleEFLR----L 446
Cdd:cd14174    19 QGCVSL--QNGKEYAVKIIEKNAghsrSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVF--------EKLRggsiL 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 447 PREEPVENGEDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKA---VRLADFD 503
Cdd:cd14174    89 AHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKvspVKICDFD 148
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
467-505 3.37e-05

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: 46.11  E-value: 3.37e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1720355205 467 IFEGVQKLHLHGYSHQDLQPQNILIDSKKA--VRLADFDQS 505
Cdd:cd14006    98 LLEGLQYLHNHHILHLDLKPENILLADRPSpqIKIIDFGLA 138
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
412-502 3.38e-05

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: 46.05  E-value: 3.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 412 DHSNLVAFYGREDDKGCLYVCVSLCewTLEEFLRLPREEPVENGEdkfAHSILLSIFEGVQKLHLHGYSHQDLQPQNILI 491
Cdd:cd14108    56 DHKSIVRFHDAFEKRRVVIIVTELC--HEELLERITKRPTVCESE---VRSYMRQLLEGIEYLHQNDVLHLDLKPENLLM 130
                          90
                  ....*....|...
gi 1720355205 492 -DSK-KAVRLADF 502
Cdd:cd14108   131 aDQKtDQVRICDF 143
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
374-584 3.42e-05

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: 46.09  E-value: 3.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 374 SEGAVYLGIY--DNREVAVKV------FRENSPRGC-KEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEWTlEEFL 444
Cdd:cd14081    13 QTGLVKLAKHcvTGQKVAIKIvnkeklSKESVLMKVeREIAIMKLI-EHPNVLKLYDVYENKKYLYLVLEYVSGG-ELFD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 445 RLPREEPVENGEdkfAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSiRWMGESQMVRR------- 517
Cdd:cd14081    91 YLVKKGRLTEKE---ARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMA-SLQPEGSLLETscgsphy 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 518 ----------------DLEDLGrLVLYVVMKGEIPFEtlkTQNDEVLL--------TMSPD--EETKDLIHCLF--SPGE 569
Cdd:cd14081   167 acpevikgekydgrkaDIWSCG-VILYALLVGALPFD---DDNLRQLLekvkrgvfHIPHFisPDAQDLLRRMLevNPEK 242
                         250
                  ....*....|....*
gi 1720355205 570 NVKncLVDLLGHPFF 584
Cdd:cd14081   243 RIT--IEEIKKHPWF 255
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
376-584 3.72e-05

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: 46.08  E-value: 3.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLG--IYDNREVAVKVFRENSPRGCKEVSCLRDC------------GDHSN---LVAFYGREDDkgclYVCV----S 434
Cdd:cd14005    14 GTVYSGvrIRDGLPVAVKFVPKSRVTEWAMINGPVPVpleialllkaskPGVPGvirLLDWYERPDG----FLLImerpE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 435 LCEwTLEEFLRlpreepvENG--EDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKA-VRLADFdqsirwmGE 511
Cdd:cd14005    90 PCQ-DLFDFIT-------ERGalSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRTGeVKLIDF-------GC 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 512 SQMVRRDLED----------------------------LGRLvLYVVMKGEIPFEtlktqNDEVLLTMSP------DEET 557
Cdd:cd14005   155 GALLKDSVYTdfdgtrvysppewirhgryhgrpatvwsLGIL-LYDMLCGDIPFE-----NDEQILRGNVlfrprlSKEC 228
                         250       260
                  ....*....|....*....|....*..
gi 1720355205 558 KDLIHCLFSPGENVKNCLVDLLGHPFF 584
Cdd:cd14005   229 CDLISRCLQFDPSKRPSLEQILSHPWF 255
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
59-86 3.89e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.09  E-value: 3.89e-05
                          10        20
                  ....*....|....*....|....*...
gi 1720355205  59 GWTPLHNAVQAGRVDIVNLLLSHGADPH 86
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
467-502 4.03e-05

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: 45.76  E-value: 4.03e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1720355205 467 IFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd13994   107 ILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDF 142
RNase_Ire1 cd10422
RNase domain (also known as the kinase extension nuclease domain) of Ire1; The model ...
630-704 4.12e-05

RNase domain (also known as the kinase extension nuclease domain) of Ire1; The model represents the C-terminal endoribonuclease domain of the multi-functional protein Ire1; Ire1 in addition contains a type I transmembrane serine/threonine protein kinase (STK) domain, and a Luminal dimerization domain. Ire1 is essential for the endoplasmic reticulum (ER) unfolded protein response (UPR), which acts as an ER stress sensor and is the oldest and most conserved component of the UPR in eukaryotes. During ER stress, IRE1 dimerizes through its N-terminal luminal domain and forms oligomers, promoting trans-autophosphorylation by its cytosolic kinase domain. This leads to a conformational change that stimulates its endoribonuclease (RNase) activity and results in the cleavage of its mRNA substrate, Hac1 in yeast and Xbp1 in metazoans, thus promoting a splicing event that enables translation into a transcription factor which activates the UPR. This RNase domain is homologous to the RNase domain of RNase L, and possesses a novel fold for a nuclease and appears to be rigid irrespective of the activation state of IRE1. Structural analysis and mutational studies have revealed that an early stage 'phosphoryl-transfer' competent conformation of IRE1 favors face-to-face dimerization of the kinase domains which precedes and is distinct from the RNase 'active' back-to-back conformation. Furthermore, in yeast IRE1, the flavonol quercetin activates the RNase and potentiates activation of the protein kinase by ADP, hinting at the possible existence of endogenous cytoplasmic ligands that may function along with stress signals from ER lumen in order to modulate IRE1 activity, thus identifying IRE1 as a target for development of ATP-competitive inhibitors to modulate the UPR with specific relevance for multiple myeloma.


Pssm-ID: 199217  Cd Length: 129  Bit Score: 43.73  E-value: 4.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 630 WTSKIDKNVMDEMNHFyekRKKNPyqDTVGDLLKFIRNIGEHINE--EKkrgMKEILGD-PS---RYFQETFPDLVIYIY 703
Cdd:cd10422    41 WREKLDKTFIDNLGKY---RKYKG--SSVRDLLRALRNKKHHYRElpPD---VQELLGPlPDgflRYFTSRFPNLLIHVY 112

                  .
gi 1720355205 704 K 704
Cdd:cd10422   113 R 113
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
467-502 4.48e-05

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: 46.56  E-value: 4.48e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1720355205 467 IFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd05600   120 MFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDF 155
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
376-548 4.51e-05

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: 45.90  E-value: 4.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIYDN-REVAVKVFRENSPRG---CKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCE-WTLEEFLRLPREe 450
Cdd:cd05059    18 GVVHLGKWRGkIDVAIKMIKEGSMSEddfIEEAKVMMKL-SHPKLVQLYGVCTKQRPIFIVTEYMAnGCLLNYLRERRG- 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 451 pvengedKFAHSILLS----IFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF--------DQ---------SIRWM 509
Cdd:cd05059    96 -------KFQTEQLLEmckdVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFglaryvldDEytssvgtkfPVKWS 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1720355205 510 G-ESQMVRR-----DLEDLGRLVLYVVMKGEIPFETLKtqNDEVL 548
Cdd:cd05059   169 PpEVFMYSKfssksDVWSFGVLMWEVFSEGKMPYERFS--NSEVV 211
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
355-505 4.63e-05

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: 45.77  E-value: 4.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 355 PMIGKLKIFIH-----DDYKIAGTSEGAVYLGIY------DNREVAVKVF---RENSPRGCKEVSCLRDCGDHSNLVAFY 420
Cdd:cd06638     2 PLSGKTIIFDSfpdpsDTWEIIETIGKGTYGKVFkvlnkkNGSKAAVKILdpiHDIDEEIEAEYNILKALSDHPNVVKFY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 421 G---REDDKGC--LYVCVSLCEW-TLEEFLR--LPREEPVEngEDKFAHsILLSIFEGVQKLHLHGYSHQDLQPQNILID 492
Cdd:cd06638    82 GmyyKKDVKNGdqLWLVLELCNGgSVTDLVKgfLKRGERME--EPIIAY-ILHEALMGLQHLHVNKTIHRDVKGNNILLT 158
                         170
                  ....*....|...
gi 1720355205 493 SKKAVRLADFDQS 505
Cdd:cd06638   159 TEGGVKLVDFGVS 171
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
456-502 4.82e-05

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: 46.15  E-value: 4.82e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720355205 456 EDKFAHSI----LLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd05601    96 DDIFEESMarfyLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADF 146
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
474-583 4.93e-05

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: 45.71  E-value: 4.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 474 LHLHGYSHQDLQPQNILIDSKKAVRLADFDQSiRWMGESQMV-----------------------RRDLEDLGrLVLYVV 530
Cdd:cd14002   115 LHSNRIIHRDMKPQNILIGKGGVVKLCDFGFA-RAMSCNTLVltsikgtplymapelvqeqpydhTADLWSLG-CILYEL 192
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355205 531 MKGEIPFET-------LKTQNDEVLL--TMSPDeeTKDLIHCLF--SPGENVKncLVDLLGHPF 583
Cdd:cd14002   193 FVGQPPFYTnsiyqlvQMIVKDPVKWpsNMSPE--FKSFLQGLLnkDPSKRLS--WPDLLEHPF 252
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
385-502 4.99e-05

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: 45.72  E-value: 4.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 385 NREVAVKVFReNSPR----GCKEVSCLR-----DCGDHSNLV----AFYGREDdkgcLYVCVSLCEWTLEEFLRLPREEP 451
Cdd:cd14133    24 GEEVALKIIK-NNKDyldqSLDEIRLLEllnkkDKADKYHIVrlkdVFYFKNH----LCIVFELLSQNLYEFLKQNKFQY 98
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720355205 452 VENGE-DKFAHSILlsifEGVQKLHLHGYSHQDLQPQNILI--DSKKAVRLADF 502
Cdd:cd14133    99 LSLPRiRKIAQQIL----EALVFLHSLGLIHCDLKPENILLasYSRCQIKIIDF 148
PHA03100 PHA03100
ankyrin repeat protein; Provisional
41-157 5.13e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.20  E-value: 5.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  41 VQQLLEKGADANACEDTwGWTPLHNAVQAGRVDI------------------VNLLLSHGADPHRRKKNGATPFIIAGIQ 102
Cdd:PHA03100  124 VEYLLDNGANVNIKNSD-GENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYN 202
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720355205 103 GDVKLLEILLSCGADVNECDENGFTAFMEAAERGNAEALRFLFAKGANVNLRRQT 157
Cdd:PHA03100  203 NNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
453-502 5.15e-05

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: 45.77  E-value: 5.15e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720355205 453 ENGEDKFAHS----ILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd07866   106 ENPSVKLTESqikcYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADF 159
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
463-524 5.55e-05

RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction mechanisms];


Pssm-ID: 440246 [Multi-domain]  Cd Length: 183  Bit Score: 44.51  E-value: 5.55e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355205 463 ILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSIRWMGES--QMVRRDLEDLGR 524
Cdd:COG0478    95 VLDKILEEIRRAHDAGIVHADLSEYNILVDDDGGVWIIDWPQAVPRDHPNaeELLERDLENLLR 158
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
445-624 5.92e-05

