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Conserved domains on  [gi|570359577|ref|NP_001275659|]
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death-associated protein kinase 1 [Homo sapiens]

Protein Classification

STKc_DAPK1 and Death_DAPK1 domain-containing protein (domain architecture ID 12995844)

STKc_DAPK1 and Death_DAPK1 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
7-275 0e+00

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 589.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577    7 ENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSREDIEREVSILKEIQHPNVITLHEVYENK 86
Cdd:cd14194     1 ENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSREDIEREVSILKEIQHPNVITLHEVYENK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577   87 TDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRIKIIDFGLAH 166
Cdd:cd14194    81 TDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRIKIIDFGLAH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  167 KIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTSA 246
Cdd:cd14194   161 KIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTSA 240
                         250       260
                  ....*....|....*....|....*....
gi 570359577  247 LAKDFIRRLLVKDPKKRMTIQDSLQHPWI 275
Cdd:cd14194   241 LAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
Death_DAPK1 cd08782
Death domain found in death-associated protein kinase 1; Death domain (DD) found in ...
1308-1393 6.65e-45

Death domain found in death-associated protein kinase 1; Death domain (DD) found in death-associated protein kinase 1 (DAPK1). DAPK1 is composed of several functional domains, including a kinase domain, a CaM regulatory domain, ankyrin repeats, a cytoskeletal-binding domain and a C-terminal DD. It plays important roles in a diverse range of signal transduction pathways including apoptosis, growth factor signalling, and autophagy. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


:

Pssm-ID: 260052  Cd Length: 82  Bit Score: 156.35  E-value: 6.65e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577 1308 LTRRKLSRLLDPPDPLGKDWCLLAMNLGLPDLVAKYNTSNGApkdfLPSPLHALLREWTTYPESTVGTLMSKLRELGRRD 1387
Cdd:cd08782     1 LTRRKLARLLDPPDPMGRDWCLLAVNLGLTDLVAKLDSTSSP----LPSPTDRLLQEWTARPPSTIGALLRKLRELGRRD 76

                  ....*.
gi 570359577 1388 AADFLL 1393
Cdd:cd08782    77 AADFLL 82
PHA03100 super family cl33710
ankyrin repeat protein; Provisional
367-639 4.24e-27

ankyrin repeat protein; Provisional


The actual alignment was detected with superfamily member PHA03100:

Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 115.92  E-value: 4.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  367 LSNYDVNQPNKhgtpplliaagCGNIQILQLLIKRGSRIDVQDKGGSNAVYWAARHGHVDTLKFLSENKCPLDVKDKSGE 446
Cdd:PHA03100    1 LYSYIVLTKSR-----------IIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNS 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  447 MALHVAARYGHA-----DVAQLLCSFGSNPNIQDKEEETPLHCAAWH--GYYSVAKALCEAGCNVNIKNREGETPLLTAS 519
Cdd:PHA03100   70 TPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  520 ARGYHD--IVECLAEHGADLNACDKdghialhlavrrcqmevIKTLLSQGCFVDYQDRHGNTPLHVACKDGNMPIVVALC 597
Cdd:PHA03100  150 ESNKIDlkILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLL 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 570359577  598 EANCNLDISNKYGRTPLHLAANNGILDVVRYLCLMGASVEAL 639
Cdd:PHA03100  213 DLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
515-768 3.54e-09

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.42  E-value: 3.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  515 LLTASARGYHDIVECLAEHGADLNACDKDGHIALHLAVRRCQMEVIKTLLSQGCFVDYQDRHGNTPLHVACKDGNMPIVV 594
Cdd:PLN03192  529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  595 ALCEANcnlDISNKY-GRTPLHLAANNGILDVVRYLCLMGASVEALTTDGKTAEDLARSEQHEHVAGLLARLRKDTHRGL 673
Cdd:PLN03192  609 ILYHFA---SISDPHaAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  674 FIQQLRPTQnLQPRIKLKLFGHSgsgkTTLVESLKCGLLRSFFRRRRPRLSSTNSSrfppSPLASKPTVSVsinnlYPGc 753
Cdd:PLN03192  686 TDDDFSPTE-LRELLQKRELGHS----ITIVDSVPADEPDLGRDGGSRPGRLQGTS----SDNQCRPRVSI-----YKG- 750
                         250
                  ....*....|....*
gi 570359577  754 eNVSVRSRSMMFEPG 768
Cdd:PLN03192  751 -HPLLRNERCCNEAG 764
 