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: 46.16  E-value: 5.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 445 RLPREEPvengedKFAHSILLSIFEGVQKLHlhgYSHQDLQPQNILIDSKKAVRLADFDQSIRWMGE------------- 511
Cdd:cd05623   169 RLPEDMA------RFYLAEMVLAIDSVHQLH---YVHRDIKPDNILMDMNGHIRLADFGSCLKLMEDgtvqssvavgtpd 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 512 --SQMVRRDLED-------------LGrLVLYVVMKGEIPF--ETL-----KTQNDE-----VLLTMSPDEETKDLIHCL 564
Cdd:cd05623   240 yiSPEILQAMEDgkgkygpecdwwsLG-VCMYEMLYGETPFyaESLvetygKIMNHKerfqfPTQVTDVSENAKDLIRRL 318
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720355205 565 FSPGENV--KNCLVDLLGHPFF--WTWENryrtLRN--------VGNESDIKVRKCKSDLLRllQHQTLEPP 624
Cdd:cd05623   319 ICSREHRlgQNGIEDFKNHPFFvgIDWDN----IRNceapyipeVSSPTDTSNFDVDDDCLK--NCETMPPP 384
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
401-502 5.96e-05

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: 45.73  E-value: 5.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 401 CKEVSCLRDCGDHSNLVAFYGREDDK--GCLYVCVSLCEWTLEEFLRlPREEPVenGEDKfAHSILLSIFEGVQKLHLHG 478
Cdd:cd07831    45 LREIQALRRLSPHPNILRLIEVLFDRktGRLALVFELMDMNLYELIK-GRKRPL--PEKR-VKNYMYQLLKSLDHMHRNG 120
                          90       100
                  ....*....|....*....|....
gi 1720355205 479 YSHQDLQPQNILIDsKKAVRLADF 502
Cdd:cd07831   121 IFHRDIKPENILIK-DDILKLADF 143
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
376-502 6.12e-05

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: 45.36  E-value: 6.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIYDNREVAVKVFRENSPRGC--KEVSCLRDCgDHSNLVAFYGR-EDDKGCLYVCVS-LCEWTLEEFLRlPREEP 451
Cdd:cd05082    20 GDVMLGDYRGNKVAVKCIKNDATAQAflAEASVMTQL-RHSNLVQLLGViVEEKGGLYIVTEyMAKGSLVDYLR-SRGRS 97
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720355205 452 VENGED--KFAhsilLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd05082    98 VLGGDCllKFS----LDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDF 146
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
467-513 6.22e-05

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: 45.49  E-value: 6.22e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720355205 467 IFEGVQKLHLHGYSHQDLQPQNILIDSKK---AVRLADFDQSIRWMGESQ 513
Cdd:cd14086   109 ILESVNHCHQNGIVHRDLKPENLLLASKSkgaAVKLADFGLAIEVQGDQQ 158
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
463-502 6.24e-05

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 45.91  E-value: 6.24e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1720355205 463 ILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:PTZ00024  124 ILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADF 163
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
365-505 6.80e-05

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: 45.42  E-value: 6.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 365 HDDYKIAGTSEGAVYLGIYDNREV------AVKVFR----ENSPRGCKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVS 434
Cdd:cd06645    10 QEDFELIQRIGSGTYGDVYKARNVntgelaAIKVIKlepgEDFAVVQQEIIMMKDC-KHSNIVAYFGSYLRRDKLWICME 88
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720355205 435 LCEW-TLEEFLRLprEEPVEngEDKFAHsILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQS 505
Cdd:cd06645    89 FCGGgSLQDIYHV--TGPLS--ESQIAY-VSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVS 155
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
374-502 6.94e-05

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: 45.09  E-value: 6.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 374 SEGAVYLGIydNRE----VAVKVF---------RENSPRGCKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEW-T 439
Cdd:cd06632    12 SFGSVYEGF--NGDtgdfFAVKEVslvdddkksRESVKQLEQEIALLSKL-RHPNIVQYYGTEREEDNLYIFLEYVPGgS 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355205 440 LEEFLRL--PREEPVengedkfahsILL---SIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd06632    89 IHKLLQRygAFEEPV----------IRLytrQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADF 146
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
385-503 6.97e-05

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: 45.40  E-value: 6.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 385 NREVAVKVFrENSP-----RGCKEVSCLRDCGDHSN---LVAFYgREDDKGCLyVCVSLCEWTLEEFLRLPReepveNGE 456
Cdd:cd14173    27 NKEYAVKII-EKRPghsrsRVFREVEMLYQCQGHRNvleLIEFF-EEEDKFYL-VFEKMRGGSILSHIHRRR-----HFN 98
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720355205 457 DKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSK---KAVRLADFD 503
Cdd:cd14173    99 ELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPnqvSPVKICDFD 148
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
402-502 7.21e-05

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: 44.94  E-value: 7.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 402 KEVSCLRDCgDHSNLVAFYG--REDDKGCLYVCVSLCEWTLEEFL------RLPREEpvengedkfAHSILLSIFEGVQK 473
Cdd:cd14119    43 REIQILRRL-NHRNVIKLVDvlYNEEKQKLYMVMEYCVGGLQEMLdsapdkRLPIWQ---------AHGYFVQLIDGLEY 112
                          90       100
                  ....*....|....*....|....*....
gi 1720355205 474 LHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd14119   113 LHSQGIIHKDIKPGNLLLTTDGTLKISDF 141
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
32-147 7.89e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.16  E-value: 7.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  32 AVQKGDVVRVQQLLEKGADANACEDT-------------WGWTPLHNAVQAGRVDIVNLLLSHGADPHRRKKNGATPFII 98
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVVSPRATgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720355205  99 AGIQGDVKL----LEILLSCGADVNEC------DENGFTAFMEAAERGNAEALRFLFAK 147
Cdd:cd22192   176 LVLQPNKTFacqmYDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNIVMFQHLVQK 234
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
369-502 8.04e-05

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: 45.12  E-value: 8.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 369 KIAGTSEGAVYLGIydNRE----VAVKVFR-ENSPRGC-----KEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEW 438
Cdd:cd07839     7 KIGEGTYGTVFKAK--NREtheiVALKRVRlDDDDEGVpssalREICLLKEL-KHKNIVRLYDVLHSDKKLTLVFEYCDQ 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355205 439 TLEEFLRLPREEPvengEDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd07839    84 DLKKYFDSCNGDI----DPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADF 143
Ank_4 pfam13637
Ankyrin repeats (many copies);
241-293 8.26e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 8.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720355205 241 TPLIAAVERKHTGLVQMLLSReGINIDARDNEGKTALLIAVDKQLKEIVQLLL 293
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLKLLL 54
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
360-502 8.36e-05

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: 45.38  E-value: 8.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 360 LKIFIHDDyKIAGTSEGAVYLG---IYDNReVAVKVFR----ENSP-RGCKEVSCLRDCgDHSNLVAFYGREDDKGCLYV 431
Cdd:cd07873     1 LETYIKLD-KLGEGTYATVYKGrskLTDNL-VALKEIRleheEGAPcTAIREVSLLKDL-KHANIVTLHDIIHTEKSLTL 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355205 432 CVSLCEWTLEEFLRlpreepvENGEDKFAHSILLSIFE---GVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd07873    78 VFEYLDKDLKQYLD-------DCGNSINMHNVKLFLFQllrGLAYCHRRKVLHRDLKPQNLLINERGELKLADF 144
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
406-502 9.37e-05

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: 45.11  E-value: 9.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 406 CLRDcGDHSNLVAFYG---REDDkgcLYVCVSLCEWTLEEFLRLPREEPVENGEDKFAhSILLSIFEGVQKLH--LHgYS 480
Cdd:cd06617    53 SMRS-VDCPYTVTFYGalfREGD---VWICMEVMDTSLDKFYKKVYDKGLTIPEDILG-KIAVSIVKALEYLHskLS-VI 126
                          90       100
                  ....*....|....*....|..
gi 1720355205 481 HQDLQPQNILIDSKKAVRLADF 502
Cdd:cd06617   127 HRDVKPSNVLINRNGQVKLCDF 148
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
374-509 9.87e-05

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: 44.74  E-value: 9.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 374 SEGAVYLGIYDNREVAVKVFRENSPRGC--KEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCE-WTLEEFLRLPREE 450
Cdd:cd14058     5 SFGVVCKARWRNQIVAVKIIESESEKKAfeVEVRQLSRV-DHPNIIKLYGACSNQKPVCLVMEYAEgGSLYNVLHGKEPK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 451 PvengEDKFAHSI--LLSIFEGVQklHLHGYS-----HQDLQPQNILIDSKKAV-RLADF----DQ---------SIRWM 509
Cdd:cd14058    84 P----IYTAAHAMswALQCAKGVA--YLHSMKpkaliHRDLKPPNLLLTNGGTVlKICDFgtacDIsthmtnnkgSAAWM 157
PHA02878 PHA02878
ankyrin repeat protein; Provisional
25-122 1.08e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 45.26  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  25 DDSSLIKAVQKGDVVRVQQLLEKGADANAcEDTWGWTPLHNAVqaGRV---DIVNLLLSHGADPHRRKK-NGATPFIIAg 100
Cdd:PHA02878  201 NNSPLHHAVKHYNKPIVHILLENGASTDA-RDKCGNTPLHISV--GYCkdyDILKLLLEHGVDVNAKSYiLGLTALHSS- 276
                          90       100
                  ....*....|....*....|..
gi 1720355205 101 IQGDVKlLEILLSCGADVNECD 122
Cdd:PHA02878  277 IKSERK-LKLLLEYGADINSLN 297
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
376-502 1.11e-04

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


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 44.82  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIYDNREVAVKVFRENSP-----------RGCKEVSCLRdcgdHSNLVAFYGREDDKG--CLyVCVSLCEWTLEE 442
Cdd:cd14159     7 GCVYQAVMRNTEYAVKRLKEDSEldwsvvknsflTEVEKLSRFR----HPNIVDLAGYSAQQGnyCL-IYVYLPNGSLED 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355205 443 FLRLPREEPVENGEDKFahSILLSIFEGVQklHLHGYS----HQDLQPQNILIDSKKAVRLADF 502
Cdd:cd14159    82 RLHCQVSCPCLSWSQRL--HVLLGTARAIQ--YLHSDSpsliHGDVKSSNILLDAALNPKLGDF 141
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
386-543 1.16e-04

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: 44.86  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 386 REVAVKV----FRENSPRgckEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVSLCEWTlEEFLRLPREEPVENGEdkfAH 461
Cdd:cd14180    32 QEYAVKIisrrMEANTQR---EVAALRLCQSHPNIVALHEVLHDQYHTYLVMELLRGG-ELLDRIKKKARFSESE---AS 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 462 SILLSIFEGVQKLHLHGYSHQDLQPQNILI--DSKKA-VRLADFD-QSIRWMGESQMVRR-------------------- 517
Cdd:cd14180   105 QLMRSLVSAVSFMHEAGVVHRDLKPENILYadESDGAvLKVIDFGfARLRPQGSRPLQTPcftlqyaapelfsnqgydes 184
                         170       180
                  ....*....|....*....|....*..
gi 1720355205 518 -DLEDLGrLVLYVVMKGEIPFETLKTQ 543
Cdd:cd14180   185 cDLWSLG-VILYTMLSGQVPFQSKRGK 210
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
452-502 1.22e-04

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: 44.57  E-value: 1.22e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720355205 452 VENG---EDKfAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd14079    94 VQKGrlsEDE-ARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADF 146
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
376-502 1.23e-04

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: 44.71  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIY--DNR----EVAVKVFRENSPRGCKEvSCLRDCG-----DHSNLVAFYGreddkgclyVCVSLCEWTLEEFL 444
Cdd:cd05057    21 GTVYKGVWipEGEkvkiPVAIKVLREETGPKANE-EILDEAYvmasvDHPHLVRLLG---------ICLSSQVQLITQLM 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720355205 445 RL-PREEPVENGEDKFAHSILLS----IFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd05057    91 PLgCLLDYVRNHRDNIGSQLLLNwcvqIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDF 153
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
370-583 1.29e-04

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: 44.45  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 370 IAGTSEGAVYLGI--YDNREVAVKVFRENSP--RGCK-----------EVSCLRDCgDHSNLVAFYGREDDKGCL----- 429
Cdd:cd06628     8 IGSGSFGSVYLGMnaSSGELMAVKQVELPSVsaENKDrkksmldalqrEIALLREL-QHENIVQYLGSSSDANHLnifle 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 430 YVCVSLCEWTLEEFLRLPrEEPVENgedkFAHSILlsifEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF------- 502
Cdd:cd06628    87 YVPGGSVATLLNNYGAFE-ESLVRN----FVRQIL----KGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFgiskkle 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 503 ---------------DQSIRWMG------ESQMVRRDLEDLGRLVLYvVMKGEIPFETLkTQ-------NDEVLLTMSPD 554
Cdd:cd06628   158 anslstknngarpslQGSVFWMApevvkqTSYTRKADIWSLGCLVVE-MLTGTHPFPDC-TQmqaifkiGENASPTIPSN 235
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1720355205 555 --EETKDLIHCLFSPGENVKNCLVDLLGHPF 583
Cdd:cd06628   236 isSEARDFLEKTFEIDHNKRPTADELLKHPF 266
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
413-502 1.37e-04

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: 44.27  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 413 HSNLVAFYG----REDDKGCLYVCVsLCEW----TLEEFLRLPREEPVENgedkfAHSILLSIFEGVQKLHLHGYSHQDL 484
Cdd:cd14012    57 HPNLVSYLAfsieRRGRSDGWKVYL-LTEYapggSLSELLDSVGSVPLDT-----ARRWTLQLLEALEYLHRNGVVHKSL 130
                          90       100
                  ....*....|....*....|.
gi 1720355205 485 QPQNILIDSKKA---VRLADF 502
Cdd:cd14012   131 HAGNVLLDRDAGtgiVKLTDY 151
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
413-583 1.48e-04

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: 44.39  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 413 HSNLVAFYGREDDKGCLYVCVSLCE-WTLEEFLrlpreepVENG--EDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNI 489
Cdd:cd14098    60 HPGIVRLIDWYEDDQHIYLVMEYVEgGDLMDFI-------MAWGaiPEQHARELTKQILEAMAYTHSMGITHRDLKPENI 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 490 LI--DSKKAVRLADF------------------------------DQSIRwMGESQMVrrDLEDLGrLVLYVVMKGEIPF 537
Cdd:cd14098   133 LItqDDPVIVKISDFglakvihtgtflvtfcgtmaylapeilmskEQNLQ-GGYSNLV--DMWSVG-CLVYVMLTGALPF 208
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720355205 538 E-----------TLKTQNDEVLLTMSPDEETKDLIHCLFSPGENVKNCLVDLLGHPF 583
Cdd:cd14098   209 DgssqlpvekriRKGRYTQPPLVDFNISEEAIDFILRLLDVDPEKRMTAAQALDHPW 265
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
369-552 1.63e-04

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: 44.26  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 369 KIAGTSEGAVYLGIYDNR-EVAVKVFREN--SPRGCKEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVS-LCEWTLEEFL 444
Cdd:cd05072    14 KLGAGQFGEVWMGYYNNStKVAVKTLKPGtmSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEyMAKGSLLDFL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 445 RlpreePVENGEDKFAHSILLS--IFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQS----------------- 505
Cdd:cd05072    94 K-----SDEGGKVLLPKLIDFSaqIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLArviedneytaregakfp 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720355205 506 IRWMGESQM------VRRDLEDLGRLVLYVVMKGEIPFETLktQNDEVLLTMS 552
Cdd:cd05072   169 IKWTAPEAInfgsftIKSDVWSFGILLYEIVTYGKIPYPGM--SNSDVMSALQ 219
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
376-514 1.65e-04

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: 44.14  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIydNRE----VAVKVFR------ENSPRGCKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEW-----TL 440
Cdd:cd06627    14 GSVYKGL--NLNtgefVAIKQISlekipkSDLKSVMGEIDLLKKL-NHPNIVKYIGSVKTKDSLYIILEYVENgslasII 90
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355205 441 EEFLRLPreepvENGEDKFAHSILlsifEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSIRWMGESQM 514
Cdd:cd06627    91 KKFGKFP-----ESLVAVYIYQVL----EGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVEKD 155
PLN03224 PLN03224
probable serine/threonine protein kinase; Provisional
440-506 1.66e-04

probable serine/threonine protein kinase; Provisional


Pssm-ID: 178763 [Multi-domain]  Cd Length: 507  Bit Score: 44.68  E-value: 1.66e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720355205 440 LEEFL----RLPREEPVENGEDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSI 506
Cdd:PLN03224  287 LEEFMmagkKIPDNMPQDKRDINVIKGVMRQVLTGLRKLHRIGIVHRDIKPENLLVTVDGQVKIIDFGAAV 357
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
378-502 1.98e-04

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: 43.90  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 378 VYLGIYDNR---EVAVKVF-RENSPRG----CKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEW-TLEEFLRLPR 448
Cdd:cd14120     9 VFKGRHRKKpdlPVAIKCItKKNLSKSqnllGKEIKILKEL-SHENVVALLDCQETSSSVYLVMEYCNGgDLADYLQAKG 87
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720355205 449 EEPvengEDKFAHsILLSIFEGVQKLHLHGYSHQDLQPQNILI--DSKKA-------VRLADF 502
Cdd:cd14120    88 TLS----EDTIRV-FLQQIAAAMKALHSKGIVHRDLKPQNILLshNSGRKpspndirLKIADF 145
PHA02798 PHA02798
ankyrin-like protein; Provisional
72-328 2.03e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.44  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  72 VDIVNLLLSHGADPHRRKKNGATPF--IIAGI---QGDVKLLEILLSCGADVNECDENGFTAFMEAAERG---NAEALRF 143
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLctILSNIkdyKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLF 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 144 LFAKGANVNLrrqttkdkrrLKQGGATALMSAAEKGH---LEVLRILLnDMKAEVDARDN-MGRNAL---IRTllNWDCE 216
Cdd:PHA02798  131 MIENGADTTL----------LDKDGFTMLQVYLQSNHhidIEIIKLLL-EKGVDINTHNNkEKYDTLhcyFKY--NIDRI 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 217 NVeEITSILIQHGADVNVRGERGKTPLIAAV-------ERKHTGLVQMLLSRegINIDARDNEGKTALLIAVDKQLKEIV 289
Cdd:PHA02798  198 DA-DILKLFVDNGFIINKENKSHKKKFMEYLnsllydnKRFKKNILDFIFSY--IDINQVDELGFNPLYYSVSHNNRKIF 274
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1720355205 290 QLLLEKGAD-KC-----DDLVWIARRNHDYHLVKLLLPYVANPDT 328
Cdd:PHA02798  275 EYLLQLGGDiNIitelgNTCLFTAFENESKFIFNSILNKKPNKNT 319
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
376-583 2.04e-04

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: 43.86  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLgIYD---NREVAVKV--FRENSPRGCKEVSCLrDCG-------DHSNLVAFYG--REDDKGCLYVCVS-LCEWTL 440
Cdd:cd06653    16 GEVYL-CYDadtGRELAVKQvpFDPDSQETSKEVNAL-ECEiqllknlRHDRIVQYYGclRDPEEKKLSIFVEyMPGGSV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 441 EEFLRlPREEPVENGEDKFAHSILlsifEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSIR------------- 507
Cdd:cd06653    94 KDQLK-AYGALTENVTRRYTRQIL----QGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRiqticmsgtgiks 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 508 ------WM------GESQMVRRDLEDLGRLVlyVVMKGEIP----FETL------KTQNDEVLLTMSPDEETKDLIHCLF 565
Cdd:cd06653   169 vtgtpyWMspevisGEGYGRKADVWSVACTV--VEMLTEKPpwaeYEAMaaifkiATQPTKPQLPDGVSDACRDFLRQIF 246
                         250
                  ....*....|....*...
gi 1720355205 566 SPgENVKNCLVDLLGHPF 583
Cdd:cd06653   247 VE-EKRRPTAEFLLRHPF 263
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
26-151 2.15e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 44.62  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  26 DSSLIKAVQKGDVVRVQQLLeKGADANACE-DTWGWTPLHNAVQAGRVDIVNLLLShgADPhrRKKN---------GATP 95
Cdd:cd22192    18 ESPLLLAAKENDVQAIKKLL-KCPSCDLFQrGALGETALHVAALYDNLEAAVVLME--AAP--ELVNepmtsdlyqGETA 92
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720355205  96 FIIAGIQGDVKLLEILLSCGADVNECDENGfTAFME---------------AAERGNAEALRFLFAKGANV 151
Cdd:cd22192    93 LHIAVVNQNLNLVRELIARGADVVSPRATG-TFFRPgpknliyygehplsfAACVGNEEIVRLLIEHGADI 162
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
402-502 2.18e-04

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: 43.75  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 402 KEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVSLC-EWTLEEFLrlprEEPVENGEdKFAHSILLSIFEGVQKLHLHGYS 480
Cdd:cd14182    58 KEIDILRKVSGHPNIIQLKDTYETNTFFFLVFDLMkKGELFDYL----TEKVTLSE-KETRKIMRALLEVICALHKLNIV 132
                          90       100
                  ....*....|....*....|..
gi 1720355205 481 HQDLQPQNILIDSKKAVRLADF 502
Cdd:cd14182   133 HRDLKPENILLDDDMNIKLTDF 154
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
412-502 2.19e-04

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: 43.82  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 412 DHSNLVAFYGREDDKGCLYVCVSLC-----EWTLEEFLRLPrEEPVEngedKFAhsilLSIFEGVQKLHLHGYSHQDLQP 486
Cdd:cd14010    52 KHPNVLKFYEWYETSNHLWLVVEYCtggdlETLLRQDGNLP-ESSVR----KFG----RDLVRGLHYIHSKGIIYCDLKP 122
                          90
                  ....*....|....*.
gi 1720355205 487 QNILIDSKKAVRLADF 502
Cdd:cd14010   123 SNILLDGNGTLKLSDF 138
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
403-505 2.40e-04

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: 43.48  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 403 EVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEWTlEEFLRLpreepVENG--EDKFAHSILLSIFEGVQKLHLHGYS 480
Cdd:cd14167    51 EIAVLHKI-KHPNIVALDDIYESGGHLYLIMQLVSGG-ELFDRI-----VEKGfyTERDASKLIFQILDAVKYLHDMGIV 123
                          90       100
                  ....*....|....*....|....*...
gi 1720355205 481 HQDLQPQNIL---IDSKKAVRLADFDQS 505
Cdd:cd14167   124 HRDLKPENLLyysLDEDSKIMISDFGLS 151
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
456-584 2.52e-04

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: 43.53  E-value: 2.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 456 EDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSIRW--------------------MGESQMV 515
Cdd:cd14004   107 DEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSAAYIksgpfdtfvgtidyaapevlRGNPYGG 186
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720355205 516 R-RDLEDLGrLVLYVVMKGEIPF-ETLKTQNDEVLLTMSPDEETKDLIHCLFSPGENVKNCLVDLLGHPFF 584
Cdd:cd14004   187 KeQDIWALG-VLLYTLVFKENPFyNIEEILEADLRIPYAVSEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
YegI COG4248
Uncharacterized conserved protein YegI with protein kinase and helix-hairpin-helix DNA-binding ...
459-503 2.53e-04

Uncharacterized conserved protein YegI with protein kinase and helix-hairpin-helix DNA-binding domains [General function prediction only];


Pssm-ID: 443390 [Multi-domain]  Cd Length: 476  Bit Score: 44.31  E-value: 2.53e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1720355205 459 FAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFD 503
Cdd:COG4248   122 FLLRTARNLAAAVAALHAAGYVHGDVNPSNILVSDTALVTLIDTD 166
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
364-502 2.54e-04