Name Accession Description Interval E-value
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
7-275 0e+00

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 589.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577    7 ENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSREDIEREVSILKEIQHPNVITLHEVYENK 86
Cdd:cd14194     1 ENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSREDIEREVSILKEIQHPNVITLHEVYENK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577   87 TDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRIKIIDFGLAH 166
Cdd:cd14194    81 TDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRIKIIDFGLAH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  167 KIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTSA 246
Cdd:cd14194   161 KIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTSA 240
                         250       260
                  ....*....|....*....|....*....
gi 570359577  247 LAKDFIRRLLVKDPKKRMTIQDSLQHPWI 275
Cdd:cd14194   241 LAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
13-275 8.65e-97

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 311.00  E-value: 8.65e-97
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577     13 YDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRrgvsrEDIEREVSILKEIQHPNVITLHEVYENKTDVILI 92
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDR-----ERILREIKILKKLKHPNIVRLYDVFEDEDKLYLV 75
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577     93 LELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENImLLDRNvpkPRIKIIDFGLAHKIDFGN 172
Cdd:smart00220   76 MEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENI-LLDED---GHVKLADFGLARQLDPGE 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577    173 EFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTSALAKDFI 252
Cdd:smart00220  152 KLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLI 231
                           250       260
                    ....*....|....*....|...
gi 570359577    253 RRLLVKDPKKRMTIQDSLQHPWI 275
Cdd:smart00220  232 RKLLVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
13-275 7.89e-87

Protein kinase domain;


Pssm-ID: 333812 [Multi-domain]  Cd Length: 259  Bit Score: 283.36  E-value: 7.89e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577    13 YDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSrrgvSREDIEREVSILKEIQHPNVITLHEVYENKTDVILI 92
Cdd:pfam00069    1 YEVLEKLGEGSFGTVYKAKHKDTGKIVAIKKIKKEKIKKK----KEKNVLREIKILKKLSHPNIVRLYDVFEDKDHLYLV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577    93 LELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVpkprIKIIDFGLAHKIDFGN 172
Cdd:pfam00069   77 LEYVEGGSLFDLLSEKGVFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDGN----LKITDFGLAKQLSSGS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577   173 EFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANV----SAVNYEFEDEYFSNTSALA 248
Cdd:pfam00069  153 KLTTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGDDIYELIldqlERIPEDFSSPFPSSLSEEA 232
                          250       260
                   ....*....|....*....|....*..
gi 570359577   249 KDFIRRLLVKDPKKRMTIQDSLQHPWI 275
Cdd:pfam00069  233 KDLLKKLLKKDPSKRLTATQALQHPWF 259
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
13-280 2.65e-47

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 174.55  E-value: 2.65e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577   13 YDTGEELGSGQFAVVKKCREKstgLQYAAKFIKKRRTKSSRrgvSREDIEREVSILKEIQHP-NVITLHEVYENKTDVIL 91
Cdd:COG0515     2 YRILRKLGEGSFGEVYLARDR---KLVALKVLAKKLESKSK---EVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577   92 ILELVAGGELFDFLAE---KESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLldrNVPKPRIKIIDFGLAHKI 168
Cdd:COG0515    76 VMEYVDGGSLEDLLKKigrKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILL---DRDGRVVKLIDFGLAKLL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  169 DFGNE-------FKNIFGTPEFVAPEIV---NYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFED 238
Cdd:COG0515   153 PDPGStssipalPSTSVGTPGYMAPEVLlglSLAYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLKIILELPT 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 570359577  239 EYFSN---------TSALAKDFIRRLLVKDPKKRMTIQDSLQHPWIKPKDT 280
Cdd:COG0515   233 PSLASplspsnpelISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKL 283
Death_DAPK1 cd08782
Death domain found in death-associated protein kinase 1; Death domain (DD) found in ...
1308-1393 6.65e-45