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: 43.60  E-value: 2.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 364 IHDDYKI-------AGTSeGAVYLGIYDN--REVAVKVFREnSPRGCKEVSCLRDCGDHSNLVAFY----------GRED 424
Cdd:cd14171     2 ILEEYEVnwtqklgTGIS-GPVRVCVKKStgERFALKILLD-RPKARTEVRLHMMCSGHPNIVQIYdvyansvqfpGESS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 425 DKGCLYVCVSLCEWTlEEFLRLPREEpveNGEDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKK---AVRLAD 501
Cdd:cd14171    80 PRARLLIVMELMEGG-ELFDRISQHR---HFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSedaPIKLCD 155

                  .
gi 1720355205 502 F 502
Cdd:cd14171   156 F 156
Ank_4 pfam13637
Ankyrin repeats (many copies);
170-259 2.56e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 2.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 170 TALMSAAEKGHLEVLRILLndmkaevdardnmgrnalirtllnwdcenveeitsiliQHGADVNVRGERGKTPLIAAVER 249
Cdd:pfam13637   3 TALHAAAASGHLELLRLLL--------------------------------------EKGADINAVDGNGETALHFAASN 44
                          90
                  ....*....|
gi 1720355205 250 KHTGLVQMLL 259
Cdd:pfam13637  45 GNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
61-262 2.71e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 44.23  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  61 TPLHNAVQAGRVDIVN-LLLSHGADPHRRKKNGATPFIIAGIQGDVKLLEILLSCGAD-VNE---CD-ENGFTAFMEAAE 134
Cdd:cd22192    19 SPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEpmtSDlYQGETALHIAVV 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 135 RGNAEALRFLFAKGANVNLRRQT----TKDKRRLKQGGATALMSAAEKGHLEVLRILLNDmKAEVDARDNMGRNAL-IRT 209
Cdd:cd22192    99 NQNLNLVRELIARGADVVSPRATgtffRPGPKNLIYYGEHPLSFAACVGNEEIVRLLIEH-GADIRAQDSLGNTVLhILV 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720355205 210 LL---NWDCENVEEITSiLIQHGADV---NVRGERGKTPLIAAVERKHTGLVQMLLSRE 262
Cdd:cd22192   178 LQpnkTFACQMYDLILS-YDKEDDLQpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
125-269 2.77e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 44.41  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 125 GFTAFMEAAERGNAEALRFLFAKGANVNLRrqTTKDKRRLKQGGA------TALMSAAEKGHLEVLRILLND--MKAEVD 196
Cdd:cd22196    94 GQTALHIAIERRNMHLVELLVQNGADVHAR--ASGEFFKKKKGGPgfyfgeLPLSLAACTNQLDIVKFLLENphSPADIS 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 197 ARDNMGRNAL--IRTLLNWDCENVEEITS----ILIQhGADVN-------VRGERGKTPLIAAVERKHTGLVQMLLSREG 263
Cdd:cd22196   172 ARDSMGNTVLhaLVEVADNTPENTKFVTKmyneILIL-GAKIRpllkleeITNKKGLTPLKLAAKTGKIGIFAYILGREI 250

                  ....*.
gi 1720355205 264 INIDAR 269
Cdd:cd22196   251 KEPECR 256
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
376-502 2.79e-04

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: 43.04  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIYDNR-EVAVKVFREN--SPRG-CKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSL-CEWTLEEFLRLPREE 450
Cdd:cd05034     9 GEVWMGVWNGTtKVAVKTLKPGtmSPEAfLQEAQIMKKL-RHDKLVQLYAVCSDEEPIYIVTELmSKGSLLDYLRTGEGR 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720355205 451 PVengedKFAHSILLS--IFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd05034    88 AL-----RLPQLIDMAaqIASGMAYLESRNYIHRDLAARNILVGENNVCKVADF 136
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
358-502 2.86e-04

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: 43.44  E-value: 2.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 358 GKLKIFIhddyKIAGTSEGAvYLGIYDNRE------VAVKVFR----ENSP-RGCKEVSCLRDCgDHSNLVAFYGREDDK 426
Cdd:cd07872     3 GKMETYI----KLEKLGEGT-YATVFKGRSkltenlVALKEIRleheEGAPcTAIREVSLLKDL-KHANIVTLHDIVHTD 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720355205 427 GCLYVCVSLCEWTLEEFLRlpreepvENGEDKFAHSI---LLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd07872    77 KSLTLVFEYLDKDLKQYMD-------DCGNIMSMHNVkifLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADF 148
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
403-514 3.06e-04

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: 43.30  E-value: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 403 EVSCLRDCgDHSNLVAFYGREDDK--GCLYVCVSLCE-WTLEEFLRLPREEpveNG--EDKFAHSILLSIFEGVQKLHLH 477
Cdd:cd08217    49 EVNILREL-KHPNIVRYYDRIVDRanTTLYIVMEYCEgGDLAQLIKKCKKE---NQyiPEEFIWKIFTQLLLALYECHNR 124
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1720355205 478 GYS-----HQDLQPQNILIDSKKAVRLADFDQSiRWMGESQM 514
Cdd:cd08217   125 SVGggkilHRDLKPANIFLDSDNNVKLGDFGLA-RVLSHDSS 165
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
376-583 3.30e-04

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: 43.15  E-value: 3.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLgIYD---NREVAVKV--FRENSPRGCKEVSCLrDCG-------DHSNLVAFYGREDDKGclyvcvslcEWTLEEF 443
Cdd:cd06651    21 GRVYL-CYDvdtGRELAAKQvqFDPESPETSKEVSAL-ECEiqllknlQHERIVQYYGCLRDRA---------EKTLTIF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 444 LRLPREEPVENG-------EDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSIR--------- 507
Cdd:cd06651    90 MEYMPGGSVKDQlkaygalTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRlqticmsgt 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 508 ----------WM------GESQMVRRDLEDLGRLVlyVVMKGEIP----FETL------KTQNDEVLLTMSPDEETKDLI 561
Cdd:cd06651   170 girsvtgtpyWMspevisGEGYGRKADVWSLGCTV--VEMLTEKPpwaeYEAMaaifkiATQPTNPQLPSHISEHARDFL 247
                         250       260
                  ....*....|....*....|..
gi 1720355205 562 HCLFSPGENvKNCLVDLLGHPF 583
Cdd:cd06651   248 GCIFVEARH-RPSAEELLRHPF 268
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
217-298 3.39e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.85  E-value: 3.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 217 NVEEITSILIQHGADVNVRGERGKTPLIAAVERKHTGLVQMLL--SREGINIDARDN--EGKTALLIAVDKQLKEIVQLL 292
Cdd:cd22192    29 DVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMeaAPELVNEPMTSDlyQGETALHIAVVNQNLNLVREL 108

                  ....*.
gi 1720355205 293 LEKGAD 298
Cdd:cd22192   109 IARGAD 114
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
367-502 3.45e-04

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: 43.05  E-value: 3.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 367 DYKIAGTSEGavyLGI-------YD---NREVAVKVFRENsPRGCKEVSCLRDCGDHSNLVA----FYGREDDKGCLYVc 432
Cdd:cd14089     1 DYTISKQVLG---LGIngkvlecFHkktGEKFALKVLRDN-PKARREVELHWRASGCPHIVRiidvYENTYQGRKCLLV- 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720355205 433 VSLCEWTLEEFLRLPreepvENGEDKF----AHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKK---AVRLADF 502
Cdd:cd14089    76 VMECMEGGELFSRIQ-----ERADSAFtereAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGpnaILKLTDF 147
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
412-583 3.48e-04

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 42.85  E-value: 3.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 412 DHSNLVAFYGREDDKGCLYVCVSLCE----WT-LEEFLRLPREEpvengedkfAHSILLSIFEGVQKLHLHGYSHQDLQP 486
Cdd:cd14007    58 RHPNILRLYGYFEDKKRIYLILEYAPngelYKeLKKQKRFDEKE---------AAKYIYQLALALDYLHSKNIIHRDIKP 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 487 QNILIDSKKAVRLADFDqsirWMGESQMVRR------------------------DLEDLGRLvLYVVMKGEIPFETlKT 542
Cdd:cd14007   129 ENILLGSNGELKLADFG----WSVHAPSNRRktfcgtldylppemvegkeydykvDIWSLGVL-CYELLVGKPPFES-KS 202
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720355205 543 QND------EVLLTMSPD--EETKDLIHCLFspgenVKNC-----LVDLLGHPF 583
Cdd:cd14007   203 HQEtykriqNVDIKFPSSvsPEAKDLISKLL-----QKDPskrlsLEQVLNHPW 251
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
369-502 4.49e-04

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: 42.64  E-value: 4.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 369 KIAGTSEGAVYL--GIYDNREVAVK-VFRENSPRGCKEVS----CLRDCGDHSNLVAFYGREDDKGCLYVCVSLCEWTlE 441
Cdd:cd08225     7 KIGEGSFGKIYLakAKSDSEHCVIKeIDLTKMPVKEKEASkkevILLAKMKHPNIVTFFASFQENGRLFIVMEYCDGG-D 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720355205 442 EFLRLPREEPVENGEDKFAhSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSK-KAVRLADF 502
Cdd:cd08225    86 LMKRINRQRGVLFSEDQIL-SWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNgMVAKLGDF 146
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
361-502 5.03e-04

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: 42.72  E-value: 5.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 361 KIFIhDDYKIAGTSEGAVYLGI--YDNREVAVKVFRENSPRG-------CKEVSCLRDCgDHSNLVAFYGREDDKGCLYV 431
Cdd:cd06633    21 EIFV-DLHEIGHGSFGAVYFATnsHTNEVVAIKKMSYSGKQTnekwqdiIKEVKFLQQL-KHPNTIEYKGCYLKDHTAWL 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720355205 432 CVSLCEWTLEEFLRLpREEPVENGEdkfAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd06633    99 VMEYCLGSASDLLEV-HKKPLQEVE---IAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADF 165
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
456-537 5.29e-04

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: 42.65  E-value: 5.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 456 EDKFAhSILLSIFEGVQKLHLHGYSHQDLQPQNILID---SKKAVRLADFDQSIRW---------------------MGE 511
Cdd:cd14113   102 EEKIR-FYLREILEALQYLHNCRIAHLDLKPENILVDqslSKPTIKLADFGDAVQLnttyyihqllgspefaapeiiLGN 180
                          90       100
                  ....*....|....*....|....*.
gi 1720355205 512 SQMVRRDLEDLGRLVlYVVMKGEIPF 537
Cdd:cd14113   181 PVSLTSDLWSIGVLT-YVLLSGVSPF 205
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
451-502 5.43e-04

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: 42.64  E-value: 5.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720355205 451 PVENGEDkfahsILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd07863   106 PAETIKD-----LMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADF 152
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
448-584 5.51e-04

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: 42.61  E-value: 5.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 448 REEPVEngeDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKA---VRLADFDQSiRWMGESQMVRR------- 517
Cdd:cd14197   104 REEAFK---EKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPlgdIKIVDFGLS-RILKNSEELREimgtpey 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 518 ---------------DLEDLGRLVlYVVMKGEIPFetLKTQNDEVLLTMSP-------------DEETKDLIHCLFSPGE 569
Cdd:cd14197   180 vapeilsyepistatDMWSIGVLA-YVMLTGISPF--LGDDKQETFLNISQmnvsyseeefehlSESAIDFIKTLLIKKP 256
                         170
                  ....*....|....*
gi 1720355205 570 NVKNCLVDLLGHPFF 584
Cdd:cd14197   257 ENRATAEDCLKHPWL 271
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
470-582 5.53e-04

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: 42.38  E-value: 5.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 470 GVQKLHLHGYSHQDLQPQNILIDSKKA---VRLADFDQSiRWMGESQMVRR-------------------------DLED 521
Cdd:cd14084   123 AVKYLHSNGIIHRDLKPENVLLSSQEEeclIKITDFGLS-KILGETSLMKTlcgtptylapevlrsfgtegytravDCWS 201
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720355205 522 LGrLVLYVVMKGEIPF------ETLKTQNDEVLLTMSP------DEETKDLIHCLFSPGENVKNCLVDLLGHP 582
Cdd:cd14084   202 LG-VILFICLSGYPPFseeytqMSLKEQILSGKYTFIPkawknvSEEAKDLVKKMLVVDPSRRPSIEEALEHP 273
PHA02946 PHA02946
ankyin-like protein; Provisional
75-279 5.65e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 43.12  E-value: 5.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  75 VNLLLSHGADPHRRKKNGATPFIIAGIQGDVKLLEILLSCGADVNECDENGFTA--FMEAAERGNAEALRFLFAKGANVN 152
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPlyYLSGTDDEVIERINLLVQYGAKIN 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 153 lrrqttkdkRRLKQGGATALMSAAEKGHlevlRILLNDMKAEVDAR--DNMGRNALIRTLLNwdcENVEEIT-SILIQHG 229
Cdd:PHA02946  135 ---------NSVDEEGCGPLLACTDPSE----RVFKKIMSIGFEARivDKFGKNHIHRHLMS---DNPKASTiSWMMKLG 198
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720355205 230 ADVNVRGERGKTPL--IAAVERKHTGLVQMLLSREGINIDARDNEGKTALLI 279
Cdd:PHA02946  199 ISPSKPDHDGNTPLhiVCSKTVKNVDIINLLLPSTDVNKQNKFGDSPLTLLI 250
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
236-298 5.69e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 43.25  E-value: 5.69e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355205 236 GERGKTPLIAAVERKHTG---LVQMLLS--------REGINIDARDN--EGKTALLIAVDKQLKEIVQLLLEKGAD 298
Cdd:cd22193    26 SSTGKTCLMKALLNLNPGtndTIRILLDiaektdnlKRFINAEYTDEyyEGQTALHIAIERRQGDIVALLVENGAD 101
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
445-502 5.82e-04

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: 42.56  E-value: 5.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355205 445 RLPREEPVEngeDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd07856    98 RLLTSRPLE---KQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDF 152
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
376-505 5.87e-04

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: 42.30  E-value: 5.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLG--IYDNREVAVKVF--RENSPRGCK-EVSCLRDCGDHSNLVAFYGR--------EDDKgcLYVCVSLC-EWTLE 441
Cdd:cd06636    30 GQVYKGrhVKTGQLAAIKVMdvTEDEEEEIKlEINMLKKYSHHRNIATYYGAfikksppgHDDQ--LWLVMEFCgAGSVT 107
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355205 442 EFLRLPREEPVEngEDKFAHsILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQS 505
Cdd:cd06636   108 DLVKNTKGNALK--EDWIAY-ICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS 168
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
385-590 5.88e-04

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: 42.35  E-value: 5.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 385 NREVAVKVFRENS-----PRGCKEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVSLCEWTLEEFLRLPREepveNGEDKF 459
Cdd:cd06616    31 GTIMAVKRIRSTVdekeqKRLLMDLDVVMRSSDCPYIVKFYGALFREGDCWICMELMDISLDKFYKYVYE----VLDSVI 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 460 AHSILLSIFEGVQKL--HL---HGYSHQDLQPQNILIDSKKAVRLADF--------------DQSIR-WMGESQM----- 514
Cdd:cd06616   107 PEEILGKIAVATVKAlnYLkeeLKIIHRDVKPSNILLDRNGNIKLCDFgisgqlvdsiaktrDAGCRpYMAPERIdpsas 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 515 -----VRRDLEDLGrLVLYVVMKGEIPFETLKTQNDEVLLT-------MSPDE------ETKDLIHCLFSPGENVKNCLV 576
Cdd:cd06616   187 rdgydVRSDVWSLG-ITLYEVATGKFPYPKWNSVFDQLTQVvkgdppiLSNSEerefspSFVNFVNLCLIKDESKRPKYK 265
                         250
                  ....*....|....
gi 1720355205 577 DLLGHPFFWTWENR 590
Cdd:cd06616   266 ELLKHPFIKMYEER 279
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
477-588 6.10e-04

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: 42.36  E-value: 6.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 477 HGYSHQDLQPQNILIDSKKAVRLADFDQSIR---------------WMGESQM---------VRRDLEDLGrLVLYVVMK 532
Cdd:cd06618   134 HGVIHRDVKPSNILLDESGNVKLCDFGISGRlvdskaktrsagcaaYMAPERIdppdnpkydIRADVWSLG-ISLVELAT 212
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355205 533 GEIPFETLKTQNdEVLLTMSPDEETKDLIHCLFSPG--ENVKNCLV----------DLLGHPFFWTWE 588
Cdd:cd06618   213 GQFPYRNCKTEF-EVLTKILNEEPPSLPPNEGFSPDfcSFVDLCLTkdhryrpkyrELLQHPFIRRYE 279
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
402-564 6.48e-04

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: 42.43  E-value: 6.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 402 KEVSCLRDCgDHSNLVAFYGR-EDDKGCLYVCVSLCEW-TLEEFLRLPREEPVEngedkFAHSILLSIFEGVQKLH-LHG 478
Cdd:cd06620    52 RELQILHEC-HSPYIVSFYGAfLNENNNIIICMEYMDCgSLDKILKKKGPFPEE-----VLGKIAVAVLEGLTYLYnVHR 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 479 YSHQDLQPQNILIDSKKAVRLADFD------QSI--------------RWMGESQMVRRDLEDLGRLVLYVVMkGEIPFE 538
Cdd:cd06620   126 IIHRDIKPSNILVNSKGQIKLCDFGvsgeliNSIadtfvgtstymspeRIQGGKYSVKSDVWSLGLSIIELAL-GEFPFA 204
                         170       180
                  ....*....|....*....|....*.
gi 1720355205 539 TLKTQNDEVLLTMSpdeeTKDLIHCL 564
Cdd:cd06620   205 GSNDDDDGYNGPMG----ILDLLQRI 226
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
403-518 6.78e-04

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: 42.29  E-value: 6.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 403 EVSCLRDCGDHSNLVAFYGR--EDDK---GCLYVCVSLCEW-TLEEFLR--LPREEPVEngeDKFAHSILLSIFEGVQKL 474
Cdd:cd06639    68 EYNILRSLPNHPNVVKFYGMfyKADQyvgGQLWLVLELCNGgSVTELVKglLKCGQRLD---EAMISYILYGALLGLQHL 144
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1720355205 475 HLHGYSHQDLQPQNILIDSKKAVRLADFDQSIRWMgeSQMVRRD 518
Cdd:cd06639   145 HNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT--SARLRRN 186
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
403-537 7.21e-04

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; 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. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 42.29  E-value: 7.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 403 EVSCLRDCGDHSNLVAFYGREDDKGCLYVCVSLCEW-TLEEFLRLPR---EEPV---ENGEDKFAHSILLSIF-----EG 470
Cdd:cd05089    52 ELEVLCKLGHHPNIINLLGACENRGYLYIAIEYAPYgNLLDFLRKSRvleTDPAfakEHGTASTLTSQQLLQFasdvaKG 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 471 VQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQS---------------IRWMGESQM------VRRDLEDLGRLVLYV 529
Cdd:cd05089   132 MQYLSEKQFIHRDLAARNVLVGENLVSKIADFGLSrgeevyvkktmgrlpVRWMAIESLnysvytTKSDVWSFGVLLWEI 211

                  ....*...
gi 1720355205 530 VMKGEIPF 537
Cdd:cd05089   212 VSLGGTPY 219
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
369-502 7.62e-04

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: 41.97  E-value: 7.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 369 KIAGTSEGAvYLGIYD--NRE----VAVKVF--RENSPR----GCKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLC 436
Cdd:cd07847     5 KLSKIGEGS-YGVVFKcrNREtgqiVAIKKFveSEDDPVikkiALREIRMLKQL-KHPNLVNLIEVFRRKRKLHLVFEYC 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720355205 437 EWT-LEEFLRLPREEPVENGEdkfahSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd07847    83 DHTvLNELEKNPRGVPEHLIK-----KIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDF 144
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
412-584 8.08e-04

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: 41.84  E-value: 8.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 412 DHSNLVAFYGREDDKGCLYVCVSLCEwtLEEFLRL-PREEPVENGEDKFahsILLSIFEGVQKLHLHGYSHQDLQPQNIL 490
Cdd:cd14187    65 AHQHVVGFHGFFEDNDFVYVVLELCR--RRSLLELhKRRKALTEPEARY---YLRQIILGCQYLHRNRVIHRDLKLGNLF 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 491 IDSKKAVRLADFD--QSIRWMGESQMV--------------------RRDLEDLGrLVLYVVMKGEIPFET-------LK 541
Cdd:cd14187   140 LNDDMEVKIGDFGlaTKVEYDGERKKTlcgtpnyiapevlskkghsfEVDIWSIG-CIMYTLLVGKPPFETsclketyLR 218
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1720355205 542 TQNDEVLLTMSPDEETKDLIHCLFSPGENVKNCLVDLLGHPFF 584
Cdd:cd14187   219 IKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELLNDEFF 261
pknD PRK13184
serine/threonine-protein kinase PknD;
376-491 8.71e-04

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 42.84  E-value: 8.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGiYD---NREVAVKVFREN-------SPRGCKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCE-WTLEEFL 444
Cdd:PRK13184   16 GEVYLA-YDpvcSRRVALKKIREDlsenpllKKRFLREAKIAADL-IHPGIVPVYSICSDGDPVYYTMPYIEgYTLKSLL 93
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720355205 445 RLPREEPVENGEDKFAHSI--LLSIF----EGVQKLHLHGYSHQDLQPQNILI 491
Cdd:PRK13184   94 KSVWQKESLSKELAEKTSVgaFLSIFhkicATIEYVHSKGVLHRDLKPDNILL 146
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
369-554 8.79e-04

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 41.94  E-value: 8.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 369 KIAGTSEGAVYLGIYDNrEVAVKVFRENSPRGCK------EVSCLRDCgDHSNLVAFYGREDdKGCLYVCVSLCEWT-LE 441
Cdd:cd14149    19 RIGSGSFGTVYKGKWHG-DVAVKILKVVDPTPEQfqafrnEVAVLRKT-RHVNILLFMGYMT-KDNLAIVTQWCEGSsLY 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 442 EFLRLPreepvengEDKFAHSILLSIF----EGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSI---RWMGESQM 514
Cdd:cd14149    96 KHLHVQ--------ETKFQMFQLIDIArqtaQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvksRWSGSQQV 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355205 515 ------------------------VRRDLEDLGrLVLYVVMKGEIPFETLKTQNDEVLLT----MSPD 554
Cdd:cd14149   168 eqptgsilwmapevirmqdnnpfsFQSDVYSYG-IVLYELMTGELPYSHINNRDQIIFMVgrgyASPD 234
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
107-262 8.91e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 42.82  E-value: 8.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 107 LLEILLSCG-----------ADVNECDENGFTAFMEAAERGNAEALRFLFAKGANVNLRRQTT----KDKRRLKQGGATA 171
Cdd:cd22194   112 IVRILLAFAeengildrfinAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpKYKHEGFYFGETP 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 172 LMSAAEKGHLEVLRILLNDMKAEVDARDNMGRN---ALIRTLLNWDCEN--VEEITSILIQHGADVN---VRGERGKTPL 243
Cdd:cd22194   192 LALAACTNQPEIVQLLMEKESTDITSQDSRGNTvlhALVTVAEDSKTQNdfVKRMYDMILLKSENKNletIRNNEGLTPL 271
                         170
                  ....*....|....*....
gi 1720355205 244 IAAVERKHTGLVQMLLSRE 262
Cdd:cd22194   272 QLAAKMGKAEILKYILSRE 290
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
463-501 9.15e-04