Death domain found in death-associated protein kinase 1; Death domain (DD) found in death-associated protein kinase 1 (DAPK1). DAPK1 is composed of several functional domains, including a kinase domain, a CaM regulatory domain, ankyrin repeats, a cytoskeletal-binding domain and a C-terminal DD. It plays important roles in a diverse range of signal transduction pathways including apoptosis, growth factor signalling, and autophagy. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260052  Cd Length: 82  Bit Score: 156.35  E-value: 6.65e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577 1308 LTRRKLSRLLDPPDPLGKDWCLLAMNLGLPDLVAKYNTSNGApkdfLPSPLHALLREWTTYPESTVGTLMSKLRELGRRD 1387
Cdd:cd08782     1 LTRRKLARLLDPPDPMGRDWCLLAVNLGLTDLVAKLDSTSSP----LPSPTDRLLQEWTARPPSTIGALLRKLRELGRRD 76

                  ....*.
gi 570359577 1388 AADFLL 1393
Cdd:cd08782    77 AADFLL 82
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
13-290 1.73e-40

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 153.05  E-value: 1.73e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577   13 YDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRgvsREDIEREVSILKEIQHPNVITLHEVYENKTDVILI 92
Cdd:PTZ00263   20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQ---VQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577   93 LELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENImLLDRnvpKPRIKIIDFGLAHKIDfgN 172
Cdd:PTZ00263   97 LEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENL-LLDN---KGHVKVTDFGFAKKVP--D 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  173 EFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYfsntSALAKDFI 252
Cdd:PTZ00263  171 RTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWF----DGRARDLV 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 570359577  253 RRLLVKDPKKRM-----TIQDSLQHPWIKPKDTQQALSRKASA 290
Cdd:PTZ00263  247 KGLLQTDHTKRLgtlkgGVADVKNHPYFHGANWDKLYARYYPA 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
367-639 4.24e-27

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 115.92  E-value: 4.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  367 LSNYDVNQPNKhgtpplliaagCGNIQILQLLIKRGSRIDVQDKGGSNAVYWAARHGHVDTLKFLSENKCPLDVKDKSGE 446
Cdd:PHA03100    1 LYSYIVLTKSR-----------IIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNS 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  447 MALHVAARYGHA-----DVAQLLCSFGSNPNIQDKEEETPLHCAAWH--GYYSVAKALCEAGCNVNIKNREGETPLLTAS 519
Cdd:PHA03100   70 TPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  520 ARGYHD--IVECLAEHGADLNACDKdghialhlavrrcqmevIKTLLSQGCFVDYQDRHGNTPLHVACKDGNMPIVVALC 597
Cdd:PHA03100  150 ESNKIDlkILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLL 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 570359577  598 EANCNLDISNKYGRTPLHLAANNGILDVVRYLCLMGASVEAL 639
Cdd:PHA03100  213 DLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254
Ank_2 pfam12796
Ankyrin repeats (3 copies);
418-508 2.42e-22

Ankyrin repeats (3 copies);


Pssm-ID: 338493 [Multi-domain]  Cd Length: 92  Bit Score: 92.48  E-value: 2.42e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577   418 WAARHGHVDTLKFLSENKCPLDVKDKSGEMALHVAARYGHADVAQLLCSFGsNPNIQDKEEETPLHCAAWHGYYSVAKAL 497
Cdd:pfam12796    3 LAAKNGDLELVKLLLEEGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDKNGRTALHYAARSGHLEIVKLL 81
                           90
                   ....*....|.
gi 570359577   498 CEAGCNVNIKN 508
Cdd:pfam12796   82 LEKGADINVKD 92
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
447-642 4.11e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738 [Multi-domain]  Cd Length: 235  Bit Score: 91.04  E-value: 4.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  447 MALHVAARYGHADVAQLLCSFGSNPNIQDKEEETPLHcAAWHGYYSVAKALCEAGCNVNIKNREGETPLLTASARGYHDI 526
Cdd:COG0666    10 LINKCFLDLLLVALLLLLSLDLSNPSDKKLNLYLELA-LLPAASLSELLLKLIVDRHLAARDLDGRLPLHSAASKGDDKI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  527 VECLAEHGADLNACDKDGHIALHLAVRRCQ-----MEVIKTLLSQG---CFVDYQDRHGNTPLHVACKDGNMPIVVALCE 598
Cdd:COG0666    89 VKLLLASGADVNAKDADGDTPLHLAALNGNppegnIEVAKLLLEAGadlDVNNLRDEDGNTPLHWAALNGDADIVELLLE 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 570359577  599 ANCNLDISNKYGRTPLHLAANNGILDVVRYLCLMGASVEALTTD 642
Cdd:COG0666   169 AGADPNSRNSYGVTALDPAAKNGRIELVKLLLDKGLHLSLLKFN 212
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
35-263 7.31e-18

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


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 89.90  E-value: 7.31e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577    35 TGLQYAAKFIkkrRTKSSRRGVSREDIEREVSILKEIQHPNVITLHEVYENKTDVIL-ILELVAGGELFDFLAEKESLTE 113
Cdd:TIGR03903    2 TGHEVAIKLL---RTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEAPPGLLFaVFEYVPGRTLREVLAADGALPA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577   114 EEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVpKPRIKIIDFGL------AHKIDFGNEFK--NIFGTPEFVA 185
Cdd:TIGR03903   79 GETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGV-RPHAKVLDFGIgtllpgVRDADVATLTRttEVLGTPTYCA 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577   186 PEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETL-ANVSAVNyefedeyFSNTSALAK----DFIRRLLVKDP 260
Cdd:TIGR03903  158 PEQLRGEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILyQQLSPVD-------VSLPPWIAGhplgQVLRKALNKDP 230

                   ...
gi 570359577   261 KKR 263
Cdd:TIGR03903  231 RQR 233
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
1307-1395 2.96e-16

DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.


Pssm-ID: 214467  Cd Length: 88  Bit Score: 75.14  E-value: 2.96e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577   1307 LLTRRKLSRLLDPPdpLGKDWCLLAMNLGLPDLVAKYNTSNgAPKDfLPSPLHALLREWTTY--PESTVGTLMSKLRELG 1384
Cdd:smart00005    2 ELTRQKLAKLLDHP--LGLDWRELARKLGLSEADIDQIRTE-APRD-LAEQSVQLLRLWEQRegKNATLGTLLEALRKMG 77
                            90
                    ....*....|.
gi 570359577   1385 RRDAADFLLKA 1395
Cdd:smart00005   78 RDDAVELLRSE 88
Death pfam00531
Death domain;
1310-1392 2.66e-15

Death domain;


Pssm-ID: 306916  Cd Length: 86  Bit Score: 72.01  E-value: 2.66e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  1310 RRKLSRLLDPPDPLGKDWCLLAMNLGLP----DLVAKYNTSngapkdfLPSPLHALLREWT--TYPESTVGTLMSKLREL 1383
Cdd:pfam00531    1 RKQLDRLLDPPPPLGKDWRELARKLGLSeneiDEIEQQNPR-------LRSQTYELLRLWEqrEGKNATVGTLLEALRKL 73