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: 41.72  E-value: 9.15e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1720355205 463 ILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLAD 501
Cdd:cd14027    95 IILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIAD 133
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
457-584 9.33e-04

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: 41.70  E-value: 9.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 457 DKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFD-----------------------QSIRWMGESQ 513
Cdd:cd05611    96 EDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGlsrnglekrhnkkfvgtpdylapETILGVGDDK 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 514 MVrrDLEDLGrLVLYVVMKGEIPF--ETLKT--QN---------DEVLLTMSPdeETKDLIHCLFSPGENVK---NCLVD 577
Cdd:cd05611   176 MS--DWWSLG-CVIFEFLFGYPPFhaETPDAvfDNilsrrinwpEEVKEFCSP--EAVDLINRLLCMDPAKRlgaNGYQE 250

                  ....*..
gi 1720355205 578 LLGHPFF 584
Cdd:cd05611   251 IKSHPFF 257
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
376-502 9.38e-04

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: 41.81  E-value: 9.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIYD------NREVAVKVF-RENSPRGC----KEVSCLRDCgDHSNLVAFYG---REDDKGCLYVCVSLCEWTLE 441
Cdd:cd05080    18 GKVSLYCYDptndgtGEMVAVKALkADCGPQHRsgwkQEIDILKTL-YHENIVKYKGccsEQGGKSLQLIMEYVPLGSLR 96
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720355205 442 EFLrlPReepvengedkfaHSILLS--------IFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd05080    97 DYL--PK------------HSIGLAqlllfaqqICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDF 151
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
387-502 9.65e-04

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 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 FGFR1 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: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 41.92  E-value: 9.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 387 EVAVKVFRENSPRG-----CKEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVSLC-EWTLEEFLRL-----------PRE 449
Cdd:cd05098    47 KVAVKMLKSDATEKdlsdlISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYAsKGNLREYLQArrppgmeycynPSH 126
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720355205 450 EPVENGEDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd05098   127 NPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADF 179
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
129-287 9.71e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 42.44  E-value: 9.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 129 FMEAAERGNAEALRFLFAKGANVNLRRQTTK------DKRRLKQGGATALMSA----AEKGHlEVLRILL-----ND--- 190
Cdd:cd22194    49 RLKKVSEAAVEELGELLKELKDLSRRRRKTDvpdflmHKLTASDTGKTCLMKAllniNENTK-EIVRILLafaeeNGild 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 191 --MKAEVDARDNMGRNALirtllNWDCEN-VEEITSILIQHGADVNVRGER--------------GKTPLIAAVERKHTG 253
Cdd:cd22194   128 rfINAEYTEEAYEGQTAL-----NIAIERrQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPE 202
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1720355205 254 LVQMLLSREGINIDARDNEGKTAL--LIAVDKQLKE 287
Cdd:cd22194   203 IVQLLMEKESTDITSQDSRGNTVLhaLVTVAEDSKT 238
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
25-262 9.80e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 42.38  E-value: 9.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  25 DDSSLIKAVQKGDVVRVQQLLEKgadaNACEDTWGWTPLHNAVQaGRVDIVNLLLSHGADPHRrkKNGATPFIIAgiqgd 104
Cdd:TIGR00870  52 GRSALFVAAIENENLELTELLLN----LSCRGAVGDTLLHAISL-EYVDAVEAILLHLLAAFR--KSGPLELAND----- 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 105 vklleillSCGADVNEcdenGFTAFMEAAERGNAEALRFLFAKGANVNLRR-----QTTKDKRRLKQGGAtALMSAAEKG 179
Cdd:TIGR00870 120 --------QYTSEFTP----GITALHLAAHRQNYEIVKLLLERGASVPARAcgdffVKSQGVDSFYHGES-PLNAAACLG 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 180 HLEVLRILLNDmKAEVDARDNMGrNALIRtLLNWDCENVEEIT-------SILIQHGADVN-------VRGERGKTPLIA 245
Cdd:TIGR00870 187 SPSIVALLSED-PADILTADSLG-NTLLH-LLVMENEFKAEYEelscqmyNFALSLLDKLRdskelevILNHQGLTPLKL 263
                         250
                  ....*....|....*..
gi 1720355205 246 AVERKHTGLVQMLLSRE 262
Cdd:TIGR00870 264 AAKEGRIVLFRLKLAIK 280
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
376-520 9.91e-04

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 41.84  E-value: 9.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIYDNR------EVAVKVFRENSpRGC------KEVSCLRDCGdHSNLVAFYG---REDDKGCLYVCVSLCEWTL 440
Cdd:cd05079    18 GKVELCRYDPEgdntgeQVAVKSLKPES-GGNhiadlkKEIEILRNLY-HENIVKYKGictEDGGNGIKLIMEFLPSGSL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 441 EEFLrlPREEPVENGEDKFAHSIllSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF--DQSIRWMGESQMVRRD 518
Cdd:cd05079    96 KEYL--PRNKNKINLKQQLKYAV--QICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFglTKAIETDKEYYTVKDD 171

                  ..
gi 1720355205 519 LE 520
Cdd:cd05079   172 LD 173
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
367-502 9.94e-04

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: 41.55  E-value: 9.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 367 DYKIAGTSEGAVYLGIYDNREV------AVKVFR----ENSPRGCKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLC 436
Cdd:cd06646    10 DYELIQRVGSGTYGDVYKARNLhtgelaAVKIIKlepgDDFSLIQQEIFMVKEC-KHCNIVAYFGSYLSREKLWICMEYC 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720355205 437 EW-TLEEFLRLprEEPVenGEDKFAHsILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd06646    89 GGgSLQDIYHV--TGPL--SELQIAY-VCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADF 150
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
376-549 1.01e-03

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: 41.64  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIYDNRE-----VAVKVFRENSPRGCK-----EVSCLRDCgDHSNLVAFYGR-EDDKgcLYVCVSLCEW-TLEEF 443
Cdd:cd05056    20 GDVYQGVYMSPEnekiaVAVKTCKNCTSPSVRekflqEAYIMRQF-DHPHIVKLIGViTENP--VWIVMELAPLgELRSY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 444 LRLPREEpvengedkFAHSILL----SIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF-------DQS------- 505
Cdd:cd05056    97 LQVNKYS--------LDLASLIlyayQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFglsrymeDESyykaskg 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720355205 506 ---IRWMG-ESQMVRR-----DLEDLGRLVLYVVMKGEIPFETLKtqNDEVLL 549
Cdd:cd05056   169 klpIKWMApESINFRRftsasDVWMFGVCMWEILMLGVKPFQGVK--NNDVIG 219
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
467-584 1.02e-03

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


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 41.42  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 467 IFEGVQKLHLHGYSHQDLQPQNILIDSKKA--VRLADF--------DQSIRW------MGESQMVRR-------DLEDLG 523
Cdd:cd14114   109 VCEGLCHMHENNIVHLDIKPENIMCTTKRSneVKLIDFglathldpKESVKVttgtaeFAAPEIVERepvgfytDMWAVG 188
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355205 524 RLVlYVVMKGEIPF------ETLKT-------QNDEVLLTMSPdeETKDLIHCLFSPGENVKNCLVDLLGHPFF 584
Cdd:cd14114   189 VLS-YVLLSGLSPFagenddETLRNvkscdwnFDDSAFSGISE--EAKDFIRKLLLADPNKRMTIHQALEHPWL 259
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
470-502 1.16e-03

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: 41.83  E-value: 1.16e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1720355205 470 GVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd05599   113 AIESIHKLGYIHRDIKPDNLLLDARGHIKLSDF 145
Ank_5 pfam13857
Ankyrin repeats (many copies);
153-206 1.17e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 1.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720355205 153 LRRQTTKDKRRLKQGGATALMSAAEKGHLEVLRILLNdMKAEVDARDNMGRNAL 206
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTAL 53
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
376-548 1.19e-03

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: 41.44  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIYD-NREVAVKVFREN--SPRGCKEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVSLCEWTLEEFLRlpreepv 452
Cdd:cd14203     9 GEVWMGTWNgTTKVAIKTLKPGtmSPEAFLEEAQIMKKLRHDKLVQLYAVVSEEPIYIVTEFMSKGSLLDFLK------- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 453 eNGEDKFAH-----SILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQS-----------------IRWMG 510
Cdd:cd14203    82 -DGEGKYLKlpqlvDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLArliedneytarqgakfpIKWTA 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1720355205 511 -ESQM-----VRRDLEDLGRLVLYVVMKGEIPFETLktQNDEVL 548
Cdd:cd14203   161 pEAALygrftIKSDVWSFGILLTELVTKGRVPYPGM--NNREVL 202
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
378-502 1.25e-03

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: 41.31  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 378 VYLGIydNRE----VAVKVFRENSPRGC-----KEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEWTLEEFLRLPR 448
Cdd:cd07836    16 VYKGR--NRTtgeiVALKEIHLDAEEGTpstaiREISLMKEL-KHENIVRLHDVIHTENKLMLVFEYMDKDLKKYMDTHG 92
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355205 449 EE-PVENGEDK-FAHSILlsifEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd07836    93 VRgALDPNTVKsFTYQLL----KGIAFCHENRVLHRDLKPQNLLINKRGELKLADF 144
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
412-502 1.28e-03

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: 41.19  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 412 DHSNLVAFYGREDD--KGCLYVCVSLCEwtLEEFLRLPREEPVEngEDKfAHSILLSIFEGVQKLHLHGYSHQDLQPQNI 489
Cdd:cd14118    72 DHPNVVKLVEVLDDpnEDNLYMVFELVD--KGAVMEVPTDNPLS--EET-ARSYFRDIVLGIEYLHYQKIIHRDIKPSNL 146
                          90
                  ....*....|...
gi 1720355205 490 LIDSKKAVRLADF 502
Cdd:cd14118   147 LLGDDGHVKIADF 159
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
463-505 1.29e-03

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: 41.76  E-value: 1.29e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1720355205 463 ILLSIfEGVQKLhlhGYSHQDLQPQNILIDSKKAVRLADFDQS 505
Cdd:cd05629   110 CVLAI-EAVHKL---GFIHRDIKPDNILIDRGGHIKLSDFGLS 148
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
467-502 1.32e-03

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: 41.21  E-value: 1.32e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1720355205 467 IFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd14078   110 IVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDF 145
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
170-298 1.64e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.92  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 170 TALMSAAEKGHLEVLRILLNDMKAEVDARDNMGRNALIRTLLNWDCENV------------EEITSILIQhgadvnvrge 237
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAvvlmeaapelvnEPMTSDLYQ---------- 88
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355205 238 rGKTPLIAAVERKHTGLVQMLLSREGINIDAR----------DNE---GKTALLIAVDKQLKEIVQLLLEKGAD 298
Cdd:cd22192    89 -GETALHIAVVNQNLNLVRELIARGADVVSPRatgtffrpgpKNLiyyGEHPLSFAACVGNEEIVRLLIEHGAD 161
Ank_5 pfam13857
Ankyrin repeats (many copies);
111-154 1.66e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 1.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1720355205 111 LLSCG-ADVNECDENGFTAFMEAAERGNAEALRFLFAKGANVNLR 154
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLK 45
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
374-502 1.68e-03