                   ....*....
gi 570359577  1384 GRRDAADFL 1392
Cdd:pfam00531   74 GRRDAAEKI 82
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
515-768 3.54e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.42  E-value: 3.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  515 LLTASARGYHDIVECLAEHGADLNACDKDGHIALHLAVRRCQMEVIKTLLSQGCFVDYQDRHGNTPLHVACKDGNMPIVV 594
Cdd:PLN03192  529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  595 ALCEANcnlDISNKY-GRTPLHLAANNGILDVVRYLCLMGASVEALTTDGKTAEDLARSEQHEHVAGLLARLRKDTHRGL 673
Cdd:PLN03192  609 ILYHFA---SISDPHaAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  674 FIQQLRPTQnLQPRIKLKLFGHSgsgkTTLVESLKCGLLRSFFRRRRPRLSSTNSSrfppSPLASKPTVSVsinnlYPGc 753
Cdd:PLN03192  686 TDDDFSPTE-LRELLQKRELGHS----ITIVDSVPADEPDLGRDGGSRPGRLQGTS----SDNQCRPRVSI-----YKG- 750
                         250
                  ....*....|....*
gi 570359577  754 eNVSVRSRSMMFEPG 768
Cdd:PLN03192  751 -HPLLRNERCCNEAG 764
 
Name Accession Description Interval E-value
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
7-275 0e+00

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 589.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577    7 ENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSREDIEREVSILKEIQHPNVITLHEVYENK 86
Cdd:cd14194     1 ENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSREDIEREVSILKEIQHPNVITLHEVYENK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577   87 TDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRIKIIDFGLAH 166
Cdd:cd14194    81 TDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRIKIIDFGLAH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  167 KIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTSA 246
Cdd:cd14194   161 KIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTSA 240
                         250       260
                  ....*....|....*....|....*....
gi 570359577  247 LAKDFIRRLLVKDPKKRMTIQDSLQHPWI 275
Cdd:cd14194   241 LAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
7-275 0e+00

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 575.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577    7 ENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSREDIEREVSILKEIQHPNVITLHEVYENK 86
Cdd:cd14105     1 ENVEDFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKASRRGVSREDIEREVSILRQVLHPNIITLHDVFENK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577   87 TDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRIKIIDFGLAH 166
Cdd:cd14105    81 TDVVLILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVPIPRIKLIDFGLAH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  167 KIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTSA 246
Cdd:cd14105   161 KIEDGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFDDEYFSNTSE 240
                         250       260
                  ....*....|....*....|....*....
gi 570359577  247 LAKDFIRRLLVKDPKKRMTIQDSLQHPWI 275
Cdd:cd14105   241 LAKDFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
7-276 1.37e-174

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 520.33  E-value: 1.37e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577    7 ENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSREDIEREVSILKEIQHPNVITLHEVYENK 86
Cdd:cd14195     1 SMVEDHYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSRRGVSREEIEREVNILREIQHPNIITLHDIFENK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577   87 TDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRIKIIDFGLAH 166
Cdd:cd14195    81 TDVVLILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNPRIKLIDFGIAH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  167 KIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTSA 246
Cdd:cd14195   161 KIEAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSNTSE 240
                         250       260       270
                  ....*....|....*....|....*....|
gi 570359577  247 LAKDFIRRLLVKDPKKRMTIQDSLQHPWIK 276
Cdd:cd14195   241 LAKDFIRRLLVKDPKKRMTIAQSLEHSWIK 270
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
7-275 1.81e-173

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 517.59  E-value: 1.81e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577    7 ENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSREDIEREVSILKEIQHPNVITLHEVYENK 86
Cdd:cd14196     1 QKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIEREVSILRQVLHPNIITLHDVYENR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577   87 TDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRIKIIDFGLAH 166
Cdd:cd14196    81 TDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  167 KIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTSA 246
Cdd:cd14196   161 EIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSHTSE 240
                         250       260
                  ....*....|....*....|....*....
gi 570359577  247 LAKDFIRRLLVKDPKKRMTIQDSLQHPWI 275
Cdd:cd14196   241 LAKDFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
19-274 2.82e-139