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: 40.92  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 374 SEGAVYLGIY--DNREVAVKVFRENSPRG-----CKEVSCLRDC--GDHSNLVAFYGreddkgCLYVCVSLceWTLEEF- 443
Cdd:cd06917    13 SYGAVYRGYHvkTGRVVALKVLNLDTDDDdvsdiQKEVALLSQLklGQPKNIIKYYG------SYLKGPSL--WIIMDYc 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355205 444 ----LR-LPREEPVEngeDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd06917    85 eggsIRtLMRAGPIA---ERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDF 145
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
376-517 1.82e-03

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: 40.91  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIYDNRE-------VAVKVFRENSPRGCK-----EVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCE-WTLEE 442
Cdd:cd05049    19 GKVFLGECYNLEpeqdkmlVAVKTLKDASSPDARkdferEAELLTNL-QHENIVKFYGVCTEGDPLLMVFEYMEhGDLNK 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 443 FLRL----------PREEPVENGEDKFAHsILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQS------- 505
Cdd:cd05049    98 FLRShgpdaaflasEDSAPGELTLSQLLH-IAVQIASGMVYLASQHFVHRDLATRNCLVGTNLVVKIGDFGMSrdiystd 176
                         170       180
                  ....*....|....*....|....
gi 1720355205 506 -----------IRWMG-ESQMVRR 517
Cdd:cd05049   177 yyrvgghtmlpIRWMPpESILYRK 200
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
124-153 1.88e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 1.88e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1720355205  124 NGFTAFMEAAERGNAEALRFLFAKGANVNL 153
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
369-554 1.96e-03

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: 40.81  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 369 KIAGTSEGAVYLGIYDNrEVAVKVFRENSPRGCK------EVSCLRDCgDHSNLVAFYGREDdKGCLYVCVSLCEWT-LE 441
Cdd:cd14151    15 RIGSGSFGTVYKGKWHG-DVAVKMLNVTAPTPQQlqafknEVGVLRKT-RHVNILLFMGYST-KPQLAIVTQWCEGSsLY 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 442 EFLRLpreepvenGEDKFAHSILLSIF----EGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSI---RWMGESQM 514
Cdd:cd14151    92 HHLHI--------IETKFEMIKLIDIArqtaQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATvksRWSGSHQF 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355205 515 ------------------------VRRDLEDLGrLVLYVVMKGEIPFETLKTQNDEVLL----TMSPD 554
Cdd:cd14151   164 eqlsgsilwmapevirmqdknpysFQSDVYAFG-IVLYELMTGQLPYSNINNRDQIIFMvgrgYLSPD 230
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
445-502 2.13e-03

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: 40.45  E-value: 2.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355205 445 RLPREEpvengedkfAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd14073    97 RLPERE---------ARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADF 145
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
470-506 2.16e-03

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: 40.47  E-value: 2.16e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1720355205 470 GVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSI 506
Cdd:cd14663   112 AVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSA 148
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
372-502 2.19e-03

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: 38.96  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 372 GTSEGAVYL-GIYDNREVAVKVFR-ENSPRGC---KEVSCLRDCGDHS-NLVAFYGREDDKGCLYVCVSLcewtLEEFLr 445
Cdd:cd13968     4 GASAKVFWAeGECTTIGVAVKIGDdVNNEEGEdleSEMDILRRLKGLElNIPKVLVTEDVDGPNILLMEL----VKGGT- 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720355205 446 LPREEPVENGEDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd13968    79 LIAYTQEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDF 135
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
439-509 2.38e-03

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: 40.44  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 439 TLEEFL--RLPREEP-VENGEDKFAHS--------ILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQS-- 505
Cdd:cd05048    94 DLHEFLvrHSPHSDVgVSSDDDGTASSldqsdflhIAIQIAAGMEYLSSHHYVHRDLAARNCLVGDGLTVKISDFGLSrd 173
                          90       100
                  ....*....|....*....|
gi 1720355205 506 ----------------IRWM 509
Cdd:cd05048   174 iyssdyyrvqsksllpVRWM 193
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
440-502 2.38e-03

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: 40.88  E-value: 2.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355205 440 LEEFLRLPREEPVENGEDKFA--HSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSK-KAVRLADF 502
Cdd:cd14013   100 LEPIIFGRVLIPPRGPKRENViiKSIMRQILVALRKLHSTGIVHRDVKPQNIIVSEGdGQFKIIDL 165
PHA02884 PHA02884
ankyrin repeat protein; Provisional
44-119 2.38e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.74  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205  44 LLEKGADANA---CEDTWGWTPLHNAVQAGRVDIVNLLLSHGADPHRRKKNGA-TPFIIAGIQGDVKLLEILLSCGADVN 119
Cdd:PHA02884   52 ILKLGADPEApfpLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSYGADIN 131
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
225-329 2.42e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 225 LIQHGADVNVRGERGKTPLIAAVERKHTGLVQMLLsREGINIDARDNEGKTALLIAVDKQLKEIVQLLLEKGA----DKC 300
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLL-KHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASisdpHAA 622
                          90       100
                  ....*....|....*....|....*....
gi 1720355205 301 DDLVWIARRNHDYHLVKLLLPYVANPDTD 329
Cdd:PLN03192  623 GDLLCTAAKRNDLTAMKELLKQGLNVDSE 651
PHA02741 PHA02741
hypothetical protein; Provisional
41-111 2.43e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 39.64  E-value: 2.43e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720355205  41 VQQLLEKGADANACEDTWGWTPLHNAVQAGRVDIVNLLLSH-GADPHRRKKNGATPFIIAGIQGDVKLLEIL 111
Cdd:PHA02741   80 IDHLIELGADINAQEMLEGDTALHLAAHRRDHDLAEWLCCQpGIDLHFCNADNKSPFELAIDNEDVAMMQIL 151
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
238-271 2.61e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 2.61e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1720355205 238 RGKTPL-IAAVERKHTGLVQMLLSReGINIDARDN 271
Cdd:pfam00023   1 DGNTPLhLAAGRRGNLEIVKLLLSK-GADVNARDK 34
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
451-505 2.65e-03

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: 40.47  E-value: 2.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720355205 451 PVENGEDKFAHSILlsifeGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQS 505
Cdd:cd05609    98 PVDMARMYFAETVL-----ALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLS 147
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
460-502 2.83e-03

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: 40.28  E-value: 2.83e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1720355205 460 AHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd05579    95 ARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDF 137
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
471-520 2.96e-03

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: 40.63  E-value: 2.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720355205 471 VQKLHLHGYSHQDLQPQNILIDSKKAVRLADFdqsirwmGESQM-VRRDLE 520
Cdd:cd05610   117 LDYLHRHGIIHRDLKPDNMLISNEGHIKLTDF-------GLSKVtLNRELN 160
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
388-502 2.97e-03

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: 40.38  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 388 VAVKVFRENSPRG-----CKEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVSLC-EWTLEEFLRLPREEPVENGED---- 457
Cdd:cd05101    59 VAVKMLKDDATEKdlsdlVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYAsKGNLREYLRARRPPGMEYSYDinrv 138
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720355205 458 -------KFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd05101   139 peeqmtfKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADF 190
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
372-583 3.16e-03

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: 40.28  E-value: 3.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 372 GTSEgaVYLGIY-DNREVAVKVFR-----ENSPRGCK-EVSCLRDCGDHSNLVAFYGRE--DDKGCLYVCVSLCEWTLEE 442
Cdd:cd14131    13 GSSK--VYKVLNpKKKIYALKRVDlegadEQTLQSYKnEIELLKKLKGSDRIIQLYDYEvtDEDDYLYMVMECGEIDLAT 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 443 FLRLPREEPVEngeDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIdSKKAVRLADF--------DQ-SIrwMGESQ 513
Cdd:cd14131    91 ILKKKRPKPID---PNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLL-VKGRLKLIDFgiakaiqnDTtSI--VRDSQ 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 514 M-------------------------VRR--DLEDLGrLVLYVVMKGEIPFETLKTQNDEVLLTMS-------PDEETKD 559
Cdd:cd14131   165 VgtlnymspeaikdtsasgegkpkskIGRpsDVWSLG-CILYQMVYGKTPFQHITNPIAKLQAIIDpnheiefPDIPNPD 243
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1720355205 560 LIHCLfspgenvKNCLV----------DLLGHPF 583
Cdd:cd14131   244 LIDVM-------KRCLQrdpkkrpsipELLNHPF 270
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
364-518 3.30e-03

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: 40.10  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 364 IHDDYKIAGTSEGAVYLGIYD--NREVAVKVFRENSPR---GCKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVS-LCE 437
Cdd:cd05052     8 ITMKHKLGGGQYGEVYEGVWKkyNLTVAVKTLKEDTMEveeFLKEAAVMKEI-KHPNLVQLLGVCTREPPFYIITEfMPY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 438 WTLEEFLRlpreepvENGEDKFAHSILL----SIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFdqsirwmGESQ 513
Cdd:cd05052    87 GNLLDYLR-------ECNREELNAVVLLymatQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADF-------GLSR 152

                  ....*
gi 1720355205 514 MVRRD 518
Cdd:cd05052   153 LMTGD 157
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
467-519 3.41e-03

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: 39.99  E-value: 3.41e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720355205 467 IFEGVQKLHLHGYSHQDLQPQNILIDSKKAVrLADFDQSIRwMGESQMVRRDL 519
Cdd:cd13995   105 VLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV-LVDFGLSVQ-MTEDVYVPKDL 155
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
474-502 3.46e-03

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: 39.81  E-value: 3.46e-03
                          10        20
                  ....*....|....*....|....*....
gi 1720355205 474 LHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd05123   109 LHSLGIIYRDLKPENILLDSDGHIKLTDF 137
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
376-552 3.58e-03

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: 39.84  E-value: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIYDNR-EVAVKVFREN--SPRGCKEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVSLCE-WTLEEFLRLPReep 451
Cdd:cd05114    18 GVVRLGKWRAQyKVAIKAIREGamSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMEnGCLLNYLRQRR--- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 452 vengeDKFAHSILLS----IFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSiRWMGESQMV------------ 515
Cdd:cd05114    95 -----GKLSRDMLLSmcqdVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMT-RYVLDDQYTsssgakfpvkws 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1720355205 516 ------------RRDLEDLGRLVLYVVMKGEIPFEtlKTQNDEVLLTMS 552
Cdd:cd05114   169 ppevfnyskfssKSDVWSFGVLMWEVFTEGKMPFE--SKSNYEVVEMVS 215
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
403-502 3.63e-03

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: 40.06  E-value: 3.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 403 EVSCLRDCgDHSNLVAFYGREddKGCLYVCVSLcEW----TLEEFLRLPR--EEPVengedkfAHSILLSIFEGVQKLHL 476
Cdd:cd06629    58 EIDTLKDL-DHPNIVQYLGFE--ETEDYFSIFL-EYvpggSIGSCLRKYGkfEEDL-------VRFFTRQILDGLAYLHS 126
                          90       100
                  ....*....|....*....|....*.
gi 1720355205 477 HGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd06629   127 KGILHRDLKADNILVDLEGICKISDF 152
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
457-546 3.66e-03

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: 39.81  E-value: 3.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 457 DKFAHS------ILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFD-------QSIRWMGE---------SQM 514
Cdd:cd14111    92 DRFRYSeddvvgYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGsaqsfnpLSLRQLGRrtgtleymaPEM 171
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1720355205 515 VR-------RDLEDLGrLVLYVVMKGEIPFETLKTQNDE 546
Cdd:cd14111   172 VKgepvgppADIWSIG-VLTYIMLSGRSPFEDQDPQETE 209
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
386-502 3.68e-03

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: 39.81  E-value: 3.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 386 REVAVKVF--RENSPRGC----KEVSCLRdCGDHSNLVAFYGREDDKGCLYVCVSLCEWTlEEFLRLpreepVENG--ED 457
Cdd:cd14072    26 REVAIKIIdkTQLNPSSLqklfREVRIMK-ILNHPNIVKLFEVIETEKTLYLVMEYASGG-EVFDYL-----VAHGrmKE 98
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1720355205 458 KFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd14072    99 KEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADF 143
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
376-548 3.92e-03

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: 39.87  E-value: 3.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIYDN-REVAVKVFREN--SPRGCKEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVSLCEWTLEEFLRLP--REE 450
Cdd:cd05067    21 GEVWMGYYNGhTKVAIKSLKQGsmSPDAFLAEANLMKQLQHQRLVRLYAVVTQEPIYIITEYMENGSLVDFLKTPsgIKL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 451 PVENGEDKFAHsillsIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQS-----------------IRWMGESQ 513
Cdd:cd05067   101 TINKLLDMAAQ-----IAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLArliedneytaregakfpIKWTAPEA 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1720355205 514 M------VRRDLEDLGRLVLYVVMKGEIPFETLKtqNDEVL 548
Cdd:cd05067   176 InygtftIKSDVWSFGILLTEIVTHGRIPYPGMT--NPEVI 214
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
385-502 4.03e-03

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: 39.71  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 385 NREVAVKVFRENSPR------GCKEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEWTLEEFLrlpreEPVENGED- 457
Cdd:cd07846    26 GQIVAIKKFLESEDDkmvkkiAMREIKMLKQL-RHENLVNLIEVFRRKKRWYLVFEFVDHTVLDDL-----EKYPNGLDe 99
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1720355205 458 KFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd07846   100 SRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDF 144
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
467-516 4.05e-03

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 39.64  E-value: 4.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720355205 467 IFEGVQKLHLHGYSHQDLQPQNILIDSKKA---VRLADFDQSiRWMGESQMVR 516
Cdd:cd14106   117 ILEGVQYLHERNIVHLDLKPQNILLTSEFPlgdIKLCDFGIS-RVIGEGEEIR 168
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
402-505 4.20e-03

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: 40.03  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 402 KEVSCLRDCgDHSNLVAFYGREDDKGCLYVCVSLCEW-TLEEFLRLPREEPVEngedkFAHSILLSIFEGVQKL-HLHGY 479
Cdd:cd06649    52 RELQVLHEC-NSPYIVGFYGAFYSDGEISICMEHMDGgSLDQVLKEAKRIPEE-----ILGKVSIAVLRGLAYLrEKHQI 125
                          90       100
                  ....*....|....*....|....*.
gi 1720355205 480 SHQDLQPQNILIDSKKAVRLADFDQS 505
Cdd:cd06649   126 MHRDVKPSNILVNSRGEIKLCDFGVS 151
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
412-505 4.33e-03

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: 39.91  E-value: 4.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 412 DHSNLVAFYGREDDKGCLYVCVSLCEWTleEFLRLPREEPvenG----ED--KF-AHSILLSIfegvQKLHLHGYSHQDL 484
Cdd:cd05574    59 DHPFLPTLYASFQTSTHLCFVMDYCPGG--ELFRLLQKQP---GkrlpEEvaRFyAAEVLLAL----EYLHLLGFVYRDL 129
                          90       100
                  ....*....|....*....|.
gi 1720355205 485 QPQNILIDSKKAVRLADFDQS 505
Cdd:cd05574   130 KPENILLHESGHIMLTDFDLS 150
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
388-502 4.57e-03

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: 39.44  E-value: 4.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 388 VAVKVFR--ENSPRGCKEVSCLRDCgDHSNLVAFYGREDDKGCLY-VCVSLCEWTLEEFLRlpREEPVEngedKFAHSIL 464
Cdd:cd14112    33 CAVKIFEvsDEASEAVREFESLRTL-QHENVQRLIAAFKPSNFAYlVMEKLQEDVFTRFSS--NDYYSE----EQVATTV 105
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1720355205 465 LSIFEGVQKLHLHGYSHQDLQPQNILIDSKKA--VRLADF 502
Cdd:cd14112   106 RQILDALHYLHFKGIAHLDVQPDNIMFQSVRSwqVKLVDF 145
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
376-501 4.60e-03

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: 39.74  E-value: 4.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 376 GAVYLGIYDN-----REVAVKVFRENSPRgcKEVSCLRD-----CG-DHSNLVAFYG-REDDKGCLYVCVSLCEW-TLEE 442
Cdd:cd05043    20 GRIFHGILRDekgkeEEVLVKTVKDHASE--IQVTMLLQessllYGlSHQNLLPILHvCIEDGEKPMVLYPYMNWgNLKL 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720355205 443 FLRLPREEPVENGEDKFAHSIL---LSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLAD 501
Cdd:cd05043    98 FLQQCRLSEANNPQALSTQQLVhmaLQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITD 159
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
38-93 4.64e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 4.64e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355205  38 VVRVqqLLEKGADANACeDTWGWTPLHNAVQAGRVDIVNLLLSHGADPHRRKKNGA 93
Cdd:PTZ00322  130 VVRV--LLEFGADPTLL-DKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAK 182
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
237-298 6.03e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 39.79  E-value: 6.03e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720355205 237 ERGKTPLIAAVERKHTGL---VQMLLS--------REGINIDARDN--EGKTALLIAVDKQLKEIVQLLLEKGAD 298
Cdd:cd22196    45 ETGKTCLLKAMLNLHNGQndtISLLLDiaektgnlKEFVNAAYTDSyyKGQTALHIAIERRNMHLVELLVQNGAD 119
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
361-502 6.58e-03

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: 38.97  E-value: 6.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 361 KIFiHDDYKIAGTSEGAVYLGiYDNREVAVKVFRENSPRG----------CKEVSCLRDCgDHSNLVAFYG---REDdkg 427
Cdd:cd06607     1 KIF-EDLREIGHGSFGAVYYA-RNKRTSEVVAIKKMSYSGkqstekwqdiIKEVKFLRQL-RHPNTIEYKGcylREH--- 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720355205 428 CLYVCVSLCEWTLEEFLRLPREePVEngEDKFAhSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd06607    75 TAWLVMEYCLGSASDIVEVHKK-PLQ--EVEIA-AICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADF 145
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
168-200 7.13e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.57  E-value: 7.13e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1720355205 168 GATALMSAAEK-GHLEVLRILLnDMKAEVDARDN 200
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLL-SKGADVNARDK 34
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
239-298 7.29e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 39.83  E-value: 7.29e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720355205 239 GKTPLIAAVERKHTG---LVQMLLS--------REGINIDARD--NEGKTALLIAVDKQLKEIVQLLLEKGAD 298
Cdd:cd22195    90 GKTCLPKALLNLNNGkndTIPILLDiaektgnlREFINSPFRDvyYRGQTALHIAIERRCKHYVELLVEKGAD 162
PHA02743 PHA02743
Viral ankyrin protein; Provisional
199-302 7.39e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 37.87  E-value: 7.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 199 DNMGRNAlIRTLLNWDCENVEEITSILIQHGADVNVRgER--GKTPLIAAVERKHTGLVQMLLSREGINIDARDNEGKTA 276
Cdd:PHA02743   54 DHHGRQC-THMVAWYDRANAVMKIELLVNMGADINAR-ELgtGNTLLHIAASTKNYELAEWLCRQLGVNLGAINYQHETA 131
                          90       100
                  ....*....|....*....|....*.
gi 1720355205 277 LLIAVDKQLKEIVQLLLEKGAdKCDD 302
Cdd:PHA02743  132 YHIAYKMRDRRMMEILRANGA-VCDD 156
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
91-123 7.42e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.57  E-value: 7.42e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1720355205  91 NGATPFIIA-GIQGDVKLLEILLSCGADVNECDE 123
Cdd:pfam00023   1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
PRK01723 PRK01723
3-deoxy-D-manno-octulosonic-acid kinase; Reviewed
473-503 7.61e-03

3-deoxy-D-manno-octulosonic-acid kinase; Reviewed


Pssm-ID: 234975  Cd Length: 239  Bit Score: 38.71  E-value: 7.61e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1720355205 473 KLHLHGYSHQDLQPQNILIDSKKAVRLADFD 503
Cdd:PRK01723  157 RFHDAGVYHADLNAHNILLDPDGKFWLIDFD 187
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
463-528 7.67e-03

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: 38.97  E-value: 7.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720355205 463 ILLSIFEGVQKLH--LHGYSHQDLQPQNILIDSKKAVRLADFDQS-IRWMGESQMVRRDLEDLGRLVLY 528
Cdd:cd13978    98 IIHEIALGMNFLHnmDPPLLHHDLKPENILLDNHFHVKISDFGLSkLGMKSISANRRRGTENLGGTPIY 166
PHA02741 PHA02741
hypothetical protein; Provisional
220-294 7.67e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 38.10  E-value: 7.67e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355205 220 EITSILIQHGADVNVRGE-RGKTPLIAAVERKHTGLVQMLLSREGINIDARDNEGKTALLIAVDKQLKEIVQLLLE 294
Cdd:PHA02741   78 EIIDHLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAIDNEDVAMMQILRE 153
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
471-502 8.18e-03

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: 38.81  E-value: 8.18e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1720355205 471 VQKLHLHGYSHQDLQPQNILIDS--KKAVRLADF 502
Cdd:cd14121   108 LQFLREHNISHMDLKPQNLLLSSryNPVLKLADF 141
PHA02736 PHA02736
Viral ankyrin protein; Provisional
224-301 8.21e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 37.55  E-value: 8.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720355205 224 ILIQHGADVNVRGER-GKTPLIAAVERKHTGLVQMLLSREGINIDARDNEGKTALLIAVDKQLKEIVQLLLEKGAdKCD 301
Cdd:PHA02736   76 LLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA-QCK 153
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
402-507 8.66e-03

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 38.76  E-value: 8.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 402 KEVSCLRDCGDHSNLVAFYGREDDKGCLYVcVSLCewTLEEFLRLPREEPVENGEDKfAHSILL------SIFEGVQKLH 475
Cdd:cd14020    52 KERAALEQLQGHRNIVTLYGVFTNHYSANV-PSRC--LLLELLDVSVSELLLRSSNQ-GCSMWMiqhcarDVLEALAFLH 127
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1720355205 476 LHGYSHQDLQPQNILIDSK-KAVRLADFDQSIR 507
Cdd:cd14020   128 HEGYVHADLKPRNILWSAEdECFKLIDFGLSFK 160
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
457-513 8.90e-03

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: 39.26  E-value: 8.90e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720355205 457 DKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFD--QSIRWMGESQ 513
Cdd:cd05625   100 EDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlcTGFRWTHDSK 158
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
231-298 9.60e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 39.09  E-value: 9.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 231 DVNVRGERGKTPLIAAVERKHTGLVQ--MLL---------SREGINIDARDN--EGKTALLIAVDKQLKEIVQLLLEKGA 297
Cdd:cd21882    18 SAYQRGATGKTCLHKAALNLNDGVNEaiMLLleaapdsgnPKELVNAPCTDEfyQGQTALHIAIENRNLNLVRLLVENGA 97

                  .
gi 1720355205 298 D 298
Cdd:cd21882    98 D 98
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
388-502 9.68e-03

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: 38.48  E-value: 9.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355205 388 VAVKVFRENSPRGC-------KEVSCLRDCgDHSNLVAFYGREDDKGCLYVcVSLCEW-TLEEFLRLPreepvengedkf 459
Cdd:cd05040    26 VAVKCLKSDVLSQPnamddflKEVNAMHSL-DHPNLIRLYGVVLSSPLMMV-TELAPLgSLLDRLRKD------------ 91
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720355205 460 AHSILLS--------IFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADF 502
Cdd:cd05040    92 QGHFLIStlcdyavqIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDF 142
 
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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