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: 426.30  E-value: 2.82e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577   19 LGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKssrrgvsREDIEREVSILKEIQHPNVITLHEVYENKTDVILILELVAG 98
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAAKFIPKRDKK-------KEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577   99 GELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRnvPKPRIKIIDFGLAHKIDFGNEFKNIF 178
Cdd:cd14006    74 GELLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADR--PSPQIKIIDFGLARKLNPGEELKEIF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  179 GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTSALAKDFIRRLLVK 258
Cdd:cd14006   152 GTPEFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFSEEYFSSVSQEAKDFIRKLLVK 231
                         250
                  ....*....|....*.
gi 570359577  259 DPKKRMTIQDSLQHPW 274
Cdd:cd14006   232 EPRKRPTAQEALQHPW 247
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
19-275 2.91e-118

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 369.63  E-value: 2.91e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577   19 LGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSsrrgvsREDIEREVSILKEIQHPNVITLHEVYENKTDVILILELVAG 98
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKD------REDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577   99 GELFD-FLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNvpKPRIKIIDFGLAHKIDFGNEFKNI 177
Cdd:cd14103    75 GELFErVVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRT--GNQIKIIDFGLARKYDPDKKLKVL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  178 FGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTSALAKDFIRRLLV 257
Cdd:cd14103   153 FGTPEFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWDFDDEAFDDISDEAKDFISKLLV 232
                         250
                  ....*....|....*...
gi 570359577  258 KDPKKRMTIQDSLQHPWI 275
Cdd:cd14103   233 KDPRKRMSAAQCLQHPWL 250
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
13-274 1.48e-115

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


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 362.95  E-value: 1.48e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577   13 YDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRgvsrEDIEREVSILKEIQHPNVITLHEVYENKTDVILI 92
Cdd:cd05117     2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDE----EMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577   93 LELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNvPKPRIKIIDFGLAHKIDFGN 172
Cdd:cd05117    78 MELCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKD-PDSPIKIIDFGLAKIFEEGE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  173 EFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTSALAKDFI 252
Cdd:cd05117   157 KLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEEAKDLI 236
                         250       260
                  ....*....|....*....|..
gi 570359577  253 RRLLVKDPKKRMTIQDSLQHPW 274
Cdd:cd05117   237 KRLLVVDPKKRLTAAEALNHPW 258
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
5-275 9.85e-112

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: 352.81  E-value: 9.85e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577    5 RQENVDDYYD-TGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSrrgvSREDIEREVSILKEIQ-HPNVITLHEV 82
Cdd:cd14106     1 STENINEVYTvESTPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQD----CRNEILHEIAVLELCKdCPRVVNLHEV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577   83 YENKTDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENImLLDRNVPKPRIKIIDF 162
Cdd:cd14106    77 YETRSELILILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNI-LLTSEFPLGDIKLCDF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577  163 GLAHKIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFS 242
Cdd:cd14106   156 GISRVIGEGEEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEELFK 235
                         250       260       270
                  ....*....|....*....|....*....|...
gi 570359577  243 NTSALAKDFIRRLLVKDPKKRMTIQDSLQHPWI 275
Cdd:cd14106   236 DVSPLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
13-275 8.65e-97

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 311.00  E-value: 8.65e-97
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577     13 YDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRrgvsrEDIEREVSILKEIQHPNVITLHEVYENKTDVILI 92
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDR-----ERILREIKILKKLKHPNIVRLYDVFEDEDKLYLV 75
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577     93 LELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENImLLDRNvpkPRIKIIDFGLAHKIDFGN 172
Cdd:smart00220   76 MEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENI-LLDED---GHVKLADFGLARQLDPGE 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359577    173 EFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTSALAKDFI 252
Cdd:smart00220  152 KLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLI 231
                           250       260
                    ....*....|....*....|...
gi 5